accession
stringlengths 6
10
| name
stringlengths 6
11
| Full Name
stringlengths 1
147
⌀ | taxon
stringlengths 3
46
⌀ | sequence
stringlengths 16
2.75k
| function
stringlengths 6
5.51k
| AlphaFoldDB
stringlengths 6
10
|
|---|---|---|---|---|---|---|
Q81VM2
|
METN1_BACAN
|
Methionine import ATP-binding protein MetN 1
|
Bacillus cereus group
|
MIELKNVSKVFTTKKGNVEALKSTSLQVKKGEVFGIIGYSGAGKSTLIRCVNLLEKPTTGNIIVNEQDLTTLSTKELAKARQKIGMIFQGFNLLKTVTVYENIALPLRLAGVPKLEIEKRVEKYLRIVDLFNRKDAYPSELSGGQKQRVAIARALSHEPEVLLSDEATSALDPETTDSILDLLLKINEEIGITILLITHEMNVIQRICDRVAVMEHGAVVESGTVKDIFTNPQHVTTKKFVNSAFAAKIPAEVQKELQRTGEIVTLSFIGNSSGEPALAVATKRFQVYPNILSGNITQLKHEAYGKLVIHMQGEQNEINHALSFLQEQGIIVEGGRTDYGKQVLFG
|
Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system.
|
Q81VM2
|
Q39249
|
VDE_ARATH
|
Protein NON-PHOTOCHEMICAL QUENCHING 1
|
Arabidopsis
|
MAVATHCFTSPCHDRIRFFSSDDGIGRLGITRKRINGTFLLKILPPIQSADLRTTGGRSSRPLSAFRSGFSKGIFDIVPLPSKNELKELTAPLLLKLVGVLACAFLIVPSADAVDALKTCACLLKGCRIELAKCIANPACAANVACLQTCNNRPDETECQIKCGDLFENSVVDEFNECAVSRKKCVPRKSDLGEFPAPDPSVLVQNFNISDFNGKWYITSGLNPTFDAFDCQLHEFHTEGDNKLVGNISWRIKTLDSGFFTRSAVQKFVQDPNQPGVLYNHDNEYLHYQDDWYILSSKIENKPEDYIFVYYRGRNDAWDGYGGAVVYTRSSVLPNSIIPELEKAAKSIGRDFSTFIRTDNTCGPEPALVERIEKTVEEGERIIVKEVEEIEEEVEKEVEKVGRTEMTLFQRLAEGFNELKQDEENFVRELSKEEMEFLDEIKMEASEVEKLFGKALPIRKVR
|
Part of the xanthophyll (or violaxanthin) cycle for controlling the concentration of zeaxanthin in chloroplasts. Catalyzes the two-step mono de-epoxidation reaction. Stereospecific for all-trans xanthophylls. Zeaxanthin induces the dissipation of excitation energy in the chlorophyll of the light-harvesting protein complex of photosystem II.
|
Q39249
|
Q0WW84
|
RB47B_ARATH
|
RNA-binding protein 47B
|
Arabidopsis
|
MQTTNGSDSTLATSGATPPNQQTPPPPQQWQQQQQQQQQWMAAMQYPPAAAMMMMQQQQMLMYPHQYVPYNQGPYQQHHPQLHQYGSYQQHQHQQHKAIDRGSGDDVKTLWVGDLLHWMDETYLHSCFSHTGEVSSVKVIRNKLTSQSEGYGFVEFLSRAAAEEVLQNYSGSVMPNSDQPFRINWASFSTGEKRAVENGPDLSVFVGDLSPDVTDVLLHETFSDRYPSVKSAKVVIDSNTGRSKGYGFVRFGDENERSRALTEMNGAYCSNRQMRVGIATPKRAIANQQQHSSQAVILAGGHGSNGSMGYGSQSDGESTNATIFVGGIDPDVIDEDLRQPFSQFGEVVSVKIPVGKGCGFVQFADRKSAEDAIESLNGTVIGKNTVRLSWGRSPNKQWRGDSGQQWNGGYSRGHGYNNGGGYANHHDSNNYHGEN
|
Heterogeneous nuclear ribonucleoprotein (hnRNP)-protein binding the poly(A) tail of mRNA and probably involved in some steps of pre-mRNA maturation.
|
Q0WW84
|
A0RIU9
|
NADD_BACAH
|
Nicotinate mononucleotide adenylyltransferase
|
Bacillus cereus group
|
MRKIGIIGGTFDPPHYGHLLIANEVYHALNLEEVWFLPNQIPPHKQGRNITSVESRLQMLELATEAEEHFSICLEELSRKGPSYTYDTMLQLTKKYPDVQFHFIIGGDMVEYLPKWYNIEALLDLVTFVGVARPGYTLHTSYPITTVEIPEFAVSSSLLRERYKEKKTCKYLLPEKVQVYIERNGLYES
|
Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
|
A0RIU9
|
P33177
|
NIFD_ANASL
|
Nitrogenase component I
|
unclassified Anabaena
|
MTPPENKNLVQENKELIQEVLKA
|
This molybdenum-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation.
|
P33177
|
E1AWD3
|
B1CG4_AMOCU
|
Brevinin-1CG4
|
Amolops
|
MFTLKKSLLLLFFLGTINLSLCEQERNADEEERRDDSDKRDVEVEKRFLSTLLNVASKVVPTLFCKITKKC
|
Antimicrobial peptide active against a variety of Gram-positive and some Gram-negative bacterial strains. Has antifungal activity against C.albicans ATCC 10231 and a slime mold isolate. Has hemolytic activity against human erythrocytes.
|
E1AWD3
|
Q02SA6
|
TAUB_PSEAB
|
Taurine import ATP-binding protein TauB
|
Pseudomonas
|
MSRLTAEAISLSFEQRGQRRAILRDLSLGLAKGESLVVLGPSGCGKSTLLNILAGFQTPDQGRVQIDGRTLEGPGGERGVVFQDDALMPWLNALDNVALGLRIRGLGKAERTARARQVLQLVGLQEYAEQSVAELSGGQRQRLGLARALAVEPDFLLLDEPFGALDALTRERMQVLLLDLWKQTGKGLFLITHSVDEALFLATDLVVMDGPPARIVKRLPVDFARRYAAGETVRSIKSDPEFGRLRQALLDEFLDVAEAEHAH
|
Part of the ABC transporter complex TauABC involved in taurine import. Responsible for energy coupling to the transport system.
|
Q02SA6
|
A4WZ55
|
CTAA_CERS5
|
Cytochrome aa3-controlling protein
|
Cereibacter
|
MAVKKRSIFEEVGQGAKAPVPQGGSIDRGQGGARRGIRLWLMALFVLVMAMIVVGGLTRLTDSGLSITEWRPVTGAVPPLNEAEWTAEFEKYRQSPQYRLMNAGMSMAEFQRIYWWEWGHRQLGRVIGLVWAVGFLGFLVARKMPRGWWPRLLALGVLGGIQGGIGWWMVASGLEGDRVAVESTRLAVHLSLAFIILGMIAWQALLLGRTEAELFQARRQREGRLYGMTTVLIVVAFLQVVLGALVAGIDAGRGFPTWPDMNGTFLPADMLYVPGVETDWRNPAWWLGLLQNPGFVQFLHRMAGYALVALGLVFWIFGRRTKHRATRGAFDLLALALLAQVALGVGTVLSAAEWQVAIAHQVGAVVIWVLILHARHLAHYPRVGSIRKGTL
|
Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme A.
|
A4WZ55
|
C5C8I6
|
HUTI_MICLC
|
Imidazolone-5-propionate hydrolase
|
Micrococcus
|
MRSTLITDIAELTTVDPEGRVLTDAAVVVEDERIAWIGPAADAPDADDRVSVEGRAVLPGWVDSHTHLVFDGDRSAEFEARMAGESYAAGGIGVTTSATRAASDDRLAELVRGRVADAVAGGTTYLETKTGYGLTVEEEARHARLLAGLREEGLVDEVTFLGAHLVPPGRDAEDYLDDVVGPMLEAVREHAGWVDVFCDTGAFDAEQTRRVLAAGVAAGLGVRLHGNQIEQGPGVGVAVEFGAASVDHVNHLSDADVEALAGTWTGWDRASATGTPGTVAGCLPACDLSTRAPLAPARRLLDAGIEVSLASNCNPGTSYTTSMNFNVGTAVLQMHLTLAEAVRAATLGGALGLRAQDRVGSLEVGKRADLHVLDAPAAIHLAYRPGMPLTHAVWRAGRRAV
|
Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is the third step in the universal histidine degradation pathway.
|
C5C8I6
|
Q3UPR7
|
TM102_MOUSE
|
Transmembrane protein 102
|
Mus
|
MASTVWGGAPWWGPPPPAPARPLTDIDFCSGAQLQELTQLIQELRVQESWSEGPKPGADLLRAKDFVFALLGLVHRQDPRFPPQAELLLLRGGIREGSLDLGHAPLGPYSRGPHYDAGFTLLVPVFSLDGTGPELLLDLESCSAWLRLPELMRGILVREAWQDCLGPPVPEESDMTHQTHSKESPTDRENSVDPSHDYVPEPEPHMSLQKSSSDLSESQSSYKDITNPETPEPLETLSSDALDADESQVPKPSEAPKAWPTLCPTQVTSWFFVKLAEVAESLIPVPGAPRLVHAARHAGVTTVLLATPEPPRHLLLFDLIPVVTVTGWPDTARSHSWAGPLVSESASFYLVPGSLPEQPSTSGWQLCFARQELALKERIPTPLLQAHAAAQALLRPLVAGTRAAAPYLLRTLLYWACERLPALYLARPENAGACCLGLLDELSRVLEAGALPHYFLSGRKLRVGDGSAALRGALAQLRGDPAQALREAVEEAKVARKGGGLAGVGGGTH
|
Selectively involved in CSF2 deprivation-induced apoptosis via a mitochondria-dependent pathway.
|
Q3UPR7
|
Q131X4
|
PURA_RHOPS
|
IMP--aspartate ligase
|
Rhodopseudomonas
|
MANVVVVGAQWGDEGKGKIVDWLSEQADIVARFQGGHNAGHTLVINGETYKLALLPSGVLRPSKLAVIGNGVVFDPQAFLDEVERLTKQGVAISPENLRVAENVTLILPLHRELDALRENASKATSIGTTQRGIGPAYEDKVGRRAIRLMDLADIDTLPHKIERLLTHHNALRRGLGLSEFEAGAILKELTALAPRLLPYAETVWRLLDIKRREGKRILFEGAQGALLDVDHGTYPYVTSSNTVAAQAATGTGMGPGSVGYVLGICKAYTTRVGQGPFPTELDNEIGRKIGERGREFGTNTGRPRRCGWFDAVLVRQTVRTCGIHGLALTKLDILDGFDSIEVCVGYMLDGKEIDHLPAGEGAQARVVPIYETIEGWKEPTANARSWADLPAQAVKYVRRVEELVGCPIALLSTSPEREDTILVQNPFEA
|
Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
|
Q131X4
|
B4TQK8
|
NFI_SALSV
|
Deoxyribonuclease V
|
Salmonella
|
MDLASLRAQQIELASSVCREDRLDKDPPAFIGGADVGFEQGGEVTRAAMVLLKYPSLELVEYKVARIATTMPYIPGFLSFREYPALLAAWEQLSQKPDLLFVDGHGISHPRRLGVASHFGLLVDVPTIGVAKKRLCGKFEPLSTEPGALSPLMDKGEQLAWVWRSKARCNPLFIATGHRVSTDSALAWVQRCMKGYRLPEPTRWADAVASGRPAFIRWQEIQR
|
DNA repair enzyme involved in the repair of deaminated bases. Selectively cleaves double-stranded DNA at the second phosphodiester bond 3' to a deoxyinosine leaving behind the intact lesion on the nicked DNA.
|
B4TQK8
|
P37242
|
THB_MOUSE
|
c-erbA-beta
|
Mus
|
MTPNSMTENGLPAWDKQKPRPDRGQDWKLVGMSEACLHRKSHVERRGALKNEQTSPHLIQATWTSSIFHLDPDDVNDQSISSAQTFQTEEKKCKGYIPSYLDKDELCVVCGDKATGYHYRCITCEGCKGFFRRTIQKSLHPSYSCKYEGKCIIDKVTRNQCQECRFKKCIYVGMATDLVLDDSKRLAKRKLIEENREKRRREELQKSIGHKPEPTDEEWELIKTVTEAHVATNAQGSHWKQKRKFLPEDIGQAPIVNAPEGGKVDLEAFSHFTKIITPAITRVVDFAKKLPMFCELPCEDQIILLKGCCMEIMSLRAAVRYDPDSETLTLNGEMAVTRGQLKNGGLGVVSDAIFDLGMSLSSFNLDDTEVALLQAVLLMSSDRPGLACVERIEKYQDSFLLAFEHYINYRKHHVTHFWPKLLMKVTDLRMIGACHASRFLHMKVECPTELFPPLFLEVFED
|
Nuclear hormone receptor that can act as a repressor or activator of transcription. High affinity receptor for thyroid hormones, including triiodothyronine and thyroxine.
|
P37242
|
A7HNV7
|
TMCAL_FERNB
|
tRNA(Met) cytidine acetate ligase
|
Fervidobacterium
|
MRVLGIVVEYNPFHFGHLHHLEEAKKLINPDYVVAVMSGNFCQRGEPAIVNKFARTEIALKNGVDVVFELPVVYAIQDAGGFALGSVGVLDRTGVVTDIVFGSESGDVTFLRKVANLLTNQTPEFEKTFKRHLKMGYSYPNARKYALMDVLSNDVEKLSKSNDILGIEYIKALIKYSSDIQPHVIKRIGADYNDEQFKGKFSSASAVRKAIKENKFEQTKEALPEWTFKILEREFSEGRGPVFLEYFDFVIAMFRKLKREDFERIYSFNEGLDLRFYESARESGNLQDFVERVKAKRFTYSRIRRAIFHVLFDMEKSFVELSNEKGPQYLRVLGFTKRGRELLKAMKKNSKVPIISTASLYRNVLEEAKKKIAEGKVSWEIDESLYIWQFERDLLASDIYTFLYPNKFQRKAGMDFEYKVIEMLG
|
Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac-AMP) and then transfers the acetyl group to tRNA to form ac(4)C34.
|
A7HNV7
|
P38426
|
TPS3_YEAST
|
Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 115 kDa subunit
|
Saccharomyces
|
MTIIVASLFLPYTPQFEADVTNSDTAKLVESSMIKVDCNNQELSNNKQERSSSVTSASSHYIGLPQEAQINGEPLQRANVGSPATGVNYHNEMEMLSSEQFLEELTANATHAANSGIPPANNPVSSGSTAQRPSVEEFFSAPSARVCSPSQEASASSISASRSSAHHNDLSSSLMKNPNLSFDSHPPRVRSSSKSAVITPVSKSVPDVDPAVVDVAKVREEFQQQASLPSMKRVSGSTAGDSSIASSSSNLRYSQQFQDNFIEDTDSEDDIDSDLETDATKKYNVPKFGGYSNNAKLRASLMRNSYELFKHLPWTIVDSDKGNGSLKNAVNIAVAEKTVKEPVSWVGTMGIPTDELPHEVCHKISKKLEQDFSSFPVVTDDITFKGAYKNYAKQILWPTLHYQIPDNPNSKAFEDHSWDYYQKVNQKFSDRIVSVYKPGDTIWIHDYHLMLVPQMVREKLPKAKIGFFLHVSFPSSEVFRCLANRERILEGIIGANFVGFQTKEYKRHFLQTCNRLLAADVSNDEVKYHCNIVSVMYAPIGIDYYHLTSQLRNGSVLEWRQLIKERWRNKKLIVCRDQFDRIRGLQKKMLAYERFLIENPEYIEKVVLIQICIGKSSDPEYERQIMVVVDRINSLSSNISISQPVVFLHQDLDFAQYLALNCEADVFLVDALREGMNLTCHEFIVSSFEKNAPLLLSEFTGSSSVLKEGAILINPWDINHVAQSIKRSLEMSPEEKRRRWKKLFKSVIEHDSDNWITKCFEYINNAWESNQETSTVFNLAPEKFCADYKASKKHLFIFKISEPPTSRMLSLLSELSSNNIVYVLSSFTKNTFESLYNGVLNIGLIAENGAYVRVNGSWYNIVEELDWMKEVAKIFDEKVERLPGSYYKIADSMIRFHTENADDQDRVPTVIGEAITHINTLFDDRDIHAYVHKDIVFVQQTGLALAAAEFLMKFYNSGVSPTDNSRISLSRTSSSMSVGNNKKHFQNQVDFVCVSGSTSPIIEPLFKLVKQEVEKNNLKFGYTILYGSSRSTYAKEHINGVNELFTILHDLTAA
|
Regulatory subunit of the trehalose synthase complex that catalyzes the production of trehalose from glucose-6-phosphate and UDP-glucose in a two step process. May stabilize the trehalose synthase complex.
|
P38426
|
Q5X6L7
|
DAPE_LEGPA
|
N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase
|
Legionella
|
MTDIKQILTDLIGFPSITPEDAGCQKYMIQFLEQLGFTCQQLNNGPVSNFFACYGKIGPLLVFAGHTDVVPVGEVSKWDTDPFSLEEKSGVLYGRGVADMKGSLACMLHMARRFIKTYPSFPGRLGFLITSGEEGDEFNLGTPYVMQKLEQQGIVIDYCIVGEPSSSLKAGDVIKIGRRGSLSAKIHLSGKQGHVAYPHLADNPIHRISPVLAELTSMQWDNGNAFFPPTSMQITYIHCGGHAGNIIPGELNLHLNFRYSTEQTDESLKTRVINAFTHHNLNPAIEWRLNGEPFLTNKGILLESCKQTVLEHIGTLPELSTSGGTSDGRFIAPYGVEVIELGLVNATIHQVNECTSLQDLNTLETMYFSICEKLLID
|
Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls.
|
Q5X6L7
|
P48709
|
RBL_NICDE
|
Ribulose bisphosphate carboxylase large chain
|
Nicotiana
|
MSPQTETKASVGFKAGVKEYKLTYYTPEYQTKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYRIERVVGEKDQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEALFKAQVETGEIKGHYLNATAGTCEEMIKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRMSGGDHIHSGTVVGKLEGERDITLGFVDLLRDDFVEQDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVKARNEGRDLAQEGNQIIREASKWSPELAAACEVWKEIVFNFAAVDVLDK
|
RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.
|
P48709
|
C1CEH8
|
LDH_STRZJ
|
L-lactate dehydrogenase
|
Streptococcus
|
MTSTKQHKKVILVGDGAVGSSYAFALVNQGIAQELGIIEIPQLHEKAVGDALDLSHALAFTSPKKIYAAQYSDCADADLVVITAGAPQKPGETRLDLVGKNLAINKSIVTQVVESGFKGIFLVAANPVDVLTYSTWKFSGFPKERVIGSGTSLDSARFRQALAEKLDVDARSVHAYIMGEHGDSEFAVWSHANIAGVNLEEFLKDTQNVQEAELIELFEGVRDAAYTIINKKGATYYGIAVALARITKAILDDENAVLPLSVFQEGQYGVENVFIGQPAVVGAHGIVRPVNIPLNDAETQKMQASAKELQAIIDEAWKNPEFQEASKN
|
Catalyzes the conversion of lactate to pyruvate.
|
C1CEH8
|
P82930
|
RT34_HUMAN
|
Mitochondrial small ribosomal subunit protein mS34
|
Homo
|
MARKKVRPRLIAELARRVRALREQLNRPRDSQLYAVDYETLTRPFSGRRLPVRAWADVRRESRLLQLLGRLPLFGLGRLVTRKSWLWQHDEPCYWRLTRVRPDYTAQNLDHGKAWGILTFKGKTESEAREIEHVMYHDWRLVPKHEEEAFTAFTPAPEDSLASVPYPPLLRAMIIAERQKNGDTSTEEPMLNVQRIRMEPWDYPAKQEDKGRAKGTPV
|
Required for mitochondrial translation, plays a role in maintaining the stability of the small ribosomal subunit and the 12S rRNA that are required for mitoribosome formation.
|
P82930
|
P01715
|
LV301_HUMAN
|
Ig lambda chain V-IV region X
|
Homo
|
MAWIPLFLGVLAYCTGSVASYELTQPPSVSVSPGQTASITCSGDKLGDKYACWYQQKPGQSPVLVIYQDSKRPSGIPERFSGSNSGNTATLTISGTQAMDEADYYCQAWDSSTAH
|
V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition . Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens . The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen .
|
P01715
|
A1WQM5
|
MIAA_VEREI
|
Isopentenyl-diphosphate:tRNA isopentenyltransferase
|
Verminephrobacter
|
MAAPDSRLPNIALAGPTAAGKTAAALALAAALGRRQAVEIISVDSALVYRGMDIGSAKPTPAERAAVPHHLIDIRDPLQAYSAAEFVQDARRLIGEIRARGALPLLVGGTMLYFKALFDGLDAMPAADPAVRARLNARAAEQGWPALHTELARVDPVTAARLAPGDSQRIQRALEVWQISGQPLSSFHAIEKGAAGAYGACACALFSLEPQDRAWLHERIARRFDAMLAAGFIAEVQALRARGDLHPDLPAMRCVGYRQVWEALDWQARHAGGPPLHGAPLHARGMDAVRERGVAATRQLAKRQITWLRSMPQRHTTACDQPQAVAQLVQAVLQRLEQHAP
|
Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
|
A1WQM5
|
Q5LXR7
|
RS3_STRT1
|
30S ribosomal protein S3
|
Streptococcus
|
MGQKVHPIGLRVGIIRDWDAKWYAEKEYADYLHEDLAIRKFIQKELADASVSTIEIVRAVNKVIVSLHTAKPGMVIGKGGSNVDALRAQLNKLTGKQVHINIVEIKKPDLDAHLVGETIARQLEQRVAFRRAQKQAIQRAMRAGAKGIKTQVSGRLNGADIARAEGYSEGTVPLHTLRADIDYAWEEADTTYGKLGVKVWIYRGEVLPARKNTKGGK
|
Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation.
|
Q5LXR7
|
A8M519
|
RL14_SALAI
|
50S ribosomal protein L14
|
Salinispora
|
MIQQESRLRVADNTGAREILCIRVLGGSGRRYASIGDVIVATVKDAIPGAGVKKGDVVKAVVVRTAKEKRRPDGSYIRFDENAAVIIKDGGDPRGTRIFGPVGRELRDKRFMKIISLAPEVL
|
Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome.
|
A8M519
|
Q73HW8
|
MIAB_WOLPM
|
tRNA-i(6)A37 methylthiotransferase
|
unclassified Wolbachia
|
MKGLYIKTYGCQMNVYDSVLMENVIKPLGFNVVSDAGKADLVILNTCHIREKAAEKLYSELGKIHSLRKEMTIVVAGCVAQAEGEEVFRRAPFVDIVVGPQSIATLPELIVKASRSKGHVINTDFPEVAKFDKLPDECYGNSQGSSAFLAIQEGCDKFCTFCVVPYTRGAEYSRPVNEIFREALKLVANGANEINLLGQNVNAYHGECEGEVWDLGKLISHIAKIEKLERIRYTTSHPRDMHESLYLAHAEEPKLMPFVHLPVQSGSNKILHAMNRKHTAEEYLEIIDRFRKLKPEIEFSSDFIVGFPGETEKDFEETMKLVEKVRYAQAYSFKYSPRPGTPGAERKDQVPEEVKTERLLRLQKLISKQQLEFNQSMVGKTIPVLFSDKKGKHQNQIIGKSPYMQSVCIDDSEDKYRDKIVNVKVLEARQSSLLGCAFH
|
Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
|
Q73HW8
|
Q6B8W3
|
RK14_GRATL
|
50S ribosomal protein L14, chloroplastic
|
Agarophyton tenuistipitatum
|
MIQIQSYLNIADNSGARKIMCIQVLGSNNPHYANIGDIIIGVVKDALPNMPIKKSDIIRAVIVRTKKTIRRNDGMSIRFDDNAAVIINQENNPRGTRVFGPIAKELRDKNFSKIISLAAEVV
|
Binds to 23S rRNA.
|
Q6B8W3
|
Q46IS0
|
RL24_PROMT
|
50S ribosomal protein L24
|
Prochlorococcus
|
MPAINKTKGSADRIKMKIRKGDTVQVISGKDKGKTGEVLKTLPYENRVLVQGINQRTKHVKPSQEGETGRIETKEFSLHASNVMIYSTKEKVASKVEIFVDKDGSKKRRLKKTGELID
|
One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.
|
Q46IS0
|
Q98QN9
|
APT_MYCPU
|
Adenine phosphoribosyltransferase
|
Mycoplasmopsis
|
MNLEKFIKDVKDFPKQGINFKDISPLLANGQALNYTIKKMAELAKDADIIVGPDARGFLFGTPTAAFLSKPFIMVRKKGKLPGEVIKHEYDLEYGKDILEIQKGVIKPGDKAIIIDDVLATGGTTKAIIDLLESQGAKVIKIILLLELTNLNGRSKFGSLQVESLVKVSV
|
Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
|
Q98QN9
|
Q6D554
|
ISPE_PECAS
|
4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase
|
Pectobacterium
|
MQPTVIETWPAPAKLNLFLYITGQRQDGYHLLQTLFQFLDYGDTLTIRPRNDDQINLLTPIDGVENEQNLIIRAARLLQQHCERRNIRPAQFGANIHIEKCLPMGGGLGGGSSNAATVLVALNHLWQSGLNVDTLAELGLQLGADVPVFIRGYAAFAEGIGEQLTPANPPEKWYLVAHPSISIATPLIFGDPELTRNSPVRDLETLLNQTFVNDCEAIARKRFREVEQLLSWLLEYAPARLTGTGACVFAEFDTEFAARQVLDQAPEWLNGFVARGVNVSPLQRRLSGQR
|
Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
|
Q6D554
|
Q6YR70
|
SSRP_ONYPE
|
Small protein B
|
Candidatus Phytoplasma asteris
|
MKTIITNKKAFYDYSLEKKKYQAGIKLLGSEVKSIRIGKINLLNSYIHIKNEEAFIVNMTILKYPFSCCLAYDENRTKKLLLQKHEIIQIKNKIKTEKLSVIPLKVYFNKNLVKLEIALSKGKKQHDKRNALKDFDAKLRIQKTLKNFNQKQ
|
Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to translate the ORF on the tmRNA; the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and targeted for degradation. The ribosome is freed to recommence translation, which seems to be the essential function of trans-translation.
|
Q6YR70
|
Q9CQW7
|
COA8_MOUSE
|
Apoptogenic protein 1, mitochondrial
|
Mus
|
MAALRPGSRALRRLLCRSFSGGGGVRLARERPTDHRDAASSRVSRFCPPRQSCHDWIGPPDKCSNLRPVHFHIPENESPLEQRLRELRQETQEWNQQFWAKQNLSFNKEKEEFIYSRLQAKGAGLRTESGQRATLDAEEMADFYKDFLSKNFQKHMRYNRDWYKRNFAITFFMGKVVLERMWSKLRQKKTSS
|
Required for cytochrome c complex (COX) IV assembly and function Protects COX assembly from oxidation-induced degradation, COX being the terminal component of the mitochondrial respiratory chain.
|
Q9CQW7
|
A0A0N7KIY3
|
BH156_ORYSJ
|
bHLH transcription factor bHLH156
|
Oryza sativa
|
MEHHHLLLQLSPPPPPPPLPAAHLMMSPSFFDAGVFADVGGDWMEDLMHLGELFGVGVGGDDDDNGGVDGGVGGGDDRMQEWQNNCEGAGSPDHQPSCGDGDGDGDGDVSPRDGELGDGDGDNSATRKRRDRSKTIVSERKRRVRMKEKLYELRALVPNITKMDKASIIADAVVYVKDLQAHARKLKEEVAALEEARPIRPPPPSAAAQRPQRQPRRVAAAAAQLARAADAAAVTTAAAAPHGARVAHVGAAQVGEGRFFVTVECEPAAAAARGGGGGVAAPVCAAVESLSCFTVESSTVGCSPDRVVATLTLKVSEAEEDVSAISECTVKLWVMAALLKEGFRPQPTVQIS
|
Transcription factor involved in positive regulation of genes involved in strategy II iron acquisition, including genes for mugineic acid (MA) family phytosiderophores biosynthesis, and genes involved in S-adenosylmethionine cycle and iron transport . May play a role in the regulation of iron deficiency response by promoting the nuclear localization of IRO2 . Possesses transactivation activity in yeast .
|
A0A0N7KIY3
|
Q2JL76
|
RS13_SYNJB
|
30S ribosomal protein S13
|
unclassified Synechococcus
|
MARIAGVDIPREKRVEIALTYIYGIGLTRSRQILAKTGINPDTRTRDLTDAEVAALRTVVEGEYQVEGDLRRQEAMNIKRLIDIGTYRGRRHRLGLPVRGQRTRTNARTRKGVRKTVAGKKKAPAKK
|
Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites.
|
Q2JL76
|
Q74K70
|
UNG_LACJO
|
Uracil-DNA glycosylase
|
Lactobacillus
|
MKKLIGNDWDEVLAPAFESEKYQELRDFLKEEYQTKQIFPDMYHIFTAFKLTSFADTKVVILGQDPYHNPGQATGMSFSVNPGVPLPPSLKNIYKELYDDVGAVPVNHGYLKKWADQGVLLLNAVLTVPYGNANGHRGKGWELITDTAIKALSDRGKVVFILWGKFAQNKIPLIDEGKNVIIKSPHPSPFSADRGFFGSRPFSRCNDALIKFGESPIDWQLPQEVNPADMA
|
Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
|
Q74K70
|
Q87JG6
|
CH602_VIBPA
|
Chaperonin-60 2
|
Vibrio
|
MAAKDVLFANDARQKMLKGVNLLADAVKVTLGPKGRNVVLDKSYGAPTITKDGVSVAKEIELKDKFENMGAQMVKQVASKANDEAGDGTTTATVLAQSFINEGLKAVASGMNPMDLKRGIDKATEAAVEKLREMSKPCSDKESITQVGSISANSDRAIGEIIAEAMEKVGRNGVITVEEGQGLDNELSVVEGMQFDRGYLSPYFITNQENGSVELDNPYILLVDKKVSSIRELLPVLEEVAKSSRSLLIIAEDIEGEALATLVVNNMRGIVRATAVKAPGFGDNRKAMMEDIAVLTAGTVISEEIGLELEKATLEQLGSAKKVTITKDTTTIVGGAAEASAIADRVASIEKQIETTTSQYDKDKLQQRVAKLSGGVAVIKIGAATEVEMKEKKDRVDDALHATRAAVEEGIVAGGGVALTKIAKELADLKGDNDDQNVGIRVALRAMEEPLRQIATNAGDEASVVANAVKAGDADYGYNAATGEYGNMIEMGILDPAKVTRSALQFAASVAGLMITTEAMITNHVEDKELDI
|
Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
|
Q87JG6
|
A0A024SH20
|
GUN2_HYPJR
|
Endo-1,4-beta-glucanase
|
Trichoderma
|
MNKSVAPLLLAASILYGGAAAQQTVWGQCGGIGWSGPTNCAPGSACSTLNPYYAQCIPGATTITTSTRPPSGPTTTTRATSTSSSTPPTSSGVRFAGVNIAGFDFGCTTDGTCVTSKVYPPLKNFTGSNNYPDGIGQMQHFVNDDGMTIFRLPVGWQYLVNNNLGGNLDSTSISKYDQLVQGCLSLGAYCIVDIHNYARWNGGIIGQGGPTNAQFTSLWSQLASKYASQSRVWFGIMNEPHDVNINTWAATVQEVVTAIRNAGATSQFISLPGNDWQSAGAFISDGSAAALSQVTNPDGSTTNLIFDVHKYLDSDNSGTHAECTTNNIDGAFSPLATWLRQNNRQAILTETGGGNVQSCIQDMCQQIQYLNQNSDVYLGYVGWGAGSFDSTYVLTETPTGSGNSWTDTSLVSSCLARK
|
Endoglucanase (EG) that cleaves the internal beta-1,4-glucosidic bonds in cellulose. The degradation of cellulose involves an interplay between different cellulolytic enzymes. Hydrolysis starts with EGs, which cut internal glycosidic linkages to reduce the polymerization degree of the substrate and creates new chain ends for exocellobiohydrolases (CBHs). The CBH release the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain. Finally, beta-1,4-glucosidases hydrolyze the cellobiose and other short cello-oligosaccharides into glucose units.
|
A0A024SH20
|
A6UPK3
|
CBID_METVS
|
Cobalt-precorrin-6A synthase
|
Methanococcus
|
MTIDFRTETTFGYTTGACAVSGAYSALYFLKNNKKLDFVEILNLKNETLIIPIQNIERSENTAFATVKKFSGKDIDITNNMTINVEVTLQKLDNNSNLKLIEIFGGNGVGIVTKRGLQIDVGDYAINPKPREMIEKNLISLLNDGEKAVVRISIPNGDEISKKTLNPKLGIIGGISILGTTGIVRPMSNDAYKESLLPQIDIAIQNGFENLVFVPGNIGTKYAKSVLNIEEDQIIEVSNFWGFMLEKAGEKGVKDITVFGHAGKIVKLAGGIFDTHSKVSDARNEILCAYTSTLCNNQELMKKILQSNTTEEIIEILAEKDILNEVFNLISKRVVERLCLRFPNIKFSCIIVDINGKILGKCFLGDRFD
|
Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.
|
A6UPK3
|
O02305
|
NH217_CAEEL
|
Nuclear hormone receptor family member nhr-217
|
Caenorhabditis
|
MCRSVSNMLDRISGLSKDASPNSTTTIQEIITLEKCLTSKVSALFLICKMLKIPACPVCDVPCRIEPHFGGIACAACAAFFRRTVSLNIGYMCKREKLCRKARKSCRACRFERCVKSAGLQRDYVRQLLTPRNTPLYILNRQDNTGGEIVRAFASPTMPKPEPTPQLGFSDILKVSNSSLFKFYLNQVEKAVKLRQKNTLTIKTNAELLKIVATQQELALEACRTCPGMDLLDKEDRKVVQKYFVFSNVWIESTWLYSLAKEHLETENNLNFDINLKKFIEQVKSTLLFSFSQFKLNIFELAAFKAICIWKLIYHETSRAMKIIAQEHYDGVASALRNYYETHTSMDHSEIAIRIGEITLLVVSIFQLYHDMAKLYVQIGIPF
|
Orphan nuclear receptor.
|
O02305
|
B1KD27
|
PROA_SHEWM
|
Glutamyl-gamma-semialdehyde dehydrogenase
|
Shewanella
|
MIENNELYLQTLGQNAKQASYGLASLTGTQKKALLSAIAASLTAKSQAILAANQKDVAAARENGLSEAMIDRLLLDDARLKGVISDIDNVISLNDPVGTELESQLLDNGLRLSRRRVPLGVIGVIYEARPNVTVDIAVLALKTGNAVILRGGKETLNSNMALSEAIREAITEQGLAADSVQLIKSPDRTLVSGLLKLDQFVDMIVPRGGQNLQRLCAEQATIPVILGGIGICHLYMDKDANIAKSIEVIANAKVQRPTVCNALDTVLIHDSLAETALPQLFSNLSAQGVSFYGCEQTKAIADKLGLAISTATDETYGQEWLSLTLGIKVVADIDTAIGHIRRYSSGHSEGILTDNIHASAHFINQVDSAAVYVNASTRFTDGGQFGLGAEVAVSTQKLHARGPMGLEALTTYKWIGLGEYTVRG
|
Catalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.
|
B1KD27
|
Q53005
|
4HBCL_RHOPA
|
4-hydroxybenzoyl-CoA synthetase
|
Rhodopseudomonas
|
MPLRDYNAAVDFVDRNVAEGRGGKIAFIDPQRSLSYGELRDAVARVGPMLARLGVEQENRIALVLKDTVDFPILFWGAIRAGIVPVLLNTRLTADQYRYLLEDSRSRVVFASSEFLPVIEEAAADLPHLRTIIAVGDAPAPTLQLANLLATEQEGGAPAATCADDIAYWQYSSGTTGMPKGVMHVHSSPRVMAENAGRRIGYREDDVVFSAAKLFFAYGLGNAMFCPMGIGATSVLYPERPTADSVFDTLRLHQPTLLFAVPTLYAAMLADPRSRTETLPDRLRLCVSAGEPLPAQVGLNWRNRFGHDIVNGVGSTEMGHLFLTNLPHAVEYGTSGVPVDGYRLRLVGDRGQDVADDEIGELLVSGGSSAAGYWNQRDKTRTTFVGEWTRTGDKYHRRADGVYTYCGRTDDIFKVSGIWVSPFEIEQALMSHAKVLEAAVIPAEDTDGLIKPKAFIVLASRGDIDPGALFDELKEHVKSAIGPWKYPRWIQIMDDLPKTSSGKLQRYLLREMTLGGIEATESAPSEPALYGRVVAGNGR
|
Catalyzes the ligation of 4-hydroxybenzoate, benzoate or cyclohex-1,4-dienecarboxylate and CoA at the expense of ATP. The enzyme shows low activity towards cyclo-2,5-dienecarboxylate, 4-fluorobenzoate, 4-chlorobenzoate and 2-methoxybenzoate.
|
Q53005
|
Q9LF27
|
WDR12_ARATH
|
Pescadillo-interacting protein 2
|
Arabidopsis
|
MDIDGEDVSRRLHVKFVTKLDSPFKVPVNSVAIPSNVTRLGLSSIVNSIIESENPEWKTEPFDFLIDGELIRMSLEEFLLAKGISAERTLEIEYIRAVTPRKEEEPSLHDDWVSAVNGSSPRFILTGCYDGLGRVWSSAGSCSHILEGHSGAISSVALVNSNDAETVTVATASKDRTLRLFKFDPAESVDSTTKVRAYKILRGHKASVQSVSAQKSGNMVCSSSWDCTINLWNTNESTSEGESVSVKKRKGNNQAEESQSEGEAVTSLVGHTQCVSSVVWPEHDVIYSSSWDHSVRRWDVETGKDSLNLFCGKALNTVDVGGESSALIAAGGSDPILRVWDPRKPGTSAPVFQFSSHSSWISACKWHKSSWFHLLSASYDGKIMLWDLRTAWPLSVIDTHNDKVLSADWWKGESVVSGGADSNLRISSGIAIS
|
Required for maturation of ribosomal RNAs and formation of the large ribosomal subunit.
|
Q9LF27
|
O21260
|
RPOA_RECAM
|
Transcriptase alpha chain
|
Reclinomonas
|
MVHKTPSFRPIIHVLKHDFNSIQVLIGPLEKNFSGSFANLLRKIIFRYTSGVSIIGLKINGIDSLHSYSLIPGVKEDVLNVLNNLKHLLIQIDDYDYKPILLTIQKKGPYIIKSKDIICPSNIKILNDDLYICTLENDSQIDLTLIGDIGCGYVLSTYFGNRKSIVYSDTNFCPIKHVSYYVRSYTTYEELIFYIKTNGTCNPLFVMKNAFSFLKDKINITF
|
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
|
O21260
|
Q0AIF2
|
SYV_NITEC
|
Valyl-tRNA synthetase
|
Nitrosomonas
|
MELAKSFDPKDIENHWYSVWETAGYFSPAKREEVNAYCIMLPPPNVTGTLHMGHAFQHTLMDALIRYHRMLGDNTLWQPGTDHAGIATQIVVERQLDQEGKDRRQMGREAFLERVWQWKEESGSTITRQMRRMGTSCDWSRERFTMDEVLSRAVTEVFVRLYREGLIYRGKRLVNWDPVLQTAVSDLEVVSVEEQGSLWHILYPFEHRAENGEKGLIVATTRPETMLGDVAVAVHPEDVRYRHLIGHHVRLPLSERTIPIIADSYVDPAFGTGCVKITPAHDFNDYQVGLRHKLIPLSIFTLDGKINDNAPVEFQGLDRFDARKKVITDLQAQELLVETRPHKLMIPRGDRTNTVIEPMLTDQWYLAMEGLAKQGLAAVESGQVRFVPENWAHVYNQWLENIQDWCISRQLWWGHRIPAWYDEDGNVIVAYDLEEARKLSGKENLHQDEDVLDTWFSSALWPFSTLGWPEQTPELKTFLPGSVLVTGFDIIFFWVARMVMMSLHFTGEVPFREVYITGLIRDAEGQKMSKSKGNVLDPLDLIDGVALTELIRKRTTGLMNPKQAESIEKATRKQFPQGIPAFGADALRFTFASLASHGRDIKFDLQRCEGYRNFCNKLWNATRFVLMNCEGKDTGLDEGLPLNFSPADKWIIGRLQQAEQSVIQAFNEYRFDLAAREMYEFIWDEYCDWYVELAKVQLNSEDEARQRATRRTLVRVLETVLRQAHPIIPFITEELWQAVAPLAGKTGASIMCQPYPQPDQLRIDEQAAADIQLLKEVVNACRTLRGEMKLSPADRIPLLIEGDRARLINFFPHLQALARLSEVDILPGGLPDTDAPVAVVGDFRLMLKIEIDVKAERERLNKEILRVEAEISKARVKLDNPDFIQRAPEKVVQQEKGRLVTFSTTLKKLDEQLRKLD
|
Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner.
|
Q0AIF2
|
U5HKE8
|
C71DZ_CATRO
|
Cytochrome P450 71D351
|
Catharanthus
|
MELYYFSTFAFLLFCFILAKTLKKSGQSNLKLPLGPPPIPILGNAHQLIGGHTHHILRDLAKKYGPLMHLKTGEVSTIVASSPEIAEEMFKTHDVLFADRPSNIVAFKILSYDYSDVVISPYGNYWRQLRKISMMELFSQRSVQSFRSIREEEVLNFIKSIGSREGTKINLSKEISLLIYGITTRAAFGEKNKNTEEFIRLLDQLTVAVAEPNIADMFPSINFLKLISRSKYKIEKIHKNFDAIVQTILNHHKDRLANHKSSSHEENGEQNKDLVDVLLNIQQRGDFDTPLGDRSVKAVIFNIFSAGTETSSTTVDWAMCEMIKNPTIMKKAQEEVRKVYNEEGNVNETKLHQLKYLKAVIKETLRLHPPVPLLLPRECREQCEIKGYTIPSKSRVIVNAWAIGRDPNYWIEPENFNPERFLESEVDFKGNSFEYLPFGGGRRICPGITFALANIELPLAQLLFHFDWKLASDETNIDKLDMTESRGVTVRREDDLCLIPFPYSASSLKGKY
|
Involved in the foliar biosynthesis of vindoline, a precursor of vinblastine and vincristine . Hydroxylates specifically tabersonine, 2,3-dihydrotabersonine and 2,3-dihydro-3-hydroxytabersonine, but has no activity with naringenin, tryptamine, secologanin, strictosidine, ajmalicine, vindoline and catharanthine .
|
U5HKE8
|
B4RBZ9
|
SYP_PHEZH
|
Prolyl-tRNA synthetase
|
Phenylobacterium
|
MRLSRYFMPTLREAPSDAQIVSHQLMLRAGMIRQEAAGIYAWLPLGLKVLKKIEQVVREEMDRAGAIEVLMPTLQLADLWRESGRYDDYGEEMLRIKDRHERDLLYGPTAEEVITDIFRAYIKSYKDLPKNLYNIQWKFRDERRPRFGVMRGREFLMKDAYSFDIDEAAARRAYNRMFCAYLNVYARLGLKAIPVRADTGPIGGDLSHEFIILADTGESQVFAHRDLVEMGAPGPDIDWDGDLEPLVQQRTRLYAASDEMHDQARFETEAPEDKRMTARGIEVGHIFYFGEKYSRPMNAKVAGPDGAERFVHMGSYGVGVSRLVGAIIEASHDEAGIVWPDSVAPFGAAVVNLRPGEAAVDAVAEQAYGALQAAGKEPLLDDRDERPGAKFASLDLVGVPWQLIVGPKGVAEGVVEIKRRATGERQTLPLDAALKAITA
|
Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro).
|
B4RBZ9
|
B1I1B2
|
RS4_DESAP
|
30S ribosomal protein S4
|
Candidatus Desulforudis
|
MARYTDARCRLCRREGTKLYLKGDRCYSPRCAVDRRPAPPGQHTPSRRKVTEFGIQLREKQKVRRIYGVLESQFRNYFHKAERQPGVTGENLLRLLELRLDNVIYRLGLGASRAEARQLVRHGHFKVNGRKVDIPSYQVRVGDVIAVRERSKGLTRIQELLDRASENNPPAWLEYDGERAVARVVALPTRENIDIPVREQLVVELYSR
|
With S5 and S12 plays an important role in translational accuracy.
|
B1I1B2
|
Q5PPK1
|
BRI3_RAT
|
Brain protein I3
|
Rattus
|
MDHKPLLQERPPAYNLEAGQGDYACGPHGYGAIPTAPPPPPYPYLVTGIPTSHPRVYNIHSRAVTRYPANSIVVVGGCPVCRVGVLEYCFTCLGIFLAIVLFPFGFLCCFALRKRRCPNCGAVFT
|
Participates in tumor necrosis factor-alpha (TNF)-induced cell death. May be a target of Wnt/beta-catenin signaling in the liver.
|
Q5PPK1
|
A3CLF8
|
GATA_STRSV
|
Glutamyl-tRNA(Gln) amidotransferase subunit A
|
Streptococcus
|
MTFNHKTIEELHDLLVKKEISAVELTQATLADIKEREAAVDSFITVSEEEALAQAAALDAKGIDADNLMSGIPLAVKDNISTKGILTTAASKILYNYKPIFDATSVEKLYGKDMIIVGKTNMDEFAMGGSSENSYFKTTKNAWDSSKVPGGSSGGSATAVASGQVRLSLGSDTGGSIRQPASFNGVVGLKPTYGRVSRFGLIAFGSSLDQIGPFSQTVKENAQLLNVISGNDPKDSTSSQEEVPDFTSKIGQDIKGMKIALPKEYMGEGIDSKVKETILAAAKHLESLGAIVEEVSLPHSKYGVAVYYIIASSEASSNLQRFDGIRYGYRAEGIENLEDVYVKSRSEGFGEEVKRRIMLGTFSLSSGYYDAYFKKAGQVRTLIMQDFAKVFEKYDLILGPTAPTVAYDLGSQNQDPVAMYLADLLTIPVNLAGLPGISIPAGFVDGLPVGLQLIGNHFDEATIYQTAAAFEATTDYHKQQPVIFGGEK
|
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
|
A3CLF8
|
O30509
|
GATB_BACSU
|
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
|
Bacillus
|
MNFETVIGLEVHVELKTKSKIFSSSPTPFGAEANTQTSVIDLGYPGVLPVLNKEAVEFAMKAAMALNCEIATDTKFDRKNYFYPDNPKAYQISQFDKPIGENGWIEIEVGGKTKRIGITRLHLEEDAGKLTHTGDGYSLVDFNRQGTPLVEIVSEPDIRTPEEAYAYLEKLKSIIQYTGVSDCKMEEGSLRCDANISLRPIGQEEFGTKTELKNLNSFAFVQKGLEHEEKRQEQVLLSGFFIQQETRRYDEATKKTILMRVKEGSDDYRYFPEPDLVELYIDDEWKERVKASIPELPDERRKRYIEELGFAAYDAMVLTLTKEMADFFEETVQKGAEAKQASNWLMGEVSAYLNAEQKELADVALTPEGLAGMIKLIEKGTISSKIAKKVFKELIEKGGDAEKIVKEKGLVQISDEGVLLKLVTEALDNNPQSIEDFKNGKDRAIGFLVGQIMKASKGQANPPMVNKILLEEIKKR
|
Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
|
O30509
|
B2V4F5
|
EFTS_CLOBA
|
Elongation factor Ts
|
Clostridium
|
MISAKSVKELRERTGAGMMDCKKALTETDGDIEKAVEVLREKGLAAAAKKSGRVAAEGLVKTYISEDKKSGAIVELNCETDFVAANEDFIAFADALAKIATSTSATTVEELVNEKFDAEATIQEALTGLIARLGENMTVRRFVKFSVDNGVVKSYIHGGGRIGVLVEVACDVESPAVEEVAKELCMQIAAANPLFLSKEEVDQDSIEKEKEIYRVQALNEGKPEKIVEKMVMGRIQKYYKEVCLLEQLWVKDSDKTITKFIDEKAKEAGSAIKVNRFVRFERGEGIEKVEENFAEEVAKQLGK
|
Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.
|
B2V4F5
|
P76193
|
YNHG_ECOLI
|
Probable L,D-transpeptidase YnhG
|
Escherichia
|
MKRASLLTLTLIGAFSAIQAAWAVDYPLPPTGSRLVGQNQTYTVQEGDKNLQAIARRFDTAAMLILEANNTIAPVPKPGTTITIPSQLLLPDAPRQGIIVNLAELRLYYYPPGENIVQVYPIGIGLQGLETPVMETRVGQKIPNPTWTPTAGIRQRSLERGIKLPPVVPAGPNNPLGRYALRLAHGNGEYLIHGTSAPDSVGLRVSSGCIRMNAPDIKALFSSVRTGTPVKVINEPVKYSVEPNGMRYVEVHRPLSAEEQQNVQTMPYTLPAGFTQFKDNKAVDQKLVDKALYRRAGYPVSVSSGATPAASNAPSVESAQNGEPEQGNMLRVTQ
|
Responsible, at least in part, for generating a meso-diaminopimelyl-3-a meso-diaminopimelyl-3 cross-link.
|
P76193
|
B8JAZ0
|
NUON_ANAD2
|
NDH-1 subunit N
|
Anaeromyxobacter
|
MSGFPTQDFVALVPVAILTMGALVLLMTEVFLTSGRRAYQAYLTMVFAAAAAGYAAWMPVPGNVFGRQAVVDSFSAFVTVVLCAGLALSALVGQSWLNARNSERGEFYALALFGTAGMVLLGMATDLLIAFIAVEVMSLSTYCLAAFLRRGKKPAEAAFKYVVLGSISSALLLYGSALLYGASGSTLFSVLPRGQGSALYLAGIALVAGGVAFKIAAVPFHAWTPDVYEGAPTPVTAFMAAGVKTAAFAVLVRLFLATESGSAAMSTSLGTVLSALAVLTMIFGNLLALPQRSVKRMLAYSSIGHAGYLLVGVVSAVVAGARDKALAGLLFYLAAYTATVIGAFAVVGALERRTRGDFEPADAWDLDRFAGLARRRPALAFAMAVFLFSLAGVPPTAGFIGKFYIFKAAMGAGLYGLAVLGVLTSVLGAYYYLRVVLYMYFLPSKDEAGEVVLSAPSLTIALAAAVAVVVLLGVVADPMVRLAQAASAIIL
|
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
|
B8JAZ0
|
B8ZSC7
|
RPOB_MYCLB
|
Transcriptase subunit beta
|
Mycobacterium
|
MLEGCILPDFGQSKTDVSPSQSRPQSSPNNSVPGAPNRISFAKLREPLEVPGLLDVQTDSFEWLIGSPCWRAAAASRGDLKPVGGLEEVLYELSPIEDFSGSMSLSFSDPRFDEVKAPVEECKDKDMTYAAPLFVTAEFINNNTGEIKSQTVFMGDFPMMTEKGTFIINGTERVVVSQLVRSPGVYFDETIDKSTEKTLHSVKVIPSRGAWLEFDVDKRDTVGVRIDRKRRQPVTVLLKALGWTSEQITERFGFSEIMRSTLEKDNTVGTDEALLDIYRKLRPGEPPTKESAQTLLENLFFKEKRYDLARVGRYKVNKKLGLHAGELITSSTLTEEDVVATIEYLVRLHEGQSTMTVPGGVEVPVETDDIDHFGNRRLRTVGELIQNQIRVGMSRMERVVRERMTTQDVEAITPQTLINIRPVVAAIKEFFGTSQLSQFMDQNNPLSGLTHKRRLSALGPGGLSRERAGLEVRDVHPSHYGRMCPIETPEGPNIGLIGSLSVYARVNPFGFIETPYRKVVDGVVSDEIEYLTADEEDRHVVAQANSPIDEAGRFLEPRVLVRRKAGEVEYVASSEVDYMDVSPRQMVSVATAMIPFLEHDDANRALMGANMQRQAVPLVRSEAPLVGTGMELRAAIDAGHVVVAEKSGVIEEVSADYITVMADDGTRRTYRMRKFARSNHGTCANQSPIVDAGDRVEAGQVIADGPCTENGEMALGKNLLVAIMPWEGHNYEDAIILSNRLVEEDVLTSIHIEEHEIDARDTKLGAEEITRDIPNVSDEVLADLDERGIVRIGAEVRDGDILVGKVTPKGETELTPEERLLRAIFGEKAREVRDTSLKVPHGESGKVIGIRVFSHEDDDELPAGVNELVRVYVAQKRKISDGDKLAGRHGNKGVIGKILPAEDMPFLPDGTPVDIILNTHGVPRRMNVGQILETHLGWVAKSGWKIDVAGGIPDWAVNLPEELLHAAPNQIVSTPVFDGAKEEELQGLLSSTLPNRDGDVMVGGDGKAVLFDGRSGEPFPYPVTVGYMYIMKLHHLVDDKIHARSTGPYSMITQQPLGGKAQFGGQRFGEMECWAMQAYGAAYTLQELLTIKSDDTVGRVKVYEAIVKGENIPEPGIPESFKVLLKELQSLCLNVEVLSSDGAAIELREGEDEDLERAAANLGINLSRNESASIEDLA
|
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
|
B8ZSC7
|
Q3Z8X4
|
RECR_DEHM1
|
Recombination protein RecR
|
Dehalococcoides
|
MKDTSLPSTAGAVNKLIDSLGKLPGIGPKSAQRLAFYLMRAPEEQVLTLSDTIRSIKNQISQCRICFNVADSELCPICQNTKREANKICVVEQPQDILALEHVGVYRGYYHVLHGAISPTEGITSQNIRINELMSRLNDGQVDEVILATNPTTEGEATAMYLSRLITPLGIKVTRLARGLPFGTELEYADDVTLSRAMEGRQNF
|
May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO.
|
Q3Z8X4
|
B2JDU7
|
RS20_PARP8
|
30S ribosomal protein S20
|
Paraburkholderia
|
MANSAQARKRARQAAKANSHNSALRSKYRTAVKAVRKAIEAGDAAQAAEIFKASAKTLDIIADKKIVHKNKAARHKSRLAAAVKGLQAPAAQ
|
Binds directly to 16S ribosomal RNA.
|
B2JDU7
|
Q99289
|
HLT_VIBPA
|
Phospholipase A2
|
Vibrio
|
MMKKTITLLTALLPLASAVAEEPTLSPEMVSASEVISTQENQTYTYVRCWYRTSYSKDDPATDWEWAKNEDGSYFTIDGYWWSSVSFKNMFYTNTSQNVIRQRCEATLDLANENADITFFAADNRFSYNHTIWSNDAAMQPDQINKVVALGDSLSDTGNIFNASQWRFPNPNSWFLGHFSNGFVWTEYIAKAKNLPLYNWAVGGAAGENQYIALTGVGEQVSSYLTYAKLAKNYKPANTLFTLEFGLNDFMNYNRGVPEVKADYAEALIRLTDAGAKNFMLMTLPDATKAPQFKYSTQEEIDKIRAKVLEMNEFIKAQAMYYKAQGYNITLFDTHALFETLTSAPEEHGFVNASDPCLDINRSSSVDYMYTHALRSECAASGAEKFVFWDVTHPTTATHRYVAEKMLESSNNLAEYRF
|
Phospholipase hydrolyzing both fatty acid esters of phospholipid, i.e. it hydrolyzes phosphatidylcholine (PC) to lysophosphatidylcholine (LPC) and then LPC to glycerophosphorylcholine (GPC).
|
Q99289
|
Q8ZRM9
|
METN1_SALTY
|
Methionine import ATP-binding protein MetN 1
|
Salmonella
|
MIKLSNITKVFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKARRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQKFIQSTLHLDIPEDYQARLKASPETDSVPMLRMEFTGQSVDAPLLSETARRFNVNNNIISAQMDYAGGVKFGIMLTEMHGTQEETQAAIAWLQDHHVKVEVLGYV
|
Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system.
|
Q8ZRM9
|
A4IJS4
|
MURG_GEOTN
|
Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase
|
Geobacillus
|
MRKKIVLTGGGTAGHVMVNVALIPKLKEQGWDIVYIGSHEGIEREIIGRIDGVPYYSVSTGKLRRYFDWKNFKDPFNVLKGVWQAYRLIQKEKPDIVFSKGGFVSVPVILGAWLNGVPSVIHESDLTPGLANKIAMPFATKICLTFPETKQHVNTDKAVYVGAVVREELKHGSAEQGRKLCQFDGQKPVLLAMGGSLGSKKINDALRASLPVLLSEFDIVHICGKGNVDTSLVGQKGYKQFEYVNEELPDLLALSDIVVSRAGANAIFELLALRKPMLLIPLSKAASRGDQILNARSFEKAGYAEVLMEEEVTNESLPAAIHRLYENKDRYKKNMEKSGSSDPLQTLLALIQNTAR
|
Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
|
A4IJS4
|
P0CO83
|
MON1_CRYNB
|
Vacuolar fusion protein MON1
|
Cryptococcus neoformans species complex
|
MTSESEPNTSLPFSPIQQTLPATPSRSTSQVSMVSAEALLSHSSPTKQLTPSHRSSLPSALPYNTLLNAPAGSPALRARASTASSSRAPSVLDDARVEHNDSETQVLEITPPMDNYELDGGSDHTSLPSDASSIKGKEKQRSNDRNEIETVGAGGEMALPSGDARKGLKELVRRSTTADKGYGGHDHRRLSEKLSQTDENLQILITQSDKMSYSPRLYYVLTNAGKPVFCSHTRPSEDDVTNLMGVAQALISIFADDDDRLRYIIKGNHRVAFLLKAPLYLFCVSDWGEPEHVLRLQLEYIHLQILSVVSSTQLLRLFQRRSNADLSTLLEGTEPFLSNLIDCSQYDFSFLTSTLQPLRMAPALRDTSAAALMPPSKFKDLLYVLLIAGGHIVTVLRPRKHSIHPSDLHLLLNTIASSSALRTTETWLPICFPKFNPSGFVHAYISYVLEDVGLVFVSADREAFEDLRVWKDMVLEKLEQDKTLSRIQEAIPLHPYTISSVGCPGLRHFIYKSRQHVQITQPIWEAPYEDGSTNQKRLVTTYQKLHDAVHAKSGQASALKLVYISTEHEACLVWATKPFELYITVSPQLSKSAVVAAANNVAKWVLAEEGRIFLKDAPVF
|
Required for multiple vacuole delivery pathways including the cytoplasm to vacuole transport (Cvt), autophagy, pexophagy and endocytosis.
|
P0CO83
|
Q9JV52
|
DCUP_NEIMA
|
Uroporphyrinogen decarboxylase
|
Neisseria
|
MTLLKNDTFLRALLKQPVEYTPIWMMRQAGRYLPEYKATRAKAGSFLDLCKNTELATEVTIQPLERFDLDAAILFSDILTVPDAMGLGLYFAEGEGPKFKRALQHEDDIAKLHVPDMEKLQYVFDAVTSIRKALDGRVPLIGFSGSPFTLACYMVEGGSSKEFRTIKTMMYSRPDLLHKILDTNAQAVTAYLNAQIDAGAQAVQIFDTWGGVLSDAAFKEFSLKYIRQIVAGLKRESEGRRVPVIVFAKGGGLWLESMAQIGADALGLDWTCNIGEARRRVGKQVALQGNFDPFALFGTPESIRTEVARILADYGHGSGHVFNLGHGINQHADPEHAKILVDTVHELSRQYHGG
|
Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
|
Q9JV52
|
B5FL01
|
PYRC_SALDC
|
Dihydroorotase
|
Salmonella
|
MTAPSQVLKIRRPDDWHVHLRDGDMLKTVVPYTSEIYGRAIVMPNLASPITTVDAAIAYRQRILDAVPAGHDFTPLMTCYLTDSLDADELERGFHEGVFTAAKLYPANATTNSSHGVTSVDAIMPVLERMEKLGMPLLVHGEVTHAEVDIFDREARFIDTVMEPLRQRLTALKVVFEHITTKDAAQYVRDGNDYLAATITPQHLMFNRNDMLVGGIRPHLYCLPILKRNIHQQALRELVASGFTRAFLGTDSAPHSRHRKETSCGCAGCFNAPSALGSYAAVFEEMNALAHFEAFCSLNGPQFYGLPVNAGWVELVRDEQQVPENIALADDSLVPFLAGETVRWSVKK
|
Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
|
B5FL01
|
A3PL43
|
URED_CERS1
|
Urease accessory protein UreD
|
Cereibacter
|
MNALTPLSARLERSDGHALVTLARSRGAVRLRDLAQRGSAKAFLPRVEGDVPEVVFLNTSGGLTGGDRLSYRLELGAGCRATATTQTAERAYAAGAGAARVEVLHEVGRDGWLDWLPQETILFEGAALERETQISLAPGAGCLMVESVVLGRAAMGETLSRLAFRDRRSILRAGKPVLVEPLALDDRALAAAGGAAMLGGARALATLAMVGPGAEDALGPARAALGEAGVEAAASAFDGKLVLRLLAADGWPLRRQVARLLTVLRGRALPRVWQV
|
Required for maturation of urease via the functional incorporation of the urease nickel metallocenter.
|
A3PL43
|
P25155
|
FA10_CHICK
|
Activated factor Xa heavy chain
|
Gallus
|
MAGRLLLLLLCAALPDELRAEGGVFIKKESADKFLERTKRANSFLEEMKQGNIERECNEERCSKEEAREAFEDNEKTEEFWNIYVDGDQCSSNPCHYGGQCKDGLGSYTCSCLDGYQGKNCEFVIPKYCKINNGDCEQFCSIKKSVQKDVVCSCTSGYELAEDGKQCVSKVKYPCGKVLMKRIKRSVILPTNSNTNATSDQDVPSTNGSILEEVFTTTTESPTPPPRNGSSITDPNVDTRIVGGDECRPGECPWQAVLINEKGEEFCGGTILNEDFILTAAHCINQSKEIKVVVGEVDREKEEHSETTHTAEKIFVHSKYIAETYDNDIALIKLKEPIQFSEYVVPACLPQADFANEVLMNQKSGMVSGFGREFEAGRLSKRLKVLEVPYVDRSTCKQSTNFAITENMFCAGYETEQKDACQGDSGGPHVTRYKDTYFVTGIVSWGEGCARKGKYGVYTKLSRFLRWVRTVMRQK
|
Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting. VAP cleaves the fusion proteins of Sendai virus, NDV, and influenza virus a at a specific single arginine-containing site, and plays a key role in the viral spreading in the allantoic sac.
|
P25155
|
Q7XRX1
|
RFC4_ORYSJ
|
Activator 1 subunit 4
|
Oryza sativa
|
MDASSSSAPDLADAYDIPWVEKYRPTRVADVGGNSDAVARLQDIARDGNMPNLILSGPPGTGKTTSILSLAHELLGPSYREAVLELNASDDRGLDVVRNKIKMFAQKKVTLQPGRHKIVILDEADSMTSGAQQALRRTMEIYSNTTRFALACNTSSKIIEPIQSRCAIVRFSRLSDQEILGRLMIVVAAEKVPYVPEGLEAIIFTADGDMRQALNNLQATVSGFRFVNQENVFKVCDQPHPLHVKNMVKNVLDGKFDEACSALKQLYDLGYSPTDIITTLFRVIKNYDMAEYLKLELLKETGFAHMRICDGVGSFLQLSGLLAKFALVRETAKAS
|
May be involved in DNA replication and thus regulate cell proliferation.
|
Q7XRX1
|
O29248
|
ILVD_ARCFU
|
Dihydroxy-acid dehydratase
|
Archaeoglobus
|
MRSDEVKKGIDRVAHRALLKALGVTDDEMDKPFIGVANAYNTIVPGHMTLDKLTQAVKEGVYAAGGVPFEFGIIGICDGIAMGHEGMCFSLPSRELVADTIEAMVEAHRFDGLVVVASCDKIIPGMLMAMLRLNIPAIAVTGGPMPYERVGGEKVSIKDAFEAAGMYKAGKLDDAGLKLYEDYCAPYCGSCQGLYTANSMQILTETLGLSLPYCSTSPCPSSRKLRIAKQSGKRVVELVMQNIKPLDFVNERSFENAITMDMLVGGSTNTVLHLPAIAKEAGIRLSLDLFDEISRRTPHIVSIDPASKEMVVDLDESGGVPMLIKKARKYFHDEMTVSGKTLYEIAEMAVLRGRDIIASPDNPLHKEGGIAILKGNLAENGAVIKAAAVSEDMMRFEGTAKVYDSEKEALNAILDGKVEEGDVVVIRYMGPKGAPGMPEMLLPTAAISGLGLQKVALITDGRFSGATRGPCIGHVSPEAAVGGNIALVEDGDKISIDIPARKLEVKLSDEELAERRAKWKPKEKELKGYLAKYAKLVRGAEEGAALL
|
Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively.
|
O29248
|
Q2J9L8
|
TSAD_FRACC
|
tRNA threonylcarbamoyladenosine biosynthesis protein TsaD
|
Frankia
|
MPPEQGPVVLGIETSCDETGVGLVRNGTLLGEALSTSMDQHARYGGVVPEIAARAHVQALVPCVRAALSSAGLFVADIGAVAVTAGPGLATALHVGVAAAKAYATALDVPLYGVHHLAGHLAADLVDGEPLPDPLIALIVSGGHTSLLRVGDLARDPITHLGDTLDDAAGECFDKVARVLGLPYPGGPAVDRAAVGHDATALAFPRPLTGRADAPYTFSFSGLKTAVARWVESHPDSPVPAGDVIASFQEAVVDVLTAKAVRACLDHGIGDLLIVGGVAANSRLRALAASRCEQTGIRLRIPARRRCTDNGVMIAALGDLLVRAGAEPSPAELTAMPGAFLERAQLGTALPALHAA
|
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
|
Q2J9L8
|
J9VPD8
|
QCR2_CRYNH
|
Cytochrome b-c1 complex subunit 2, mitochondrial
|
Cryptococcus neoformans species complex
|
MYSLNRLPRSAAFKSSANLLRRNASTTSAGGVNVVGFENKGPAATSSLTVAIKAGSRYETTPGVAHVLKSFAYKATASASALRTAREAELYGGVLSAALTREHLLLSAEFLRGDEEHFLNVLASVLSSSQFYRHELSELVLPVVEAETISSQAIPSTIALDLAHSLAFRRGLGNSLYANKNYPVSIDDVKSFGEAAFAKSNIAVIGTGVSTEALAKAVSNAFGAGTSSGSKLSTPKANYYGGETRVPLDIHAPATATPTMVIAFGTSSPASADLKVLKHLLGGETSVKWTPGASPLAQAADKIPGASAKAFLLPYSDAALFGVVLSAPTSAETKTLAQEVASIVKNAGEFKEEEVKRAVAKATFEDAASTETLSGFVAAAGPAALVGSVPEAQSFSGVSASSISKAAGELLKGKPTVVSIGNISVLPYADELGL
|
Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
|
J9VPD8
|
A4WBC7
|
HEM1_ENT38
|
Glutamyl-tRNA reductase
|
Enterobacter
|
MTLLALGINHKTAPVALRERVTFSPDTLDQALDSLLAQPMVQGGVVLSTCNRTELYLSVEEQDNLHEALIRWLCEYHNLNEEELRTSVYWHQDNDAVSHLMRVASGLDSLVLGEPQILGQVKKAFADSQKGHLKASELERMFQKSFSVAKRVRTETDIGASAVSVAFAACTLARQIFESLSTVTVLLVGAGETIELVARHLREHKVKHMIIANRTRERAQVLADEVGAEVIALSDIDERLKDADIIISSTASPLPIIGKGMVERALKSRRNQPMLLVDIAVPRDVEPEVGKLANAYLYSVDDLQSIISHNLAQRKAAAVQAETIVEQESGEFMAWLRAQSASETIREYRGQAEQVRDDLTAKAMAALEQGGDPQVIMQDLAWKLTNRLIHAPTKSLQQAARNGDDERLTILRNSLGLE
|
Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
|
A4WBC7
|
P0A2U8
|
AMIE_STRPN
|
Oligopeptide transport ATP-binding protein AmiE
|
Streptococcus
|
MTKEKNVILTARDIVVEFDVRDKVLTAIRGVSLELVEGEVLALVGESGSGKSVLTKTFTGMLEENGRIAQGSIDYRGQDLTALSSHKDWEQIRGAKIATIFQDPMTSLDPIKTIGSQITEVIVKHQGKTAKEAKELAIDYMNKVGIPDADRRFNEYPFQYSGGMRQRIVIAIALACRPDVLICDEPTTALDVTIQAQIIDLLKSLQNEYHFTTIFITHDLGVVASIADKVAVMYAGEIVEYGTVEEVFYDPRHPYTWSLLSSLPQLADDKGDLYSIPGTPPSLYTDLKGDAFALRSDYAMQIDFEQKAPQFSVSETHWAKTWLLHEDAPKVEKPAVIANLHDKIREKMGFAHLAD
|
Part of the binding-protein-dependent transport system for oligopeptides. Probably responsible for energy coupling to the transport system.
|
P0A2U8
|
O81488
|
ALFL4_ARATH
|
PHD finger protein ALFIN-LIKE 4
|
Arabidopsis
|
MEAGGAYNPRTVEEVFRDFKGRRAGMIKALTTDVQEFFRLCDPEKENLCLYGHPNEHWEVNLPAEEVPPELPEPVLGINFARDGMAEKDWLSLVAVHSDAWLLAVAFFFGARFGFDKADRKRLFNMVNDLPTIFEVVAGTAKKQGKDKSSVSNNSSNRSKSSSKRGSESRAKFSKPEPKDDEEEEEEGVEEEDEDEQGETQCGACGESYAADEFWICCDLCEMWFHGKCVKITPARAEHIKQYKCPSCSNKRARS
|
Histone-binding component that specifically recognizes H3 tails trimethylated on 'Lys-4' (H3K4me3), which mark transcription start sites of virtually all active genes.
|
O81488
|
Q9KXS0
|
KGUA_STRCO
|
GMP kinase
|
Streptomyces albidoflavus group
|
MAATPRGTSPVPPDARPRLTVLSGPSGVGKSTVVAHMRKEHPEVWLSVSATTRRPRPGEQHGVHYFFVSDEEMDKLIANGELLEWAEFAGNRYGTPRTAVLERLEAGEPVLLEIDLQGARQVRESMPEARLVFLAPPSWDELVRRLTGRGTEPPEVIERRLAAAKVELAAEPEFDQTLVNTSVEDVARELLALTNVV
|
Essential for recycling GMP and indirectly, cGMP.
|
Q9KXS0
|
B1YIU9
|
TMCAL_EXIS2
|
tRNA(Met) cytidine acetate ligase
|
Exiguobacterium
|
MRMTAIISEYNPFHNGHLYQAKIARQETGADLIVAIMSGTFTQRGEPAFTDKWTRAQAAVASGEIDLVLELPFYFAVQRADRFALGGVTIAETIGAESLSFGSECGQLEPFIEAAAENQEATPRYQELMQEGLARGLSSATAASHAFREMTTTLDLTTPNNTLGYYYARAASTITLHTTKRIGSGYHDLSTGDIMSATAIRAYHATHHSLIGLPELTAETLRNAVFASFEPYYPFIRHRLLTTPLDDLMQFNGIDSSLAPRLIEGARKNETFDNFMTAVKTRRYTRTSLQRVLIYLLTSSKSSEFENIAFDRIDYVRPLAFNDNGRLALREIKQRIPVISTFEKHPWLIKESHVTAAYAVPLARYDRLEEHRRFAHFAGSVSK
|
Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac-AMP) and then transfers the acetyl group to tRNA to form ac(4)C34.
|
B1YIU9
|
Q0SS95
|
TMCAL_CLOPS
|
tRNA(Met) cytidine acetate ligase
|
Clostridium
|
MNITGIITEYNPFHLGHELHLKNSKEITNCDGVICVMSGNFVQRGLPALTDKWTRTKMALEAGVDLVVELPTLFATSSAEFFAFGAVSLLNSLNVVNNICFGSECGDIDLIKKLSEIIVNEPPIFKEYLKDYLKEGLPFPKARSEALMKYLDYNNYKTDFSYLEKVLNSSNNILAIEYCKSLYKLQSTIKPFTIQRLGADYNDEELSKNEIASASAIRKSIYTSNIEESLDFMPEYSYNLLKNTSFSDLDKMFDLVKYAIVSNPNILKEIPEASEGIDNKIIQNIGKANSLDELINLCKSKRYSYTRLNRILCHILLNVNKDLLSLRKYSPNYVRILGFNNKGREILKEIKKNSEINIVNKLSKAKTDPLLEFDIKATNIYSFLNPSVKINSDYLISPIIFR
|
Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac-AMP) and then transfers the acetyl group to tRNA to form ac(4)C34.
|
Q0SS95
|
Q0TNR1
|
SP2AB_CLOP1
|
Stage II sporulation protein AB
|
Clostridium
|
MDNKMRLEFLAKSENEGFARVSVSAFIAQLDPTIEELTDIKTAVSEAVTNAIIHGYECDESKVVIIEASICEDEISITVEDNGIGIENLEEAREPLYTSKPELERSGMGFTVMETFMDSLEVYSEKDKGTKIIMKKKMNT
|
Binds to sigma F and blocks its ability to form an RNA polymerase holoenzyme (E-sigma F). Phosphorylates SpoIIAA on a serine residue. This phosphorylation may enable SpoIIAA to act as an anti-anti-sigma factor that counteracts SpoIIAB and thus releases sigma F from inhibition.
|
Q0TNR1
|
Q92BR6
|
SODM_LISIN
|
Superoxide dismutase [Mn]
|
Listeria
|
MTYELPKLPYTYDALEPNFDKETMELHYTKHHNTYVTKLNEAVSGHPELAEKPVEELVANLDSVPEDIRGAVRNHGGGHANHTLFWSILSPNGGGAPTGDLKSAIESEFGTFDDFKEKFNAAAAARFGSGWAWLVVNNGKLEIVSTANQDSPLSDGKTPVLGLDVWEHAYYLKFQNRRPEYIDTFWNVVNWDEANKRFDAAK
|
Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
|
Q92BR6
|
B3R6D5
|
PPNP_CUPTR
|
Xanthosine phosphorylase
|
Cupriavidus
|
MEVSQFDNVSVVKKANLYFDGKCVSHTVLFPDGTRKTLGVIFPASLTFNTGAAEIMEINAGTCRVRLAGSEDWQAYGAGQQFSVPGNSSFDIEVQETLDYVCHFE
|
Catalyzes the phosphorolysis of diverse nucleosides, yielding D-ribose 1-phosphate and the respective free bases. Can use uridine, adenosine, guanosine, cytidine, thymidine, inosine and xanthosine as substrates. Also catalyzes the reverse reactions.
|
B3R6D5
|
A8ILV4
|
CH601_AZOC5
|
Chaperonin-60 1
|
Azorhizobium
|
MAAKEVKFAGEAREKMLRGVDILANAVKVTLGPKGRNVVIEKSFGAPRITKDGVSVAKEIELEDKFENLGAQLVREVASKTNDLAGDGTTTATVLAQAIVKEGAKAVAAGMNPMDLKRGIDLATAAAVKDIQARAKKVSSSAEVAQVGTISANGDSSIGEMIAGAMQKVGNEGVITVEEAKTAETELEVVEGMQFDRGYLSPYFITNAEKMIADLEDPFLLIFEKKLSGLQPILPVLEAVVQSGKPLVIVAEDVEGEALATLVVNKLRGGLKVAAVKAPGFGDRRKAMLEDIAILTGGQVISEDLGIKLENVTLAQLGRAKKVILEKEKTTIVDGVGEKAEIEARVAQIKAQIEETSSDYDREKLQERLAKLAGGVAVIRVGGSTEVEVKEKKDRVDDALNATRAAVEEGIVPGGGVALLRAKKAVEALSSENPDIAAGIKIVLRALEAPIRQIAENSGVEGSIVVGKVLESEGNFGFNAQTEQYVDLVAEGVVDPAKVVRTALQDASSVASLLVTTEALIAELPKKDAGMPAMPGGGMGGMGGMDF
|
Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
|
A8ILV4
|
A6W2V3
|
RPIA_MARMS
|
Phosphoriboisomerase A
|
Marinomonas
|
MTQDELKQAVAKAAMAYIQPMLEADTIVGVGTGSTANLFIDELAKHKGLFDGTVASSEASAERLKKHGIPVYDLNSVDSIRVYVDGADESNDNLHLIKGGGAALTREKIVAACSDEFVCIADESKLVKVLGDFPLPVEIIPMARGHVARELVKLGGDPVYREGVVTDNGNHILDVYNLEILDPIALEKSIDGIVGVVTNGLFAKRSADVLLLATKEGIKTLKK
|
Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
|
A6W2V3
|
A5VVJ5
|
HUTI_BRUO2
|
Imidazolone-5-propionate hydrolase
|
Brucella
|
MTKNSSTVFTHARIATLEEKAANLGLIEEAALVVKDARIVYAGPENKLPGEYASFEKIDCGNRLITPGLIDCHTHLVHAGNRAHEFELRLQGATYEEVARAGGGIVSSVRNLRAASEDDLVRETLPRLDALIAEGVTTVEVKSGYGLDRDSEIKSLKAARRLGEERDVAIRTTFLGAHALPPEMNGDKAAYIDRVINDMLPAIAEQGLADAVDGFCEGIAFLPDEIARVFDAAKAHDIPVKLHADQLSNLHGAALAASYGALSADHLEYTDADGAAAMASAGTVAVLLPGAYYFIRETQKPPVEAFRAAGTKMALATDNNPGTSPLTSLLLTMNMGATLFRMTVEECIAGVTREAARALGILDQTGTLEIGKDADLAIWDIERPAELVYRIGFNPLWKRVFKGQI
|
Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is the third step in the universal histidine degradation pathway.
|
A5VVJ5
|
Q5RJA1
|
RFX6_DANRE
|
Regulatory factor X 6
|
Danio
|
MYVIHLAEADESNASISSEEDLGHLDYSKPFAAKQTQPKKSISQIIKDKKKQTQLTLQWLEDNYIVCEGVCLPRCILYAHYLDFCRKEKLDPACAATFGKTIRQKFPLLTTRRLGTRGHSKYHYYGIGIKESSAYYHSVYSGKGLTRFSGSKLKNEGGFTRKYSLSSKTGTLLPEFPSAQHLVLQDSVSKEKVDTLIMMYKTHCQCILDNAINVNFEEIQNFLLHFWQGMPEHLLPLLENPVIVDIFCVCDSILYKVLTDVLIPATMQDMPESLLADIRNFAKHWEHWMLSSLENLPEILSEKKVPIARRFVSSLKRQTSFLHLAQIARPALFDQIVVTSMVNDIDKVDLNSIGSQALLSVTNDQDSDFYSEYDSISVFQELKDLLRKNATVESFIEWLDSVVEQKVIKPSKQNGRSVKKRAQDFLLKWSFFGARVMHNLTLNNATSFGSFHLIRMLLDEYILLAIETQFNNDKEQDLQNLLEKYMRSADASKATFTASPSSCFLANRNKPGVSSSDSAVKDEIPPEDDYLTLAAAQQGLGAGTVVYHSADPDNFTIAGQMDFSQNSAPLMTPPISPAMMNRSSVINQGPMAMRPQTSCPIQGQLPCQTFPEPLYQSLHNPPSGSYPNASYYQPMFRTQTHTESGRYAFSGHHLSKDCFSNSCTASPYGTRGSSGGYTAAGDAGMETEAVQMLESSGFGFGGTTGAADGCSGPVCSSGHRYYGSSSGYVDAPRMGTFIDQHVSVISSVSSIRSVSAYAEAHDPLNILDDTSRKTRPYYTELSAMGTHTAGSSIAHSCSVSAPCMYGAPAPYHSQNTLLPLQGATEIREMMSSLPPINTVFMGSTSGPP
|
Transcription factor required to direct islet cell differentiation during endocrine pancreas development.
|
Q5RJA1
|
B3WA01
|
RL7_LACCB
|
50S ribosomal protein L7/L12
|
Lacticaseibacillus
|
MALDVDGIIAQLKDASILELNDLVKSIEDEFGVKAAAPVAAGAAAGADAAAAKDTYDVELTEAGQEKVKVIKAVREITGLGLKDAKGMVDAAPKVIKEGLSEDDANKLKEQLEGVGATVTLK
|
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation.
|
B3WA01
|
P13083
|
PAHO_CAVPO
|
Pancreatic icosapeptide-like
|
Cavia
|
MTATRCCLWLLLLGTCMALLLPEAWGAPLEPVYPGDDATPQQMAQYAAEMRRYINMLTRPRYGKSAEEDALGLPVWRQSHAAAPGGSHRHPPAGLPAAKGGTGVSGSPPKPWDCLPCRAHSLPSQS
|
Pancreatic hormone is synthesized in pancreatic islets of Langerhans and acts as a regulator of pancreatic and gastrointestinal functions.
|
P13083
|
P0CT53
|
EF1A1_SCHPO
|
Elongation factor 1-alpha-A
|
Schizosaccharomyces
|
MGKEKGHINVVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEATELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPKYNVTVIDAPGHRDFIKNMITGTSQADCAVLIIGGGTGEFEAGISKDGQTREHALLAYTLGVKQLIVAVNKMDTTGWSQARFEEIVKETSNFIKKVGFNPKTVPFVPVSGFQGDNMIEPTTNMPWYQGWQKETKAGVVKGKTLLEAIDSIEPPARPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMIVTFAPAGVTTEVKSVEMHHESLDAGLPGDNVGFNVKNVSVKDIRRGNVCGDSKNDPPMGCASFTAQVIILNHPGQISAGYSPVLDCHTAHIACKFAELIEKIDRRSGKKIEESPKFVKSGDACIAKMVPSKPMCVEAFTDYAPLGRFAVRDMRQTVAVGVIKAVEKVAPGAAKVTKAAVKAGAKK
|
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
|
P0CT53
|
Q3ANR3
|
RS18_CHLCH
|
30S ribosomal protein S18
|
Chlorobium
|
MKPRATSSHGYKAQGNKALNGALTSKKKVSKNQVVFFDYRDERKLKRFINDQGKIIPRRITGLSAKEQNLLTHSVKWARFLAVIPYVVDEYK
|
Binds as a heterodimer with protein S6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit.
|
Q3ANR3
|
Q8REA7
|
NADE_FUSNN
|
NH(3)-dependent NAD(+) synthetase
|
Fusobacterium
|
MNKLDLNLKEVHNELVEFLRENFKKAGFSKAVLGLSGGIDSALVAYLLRDALGKENVLAIMMPYKSSNPDSLNHAKLVVEDLKINSKTIEITDMIDAYFKNEKEATSLRMGNKMARERMSILFDYSSKENALVVGTSNKTEIYLGYSTQFGDAACALNPIGDLYKTNIWDLSRYLKIPNELIEKKPSADLWEGQTDEQEMGLTYKEADQVMYRLLEENKTVEEVLAEGFNKDLVDNIVRRMNRSEYKRRMPLIAKIKR
|
Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
|
Q8REA7
|
P28646
|
SSR1_RAT
|
SRIF-2
|
Rattus
|
MFPNGTAPSPTSSPSSSPGGCGEGVCSRGPGSGAADGMEEPGRNSSQNGTLSEGQGSAILISFIYSVVCLVGLCGNSMVIYVILRYAKMKTATNIYILNLAIADELLMLSVPFLVTSTLLRHWPFGALLCRLVLSVDAVNMFTSIYCLTVLSVDRYVAVVHPIKAARYRRPTVAKVVNLGVWVLSLLVILPIVVFSRTAANSDGTVACNMLMPEPAQRWLVGFVLYTFLMGFLLPVGAICLCYVLIIAKMRMVALKAGWQQRKRSERKITLMVMMVVMVFVICWMPFYVVQLVNVFAEQDDATVSQLSVILGYANSCANPILYGFLSDNFKRSFQRILCLSWMDNAAEEPVDYYATALKSRAYSVEDFQPENLESGGVFRNGTCASRISTL
|
Receptor for somatostatin with higher affinity for somatostatin-14 than -28. This receptor is coupled to phosphotyrosine phosphatase and Na(+)/H(+) exchanger via pertussis toxin insensitive G proteins.
|
P28646
|
Q0VML3
|
YIDD_ALCBS
|
Putative membrane protein insertion efficiency factor
|
Alcanivorax
|
MKSLLLGAIWLYQKVLSPWIGNQCRFYPTCSEYARQAVETHGSLRGSALAAKRLCKCHPWHPGGFDYVPGAVPGAEPDQEQHQCTPLCNHHSEDHSQ
|
Could be involved in insertion of integral membrane proteins into the membrane.
|
Q0VML3
|
Q9CEJ1
|
MRNC_LACLA
|
Mini-RNase III
|
Lactococcus
|
MNKQQAELLNGIALAYIGDAIYEVFVREYLLDKGLTKPAMLQKNATKFVSAKAQAKIISAMDEVDFLTEYELTYFKRGRNAHSKTTAKNTDVVTYRISTGFEAVVGILHLTQQKERLQEFWDFSLKTIEADLV
|
Involved in correct processing of both the 5' and 3' ends of 23S rRNA precursor. Processes 30S rRNA precursor transcript even in absence of ribonuclease 3 (Rnc); Rnc processes 30S rRNA into smaller rRNA precursors.
|
Q9CEJ1
|
Q501S4
|
CSKMT_DANRE
|
Methyltransferase-like protein 12, mitochondrial
|
Danio
|
MLLNRFLVPLRSLQKLTQARRWHQTSLINDLVVNMDKKAMWDRFYTENGSKGQFKNFEWFFGFPSVKDLVLPALQAMSCSHSGPLHILDMGCGTSALGPCIYSTSPCAVRVTCADISPVAVKLMEEHTKSTSTQPCNPSSALVFLELDCTQMTGHFKSRSLDLILDKGTTDALVRSKEGQVKAGQILRQSLQVLRPSGSFLQFSDEDPDARLIWLEREVQGAEVTADVGVQEIGELRGVSYFCYQISPRSRPHS
|
Protein-lysine methyltransferase that selectively trimethylates citrate synthase (CS) in mitochondria. Seems to conduct trimethylation in a highly distributive manner rather than in a processive manner, and thus introduces a single methyl group per binding event.
|
Q501S4
|
P93087
|
CALM_CAPAN
|
Calmodulin
|
Capsicum
|
MADQLTDDQISEFKEAFSLFDKDGDGCITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLNLMARKMKDTDSEEELKEAFRVFDKDQNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYDEFVKVMMAK
|
Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.
|
P93087
|
C0M749
|
RIMM_STRE4
|
Ribosome maturation factor RimM
|
Streptococcus
|
MEYFSVGKIVNTQGLQGEMRVLSVSDFTEERFQKGARLALFDDKDRFVQEVEIASHRKHKQFDIIKFKGMYHINAIEQFKGYSLKIAKENQGKLAEGEFYYHQIIGLEVYEKDQLVGEIKEILQPGANDVWVVKRQSKRDLLLPYIPSVVLCVDIEKHRVDVEIMEGLDDED
|
An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Probably interacts with S19. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
|
C0M749
|
I6X7F9
|
CDDTR_MYCTU
|
Transcriptional regulator Rv3488
|
Mycobacterium tuberculosis complex
|
MREFQRAAVRLHILHHAADNEVHGAWLTQELSRHGYRVSPGTLYPTLHRLEADGLLVSEQRVVDGRARRVYRATPAGRAALTEDRRALEELAREVLGGQSHTAGNGT
|
May have transcription regulation and metal-detoxifying functions through which it may enhance intracellular survival of mycobacteria. Binds to its own promoter region and to the Rv1999c promoter region. It displays strong affinity for cadmium ions, but can also bind zinc, manganese and nickel. Expression increases the intracellular survival of recombinant M. smegmatis in murine macrophage cell line and increases its tolerance to cadmium ions.
|
I6X7F9
|
Q978K9
|
TRUD_THEVO
|
tRNA-uridine isomerase D
|
Thermoplasma
|
MNKPENFEEAIEIKRDPEDFSVEEIADIEPDPNGKYTIIKARVRDWDTNRIAAEIARRLHMSRKRVTFAGTKDKRAVKLQYFCINSADVDVASLSGIKDFEVIESFKSSHYLTLGDLIANHFKIRFYGIDPEMFRERYVHIISKGGFPNFFGDQRFGSRRRNTHEIGKLIIKGEYEEAVKKYIYDEKYDKESYRKHFIDTLDYKTALERFPHSLSFERSLIGYYARNGTFKGAFDSLPKNLTIMFVHAYQSYLFNRILDERLKIYGLNAVLPGDIAFPVDAYFNPDKSKPIEVNSYNREKISKLVSSDKIRISLPIFGYKTWIDNSDFGDVEYGILKEEGISQDDFKNKDFAYLSSSGDRRIISAKPINFSLENNVVEFTLGKGIYATVFLSSIGRLKENVYSDSEAEL
|
Could be responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
|
Q978K9
|
Q54Y25
|
SDHF4_DICDI
|
Succinate dehydrogenase assembly factor 4, mitochondrial
|
Dictyostelium
|
MNNLISKFNKIIYLNATKQTNKINCSFYSTTINNNNNNNNNNNNNNISNKKAEMSKENQQLLQDLEEEFDEDEFKPYVNPITKEIGGPKGPEPTRYNDWERNGRVSDF
|
Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Binds to the flavoprotein subunit SdhA in its FAD-bound form, blocking the generation of excess reactive oxigen species (ROS) and facilitating its assembly with the iron-sulfur protein subunit SdhB into the SDH catalytic dimer.
|
Q54Y25
|
Q631P9
|
SYY2_BACCZ
|
Tyrosyl-tRNA synthetase 2
|
Bacillus cereus group
|
MNIIDELEWRGAVNQQTDEEGLRKLVEEKKISLYCGVDPTGDSMHIGHLIPFMMMKRFQLAGHHPVILIGGATGTIGDPSGRQSERQLQTLEVVQHNVDALTAQMKKLFDFGGNSEVKMVNNYDWTHEINIIEFLRDYGKNFSINSMLAKDIVASRLDTGISFTEFTYQILQAMDFHHLYKKEDVQLQIGGSDQWGNITSGLDLIRKLEGHEAKVFGLTIPLLLKSDGTKFGKSAGGAVWLDPEKTTPFEFYQFWVNTDDRDVVKYLKYFTFLTKERIDELAVKVETEPHKREAQKVLAEEMTKFVHGEEALLQAVKITAALFSGDIKSLTADEIEQGFKEMPTFQSSKETKNIVEWLVDLGIEPSRRQAREDINNGAISMNGEKVTDVGTDVTVENSFDGRFIIIRKGKKNYSLVKLG
|
Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
|
Q631P9
|
Q0HV11
|
AROA_SHESR
|
5-enolpyruvylshikimate-3-phosphate synthase
|
Shewanella
|
MKQLRLEPVVQVRGEINIPGSKSISNRALLLATLAKGTTTLTNLLDSDDIRHMLASLKQLGVGYRLSQNNTVCELTGLGGAISADTAQTLFLGNAGTAMRPLCAALTLGRGEFTLTGEPRMEERPIGDLVDALKQLGANIMYLKNEGFPPLTINATGLNGGDVEIAGDLSSQFLTALLMVAPLAKGSVNIHVKGELVSKPYIDITLALMAQFGVQVINHDYARFEILAGQQYVSPGKVLVEGDASSASYFLAAGAIKGGEVKVTGVGRLSIQGDVKFADVLEKMGADIEWGDDYIIARGAPLTAVDLDMNHIPDAAMTIATAALFAKGTTTIRNIYNWRIKETDRLAAMATELRKVGALVEEGHDYIQITPPAVLNTAEIDTYNDHRMAMCFSMMAFADCGITINDPDCTSKTFPDYFAQFASLKA
|
Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
|
Q0HV11
|
A1T884
|
RUVB_MYCVP
|
Holliday junction ATP-dependent DNA helicase RuvB
|
Mycolicibacterium
|
MGRFSEDSADEPDEREMSAALTVGEGDIDASLRPRSLGEFIGQPRVREQLQLVLEGAKNRGGTPDHILLSGPPGLGKTSLAMIIAAELGSSLRVTSGPALERAGDLAAMLSNLVEHDVLFIDEIHRIARPAEEMLYLAMEDFRVDVVVGKGPGATSIPLEVAPFTLVGATTRSGALTGPLRDRFGFTAHMDFYEPSELERVLARSAGILGIELGAEAGAEIARRSRGTPRIANRLLRRVRDYAEVRADGVITRDIAKYALEVYDVDELGLDRLDRAVLSALTRSFGGGPVGVSTLAVAVGEEATTVEEVCEPFLVRAGMIARTPRGRVATAQAWTHLGMKPPANAVGLGQTGLFD
|
The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing.
|
A1T884
|
P69004
|
ACT2_MESFR
|
Actin-15B
|
Mesocentrotus
|
MCDDDVAALVIDNGSGMVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNSPAMYVAIQAVLSLYASGRTTGIVFDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMQTAASSSSLEKSYELPDGQVITIGNERFRAPEALFQPAFLGMESAGIHETCYNSIMKCDVDIRKDLYANTVLSGGSTMFPGIADRMQKEITALAPPTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF
|
Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
|
P69004
|
P35756
|
IR31_HAEIF
|
Iron-regulated 31 kDa protein
|
Haemophilus
|
KFKVVTTFTVIQDIAQNVAGDAAT
|
May be involved in iron uptake.
|
P35756
|
Q6ENH1
|
NDHJ_ORYNI
|
NADH-plastoquinone oxidoreductase subunit J
|
Oryza
|
MQQGWLSNWLVKHEVVHRSLGFDHRGIETLQIKAEDWDSIAVILYVYGYNYLRSQCAYDVAPGGSLASVYHLTRIQYGIDNPEEVCIKVFAQKDNPRIPSVFWIWRSSDFQERESFDMVGISYDNHPRLKRILMPESWIGWPLRKDYITPNFYEIQDAH
|
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
|
Q6ENH1
|
Q9LN20
|
P4H3_ARATH
| null |
Arabidopsis
|
MAKLRHSRFQARKWSTLMLVLFMLFMLTIVLLMLLAFGVFSLPINNDESSPIDLSYFRRAATERSEGLGKRGDQWTEVLSWEPRAFVYHNFLSKEECEYLISLAKPHMVKSTVVDSETGKSKDSRVRTSSGTFLRRGRDKIIKTIEKRIADYTFIPADHGEGLQVLHYEAGQKYEPHYDYFVDEFNTKNGGQRMATMLMYLSDVEEGGETVFPAANMNFSSVPWYNELSECGKKGLSVKPRMGDALLFWSMRPDATLDPTSLHGGCPVIRGNKWSSTKWMHVGEYKI
|
Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in proline-rich peptide sequences of plant glycoproteins and other proteins. Hydroxyprolines are important constituent of many plant cell wall glycoproteins such as extensins, hydroxyproline-rich glycoproteins, lectins and arabinogalactan proteins.
|
Q9LN20
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.