entry
stringlengths 6
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| entry_name
stringlengths 5
11
| protein_name
stringlengths 3
2.44k
| sequence
stringlengths 2
35.2k
| function
stringlengths 7
11k
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A1A5H8
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YES_DANRE
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Tyrosine-protein kinase yes (EC 2.7.10.2) (p61-Yes)
|
MGCVKSKEDKGPTQKYRPDPTNPTPGSHMGLYGPDPTQMGQSPALKGPTNNYNSRSSGLTPFGGSSSVITPFGGASSSFSTVAVNNPFPGVVTGGVTFFVALYDYEARTSDDLSFSKGDRFQIINNTEGDWWEARSINTGQKGYIPSNYVAPADSIQAEEWYFGKMGRKDAERLLLLPGNQRGTFLVRESETTKGAYSLSIRDWDEMKGDNVKHYKIRKLDSGGYYITTRAQFDTLQKLVKHYTEHADGLCYRLTTVCPTVKPQTQGLAKDAWEIPRESLRLELKLGQGCFGEVWMGTWNGTTKVAIKTLKPGTMSPEAFLQEAQIMKKLRHDKLVPLYAVVSEEPIYIVTEYMGKGSLLDFLKEGEGKYLKLPQLVDMAAQIADGMAFIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMVNREVLEQVERGYRMPCPQGCPESLHEMMRLCWKKEPDERPTFEYIQSFLEDYFTATEPQYQPGDNL
|
Non-receptor protein tyrosine kinase that is involved in the regulation of cell growth and survival, apoptosis, cell-cell adhesion, cytoskeleton remodeling, differentiation, G2/M progression and cytokinesis (By similarity). Required for convergent extension cell movements during gastrulation, acting with fyna via rhoa. May be required for epiboly to occur, possibly through its effects in calcium signaling. During embryonic development, phosphorylates ptk2.1/fak. {ECO:0000250, ECO:0000269|PubMed:15572145, ECO:0000269|PubMed:15815683}.
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A1A5Q0
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LMOD2_RAT
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Leiomodin-2 (Cardiac leiomodin) (C-LMOD) (Leiomodin)
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MSTFGYRRGLSKYESIDEDELLASLTAEELKELERELEDIEPDRNLPVGLRQKSLTEKTPTGNFSREALMAYWEKESQKLLEKERLGECGKLAEEDKEESEEELIFTESNSEVSEEVCTEEEEESTEEEEEEEEEDSEEEEVTTEVTKHINGTVSHNGVNPDNSKPKTFKSQIENINLTNGNSGGTQRNTESPAAIHPCGNPTVIEDALEKIKNNDPDTTEVNLNNIENITTQTLSRFAEALKENTVVKTFSLANTHADDAAAIAIAEMLKVNEHITSVNVESNFITGKGILAIMRALQHNTVLTELRFHNQRHIMGSQVEMEIVKLLKENTTLLRLGYHFELPGPRMSMTSILTRNMDKQRQKRMQEQKQQEGHDGGATLRTKVWQRGTPGSSPYASPRQSPWSSPKVSKKVHTGRSRPPSPVAPPPPPPPPPLPPHMLPPPPPPPAPPLPGKKLITRNIAEVIKQQESAQRALQNGQRKKKGKKVKKQPNNILKEIKNSLRSVQEKKMEESSRPSTPQRSAHENLMEAIRGSSIRQLRRVEVPEALR
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Mediates nucleation of actin filaments and thereby promotes actin polymerization. Plays a role in the regulation of actin filament length (By similarity). Required for normal sarcomere organization in the heart, and for normal heart function.
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A1A5Q5
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KDM4D_RAT
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Lysine-specific demethylase 4D (EC 1.14.11.66) (JmjC domain-containing histone demethylation protein 3D) (Jumonji domain-containing protein 2D) ([histone H3]-trimethyl-L-lysine(9) demethylase 4D)
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MKTKSTCAQNPNCSIMIFRPTKEEFNDFDKYIAYMESQGAHRAGLAKVIPPKEWRARQSYDNISNILIATPLQQVVSGQAGVFTQYHKKKKAMTVGQYRHLANSKKYQTPPHLDFEDLERKYWKNRLYESPIYGADVSGSLFDGKTQQWNVGHLGTIQDLLEQECGIVIEGVNTPYLYFGMWKTSFAWHTEDMDLYSINYLHFGQPKTWYAVPPEHGRRLELLAKELFPGSSQGCQAFLRHKVALISPTVLKENGIPFGRITQEAGEFMVTFPYGYHAGFNHGFNCAEAINFATPRWIDYGKVASQCSCGEARVSFSMDAFVRILQPERYEMWKRGQDQAVVDHTEAMGPTSQELTTWRVIQAPRKTWGLKHLRLRQVSRCLLPVATDSNIANNTQMCHTSRQAADSKGDEVQESDPAIAPPYPLGLSSPGHMSTGKRGLGRRPCELGVQESTNGAPVKRRLPEGRDDRSPSPELQSQSVTGDLIVNSDLVNPGPQHPVTASEGGLTSDP
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Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27', H3 'Lys-36' nor H4 'Lys-20'. Demethylates both di- and trimethylated H3 'Lys-9' residue, while it has no activity on monomethylated residues. Demethylation of Lys residue generates formaldehyde and succinate.
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A1A696
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OHK3_ORYSJ
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Probable histidine kinase 3 (OsHK3) (EC 2.7.13.3) (OsCRL2)
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MDEMSCGGGGGGARWKRARVAGMGEGKAGGGGGAAFLGLERVGMVVRMLPVPEKVSARARVVRGSLVAHFRGWRVVRETWWWVLLLWILAGSLGSFYLFLFMNAQSLDKRRDSLASMCDERARMLQDQFNVSMNHLQALAILVSTFHHSKTPSAIDQMTFARYAERTAFERPLTSGVAYAVRVTHGEREQFERQQGWAIKKMYSSSNKKQSSPGPGPGDAAVAEIREPAEEYAPVIFAQDAYKHVISFDMLSGNEDRDNILRARKSGKGVLTAPFKLLNNRLGVILTYTVYKYELPAYARPHERIQAAIGYLGGIFDIQALVEKLLKQLASQESIMVNVYDTTNESPISMYGDDTGSGMCHVSVLNFGDPSRKHEMHCRFEKKPPWPWLAITSSFGTLVIALLTGHIFQATVHRIAKVEDDFHKMSELKKRAEDADVAKSQFLATVSHEIRTPMNGVLGMLQMLMDTDLDTTQQDYVRTAQASGKALVSLINEVLDQAKIESGKLELETVPFDLRTVCDDILSLFCGKAQEKGLELAVYVSDQVPQILIGDPGRIRQIITNLVGNSIKFTERGHIYLTVHVVEEVMSCLEVETGIQNTNTLSGYPVANRRCSWESIRLFNRELHSSEKSFAPIASDSISLVISVEDTGVGIPFEAQSRVFTPFMQVGPSIARIHGGTGIGLSISKCLVGLMKGEIGFASKPHVGSTFTFTAVLMRAHCKGNDIKSSEFKGINALVVDHRPVRAKVTKYHLQRLGVKTELTAELNQFISKLNSGSLTAKLVLIDKETWLKESHCTPLLVNKLRNNDKPDSPKLFLLGSSASSPKGGSDTSREHNLNVIMKPLRASMLQVSLRRALGGVDKVHCRNGVVGNSTLGSLLHKKQIIVVDDNIVNLKVAAGALKKYGAEVTCADSGKKAITLLKPPHNFDACFMDIQMPEMDGFEATRRIRVMERDLNERIERGEAPPECASIQRWRTPILAMTADVIQATHEECLKSEMDGYVSKPFEGEQLYSEVARFFQNHDQVE
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Cytokinin receptor related to bacterial two-component regulators. Functions as a histidine kinase and transmits the stress signal to a downstream MAPK cascade.
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A1A698
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OHK4_ORYSJ
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Probable histidine kinase 4 (OsHK4) (EC 2.7.13.3) (OsCRL1b)
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MGVGGGGGGGGGEAAAAVAVEGDEAGKGRRWWRVKVKLSTVAVVAWVLASAALWAGLHWRFRRAALHKAEEALVCMCEERARMLQDQFAVSVNHVHALAILVATFHYDKHPPALDQDTFAVYAARTSFERPLLSGVAYAQRVVHADRESFERQQGWIIKTMKHEPSPAQDEYAPVIYSQETISYIEGLDVMSGEEDRENILRARATGKAVLTRPFRLMSNHLGVVLTFPVYLVDLPNDTAVEDRVAATAGYLGGAFDVESLVENLLRQLAGNQELVVNVYDVTNHSNPLVMYGSEVPLGIPSPSHTYTLDFGDPLRKHQMVCRYRNKLHVSWSAITTPSGVFVICMLVGYIIYAAWSRYDNVKEDCRKMEALKKRAEAADIAKSQFLATVSHEIRTPMNGVLGMLDMLLDTELKSTQRDYAQTAQVCGKALISLINEVLDRAKIEAGKIDLESVPFDLRSILDDVISLFSSKSREKGIELAVYVSERVPEILLGDPGRFRQIITNLVGNSIKFTERGHIFVQVHLADHSNLATEAKIEPVVNGMNGHKDEAIAIPTSGSHNTLSGFEAADSRNNWENFKLLLSYEKNEMPYESDSDKVTLVVSVEDTGIGIPLHAQGRVFTPFMQADSSTSRNYGGTGIGLSISKCLVEIMGGQINFVSRPLVGSTFTFTAVLRRCDKNAISDSKTVALHPLPSSFKGLSALLVDKRPVRATVTKYHLQRLGITSEVVGTIDPTFGVLSGRNGSSLTSIGKKQPCMLLIESDSWGPQMDVSLHARLQEMKQSDRIHVLPKVFLLSAAESDKVKKIHAVDSVIPKPLKASALAACLFQALGITQPSHEKRDDSGSLHGRDGSGSLHGLLLGKNILVVDDNKVNLRVAAGTLKKYGAKVECVESGKDALSLLQVPHKFDLCLMDIQMPEMDGFEATRQIRAMEGKANEQADDSESGSEIAAKTAKWHLPILAMTADVIQATHEECTKCGMDGYVSKPFEEKQLFQAVQKFLGPCVSS
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Cytokinin receptor related to bacterial two-component regulators. Functions as a histidine kinase and transmits the stress signal to a downstream MAPK cascade.
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A1A699
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OHK6_ORYSJ
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Probable histidine kinase 6 (OsHK6) (EC 2.7.13.3) (OsCRL1a)
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MGKPEARSGWRNAAAAAWVLVAVACAAYMHWHLRRETMDRAEERLVSMCEERARMLQEQFGVTVNHVHALAILISTFHFEKFPSAIDQDTFAKYTARTSFERPLLNGVAYAQRIFHHEREMFENQQGWIMKTMKRQAAPPQDEYAPVIFSQDTVSYLARIDMMSGEEDRENILRARATGKAVLTNPFRLLGSNHLGVVLTFAVYRPGLAADASVEERVEATAGYLGGAFDVESLVENLLSKLAGNQDIVVNVYDVTNASEPMAMYGPQSPDGKVSLFHVSTLDFGDPFRAHEMRCRYRQKPPLPWSAITNPLGTFVIWMLVGYIICAAWSRYDKVSEDCRKMEELKTQAEAADVAKSQFLATVSHEIRTPMNGVLGMLDMLLGTDLSMTQKDYAQTAQMCGRALITLINDVLDRAKIEAGKLELEAVPFDLRSLMDDVISLFSSKSREKCIELAVFVCDDVPKVVIGDPWRYRQILTNLVGNAVKFTERGHVFVRVCLAENSKVEANQVLNGTMNGKDGKVETTANGAFNTLSGFQAADERNNWDYFKLLLSDKEPHMDELECDRSYQNDCDCVTLMISIEDTGVGIPLHAQDRVFTPFMQADSSTSRNYGGTGIGLSISKCLAELMGGQISFTSRPFVGSTFTFSAVLKRSCKDTSSDSKRSLSEALPTAFKGMKAILVDGRPVRGAVTRYHLNRLGIVVKVVNNLSMGLQTLAGQNGVKESREKLSMLFIESDIWRPETDILLLNRLHELKNNGQVHELPKLVLLVTSEADKDRYGSAFDIVMYKPIRASTIASCLQQLLKVVMPERKDNQNRPSFLRSLLIGKNILIVDDNKVNLRVAAAALKKYGAKVHCVESGKDAVSLLQQPHCFDACFMDVQMPEMDGFEATRQIRQMEVKANEERKALDLMEGSTFVESHLPVLAMTADVIQATYEECIKSGMDGYVSKPFDEEQLYQAVSRLVVGTKESAV
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Cytokinin receptor related to bacterial two-component regulators. Functions as a histidine kinase and transmits the stress signal to a downstream MAPK cascade.
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A1A6H3
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RBSK_ARATH
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Ribokinase (AtRBSK) (RK) (EC 2.7.1.15)
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MMKGISSVSQSINYNPYIEFNRPQLQISTVNPNPAQSRFSRPRSLRVLSLSADPSANRNPKSAVDAHAPPLVVVGSANADIYVEIERLPKEGETISAKTGQTLAGGKGANQAACGAKLMYPTYFVGRLGEDAHGKLIAEALGDDGCGVHLDYVRSVNNEPTGHAVVMLQSDGQNSIIIVGGANMKAWPEIMSDDDLEIVRNAGIVLLQREIPDSINIQVAKAVKKAGVPVILDVGGMDTPIPNELLDSIDILSPNETELSRLTGMPTETFEQISQAVAKCHKLGVKQVLVKLGSKGSALFIQGEKPIQQSIIPAAQVVDTTGAGDTFTAAFAVAMVEGKSHEECLRFAAAAASLCVQVKGAIPSMPDRKSVLKLLKFSI
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Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway (By similarity). Can also use xylose and fructose as carbohydrate substrates with a low efficiency. Can use GTP, and, to a lower extent, CTP and UTP as alternative phosphoryl donors. {ECO:0000255|HAMAP-Rule:MF_03215, ECO:0000269|PubMed:27601466}.
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A1A6M1
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PTAC5_ARATH
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Protein disulfide isomerase pTAC5, chloroplastic (EC 5.3.4.1) (Protein PLASTID TRANSCRIPTIONALLY ACTIVE 5) (pTAC5)
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MASSSLPLSLPFPLRSLTSTTRSLPFQCSPLFFSIPSSIVCFSTQNPDREEVRWLREEQRWIREEQRWIREEQRWIRERESLLQEISDLQLRIQSLESRNSQLGNSIPDTISNIAALLQVLKEKNRISESGLSATPMVLESTREQIVEEVEEEEKRVIIAEEKVRVSEPVKKIKRRILKVGSEGDDVQALQEALLKLGFYSGEEDMEFSSFSSGTASAVKTWQASLGVREDGVMTAELLQRLFMDEDVETDKDEASTMKKEEAGNGAVFTSVTQVPEKKQSIVKDQSDREVDVTQNRVFLLGENRWEDPSRLIGRNKPVDRSESTNTKTRCITCRGEGRLMCLECDGTGEPNIEPQFMEWVGEDTKCPYCEGLGYTVCDVCDGKKNL
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Exhibits zinc-dependent disulfide isomerase activity. Required for seedling and chloroplast development under heat stress, probably by maintaining plastid-encoded RNA polymerase (PEP)-dependent transcription.
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A1ACB2
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HCHA_ECOK1
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Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
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MTVQKSKNPQVDIAEDNAFFPSEYSLSQYTSPVSDLDGVDYPKPYRGKHKILVIAADERYLPTDNGKLFSTGNHPIETLLPLYHLHAAGFEFEVATISGLMTKFEYWAMPHKDEKVMPFFEQHKSLFRNPKKLADVVASLNADSEYAAIFVPGGHGALIGLPESEDVAAALQWAIENDRFVISLCHGPAAFLALRHGDNPLNGYSICAFPDAADKQTPEIGYMPGHLTWYFGEELKKMGMNIINDDITGRVHKDRKVLTGDSPFAANALGKLAAQEMLAAYAG
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Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress. {ECO:0000255|HAMAP-Rule:MF_01046}.
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A1B198
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HPBD_PARDP
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4-hydroxyproline betaine 2-epimerase (Hyp-B 2-epimerase) (EC 5.1.1.22) ((4R)-4-hydroxyproline betaine 2-epimerase)
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MKIAEIHVYAHDLPVKDGPYTIASSTVWSLQTTLVKIVADSGLAGWGETCPVGPTYAPSHALGARAALAEMAPGLIGANPLQPLVLRRRMDGLLCGHNYAKAAIDIAAYDLMGKHYGVRVADLLGGVAAERVPSYYATGIGQPDEIARIAAEKVAEGFPRLQIKIGGRPVEIDIETVRKVWERIRGTGTRLAVDGNRSLPSRDALRLSRECPEIPFVLEQPCNTLEEIAAIRGRVQHGIYLDESGEDLSTVIRAAGQGLCDGFGMKLTRIGGLQQMAAFRDICEARALPHSCDDAWGGDIIAAACTHIGATVQPRLNEGVWVAQPYIAQPYDEENGIRIAGGHIDLPKGPGLGITPDESLFGPPVASFS
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Catalyzes the 2-epimerization of trans-4-hydroxy-L-proline betaine (tHyp-B) to cis-4-hydroxy-D-proline betaine (cHyp-B). Is involved in a catabolic pathway that degrades tHyp-B to alpha-ketoglutarate. This pathway would permit the utilization of tHyp-B as a carbon and nitrogen source in the absence of osmotic stress, since tHyp-B functions as an osmolyte and is not catabolized when it is needed as osmoprotectant. Can also catalyze the racemization of L-proline betaine.
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A1B2F3
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AZTC_PARDP
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High-affinity zinc uptake system protein AztC
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MKDWLFRIATCSIMTFSSLAAAQAEPLDVVATFSIIGDFAAKVGGDRIRLNVLVGPDSDTHVYEPRPADAIALAGADVVLTNGLEFEGFLTRLIAASGTDAAVATLTDGVETMEEPGGGHYHYIDGKAVFHAGAHDPHAWQAVPNAKVYVQNIAAAFCAADAEGCAAYQANAARYIGELDALDTEIRAAIAALPQDRRTVVVAHNAFRYFEAAYGVHFLSPQGVSTESEAAAADVAGLIREIRARNASAIFAENISDTRLLEQIAREAGLPLAGTLYSDALSGPDGPASNYIAMMRHNAGAIAAALAAR
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Part of the ATP-binding cassette (ABC) transport system AztABCD involved in zinc import. Binds zinc with high affinity and specificity and delivers it to the membrane permease for translocation into the cytoplasm.
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A1B2F4
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AZTD_PARDP
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Zinc chaperone AztD
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MLRHLAGASALALTLAGAGFAQDHDHDHEDVTLYRVFVGDHEKGQVTAFDLAEPDHRWTFPTTGQVKLYSVAGGAVVAAVQSDADTVQFIRSGISFHDHGDHRDIEVGDPAAIDASLTGPRPFHLVEHDGKVVLNYDQGGYAEILDGHALAEGKAEPGRFPQARAHHGFVAPLGGNWLSTVASDEKVEGDASVPRLGLQAFDAEGNPAGNLATCTGIHGEAFSGAYLAAGCKEGVLTVKAGANGSEYKLLPYPADLPQGVTTGTLLGSTGIQVFLGNYGPDGLVVIDPVDEPHYRYIKLPFRRVDFALDPAKPSTGYVLTEDGSLHRIDLLKAEIVASAKVTEPYSMDGHWNDPRPRIAMAGDEIVVTDPNAGLVRRIATEDLSERGTVPVEGKPYNIAVTGGSGVTH
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Acts as a zinc chaperone in the AztABCD zinc transport system. Directly transfers one zinc cation to the solute binding protein AztC the transfer occurs without the formation of a stable interaction. Binds 3 Zn(2+), two with high affinity and one with low affinity, and transfers only Zn(2+) bound to site 2 to AztC. Likely functions to store zinc in the periplasm and may be important for zinc accumulation in zinc-limited environments.
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A1B8Z0
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BHCD_PARDP
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Iminosuccinate reductase (EC 1.4.1.-)
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MLVVAEKEIAGLMTPEAAFEAIEAVFASMARRKAYNFPVVREAIGHEDALYGFKGGFDASALVLGLKAGGYWPNNQKHNLINHQSTVFLFDPDTGRVSAAVGGNLLTALRTAAASAVSIKYLAPKGAKVLGMIGAGHQSAFQMRAAANVHRFEKVIGWNPHPEMLSRLADTAAELGLPFEAVELDRLGAEADVIVSITSSFSPLLMNEHVKGPTHIAAMGTDTKGKQELDPALVARARIFTDEVAQSVSIGECQHAIAAGLIREDQVGELGAVVAGDDPGRGDAEVTIFDGTGVGLQDLAVAQAVVELAKHKGVAQEVEI
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Imine reductase that catalyzes the NADH-dependent reduction of iminosuccinate to L-aspartate. Is essential for the growth of P.denitrificans in the presence of glycolate and glyoxylate since it functions in glyoxylate assimilation via the beta-hydroxyaspartate cycle (BHAC). Thereby BhcD regenerates the amino group donor for the first step of the BHAC.
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A1B8Z1
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BHCC_PARDP
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3-hydroxy-D-aspartate aldolase (EC 4.1.3.41) (beta-hydroxyaspartate aldolase)
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MNAKTDFSGYEVGYDIPALPGMDESEIQTPCLILDLDALERNIRKMGDYAKAHGMRHRSHGKMHKSVDVQKLQESLGGSVGVCCQKVSEAEAFARGGIKDVLVTNEVREPAKIDRLARLPKTGATVTVCVDDVQNIADLSAAAQKHGTELGIFVEIDCGAGRCGVTTKEAVVEIAKAAAAAPNLTFKGIQAYQGAMQHMDSFEDRKAKLDAAIAQVKEAVDALEAEGLAPEFVSGGGTGSYYFESNSGIYNELQCGSYAFMDADYGRIHDAEGKRIDQGEWENALFILTSVMSHAKPHLAVVDAGLKAQSVDSGLPFVYGRDDVKYIKCSDEHGVVEDKDGVLKVNDKLRLVPGHCDPTCNVHDWYVGVRNGKVETVWPVSARGKGY
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Catalyzes the condensation of glyoxylate and glycine into (2R,3S)-beta-hydroxyaspartate ((3S)-3-hydroxy-D-aspartate). Is essential for the growth of P.denitrificans in the presence of glycolate and glyoxylate since it functions in glyoxylate assimilation via the beta-hydroxyaspartate cycle (BHAC). Is also able to catalyze the reverse reaction in vitro, i.e. the cleavage of (3S)-3-hydroxy-D-aspartate, and that of D-threonine to a lesser extent.
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A1BPI0
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OAZ3_RAT
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Ornithine decarboxylase antizyme 3 (AZ3) (ODC-Az 3)
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MPCTRSRPSLYSLSYIKRGKTRNCLYPFWSPYAYYLYCYKYRITLREKMLPCCYRSITYKEQEDLTLRPHCCLPCSCLPYSCLPCSESLEGLQVGRSTAQEKDHSQLKELYSAGNLTVLSADPLLHQDPVQLDFHFRLTPHSSAHWHGLLCDHQLFLDIPFQALEQGNRESLTATLEYVEEKTNVDSVFVNFQSNHKDRGALLRAFSYMGFEVVRPDHPALPPWDNVIFMVYPLERDLGQPGQ
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Ornithine decarboxylase (ODC) antizyme protein that negatively regulates ODC activity and intracellular polyamine biosynthesis and uptake in response to increased intracellular polyamine levels. Binds to ODC monomers, inhibiting the assembly of the functional ODC homodimers. Does not target the ODC monomers for degradation, which allows a protein synthesis-independent restoration of ODC activity. Stabilizes AZIN2 by interfering with its ubiquitination. Involved in the translocation of AZNI2 from ER-Golgi intermediate compartment (ERGIC) to the cytosol. Probably plays a key role in spermatogenesis by regulating the intracellular concentration of polyamines in haploid germ cells (By similarity).
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A1C2U6
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GDF8_MACMU
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Growth/differentiation factor 8 (GDF-8) (Myostatin)
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MQKLQLCVYIYLFMLIVAGPVDLNENSEQKENVEKEGLCNACTWRQNTKSSRIEAIKIQILSKLRLETAPNISKDAIRQLLPKAPPLRELIDQYDVQRDDSSDGSLEDDDYHATTETIITMPTESDFLMQVDGKPKCCFFKFSSKIQYNKVVKAQLWIYLRPVETPTTVFVQILRLIKPMKDGTRYTGIRSLKLDMNPGTGIWQSIDVKTVLQNWLKQPESNLGIEIKALDENGHDLAVTFPGPGEDGLNPFLEVKVTDTPKRSRRDFGLDCDEHSTESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGECEFVFLQKYPHTHLVHQANPRGSAGPCCTPTKMSPINMLYFNGKEQIIYGKIPAMVVDRCGCS
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Acts specifically as a negative regulator of skeletal muscle growth.
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A1C3L3
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FAP1_STRPA
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Fap1 adhesin (Adhesin Fap1) (Fimbriae-associated protein Fap1) (Serine-rich repeat protein Fap1)
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MGKYKRAGETSRKTRVKMHKSGKNWVRTLISQIGLMHFLGGSISEKKINVDVYEQKNISASTILKGAVALGALTGATVVSGNVFADETVLAKETTLTTTDANEVKLSSENFDSEKAEEKISLSQSESASESVSESISESVSESVSTSESVSESVSESVSESISESVSESISESISESVSESTSTSIVLSESGAASGNKATSKGTEEKQDSVRENLDKMISEAEVLNDMAARKLITLDAEQQLELMKSLVATQSQLEATKNLIGDPNATVADLQIAYTTLGNNTQALGNELIKLNPNGQIYAVLNNTEASRAATLRSTTTGTKTTFTISDFSNGGTQYYWAGGNANNLKNPISSISAVYDSATGKISWTVEYDPTTILKSPALKTLKTYTGIYIDTSSDSKLSTPTNVLIDGAATNPVTNFYGNGSKGIEYVSKGTTKGVTKHTITFDTAFSGRANDLADLKIKMLAATTLSDPHFYEDGSKGNYGRYNGQTAPYVIANDSGTAIGGYQVSGVNADSIPSDTTSQSESTSKSESTSKSISESVIESISESVIGSVSESVSESVSESVSESITESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESISESVSESVSESVSESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESVSESVSESISESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESISESVSESVSESISESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESVSESVSESVSESVSESISESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESVSESVSESVSESISESVSESVSESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESISESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESISESVSESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESVSESVSESVSESISESVSESVSESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESVSESVSESISESVSESVSESISESVSESVSESVSESVSESVSESISESVSESISESVSESVSESISESVSESVSESISERTLPNTGENVSSSLGLVGLSGLLFGALLGRKKRKSEDAE
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The major structural element of fimbriae. Required for adherence to saliva-coated hydroxyapatite beads (SHA), an in vitro tooth model. A Fap1-dependent increase in adherence is seen as the pH is reduced from pH 8 to pH 5.
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A1C3L9
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GTFA_STRPA
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UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase GtfA subunit (EC 2.4.1.-) (Glycosyltransferase Gtf1) (Glycosyltransferase GtfA)
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MTIYNINLGIGWASSGVEYAQAYRAQILRSLGMPAKFIFTNMFQSENLEHFTKNIGFEDNEIIWLYGYFTDVKISGTTYKKDDLEATFSQCPTKKEASSDRKLIRYYFENQELYINASLYGENQEYVQRVEYVVKGKLIRKDYYSYTKVFSEFYSPGENGVQLCNRSFYNEDGSIAYEEILSNEKSTFVFSNKICYGLEELLEFMLEDLSLTKSDLILLDRATGIGQVVFENIGAAKLAVVIHAEHFNEKNTDEHNILWNNYYEYQFTNADKVNAFITSTERQKILLEEQFTQYTSLHPKIVAIPVGSLDQLKFPEQSRKSFSMMTGSRLAIEKHIDWLIEGVALAQKRLPELTFDIYGEGGERRKLTELLTKLHAGEFIELKGHKQLDEIYQNYELYLTASTSEGFGLTLMEAVGSGLPIIGFDVPYGNQTFVCSGENGLLIERPKGDDRSRIVQAFADSIYEYFTKFKMADAQQYSYNIAENYKHEKLVERWKDFIEEMLND
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Required for polymorphic O-glycosylation of serine-rich repeat protein Fap1. Catalyzes the first step in glycosylation by transferring N-acetylglucosamine from UDP-GlcNAc to serine residues in Fap1. Part of the accessory SecA2/SecY2 system specifically required to export Fap1, a serine-rich fimbrial adhesin encoded upstream in the same operon. The GtfA-GtfB (Gtf1-Gtf2 in this bacteria) complex adds GlcNAc from UDP-GlcNAc to Fap1, attaching the first sugar residue. Cannot use not UDP-Glc as substrate. This subunit has very low glycosyltransferase activity the GtfB stabilizing protein enhances membrane association, protease resistance and glycosyltransferase activity.
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A1C3M0
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GTFB_STRPA
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UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase stabilizing protein GtfB (Glycosyltransferase chaperone Gtf2) (Glycosyltransferase stabilizing protein GtfB) (Glycosyltransferase-stabilizing protein Gtf2)
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MIRLFEWLTQESLDLHYSLEESGIHGTSIVLNDDGFLPEGIISPYTFFCEVEMDGSPLYFNQLEVPYLWQITGTNIEGEIWNRSSKRGVIHYHEPKYLRFVQSVDWLYPDGSIYMTDHYNKYGWAFARTYFFSDQQVSHKKYYTKSGQEVLSENILTGDILLNWKGKVYHFTKKVDFFLFYFKKSGLDLSSIWYNSLGMPFLISYYLGGEGRDILFWQENLADQLPGNMQIIFSGRTSRTKKVIVQDRSVYKKLLHLVEEKNKEMISFLNIIYPKLRENYSRKEILIVTNSDQIEGIETLTDNLSAYTFHIGALTSMSDKLQNIGQKENVLLYPNMSPKTMLDLLEQCDIYLDINHGNEVLSIVRLAFERSLLILAYDNTVHSPIFHHESGIFNHSKPQTLSDWLLNLDDYSQTVSCWRSDLFPMTYRDYKQVLVSNVD
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Required for the polymorphic O-glycosylation of the serine-rich repeat protein Fap1. A stabilizing protein that is part of the accessory SecA2/SecY2 system specifically required to export Fap1, a serine-rich fimbrial adhesin encoded upstream in the same operon. The GtfA-GtfB (Gtf1-Gtf2 in this bacteria) complex adds GlcNAc from UDP-GlcNAc to Fap1, attaching the first sugar residue. Cannot use not UDP-Glc as substrate. Stabilizes the glycosylation activity of GtfA, causing it to partially localize to the cellular membrane where it is more protease resistant.
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A1C8C3
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OBLA_ASPCL
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Ophiobolin F synthase oblA (acOS) (Bifunctional sesterterpene synthase oblA) (Ophiobolin biosynthesis cluster protein A) [Includes: Ophiobolin F cyclase (EC 4.2.3.145); Geranylgeranyl diphosphate synthase (GGDP synthase) (GGS) (EC 2.5.1.29); Geranylfarnesyl diphosphate synthase (GFDP synthase) (EC 2.5.1.81)]
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MACKYSTLIDSSLYDREGLCPGIDLRRHVAGELEEVGAFRAQEDWRRLVGPLPKPYAGLLGPDFSFITGAVPECHPDRMEIVAYALEFGFMHDDVIDTDVNHASLDEVGHTLDQSRTGKIEDKGSDGKRQMVTQIIREMMAIDPERAMTVAKSWASGVRHSSRRKEDTNFKALEQYIPYRALDVGYMLWHGLVTFGCAITIPNEEEEEAKRLIIPALVQASLLNDLFSFEKEKNDANVQNAVLIVMNEHGCSEEEARDILKKRIRLECANYLRNVKETNARADVSDELKRYINVMQYTLSGNAAWSTNCPRYNGPTKFNELQLLRSEHGLAKYPSRWSQENRTSGLVEGDCHESKPNELKRKRNGVSVDDEMRTNGTNGAKKPAHVSQPSTDSIVLEDMVQLARTCDLPDLSDTVILQPYRYLTSLPSKGFRDQAIDSINKWLKVPPKSVKMIKDVVKMLHSASLMLDDLEDNSPLRRGKPSTHSIYGMAQTVNSATYQYITATDITAQLQNSETFHIFVEELQQLHVGQSYDLYWTHNTLCPTIAEYLKMVDMKTGGLFRMLTRMMIAESPVVDKVPNSDMNLFSCLIGRFFQIRDDYQNLASADYAKAKGFAEDLDEGKYSFTLIHCIQTLESKPELAGEMMQLRAFLMKRRHEGKLSQEAKQEVLVTMKKTESLQYTLSVLRELHSELEKEVENLEAKFGEENFTLRVMLELLKV
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Bifunctional sesterterpene synthase part of the gene cluster that mediates the biosynthesis of the sesterterpenes ophiobolins, fungal phytotoxins with potential anti-cancer activities. The first step of the pathway is performed by the sesterterpene synthase oblA that possesses both prenyl transferase and terpene cyclase activity, converting isopentenyl diphosphate and dimethylallyl diphosphate into geranylfarnesyl diphosphate (GFPP) and further converting GFPP into ophiobolin F, respectively. Other sesterterpenoids (C(25) terpenoids) are found as minor products of oblA. It is expected that ophiobolin F is then oxidized to ophiobolin A via ophiobolin C and ophiobolin B intermediates by the combined action of the cytochrome P450 monooxygenase oblB and the FAD-dependent oxidoreductase oblC (Probable). Although oblB catalyzes multistep oxygenations at C5 and C21/C7 in a relatively efficient manner, it is unable to convert ophiobolin F to ophiobolin C and produces instead several unexpected derivatives.
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A1C9U5
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SKP1_ASPCL
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E3 ubiquitin ligase complex SCF subunit sconC (Sulfur controller C) (Sulfur metabolite repression control protein C)
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MSTTVTLTSSDGVDLTVDRDVAERSVLIKNMLEDLGESGEAIPIPNVNEVVLKKVIEWCTHHKNDPPSTGDDDDSRRKTTDIDEWDQKFMQVDQEMLFEIILAANYLDIKALLDVGCKTVANMIKGKSPEEIRKTFNIQNDFTPEEEDQIRRENEWAEE
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Essential component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes, which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. Controls sulfur metabolite repression, probably by mediating the inactivation or degradation of the metR transcription factor (By similarity).
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A1CAZ7
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UBA4_ASPCL
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Adenylyltransferase and sulfurtransferase uba4 (Common component for nitrate reductase and xanthine dehydrogenase protein F) (Ubiquitin-like protein activator 4) [Includes: Molybdopterin-synthase adenylyltransferase (EC 2.7.7.80) (Adenylyltransferase uba4) (Sulfur carrier protein MOCS2A adenylyltransferase); Molybdopterin-synthase sulfurtransferase (EC 2.8.1.11) (Sulfur carrier protein MOCS2A sulfurtransferase) (Sulfurtransferase uba4)]
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MENLEQTCASLRAQIAATEAQLAGLKRDLEVAEQAAAEIKAQDVKSTGIREEGSEKKNPWPLLSEEYKRYGRQMIVPQLGLQGQLKLRSARVLIVGAGGLGCPAALYLAGAGVGTLGLVDGDTVEHSNLHRQVLHRSKNVGKFKVDSAIEYLRELNPHPTYVPYRAHLTPQEAPEIFKDYDIVLDCTDNPATRYLISDTAVLLGKPLVSASALRTEGQLIVLNNPPRPVGDKSGGPCYRCVFPKPPPATSVVSCADGGIIGPVVGTMGVLQAIEAIKVITSSPADETSASPPSLLIFSAYSTPPFRSIKIRSRRANCAVCSAEASVTVETLKTGSTDYVFFCGVAGPETLLRPEERITPLEFKKKHPGQVSHEQELGGSKEPTIIDVREQVQFDICSLDNSINIPISTILSSAASPTTSTPESLPSWLPHDIVSSSSTDPIYVVCRLGNDSQIAVRKMKELGLDQGGKRFICDIQGGLRAWREQIDPDWPEY
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Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers urm1 and mocs2a. Its N-terminus first activates urm1 and mocs2a as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to urm1 and mocs2a to form thiocarboxylation (-COSH) of their C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as nucleophile towards urm1 and mocs2a. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor nfs1 probably acting as a sulfur donor for thiocarboxylation reactions (By similarity).
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A1CLY8
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CCSA_ASPCL
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Polyketide synthase-nonribosomal peptide synthetase (PKS-NRPS) (EC 2.3.1.-) (EC 6.3.2.-) (Cytochalasin biosynthesis protein A)
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MGSFQNSSEPIAIIGTGCRFPGGCDSPSKLWELLRAPRDLLKEIPESRFSVDSFYHPDNAHHGTSNVRHSYFLEEDLRQFDVQFFGIKPIEANAVDPQQRLLLETVYEGLESAGLSIQRLQGSDTAVYVGVMSADFTDLVGRDTETFPTYFATGTARSILSNRLSYFFDWHGPSLTIDTACSSSLIAMHHAVQTLRSGDSSLAIVAGSNLILGPEQYIAESKLQMLSPTGRSRMWDAAADGYARGEGVAAIVLKRLSQAIADGDHIECVIRETGVNQDGKTPGITMPSATAQAALIRSTYAKAGLDLSNRSDRPQYFEAHGTGTPAGDPIEARAIQTAFFGPDLNFTADSRKDTLFVGSIKTVVGHTEGTAGLAAVIKASLALQSGTIPPNRLLEQLNPAIKPFYNSLKILAAAEDWPQLSRGGVRRVSVNSFGFGGANSHAILESYEPSLHSHKGTRDISFSPFTFSAASETALVASLRAYRDLLSTRSDVRLTDLAWTLNSRRSTLASRVAIAASDKDDLVLKLDDRAENYDGSDTFMDAGHRKPNANELRILGVFTGQGAQWARMGAELIEQCPGASKVVDALEQSLRSLPPQDRPTWSLREQLLAPPSSSMVSTASISQPLCTAIQIMLVDMLREAGIQFSAVVGHSSGEIGAAYAAGCLSAKDAIRVAYYRGVHLKSALQKGSMLAVGTTFEDAQDLCNLPTFEDRLCVAASNSPSSVTISGDSDAIEEIKVVFDEEKKFTRLLKVDRAYHSHHMQDCVEPYVRSLRQCSVTFRPPNRNQCVWISSVFVQDIHQLSEDGSDRYWGSNLARPVMFAEALQLLLSLEGSFDLAVEVGPHPALKGPASQTIQDALGYSIPYTGVLSRGNSDVEAFAAALGSIWTAFGDGAVDFSRLQKFTSGSAAQPQLLKGLPTYQWDHNRVFWHESRVSKAFRTRKDVPNELLGRQVLDGAPNQLRWRNILRPREIAWLEGHQVQGQMVFPCAGYVSACAEASMRLAVGQNVESIELEEFVVGQAIVFNDSNSEVETLATLTEVVHRQQTISANFAFYSCPTGGESLELVRNASCRLRITVGDSAVDLLQPQAEADFALLEVESDRFYNALGQLGFGYTGPFRSLTALKRKLGIARGLIENAPPSFNHSQPLLIHPATLDAAIQSIMLAYCYPGDSMLRAIHLPTGIEKLTLNPVNCLKFAGQSVQVPFDSSASTGSGRSLQGDVSIYSLDGSRAVQLEGLQTQPLSSPTEASDLNIFTELVWGVDRPDCEEILRTTVVEDFDAELLFSLERVAYFYLRSLGEAVPERERNGLEWHHKRLFAYVDHVLSRVARGVNRFARPEWAADSKNDILKILQKYPDNIDLRLMRAVGENLPAVVRGQLTMLEPMIQDNMLNDFYVIAHGMPRYTKYLAAMASQISHRYPHMNVLEIGAGTGGATKSFLKELGEGFSTYTFTDISSGFFEKASQVFASYSAKMNFKVLDIEKDIESQGFAPESFDLIIASLVLHATRDLAQTVRNVRRLLKPGGYLLLLEITENEQMRFGLIFGGLPGWWLGYEDGRPFSPCVDIEEWSRVLEQNGFSGIETAIPHHDTLPAPLSVIVSQAVNEKVQFLHNPLDSIRGSTVIPRLTIIGGGGRRSAQLIDAVSSLVQPQCGQLRVVDSLQKICSEVLPVGGSVLSLTDFDEPVFKSMDADKLRGFQEIFKQSKNVLWVTQGSRSGDPYARMVVGFGRTIVLEMLHLRLQFLDVSPSSSPDASAIAEAMLRLEVSGSWEDEGAEDGAVLHSVEPELSISDGRCWVPRFKPNKEQNERYNSVRRSIETEQSFSDTCVELVYRDNSLSLLEVTHSSSEPLAEPSTKYLELDVNYSVSKAVEVVPGCYLFLILGRDTDTGDRFIALSPKQSSRVRIPRALVLPQHTSHGTINENSLDAFFHEIVARSILRDVPYGSAAIALQPNSLLADALREAAQDKGVTLHLWSTQASDLESEWTYIHRKASKTEVQNAIPRNVTCFFDMGGDESIATKILACLPDHTQAKKEASITAHEAHLIPTVLPDIRSLLMDIGRAMRTRGKSSSPDLRIVDLTDIVKGQADSETSIINWLESSSRVPVAVEPIEARVQFRSDRTYWLVGLTGGLGLSLCEWMAQQGARYIVLSSRSPKVDGRWLAKMNRMGVTVEVVANDISNRDSVQRVYNKIRTELPPISGVAQGAMVLHDTMFLDLDMERMNKVLRPKVDGSTYLEEIFHDTELEFFVFFSSMAAVTGNPGQSAYAAANMFMASLANQRRQRGLNASAVHIGAIFGNGYVTRELTLVQQEFLRKVGNLWLSEHDFRRLFAEAVYAGRHHRGRSPELSTGLKILESDESESITWFNNPVFQHCIKQSGRVDLISETSTSAAPVKVRLAEASSSADIYDIISDAFVTKLKTSLQVEGDRPIVDLTADTLGIDSLVAVDIRSWFIKELQVEIPVLKILSGATVGEMVTQAQELLPKELTPNLDPNAEAKPSKPKNTVQPKQQTKKTIQLQNVAKAPQPALSQQVSSGVQNMIKTNPPKEAEAKQPRPEVKQAAPKDSQYPTALETPSKLQDPSRNIVVAKDLAAEEKHLTDQEPVPSNMSSSSWSEIDESEGKVETSSSSSSTSASQIITKTKPVEVKKSVPMAFGQSRFWFLRHYLEDPSSFNITVSIQLDGPLKIDHFARAVQVVGQRHEALRTRFVTDEAQGTTKQEVLALSNLTLEERTISTDEEAEGVYQELKGYAFDLEKGENIRIILLKRSNRSFTLIIAYHHINMDGVSLEVLLRDLQMAYDSKFLSPRILQYADFSEQQRRDYQSGKWAEDLAFWKKEFQTMPGPLPLLSMARTSTRSPLTAYKTHSAEFHIDPATLDTIQSTCQRMKVTPFHFHLAVFYTMLIRLVDVENLCIGISSANRSQQDTLQSVGLYLNLLPLNFTPQLDQTFTNVLHIVREKSVQAFAHSKVPFDVIVNELGAARSATHSPLFQVLVNYRAGVSERRSFCNCDSKVLTFEQGQTPYDLSLDVIDNPGGDCHVIMAGQSVLYGAEHVAVLRGVYQNLLVAFSRNPALRLNVPPLYDTDEVKHAIKLGHGPAYNYQWPATIPERIDEIVERYPTHVALIDGDGRKMSYTEMARRVNTLAVVLLRQDIGQGSKVGVFMEPGSSWICSLLAILRLDAIYIPLDSRMGLDRLSTIVRDCKPDLLLVDNTTLSNVALLGLSCPTLNVDVVSPGSDQQHVPNTAQPSSTAVIMYTSGSTGVPKGIVMQHHTFRNNIETSTEKWDFREGRETTLQQSSYSFDMSLSQTFLTLSNGGTLRIVPKKLRGDPKAIASLITAEGITFTETTPSEYISWLRYGDVDDLRKSKWRIAVSGGETITTNLTGLLRQLEKSDLRLIDCYGPTEITFCSHGREVQYDGEGDILSPAFRTWPNYSVYIVDSHMKPVPIGIPGEILIGGAGVVAGYVHSELDARGFARNNFMNTMFLENAWTRLHRTGDFGRLDQEGNLILGGRIAGDTQVKLRGIRIDLQEIESAILSSGDGKIVDAAVTVRESADSGSEYLMAFVTTLDAGDLSLERIRQELPLPQHMRPANIITLDQLPMTASNKVDRLALKSLPLPPGSHVADTGTDESPSMAKMRDVWATVIPQEVLAHFELGPASNFFQVGGDSMLLVRLQTEINKVFGTSISLFQLFDASSLTGMVSLIDHSESTSQRSEVDWETETTISPSLLQVPATKRFFAHPAVVVLTGATGFLGRAIVNRLLKDCSVQKIHCVAVRRDPSSLPDDFKSPKVVLHRGDLTLPQLGLTDRAATEIFAEADAVIHNGADVSFMKTYQSLKQANLEATKELVRLSAPHRLSFHYISSASVTRLAGQESFDQSSVSAFPPSAEDGYVASKWASERYLEKVSDQCGLPIWIHRPSSIVGEGAPDTDMMASLLGYSRTLRAIPQTDGWTGWLDFVSADRVAMQIADEVYEDYSWPGTVKYLYEAGDREIPLSDLRGVLERETGESFESIPLEEWVLRAEGQGLHPLLGEYLRRVSGIPLVLPRLVQQGSFF
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Hybrid PKS-NRPS synthetase part of the gene cluster that mediates the biosynthesis of the mycotoxins cytochalasins E and K. The hybrid PKS-NRPS synthetase ccsA and the enoyl reductase ccsC are responsible for fusion of phenylalanine with an octaketide backbone and subsequent release of the stable tetramic acid precursor. The polyketide synthase module (PKS) of the PKS-NRPS ccsA is responsible for the synthesis of the octaketide backbone. The downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the octaketide with a phenylalanine. A reductase-like domain (R) at the C-terminus catalyzes the reductive release of the polyketide-amino acid intermediate. Because ccsA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase ccsC. Upon formation of the 11-membered carbocycle-fused perhydroisoindolone intermediate, a number of oxidative steps are required to afford the final cytochalasin E and K, including two hydroxylations at C17 and C18, one alcohol oxidation at C17, one epoxidation at C6 and C7 and two Baeyer-Villiger oxidations. The oxidative modification at C17, C18 and the C6-C7 epoxidation are likely to be catalyzed by the two cytochrome P450 oxygenases ccsD and ccsG. CcsD may be responsible for the epoxidation of the C6-C7 double bond. CcsG may be responsible for the successive oxidative modifications at C17 and C18. The double Baeyer-Villiger oxidations of ketocytochalasin to precytochalasin and cytochalasin Z(16) are among the final steps leading to cytochalasin E and K and are catalyzed by ccsB. The first oxygen insertion step follows that of the classic BVMO mechanism, generating the ester precytochalasin. Release of precytochalasin into an aqueous environment can generate the shunt product iso-precytochalasin through spontaneous isomerization. Alternatively, precytochalasin can undergo further oxidation by ccsB to yield the in-line carbonate-containing cytochalasin Z(16). Cytochalasin Z(16) is a precursor to cytochalasin E and cytochalasin K, whereas iso-precytochalasin is a precursor to cytochalasin Z(17) and rosellichalasin. The hydrolyase ccsE may catalyze hydrolysis of epoxide bond in cytochalasin E to afford cytochalasin K. The function of ccsF has not been assigned but it may play a role in post-PKS-NRPS biosynthetic step, resistance or transport of cytochalasins and related PKS-NRPS products.
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A1CP85
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ARO1_ASPCL
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Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); Shikimate dehydrogenase (EC 1.1.1.25)]
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MIEPTKISILGQESIVADFGLWRNYVAKDLISGCPSTTYVLITDTNIGSIYTPSFQKSFEEAAAAVTPSPRLLTYYAPPGEVSKSRQTKADIEDWMLSQSPPCGRDTVIIALGGGVIGDLTGFVAATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPARIYIDLEFLETLPVREFINGMAEVIKTAAISSEEEFTALEDNAETILAAVRREVKPGQRRFDGIEQILKARILASARHKAFVVSEDEREGGLRNLLNWGHSIGHAIEAILTPQILHGECVAIGMVKEAELARHLGVLKGVAVARIVKCIAAYGLPTSLKDARIRKLTAGKHCSVDQLLFNMALDKKNDGPKKKVVLLSAIGRTYEPRASVVANEDIGVVLAPSIEVFPGVSPKSTVICAPPGSKSISNRALVLAALGSGTCRIKNLLHSDDTEVMLNALERIGAATFSWEEEGEVLVVNGKGGALQAHPSELYLGNAGTASRFLTTVATLATPSNVDFSILTGNNRMKQRPIGDLVEALIANGAQVEYMESKGSLPLKIAASGGFTGGQINLAAKVSSQYVSSLLMCAPYAKEPVTLKLVGGKPISQPYIDMTTAMMRSFGIDVQKSTTEEHTYHIPQGRYTNPAEYVVESDASSATYPLAIAAVTGTTCTVPNIGSKSLQGDARFAVDVLRPMGCTVEQTDTSTTVTGPADGVLRPLPNVDMEPMTDAFLGASVLAAIARGEGSNHTTRIYGIANQRVKECNRIKAMHDELAKFGVVCREHEDGLEIDGIDRANLRQPAGGVFCYDDHRVAFSFSVLSLVAPKPTLILEKECVGKTWPGWWDTLRLKFAVKLEGRELKEAESPVLTSAEKASASVFIIGMRGAGKTTSGHWVASTLNRPFIDLDDELERIEGMTIPDIIKERGWQGFRDAELSLLQRTMKERPTGHVFACGGGVVEVPEARKLLINWHKSKGNVLLIMRDIKQVMDFLNIDKTRPAYVEDMMGVWLRRKPWFQECSNIQYYSQHASSGLTRASEDFARFVKIVTGQVDSLGAIKKKQHSFFVSLTLPDLRPAGDILEQACVGSDAVELRVDLLKDPSSSNGIPSVDYVAEQMSFLRSHTTLPLIFTIRTKSQGGFFPDEAHEEAMQLYQLAFRSGCEFVDLEIAFPDELLRTVSEMKGYSKIIASHHDPKGELSWANMSWMKYYNRALEYGDVIKLVGVATKLDDNTALRKFKSWAEEAHDVPLIAINMGDNGQLSRILNGFMTPVSHPALPFKAAPGQLSATEICKGLSLMGQIKKKRFALFGTPISESRSPALHNSLFAELGLPHEYTRLETANAEDVKEFIRAPDFGGASVTIPLKLDIMPLLDEIAPEAEIIGAVNTIVPVSDGEGKPQRLVGHNTDWQGMVQCLRNAGAYGSNGDASALVVGGGGTCRAGIYALHQMGYSPIYIVGRNLGKLQAMASTFPSSYNIRILEGNETLEHVPHVAIGTIPGDQPIDPGMREILCHMFARAEEADADAVRSIEGSPRVLLEMAYKPPVTALMQLATDAGWTTIPGLEVLVGQGFYQGGITQFQHWTGIRPLYEHARDAVLGTKAD
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The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}.
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A1CQG2
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RSP5_ASPCL
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Probable E3 ubiquitin-protein ligase hulA (EC 2.3.2.26) (HECT ubiquitin ligase A) (HECT-type E3 ubiquitin transferase hulA)
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MGSNLPSQPNLRLTIIAADGLYKRDVFRFPDPFAVATVGGEQTQTTSVIKKTLNPYWNEMFDLRVNEESILAIQIFDQKKFKKKDQGFLGVINVRIGDVIDLEMGGDEMLTRDLKKSNDNLVVHGKLIINLSTNLSTPNTNQANGLHRSHIQPSTSSGLVPQVGASAAHPAASPAPIDPAASNPSLHPQRVPSTNRPPSTVAPGAAAGATPTNTQGSRTNLSSFEDSQGRLPAGWERREDNLGRTYYVDHNTRTTTWTRPSSNYNEQTQRTQREANMQLERRAHQSRMLPEDRTGANSPNLPETSQQAPTPPAGGSANAVSMMATGATTAGTGELPPGWEQRTTPEGRPYFVDHNTRTTTWVDPRRQQYIRMYGQNANGTNTTIQQQPVSQLGPLPSGWEMRLTNTARVYFVDHNTKTTTWDDPRLPSSLDQGVPQYKRDFRRKLIYFRSQPALRIMSGQCHVKVRRNNIFEDSYAEIMRQSASDLKKRLMIKFDGEDGLDYGGLSREFFFLLSHEMFNPFYCLFEYSAHDNYTLQINPHSGVNPEHLNYFKFIGRVVGLAIFHRRFLDSFFIGAFYKMMLRKKVSLQDMEGVDEDLHRNLTWTLDNDIEGVLELTFAVDDEKFGERRTIDLKPGGRDIPVTNENKGEYVELVTEWKIVKRVEEQFNAFMSGFNELIPADLVNVFDERELELLIGGIADIDVDDWKKHTDYRGYQESDDVIQNFWKVVRTWDAEQKSRLLQFTTGTSRIPVNGFKDLQGSDGPRRFTIEKSGDPVALPKSHTCFNRLDLPPYKTYETLEHKMSIAVEETLGFGQE
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E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Probably involved in the regulatory network controlling carbon source utilization.
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A1CZG3
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SKP1_NEOFI
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E3 ubiquitin ligase complex SCF subunit sconC (Sulfur controller C) (Sulfur metabolite repression control protein C)
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MTTVTLTSSDGVDITVDRDVAERSILIKNMLEDLGESDEAIPIPNVNEVVLKKVIEWCTHHKNDPPSTGDDDDSRRKTTDIDEWDQKFMQVDQEMLFEIILAANYLDIKALLDVGCKTVANMIKGKSPEEIRKTFNIQNDFTPEEEDQIRRENEWAEE
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Essential component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes, which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. Controls sulfur metabolite repression, probably by mediating the inactivation or degradation of the metR transcription factor (By similarity).
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A1D244
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ARO1_NEOFI
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Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); Shikimate dehydrogenase (EC 1.1.1.25)]
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MTGPTKISILGQESIVADFGLWRNYVAKDLISGCPSTTYVLITDTNIGSIYTPGFQKSFEEAAASVSPSPRLLIYNAPPGEVSKSRQTKADIEDWMLSQSPPCGRDTVVIALGGGVIGDLTGFVAATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPLGKNLIGAIWQPSRIYIDLEFLETLPVREFINGMAEVIKTAAISSEEEFTALEDNAETILSAVRREVKPGQRRFEGIEEILKARILASARHKAFVVSADEREGGLRNLLNWGHSIGHAIEAILTPQILHGECVAIGMVKEAELARHLGILKGVAVARIVKCIAAYGLPTSLKDSRIRKLTAGKHCSVDQILFNMALDKKNDGPKKKIVLLSAIGRTYEPRASVVPNEDIGVVLAPSIEVYPGVSPASEVVCAPPGSKSISNRALVLAALGSGTVRIKNLLHSDDTEVMLNALERLGAATFSWEEEGEVLVVNGKGGALQAHPSPLYLGNAGTASRFLTTVATLATASSVDSSVLTGNNRMKQRPIGDLVDALTANGAQIEYVENKGSLPLKIAASGGFTGGQINLAAKVSSQYVSSLLMCAPYAKEPVTLKLVGGKPISQPYIDMTTAMMRSFGIDVKKSTTEEHTYHIPQGRYINPAEYVVESDASSATYPLAIAAVTGTTCTIPNIGSKSLQGDARFAVDVLRPMGCTVEQTDTSTTVTGPADGVLRPLPNVDMEPMTDAFLGASVLAAIARGKDSNHTTRIYGIANQRVKECNRIKAMHDELAKFGVVCREHDDGLEIDGIDRSTLRQPAGGVFCYDDHRVAFSFSVLSLVAPKPTLILEKECVGKTWPGWWDTLRQKFAVKLEGKELKEAESPVLTRAEKASASVFIIGMRGAGKTTSGNWVASTLKRPFIDLDDELERIEGMTIPDIIKQRGWQGFRDAELSLLQRTMKERPTGHVFACGGGVVEIPEARKLLIDWHKTKGNVLLIMRDIKQVMAFLNIDKTRPAYVEDMLGVWLRRKPWFQECSNIQYYSQHASAGLPRASEDFARFIKFVTGLEDSLSTIKKKQHSFFVSLTLPDVRGADQILEQACVGSDAVELRVDLLEDPDSANGIPTVDFVADQISYLRSRITLPVIFTIRTKGQGGRFPDDAHAEAMQLYRLAVRSGCEFVDLEIAFPDEMLRAVTEMKGYSKIITSHHDPKGELSWANMSWMKYYNRALEYGDVIKLVGVARNLDDNTALRKFKNWAEEAHDVPLIAINMGGNGQLSRILNGFMTPVSHPALPFRAAPGQLSATDIRKGLSLMGEIKKKRFALFGSPISESRSPALHNTLFAEMGLPHEYTRLETANVEDVKDFIRAPDFGGASVTIPLKLDIMPLLDEITAEAEIIGAVNTVVPVSDGEGKPQRLVGHNTDWQGMVQCLRNAGAYGADGNASGLVVGGGGTSRAAIYALHHMGFSPIYIVGRNPAKLESMVATFPTGYNIRIVEGNEKLEHVPHVAIGTIPADRPIDPGMREILCHMFERAQEADADAARTIEGSPRVLLEMAYKPRVTALMQLAVDAGWTTVPGLEALIGQGVHQFQHWTGIRPLYERARAIVLG
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The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}.
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A1D3C5
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RSP5_NEOFI
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Probable E3 ubiquitin-protein ligase hulA (EC 2.3.2.26) (HECT ubiquitin ligase A) (HECT-type E3 ubiquitin transferase RSP5)
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MGSNLPAQPNLRLTIIAADGLYKRDVFRFPDPFAVATVGGEQTHTTSVIKKTLNPYWNEMFDLRVNEDSILAIQIFDQKKFKKKDQGFLGVINVRIGDVIDLQMGGDEMLTRDLKKSNDNLVVHGKLIINLSTNLSTPNTNQANGLHRSHVQSSTSSGLVPQVAPSSSHPAASGAAPVDPSASNPSLNPQRVPSTTRPSSTAAPASAAGAAASNTHGSRTNLSSFEDSQGRLPAGWERREDNLGRTYYVDHNTRTTTWTRPSSNYNEHAQRSQREANMQLERRAHQSRMLPEDRTGANSPNLPESSQQAHTPPAGGSANAVSMMATGATTAGTGELPPGWEQRTTPEGRPYFVDHNTRTTTWVDPRRQQYIRMYGQNANGTNTTIQQQPVSQLGPLPSGWEMRLTNTARVYFVDHNTKTTTWDDPRLPSSLDQGVPQYKRDFRRKLIYFRSQPALRIMSGQCHVKVRRNNIFEDSYAEIMRQSASDLKKRLMIKFDGEDGLDYGGLSREFFFLLSHEMFNPFYCLFEYSAHDNYTLQINPHSGVNPEHLNYFKFIGRVVGLAIFHRRFLDSFFIGAFYKMMLRKKVSLQDMEGVDEDLHRNLTWTLDNDIEGVLELTFSVDDEKFGERRTIDLKPGGRDIPVTNENKAEYVELVTEWKIVKRVEEQFNAFMSGFNELIPADLVNVFDERELELLIGGIADIDVDDWKKHTDYRGYQESDEVIQNFWKVVRSWDAEQKSRLLQFTTGTSRIPVNGFKDLQGSDGPRRFTIEKSGDPAALPKSHTCFNRLDLPPYKSYETLEHKMSIAVEETLGFGQE
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E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Probably involved in the regulatory network controlling carbon source utilization.
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A1DED8
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UBA4_NEOFI
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Adenylyltransferase and sulfurtransferase uba4 (Common component for nitrate reductase and xanthine dehydrogenase protein F) (Ubiquitin-like protein activator 4) [Includes: Molybdopterin-synthase adenylyltransferase (EC 2.7.7.80) (Adenylyltransferase uba4) (Sulfur carrier protein MOCS2A adenylyltransferase); Molybdopterin-synthase sulfurtransferase (EC 2.8.1.11) (Sulfur carrier protein MOCS2A sulfurtransferase) (Sulfurtransferase uba4)]
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MENLEQTCASLRAQIAATEAQLAGLKRELEIAEQAAADVKAQDTTITITADEGRINGTRTWPLLSEEYKRYGRQMIVPQVGLQGQLKLRSARVLIVGAGGLGCPAALYLAGAGVGTLGLVDGDTVENSNLHRQVLHRSKNVGKFKVDSAIEYLREAHLTPQEAPSIFKDYDIILDCTDNPATRYLISDTAVLLGKPLVSASALRTEGQLMVLNYPPRPVGDKSGGPCYRCVFPKPPPANSVVSCADGGILGPVVGTMGVLQALEAIKVITSPAVNPSASPPSLLIFSAYSTPPFRTIRLRARRANCAVCSADASVTLETLKIGSTDYVFFCGVAGLEATLSPEERISPLELRKRHPKEVPQDGGSISKEPTIIDVREKVQFDICNLEHSVNIPISTILSSASNAANADANAQPSLPSWLPRELASADSTNPIYVVCRHGNDSQIAVRRLKELGLDRGGQRYVGDIQGGLRAWREQIDPDWPEY
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Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers urm1 and mocs2a. Its N-terminus first activates urm1 and mocs2a as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to urm1 and mocs2a to form thiocarboxylation (-COSH) of their C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as nucleophile towards urm1 and mocs2a. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor nfs1 probably acting as a sulfur donor for thiocarboxylation reactions (By similarity).
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A1E959
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ODAM_HUMAN
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Odontogenic ameloblast-associated protein (Apin)
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MKIIILLGFLGATLSAPLIPQRLMSASNSNELLLNLNNGQLLPLQLQGPLNSWIPPFSGILQQQQQAQIPGLSQFSLSALDQFAGLLPNQIPLTGEASFAQGAQAGQVDPLQLQTPPQTQPGPSHVMPYVFSFKMPQEQGQMFQYYPVYMVLPWEQPQQTVPRSPQQTRQQQYEEQIPFYAQFGYIPQLAEPAISGGQQQLAFDPQLGTAPEIAVMSTGEEIPYLQKEAINFRHDSAGVFMPSTSPKPSTTNVFTSAVDQTITPELPEEKDKTDSLREP
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Tooth-associated epithelia protein that probably plays a role in odontogenesis, the complex process that results in the initiation and generation of the tooth. May be incorporated in the enamel matrix at the end of mineralization process. Involved in the induction of RHOA activity via interaction with ARHGEF and expression of downstream factors such as ROCK. Plays a role in attachment of the junctional epithelium to the tooth surface.
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A1E960
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ODAM_MOUSE
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Odontogenic ameloblast-associated protein (Apin)
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MKIIILLGLIGASSSAPLISQRLLSASNSHELLLNLNNGQLLPLQFQGAFNSWIPPFPGFLQQQQAQVSGRPQFTLSTLESFAGLFPNQIPLSRQVGLAQGGQAGQPDLSQQQTPPQTQQSASPMSYVVPVKVPQDQTQMFQYYPVYMLLPWEQPQTVTSSPQHTGQQLFEEQIPFYNQFGFAPPQAEPGVPGGQQHLAFDSFVGTAPETPGMPVEGSLLYPQKEPISFKHDNAGVFMPTTSPKPSTDNFFTSGIDPTIAPEQKVKTDSLREP
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Tooth-associated epithelia protein that probably plays a role in odontogenesis, the complex process that results in the initiation and generation of the tooth. May be incorporated in the enamel matrix at the end of mineralization process. Involved in the induction of RHOA activity via interaction with ARHGEF and expression of downstream factors such as ROCK. Plays a role in attachment of the junctional epithelium to the tooth surface.
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A1EC31
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TDIF_ZINVI
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CLAVATA3/ESR (CLE)-related protein TDIF (Tracheary element differentiation inhibitory factor) [Cleaved into: TDIFp]
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MDIDLLWSFGGWFFILFPETINYCMAKLRSTSQISHFTNPRSCSSLFFVALLIITILITMLQSSTSMEVTSLPTHQPTSSNSHDESSTSSTATTTTDLHPKRTHHQSHPKPTRSFEAGAHEVPSGPNPISNR
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[TDIFp]: Extracellular signal peptide that regulates cell fate. Represses tracheary element differentiation but promotes the formation of procambial cells adjacent to phloem cells in the veins.
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A1IHE6
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ACMA_GORST
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Acetone monooxygenase (methyl acetate-forming) (ACMO) (EC 1.14.13.226) (NADPH-dependent acetone monooxygenase)
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MSTTTLDAAVIGTGVAGLYELHMLREQGLEVRAYDKASGVGGTWYWNRYPGARFDSEAYIYQYLFDEDLYKGWSWSQRFPGQEEIERWLNYVADSLDLRRDISLETEITSAVFDEDRNRWTLTTADGDTIDAQFLITCCGMLSAPMKDLFPGQSDFGGQLVHTARWPKEGIDFAGKRVGVIGNGATGIQVIQSIAADVDELKVFIRTPQYALPMKNPSYGPDEVAWYKSRFGELKDTLPHTFTGFEYDFTDAWEDLTPEQRRARLEDDYENGSLKLWLASFAEIFSDEQVSEEVSEFVREKMRARLVDPELCDLLIPSDYGFGTHRVPLETNYLEVYHRDNVTAVLVRDNPITRIRENGIELADGTVHELDVIIMATGFDAGTGALTRIDIRGRDGRTLADDWSRDIRTTMGLMVHGYPNMLTTAVPLAPSAALCNMTTCLQQQTEWISEAIRHLRATGKTVIEPTAEGEEAWVAHHDELADANLISKTNSWYVGSNVPGKPRRVLSYVGGVGAYRDATLEAAAAGYKGFALS
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Plays an important role in the metabolism of acetone derived from propane oxidation. Catalyzes the oxidation of acetone to methyl acetate. Exhibits high catalytic efficiency towards various linear and cyclic ketones, such as butanone, 2-pentanone, 2-heptanone, 2-octanone, 2-nonanone, 2-decanone, cyclobutanone, cyclopentanone and cyclohexanone. Elicits the highest catalytic efficiency towards butanone and cyclobutanone. Is highly specific for NADPH and cannot use NADH.
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A1JIG4
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FADB_YERE8
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Fatty acid oxidation complex subunit alpha [Includes: Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC 4.2.1.17) (EC 5.1.2.3) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)]
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MLYQSETLQLHWLENGIAELVFDAPGSVNKLDTQTVANLGEALVVLEKQSELKGLLLRSAKAAFIVGADITEFLSLFNEPPEKLHQWLVFANDIFNRLEDLPVPTIAAINGYALGGGCECILATDFRVASPEARIGLPETKLGIMPGFGGSVRLPRLLGADSALEIIAAGKDIIAKDALKVGLVDAVVAPEKLVDAALSILNQAIDGKLDWQAARRPKLEPLKLNPTEAAMCFTIAKGMVMQVAGKHYPAPLTAVKTIEAAAKFGRAEALILETNSFVPLAGSNEARALVGIFLNDQYVKGQAKKLSKGVSAPKQAAVLGAGIMGGGIAYQSALKGVPVIMKDINDKSLTLGMNEAAKLLNKQLERGKIDGLKMANILATIQPTLDYAGIERAQVIVEAVVENPKVKAAVLAEVETLIGEETVLASNTSTIPIDQLAKSLKRPENFCGMHFFNPVHRMPLVEIIRGTKTSDKTIAAVVAYATQMGKTPIVVNDCPGFFVNRVLFPYLAGFGMLVRDGADFRQIDKVMEKQFGWPMGPAYLLDVVGIDTAHHAQAVMAVGFPERMNKDYRDAVDVMFDNQRFGQKNGQGFYRYTQDTKGKPRKENDEQVDALLAQVSQPLQKFSDDDIIARTMIPMINEVVRCLEEGIIASPAEGDMALVYGLGFPPFHGGVFRYLDTIGSANYVEMAQRYTHLGALYQVPPGLRAKAEHNESYYPVAAALLDVSISQPA
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Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}.
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A1JUB7
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YADA_YERE8
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Adhesin YadA (Protein Yop1) (Trimeric autotransporter adhesin YadA) (TAA YadA) (Type 5 secretion system autotransporter YadA)
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MTKDFKISVSAALISALFSSPYAFANNDEVHFTAVQISPNADPDSHVVIFQPAAEALGGTNALAKSIHSIAVGASAEAAKQAAVAVGAGSIATGVNSVAIGPLSKALGDSAVTYGAASTAQKDGVAIGARAFTSDTGVAVGFNSKVDAKNSVAIGHSSHVAVDHDYSIAIGDRSKTDRKNSVSIGHESLNRQLTHLAAGTKDTDAVNVAQLKKEIEKTQVNANKKSAEVLGIANNYTDSKSAETLENARKEAFDLSNDALDMAKKHSNSVARTTLETAEEHTNKKSAETLARANVYADSKSSHTLQTANSYTDVTVSNSTKKAIRESNQYTDHKFRQLDNRLDKLDTRVDKGLASSAALNSLFQPYGVGKVNFTAGVGGYRSSQALAIGSGYRVNESVALKAGVAYAGSSDVMYNASFNIEW
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Collagen-binding outer membrane protein forming a fibrillar matrix on the bacterial cell surface and phagocytosis resistance (By similarity). Promotes initial attachment and invasion of eukaryotic cells (Probable). Also protects the bacteria by being responsible for agglutination, serum resistance and complement inactivation. Gly-389 plays an important role in this protein replacing it with increasingly large polar residues decreases expression levels and trimer stability. Residues larger than Ser (Thr, Asn or His) significantly decrease serume resistance and bacterial autoagglution without affecting adhesion to host cells or host cell cytokine production.
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A1KI36
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KGD_MYCBP
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Multifunctional 2-oxoglutarate metabolism enzyme (2-hydroxy-3-oxoadipate synthase) (HOA synthase) (HOAS) (EC 2.2.1.5) (2-oxoglutarate carboxy-lyase) (2-oxoglutarate decarboxylase) (Alpha-ketoglutarate decarboxylase) (KG decarboxylase) (KGD) (EC 4.1.1.71) (Alpha-ketoglutarate-glyoxylate carboligase) [Includes: 2-oxoglutarate dehydrogenase E1 component (ODH E1 component) (EC 1.2.4.2) (Alpha-ketoglutarate dehydrogenase E1 component) (KDH E1 component); Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (EC 2.3.1.61) (2-oxoglutarate dehydrogenase complex E2 component) (ODH E2 component) (OGDC-E2) (Dihydrolipoamide succinyltransferase)]
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MANISSPFGQNEWLVEAMYRKFRDDPSSVDPSWHEFLVDYSPEPTSQPAAEPTRVTSPLVAERAAAAAPQAPPKPADTAAAGNGVVAALAAKTAVPPPAEGDEVAVLRGAAAAVVKNMSASLEVPTATSVRAVPAKLLIDNRIVINNQLKRTRGGKISFTHLLGYALVQAVKKFPNMNRHYTEVDGKPTAVTPAHTNLGLAIDLQGKDGKRSLVVAGIKRCETMRFAQFVTAYEDIVRRARDGKLTTEDFAGVTISLTNPGTIGTVHSVPRLMPGQGAIIGVGAMEYPAEFQGASEERIAELGIGKLITLTSTYDHRIIQGAESGDFLRTIHELLLSDGFWDEVFRELSIPYLPVRWSTDNPDSIVDKNARVMNLIAAYRNRGHLMADTDPLRLDKARFRSHPDLEVLTHGLTLWDLDRVFKVDGFAGAQYKKLRDVLGLLRDAYCRHIGVEYAHILDPEQKEWLEQRVETKHVKPTVAQQKYILSKLNAAEAFETFLQTKYVGQKRFSLEGAESVIPMMDAAIDQCAEHGLDEVVIGMPHRGRLNVLANIVGKPYSQIFTEFEGNLNPSQAHGSGDVKYHLGATGLYLQMFGDNDIQVSLTANPSHLEAVDPVLEGLVRAKQDLLDHGSIDSDGQRAFSVVPLMLHGDAAFAGQGVVAETLNLANLPGYRVGGTIHIIVNNQIGFTTAPEYSRSSEYCTDVAKMIGAPIFHVNGDDPEACVWVARLAVDFRQRFKKDVVIDMLCYRRRGHNEGDDPSMTNPYMYDVVDTKRGARKSYTEALIGRGDISMKEAEDALRDYQGQLERVFNEVRELEKHGVQPSESVESDQMIPAGLATAVDKSLLARIGDAFLALPNGFTAHPRVQPVLEKRREMAYEGKIDWAFGELLALGSLVAEGKLVRLSGQDSRRGTFSQRHSVLIDRHTGEEFTPLQLLATNSDGSPTGGKFLVYDSPLSEYAAVGFEYGYTVGNPDAVVLWEAQFGDFVNGAQSIIDEFISSGEAKWGQLSNVVLLLPHGHEGQGPDHTSARIERFLQLWAEGSMTIAMPSTPSNYFHLLRRHALDGIQRPLIVFTPKSMLRHKAAVSEIKDFTEIKFRSVLEEPTYEDGIGDRNKVSRILLTSGKLYYELAARKAKDNRNDLAIVRLEQLAPLPRRRLRETLDRYENVKEFFWVQEEPANQGAWPRFGLELPELLPDKLAGIKRISRRAMSAPSSGSSKVHAVEQQEILDEAFG
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Shows three enzymatic activities that share a first common step, the attack of thiamine-PP on 2-oxoglutarate (alpha-ketoglutarate, KG), leading to the formation of an enamine-thiamine-PP intermediate upon decarboxylation. Thus, displays KGD activity, catalyzing the decarboxylation from five-carbon 2-oxoglutarate to four-carbon succinate semialdehyde (SSA). Also catalyzes C-C bond formation between the activated aldehyde formed after decarboxylation of alpha-ketoglutarate and the carbonyl of glyoxylate (GLX), to yield 2-hydroxy-3-oxoadipate (HOA), which spontaneously decarboxylates to form 5-hydroxylevulinate (HLA). And is also a component of the 2-oxoglutarate dehydrogenase (ODH) complex, that catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). The KG decarboxylase and KG dehydrogenase reactions provide two alternative, tightly regulated, pathways connecting the oxidative and reductive branches of the TCA cycle (By similarity).
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A1KXE4
|
F168B_HUMAN
|
Myelin-associated neurite-outgrowth inhibitor (Mani) (p20)
|
MNPVYSPGSSGVPYANAKGIGYPAGFPMGYAAAAPAYSPNMYPGANPTFQTGYTPGTPYKVSCSPTSGAVPPYSSSPNPYQTAVYPVRSAYPQQSPYAQQGTYYTQPLYAAPPHVIHHTTVVQPNGMPATVYPAPIPPPRGNGVTMGMVAGTTMAMSAGTLLTAHSPTPVAPHPVTVPTYRAPGTPTYSYVPPQW
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Inhibitor of neuronal axonal outgrowth. Acts as a negative regulator of CDC42 and STAT3 and a positive regulator of STMN2. Positive regulator of CDC27.
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A1KZ92
|
PXDNL_HUMAN
|
Probable oxidoreductase PXDNL (EC 1.-.-.-) (Cardiac peroxidase) (Inactive peroxidasin-like protein) (Polysomal ribonuclease 1) (PRM1) (Vascular peroxidase 2)
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MEPRLFCWTTLFLLAGWCLPGLPCPSRCLCFKSTVRCMHLMLDHIPQVPQQTTVLDLRFNRIREIPGSAFKKLKNLNTLLLNNNHIRKISRNAFEGLENLLYLYLYKNEIHALDKQTFKGLISLEHLYIHFNQLEMLQPETFGDLLRLERLFLHNNKLSKIPAGSFSNLDSLKRLRLDSNALVCDCDLMWLGELLQGFAQHGHTQAAATCEYPRRLHGRAVASVTVEEFNCQSPRITFEPQDVEVPSGNTVYFTCRAEGNPKPEIIWIHNNHSLDLEDDTRLNVFDDGTLMIRNTRESDQGVYQCMARNSAGEAKTQSAMLRYSSLPAKPSFVIQPQDTEVLIGTSTTLECMATGHPHPLITWTRDNGLELDGSRHVATSSGLYLQNITQRDHGRFTCHANNSHGTVQAAANIIVQAPPQFTVTPKDQVVLEEHAVEWLCEADGNPPPVIVWTKTGGQLPVEGQHTVLSSGTLRIDRAAQHDQGQYECQAVSSLGVKKVSVQLTVKPKALAVFTQLPQDTSVEVGKNINISCHAQGEPQPIITWNKEGVQITESGKFHVDDEGTLTIYDAGFPDQGRYECVARNSFGLAVTNMFLTVTAIQGRQAGDDFVESSILDAVQRVDSAINSTRRHLFSQKPHTSSDLLAQFHYPRDPLIVEMARAGEIFEHTLQLIRERVKQGLTVDLEGKEFRYNDLVSPRSLSLIANLSGCTARRPLPNCSNRCFHAKYRAHDGTCNNLQQPTWGAALTAFARLLQPAYRDGIRAPRGLGLPVGSRQPLPPPRLVATVWARAAAVTPDHSYTRMLMHWGWFLEHDLDHTVPALSTARFSDGRPCSSVCTNDPPCFPMNTRHADPRGTHAPCMLFARSSPACASGRPSATVDSVYAREQINQQTAYIDGSNVYGSSERESQALRDPSVPRGLLKTGFPWPPSGKPLLPFSTGPPTECARQEQESPCFLAGDHRANEHLALAAMHTLWFREHNRMATELSALNPHWEGNTVYQEARKIVGAELQHITYSHWLPKVLGDPGTRMLRGYRGYNPNVNAGIINSFATAAFRFGHTLINPILYRLNATLGEISEGHLPFHKALFSPSRIIKEGGIDPVLRGLFGVAAKWRAPSYLLSPELTQRLFSAAYSAAVDSAATIIQRGRDHGIPPYVDFRVFCNLTSVKNFEDLQNEIKDSEIRQKLRKLYGSPGDIDLWPALMVEDLIPGTRVGPTLMCLFVTQFQRLRDGDRFWYENPGVFTPAQLTQLKQASLSRVLCDNGDSIQQVQADVFVKAEYPQDYLNCSEIPKVDLRVWQDCCADCRSRGQFRAVTQESQKKRSAQYSYPVDKDMELSHLRSRQQDKIYVGEDARNVTVLAKTKFSQDFSTFAAEIQETITALREQINKLEARLRQAGCTDVRGVPRKAEERWMKEDCTHCICESGQVTCVVEICPPAPCPSPELVKGTCCPVCRDRGMPSDSPEKR
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Probable oxidoreductase (Probable). Lacks peroxidase activity. Inhibits the peroxidase activity of PXDN through its interaction. [Isoform PMR1]: Endonuclease selectively degrading some target mRNAs while they are engaged by translating ribosomes, among which albumin and beta-globin mRNAs.
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A1L0T0
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HACL2_HUMAN
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2-hydroxyacyl-CoA lyase 2 (EC 4.1.2.-) (Acetolactate synthase-like protein) (IlvB-like protein)
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METPAAAAPAGSLFPSFLLLACGTLVAALLGAAHRLGLFYQLLHKVDKASVRHGGENVAAVLRAHGVRFIFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPVDVLYPYFMVQKEMVPAKPPKGLVGRVVSWYLENYLANLFAGAWEPQPEGPLPLDIPQASPQQVQRCVEILSRAKRPLMVLGSQALLTPTSADKLRAAVETLGVPCFLGGMARGLLGRNHPLHIRENRSAALKKADVIVLAGTVCDFRLSYGRVLSHSSKIIIVNRNREEMLLNSDIFWKPQEAVQGDVGSFVLKLVEGLQGQTWAPDWVEELREADRQKEQTFREKAAMPVAQHLNPVQVLQLVEETLPDNSILVVDGGDFVGTAAHLVQPRGPLRWLDPGAFGTLGVGAGFALGAKLCRPDAEVWCLFGDGAFGYSLIEFDTFVRHKIPVMALVGNDAGWTQISREQVPSLGSNVACGLAYTDYHKAAMGLGARGLLLSRENEDQVVKVLHDAQQQCRDGHPVVVNILIGRTDFRDGSIAV
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Endoplasmic reticulum 2-OH acyl-CoA lyase involved in the cleavage (C1 removal) reaction in the fatty acid alpha-oxydation in a thiamine pyrophosphate (TPP)-dependent manner. Involved in the phytosphingosine degradation pathway.
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A1L167
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U2QL1_HUMAN
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Ubiquitin-conjugating enzyme E2Q-like protein 1 (EC 2.3.2.23) (E2Q-like ubiquitin-conjugating enzyme 1)
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MKELQDIARLSDRFISVELVDESLFDWNVKLHQVDKDSVLWQDMKETNTEFILLNLTFPDNFPFSPPFMRVLSPRLENGYVLDGGAICMELLTPRGWSSAYTVEAVMRQFAASLVKGQGRICRKAGKSKKSFSRKEAEATFKSLVKTHEKYGWVTPPVSDG
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Probable E2 ubiquitin-protein ligase that catalyzes the covalent attachment of ubiquitin to target proteins. May facilitate the monoubiquitination and degradation of MTOR and CCNE1 through interaction with FBXW7.
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A1L190
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SYCE3_HUMAN
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Synaptonemal complex central element protein 3 (Testis highly expressed gene 2 protein) (THEG-2)
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MDDADPEERNYDNMLKMLSDLNKDLEKLLEEMEKISVQATWMAYDMVVMRTNPTLAESMRRLEDAFVNCKEEMEKNWQELLHETKQRL
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Major component of the transverse central element of synaptonemal complexes (SCS), formed between homologous chromosomes during meiotic prophase. Required for chromosome loading of the central element-specific SCS proteins, and for initiating synapsis between homologous chromosomes. Chromosome loading appears to require SYCP1. Required for fertility.
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A1L1K8
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HABP4_RAT
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Intracellular hyaluronan-binding protein 4 (IHABP-4) (IHABP4) (Hyaluronan-binding protein 4) (Ki-1/57 intracellular antigen)
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MKGALGSPVAAAGAAMQETFGCVVANRFHQLLDDESDPFDILREAEHRRQQQLQRKRRDEAAAASGAGHRGGRSPAVASGHRPGAAGRRESQKERKSLAVSSAQQPDSPGGPQPPGQKRTPRRGEQQGWNDNRGTDVVLDRAERRSYREYRPYDTERQAESTAEKFTDEKPVDRFDRDRPLRGRGGPRGGLRNRGRGGPGNRAFDSFDQRGKRDFERYGSSDKANRMEDSMGGCGVRTWGSGKDTSDTEPPAPMEETSMMEECQGVLDEESASKVPELEVEEENQVQEMTLDEWKNLQEQTRPKPEFNIRKPESTVPSKAVVIHKSRYRDDIVKDDYEDESHVFRKAANDITSQLEINFGNLPRPGRGARGSTRGGRGRIRRTENYGPRAEVVTQDVAPNPDDPEDFPALA
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Ribosome-binding protein that promotes ribosome hibernation, a process during which ribosomes are stabilized in an inactive state and preserved from proteasomal degradation (By similarity). Acts via its association with EEF2/eEF2 factor at the A-site of the ribosome, promoting ribosome stabilization in an inactive state compatible with storage (By similarity). Plays a key role in ribosome hibernation in the mature oocyte by promoting ribosome stabilization (By similarity). Ribosomes, which are produced in large quantities during oogenesis, are stored and translationally repressed in the oocyte and early embryo (By similarity). Also binds RNA, regulating transcription and pre-mRNA splicing. Binds (via C-terminus) to poly(U) RNA. Seems to play a role in PML-nuclear bodies formation (By similarity). Negatively regulates DNA-binding activity of the transcription factor MEF2C in myocardial cells in response to mechanical stress.
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A1L1N5
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HN1BA_DANRE
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Hepatocyte nuclear factor 1-beta-A (HNF-1-beta-A) (HNF-1B-A) (Hepatocyte nuclear factor 1-beta-2) (HNF-1B-2) (Transcription factor 2) (TCF-2) (Variant hepatic nuclear factor 1) (vHNF1)
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MFANMVSKLTSLQQELLSALLDSGVTKDVLLQALEDLDPSPSAFGVKLDSLQMSPSGSKLSDTDSKPVFHTLTNGHSKGKLSGDEGSEDGDDYDTPPILKELQSQNTEEAAEQRAEIERMLAEDPWRAARMIKGYMQQHNIPQREVVDVTGLNQSHLSQHLNKGTPMKTQKRAALYTWYVRKQREILRQFNQATQGSGATMLDKGNQDQVLLFFSEFSQSGQGMVQPGDDAAIEPACKKLRRNRFKWGPASQQILYQAYERQKNPSKEEREALVEECNRAECLQRGVSPSKAHGLGSNLVTEVRVYNWFANRRKEEAFRQKLAMDAYSGPAHSLNSLLSHSSPHHPQTSSSPPSKMQGVRYSQQGPGEVTSSTTINHHSSNAMSTSQSVLQQVSPGALDPSHSLLSPDAKMISVSGGGLPPVSTLTNIHASHHVHQQTPNLIMPLSGVMAIAQSLNTSQAQTVPVINSVAGSLAALQPVQFSQQLNSQHQQLMQQSSGHMSQQSFMASVSHSHMYPHKQEPPQYSHSSRFPPAMVVTDANSLSTLSSMSSSKQCPLQAW
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Transcription factor that binds to the inverted palindrome 5'-GTTAATNATTAAC-3' (By similarity). Required for induction of rhombomere r5/r6 gene expression in the hindbrain.
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A1L1V4
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LOL2B_DANRE
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Lysyl oxidase homolog 2B (EC 1.4.3.13) (Lysyl oxidase-like protein 2B)
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MLALWSISFVLLCSWRLSYAQYEHLGFAIAYQEPEQDLYTPPELPADTPRIQLRLAGEKRKHNEGRVEVFYEGEWGTVCDDDFTIHAAQVICRELGYFEAISWSPSSKYGKGEGRIWFDNVHCKGKEKSLAQCESNGIGVSDCKHSEDVGVVCSDKRIPGFKFVNTLTNNINSLNIQVEDVRIRPILASYRKRIPVTEGYVEVKDGGKWKQICDDEWTQMNSRVICGMFGFPGQKRYNTRVYKMFARRRKPSYWDYTINCTGKEAHLSSCTLGHTLSNSTCEEGTPVVVSCIPGRAFAPTPMTGYKKAFRQEQPLVRLRGGAVVGEGRVEVLKNGEWGTICDDNWNLLAATVVCRELGFGSAKEALSGGQLGQGMGPVHMNEVQCSGFEKSVTECSFNMEKDSEGCSHEEDAGVKCNVPAMGFQQRLRLSGGRNPFEGRVEVLVERNGSLVWGTVCGEGWTTMEAMVVCRQLGLGFASNAFQETWYWPGAVNADAVVMSGVRCAGTEMSLSHCLHHGEYLSCPKGGGRFAAGVSCSETAPDLVLNPQVVEQTTYLEDRPMFMLQCAYEENCLASTSSATPANSPRRLLRFSSQIHNNGQSDFRPKISRENWVWHDCHRHYHSMEVFTHYDLLSTNGTKVAEGHKASFCLEDSECDEGIEKRYECANFGEQGITVGCWDTYRHDIDCQWVDITDVKPGDYIFQIVINPNYEVAESDYTNNIVKCRCRYDGHRIWMYNCHIGGSFSAETEDTFPGLINNQVTHR
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Mediates the post-translational oxidative deamination of lysine residues on target proteins leading to the formation of deaminated lysine (allysine) (By similarity). Acts as a transcription corepressor and specifically mediates deamination of trimethylated 'Lys-4' of histone H3 (H3K4me3), a specific tag for epigenetic transcriptional activation (By similarity). Shows no activity against histone H3 when it is trimethylated on 'Lys-9' (H3K9me3) or 'Lys-27' (H3K27me3) or when 'Lys-4' is monomethylated (H3K4me1) or dimethylated (H3K4me2) (By similarity). Also mediates deamination of methylated TAF10, a member of the transcription factor IID (TFIID) complex, which induces release of TAF10 from promoters, leading to inhibition of TFIID-dependent transcription (By similarity). LOXL2-mediated deamination of TAF10 results in transcriptional repression of genes required for embryonic stem cell pluripotency (By similarity). Involved in epithelial to mesenchymal transition (EMT) and participates in repression of E-cadherin, probably by mediating deamination of histone H3 (By similarity). When secreted into the extracellular matrix, promotes cross-linking of extracellular matrix proteins by mediating oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin (By similarity). Acts as a regulator of sprouting angiogenesis, probably via collagen IV scaffolding. Acts as a regulator of chondrocyte differentiation, probably by regulating expression of factors that control chondrocyte differentiation (By similarity). Required with loxl2a for correct expression of Sox2 and for neural differentiation.
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A1L259
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URAD_DANRE
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2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase (OHCU decarboxylase) (EC 4.1.1.97) (Parahox neighbor) (Ureidoimidazoline (2-oxo-4-hydroxy-4-carboxy-5-) decarboxylase)
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MDINVVNALAYEDFVKLFGNVVEKCPLISAAIWSYRPFKDLADIEARISEFIHSLPDSGKEGILRCHPDLAGRDLQSGTLTPESQEEQSQAGMTTLDSAEIVHMYRLNSEYKERFGFPFVICARLNNKADIVRQLSERLKNRRTAELECAIEEVKKICSLRLHSIVLSDIQTKL
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Catalyzes the stereoselective decarboxylation of 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU) to (S)-allantoin.
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A1L2G3
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BAP1_DANRE
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Ubiquitin carboxyl-terminal hydrolase BAP1 (EC 3.4.19.12) (BRCA1-associated protein 1)
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MNKGWLELESDPGLFTLLVEDFGVKGVQVEEIYDLQSKCQSPVYGFIFLFKWIEERRSRRKVSTLVDETSVIDDDIVNDMFFAHQLIPNSCATHALLSVLLNCSGVELGMTLSRMKAFTKGFNPESKGYAIGNAPELAKAHNSHARPEPRHLPEKQNGISAVRTMEAFHFVSYVPIKDRLFELDGLKAYPIDHGPWGEDEEWTDKARRVIMERIGLATAGEPYHDIRFNLMAVVPDRRIKYESKLDILKRNRQIILEGLQQIREKKVIRMTQQESGQDRKQQDSSSSEDTPPVVKKEEVQETPIPSGAEQATPTEAQEGAASLPSPAGKVRSMAKPALPAGGAPPPAPLPAPSTNTIVQRLPAFLDNHNYAKSPMQEEEDLAAGVGRSRPPQPPYSDDEDDYDDEEEECSTAGVTNSRVRRKLGLRTRTMSRTAVGGVAAMEGQLALSVLAEKLKKEVQRKDALATTGSTPLNVRTEGRTGGISITSACQPSPTPSNESTDTASEIGSAFNSPLRSPARSQATTRPSSPVASHVGRVLFGEEEGLPRLDARHNRAVRDLGVLVSSTQLQLQEDGVIFALPPTEALEGLKKVGGVDKKKKEEASGPGGEEEVKEGPSVEMKAEDVKESVDVKPEKENLPTTDVENSTKPPGEKYTPKELLALLKYVEADIANYEVYLKEEVEKRKKYKIDDQRRTHNYDEFICTFISMLAQEGMLASLVEQNISVRRRQGVSIGRLHKQRKPDRRKRSRPYKAKRQ
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Deubiquitinating enzyme that plays a key role in chromatin by mediating deubiquitination of histone H2A. Catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1) (By similarity).
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A1L314
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MPEG1_MOUSE
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Macrophage-expressed gene 1 protein (Macrophage gene 1 protein) (Mpg-1) (Perforin-2) (P-2) (Protein MPS1)
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MNSFMALVLIWMIIACAEADKPLGETGTTGFQICKNALKLPVLEVLPGGGWDNLRNVDMGRVMDLTYTNCKTTEDGQYIIPDEVYTIPQKESNLEMNSEVLESWMNYQSTTSLSINTELALFSRVNGKFSTEFQRMKTLQVKDQAVTTRVQVRNRIYTVKTTPTSELSLGFTKALMDICDQLEKNQTKMATYLAELLILNYGTHVITSVDAGAALVQEDHVRSSFLLDNQNSQNTVTASAGIAFLNIVNFKVETDYISQTSLTKDYLSNRTNSRVQSFGGVPFYPGITLETWQKGITNHLVAIDRAGLPLHFFIKPDKLPGLPGPLVKKLSKTVETAVRHYYTFNTHPGCTNVDSPNFNFQANMDDDSCDAKVTNFTFGGVYQECTELSGDVLCQNLEQKNLLTGDFSCPPGYSPVHLLSQTHEEGYSRLECKKKCTLKIFCKTVCEDVFRVAKAEFRAYWCVAAGQVPDNSGLLFGGVFTDKTINPMTNAQSCPAGYIPLNLFESLKVCVSLDYELGFKFSVPFGGFFSCIMGNPLVNSDTAKDVRAPSLKKCPGGFSQHLAVISDGCQVSYCVKAGIFTGGSLLPVRLPPYTKPPLMSQVATNTVIVTNSETARSWIKDPQTNQWKLGEPLELRRAMTVIHGDSNGMSGGEAAGITLGVTIALGIVITLAIYGTRKYKKKEYQEIEEQESLVGSLATDATVLNGEEDPSPA
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Plays a key role in the innate immune response following bacterial infection by inserting into the bacterial surface to form pores. By breaching the surface of phagocytosed bacteria, allows antimicrobial effectors to enter the bacterial periplasmic space and degrade bacterial proteins such as superoxide dismutase sodC which contributes to bacterial virulence. Shows antibacterial activity against a wide spectrum of Gram-positive, Gram-negative and acid-fast bacteria. Reduces the viability of the intracytosolic pathogen L.monocytogenes by inhibiting acidification of the phagocytic vacuole of host cells which restricts bacterial translocation from the vacuole to the cytosol. Required for the antibacterial activity of reactive oxygen species and nitric oxide.
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A1L390
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PKHG3_HUMAN
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Pleckstrin homology domain-containing family G member 3 (PH domain-containing family G member 3)
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MPVSTSLHQDGSQERPVSLTSTTSSSGSSCDSRSAMEEPSSSEAPAKNGAGSLRSRHLPNSNNNSSSWLNVKGPLSPFNSRAAAGPAHHKLSYLGRVVREIVETERMYVQDLRSIVEDYLLKIIDTPGLLKPEQVSALFGNIENIYALNSQLLRDLDSCNSDPVAVASCFVERSQEFDIYTQYCNNYPNSVAALTECMRDKQQAKFFRDRQELLQHSLPLGSYLLKPVQRILKYHLLLQEIAKHFDEEEDGFEVVEDAIDTMTCVAWYINDMKRRHEHAVRLQEIQSLLINWKGPDLTTYGELVLEGTFRVHRVRNERTFFLFDKTLLITKKRGDHFVYKGNIPCSSLMLIESTRDSLCFTVTHYKHSKQQYSIQAKTVEEKRNWTHHIKRLILENHHATIPQKAKEAILEMDSYYPNRYRCSPERLKKAWSSQDEVSTNVRQGRRQSEPTKHLLRQLNEKARAAGMKGKGRRESESSRSSRRPSGRSPTSTEKRMSFESISSLPEVEPDPEAGSEQEVFSAVEGPSAEETPSDTESPEVLETQLDAHQGLLGMDPPGDMVDFVAAESTEDLKALSSEEEEEMGGAAQEPESLLPPSVLDQASVIAERFVSSFSRRSSVAQEDSKSSGFGSPRLVSRSSSVLSLEGSEKGLARHGSATDSLSCQLSPEVDISVGVATEDSPSVNGMEPPSPGCPVEPDRSSCKKKESALSTRDRLLLDKIKSYYENAEHHDAGFSVRRRESLSYIPKGLVRNSISRFNSLPRPDPEPVPPVGSKRQVGSRPTSWALFELPGPSQAVKGDPPPISDAEFRPSSEIVKIWEGMESSGGSPGKGPGQGQANGFDLHEPLFILEEHELGAITEESATASPESSSPTEGRSPAHLARELKELVKELSSSTQGELVAPLHPRIVQLSHVMDSHVSERVKNKVYQLARQYSLRIKSNKPVMARPPLQWEKVAPERDGKSPTVPCLQEEAGEPLGGKGKRKPVLSLFDYEQLMAQEHSPPKPSSAGEMSPQRFFFNPSAVSQRTTSPGGRPSARSPLSPTETFSWPDVRELCSKYASRDEARRAGGGRPRGPPVNRSHSVPENMVEPPLSGRVGRCRSLSTKRGRGGGEAAQSPGPLPQSKPDGGETLYVTADLTLEDNRRVIVMEKGPLPSPTAGLEESSGQGPSSPVALLGQVQDFQQSAECQPKEEGSRDPADPSQQGRVRNLREKFQALNSVG
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Plays a role in controlling cell polarity and cell motility by selectively binding newly polymerized actin and activating RAC1 and CDC42 to enhance local actin polymerization.
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A1L3G9
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NMP1B_XENLA
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Nuclear envelope integral membrane protein 1b
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MAGEVEGRGCGFSLGVLVTLLVLPLPSLCTLSTEKELHVIKLYEGRMVRYNESRNFCYQRTYEPKWSDVWTKIQIRINSTKMIRVTQVDNEEKLKEMETFNMFDFFSSFLKEKLNDTFIYVNLYSNKTCVKVHLTDTDTYYSVALSRGFDPRLFFVFLCGLLLFFYGDTLSRSQLFFYSTGITVGMLASMLILVFMLSKLMPKKSPFFALLLGGWSVSIYVIQLVFRNLQAICSEYWQYLIVYLGIVGFVSFAFCYIYGPLENERSINILNWTLQLIGLLLMYVSVQIQHIAVTIVVIAFCTKQIEYPVQWIYILYRKIKLKRAKPGPPRLLTEEEYRKQADVETRKALEELRECCSSPDFAAWKTISRIQSPKRFADFVEGSSHLTPNEVSVHEHEYGLGGSFLEDELFGEDSDVEEEMEIEPPLYPIPRSVF
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In concert with ran, required for proper eye development. May be involved in the expression of early eye marker genes. Contributes to nuclear envelope stiffness in germ cells (By similarity). Required for fertility (By similarity).
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A1L3P4
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SL9A6_MOUSE
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Sodium/hydrogen exchanger 6 (Na(+)/H(+) exchanger 6) (NHE-6) (Sodium/hydrogen exchanger) (Solute carrier family 9 member 6)
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MAGARRGWRLAPVRRGVCGPRARPLMRPLWLLFAVSFFGWTGALDGSGGTTRAMDEEIVSEKQAEESHRQDSANLLIFILLLTLTILTIWLFKHRRARFLHETGLAMIYGLLVGLVLRYGIHVPSDVNNVTLSCEVQSSPTTLLVNVSGKFYEYTLKGEISSHELNNVQDNEMLRKVTFDPEVFFNILLPPIIFYAGYSLKRRHFFRNLGSILAYAFLGTAISCFVIGSIMYGCVTLMKVTGQLAGDFYFTDCLLFGAIVSATDPVTVLAIFHELQVDVELYALLFGESVLNDAVAIVLSSSIVAYQPAGDNSHTFDVTAMFKSIGIFLGIFSGSFAMGAATGVVTALVTKFTKLREFQLLETGLFFLMSWSTFLLAEAWGFTGVVAVLFCGITQAHYTYNNLSTESQHRTKQLFELLNFLAENFIFSYMGLTLFTFQNHVFNPTFVVGAFIAIFLGRAANIYPLSLLLNLGRRSKIGSNFQHMMMFAGLRGAMAFALAIRDTATYARQMMFSTTLLIVFFTVWVFGGGTTAMLSCLHIRVGVDSDQEHLGVPDNERRTTKAESAWLFRMWYNFDHNYLKPLLTHSGPPLTTTLPACCGPIARCLTSPQAYENQEQLKDDDSDLILNDGDISLTYGDSTVNTESATASAPRRFMGNSSEDALDRELTFGDHELVIRGTRLVLPMDDSEPALNSLDDTRHSPA
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Endosomal Na(+), K(+)/H(+) antiporter. Mediates the electroneutral exchange of endosomal luminal H(+) for a cytosolic Na(+) or K(+). By facilitating proton efflux, SLC9A6 counteracts the acidity generated by vacuolar (V)-ATPase, thereby limiting luminal acidification. Responsible for alkalizing and maintaining the endosomal pH, and consequently in, e.g., endosome maturation and trafficking of recycling endosomal cargo. Plays a critical role during neurodevelopment by regulating synaptic development and plasticity. Implicated in the maintenance of cell polarity in a manner that is dependent on its ability to modulate intravesicular pH (By similarity). Regulates intracelular pH in some specialized cells, osteoclasts and stereocilia where this transporter localizes to the plasma membrane.
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A1L3X0
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ELOV7_HUMAN
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Elongation of very long chain fatty acids protein 7 (EC 2.3.1.199) (3-keto acyl-CoA synthase ELOVL7) (ELOVL fatty acid elongase 7) (ELOVL FA elongase 7) (Very long chain 3-ketoacyl-CoA synthase 7) (Very long chain 3-oxoacyl-CoA synthase 7)
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MAFSDLTSRTVHLYDNWIKDADPRVEDWLLMSSPLPQTILLGFYVYFVTSLGPKLMENRKPFELKKAMITYNFFIVLFSVYMCYEFVMSGWGIGYSFRCDIVDYSRSPTALRMARTCWLYYFSKFIELLDTIFFVLRKKNSQVTFLHVFHHTIMPWTWWFGVKFAAGGLGTFHALLNTAVHVVMYSYYGLSALGPAYQKYLWWKKYLTSLQLVQFVIVAIHISQFFFMEDCKYQFPVFACIIMSYSFMFLLLFLHFWYRAYTKGQRLPKTVKNGTCKNKDN
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Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme with higher activity toward C18 acyl-CoAs, especially C18:3(n-3) acyl-CoAs and C18:3(n-6)-CoAs. Also active toward C20:4-, C18:0-, C18:1-, C18:2- and C16:0-CoAs, and weakly toward C20:0-CoA. Little or no activity toward C22:0-, C24:0-, or C26:0-CoAs. May participate in the production of saturated and polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. {ECO:0000255|HAMAP-Rule:MF_03207, ECO:0000269|PubMed:19826053, ECO:0000269|PubMed:20937905, ECO:0000269|PubMed:21959040, ECO:0000269|PubMed:34117479}.
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A1L4H1
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SRCRL_HUMAN
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Soluble scavenger receptor cysteine-rich domain-containing protein SSC5D (Soluble scavenger protein with 5 SRCR domains) (SSc5D)
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MRVLACLLAALVGIQAVERLRLADGPHGCAGRLEVWHGGRWGTVCDDGWDLRDAAVACRQLGCGGALAAPGGAFFGEGAGPVWLSELACRGNEGQLGLCHHRGWKAHICSHEEDAGVVCAGQRVANSRDDSTSPLDGAPWPGLLLELSPSTEEPLVTHAPRPAGNPQNASRKKSPRPKQAKSTRAPLLTTGAPRQERLRLVSGPHRCAGRLEVWHGGRWGTVCDDGWDLRDAAVACRELGCGGALAAPGGARFGPGAGPVWMDDVGCGGGEQALRDCPRSPWGRSNCDHSEDAGLVCTGPAPRLRLADGPHGCAGRLEVWHGGRWGSVCDDAWDLRDAAVACRELGCGGALAAPGGAFFGEGSGPIILDDLRCRGNETALRFCPARPWGQHDCHHREDAGAVCDGMPLGYVPPTAPTDSNNSTPREAASRPPSTMTSQAPGTAGVSPPPASPTVLWEPGPEAGSPQLRLVAGPSKCSGRLEVWHDQRWGTVCDDSWDMRDSAVVCRELGCGGPQQPDPAAGRFGWGAGPIWLDDVGCVGTEASLSDCPAAPWGKHNCAHNEDVGVTCTGPPGLDSISDPFSWSWIPGLGRDRDAWLPGELATKPSASVTASVLEKTTTKAPGKMPKSTKKWVTKNAKRPTTQPPVMPTTKHSRAQSPPDLTSQTTAALTTEASRRPTSEFTRRPTTEAPQRWTSHTTATLTPQAPRERTTKTMAMLTTQGPQEMTSESTIKSIPQASLEPSAEIPEGSPESPKDPAPSPSVSTTGESGLFRVRLADGPNRCAGRLEVWHAGRWGTVCDDNWDLRDATVACWELGCGKVRPRVGKTHYGPGTGPIWLDDMGCKGSEASLSDCPSGAWGKHNCDHEEDVGLTCTGYTDYDDYPPWTWDPTSREDLAKGTTTAGVPGHTLPWRTTRRPGSSSPAIRRLPDTGSKDGYKLPWTWDTPSGRGLAEGTPTAGKLGPTLGAGTTRSPGSPPTLRVHGDTGSPRKPWPERRPPRPAATRTAPPTPSPGPSASPGPPGPALTSDSSRELTPHSALTSEATSDAPDTSPPTPDPASRTNPDLILTSPDFALSTPDSSVVPALTPEPSPTPLPTLPKELTSDPSTPSEVTSLSPTSEQVPESDTTPDLDTTPYSSTVSEYSRSPDPSPSPHPTTTPDPTMAPDPITTLNPTVTPHFPTTPHPTTTPHPTTITHSTMIPDPTTTPQPFTTITHSTMIPDPTTTPQPFTTMQPTTTPHSTTPHPTTTPHPTTITHSTMIPDPTTTPQPFTTMQPTTMPHPTTTPHPTTTPHPTTTPHPTTTPHPTMTPDPTTTPYPTTTPDPTTTPHPTTPDPSSTPVITTVSLPTSLGTELSSPTLAPTVKPSLHPQLTFTAPAPHTSTSQIPTLEPSPALESSPSRSSTATSMDPLSTEDFKPPRSQSPNLTPPPTHTPHSASDLTVSPDPLLSPTAHPLDHPPLDPLTLGPTPGQSPGPHGPCVAPTPPVRVMACEPPALVELVAAVRDVGGQLQRLTQVVEQERQERQALLLGLTQLVEAARGLGQLGEAVKRLAEMAWTTSMPAPTTTTPEEEERPLRGDV
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Binds to extracellular matrix proteins. Binds to pathogen-associated molecular patterns (PAMPs) present on the cell walls of Gram-positive and Gram-negative bacteria and fungi, behaving as a pattern recognition receptor (PRR). Induces bacterial and fungal aggregation and subsequent inhibition of PAMP-induced cytokine release. Does not possess intrinsic bactericidal activity. May play a role in the innate defense and homeostasis of certain epithelial surfaces (By similarity).
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A1S1I8
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FADB_SHEAM
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Fatty acid oxidation complex subunit alpha [Includes: Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC 4.2.1.17) (EC 5.1.2.3) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)]
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MIYQSPTIQVELTADKIARLCFNAPGSVNKFDRETLASLNAALDVLKDSDAKAAVLTSGKDTFIVGADITEFLALFAEEDAKLMEWIAQANVVFNKLEDLPFPTVSAIKGFALGGGCEAILATDFRVADTSAKIGLPETKLGLIPGFGGTVRLPRLIGADNALEWITTGKDQRPEDALKVGAIDAVVAPENLEAAAIQMLNDALAGKLDWQARRARKQAPLTLPKLEAMMSFTTAKGMVYAVAGKHYPAPMAAVSVVEQAAGMSRAEALVVEHNAFIKLAKTDVATALIGIFLNDQLVKGKAKKASKLAKDIKHAAVLGAGIMGGGIAYQSASKGTPIVMKDINQAALDLGVNEAAKLLSAQVARGRSTPDKMAKVLNNITPALDYAPLKDVNVVVEAVVENPKVKAMVLADVENVVADDAIIASNTSTISIDLLAKSLKNPARFCGMHFFNPVHKMPLVEVIRGKDTSEETVASVVAYASKMGKTPIVVNDCPGFFVNRVLFPYFAGFNGLLADGGDFAAIDKVMEKQFGWPMGPAYLLDVVGLDTGHHAQAVMADGFPDRMGKSDKDAIDVMYEAGRLGQKNGKGFYQYSIDKRGKPKKDVDPASYTMLAEAFGAQKAFEADEIIARTMIPMIIETVRCLEEGIVASPAEADMGLVYGLGFPPFRGGVFRYLDTMGVANFVALADKYAHLGGLYQVTDAMRELASNNGSYYPKA
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Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}.
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A1TDK2
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KGD_MYCVP
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Multifunctional 2-oxoglutarate metabolism enzyme (2-hydroxy-3-oxoadipate synthase) (HOA synthase) (HOAS) (EC 2.2.1.5) (2-oxoglutarate carboxy-lyase) (2-oxoglutarate decarboxylase) (Alpha-ketoglutarate decarboxylase) (KG decarboxylase) (KGD) (EC 4.1.1.71) (Alpha-ketoglutarate-glyoxylate carboligase) [Includes: 2-oxoglutarate dehydrogenase E1 component (ODH E1 component) (EC 1.2.4.2) (Alpha-ketoglutarate dehydrogenase E1 component) (KDH E1 component); Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (EC 2.3.1.61) (2-oxoglutarate dehydrogenase complex E2 component) (ODH E2 component) (OGDC-E2) (Dihydrolipoamide succinyltransferase)]
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MNSPSPFGQNEWLVEEMYRKFREDPSSVDPSWHEFLVDYSPEPTNDAPAGNGKPAAAPTAPPEPASAPAPKPASTNGGAPPAKADTSTTRAPEKKPEEKTSPAPKAKTAAPAGVSDDDETQVLRGAAAAVVKNMSASLDVPTATSVRAIPAKAMIDNRIVINNHLKRTRGGKISFTHLLGYAIVQAVKKFPNMNRHFAEIDGKPVAVTPAHTNLGLAIDLPGKDGKRSLVVAAIKNCETMHFGQFIAAYEDIVRRARDGKLTAEDFAGVTISLTNPGTIGTVHSVPRLMKGQGAIVGAGAMEYPAEFQGASEERIAELGVGKLMTLTSTYDHRIIQGAESGDFLRTIHTLLLDDEFYDEIFRELGIPHEPVRWRIDNPDSIEDKNARVIELIAAYRNRGHLMADIDPLRLDKTRFRSHPDLDVNTHGLTLWDLDREFKVNGFAGKTHKKLRDILGLLRDAYCRHIGVEYTHILEPEQQQWLQERIEVKHEKPTVAEQKYILSKLNAAEAFETFLQTKYVGQKRFSLEGAETVIPMMDAAIDQCAEHGLDEVVIGMPHRGRLNVLANIVGKPYSQIFTEFEGNLNPSQAHGSGDVKYHLGANGTYIQMFGDNDIDVSLVANPSHLEAVDPVLEGLVRAKQDILDKGNGPDGFTVVPMMLHGDAAFAGQGVVAETLNLALLRGYRTGGTIHIIVNNQIGFTTSPYDSRSSEYCTDVAKMIGAPIFHVNGDDPEACVWVAKLAVDFRQKFKKDVVIDMLCYRRRGHNEGDDPSMTQPTMYDVIDTKRGVRKSYTEALIGRGDISMKEAEDALRDYQGQLERVFNEVRELEKHAIAPSSSVESDQMVPAGMSTAVDKSLLARIGDAHLGYPDDFNVHPRVKPVLEKRREMAYEGKVDWAFAELLALGTFLAEGKTIRFTGQDTRRGTFTQRHSVIIDRQTGREFTPLDLLTVDSDGNPTGGKFMAYDSALSEFAAVGFEYGYSVGNPNALVLWEAQFGDFVNGAQSIIDEFISSGEAKWGQLSDVVLLLPHGHEGQGPDHTSGRIERFLLLWAEGSMTIAMPSTPANYFHLLRRHGLDGIHRPLIVFTPKSMLRNKAAVSDLKDFTEMKFRSVLEEPTYTEGTGDRSKAKRILLTSGKLYYELAARKSKEGRDDVAILRLEQLAPLPKRRLAATLDEYPNAEQYFWVQEEPANQGAWPTLGLTLPEVLPEKLAGIKRISRRAMSAPSSGSSKVHAVEQQEIIDEAFG
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Shows three enzymatic activities that share a first common step, the attack of thiamine-PP on 2-oxoglutarate (alpha-ketoglutarate, KG), leading to the formation of an enamine-thiamine-PP intermediate upon decarboxylation. Thus, displays KGD activity, catalyzing the decarboxylation from five-carbon 2-oxoglutarate to four-carbon succinate semialdehyde (SSA). Also catalyzes C-C bond formation between the activated aldehyde formed after decarboxylation of alpha-ketoglutarate and the carbonyl of glyoxylate (GLX), to yield 2-hydroxy-3-oxoadipate (HOA), which spontaneously decarboxylates to form 5-hydroxylevulinate (HLA). And is also a component of the 2-oxoglutarate dehydrogenase (ODH) complex, that catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). The KG decarboxylase and KG dehydrogenase reactions provide two alternative, tightly regulated, pathways connecting the oxidative and reductive branches of the TCA cycle (By similarity).
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A1TFU9
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HPXO_MYCVP
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FAD-dependent urate hydroxylase (EC 1.14.13.113) (Flavoprotein urate hydroxylase)
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MKVVIVGAGMGGMSAAIALRQIGIDTVVYERVTENKPVGAAISVWSNGVKCLNYLGLQEETAELGGKVETMSYVDGHTGDTMCRFSMHPLIEQVGQRPYPIARAELQLMLMKAYGIDDINFGMKMVGVENDTAGSAAKATFADGTTVSADVIIGADGAGSITREYVLGGPVSRRYAGYVNYNGLVSTDDAIGPATEWTTYVGDGKRVSVMPVSDDRFYFFFDVVEPQGSPYEEGRVREVLRAHFAGWTPGVQTLIDTLDPLATNRVEILDLDPFHTWVKGRVAVLGDAAHNTTPDIGQGGCSAMEDAIALQWAFKDHPDDVHAALAAYQSARTERAADLVLRARKRCDVTHAKDPQVTSRWYDELRNEDGTNIIRGIVGNIVGGPLTPVTAATEG
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Catalyzes the hydroxylation of urate to 5-hydroxyisourate (HIU). Is likely to be involved in the urate degradation pathway to allantoin. Prefers NADH over NADPH as the electron donor.
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A1UK81
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KGD_MYCSK
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Multifunctional 2-oxoglutarate metabolism enzyme (2-hydroxy-3-oxoadipate synthase) (HOA synthase) (HOAS) (EC 2.2.1.5) (2-oxoglutarate carboxy-lyase) (2-oxoglutarate decarboxylase) (Alpha-ketoglutarate decarboxylase) (KG decarboxylase) (KGD) (EC 4.1.1.71) (Alpha-ketoglutarate-glyoxylate carboligase) [Includes: 2-oxoglutarate dehydrogenase E1 component (ODH E1 component) (EC 1.2.4.2) (Alpha-ketoglutarate dehydrogenase E1 component) (KDH E1 component); Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (EC 2.3.1.61) (2-oxoglutarate dehydrogenase complex E2 component) (ODH E2 component) (OGDC-E2) (Dihydrolipoamide succinyltransferase)]
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MSSSPSPFGQNEWLVEEMYRKFREDPSSVDPSWHEFLVDYNPEPTTDSSASENGQQTRTAAPKAPPEPAPAPAPKTPDSKTPDSKSQAPKQDSKPQESKPQAKAKPAESKSSTKPADAKSEKSGKSGTNGAAKPAAQPADDSDQNQVLRGAAAAVAKNMSASLDVPTATSVRAIPAKLMIDNRVVINNHLKRTRGGKISFTHLIGYAIVAAVKKFPNMNRHFAEVDGKPNAVTPAHTNLGLAIDLQGKDGNRQLVVAAIKKADTMRFGQFIAAYEDIVRRARDGKLTAEDFSGVTISLTNPGTIGTVHSVPRLMRGQGAIIGVGAMEYPAEFQGASEERIADLGIGKLITLTSTYDHRIIQGAESGDFLRTVHQLLLSDDFFDEIFRELGIPYEPVRWRTDNPDSIEDKNARVIELIAAYRNRGHLMADIDPLRLDSNRFRSHPDLDVLTHGLTLWDLDREFKVNGFAGAERKKLRDVLAVLRDAYCRHIGVEYTHILEPEQQQWLQERIEGKHEKPTVAQQKYILSRLNAAEAFETFLQTKYVGQKRFSLEGAETVIPAMDAVIDQCAEHALDEVVIGMPHRGRLNVLANIVGKPYSQIFSEFEGNLNPSQAHGSGDVKYHLGSSGTYLQMFGDNDITVSLTANPSHLEAVDPVMEGLVRAKQDLLDKGDTEDGYTVVPLMLHGDAAFAGQGVVAETLNLALLRGYRTGGTIHLIVNNQIGFTTSPAAAKSSEYCTDVAKMIGAPIFHVNGDDPEAAVWVSRLAVDFRQKFKKDVVIDLLCYRRRGHNEGDDPSMTQPSMYDVIDTKRGVRKSYTEALIGRGDISMKEAEDALRDYQGQLEQVFNEVRELEKHEIEPSESVEADQQIPAKLATAVDKSLLARIGDAHLAVPEGFTVHPRVKPVLEKRREMAYEGKVDWAFAELLALGTMISEGKLVRLSGQDTRRGTFTQRHSVVIDRKTGKEFTPLQLLATDSDGNPTGGKFLVYDSPLSEFAAVGFEYGYSVGNPDAMVLWEAQFGDFINGAQSIIDEFISSGEAKWGQLSDVVLLLPHGHEGQGPDHTSGRIERFLQLWAEGSMTIALPSTPANYFHLLRRHSLDGIQRPLIVFTPKSMLRNKAAVSDIRDFTEQKFRSVLEEPTYTDGDGDRNKVTRILLTSGKIYYELVARKNKESRDDVAIVRIEQLAPLPKRRLAETLDKYPNVEEKFWVQEEPANQGAWPTFGLTLPEMLPDHFTGIKRISRRAMSAPSSGSSKVHAVEQQEILDEAFAP
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Shows three enzymatic activities that share a first common step, the attack of thiamine-PP on 2-oxoglutarate (alpha-ketoglutarate, KG), leading to the formation of an enamine-thiamine-PP intermediate upon decarboxylation. Thus, displays KGD activity, catalyzing the decarboxylation from five-carbon 2-oxoglutarate to four-carbon succinate semialdehyde (SSA). Also catalyzes C-C bond formation between the activated aldehyde formed after decarboxylation of alpha-ketoglutarate and the carbonyl of glyoxylate (GLX), to yield 2-hydroxy-3-oxoadipate (HOA), which spontaneously decarboxylates to form 5-hydroxylevulinate (HLA). And is also a component of the 2-oxoglutarate dehydrogenase (ODH) complex, that catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). The KG decarboxylase and KG dehydrogenase reactions provide two alternative, tightly regulated, pathways connecting the oxidative and reductive branches of the TCA cycle (By similarity).
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A1X149
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CAV1_ECHTE
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Caveolin-1
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MSGGKYVDSEGHLYTLPIREQGNIYKPNNKAMAEDMNEKQVYDAHTKEIDLVNRDPKHLNDDVVKIDFEDVIAEPEGTHSFDGIWKASFTTFTVTKYWFYRLLSGIFGIPMALIWGVYFAILSFLHIWAVVPCIKSFLIEIQCISRVYSIYVHTFCDPLFEAIGKIFSNIRISTQKEI
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May act as a scaffolding protein within caveolar membranes. Forms a stable heterooligomeric complex with CAV2 that targets to lipid rafts and drives caveolae formation. Mediates the recruitment of CAVIN proteins (CAVIN1/2/3/4) to the caveolae (By similarity). Interacts directly with G-protein alpha subunits and can functionally regulate their activity (By similarity). Involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Its binding to DPP4 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner (By similarity). Recruits CTNNB1 to caveolar membranes and may regulate CTNNB1-mediated signaling through the Wnt pathway (By similarity). Negatively regulates TGFB1-mediated activation of SMAD2/3 by mediating the internalization of TGFBR1 from membrane rafts leading to its subsequent degradation (By similarity).
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A1X150
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MET_ECHTE
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Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
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MKAPAALAPGILVLLLTLVQKGGGECREALAKSEMNVNMRYRLPNFTADTPIQNVVVHEGHVFLGAINSIYVLRERDLQQVSEYKTGPVWEHPDCLPCQACGLAGGQWRENVNMALLVETYYDDQLISCGSVHRGTCQRHVLPRDNPADIQAEVHCMHSPRADEDEASQCPDCVVSALGTKVLLAEKQRFVNFFVGNTLNGSSLPGHALHSISVRRIKETQDGFKFLTDKSYIDVLPEFQASYPIKYIHAFESNRFIYFLTVQRETLDSPSFHTRIIRFCSADSGLRSYMEMPLECILTEKRRKRALRSEVFNVLQAAYVGKPGAQLAKQIGASAHDDILYGVFSQSRPDSAEPTDRSALCAFPVKYVDEFFHRIVNKNNVRCLQHFYGPNHLHCFNRTLLRNSSGCEVRSDEYRTEFTTALQRIDLSAGHFSQVLLTSISTFIKGDLTIANLGTSEGRFMQVVVSRSGSWTPHVDFRLDSHAVSPEVIVEHPVNQNGYTLVVTGKKITKIPLDGLGCEHFQSCSQCLSAPPFVQCGWCHDKCARAEDCPNGTWTQEICLPTIYEVFPASAPLEGGTTLTVCGWDFGFRRNNKSDFKRTRVLIGNESCPLTLSESTPNMLKCTVGPAMSEHSNLSIIISNVRGTAPQYRTFSYVDPEITSISPSYGPKAGGTLVTLTGKYLNSGNSRHISIGGKTCTLKSVSDSVLECYTPAQSISADFPVKLKIDLANREAYSFSYQENPLVVEIHPTKSFVSGGSTITVVGKNLNSVSVPRMIINVHEVEMNFTVACQQRSNSELICCTTPSLQQLDLQLPLKATAFFMLDGIHSRDFDLIYVPNPVFKLFEKPVMISMGNENVLEIKGNDIDPEAVKGEVLKVGNKSCENIHSYPESVLCTVPNDLLKLNSELNIEWKQAVSSTVLGKVIVQPDQNFTGLIVGVVSISVILLSSLGLFLWLKKRKQIKDLGSELVCYDARVHTPHLDRLVSARSVSPTTEMVSNESVDYRATFPEDQFPNSSQNGSCRQVQYPLPDLSPILTSGDSDISSPLLQNTVHIDLSALNPELVQAVQHVVIGPSSLIVHFNEVIGRGHFGCVYHGTLLDNDDRKIHCAVKSLNRITDIGEVSQFLTEGIIMKDFSHPNVLSLLGICLRSEGSPLVVLPYMKHGDLRNFIRNETHSPTVKDLIGFGLQVAKGMKYLASKKFVHRDLAARNCMLDGKFTVKVADFGLARDMYDKEYYSVHNKTGAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELMTRGAPPYPDVNTFDITVYLLQGRRLLQPEYCPDPLYEVMLKCWHPKAEMRPSFTELVSRISAIFSTFIGEHYVHVNATYVNVKCVAPYPSLLSSHDTVDGEVDT
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Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to hepatocyte growth factor/HGF ligand. Regulates many physiological processes including proliferation, scattering, morphogenesis and survival. Ligand binding at the cell surface induces autophosphorylation of MET on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with the PI3-kinase subunit PIK3R1, PLCG1, SRC, GRB2, STAT3 or the adapter GAB1. Recruitment of these downstream effectors by MET leads to the activation of several signaling cascades including the RAS-ERK, PI3 kinase-AKT, or PLCgamma-PKC. The RAS-ERK activation is associated with the morphogenetic effects while PI3K/AKT coordinates prosurvival effects. During embryonic development, MET signaling plays a role in gastrulation, development and migration of muscles and neuronal precursors, angiogenesis and kidney formation. In adults, participates in wound healing as well as organ regeneration and tissue remodeling. Promotes also differentiation and proliferation of hematopoietic cells (By similarity).
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A1X283
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SPD2B_HUMAN
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SH3 and PX domain-containing protein 2B (Adapter protein HOFI) (Factor for adipocyte differentiation 49) (Tyrosine kinase substrate with four SH3 domains)
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MPPRRSIVEVKVLDVQKRRVPNKHYVYIIRVTWSSGSTEAIYRRYSKFFDLQMQMLDKFPMEGGQKDPKQRIIPFLPGKILFRRSHIRDVAVKRLIPIDEYCKALIQLPPYISQCDEVLQFFETRPEDLNPPKEEHIGKKKSGGDQTSVDPMVLEQYVVVANYQKQESSEISLSVGQVVDIIEKNESGWWFVSTAEEQGWVPATCLEGQDGVQDEFSLQPEEEEKYTVIYPYTARDQDEMNLERGAVVEVIQKNLEGWWKIRYQGKEGWAPASYLKKNSGEPLPPKPGPGSPSHPGALDLDGVSRQQNAVGREKELLSSQRDGRFEGRPVPDGDAKQRSPKMRQRPPPRRDMTIPRGLNLPKPPIPPQVEEEYYTIAEFQTTIPDGISFQAGLKVEVIEKNLSGWWYIQIEDKEGWAPATFIDKYKKTSNASRPNFLAPLPHEVTQLRLGEAAALENNTGSEATGPSRPLPDAPHGVMDSGLPWSKDWKGSKDVLRKASSDMSASAGYEEISDPDMEEKPSLPPRKESIIKSEGELLERERERQRTEQLRGPTPKPPGVILPMMPAKHIPPARDSRRPEPKPDKSRLFQLKNDMGLECGHKVLAKEVKKPNLRPISKSKTDLPEEKPDATPQNPFLKSRPQVRPKPAPSPKTEPPQGEDQVDICNLRSKLRPAKSQDKSLLDGEGPQAVGGQDVAFSRSFLPGEGPGRAQDRTGKQDGLSPKEISCRAPPRPAKTTDPVSKSVPVPLQEAPQQRPVVPPRRPPPPKKTSSSSRPLPEVRGPQCEGHESRAAPTPGRALLVPPKAKPFLSNSLGGQDDTRGKGSLGPWGTGKIGENREKAAAASVPNADGLKDSLYVAVADFEGDKDTSSFQEGTVFEVREKNSSGWWFCQVLSGAPSWEGWIPSNYLRKKP
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Adapter protein involved in invadopodia and podosome formation and extracellular matrix degradation. Binds matrix metalloproteinases (ADAMs), NADPH oxidases (NOXs) and phosphoinositides. Acts as an organizer protein that allows NOX1- or NOX3-dependent reactive oxygen species (ROS) generation and ROS localization. Plays a role in mitotic clonal expansion during the immediate early stage of adipocyte differentiation (By similarity). {ECO:0000250, ECO:0000269|PubMed:12615925, ECO:0000269|PubMed:19755710, ECO:0000269|PubMed:20609497}.
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A1XBS5
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CBAR1_HUMAN
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CBY1-interacting BAR domain-containing protein 1
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MMRRTLENRNAQTKQLQTAVSNVEKHFGELCQIFAAYVRKTARLRDKADLLVNEINAYAATETPHLKLGLMNFADEFAKLQDYRQAEVERLEAKVVEPLKTYGTIVKMKRDDLKATLTARNREAKQLTQLERTRQRNPSDRHVISQAETELQRAAMDASRTSRHLEETINNFERQKMKDIKTIFSEFITIEMLFHGKALEVYTAAYQNIQNIDEDEDLEVFRNSLYAPDYSSRLDIVRANSKSPLQRSLSAKCVSGTGQVSTCRLRKDQQAEDDEDDELDVTEEENFLK
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Acts as a positive regulator of ciliary hedgehog signaling (By similarity). Probable regulator of ciliogenesis involved in limb morphogenesis. In cooperation with CBY1 it is involved in the recruitment and fusion of endosomal vesicles at distal appendages during early stages of ciliogenesis. Plays an important role in the mitochondrial function and is essential for maintaining mitochondrial morphology and inner membrane ultrastructure. In vitro, can generate membrane curvature through preferential interaction with negatively charged phospholipids such as phosphatidylinositol 4,5-bisphosphate and cardiolipin and hence orchestrate cristae shape.
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A1XGB4
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PIMP1_CAPAN
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CASP-like protein PIMP1 (CASP-like protein 4D1) (CaCASPL4D1) (Pathogen-induced membrane protein 1) (CaPIMP1)
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MTPPPTSTVPPYVSLIVRILTLICLLISFIVIATNNQTVSTVAGDVKIKFKDFYAYRYLIATVIIGMAYTLLQIAFSISLLTTGNRIGGEGFLLFDFYGDKFISYFLVTGAAASFGMTQDLKQLEGSDNYSKFLNTSNAAASLCLIGFFFAVASSIFSSYNLPKRI
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Required for defense response to Xanthomonas campestris pv. vesicatoria (Xcv). In heterologous systems, confers resistance to bacterial pathogens such as Pseudomonas syringae pv. tomato but susceptibility to pathogenic oomycetes such as Hylaloperonospora parasitica when expressed in Arabidopsis thaliana. May be involved in the regulation of responses to bitoic and abiotic stresses.
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A1XLE2
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TFP_LEPSV
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Phenyl-N-(sulfonatooxy)methanimidothioate sulfolyase (EC 4.8.1.7) (EC 4.8.1.8) (Thiocyanate-forming protein) (LsTFP) (LsatTFP)
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MALTLQGEWIKIEQKGGPAPGPRSSHCMAVVGDKLYMFGGELKPQFHLDKHLYVFDFKTNTWSIAEPKGEAPSLSCLGVRMVAVGTKIYIFGGRDENRNYSDFYSYDTVKKEWKFLTKLDEERVPEARSFPAIAADDNHVYIFGGVSKGGVQSTPFRFKSTIVYNIAEGTWSQLPNPGPDFEPRGGAGLAVIDKKLWVVCGFANSTSGGINDYNSNKVQYYDLVSGKWIEVKTSGVKPSGRSVFAYAVIGKQIVIYGGEIFRDENGHLGPGTMSNEGYALDTETLVWEKLVDGGEPMTPLGWTANCTGTVYGKTGLLMHGGKQPFNNRTDDFYFYSF
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Specifier protein that contributes to constitutive and herbivore-induced simple nitrile formation (By similarity). Catalyzes thiocyanate and simple nitrile formation from benzylglucosinolate in the presence of myrosinase. Converts also aliphatic glucosinolates to both epithionitriles and simple nitriles.
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A1XRN2
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PLIA_ATRNM
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Phospholipase A2 inhibitor anMIP (alpha-PLI) (Myotoxic phospholipase A2 inhibitory protein) (MIP)
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MRLILLSGLLLLGTFLANGDEKDSDVQMLNSMIEAVMILQRDFANLRHALMTVHNARSFGRGSERLYVTNKEVSKFEGLEEICSQAGGHIPSPQLENQNKAFEDVLERHNKAAYLVVGDSANFTNWAAGQPNEADGTCVKADTHGSWHSASCDDNLLVVCEFYFIL
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This phospholipase A2 inhibitor neutralizes the activity of basic PLA2 myotoxins of its own and related venoms. The inhibitory profile shows specificity towards group II PLA2, either belonging to the catalytically-active (D49) or -inactive (K49) subtypes.
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A1XSY8
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EGR2_PIG
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E3 SUMO-protein ligase EGR2 (EC 2.3.2.-) (E3 SUMO-protein transferase ERG2) (Early growth response protein 2) (EGR-2)
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MMTAKAVDKIPVTLSGFVHQLSDNIYPVEDLAATSVTIFPNAELGSPFDQMNGVAGDGMINIDMTGEKRSLDLPYPSSFAPVSAPRNQTFTYMGKFSIDPQYPGASCYPEGIINIVSAGILQGVTSPASTTASSNVTSASPNPLATGPLGVCTMSQTQPDLDHLYSPPPPPPYSGCAGDLYQDPSAFLSAATTSTSSSLAYPPPPSYPSPKPATDPGLFPMIPDYPGFFPSQCQRDLHGTAGPDRKPFPCPLDSLRVPPPLTPLSTIRNFTLGGPSAGTTGPGASGGSEGPRLPGSSAAAAAAAYNPHHLPLRPILRPRKYPNRPSKTPVHERPYPCPAEGCDRRFSRSDELTRHIRIHTGHKPFQCRICMRNFSRSDHLTTHIRTHTGEKPFACDYCGRKFARSDERKRHTKIHLRQKERKSSAPSSSVPAASTASCTGGAQPGGPLCSSNSSTIGGGSLGPCSSRTRTP
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Sequence-specific DNA-binding transcription factor (By similarity). Plays a role in hindbrain segmentation by regulating the expression of a subset of homeobox containing genes and in Schwann cell myelination by regulating the expression of genes involved in the formation and maintenance of myelin (By similarity). Binds to two EGR2-consensus sites EGR2A (5'-CTGTAGGAG-3') and EGR2B (5'-ATGTAGGTG-3') in the HOXB3 enhancer and promotes HOXB3 transcriptional activation (By similarity). Binds to specific DNA sites located in the promoter region of HOXA4, HOXB2 and ERBB2 (By similarity). Regulates hindbrain segmentation by controlling the expression of Hox genes, such as HOXA4, HOXB3 and HOXB2, and thereby specifying odd and even rhombomeres (By similarity). Promotes the expression of HOXB3 in the rhombomere r5 in the hindbrain (By similarity). Regulates myelination in the peripheral nervous system after birth, possibly by regulating the expression of myelin proteins, such as MPZ, and by promoting the differentiation of Schwann cells (By similarity). Involved in the development of the jaw openener musculature, probably by playing a role in its innervation through trigeminal motor neurons (By similarity). May play a role in adipogenesis, possibly by regulating the expression of CEBPB (By similarity). E3 SUMO-protein ligase helping SUMO1 conjugation to its coregulators NAB1 and NAB2, whose sumoylation down-regulates EGR2 transcriptional activity.
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A1XWY7
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CFAT_PETHY
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Coniferyl alcohol acyltransferase (PhCFAT) (EC 2.3.1.-) ((E)-cinnamyl alcohol acyltransferase) (EC 2.3.1.224) ((E)-sinapoyl alcohol acyltransferase) (EC 2.3.1.-) (Geraniol acyltransferase) (EC 2.3.1.-) (Octan-1-ol acyltransferase) (EC 2.3.1.-)
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MGNTDFHVTVKKKEVVAAVLPMHHEHWLPMSNLDLLLPPLDFGVFFCYKRSKINNDTKDDDETIKKALAETLVSFYALAGEVVFNSLGEPELLCNNRGVDFFHAYADIELNNLDLYHPDVSVHEKLIPIKKHGVLSVQVTGLKCGGIVVGCTFDHRVADAYSANMFLVAWAAIARKDNNINTVIPSFRRSLLNPRRPPQFDDSFIDSTYVFLSSPPKQPNDVLTSRVYYINSQEINLLQSQATRNGSKRSKLECFSAFLWKTIAEGGIDDSKRCKLGIVVDGRQRLRHDSSTTMKNYFGNVLSVPYTEASVGQLKQTPLGKVADLVHTCLDNVANEHHFPSLIDWVELHRPRQAIVKVYCKDECNDEAAIVVSSGLRFPLSQVNFGWGCPDFGSYIFPWGGQTGYVMPMPSPNKNGDWIVYMHLQKKHLDLVETRAPHIFHPLTACYLDLTATY
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Acyltransferase involved in the biosynthesis of the floral volatile isoeugenol, and which promotes the formation of phenylacetaldehyde, phenylethyl alcohol, phenyl-ethyl acetate, phenylethyl benzoate and benzyl acetate. Catalyzes the acetylation of coniferyl alcohol to produce coniferyl acetate. Also active toward 1-octanol, cinnamyl alcohol, geraniol and sinapyl alcohol.
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A1Y2K1
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FYN_PIG
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Tyrosine-protein kinase Fyn (EC 2.7.10.2) (Proto-oncogene c-Fyn) (p59-Fyn)
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MGCVQCKDKEATKLTEERDGSLNQSSGFRYGTDPTPQHYPSFGVTSIPNYNNFHAAGGQGLTVFGGVSSSSHTGTLRTRGGTGVTLFVALYDYEARTEDDLSFHKGEKFQILNSSEGDWWEARSLTTGETGYIPSNYVAPVDSIQAEEWYFGKLGRKDAERQLLSFGNPRGTFLIRESETTKGAYSLSIRDWDDMKGDHVKHYKIRKLDNGGYYITTRAQFETLQQLVQHYSERAAGLCCRLVVPCHKGMPRLTDLSVKTKDVWEIPRESLQLIKRLGNGQFGEVWMGTWNGNTKVAIKTLKPGTMSPESFLEEAQIMKKLKHDKLVQLYAVVSEEPIYIVTEYMNKGSLLDFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPQDCPISLHELMIHCWKKDPEERPTFEYLQGFLEDYFTATEPQYQPGENL
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Non-receptor tyrosine-protein kinase that plays a role in many biological processes including regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. Inactive FYN is phosphorylated on its C-terminal tail within the catalytic domain. Following activation by PKA, the protein subsequently associates with PTK2/FAK1, allowing PTK2/FAK1 phosphorylation, activation and targeting to focal adhesions. Involved in the regulation of cell adhesion and motility through phosphorylation of CTNNB1 (beta-catenin) and CTNND1 (delta-catenin). Regulates cytoskeletal remodeling by phosphorylating several proteins including the actin regulator WAS and the microtubule-associated proteins MAP2 and MAPT. Promotes cell survival by phosphorylating AGAP2/PIKE-A and preventing its apoptotic cleavage. Participates in signal transduction pathways that regulate the integrity of the glomerular slit diaphragm (an essential part of the glomerular filter of the kidney) by phosphorylating several slit diaphragm components including NPHS1, KIRREL1 and TRPC6. Plays a role in neural processes by phosphorylating DPYSL2, a multifunctional adapter protein within the central nervous system, ARHGAP32, a regulator for Rho family GTPases implicated in various neural functions, and SNCA, a small pre-synaptic protein. Participates in the downstream signaling pathways that lead to T-cell differentiation and proliferation following T-cell receptor (TCR) stimulation. Phosphorylates PTK2B/PYK2 in response to T-cell receptor activation. Also participates in negative feedback regulation of TCR signaling through phosphorylation of PAG1, thereby promoting interaction between PAG1 and CSK and recruitment of CSK to lipid rafts. CSK maintains LCK and FYN in an inactive form. Promotes CD28-induced phosphorylation of VAV1. In mast cells, phosphorylates CLNK after activation of immunoglobulin epsilon receptor signaling (By similarity).
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A1Y9I9
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TOMT_MOUSE
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Transmembrane O-methyltransferase homolog (mTOMT) (EC 2.1.1.6) (Catechol O-methyltransferase 2)
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MSPAIALAFLPLVVTLLVRYRHHFRLLVRTVLLRGFRDCLSGLRIEERAFSYVLTHALPGDPGHILTTLDHWSSCCEYLSHMGPVKGQILMRLVEEKAPACVLELGTYCGYSTLLIARALPPGSRLLTVERDSRTAAVAEKVIRLAGFDEQMVELIAGSSEEVIPRLRAQHQLNRADLVLLAHRPRYYLRDLQLLEAHALLPHGATVLADHVLFPGAPRFLQYTKSCGRYRCRLHHTSLPDFPAIKDGIAQLTYTGPG
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Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Required for auditory function. Component of the cochlear hair cell's mechanotransduction (MET) machinery. Involved in the assembly of the asymmetric tip-link MET complex. Required for transportation of TMC1 and TMC2 proteins into the mechanically sensitive stereocilia of the hair cells. The function in MET is independent of the enzymatic activity.
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A1YB07
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AMOL2_DANRE
|
Angiomotin-like 2a
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MRTAEESSGTVLHRLIQEQLRYGNPTDPTLLAIQQQALRGGSSGGGAGSPRSSLESLTQEESLSPQLSARQEPQGQEHQGDFQHSESPVCHLYQLHTEELPTYEEAKAHSQYLAYQRGQIGLHQGSLESPGGVGGAEQDDSMWDAKREHARSLSERLLQLSLERNCAHDNIPMSSSHSYPQLSNNHSDTVVNEQSVHQPDQRGPPPEYPFMVRSPGYMLSHSQEHGHYYNEPPPAFHSQHYRLFPTQPQAPRHNGLPTLTPAGQDVNVGGYSIPANNFQMEQLIKENERLKREVDSYSEKAARLQKLEQEIQRISEAYETLMKGSAKREALEKTMRNKLESEIKRLHDFNRDLRDRLETANKQRAAIEVEDKSRHAFAKLVEQNEDHLRERERLEKETQHLRASGEEWKRRREALEQALITAQTRNRQLEEELRRKRAYVEKVERMQSALAQLQAACEKREALELRLRTRLEQELKSLRAQQWQAQTQHASPGSYLDLNVSSLQQQLREREEQVLALEADITRWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRNSPNSSFNEDLPSPNHRHQEMENRIRALYAQLLEKDAIIKVMQQRSRREQGRPELQGLRPARSVPSINTVATASTTRAKGKSLSDDQTAVASLPPLPHLLAKIQCRDSSTQCDSEEPSCKAEPADVAVSAPEPSTASSSESTSLKTTQISSAVENDMVEILI
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Regulates the translocation of phosphorylated SRC to peripheral cell-matrix adhesion sites. Required for proper architecture of actin filaments and for cell movements during embryogenesis. Inhibits the Wnt/beta-catenin signaling pathway, probably by recruiting CTNNB1 to recycling endosomes and hence preventing its translocation to the nucleus. Participates in angiogenesis. May play a role in the polarity, proliferation and migration of endothelial cells. Selectively promotes FGF-induced MAPK activation through SRC.
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A1YER0
|
SIX1_GORGO
|
Homeobox protein SIX1 (Sine oculis homeobox homolog 1)
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MSMLPSFGFTQEQVACVCEVLQQGGNLERLGRFLWSLPACDHLHKNESVLKAKAVVAFHRGNFRELYKILESHQFSPHNHPKLQQLWLKAHYVEAEKLRGRPLGAVGKYRVRRKFPLPRTIWDGEETSYCFKEKSRGVLREWYAHNPYPSPREKRELAEATGLTTTQVSNWFKNRRQRDRAAEAKERENTENNNSSSNKQNQLSPLEGGKPLMSSSEEEFSPPQSPDQNSVLLLQGNMGHARSSNYSLPGLTASQPSHGLQTHQHQLQDSLLGPLTSSLVDLGS
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Transcription factor that is involved in the regulation of cell proliferation, apoptosis and embryonic development (By similarity). Plays an important role in the development of several organs, including kidney, muscle and inner ear (By similarity). Depending on context, functions as transcriptional repressor or activator (By similarity). Lacks an activation domain, and requires interaction with EYA family members for transcription activation (By similarity). Mediates nuclear translocation of EYA1 and EYA2 (By similarity). Binds the 5'-TCA[AG][AG]TTNC-3' motif present in the MEF3 element in the MYOG promoter and CIDEA enhancer (By similarity). Regulates the expression of numerous genes, including MYC, CCNA1, CCND1 and EZR (By similarity). Acts as activator of the IGFBP5 promoter, probably coactivated by EYA2 (By similarity). Repression of precursor cell proliferation in myoblasts is switched to activation through recruitment of EYA3 to the SIX1-DACH1 complex (By similarity). During myogenesis, seems to act together with EYA2 and DACH2 (By similarity). Regulates the expression of CCNA1 (By similarity). Promotes brown adipocyte differentiation (By similarity).
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A1YES6
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APEX1_GORGO
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DNA-(apurinic or apyrimidinic site) endonuclease (EC 3.1.11.2) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) endonuclease, mitochondrial]
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MPKRGKKGAVAEDGDELKTEPEAKKSKTAAKKNDKEAAGEGPALYEDPPDQKTSPSGKPATLKICSWNVDGLRAWIKKKGLDWVKEEAPDILCLQETKCSENKLPAELQELPGLSYQYWSAPXXKEGYSGVGLLSRQCPLKVSYGIGEEEHDQEGRVIVAEFDSFVLVTAYVPNAGRGLVRLEYRQRWDEAFRRFLKGLASRKPLVLCGDLNVAHEEIDLRNPKGNKKNAGFTPQERQGFGELLQAVPLADSFRHLYPNTPYAYTFWTYMMNARSKNVGWRLDYFLLSHSLLPALCDSKIRSKALGSDHCPITLYLAL
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Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 are DNA repair and redox regulation of transcriptional factors. Functions as a apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Does also incise at AP sites in the DNA strand of DNA/RNA hybrids, single-stranded DNA regions of R-loop structures, and single-stranded RNA molecules. Has a 3'-5' exoribonuclease activity on mismatched deoxyribonucleotides at the 3' termini of nicked or gapped DNA molecules during short-patch BER. Possesses a DNA 3' phosphodiesterase activity capable of removing lesions (such as phosphoglycolate) blocking the 3' side of DNA strand breaks. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation. Acts as a loading factor for POLB onto non-incised AP sites in DNA and stimulates the 5'-terminal deoxyribose 5'-phosphate (dRp) excision activity of POLB. Plays a role in the protection from granzymes-mediated cellular repair leading to cell death. Also involved in the DNA cleavage step of class switch recombination (CSR). On the other hand, APEX1 also exerts reversible nuclear redox activity to regulate DNA binding affinity and transcriptional activity of transcriptional factors by controlling the redox status of their DNA-binding domain, such as the FOS/JUN AP-1 complex after exposure to IR. Involved in calcium-dependent down-regulation of parathyroid hormone (PTH) expression by binding to negative calcium response elements (nCaREs). Together with HNRNPL or the dimer XRCC5/XRCC6, associates with nCaRE, acting as an activator of transcriptional repression. Stimulates the YBX1-mediated MDR1 promoter activity, when acetylated at Lys-6 and Lys-7, leading to drug resistance. Acts also as an endoribonuclease involved in the control of single-stranded RNA metabolism. Plays a role in regulating MYC mRNA turnover by preferentially cleaving in between UA and CA dinucleotides of the MYC coding region determinant (CRD). In association with NMD1, plays a role in the rRNA quality control process during cell cycle progression. Associates, together with YBX1, on the MDR1 promoter. Together with NPM1, associates with rRNA. Binds DNA and RNA (By similarity).
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A1YF08
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PDX1_GORGO
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Pancreas/duodenum homeobox protein 1 (Homeodomain protein PDX1) (Insulin promoter factor 1) (IPF-1)
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MNGEEQYYAATQLYKDPCAFQRGPAPEFSASPPACLYMGRQPPPPPPPHPFPGALGALEQGSPPDISPYEVPPLADDPAVAHLHHHLPAQLALPHPPAGPFPEGAEPGVLEEPNRVQLPFPWMKSTKAHAWKGQWAGGAYAAEPEENKRTRTAYTRAQLLELEKEFLFNKYISRPRRVELAVMLNLTERHIKIWFQNRRMKWKKEEDKKRGGGTAVGGGGVAEPEQDCAVTSGEELLALPPPPPPGGAVPPAAPVAAREGRLPPGLSASPQPSSVAPRRPQEPR
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Activates insulin and somatostatin gene transcription. Key regulator of islet peptide hormone expression but also responsible for the development of the pancreas, most probably by determining maturation and differentiation of common pancreatic precursor cells in the developing gut. Binds the DNA sequence 5'-CC[CT]TAATGGG-3' (By similarity).
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A1YFZ3
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APEX1_PANPA
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DNA-(apurinic or apyrimidinic site) endonuclease (EC 3.1.11.2) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) endonuclease, mitochondrial]
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MPKRGKKGAVAEDGDELRTEPEAKKSKTAAKKNDKEAAGEGPALYEDPPDQKTSPSGKPATLKICSWNVDGLRAWIKKKGLDWVKEEAPDILCLQETKCSENKLPAELQELPGLSHQYWSAPSDKEGYSGVGLLSRQCPLKVSYGIGEEEHDQEGRVIVAEFDSFVLVTAYVPNAGRGLVRLEYRQRWDEAFRKFLKGLASRKPLVLCGDLNVAHEEIDLRNPKGNKKNAGFTPQERQGFGELLQAVPLADSFRHLYPNTPYAYTFWTYMMNARSKNVGWRLDYFLLSHSLLPALCDSKIRSKALGSDHCPITLYLAL
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Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 are DNA repair and redox regulation of transcriptional factors. Functions as a apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Does also incise at AP sites in the DNA strand of DNA/RNA hybrids, single-stranded DNA regions of R-loop structures, and single-stranded RNA molecules. Has a 3'-5' exoribonuclease activity on mismatched deoxyribonucleotides at the 3' termini of nicked or gapped DNA molecules during short-patch BER. Possesses a DNA 3' phosphodiesterase activity capable of removing lesions (such as phosphoglycolate) blocking the 3' side of DNA strand breaks. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation. Acts as a loading factor for POLB onto non-incised AP sites in DNA and stimulates the 5'-terminal deoxyribose 5'-phosphate (dRp) excision activity of POLB. Plays a role in the protection from granzymes-mediated cellular repair leading to cell death. Also involved in the DNA cleavage step of class switch recombination (CSR). On the other hand, APEX1 also exerts reversible nuclear redox activity to regulate DNA binding affinity and transcriptional activity of transcriptional factors by controlling the redox status of their DNA-binding domain, such as the FOS/JUN AP-1 complex after exposure to IR. Involved in calcium-dependent down-regulation of parathyroid hormone (PTH) expression by binding to negative calcium response elements (nCaREs). Together with HNRNPL or the dimer XRCC5/XRCC6, associates with nCaRE, acting as an activator of transcriptional repression. Stimulates the YBX1-mediated MDR1 promoter activity, when acetylated at Lys-6 and Lys-7, leading to drug resistance. Acts also as an endoribonuclease involved in the control of single-stranded RNA metabolism. Plays a role in regulating MYC mRNA turnover by preferentially cleaving in between UA and CA dinucleotides of the MYC coding region determinant (CRD). In association with NMD1, plays a role in the rRNA quality control process during cell cycle progression. Associates, together with YBX1, on the MDR1 promoter. Together with NPM1, associates with rRNA. Binds DNA and RNA (By similarity).
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A1YG22
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MYC_PANPA
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Myc proto-oncogene protein (Proto-oncogene c-Myc) (Transcription factor p64)
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MPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSGSPNPARGHSVCSTSSLYLQDLSAAASECIDPSVVFPYPLNDGSSPKSCPSQDSSAFSPSSDSLLSSTESSPQGSPEPLVLHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQAPGKRSESGSPSAGGHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRVKLDSVRVLRQISNNRKCTSPRSSDTEENDKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSVQAEEQKLISEEDLLRKRREQLKHKLEQLRNSCA
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Transcription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. Activates the transcription of growth-related genes. Binds to the VEGFA promoter, promoting VEGFA production and subsequent sprouting angiogenesis. Regulator of somatic reprogramming, controls self-renewal of embryonic stem cells. Functions with TAF6L to activate target gene expression through RNA polymerase II pause release (By similarity). Positively regulates transcription of HNRNPA1, HNRNPA2 and PTBP1 which in turn regulate splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform (By similarity).
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A1YG32
|
S38A2_PANPA
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Sodium-coupled neutral amino acid symporter 2 (Amino acid transporter A2) (Solute carrier family 38 member 2) (System A amino acid transporter 2) (System A transporter 1) (System N amino acid transporter 2)
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MKKAEMGRFNISPDEDSSSYSSNSDFNYSYPTKQAALKSHYADVDPENQNFLLESNLGKKKYETEFHPGTTSFGMSVFNLSNAIVGSGILGLSYAMANTGIALFIILLTFVSIFSLYSVHLLLKTANEGGSLLYEQLGYKAFGLVGKLAASGSITMQNIGAMSSYLFIVKYELPLVIQALTNIEDKTGLWYLNGNYLVLLVSLVVILPLSLFRNLGYLGYTSGLSLLCMVFFLIVVICKKFQVPCPVEAALIINETINTTLTQPTALVPALSHNVTENDSCRPHYFIFNSQTVYAVPILIFSFVCHPAVLPIYEELKDRSRRRMMNVSKISFFAMFLMYLLAALFGYLTFYEHVESELLHTYSSILGTDILLLIVRLAVLMAVTLTVPVVIFPIRSSVTHLLCASKDFSWWRHSLITVSILAFTNLLVIFVPTIRDIFGFIGASAASMLIFILPSAFYIKLVKKEPMKSVQKIGALFFLLSGVLVMTGSMALIVLDWVHNAPGGGH
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Symporter that cotransports neutral amino acids and sodium ions from the extraccellular to the intracellular side of the cell membrane. The trasnport is pH-sensitive, Li(+)-intolerant, electrogenic, driven by the Na(+) electrochemical gradient and cotransports of neutral amino acids and sodium ions with a stoichiometry of 1:1. May function in the transport of amino acids at the blood-brain barrier (By similarity). May function in the transport of amino acids in the supply of maternal nutrients to the fetus through the placenta (By similarity). Maintains a key metabolic glutamine/glutamate balance underpinning retrograde signaling by dendritic release of the neurotransmitter glutamate (By similarity). Transports L-proline in differentiating osteoblasts for the efficient synthesis of proline-enriched proteins and provides proline essential for osteoblast differentiation and bone formation during bone development (By similarity).
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A1YKT1
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TCP18_ARATH
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Transcription factor TCP18 (Protein BRANCHED 1) (Protein TEOSINTE BRANCHED 1-LIKE 1)
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MNNNIFSTTTTINDDYMLFPYNDHYSSQPLLPFSPSSSINDILIHSTSNTSNNHLDHHHQFQQPSPFSHFEFAPDCALLTSFHPENNGHDDNQTIPNDNHHPSLHFPLNNTIVEQPTEPSETINLIEDSQRISTSQDPKMKKAKKPSRTDRHSKIKTAKGTRDRRMRLSLDVAKELFGLQDMLGFDKASKTVEWLLTQAKPEIIKIATTLSHHGCFSSGDESHIRPVLGSMDTSSDLCELASMWTVDDRGSNTNTTETRGNKVDGRSMRGKRKRPEPRTPILKKLSKEERAKARERAKGRTMEKMMMKMKGRSQLVKVVEEDAHDHGEIIKNNNRSQVNRSSFEMTHCEDKIEELCKNDRFAVCNEFIMNKKDHISNESYDLVNYKPNSSFPVINHHRSQGAANSIEQHQFTDLHYSFGAKPRDLMHNYQNMY
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Transcription factor that prevents axillary bud outgrowth and delays early axillary bud development. Indirectly required for the auxin-induced control of apical dominance.
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A1YKW7
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RTXA_KINKI
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Cytolysin RtxA (Repeats in toxin A)
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MNLATTKAKLKSGAQAGVQALNKAGHAAKTGTVAAGKATVAGAKSLYLTIPKDYDIEKGGSLNELIKAADELGIARLQEDANNIESAKKSIDTVEKLLSFTQTGVAVSAKKLDELLQKYSSSQLAKSLGSSANIDSKLTKTNHILSTLSSFLGTALAGMDLDSLVKQGDASATDLAKASLDLINELVNNISNSVQSIEAFSEQLGRLGAAISQTKGLSGLGNKLQNLPNFGKANLALEMISGLLSGISAGFTLADKNASTEKKVAAGFELSNQVIGNVTKAISSYVLAQRAAAGLSTTGAVASLITASIMLAISPLAFMNAADKFKNASLIDEFAKQFKKFGYDGDSLLAEYQRGAGTIEASLTAINTALGAVSAGVSAAAVGSVVGSPVALLVAGVTGLISGILEASKQAMFESVANRLQSKILAWEKENGGKNYFENGYDARHAHYLERNLKLLSELNKELQAERVIAITQQRWDANIGELAGITKLGDRISSGKAYADAFEDGKKLDGASNVTVDTRTGVVDISNANGKKTQALHFTSPLLTAGTETRERVQNGKYSYINQLKFNRVKSWTVKDGEANSRLDFSKVIQHVAFNDEDGRLSGKTEEIALNVNAGSGNDDIFAGQGKMNVDGGTGHDRVFYSKDGGLGQVNVDGTKATEAGSYTVNRSINNGSFYHEVIKRQTTQVGKRTETLEYRDFELKRPEHGYQTTDTLKSVEEIVGSQFSDTFKGSKFADIFHGGDGNDTLEGNDGDDRLFGGNGDDHLYGGNGDDLLDGGKGNDVINGGDGNDVYISRKGDGNDTLYDSHGSDKLAFADADLSELTIERTAQGIMIKRNDGSGSINMAEWYKTLSQQNYHGNATDDKIEQIIGKNGDYITSEQIDKLLKDKQTGTITSAQLQQLAQENKSKSIDSGNLASTLNKLIESMASFGSRGATASNYLQPAHKSPQNVLAPSAV
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Bacterial cytolysin that attacks host cell membranes and causes cell rupture by forming a pore. Binds and permeabilizes target cells by forming cation-selective pores. Constitutes the key virulence cytotoxin of K.kingae. Binds cholesterol and oligosaccharides on the surface of host cells. Does not bind beta-2 integrin (ITGB2) on the host cell surface.
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A1YYW7
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ALPH_SPHSX
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Alkaline phosphatase PhoK (EC 3.1.3.1) (SPAP protein)
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MLKHVAAALLLATAMPVVAQSPAPAAAPAPAARSIAATPPKLIVAISVDQFSADLFSEYRQYYTGGLKRLTSEGAVFPRGYQSHAATETCPGHSTILTGSRPSRTGIIANNWFDLDAKREDKNLYCAEDESQPGSSSDKYEASPLHLKVPTLGGRMKAANPATRVVSVAGKDRAAIMMGGATADQVWWLGGPQGYVSYKGVAPTPLVTQVNQAFAQRLAQPNPGFELPAQCVSKDFPVQAGNRTVGTGRFARDAGDYKGFRISPEQDAMTLAFAAAAIENMQLGKQAQTDIISIGLSATDYVGHTFGTEGTESCIQVDRLDTELGAFFDKLDKDGIDYVVVLTADHGGHDLPERHRMNAMPMEQRVDMALTPKALNATIAEKAGLPGKKVIWSDGPSGDIYYDKGLTAAQRARVETEALKYLRAHPQVQTVFTKAEIAATPSPSGPPESWSLIQEARASFYPSRSGDLLLLLKPRVMSIPEQAVMGSVATHGSPWDTDRRVPILFWRKGMQHFEQPLGVETVDILPSLAALIKLPVPKDQIDGRCLDLVAGKDDSCAGQ
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Alkaline phosphatase with broad substrate specificity. Precipitates uranium from alkaline solutions.
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A1Z0M0
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HEPC_LARCR
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Hepcidin
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MKTFSVAVAVAVVLAFICLQESSAVPANEEQELEQQIYFADPEMPVESCKMPYYMRENRQGSPARCRFCCRCCPRMRGCGICCRF
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Seems to act as a signaling molecule involved in the maintenance of iron homeostasis. Seems to be required in conjunction with HFE to regulate both intestinal iron absorption and iron storage in macrophages (By similarity). Has very strong antibacterial activity against the marine Gram-negative bacteria V.alginolyticus (MIC=24 uM), V.fluvialis, V.harveyis (MIC=12 uM) and V.parahaemolyticus (MIC=6 uM). Has antibacterial activity against the Gram-negative bacteria A.hydrophila (MIC=6 uM), E.coli (MIC=24 uM), and E.coli BL21(DE3)plysS (MIC=6 uM), and the Gram-positive bacteria B.cereus (MIC=24 uM), B.subtilis (MIC=6 uM), C.glutamicum (MIC=3 uM), M.luteus (MIC=3 uM), M.lysodeikticus, S.aureus (MIC=6 uM) and S.epidermis (MIC=12 uM). Possesses antifungal activity against A.niger (MIC=24 uM), F.graminearum (MIC24 uM) and F.solani (MIC=24 uM), but lacks antifungal activity against the yeasts P.pastoris GS115 and C.albicans.
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A1Z198
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NL1B2_MOUSE
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NACHT, LRR and PYD domains-containing protein 1b allele 2 (EC 3.4.-.-) [Cleaved into: NACHT, LRR and PYD domains-containing protein 1b, C-terminus (Nlrp1b1-CT); NACHT, LRR and PYD domains-containing protein 1b, N-terminus (Nlrp1b1-NT)]
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MEESQYKQEHNKKVAQDEGQEDKDTIFETIEAIEAKLMELKTNPESTFNYGIFPEVYMNQGEEILYPAWSLKEENLFQTFKSLRLFQKLCPRGSGNLVKKSWYPCVPEEGGHIINIQDLFGPNIGTQKEPQLVIIEGAAGIGKSTLARQVKRAWMEGELYRDHFQHVFFFSCRELAQCKKLSLAELITQGQDVPTAPINQILSHPEKLLFILDGIDEPAWVLADQNPELCLYWSQTQPVHTLLGSLLGKSILPEASFLLTTRTTALQKFIPSLPQSCQVEVLGFSDFEQEIYIYKYFAKQIFGIKALMMVESNPVLLTLCEVPWVCWLVCNCLKKQMEQGGDVSLTSQTTTAICLKYISLTIPVHHMRTQLRALCSLAAEGIWKRRTLFSESDLCKQGLDEDAVAIFLKTGVLQKQASSLSYSFAHLCLQEFFASMSCILEDSEERHGDMEMDRIVETLVERYGRQNLFEAPTVRFLFGLLSKEGLKEMEKLFSCSLPGKTKLKLLWHILGKSQPHQPPCLGLLHCLYENQDMKLLTHVMHDLQGTIVPDTDDITHTVLQTNVKHLVVRTDMELMVVTFCIQFCSHMRSLQLNMEGQQGYALTAPRMVLYRWTPITNASWKILFYNLKFNSNLEGLDLSGNPLSYSAVQYLCDAMIYPGCQLKTLWLVECGLTPTYCSLLASVLSACSSLRELDLQLNDLCDDGVRMLCEGLRNRACNLRILRLDLYSLSAQVITELRTLEENNLKLHISSIWMPQMMVPTENMDEEDILTSFKQQRQQSGANPMEILGTEEDFWGPIGPVATEVVYRERNLYRVQLPMAGSYHCPSTRLHFVVTRAVTIEIEFCAWSQFLDKTPLQQSHMVVGPLFDIKAEQGAVTAVYLPHFVSLKDTKASTFDFKVAHFQEHGMVLETPDRVKPGYTVLKNPSFSPMGVVLRIIPAARHFIPITSITLIYYRVNQEEVTLHLYLVPNDCTIQKAIDDEEMKFQFVRINKPPPVDNLFIGSRYIVSGSENLEITPKELELCYRSSKEFQLFSEIYVGNMGSEIKLQIKNKKHMKLIWEALLKPGDLRPALPRIAQALKDAPSLLHFMDQHREQLVARVTSVDPLLDKLHGLVLNEESYEAVRAENTNQDKMRKLFNLSRSWSRACKDLFYQALKETHPHLVMDLLEKSGGVSLGS
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Acts as the sensor component of the Nlrp1b inflammasome, which mediates inflammasome activation in response to various pathogen-associated signals, leading to subsequent pyroptosis (By similarity). Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation (By similarity). Acts as a recognition receptor (PRR): recognizes specific pathogens and other damage-associated signals: in response to pathogen-associated signals, the N-terminal part of Nlrp1b is degraded by the proteasome, releasing the cleaved C-terminal part of the protein (NACHT, LRR and PYD domains-containing protein 1b, C-terminus), which polymerizes to initiate the formation of the inflammasome complex: the inflammasome directly recruits pro-caspase-1 (proCASP1) independently of PYCARD/ASC and promotes caspase-1 (CASP1) activation, which subsequently cleaves and activates inflammatory cytokines IL1B and IL18 and gasdermin-D (GSDMD), leading to pyroptosis (By similarity). In the absence of GSDMD expression, the Nlrp1b inflammasome is able to recruit and activate CASP8, leading to activation of gasdermin-E (GSDME) (By similarity). Activation of Nlrp1b inflammasome is also required for HMGB1 secretion the active cytokines and HMGB1 stimulate inflammatory responses (By similarity). Contrary to Nlrp1b allele 1, allele 2 is not activated by Bacillus anthracis lethal toxin. [NACHT, LRR and PYD domains-containing protein 1b allele 2]: Constitutes the precursor of the Nlrp1b inflammasome, which mediates autoproteolytic processing within the FIIND domain to generate the N-terminal and C-terminal parts, which are associated non-covalently in absence of pathogens and other damage-associated signals. [NACHT, LRR and PYD domains-containing protein 1b, N-terminus]: Regulatory part that prevents formation of the Nlrp1b inflammasome: in absence of pathogens and other damage-associated signals, interacts with the C-terminal part of Nlrp1b (NACHT, LRR and PYD domains-containing protein 1b, C-terminus), preventing activation of the Nlrp1b inflammasome. In response to pathogen-associated signals, this part is ubiquitinated by the N-end rule pathway and degraded by the proteasome, releasing the cleaved C-terminal part of the protein, which polymerizes and forms the Nlrp1b inflammasome. [NACHT, LRR and PYD domains-containing protein 1b, C-terminus]: Constitutes the active part of the Nlrp1b inflammasome. In absence of pathogens and other damage-associated signals, interacts with the N-terminal part of Nlrp1b (NACHT, LRR and PYD domains-containing protein 1b, N-terminus), preventing activation of the Nlrp1b inflammasome. In response to pathogen-associated signals, the N-terminal part of Nlrp1b is degraded by the proteasome, releasing this form, which polymerizes to form the Nlrp1b inflammasome complex: the Nlrp1b inflammasome complex then directly recruits pro-caspase-1 (proCASP1) and promotes caspase-1 (CASP1) activation, leading to gasdermin-D (GSDMD) cleavage and subsequent pyroptosis.
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A1Z1Q3
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MACD2_HUMAN
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ADP-ribose glycohydrolase MACROD2 (MACRO domain-containing protein 2) (O-acetyl-ADP-ribose deacetylase MACROD2) (EC 3.5.1.-) ([Protein ADP-ribosylaspartate] hydrolase MACROD2) (EC 3.2.2.-) ([Protein ADP-ribosylglutamate] hydrolase MACROD2) (EC 3.2.2.-)
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MYPSNKKKKVWREEKERLLKMTLEERRKEYLRDYIPLNSILSWKEEMKGKGQNDEENTQETSQVKKSLTEKVSLYRGDITLLEVDAIVNAANASLLGGGGVDGCIHRAAGPCLLAECRNLNGCDTGHAKITCGYDLPAKYVIHTVGPIARGHINGSHKEDLANCYKSSLKLVKENNIRSVAFPCISTGIYGFPNEPAAVIALNTIKEWLAKNHHEVDRIIFCVFLEVDFKIYKKKMNEFFSVDDNNEEEEDVEMKEDSDENGPEEKQSVEEMEEQSQDADGVNTVTVPGPASEEAVEDCKDEDFAKDENITKGGEVTDHSVRDQDHPDGQENDSTKNEIKIETESQSSYMETEELSSNQEDAVIVEQPEVIPLTEDQEEKEGEKAPGEDTPRMPGKSEGSSDLENTPGPDAGAQDEAKEQRNGTK
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Removes ADP-ribose from aspartate and glutamate residues in proteins bearing a single ADP-ribose moiety. Inactive towards proteins bearing poly-ADP-ribose. Deacetylates O-acetyl-ADP ribose, a signaling molecule generated by the deacetylation of acetylated lysine residues in histones and other proteins.
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A1Z651
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POL_XMRV6
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Gag-Pol polyprotein (Pr180gag-pol) [Cleaved into: Matrix protein p15 (MA); RNA-binding phosphoprotein p12 (pp12); Capsid protein p30 (CA); Nucleocapsid protein p10 (NC-pol); Protease p14 (PR) (EC 3.4.23.-); Reverse transcriptase/ribonuclease H p80 (RT) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4); Integrase p46 (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
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MGQTVTTPLSLTLQHWGDVQRIASNQSVDVKKRRWVTFCSAEWPTFNVGWPQDGTFNLGVISQVKSRVFCPGPHGHPDQVPYIVTWEALAYDPPPWVKPFVSPKPPPLPTAPVLPPGPSAQPPSRSALYPALTPSIKSKPPKPQVLPDSGGPLIDLLTEDPPPYGAQPSSSARENNEEEAATTSEVSPPSPMVSRLRGRRDPPAADSTTSQAFPLRMGGDGQLQYWPFSSSDLYNWKNNNPSFSEDPGKLTALIESVLITHQPTWDDCQQLLGTLLTGEEKQRVLLEARKAVRGNDGRPTQLPNEVNAAFPLERPDWDYTTTEGRNHLVLYRQLLLAGLQNAGRSPTNLAKVKGITQGPNESPSAFLERLKEAYRRYTPYDPEDPGQETNVSMSFIWQSAPDIGRKLERLEDLKSKTLGDLVREAEKIFNKRETPEEREERIRREIEEKEERRRAEDEQRERERDRRRHREMSKLLATVVIGQRQDRQGGERRRPQLDKDQCAYCKEKGHWAKDCPKKPRGPRGPRPQTSLLTLGDXGGQGQEPPPEPRITLKVGGQPVTFLVDTGAQHSVLTQNPGPLSDKSAWVQGATGGKRYRWTTDRKVHLATGKVTHSFLHVPDCPYPLLGRDLLTKLKAQIHFEGSGAQVVGPMGQPLQVLTLNIEDEYRLHETSKEPDVPLGSTWLSDFPQAWAETGGMGLAVRQAPLIIPLKATSTPVSIKQYPMSQEARLGIKPHIQRLLDQGILVPCQSPWNTPLLPVKKPGTNDYRPVQDLREVNKRVEDIHPTVPNPYNLLSGLPPSHQWYTVLDLKDAFFCLRLHPTSQPLFAFEWRDPEMGISGQLTWTRLPQGFKNSPTLFDEALHRDLADFRIQHPDLILLQYVDDLLLAATSEQDCQRGTRALLQTLGNLGYRASAKKAQICQKQVKYLGYLLKEGQRWLTEARKETVMGQPTPKTPRQLREFLGTAGFCRLWIPGFAEMAAPLYPLTKTGTLFNWGPDQQKAYQEIKQALLTAPALGLPDLTKPFELFVDEKQGYAKGVLTQKLGPWRRPVAYLSKKLDPVAAGWPPCLRMVAAIAVLTKDAGKLTMGQPLVILAPHAVEALVKQPPDRWLSNARMTHYQAMLLDTDRVQFGPVVALNPATLLPLPEKEAPHDCLEILAETHGTRPDLTDQPIPDADYTWYTDGSSFLQEGQRRAGAAVTTETEVIWARALPAGTSAQRAELIALTQALKMAEGKKLNVYTDSRYAFATAHVHGEIYRRRGLLTSEGREIKNKNEILALLKALFLPKRLSIIHCPGHQKGNSAEARGNRMADQAAREAAMKAVLETSTLLIEDSTPYTPPHFHYTETDLKRLRELGATYNQTKGYWVLQGKPVMPDQSVFELLDSLHRLTHLSPQKMKALLDREESPYYMLNRDRTIQYVTETCTACAQVNASKAKIGAGVRVRGHRPGTHWEVDFTEVKPGLYGYKYLLVFVDTFSGWVEAFPTKRETAKVVSKKLLEDIFPRFGMPQVLGSDNGPAFASQVSQSVADLLGIDWKLHCAYRPQSSGQVERMNRTIKETLTKLTLASGTRDWVLLLPLALYRARNTPGPHGLTPYEILYGAPPPLVNFHDPEMSKLTNSPSLQAHLQALQAVQQEVWKPLAAAYQDQLDQPVIPHPFRVGDAVWVRRHQTKNLEPRWKGPYTVLLTTPTALKVDGISAWIHAAHVKAATTPPAGTAWKVQRSQNPLKIRLTRGAP
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[Gag-Pol polyprotein]: Plays a role in budding and is processed by the viral protease during virion maturation outside the cell. During budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-like ubiquitin ligases that conjugate ubiquitin molecules to Gag, or to Gag binding host factors. Interaction with HECT ubiquitin ligases probably link the viral protein to the host ESCRT pathway and facilitate release. [Matrix protein p15]: Targets Gag and gag-pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. Also mediates nuclear localization of the pre-integration complex (By similarity). [Capsid protein p30]: Forms the spherical core of the virion that encapsulates the genomic RNA-nucleocapsid complex. [Nucleocapsid protein p10]: Involved in the packaging and encapsidation of two copies of the genome. Binds with high affinity to conserved UCUG elements within the packaging signal, located near the 5'-end of the genome. This binding is dependent on genome dimerization (By similarity). [Protease p14]: The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. {ECO:0000255|PROSITE-ProRule:PRU00275}. [Reverse transcriptase/ribonuclease H p80]: Multifunctional enzyme that converts the viral dimeric RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5' endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA binds to the primer-binding site (PBS) situated at the 5' end of the viral RNA. RT uses the 3' end of the tRNA primer to perform a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for a polypurine tract (PPT) situated at the 5' end of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H probably can proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPT that has not been removed by RNase H as primers. PPT and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends (By similarity). [Integrase p46]: Catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA. The first step in the integration process is 3' processing. This step requires a complex comprising the viral genome, matrix protein and integrase. This complex is called the pre-integration complex (PIC). The integrase protein removes 2 nucleotides from each 3' end of the viral DNA, leaving recessed CA OH's at the 3' ends. In the second step that requires cell division, the PIC enters cell nucleus. In the third step, termed strand transfer, the integrase protein joins the previously processed 3' ends to the 5' ends of strands of target cellular DNA at the site of integration. The last step is viral DNA integration into host chromosome (By similarity).
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A1Z6E0
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GUS_DROME
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Protein gustavus
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MGQKISGGVKTVSRNDSQSTFKPIIPRELQADFVKPARIDILLDMPPASRDLQLKHSWNSEDRSLNIFVKEDDKLTFHRHPVAQSTDCIRGKVGLTKGLHIWEIYWPTRQRGTHAVVGVCTADAPLHSVGYQSLVGSTEQSWGWDLGRNKLYHDSKNCAGVTYPAILKNDEAFLVPDKFLVALDMDEGTLSFIVDQQYLGIAFRGLRGKKLYPIVSAVWGHCEITMRYIGGLDPEPLPLMDLCRRTIRQKIGRTNLEEHIQQLQLPLSMKTYLLYKNRR
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Involved in the localization of vas to the posterior pole of the oocyte. Required maternally in the germ line for efficient primordial germ cell formation.
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A1Z6H7
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PO210_DROME
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Nuclear pore membrane glycoprotein 210 (Nuclear pore protein gp210) (Glycoprotein 210 kDa) (Nuclear pore membrane glycoprotein gp188) (Nucleoporin Nup210) (Nup210)
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MDSILCMILLILVRNHASEAARLNHPRVLLPIFEDKAINFTLEVDEPNCYKWSSSRQDLISVMPIYKGFSECAYQAVVTVRTHDRRRNTAIVFAEEVQTGETLRSDVIVDVIASLNVRTATRQLYLEEAPAMFELHAFDEQGNEFFTLEGIEFDWEILEPGSKRPTAMRYLTFTDSPYHTVPPTIEKFEADGKKGHMILLEGINTGTAKVTIAMPQAEYKHVRPVEVYISVLANIIIEPSEVTIMAGDSVSFRILQLKMDRLHVIDNNQYYLEVEDSSIAYLRGNSATGAALGRTQVFLRDRNMADSDEVQKGPSALLTVAYPNRLSISLLPHLNWVTVQGEHHAIALDLFAADGQKITMGTKYSINSEVDESFFAIVDRTRNGSRLFGQAKKEGITQVYGSYKDLSVQAELQIFEELQLAPTKVVLPYDPNSLKPLKLQFHASGGDNNYAWFSGNPQVIQIDTQGQATTEIRDVKSAYVNQEVLKDGGKLTAHTTVKVALSKNQKISRVAHIYFLPPERLQITRSNFETALKDFVHVHVGVYARINNSEVPYTSCDNLHFQLDFSQPILQLEGNEGAEAAHEACHVLRLRATAVGTTSLRVSYMYMDKVLYDIIDLYVFEPLVVLNPIENEVVLPVGSSRNIIYANGPQRSFTVAAEIIQSTAFDEKILKVSKLEFDTQNLITAFTVLCRELGETQFTYRVHNSLPTSSFALYQSEVTTKVHCVRPRFLKLYARHNLRDSCPLEKRTSLLFLKDPENKIEIEIEVHDSNNRRLMNISSLGLDWEFSAGEERYQKNIIPHRQISELEFNHGVTLPSRDLLVLTLSEVATNFRIKGTVSQYNDKLLAQHGIHAERPPFGIKNPQTGLIYTPLIENEIRLHAVNSTLLPKDYMSIFLASGYSERIPIAQGSGYLQLELSEAGIVQVEYNENTRILVLTPLRLGHVRLELTDRCLMNEPSHLSISVVGIGAIEVVSMDRLERTTRIEAIVRLFDTNDNLLLVDQSKLSAYDLSEVVADQSILSVRLGEQENVGPGEIRYTITGNQVGETKILFQSGKGIYKVASDPLNIQVFAPIRLFPRDSTLVVGSSIQVYFHGGPHPNTNMIISVEKEQVATISSTVVTAHKLGTTKIVGKCLLKNPVTGKDEVVSQDSVEVHVVALKGVQIRTPLVRIHSGAVMPATLWGLSDLSPMILGTLQNTKISWKVSQPQVVEIFNVFTTAGIEYQSGDLISVRVRALNPGKATITASVTLADGTILPPATVDLQVFKTLELVTPNAIKMDSILAAPRSILQLKSNMDNVVYKLDDRSNGIVSVTPDGLVHTKDSLGRDLIIATTADQSLPIGIEVKNVQYILVTLMPILKLRELEHKIPRGMNFVFKVSLHDNLGNELSHNIEDFNGLRYELGNKDDVDVQIDNNLTFALNLMRETNNVIGISLKDSTGVKHSMDFIKLSVVESDNLFPTKTIFSVGDIICFDSPLTLSSTWRSSNEQIVYINKHTGIAQVLSHRLKPGEKIEITNGDETKRGGFLKYDLEVRESDTILFVKSVDTFSGPEYRGQLVIRNHLQSEKYSNLIAQNVSKCARELGSVPVNFFTCRLAAKDALGRNLLKMYKVDALFEPSIGQYSCRLQLLTGFIELLSIVKTHDVYLELEAVVAKGVSDKMSLKLVPGIKVFPESVRVTDLKPHEIHISGLDKALLKVQVKPSDSKYFAVDFIEHGHGLSKYRLELFDDLPLDENFYILVVSPDTKQSIEVPIIGNTMLAPKCTDRRYGGPLVYRILENLGFVLTTTVIVIISIWVYMSCFQTQGVTQVNFEAFKKGKSRTELMQQSGRSSQDDTFGDSFNVRNFSPDRRRPPSNALSESYIYGHPRLNSSNRSENSTSFS
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Component of the nuclear pore complex.
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A1Z6S7
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GDS1_DROME
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GTPase-GDP dissociation stimulator vimar
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MATAEIDDLIEKLKTTSVSPANTTNLLCEISATKDPKLFDKHELAECFLGLTKCDDTNVRKEAAKCIAEITKSEVQRKKFTKRNIIAAFLECLRQVPTSDGSMELPIQICRALGNICYLNDEARDLILELEGDAVLLRLLDITTIEDVANAAQFIKVRGGLLSNYLLGGEGLAKRAMELGVMKKLQGIIDIGASNVEQHEDLLLNTLPLLSILTENVSDLNFDSSLNIQLSRILAASTNPDLAEMCLELLHYQAESDEVKLILAKDGLCETIYNLLEKYKTLASTSEARALMKLACELIVLILTGDDSMHYLYTTPLLKNMVDWLDSTDIDLLTTGVLALGNFARTDSHCIYFVEQQTMNKLLEVLAKNNGVKDDVRLQHALLSALRNLVIPKPNKNAVIQAGLVQTILPMLEIHQPPVVFKLLGTLRMTVDGQEKLALELLKNKTLIEQLVHWSKSSDYAGVTGESLRLMAWLIKHAYLSKIAYALPRKGDAPAEQIADKIPLTQDYDRSSLSEFLANEGTVEAMVSMLTAQHLVMQNEALIALCILSVVYLSQPSEAAQAQLLQDELVKCEVGKKLAELISKSSDTMTKEIVENLQNCVNLLKSSEQLVAHLEQHNINELLKSIPILTEYCTL
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Probably acts as a GEF (guanine nucleotide exchange factor) for the Rho family of small GTP-binding proteins (G proteins) that stimulates the dissociation of GDP to enable subsequent binding of GTP (By similarity). May also chaperone the processing and/or trafficking of small GTPases independently of GEF activity (By similarity). By interacting with Miro, promotes mitochondrial fission in response to high calcium concentrations.
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A1Z6W3
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PRIC1_DROME
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Protein prickle (Protein spiny legs)
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MSSLSTGGGAGGSSGGPGGADAAAAPAAGQATVTATGNMEPAMVPRTANLLACKQWWRVCFLYGDQQKYYRQLYSKAAAQRLADANQEPDNARDREYDTVDCDLIAGQLDAVEDADDGIDLGDHSSTPKGGATTAGRPLFPHSSSPRRSKKLLRSLRAHVRGEKLPKNDTTTANESSEVTQRNARVTVLDDPFLFGIDADHLGDLVVRGKRYSTLDATENMARFYAEQEATAQVLEIIEQEEESPEQEAPKPALPPKQKQQRPVPPLPPPPANRVTQDQGTQPAAPQVPLQPLTAGDLQFLNLSLRQRSLPRSMKPFKDAHDISFTFNELDTSAEPEVATGAAQQESNEPISRTPLTQISYLQKIPTLPRHFSPSGQGLATPPALGSGGMGLPSSSSASALYAAQAAAGILPTSPLPLQRHQQYLPPHHQQHPGAGMGPGPGSGAAAGPPLGPQYSPGCSANPKYSNAQLPPPPHHHHQLSPALSTPSPPSLLHHPAGGTSSASAHAPFLGGPHMDMQRQSHSDDDSGCALEEYTWVPPGLRPDQVRLYFSQIPDDKVPYVNSPGEQYRVRQLLHQLPPHDNEVRYCHSLTDEERKELRLFSTQRKRDALGRGNVRQLMSARPCDGCDDLISTGDIAVFATRLGPNASWHPACFACSVCRELLVDLIYFHRDGRMYCGRHHAETLKPRCSACDEIILADECTEAEGRAWHMNHFACHECDKQLGGQRYIMREGKPYCLHCFDAMFAEYCDYCGEAIGVDQGQMSHDGQHWHATDECFSCNTCRCSLLGRAFLPRRGAIYCSIACSKGEPPTPSDSSGTGMYTTPTPPTQRVRPHPQAPLPARIPSSHASSSPPMSPQQQQQHQATFNQAMYQMQSQQMEAAGGLVDQSKSYAASDSDAGVVKDLEHGGHMGGGDLTDFSGGRASSTSQNLSPLNSPGDFQPHFLPKPMELQRDGVYNFNEMSSNLDAAWSAKPTNSYHLQRQLLENPHTASMPELAGKLVAPPAHMQHLSQLHAVSSHQFQQHEYADILHPPPPPPGEIPELPTPNLSVASTALPPELMGSPTHSAGDRSLNTPMSTQSASHAPPHPVSILSGASSSSPMSGEPAKKKGVRFEGIPDTLPRSRSYSGNGAGTSGGGERERDRDKDKEGGGRHGHGHSSRRRRRRKSSSSSSHHRSGSGHRSHSTTRADTYAPAQPLSSSYQGPPSVLQAANLVHESPSRQQREREREREREESEESDVCSTCSSSSSSSEDYMMMYQLPQRRHYGGVRVSYVPNDALAYDRKRKPSELGGDKDKNCIIS
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Acts in a planar cell polarity (PCP) complex polarization along the apical/basal axis of epithelial cells. Correct expression of the alternative isoforms is required for PCP signaling in imaginal disks. PCP signaling in the wing disk requires the receptor fz and the cytoplasmic proteins dsh and pk. These act in a feedback loop leading to activation of the jnk cascade and subsequent polarized arrangement of hairs and bristles. Dgo and pk compete with one another for dsh binding, thereby modulating fz dsh activity and ensuring tight control over fz PCP signaling. Vang, stan and pk function together to regulate the establishment of tissue polarity in the adult eye.
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A1Z7A6
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ASAP_DROME
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ArfGAP with SH3 domain, ANK repeat and PH domain-containing protein
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MPPSLIAVSEFVEETRSDYSSPTTSTFASRMPDCRHTIGVLEERLEFDREGLTKLKKAVKAIHNSGNTHVDNEMFMVRALERLGGKVIEQDEPDIGAAFLKFSVVTKELSALMKTLMQNINNIVMFPVDSMLKSELRGVKGDMKRPFDKAAKDYEAKFIKIEKEKKAQAKEAGMVRTEIDAAVVAEEMEKERRLYQLQTCEYLLKYKDIKTKTGIELLQHLIEYYHALSNYFKDGLQTIEHFGTYIGDLSEKLHEIKQKQDEDRRSLLDLRTVLRSTPDFERVDNVPSSESRSGGAGYSLHQLQGDKHHGVTRQGHLLKKSEGKVRRVWQKRRCRVTSDGFLDIFHADESKPPTRVNLLTCQIKPVPDDKRGFDLISYNRPYHFQAEDEGDQKAWMAVLVNCKEKALTKAFQHANPQMSPSLVELQKTVIRYVQLLPGNDRCCDCGSRNDVTWISLNFGILVCIQCSGVHRDLGVHHSRIQSLTLDNLTTANLLIARAMGNSTLNDIMEAKLGRGKLQHESSMEERYDFIRAKYVAKRYVMRTCSDDNDLRCDLEQAVVNADMSQLLQVWAEGADLTCCLPSSDAGETALHLAVLREMGSTLHIVDFLIQNMPPKGLNKATNPAGLLDVTGKNTALHLCALHDRRECMKLLLRSGADYELKNSQNKTALDIAKEMGHNSCRELIECAIKREKSAFDHINTDWNLPNEDGSTDFSDDETVIDERKSRSRPPSFAGGDSPVLRSRSSTCDSIQSSSSPIANCPSRQFTLPSGLPSYTHSAGTSPKQHISVGQYLGSATNVGGNGPGNGGSSPSSASSQSVRAARNSLNMQSDLGGHVTGARKSTSTANMNSLKKRTAPAPPPGTLGSASSSSFYGTLPHPPRHSQNFDASDIRAINHKNQSLDVAYGTLPHLRSVESSPRGGGGYGYGVSQDPGGSGNGSNNSLMPAMTTFGHKRSPSGESLNRNIHLAGAKLVLPPTGELPTLKHVDKSALTRPKIPPPGPPSEREISNGQSNESISSMDEGPVAPPRKLVNQSANFPDYESWHTDMDSSGGGLDHSAESNVSSSDNDRLNSSPDNPSKTGGAGLGGKFHYNGQRRCRALYDCVADNDDELEFKEGEILIVLNERTDDENWMEGIIEGQPTRKGMFPVSFVHMLPD
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Probable GTPase-activating protein (GAP) for Arf family proteins (Probable). Involved in Golgi apparatus organization by targeting Arf1 to the Golgi, which may be important for membrane trafficking during epithelial morphogenesis. Regulates the positioning of interommatidial precursor cells during compound eye morphogenesis together with Arf6 and Cindr. Required for cleavage furrow ingression in early embryonic cells.
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A1Z7A8
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COIL_DROME
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Coilin
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MQHSSMKVDLSNFFKDERRNSLVFIDAAWNNIKDLQDHIQNLFSLKDISLLTSDGCYLPPRESIKVLNSAEGLKAFRFASHDSDTFVSPAPVKSSKKRKNRSVEEQVHLTASTPLRPSKRSKNQNNSEWINIAENPSRVRKKELLDMAPGPSVQSKLLTNKGTPKAPETQTEVSNMSANIETENKESAPQIKNKSKNKKPTKSPEASDQVENEPAPKSISRCTLKEGKMSESKNQETSPDILSEKSGVVTKENETREEQQDKTHLESNKIPDKLSQLKAGDQIEKSPGIAASLLSISFRSPLLEMPFNVPRIFQFPTKKQQIEILEYKKLKPISPRFLLQKGAKSDDTAKQFPSNGKDSTLKPKSYEILHDEELPDVKDKKNVSEGIKRAVAPLCEDIIETSTTLPGAIGAVESAYLDNSTEAETTLPSEAEATNPLELTESFLQNNTSMEKTPKVEKILPDDGSASPIKNNVDSKDVKTVTVPIFEEQLVSDSDDDVMLVDDSNIDVSYGDSDIEPIPVVENRQSLDIIRDLLRTATPLNSLPSRGDTVIFKLLKIKGNANSGTTEFVAGRCTYVNRRTKIVTVETITYPPEIGRMLRQYYMSGLDESSEDVRTLSIHLKDMLEAKIIVATID
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Component of nuclear coiled bodies, also known as Cajal bodies or CBs, which are involved in the modification and assembly of nucleoplasmic snRNPs. Required for Cajal body formation.
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A1Z7K9
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PAN2_DROME
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PAN2-PAN3 deadenylation complex catalytic subunit PAN2 (EC 3.1.13.4) (PAB1P-dependent poly(A)-specific ribonuclease) (Poly(A)-nuclease deadenylation complex subunit 2) (PAN deadenylation complex subunit 2)
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MDYVYCGTDPIGASEDILSVYDAGSAPGNGHFSPSFNGFNIGTTDPEYVELVPVLADGGEHFGVSSVAFDDYEELLWMGNQGGHVTSYYTNSMQKYTSFQVHATDIVRDISTLDSGVLALTQTSLRHQIRRGLPKFTFKSNNMKEMVSMLQLSPHRLVMAGLQDELIDFDLRTLKETRIEHVGAGGCTVLRKNSRYLFAGDQLGTVTLRDLNSLSVQHTIKTHTNILSDFSVQGNLLISCGYSGRQNNLAIDRFLMVYDLRMLRLIAPIQVMIDPQMLKFLPSLTSQLAVVSSYGQVQLVDTVELSEPRVSMYQINTNGSQCLSFDISSSSQAMAFGDQSGHINMIAAVQTPQPQFNLYSRSTEFADVVPQLPMVSITDTNFPLSSVMLPHLTTGTQWFSDWPEELLRYRYHRPKTIDPEVLSNMKMQGPIGYSPNPRTARRNQIPYVIEQGGVCSPNGNGTAAATKAENGVKIIPRRYRKVELKYTKLGTQDFDFDQHNQTCFAGLEATLPNSYCNAMLQILYFTDALRVKLLEHSCIKEFCLSCELGFLFNMLDKSTASSPCQASNFLRSFRTVPEASALGLILTDRSSNVNLISLIQNWNRFILHQMHYEIFDSSKNASTYSGSVQTSTNAENAGSSETSGSSDLYDSISDENSKEDDRERSKINAETDISKIFGTKQICINRCIKCQEEKIKESILLACNLSYPNHIKDSDQYFNFGTILKRSLSSEKSIQAFCERCKKFSPTNQSVKVTSLPQILSINCGLNNEKDITFLKRQLNRCSEKTTVDAAASLSTSKPCRYGANCSRSDCHFMHPDRKSPSHTSQPNAVNNSPNGRQKSWFPLTFTMGINDQGEVQVQTQSDASSGKSEQEEETEKPPTKGLDNNRMYALHAVVCQVDDGTQKNLVSLINVQRPYHTMKLAESADDPQSQWYIFNDFSISPVSPQESVWFTLDWKVPCILFYRHVEDDSESASTTSSTVTESEETIPSESSSGSPTNLSNPFLEEIVSPMLGNLSADATLQPLQSDEMPQSGDLVAMDAEFVTLNPEENEIRPDGKTATIKPCHMSVARISCIRGQGPAEGVPFMDDYISTQEKVVDYLTQFSGIKPGDLDANFSKKRLTALKYSYQKLKYLVDVGVIFVGHGLKNDFRVINIYVPSEQIIDTVHLFHMPHHRMVSLRFLAWHFLGTKIQSETHDSIEDARTTLQLYKHYLKLQEEKKFANALKNLYERGKQLQWKVPED
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Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in general and miRNA-mediated mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein (PABP). PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenylation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. {ECO:0000255|HAMAP-Rule:MF_03182}.
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A1Z7T0
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PKN_DROME
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Serine/threonine-protein kinase N (EC 2.7.11.13) (Protein kinase related to PKN)
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MSDSYYQGEYIKHPVLYELSHKYGFTENLPESCMSIRLEEIKEAIRREIRKELKIKEGAEKLREVAKDRRSLSDVAVLVKKSKSKLAELKSELQELESQILLTSANTAVNSNGQESITACIDPNGGFLVSGAVGGLGGGNTALEGGAPATANDKVLASLEKQLQIEMKVKTGAENMIQSLGIGCDKKLLAEAHQMLADSKAKIEFLRLRIIKVKQNREQADRLKASRQMIDEHGQTIGGNNSSQPQSLETTLEERIEELRHRLRIEAAVVDGAKNVIRTLQTANRAPDKKALQEAHGRLSESSRKLDLLRYSLDLRRQELPADSPAAQQLKTELQIVQLSTSPAPVTYTSLQSGQAGILGGKPYQSVSSLGRCASVTGKLEVRLLGCQDLLEDVPGRSRRDKDNNSSPGDLRSFVKGVTSRSSSKSYSVKDETSIEIMAVIKLDNITVGQTSWKQCSQQAWDQRFSIDLDRSRELEIGVYWRDWRSLCAVKVLRLEEFIDDVRHGMALQLEPQGLLFAEVKFLNPMISQKPKLRRQRMIFNRQQAKNISRAKQMNINVATWGRLLKRNAPNHVHMGSAGSGSSLTGSSPMVVGGSRDSESPISRTPSSDALVEPEPYTPGEQAQNLEFDPDAGINEHVETPGEYPDPAASGLSGMRPLSMHMQGISVLPPESPPVATGAAGRPNTLSLQMPGASKGQVIQGGRTAAPTTAPPPPPVLKATSTTPILDQEVIPQLGKLYVGSSQQQYAQQSSPIIQEPATPTIYGNSAAAGAPQFPQPAQRQEKQPPQQQPIYANQYELNVAKAAAAASVYSPSSSTTSNSNQQQQQQRRNVARGLQYRESGGLETGRAGKQPPNAGMLSMDNFRLLSVLGRGHFGKVILSQLRSNNQYYAIKALKKGDIIARDEVESLLSEKRIFEVANAMRHPFLVNLYSCFQTEQHVCFVMEYAAGGDLMMHIHTDVFLEPRAVFYAACVVLGLQYLHENKIIYRDLKLDNLLLDTEGYVKIADFGLCKEGMGFGDRTGTFCGTPEFLAPEVLTETSYTRAVDWWGLGVLIFEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSLEAIAVMRRLLRKNPERRLGSSERDAEDVKKQAFFRSIVWDDLLLRKVKPPFVPTINHLEDVSNFDEEFTSEKAQLTPPKEPRHLTEEEQLLFQDFSYTAEWC
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Pkc-related serine/threonine-protein kinase and Rho/Rac effector protein that participates in specific signal transduction responses in the cell. May play a role in the regulation of cell cycle progression, actin cytoskeleton assembly, cell migration, cell adhesion and transcription activation signaling processes (By similarity). Plays a role in regulating Rho-mediated dorsal closure during embryogenesis. {ECO:0000250, ECO:0000269|PubMed:10323867, ECO:0000269|PubMed:17507675}.
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A1Z7Z9
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CP131_DROME
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Centrosomal protein of 131 kDa (5-azacytidine-induced protein 1) (Dilatory protein)
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MDLCLKGSQINLATRQKTKPKYTSRSLTTLHNPCPHFRPRSANFLQQRSRSSPFLGRPQSADPKFGRRLSNYFVEKELRNGGKRQVSSNDLLKSLLEEPIKRSWLCRSTCNSSESDYSLHKRTPDSSEEGEQFLVNMPVGEKVKSYSSYSGNQGLSNGALLQRTAKPDLPGRVSFSKPNMHADLDSSDCDNDKQEVRPSISAPGPLTLPSFLSKVEQADPVGQKKSVHFGSTAAEGEVLAETYEYPKCPSENCTCSTRSSSTTSTNEASASDVKCACDAPSCRFMESSKQVEPTSPTPTLPKAPSSELDVIREYKQAVEGVQVVKNHLGTDTLNNIEILPNYLDKYASPTKEKQNNLSETKNMATNSSAVNNGSVVYRPVGNPRNFGAENNFLPAVQDDRRSFANGSSDGVINNYLKVASTPPFVGKKKENVKPASADPIARSSKSKVTKSTINPAPLGKMKKAISVGSLREERKLSEYNLDKVDSWMSMQDQKQYDGKHKPGLEDLDEAQDNDTASQLSLKSNEDSRDSTYDEIVSVIKEIEEDKKRDNFSEGIPSELNLNLDSRCETADTVTVSEGKVPESGDKYKDILAYLNNVESSCDKTLMETRRSIPDSNRSEVEFVVEPDVTDEVPKLSELLMLPNHQLARRVIALSLRANELANAIHMSKEHVFQLRGEKQKSLRAEKSTAAAKLRDQKKHYEEVVTRHQGFIEQLLKDKGSLCEKVAALTRRLESQNQAWEHRLETELARTKETTMAGEKIRRERWVRENTKKIKELTVKGLEAEINKMNCDHQREVTELKRTHQMQLLDALEEARTKHEQIETSIRESCAQDREAIIEKERTAIRERFERQLEEEQRTQAEQRQKLTEEFAAERDRLQSELRQRENEHQARRQEALREQEQELEQAKFEMQERMAKQEEKYQNRVNTIEQQYQADFELWKTEHENKTKLAQAEKENAIRQHYRAERDRQLDELVVRMEADALQHKEEHELKMNRLKEKYEKDLVLAESVEKSLREKYAETRGKLAEADAQVRNSQAEVKQLQLELSHSKKMCGDIIMERDRLRDNLNADIQSELGVLNERHKQEMDQLQKRVHQTIQRQEETIEILKGDNDALRQQCLKLNAVIRQQRKDYCVK
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Cilium-specific protein with a role in cilium/flagellum formation. May be involved in transport of components into the growing cilium. In germ cells and sensory neurons, plays a role with Cby in the building of the transition zone necessary for the formation of the ciliary cap and for the correct elongation of the axoneme.
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A1Z877
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NDG_DROME
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Nidogen (Entactin)
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MPTFGSKLLACLLLSSVILVSGQFEHYLDSLRASELYEFEDGSLGSIHLLPKGDSETIVLQLEQPIHFYGEQYEQLYINTNGILTFNSEFPEYLNQPFPLEYASIAAFYSNVDTSFSDEGTSISLFESKEQSILDRASSLVRYAFSSQSEFEARQVIVATWRNVGYFDSKTDRLNTFQVALIANEQSTFVQFIYPDGGLNWLQGETAGLGLPDIRAQAGFVAEDGRFYTLNGSGSENARFLSESTNLGVPGVWLFEVAPIENEQNVRSPDNAESLTESPALALSCQAHAHQCHEKAECHDKAEGYCCVCGSGFYGNGKSCLANDQPIRVTGTLTGELNKQPVSEEAKLQSYVVTSEGRTYTTINPLTPELGAQLRLVLPLLTTVPWLFAKSVGGVANGYQLTGGVYTHVSRLQFDSGENLHVNQTFEGLNYWDQLSVKIEIYGEVPAVAADAVLILPDYVEEYTFERPGELKSVQVLNINITEEQRVLGLQVEQRILYRSCLRDDEADPSATKVLQKISKVALDYVERDQALRIGAMSKVGVTPESNACNDGTADCVENSVCVPYEDTYRCDCYHGFAAQLDERGVEVCLDIDECATGSHVCDENAVCDNTEGGFNCYCTEGFEGNGYRCLSNSTADNIEYPPAVEGQAEPTSEPSPNPSPYPDQGQDQEREREDDQYPQPNPYPYPEEQIPQHPDECYRCSKDADCYQGRCTCHEGFDGDGYTCTNICGHGEVWENGRCEPLLLERHDVDPLCDALGECRCPYGYELSEDSQRCTYVQEFDGERNADLIPCDVDENCHINATCNWYGQELRHICTCQPGFRGDGYNCDPISDDSCAIRPDICDVHADCVYEEHLGKSECQCQAGYTGNGFNCQLAAECQSAEHCGENAFCDDGVCRCQADFERDVSDRCVPAGRCGSVFCGSNAICKWDSAEGVQYCDCLDGYQGDALTGCTSKPLSCHVLNNCGIHATCEPTEDPANYECQCIAGFKGDGYVCIEEQNCLNNPTLCDMNAQCRSTNSGLVCVCNQGFFGNGSLCQERQHQDSDFLIVSQGVMIARVPLNGRNVRPISVAQMAIGLDKDCVEGRVYWGDISTKKIVSTKYDGTDLRPFITTDIESPEGIAIDVISRRLYWADSAKDTIEVASLDDPSLRAVIINKQLVNPRGIAVDPYREKLFWSDWDRESPKIEMSNLDGTGRELLLGKDDVTLPNSLVVLENSGEVCYADAGTKKVECIEPQNRQIRTISNELSYPFGITFTHDQFYWTDWTTKKVEIVDSLGARQTPIQPPFFGSHKMYGMTVVEQHCPQYQSPCQISNGGCTDSRLCLVNRQAPSGKSCKCTSASTGCTVLAPGY
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Cell adhesion glycoprotein which is widely distributed in basement membranes. Involved in cell-extracellular matrix (ECM) interactions probably by connecting the laminin and collagen IV networks. Required for permeability and mechanical stability of basement membranes, and ECM dependent neural plasticity. Not involved in assembly of the embryonic basement membrane.
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A1Z8D0
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PWP1_DROME
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Periodic tryptophan protein 1 homolog (PWP1) (Protein no child left behind)
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MAEEGPPEPSIDFVPALCFVPRGVAKDRPDKIVLTQAELARIIGDTQQELDEESDDDAEEGENAEEDQNDMDVDDHADANSENRDPQDEFQFQEYDNEANANVTSLANIVDAGEQIPDEDEDSEAEDEVIKPSDNLILVGHVQDDAASMEVWVFNQEEEALYTHHDFLLPSFPLCIEWMNHDAGSEKAGNMCAIGCMDPIITVWDLDIQDAIEPTFKLGSKGSRKQNKEQYGHKDAVLDLSWNTNFEHILASGSVDQTVILWDMDEGQPHTTITAFGKQIQSLEFHPQEAQSILTGCADGYVRLFDCRDAEGVNSSSIEWKVDGEVEKVLWHPTQTDYFIVGTNDGTLHYADKRSPGQLLWSVKAHNEEISGVCFNNQKPNLLTSTSTEGTLKVWNFDGTEAKHVYEHEFNMGRLQCMRQCPEDPYTLAFGGEKPPRCAIFNIKNSIAVRRTFGIPDAE
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Chromatin-associated factor that regulates transcription. Regulates Pol I-mediated rRNA biogenesis and, probably, Pol III-mediated transcription. Regulates the localization to the nucleolus of Cdk7, a regulator of the Pol I-elongation factor TFIIH. Acts as regulator of cell proliferation and tissue growth as part of the TORC1 and Myc signaling pathway in response to nutrients. Required in males for both germline stem cell (GSC) maintenance and early stages of germ cell differentiation of germ cell cysts. Not required for female germline stem cell (GSC) maintenance, but necessary to regulate germ cell differentiation and egg chamber development. In female somatic cells, required for follicle stem cell survival and maintenance.
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A1Z8N1
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TRE11_DROME
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Facilitated trehalose transporter Tret1-1 (DmTret1-1)
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MSGRDNRGAGGGGGGHQPLSNAMGKLKEKLTRVGDELGYHRVESNLSTSNTATSLDTILPEDPFLFPQVSPQRHPQNTVRTQRLLEDEPPLSFRPLLEDDDINEPPTQQQQRTPLRASGSLELTPLPPPPTSLEIREHRDRQQRGAQGDELQRSKQSLKGSRVSFERRDTGNSNTNSNKAAESSDEDSFEEKRTGFQQQKATSVDHKGILKDLKHILANDNRRQFQAKKHVSLDVKGTRFLQDLLKESSSEEEFHKTRREFQGRKHQSLDPRVTFKLDKVLQGSSTDSDEEGEDAEHKRLIHRPKDITKPVIIDLKDLESESDEDFLTSRQHFQQQRSISTDSRKSRRLYEMDEMDNKRGENIRHAVPFVRQITEDGKPKLEVYRPTTNPIYIWTQVLAALSVSLGSLVVGFVSAYTSPALVSMTDRNITSFEVTQDAGSWVGGIMPLAGLAGGIAGGPLIEYLGRRNTILATAVPFIVSSLLIACAVNVAMVLCGRFLAGFCVGIASLSLPVYLGETVQPEVRGTLGLLPTAFGNIGILLCFVAGSFMNWSMLAFLGAALPVPFLILMFLIPETPRWFVGRGLEERARKALKWLRGKEADVEPELKGLMRSQADADRQASRNTMLELLKLNNLKPLSISLGLMFFQQFSGINAVIFYTVQIFKDAGSTIDGNLCTIIVGIVNFLATFIGIVLIDRAGRKILLYVSDIAMVLTLFVLGGFFYCKTYGPDVSHLGWLPLTCFVIYILGFSLGFGPIPWLMMGEILPAKIRGSAASVATAFNWFCTFVVTKTFQDLTVAMGAHGAFWLFGAICFVGLFFVIIYVPETQGKTLEDIERKMMGRVRRMSSVANIKPLSFNM
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Low-capacity facilitative transporter for trehalose. Does not transport maltose, sucrose or lactose. Mediates the bidirectional transfer of trehalose. Responsible for the transport of trehalose synthesized in the fat body and the incorporation of trehalose into other tissues that require a carbon source, thereby regulating trehalose levels in the hemolymph.
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A1Z8P9
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TPR_DROME
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Nucleoprotein TPR (Megator) (Nuclear envelope antigen Bx34)
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MDLSGPQTLNNILQPDELKLVPEDVQKKLSEYINNFSDEYCKNRAAANRLAEAEQKKEELENKMEDYLVKFTSFELNVNELRTHLDQMSSERVNLMDTIAKGEQTISQLRKEKASVVEERDSMMKVIERQQAELERLKQDLHTYQQQLSSAIAAKCEAIARVDEIQSKEVALELKENRMESERDMLHKEILLISGDLNKSNAELQNIRREHTINTMQLQSCLKEKTESLKLMQEQYEQAVKTIGELTSKIEMQNDTAFKQNQATEEYVGKLKKELDAKEKLFEIFKSTESDHLIQREELLQGISEIKRLLEEAEEQCAQLTEQMETMKQKHSAELDEQNKKIQAMEQELASANDLLKQARESNLESAICQLAPSAAVASRLIRSDLSLTELYSMYAKSSEELEMRNCEIEQLKLQLKSIIAEISESAPILEKQNSDYQKMKETNSELLREHDELLQNKLCLERELERALSTLNHNQNENKKLKQTHTDLSRQVCMLLDELNCIRAGVKHVRIQPTRQLPTSESLISDNLVTFSSIEELVDRNTYLLNMSRELTELLEASEKNQDKMLLEQSKNHIRKLDARFAELEDLLTQKNNTVTTLLSKCDRYKKLYFAAQKKLGQNTVDLDDSNLEPNDSALDTSEQPAANFEESRKLEKRVRQLEQQLEGEVKKYASLKENYDYYTSEKRKNDALAQEQFDSMRKEVRELTSSNCKLMNTTEFQKEQIELLHKNIGTYKQQVTTLEERTKNYEKTIIKHEQTVHLLKDEMMAAHRKHAAADAEAQSLRQENRILRDTSSRLQIEKETYHREQQSQSLLLNSLEFIKTNLERSEMEGRQRLEQRLDDTVRELAAQRRHFQEEEEKFRESINEFKRQAETAIKLKDEEKQLADKWQAELTSVREELAEKVNKVNELSKKLQEVLTPTLNDNPITAANKRAREFELKLDQATVEIESLTKELAKTREHGEQFYKMSQSAESEIKRLHELHGELVAKQEEEIKKLRSSEAELKTRISDLEAEAMLSNVTEQSKTVNQSGQLKSAQDDLKSLLEKLTEANCTIRTLRSENTSLVESLNAAEVKYANGMIQHSADIQELTRYKAEFFKANDELNQLKSGRESLQAAYDELLRSNAEAQKLLDKEREESEKRVADLHALNSNLHDQIEALASKLAVLASQSQNPNSSLNESAMDGDQSLNASGLTAAEEGRNNEQLLKIIKFLRKEKDLFAAKLDILKAENARLISEHAIQQKKVDELNGYLNQERAKSQTDVVSANKHEEVLRKIETLNAITDSNRILREERNALTLRVAELTDRISSVEKELFPLQCSNKELTSKIEEINVENTSLRTEAIKWRQRANALVEKSNRNPEEFKRLQAEREHLAKLLTAEKELNKKQSDELTVLKQRMNTEIPMLNKQMQILDEARKKQVDEFTNLKQNNTRQTQDIMELKNRLLQKEEELLKANEELETKDKTIADKETKELQLRKLAKRYKDFYIGLQSQGGGTESAAELEKVRSELEEVNNQLRALKDEHEKITKECDEVKKRTEPETDTSAIRQEYKAKLDKLVVDLTVARTDLVNQETTFAGTKSSYDETIARLEKELQENIAANKDINQRLTRENESLHMRINQLTRQLGSQQSTKPSTSSVAEKGNISESSPRTANVKPMSGSATVQQSATVTPWRGGETPLASIRPISVQNSRTAAILPTSQQPPAGSSTSTSSSSSSSSTSTTSAAGGGSSAVAQTALVPPQQQVHTTGSAALESMASSSPTSSHTDYMPSTSSASVAVAAIPPMGASSAAESSQEAESIQHPQQNDSQLFVGGAQQQVVALVSPRVEGSSSSSSSTSVPTATAPSIQDGGSQSQQPSTSGSSSSSSTVVSSHSRHTPSSSNVTTTQAGCSSQGIKRPRDIEGDSSTGTEEGVAEKMSKITKRLRGPMHSGELSAGHIGDSGMDVDQMPTSSQRDQEDDIQVVDSDDEEDVLADADDGPIDGGEAEQEGYEDSYEQDNEMDDNEGGDDDNDIAVDAQDNNEVDIEVPEQHMQAQEESQSLDNQAIATASASTQENNQSQAITSGSGESSNPVTLPQAEASNWKQAAASTSTAAARRNESSVEIVSSPQVSNFCEQPARLESAEVDGTAEVAGGAPHESAGPSDTGAASASSPQKQSEAGESSGSDALKAADDGGDHADGTDNAREADEAFAEETMATGQGEDSQPLGNDNPNVGTSQSEVSHNQANLGEGNPTEDSEGADGVSSEGEKQAVGVEEEGREAEATSPSENTRFRTLRSAVPTRRGHRAMRGGSPNSQNRPQRIVWQRDTSPGNIQQNQMSANNNRFAQRTRNRRPIRRPPPNNFNNGGRFP
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Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC. Plays a role in chromosomal organization and gene expression regulation stimulates transcription by promoting the formation of an open chromatin environment. Binds chromatin to nucleoporin-associated regions (NARs) that define transcriptionally active regions of the genome. Associates with extended chromosomal regions that alternate between domains of high density binding with those of low occupancy. Preferentially binds to NARs of the male X chromosome. In males, together with Nup153, required for the localization of the male-specific lethal (MSL) histone acetyltransferase complex to the X chromosome and therefore for the transcription of dosage compensation genes. In males, restrains dosage-compensated expression at the level of nascent transcription probably by interacting with the MSL complex and by modulating RNA Polymerase II phosphorylation status and activity. During mitosis forms a gel-like spindle matrix complex together with Skeletor (Skel), Chro, east, and Asator embedding the microtubule spindle apparatus. During interphase localizes Mad1 to the nuclear pore complex and thereby might act as a scaffold to assemble the Mad1-C-Mad2 complex, an heterotetramer that catalyzes the structural conversion of open-Mad2 (O-Mad2) into closed-Mad2 (C-Mad2) which is essential for spindle-assembly checkpoint (SAC). During the metaphase-anaphase transition and before chromosome congression, is phosphorylated by Msp-1 this modification releases Mad1 from the nuclear pore complex and thereby promotes assembly of SAC ensuring a timely and effective recruitment of spindle checkpoint proteins like Mad1, Mad2 and Mps1 to unattached kinetochores (KT). In testes, has a role in stem cell asymmetric division and maintenance via regulation of mitotic spindle assembly checkpoint (SAC) complex.
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A1Z8R8
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PARL_DROME
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Presenilins-associated rhomboid-like protein, mitochondrial (EC 3.4.21.105) (Mitochondrial intramembrane-cleaving protease Parl) (Rhomboid-7)
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MLMSRALCRSWLPQVARRCHANVNVPILRINSGHPAARSCRQIHSNRKQSSNLKPTTGEPAAAEQNTPVPVNNVIKAVAFTGAFTVGCFAGATILEYENTRSLILEKARQARFGWWQSRSLADRDYWTQIKQDIRRHWDSLTPGDKMFAPILLCNLVAFAMWRVPALKSTMITYFTSNPAAKVVCWPMFLSTFSHYSAMHLFANMYVMHSFANAAAVSLGKEQFLAVYLSAGVFSSLMSVLYKAATSQAGMSLGASGAIMTLLAYVCTQYPDTQLSILFLPALTFSAGAGIKVLMGIDFAGVVMGWKFFDHAAHLGGAMFGIFWATYGAQIWAKRIGLLNYYHDLRRTKQK
|
Mitochondrial intramembrane protease which plays a critical role in the regulation of mitochondrial function. Essential for mitochondrial development and fusion during spermatogenesis and the development of neurons and muscles. Essential for proteolytic processing of Pink1 and HtrA2 into their mature forms. May also be involved, but not required, for the proteolytic processing of Opa1.
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A1Z8X3
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RTTN_DROME
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Protein rotatin homolog (Anastral spindle 3)
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MSTKQSPALQLAEGQLTKLTSESEEIRMRALDQIETRFIRCLQLGEPIQFKPVLLLKQLIRWFGYTPPLVPDRVLAMIMELLRSEYAEAVIRKIPYERFKAELQKVRRVLHKQESKRVSELLDDMNLLLLEKYNIDRVTPSVSSLSSNDIPSQATESADSSSNQIYDNLKPEDYEPSWSHPCLDDVATMKSMIDLPRNSVELQLQLTELIIRMGDYPTEYFLQPPFVFLHLVQLQTMTDGSLIHVNRALIACLRLLQQRILLRRNTLSYADRFDPPSRPKQVKVVSALVILLENCMKLIRPLLFSCTNDNWHIMELIVEIVRTHDVLSSKIPLVSITLIADAVKSLLAYCNSVEGSCMTQLMDSLRIPRLQSLILNGVLHDMVALNINYDKRMDRRQAKALIQPIVLDSAYLSGMPERMKSLNTLISSLDSGPSPDEELIKLKRAYSVALNQLHPNTELTGSLLIQKYRQVCLVLVQLGSETLVKQLFGAVVKCIPFYAGNLKLRKDADELLYTLVDLPALKLRSLIYRLMIKSTVAHFHSFMNKTVYMTGCSNVDLIRQHILGVPLTPLLLRRMIIQSSEANTSERMQQWCLDYPIMIMKLNAILAPQDFSVVFPLLLPVLPLLISRSVTHKILHNVIWNVLEPDSSRLDPQLMLRGYVYFMFHPDGEVRSEATTTIAYVLQCQEQTNRYLPTASNVPVEHIANDLCIIQPPFCYRSIFIKCSDERFQGQRSLDALFRLLQAKDIKSNIRKSTMTQLNVLLRNWRACEEFSTKEDGYRLIMESLHNALKKGNDTDILLPTVSILMKLLFNDDEFRLEVANTFGVYTLLLRALFLFPHLEQLRQDVSICLFQMLFQNCITSTEDKLVLNANMEPLILPVTYEIEHKVIPTAVTEGLELQQNVEATHFGRDRAKAAQHWRLYMAYRVCQVPSSITLESVSALDIRESLKIKMADLALVRSSDLNEQLSCQFIAAENCSKHEDLQKTVSAIQLFLVVLRNSLSDTVAENLWKLIHKYIRLAPGNEADDKVYKSMLDLCVTCIRFSQPHAINGLSYALETDHHHSFQLLLHDSQISLDKLFLICQCMMQLLSNELSDDSMNWYGKFFMQLSAVAKTHFELRQLQHVRCILCMLRFVSERNLKFSNAQLMSYSQHFIQLSSNLRTSTQTGSEWQRDCLYIICQLQIHLIYQEPKASSKASIPNDVGASYKVLRYFLTLCGHGDSEVRALSWVSLANWITICGSQVAEILPRLDFLPGGLPACCLTTLTDAHEMMLIRELAGRVFILLMPLIGAESSLELLRKHDLLKTAYNSLKAIHDTPWMFKKIVGERHSCEVISCYVAICTKMVAMKPEWCAALCGHSLMSGLSDVMKKLKSQASCSIPLVELCASQICELYSMCYTNNFEFLKMTICRDSVFLQNYLTLINDVLSLECPEYMVIPLLKMFLIFCTDSNSNSFLIEQIKNKPSLFMDFFLFGLHVKLINSPFQRFTLSALSLVFTKAQLAAYDISMLSELEKFELAFSDPDIAKDGKQEFESKKKQSVSQCIYDESSDNSDDNKQRPNHAIQATNAAIIIFHRLDQLFDRYYLSKALNFLELPAVGQVQVCEALGELLKASTWAVKAAGESKLLGKVVHILDDFLNDEKIGNAAVYVKRVGPHKAQSIISNLLVLINMLSQWHSSPNSEIIQTSMAANIAKILIRIWPWLSHSYHLKKVTVQLIMFLTEHSFEMCKQISLLQSGHAQSLLHLMARVADFETTKKEIPNKEPSLNMVPALRVMVNCCCCTEGRLSLSKMNLLDMFDTILPANPCSTHLKVRPPVLIAWLGFWEVFSRYDVGGKACHLQSLINTIRRSPPLSHKRILCLRILRNMCFFNGNRPRLVELADFINLLRDILEQRVQKAPTSEKNGLNSFEEHRLAVLMLWKLFGFGAKYKGMLRGTKLFKLLIGLRVEMSVVFSEEENKYAGVPYANDLAKLLEKLMESMRQ
|
Participes in the structural integrity of both centrioles and basal bodies and in centriole cohesion. Participates in the later stages of centriole assembly through the interaction with Rcd4 leading to the centriole to centrosome conversion.
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A1Z9E2
|
LIN54_DROME
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Protein lin-54 homolog (Myb complex protein of 120 kDa)
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MDTSGGNLDSLDDTEPLPELSFEDFLEPTSEKSSQHMEIEALDSEEDNIGGEDLADPANDSLNTPQFKKNVVHILEDKRLNSSGLTVLKSHAIKMVTAGGTPPAKAQVTDVKILNKLKPIPSSTLKIGSTTIATKSTPGSITKTLGNLTQIRTKDGQVIFVQKSVPGTQSSTAVTGSPSGGIRRLVAPSGIQKAVLSKGVTMASTGLVKAAVPAKASTSVPGSAITLKGIQPLAGGTAKASTSSTTATTSPSLAQPNKIQVVRTADGKIIKINQAGPSLLVNAKQGTGTTVTPGGSAATSVKLSPSTGNVVLNKPVGQVVVRTETPVKTATGSVASASATPGKMLVQSGGKQILVSNKNIIKLSPNASATSSTTHTTGGQTPSTSSGLHAIQLPGKGGIQYVRVLNNNKSAAGTSATASIPKTVQTQKITVVRPPAATGVPATSTTTSAAAASPAAASKANLAMGNTNKIVMRSMGGSIVPLPSVQTLVSKRALGAISNASKPASAASSSATPSASQELPRKHRLTDLNVQLKQSASVSSEASDSSDAGPEAKKPRYVITMQQGSQKAASQPVQKLINRTANVQRVVSSSTSPSSNSTKKIYNYVQPTGSNGAKYMICNSGVPQSSTSAMRRGYTGYVENKTRRPPPISPQQHRFKQMGPQQQSKHQQLQAQAKQRIRQQQLPTEQSTPIKVEPKLPTLPPGVKANVPAKPLFEVLKPPATAAAAGAVDPLGGMTSRRKHCNCSKSQCLKLYCDCFANGEFCQDCTCKDCFNNLDYEVERERAIRSCLDRNPSAFKPKITAPNSGDMRLHNKGCNCKRSGCLKNYCECYEAKIPCSSICKCVGCRNMEDRPDVDMDSLDGLMGVEGQKKDKAKNKQLNENRANIYFTDDVIEATIMCMISRIVMHEKQNVAVEDMEREVMEEMGESLTQIIAFAKEKQETSQIDESKPSS
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Component of the DREAM complex, a multiprotein complex that can both act as a transcription activator or repressor depending on the context. In follicle cells, the complex plays a central role in the site-specific DNA replication at the chorion loci. During development, the complex represses transcription of developmentally controlled E2F target genes.
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A1Z9G2
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SYF1_DROME
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Pre-mRNA-splicing factor syf1 homolog (Pre-mRNA-splicing factor fandango) (Protein faint sausage)
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MVTKTIKSLNLEINFEVEDVPYEEEILRNAYSVKHWLRYIDHKAKAPNNGVNMVYERALKELPGSYKIWHNYLRTRRKQVRGKIPTDPMYEEVNSAFERALVFMHKMPRIWMDYGAFMTSQCKITRTRHVFDRALRALPITQHGRIWPLYLQFVRRFEMPETALRVYRRYLKLFPEDTEEYVDYLQEADRLDEAAQQLAHIVDNEHFVSKHGKSNHQLWNELCDLISKNPHKVHSLNVDAIIRGGLRRYTDQLGHLWNSLADYYVRSGLFDRARDIYEEAIQTVTTVRDFTQVFDEYAQFEELSLNRRMEQVAANEAATEEDDIDVELRLSRFEYLMERRLLLLNSVLLRQNPHNVHEWHKRVTLYEDKPAEIISTYTEAVQTVQPKQAVGKLHTLWVEFAKFYEANGQVEDARVVFERGTEVEYVKVEDLAAVWCEWAEMELRQQQFEAALKLMQRATAMPKRKIAYYDDTETVQARLHRSLKVWSMYADLEESFGTFKTCKAVYERIIDLKICTPQIIINYGMFLEEHNYFEEAYRAYEKGISLFKWPNVYDIWNSYLTKFLERYGGTKLERARDLFEQCLDQCPPEHAKYFYLLYAKLEEEHGLARHAMSVYDRATSAVKEDEMFDMYNIFIKKAAEIYGLPRTREIYEKAIESLPEQNMRHMCVKFAELETKLGEVDRARAIYAHCSQVCDPRITADFWQTWKEFEVRHGNEDTMREMLRIKRSVQATYNTQVNMMAAQFLSTNNGAAADAGAGAGPDAMRLLEEKARQAAAESKQKPIEKAASNIMFVRGETQGGAKDKKDTVVNPDEIDIGDSDEDDEEEDDDEENEMTNENQASAAVTKTDEEGLVMKKLRFEQKAIPAKVFGSLKPSNQGDSDGE
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Subunit of the NTC(Nineteen)/Prp19 complex, which is part of the spliceosome. The complex participates in spliceosome assembly, its remodeling and is required for efficient spliceosome activation. Essential for efficient pre-mRNA splicing. In embryos, efficient pre-mRNA splicing of zygotic transcripts is essential during dynamic cellular processes that require rapid division and/or dramatic changes in gene expression such as blastoderm cellularization, tracheal branching morphogenesis, Malpighian morphogenesis and epidermal development. Part of its role in promoting embryo tracheal development is also due to specifically splicing bnl transcripts which results in the activation of the BNL-FGF pathway.
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A1Z9J4
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DJ1A_DROME
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Protein DJ-1alpha
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MLSVLRKSFPNGVTHAHRVIRCKSNQDKCAKNALIILAPGAEEMEFTISADVLRRGKILVTVAGLHDCEPVKCSRSVVIVPDTSLEEAVTRGDYDVVVLPGGLAGNKALMNSSAVGDVLRCQESKGGLIAAICAAPTALAKHGIGKGKSITSHPDMKPQLKELYCYIDDKTVVQDGNIITSRGPGTTFDFALKITEQLVGAEVAKEVAKAMLWTYKP
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Plays an important role in cell protection against oxidative stress and cell death acting as oxidative stress sensor. Does not play a role in methylglyoxal detoxification (By similarity).
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A1Z9L3
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DHX8_DROME
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ATP-dependent RNA helicase DHX8 (EC 3.6.4.13) (Peanuts)
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MDELQKLEYLSLVSKICTELDNHLGINDKDLAEFIIDLENKNRTYDTFRKALLDNGAEFPDSLVQNLQRIINLMRPSRPGGASQEKTVGDKKEDKKSQLLKMFPGLALPNDTYSKKEESDDDEKVKAKPEKHSETHKKTDMSDVDAAMMELEALAPGEGATLVRPHKEVSSRDRHKRRSRDRDTKRRSRSREDRHSDRRRSRSRDKERRRRSRSRDNRRRSRSREDRDRDRDRRHKSSSSRDHHERRRRSRSRSTERRDRRDRSRDCSEKMPPPSAAMTDDPEAGKIYSGKIANIVPFGCFVQLFGLRKRWEGLVHISQLRAEGRVTDVTEVVTRNQTVKVKVMSITGQKVSLSMKEVDQDSGKDLNPLSHAPEDDESLRDRNPDGPFSSSTSMLNLQGNGMEGDEHESRKRVTRISSPERWEIKQMISSGVLDRSEMPDFDEETGLLPKDEDDEADIEIEIVEEEPPFLSGHGRALHDLSPVRIVKNPDGSLAQAAMMQSALSKERREQKMLQREQEIEAMPTSLNKNWIDPLPEDESRSLAANMRGMAAAPPEVPEWKKHVIGGKKSSFGKKTDLTLVEQRQSLPIYKLRDDLIKAVTDNQILIVIGETGSGKTTQITQYLGECGFTARGKIGCTQPRRVAAMSVAKRVAEEYGCRLGQEVGYTIRFEDCTSPETIIKYMTDGMLLRECLMEAELKSYSVIMLDEAHERTIHTDVLFGLLKTAVQKRPELKLIVTSATLDAVKFSQYFFKAPIFTIPGRTFPVEVLYTKEPETDYLDASLITVMQIHLREPPGDILLFLTGQEEIDTACEILYERMKSLGPDVPELIILPVYSALPSEMQTRIFDPAPAGSRKVVIATNIAETSLTIDGIFYVVDPGFVKQKVYNSKTGMDSLVVTPISQAAAKQRAGRAGRTGPGKTYRLYTERAYRDEMLPTPVPEIQRTNLATTVLQLKTMGINDLLHFDFMDAPPVESLVMALEQLHSLSALDDEGLLTRLGRRMAEFPLEPNLSKMLIMSVALQCSDEILTIVSMLSVQNVFYRPKDKQALADQKKAKFNQAEGDHLTLLAVYNSWKNNKFSNAWCYENFVQIRTLKRSQDVRKQLLGIMDRHKLDVVSAGKNSVRIQKAICSGFFRNAAKKDPQEGYRTLVDSQVVYIHPSSALFNRQPEWVIYHELVQTTKEYMREVTTIDPKWLVEFAPSFFRFSDPTKLSKFKKNQRLEPLYNKYEEPNAWRISRVRRRRN
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Involved in pre-mRNA splicing as component of the spliceosome. Facilitates nuclear export of spliced mRNA by releasing the RNA from the spliceosome (By similarity). Before and after egg-chamber formation, required for nurse-cell chromatin dispersal (NCCD) probably by playing a role in spliceosome localization to chromatin/interchromatin spaces.
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Subsets and Splits
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