Datasets:
jonghyunlee
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UniProt_function_text_descriptions

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2.44k
sequence
stringlengths
2
35.2k
function
stringlengths
7
11k
Q9ZPV7
RER1D_ARATH
Protein RER1D (AtRER1D)
MEDEPGSENEADTIVASPLAKWRIEFSKSFQNYLDRSAPNIVRRWLVTLVAAVIYIYRVYSVYGYFVISYGLATYILNLLIGFLSPKVDPELEALDPDSLPVDESDEYKPFVRRLPEFKFWYAATKAFVVAFVMTFFSFLDVPVFWPILLCYWLVLYSLTMKRLIVHMFKYRYFPFDVRKPVKLLKFLVNSVLTFLRLKKGDGGDDRPSSSNSSQGNEKQD
Involved in the retrieval of endoplasmic reticulum membrane proteins from the early Golgi compartment.
Q9ZPW9
NLTP8_ARATH
Non-specific lipid-transfer protein 8 (LTP 8)
MNVLKCLAIISVLGIFFIPRYSESAISCSVVLQDLQPCVSYLTSGSGNPPETCCDGVKSLAAATTTSADKKAACQCIKSVANSVTVKPELAQALASNCGASLPVDASPTVDCTTVG
Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues (By similarity).
Q9ZPZ1
GAUT2_ARATH
Putative galacturonosyltransferase 2 (EC 2.4.1.-) (Like glycosyl transferase 2)
MTDACCLKGNEDKMVPRFGHGTWIGKAFNDTPEMLHERSLRQEKRLERANELMNDDSLQKLETAAMARSRSVDSAPLGNYTIWKNEYRRGKSFEDMLRLMQDQIIMARVYSGLAKFTNNLALHQEIETQLMKLAWEEESTDIDQEQRVLDSIRDMGQILARAHEQLYECKLVTNKLRAMLQTVEDELENEQTYITFLTQLASKALPDAIHCLTMRLNLEYHLLPLPMRNFPRRENLENPKLYHYALFSDNVLAASVVVNSTVMNAQDPSRHVFHLVTDKLNFGAMSMWFLLNPPGEATIHVQRFEDFTWLNSSYSPVLSQLESAAMKKFYFKTARSESVESGSENLKYRYPKYMSMLNHLRFYIPRIFPKLEKILFVDDDVVVQKDLTPLWSIDLKGKVNENFDPKFCGWAYGMNIFDLKEWKKNNITETYHFWQNLNENRTLWKLGTLPPGLITFYNLTQPLQRKWHLLGLGYDKGIDVKKIERSAVIHYNGHMKPWTEMGISKYQPYWTKYTNFDHPYIFTCRLFE
May be involved in pectin and/or xylans biosynthesis in cell walls.
Q9ZQ91
CXE7_ARATH
Probable carboxylesterase 7 (AtCXE7) (EC 3.1.1.1)
MDSVIAFDRSPMFRVYKSGRIERLLGETTVPPSLTPQNGVVSKDIIHSPEKNLSLRIYLPEKVTVKKLPILIYFHGGGFIIETAFSPPYHTFLTSAVAAANCLAISVNYRRAPEFPVPIPYEDSWDSLKWVLTHITGTGPETWINKHGDFGKVFLAGDSAGGNISHHLTMRAKKEKLCDSLISGIILIHPYFWSKTPIDEFEVRDVGKTKGVEGSWRVASPNSKQGVDDPWLNVVGSDPSGLGCGRVLVMVAGDDLFVRQGWCYAEKLKKSGWEGEVEVMETKNEGHVFHLKNPNSDNARQVVKKLEEFINK
Carboxylesterase acting on esters with varying acyl chain length.
Q9ZQE6
CML30_ARATH
Calmodulin-like protein 30
MSNVSFLELQYKLSKNKMLRKPSRMFSRDRQSSGLSSPGPGGFSQPSVNEMRRVFSRFDLDKDGKISQTEYKVVLRALGQERAIEDVPKIFKAVDLDGDGFIDFREFIDAYKRSGGIRSSDIRNSFWTFDLNGDGKISAEEVMSVLWKLGERCSLEDCNRMVRAVDADGDGLVNMEEFIKMMSSNNV
Potential calcium sensor.
Q9ZQH1
CML48_ARATH
Probable calcium-binding protein CML48 (Calmodulin-like protein 48)
MSYSNAYAPSAPELPESFVQQQHDGESRYTYAYPSYQPTQQFSSYSGMFSPETHPEIVRSFESADRNRSGFLEESELRQALSLSGYDGISNRTIRLLLFIYKIPVDSLLRLGPKEYVELWNCLAQWRAIFNRYDRDRSGKMNSTQLRDAFYNLGCVLPTSVHQLIVSQFDDGTGKTVDLCFDSFLECGMIVKGLTEKFRENDPGYTGYATLSYDVFMLMVIPFIATYD
Potential calcium sensor.
Q9ZQR5
TBL13_ARATH
Protein trichome birefringence-like 13
MATTSHNKPSLFPLLSLLCFISIFLLLSLSKRASLSSPKTHRSATVFPPKPDGSLSPLSATCDFSEGSWIYDPNPRSTRYTSSCKEIFKGWNCIRNNKTNGFEISNWRWKPKHCDLPSFDPLKFLQSHRNTNIGFVGDSLNRNMFVSLFCMLKSVTGELKKWRPAGADRGFTFSQYNLTIAYHRTNLLARYGRWSANAKGGELESLGFKEGYRVDVDIPDSSWAKASSFHDILILNTGHWWWAPSKFDPVKSPMLFFEGGRPILPPIPPATGLDRVLNNMVNFVEKTKRPGGIIFFRTQSPRHFEGGDWDQGGTCQRLQPLLPGKVEEFFSVGNNGTNVEVRLVNQHLYNSLKSRSAFHVLDITRMSEYRADAHPAAAGGKNHDDCMHWCLPGLTDTWNDLFVATLHTIKAL
May act as a bridging protein that binds pectin and other cell wall polysaccharides. Probably involved in maintaining esterification of pectins (By similarity). May be involved in the specific O-acetylation of cell wall polymers (By similarity).
Q9ZQV3
NAS6_HORVU
Probable nicotianamine synthase 6 (EC 2.5.1.43) (HvNAS6) (S-adenosyl-L-methionine:S-adenosyl-L-methionine:S-adenosyl-methionine 3-amino-3-carboxypropyltransferase 6)
MDAQNKEVDALVQKITGLHAAIAKLPSLSPSPDVDALFTDLVTACVPPSPVDVTKLGSEAQEMREGLIRLCSEAEGKLEAHYSDMLAAFDNPLDHLGMFPYYSNYINLSKLEYELLARYVPGGIARPAVAFIGSGPLPFSSYVLAARHLPDAMFDNYDLCSAANDRASKLFRADKDVGARMSFHTADVADLTRELAAYDVVFLAALVGMAAEDKAKVIPHLGAHMADGAALVVRSAQARGFLYPIVDPQDIGRGGFEVLAVCHPDDDVVNSVIIAHKSKDVHANERPNGRGGQYRGAVPVVSPPCRFGEMVADVTHKREEFTNAEVAF
Synthesizes nicotianamine, a polyamine that is the first intermediate in the synthesis of the phytosiderophores of the mugineic acid type found in gramineae which serves as a sensor for the physiological iron status within the plant, and/or might be involved in the transport of iron.
Q9ZQV6
NAS4_HORVU
Probable nicotianamine synthase 4 (EC 2.5.1.43) (HvNAS4) (S-adenosyl-L-methionine:S-adenosyl-L-methionine:S-adenosyl-methionine 3-amino-3-carboxypropyltransferase 4)
MDGQSEEVDALVQKITGLHAAIAKLPSLSPSPDVDALFTDLVTACVPPSPVDVTKLAPEAQAMREGLIRLCSEAEGKLEAHYSDMLAAFDNPLDHLGVFPYYSNYINLSKLEYELLARYVPGRHRPARVAFIGSGPLPFSSYVLAARHLPDTVFDNYDLCGAANDRATRLFRADKDVGARMSFHTADVADLTDELATYDVVFLAALVGMAAEDKAKVIAHLGAHMADGAALVARHGARGFLYPIVDPQDIGRGGFEVLAVCHPDDDVVNSVIIAQKSNDVHEYGLGSGRGGRYARGTVVPVVSPPCRFGEMVADVTQKREEFANAEVAF
Synthesizes nicotianamine, a polyamine that is the first intermediate in the synthesis of the phytosiderophores of the mugineic acid type found in gramineae which serves as a sensor for the physiological iron status within the plant, and/or might be involved in the transport of iron.
Q9ZQV7
NAS2_HORVU
Probable nicotianamine synthase 2 (EC 2.5.1.43) (HvNAS2) (S-adenosyl-L-methionine:S-adenosyl-L-methionine:S-adenosyl-methionine 3-amino-3-carboxypropyltransferase 2)
MAAQNNQEVDALVEKITGLHAAIAKLPSLSPSPDVDALFTELVTACVPPSPVDVTKLGPEAQEMREGLIRLCSEAEGKLEAHYSDMLAAFDKPLDHLGMFPYYNNYINLSKLEYELLARYVPGGYRPARVAFIGSGPLPFSSFVLAARHLPDTMFDNYDLCGAANDRASKLFRADRDVGARMSFHTADVADLAGELAKYDVVFLAALVGMAAEDKAKVIAHLGAHMADGAALVVRSAHGARGFLYPIVDPQDIGRGGFEVLAVCHPDDDVVNSVIIAQKSKDVHADGLGSGRGAGGQYARGTVPVVSPPCRFGEMVADVTQNHKRDEFANAEVAF
Synthesizes nicotianamine, a polyamine that is the first intermediate in the synthesis of the phytosiderophores of the mugineic acid type found in gramineae which serves as a sensor for the physiological iron status within the plant, and/or might be involved in the transport of iron.
Q9ZQV8
NAS3_HORVU
Probable nicotianamine synthase 3 (EC 2.5.1.43) (HvNAS3) (S-adenosyl-L-methionine:S-adenosyl-L-methionine:S-adenosyl-methionine 3-amino-3-carboxypropyltransferase 3)
MAAQNNNKDVAALVEKITGLHAAIAKLPSLSPSPDVDALFTELVTACVPPSPVDVTKLGPEAQEMREGLIRLCSEAEGKLEAHYSDMLAAFDNPLDHLGIFPYYSNYINLSKLEYELLARYVRRHRPARVAFIGSGPLPFSSFVLAARHLPDTMFDNYDLCGAANDRASKLFRADTDVGARMSFHTADVADLASELAKYDVVFLAALVGMAAEDKAKVIAHLGAHMADGAALVVRSAHGARGFLYPIVDPQDIGRGGFEVLAVCHPDDDVVNSVIIAQKSKEVHADGLGSARGAGRQYARGTVPVVSPPCRFGEMVADVTQNHKRDEFANAEVAF
Synthesizes nicotianamine, a polyamine that is the first intermediate in the synthesis of the phytosiderophores of the mugineic acid type found in gramineae which serves as a sensor for the physiological iron status within the plant, and/or might be involved in the transport of iron.
Q9ZQX0
ALB1_GLYSO
Albumin-1 (A1) [Cleaved into: Albumin-1 chain b (A1b) (Leginsulin); Albumin-1 chain a (A1a)]
MAVFLLATSTIMFPTKIEAADCNGACSPFEVPPCRSSDCRCVPIGLFVGFCIHPTGLSSVAKMVDEHPNLCQSDDECMKKGSGNFCARYPNNYIDYGWCFDSDSEALKGFLAMPRATTK
A1b binds to basic 7S globulin (BG) and stimulates its phosphorylation activity.
Q9ZQX8
NET1C_ARATH
Protein NETWORKED 1C
MEIAAKSNSKRMYSWWWDSHNTPKNSKWLQDNLADMDSNVKQMIKVLEEDADSFARRAEMYYRKRPELMKLVEEFYRAYRALAERYNHATGVIHKAHETIAEAFPNQVPLIFGDESHGGALTNDVDPQTPDMPPPFRARGNPDEFQQDALGFSLSHVHDVKRNIDFSEEPLFVSNGKARKGLNFNDHGDGKGRNGLKDHILSESERASKAEAEVVALKDSLSKMQAEKQASLALFEKNLERLSNLESEVSRAQADSRGINDRAASAEAEIQTLRETLYKLESEKESSFLQYHKCLQKIADLEDGLSVAHKEAGERASKAETETLALKRSLAKAETDKETALIQYRQCLNTISNLEERLRKAEEDARLINERAEKAGVEVENLKQTVSKLIKDKEASELQFQQCLNIIASLKVKLHHAQEETQSLSHEIEDGVAKLKFSEEKCLLLERSNQNLHSELDSLLEKLGNQSQKLTEKQTELVKLWSCVQAEHLHFQEAETAFQTLQQLHSQSQEELNNLAVELQTVSQIMKDMEMRNNELHEELEQAKVENKGLNDLNFTMEKLVQKNLMLEKSISYLNSELESFRRKLKTFEEACQSLSEEKSCLISENQHNVIENTVLIEWLRQLRLEAVGIATEKTDLEGKAKTIGDKLTDAETENLQLKRNLLSIRSEKHHLEDEITNVKDQLHEKEKEFEEIKMEKEKLIQEVFKERKQVELWESQAATFFCDKQISVVHETLIEATTRELAEACKNLESKSASRDADIEKLKRSQTIVLLNESIKSLEDYVFTHRESAGEVSKGADLMDEFLKLEGMCLRIKAIAEAIMEKEKFLMLENTNTYSMLEASLKQIKELKTGGGRSMRKQDGGSGRMRKQSHETEMVMKDIVLDQTSDGSSYEIVSKKGNSELDHLGFVELKPVKTHKTETKALSEESLIVEKVEIFDGFMDPNREVNKRRVLERLDSDLQKLENLQITVEDLKSKVETVEKEKTKVGENEYKTIKGQLEEGEEAIEKLFTVNRKLTTKAESEKDIDRRRRIFEHARRGTEKIGRLQSEIQRIQFLLMKLEGEREHRLRSKISDTKVLLRDYIYGRTRSVSMKKRTKKRSVFCGCVQQPESP
Plant-specific actin binding protein. May be part of a membrane-cytoskeletal adapter complex.
Q9ZR02
CML6_ARATH
Calmodulin-like protein 6
MDSTELNRVFQMFDKDGDGKITTKELNESFKNLGIIIPEDELTQIIQKIDVNGDGCVDIEEFGELYKTIMVEDEDEVGEEDMKEAFNVFDRNGDGFITVDELKAVLSSLGLKQGKTLEECRKMIMQVDVDGDGRVNYMEFRQMMKKGRFFSSLS
Potential calcium sensor.
Q9ZR41
GLRX_SOLLC
Glutaredoxin
MSLAKAKEIVSGNPVAVFSKTYCPFCVSVKDLLSKLGATFKAVELDSEKDGSEIQAALAEWTGQRTVPNVFIGRKHIGGCDATTALHREGKLLPLLTEAGAIAKTSTA
Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins (By similarity).
Q9ZRA3
DAD1_PEA
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1 (Oligosaccharyl transferase subunit DAD1) (Defender against cell death 1) (DAD-1) (Peadad)
MAKTSSTTKDAQDLFHAIWSAYSATPTNLKIIDLYVVFAVFTALLQDVYMALVGPFPFNSFLSGVLSCVGTAVLAVCLRIQVNKENKEFKDLGPERAFADFVLCNLVLHLVIMNFLG
Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Q9ZRF1
MTDH_FRAAN
Probable mannitol dehydrogenase (EC 1.1.1.255) (NAD-dependent mannitol dehydrogenase)
MAIEQEHRKKASGWAARDSSGVLSPFNFYRRETGEKDVTFKVLYCGICHSDLHMVKNEWGFSTYPLVPGHEIVGEVTEVGSKVQKFKVGDRVGVGCIVGSCRSCENCTDHLENYCPKQILTYGAKYYDGSTTYGGYSDIMVADEHFIVRIPDNLPLDGAAPLLCAGITTYSPLRYFGLDKPGMHVGVVGLGGLGHVAVKFAKAMGVKVTVISTSPKKEEEALKHLGADSFLVSRDQDQMQAAIGTMDGIIDTVSAQHPLLPLIGLLNSHGKLVMVGAPEKPLELPVFPLLMGRKMVAGSGIGGMKETQEMIDFAARHNITADIEVIPIDYLNTAMERLVKADVRYRFVIDIGNTLKVRS
Oxidizes mannitol to mannose. Provides the initial step by which translocated mannitol is committed to central metabolism and, by regulating mannitol pool size, is important in regulating salt tolerance at the cellular level (By similarity).
Q9ZRU9
LSM4_FAGSY
Probable U6 snRNA-associated Sm-like protein LSm4 (Glycine-rich protein 2)
MLPLSLLKTAQGHPMLVELKSGETYNGHLVNCDTWMNIHLREVICTSKDGDRFWRMPDCYIRGNTIKYLRVPDEVIDKVQEETKSRADRKPPGVGRGRGRGREEGSGARQVRGAGRDVMMQVAKAWVEVRGRGASAGKSGGRGGRGRG
Binds specifically to the 3'-terminal U-tract of U6 snRNA.
Q9ZRX0
TCTP_PSEMZ
Translationally-controlled tumor protein homolog (TCTP)
MIVYQDLLSGDELLSDSFPYKELYNGVLWEVEGKWVVQGAVDVDIGANPSAEGGDEEGVKIRLVKVVDIVDTFRLQEQPPFDKKQFLGFIKRYIKNLATKLSEERQAEFKKNVEGAAKMLVSKLSDLQFFVGESMHDDGSMVFAYYKDGATDPTFLYFADGLKEVKC
Involved in calcium binding and microtubule stabilization.
Q9ZS88
DER22_ARATH
Derlin-2.2 (AtDerlin2-2)
MAQAVEEWYKQMPIITRSYLTAAVITTVGCSLDIISPYNLYLNPTLVVKQYQYWRLVTNFLYFRKMDLDFMFHMFFLARYCKLLEENSFRGKTADFLYMLLFGASVLTGIVLIGGMIPYLSASFAKIIFLSNSLTFMMVYVWSKQNPYIHMSFLGLFTFTAAYLPWVLLGFSILVGASAWVDLLGMIAGHAYYFLAEVYPRMTNRRPLKTPSFLKALFADEPVVVARPEDVRFAAAPFDEIHQD
May be involved in the degradation process of specific misfolded endoplasmic reticulum (ER) luminal proteins.
Q9ZSR8
RSSA_BRANA
Small ribosomal subunit protein uS2 (40S ribosomal protein SA) (Laminin receptor-like protein) (p40)
MAANGSTQLSQKEADIKMMCAAEVHLGTKNCNYQMERYVFKRRNDGIYIFNLGKTWEKLMMAARVIVAIENPQDIIVQSARPYGQRAVLKFAQYTGANAIAGRHTPGTFTNQMQTSFSEPRLLILTDPRTDHQPIKEGALGNIPIIAFCDTDSPMRFVDIGIPANNKGKHSIGCLFWLLARMVLQMRGTIRPAQKWDVMVDLFFYREPEETKPEDEDEVAPQAEFGLPAPEYGGGDQWTTAAIPDAAWPGEAQAPISAAPAAGSWNDSAAPAAAEGGWDAAVPPTTAVTNWE
Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. {ECO:0000255|HAMAP-Rule:MF_03015}.
Q9ZSW9
TCTP_HEVBR
Translationally-controlled tumor protein homolog (TCTP)
MLVYQDLLTGDELLSDSFPYKEIHNGILWEVEGKWVVQGAVDVDIGANPSAEGADEDEGVDDQAVKVVDIVDTFRLQEQPAFDKKQFVTYMKRFIKLLTPKLDEEKQESFKKNIEGATKFLLSKLSDLQFFVGESMHDDGSLVFAYYRGGATDPTFLYFAYALKEVKC
Involved in calcium binding and microtubule stabilization.
Q9ZTA3
AOP1C_ARATH
Probable 2-oxoglutarate-dependent dioxygenase AOP1 (EC 1.14.11.-)
MDSDFVPPSVSFQLPVIDFSDQNLKPGSSKWDEVTADVLKALEDYGCFEASFDKLSVELNRSVFEAMEDLFELPIPTKQRNVSSKPFHGYLCHNLYESLGINDANVLEKVNDFTQQLWPDHGNKSISETIHLFSEQLVELDLMVRRMIMESFGIENYIDEHLNSTYYLTRLMKYTSPPDDDDDDDEETKLGLRSHTDKNIITILHQYQVDGLEVKTKDDKWIKVKPSQDSVLVMVGDSLCALLNGRLHSPYHRVIMTGKKTRYSTGLFSIPKTGVIIDSPEELVDKEHPRIFKPFEYTDFLHFFQTEAGRIAQSALHAFAAF
Probable 2-oxoglutarate-dependent dioxygenase that may be involved in glucosinolates biosynthesis. May play a role in the production of aliphatic glucosinolates (By similarity).
Q9ZTN2
ERD2_PETHY
ER lumen protein-retaining receptor (HDEL receptor) (PGP169-12)
MNIFRLAGDMTHLASVLVLLLKIHTIKSCAGVSLKTQELYALVFVTRYLDIFTDFISLYNTTMKLVFLGSSLSIVWYMRHHKIVRRSYDKDQDTFRHLFLVLPCLLLALVINEKFTFKEVMWTFSIYLEAVAILPQLVLLQRTRNIDNLTGQYIFLLGAYRSFYILNWVYRYFTEPHFVHWITWIAGLIQTLLYADFFYYYFQSWKNNTKLELPA
Required for the retention of luminal endoplasmic reticulum proteins. Determines the specificity of the luminal ER protein retention system. Also required for normal vesicular traffic through the Golgi. This receptor recognizes H-D-E-L (By similarity).
Q9ZTX0
SCAM_PEA
Secretory carrier-associated membrane protein (Secretory carrier membrane protein)
MAGRYDPNPFDEEQVNPFSNPRSAASATNSRPAPLNPDRADYNYGFGPTVDIPLDTSTDGKKKERDLQAKEAELRKREQEVRRKEEAIARAGIVIEEKNWPPFFPIIHHDITNEIPIHLRTLQYVAFFSLLGLVLCLTWNVVSVTAAWIKGEGVKIWFLAIIYFIAGVPGAYALWYRPLYRAFRTDSAIKFGWFFMFYLLHIGFCILAAVAPPIVFKGKSLTGILSAIDVVGDYTLVGIFYFIGFGFFCLETLISIWVIQQVYMHFRGGGKTAEMKREAALGAMGAALR
Probably involved in membrane trafficking.
Q9ZUA3
MP703_ARATH
Microtubule-associated protein 70-3 (AtMAP70-3) (70 kDa microtubule-associated protein 3)
MEEGGYAFEVNNGRPTASEFGTTARISSPSLTMSSSFREGGGGGGSKGLTRRRSMKPSFDADNEFITLLHGSDPVKVELNRLENDVRDKDRELSESQAEIKALRLSERQREKAVEELTEELGKMSEKLKLTENLLDSKNLEIKKINEEKRASMAAQFAAEATLRRVHAAQKDDDMPPIEAILAPLEAELKLARHEIVKLQDDNRALDRLTKSKEAALLDAERTVQSALAKASMVDDLQNKNQELMKQIEICQEENRILDKLHRQKVAEVEKFTQTVRELEEAVLAGGTAANAVRDYQRKFQEMNEERRILDRELARAKVSASRVATVVANEWKDGSDKVMPVKQWLEERRFLQGEMQQLRDKLAIADRAAKSEAQLKEKFQLRLRVLEESLRGPSSSGNRSTPEGRSMSNGPSRRQSLGGADIIPKLTSNGFFSKRSPSSQFRSLNASTSTILKHAKGTSRSFDGGSRSLDRSKVLTNEPRSKFPLNQSSEGTSGGGSPNSTKQGDSEKAAGTNNDSVPGVLHDLLQKEVITLRKAANDKDQSLRDKDEAIEMLAKKVETLTKAMEVEAKKMRREVAAMEKEVSAMRVDNKGSDSRTRRHSTNSKGASTTAQLLSGRGSGRMGMTRSTQ
Plant-specific protein that interact with microtubules.
Q9ZUB8
SKI22_ARATH
F-box protein SKIP22 (SKP1-interacting partner 22)
MKLRLRHHETRETLKLELADADTLHDLRRRINPTVPSSVHLSLNRKDELITPSPEDTLRSLGLISGDLIYFSLEAGESSNWKLRDSETVASQSESNQTSVHDSIGFAEVDVVPDQAKSNPNTSVEDPEGDISGMEGPEPMDVEQLDMELAAAGSKRLSEPFFLKNILLEKSGDTSELTTLALSVHAVMLESGFVLLNHGSDKFNFSKELLTVSLRYTLPELIKSKDTNTIESVSVKFQNLGPVVVVYGTVGGSSGRVHMNLDKRRFVPVIDLVMDTSTSDEEGSSSIYREVFMFWRMVKDRLVIPLLIGICDKAGLEPPPCLMRLPTELKLKILELLPGVSIGNMACVCTEMRYLASDNDLWKQKCLEEVNNFVVTEAGDSVNWKARFATFWRQKQLAAASDTFWRQNQLGRRNISTGRSGIRFPRIIGDPPFTWFNGDRMHGSIGIHPGQSARGLGRRTWGQLFTPRCNLGGLN
Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins.
Q9ZUH1
Y2424_ARATH
BTB/POZ domain-containing protein At2g24240
MGISKDRIKFNVGGRLFETTATTLANAGRDSFFGALFDDEWNLSPLEDSILFVDRNSDCFAVLLDLLRTGDLNVPANIPERLLHREASFYGLLDHVRTAKWGPFDGNRLRLSDSVKGIAPGDGTAIRAGPDGGCCVAHGSVVHVFDWMLEEHSPINLDYQRVNDVGWIDSDNIVLSACEKLGRGDGGMGLFSSSSGDLRYKFQVCHENQVKSYTAGALSFSPDYEIFASCKGRSNEYGIGVWDQITGKQTDFFYESPGWSLGDADKLQWLNGKNCLLVATLFPRKDNCYISLLDFRDKNMVWSWSDIGSPMAIDEKRVRDAIAMEDSNSICVVNEFEDLGFIDLRMYGGSVRWSSRSKLMKSKMPDEPCYPKLALHEGQLFSSMNDSISVFCGPDWVLTSRLRRSYGGSICDFSIGGDRLFALHSEENVFDVWETPPCPII
May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Q9ZUK6
NLTP7_ARATH
Non-specific lipid-transfer protein 7 (LTP 7)
MAGLMKLGCLVFVFVIAAGPITAKAALSCGEVNSNLKPCTGYLTNGGITSPGPQCCNGVRKLNGMVLTTLDRRQACRCIKNAARNVGPGLNADRAAGIPRRCGIKIPYSTQIRFNTKCNTYIC
Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues (By similarity).
Q9ZUN5
TET2_ARATH
Tetraspanin-2
MALANNLTAILNLLALLCSIPITASGIWLASKPDNECVNLLRWPVVVLGVLILVVSATGFIGAYKYKETLLAVYLCCMAILIGLLLVVLIFAFVVTRPDGSYRVPGRGYKEYRLEGFSNWLKENVVDSKNWGRLRACLADTNVCPKLNQEFITADQFFSSSKITPLQSGCCKPPTACGYNFVNPTLWLNPTNMAADADCYLWSNDQSQLCYNCNSCKAGLLGNLRKEWRKANLILIITVVVLIWVYVIACSAFRNAQTEDLFRKYKQGWV
May be involved in the regulation of cell differentiation.
Q9ZV27
SMR10_ARATH
Cyclin-dependent protein kinase inhibitor SMR10 (Protein SIAMESE-RELATED 10)
MGFSDAGIYLSDPNNLCQTELGFFHEPSLGFSDQSDPQNEFHITPPIYQELQDQDLEPKSQETNNCSRKEGATVKKEEEEEDDYCKTPTRSDQILSAMPRICPPAPRKPKRVPSRSLKVRNSYRSKRMIILNVSREIDCLFNPTSLCNKIKKARYI
Probable cyclin-dependent protein kinase (CDK) inhibitor that functions as a repressor of mitosis in the endoreduplication cell cycle.
Q9ZV71
B3GT3_ARATH
Probable beta-1,3-galactosyltransferase 3 (EC 2.4.1.-)
MSTKIKGELFPSRSLVSKKWTFLLCFGSFCFGILFTDRMWIIPESKDMPRPSVSTEAERLKLISEGCDPKTLYQKEVNRDPQALFGEVSKTHNAIQTLDKTISSLEMELAAARSAQESLVNGAPISNDMEKKQLPGKRRYLMVVGINTAFSSRKRRDSVRTTWMPSGEKRKKLEEEKGIIIRFVIGHSATAGGILDRSIEAEDKKHGDFLRLDHVEGYLELSGKTKTYFSTAVSKWDAEFYVKVDDDVHVNIATLGETLVRHRKKHRVYLGCMKSGPVLSQKGVRYHEPEYWKFGENGNKYFRHATGQLYAISRDLASYISLNQHVLHKYANEDVTLGAWFIGLDVTHIDDRRLCCGTPPDCEWKAQAGNICVASFDWTCSGICRSADRIKEVHKRCGEPENAIWKARF
Beta-1,3-galactosyltransferase that transfers galactose from UDP-galactose to substrates with a terminal glycosyl residue.
Q9ZV89
TBL42_ARATH
Protein trichome birefringence-like 42
MNFHQVLFLLLLIFLVDLSDYGVLADKTNDGYKNATKCNIYQGRWIYDNSSNPLYGTSTCPFIGLDCQKFGRPDKNYLHYRWQPTGCDIPRFNGRDFLTRFKGKKILFVGDSLSNNMWVSLSCMLHAAVPNAKYTFQLNKGLSTFTIPEYGISVNFLKNGFLVDLVSDKTRGLILKLDSISRGNQWLGSDVAIFNTFHWWSHTGRAKTWDYFQTGDKIVKEMNRMEAFKIALTTWSKWIDHNIDPSKTRVFYQGVSPVHLNGGEWGKPGKTCLGETVPVQGPSYPGRPNEGEAIVKSVIGRMAKPVELLDVTAMTEMRKDGHPSIYAGGGDRLNDCSHWCLPGVPDAWNQLLYTALLSH
May act as a bridging protein that binds pectin and other cell wall polysaccharides. Probably involved in maintaining esterification of pectins (By similarity). May be involved in the specific O-acetylation of cell wall polymers (By similarity).
Q9ZVQ6
P2B10_ARATH
F-box protein PP2-B10 (Protein PHLOEM PROTEIN 2-LIKE B10) (AtPP2-B10)
MGRKRRVKSESSPFDSFPEDCISYIISFTNPRDACVAATVSKTFESTVKSDIIWEKFLPADYESLIPPSRVFSSKKELYFSLCNDPVLFDDDKKSVWLEKASGKRCLMLSAMNLSIIWGDNPQYWQWIPIPESRFEKVAKLRDVCWFEIRGRTNTRVLSPRTRYSAYIVFKGVDKCYGFQNVAIEAAVGVVGQEPSRRLICFSEAIRRGRRNVVKPKQREDGWMEIELGEFFNDGGIMDNDEIEMSALETKQLNRKCGLIIQGIEIRPAKIL
Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins.
Q9ZWB8
RIC8_ARATH
CRIB domain-containing protein RIC8 (ROP-interactive CRIB motif-containing protein 8) (Target of ROP protein RIC8)
MINLHNAENEKEAEMQIGTPTDVKHVAHIGWDGGSVNHNPPSWMKDFKVLGGYSPALIGNIKEDASCIFEDSTRSRDIPRLPKSSRERSSTLGGSPTKERSRRRGSSQYNGNPKVSRRSSKESSAIPQDGGFNKKSRRKKSKDCVDGGSRRSSRRVRGSQVESISDSSSTSDAGYLT
Functions as downstream effector of Rho-related GTP binding proteins of the 'Rho of Plants' (ROPs) family. Participates in the propagation of ROP GTPase signals in specific cellular responses (By similarity).
Q9ZWD1
PR1G1_ARATH
PRA1 family protein G1 (AtPRA1.G1)
MLAPGESVLIPAEEISLSAGDVISLSVHNLIASVSSYRPWWSEFLAFGSIDRPSSFSPAVSRVKLNLHHFAVNYVLLTAASITLFLIGDPMALVTVASFVAMWLLLYFYRDHPLVLYGRHISDRVIVFGLILGSLWALWFINSLQCLILGVVTSVLLCLVHAIIRNSDDLFVQEKDVVVPSNFLHWS
May be involved in both secretory and endocytic intracellular trafficking in the endosomal/prevacuolar compartments.
Q9ZWH8
NAS7_HORVU
Probable nicotianamine synthase 7 (EC 2.5.1.43) (HvNAS7) (S-adenosyl-L-methionine:S-adenosyl-L-methionine:S-adenosyl-methionine 3-amino-3-carboxypropyltransferase 7)
MDAQSKEVDALVQKITGLHAAIAKLPSLSPSPDVDALFTDLVTACVPPSPVDVTKLAPEAQAMREGLIRLCSEAEGKLEAHYSDMLAAFDNPLDHLGVFPYYSNYINLSKLEYELLARYVPGGIAPARVAFIGSGPLPFSSYVLAARHLPDTVFDNYVPVRAANDRATRLFRADKDVGARMSFHTADVADLTDELATYDVVFLAALVGMAAEDKGQGDPHLGAHMADGAALVRSAHGARGFLYPIVDPQDIGRGGFEVLAVCHPDDDVVNSVIIAQKSKDMFANGPRNGCGGRYARGTVPVVSPPCRFGEMVADVTQKREEFAKAEVAF
Synthesizes nicotianamine, a polyamine that is the first intermediate in the synthesis of the phytosiderophores of the mugineic acid type found in gramineae which serves as a sensor for the physiological iron status within the plant, and/or might be involved in the transport of iron.
Q9ZWI7
RER1C_ARATH
Protein RER1C (AtRER1C)
MESAATAVVPPAAAATTATATDDNLQSSDSSSPADAVNRLIHAFSQRQQHLLDKTVPHVLYRWIACLCVVLIYIVRVYFVEGFYIITYAIGIYLLNLIIAFLSPQEDPEASLTSGGSLPTRRSDEYRPFVRRLPEFKFWLSIIRAFIIGFMMTFFEVFDVPVFWPILLFYWVMLFFLTMRKQIQHMIKYRYVPFSFGKKQYGKKPAPTESSE
Involved in the retrieval of endoplasmic reticulum membrane proteins from the early Golgi compartment.
Q9ZWQ7
DAD1_CITUN
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1 (Oligosaccharyl transferase subunit DAD1) (CitDAD-1-1) (Defender against cell death 1) (DAD-1)
MARSTGKDAQALFHSLRSAYAATPTTLKIIDLYVGFAVFTALIQVVYMAIVGSFPFNSFLSGVLSCVGTAVLAVCLRIQVNKDNKEFKDLPPERAFADFVLCNLVLHLVIMNFLG
Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Q9ZXA5
TMP_BPPHC
Probable tape measure protein (TMP) (Gene product 43) (gp43)
MARPIQITIMGDADQLSETLDQASEEVSAFGEQAKGLALAAGGAIAVGIGAGIAEALEREAGNDVLAAQLGATPAEAKRLGEAAGEVYSAGYGESVADANEALKGLWQQGLVPAGATADDNGEHFEKAMDVATVLGDEVGPTSNAVGQMLKTGMAKNADEAFDILVRGAQEGANKSEDLLDTFNEYGVQFKGIGLDGKTAMGLLSQGLQGGARDADLVADSLKEFGLIVRAGGDEVNAAYKSMGLNGAEMTKAIAQGGPVAKDALDKTLDGLRKIKDPAERIATAVTLFGTQAEDMQDALLKLDPSSAVETLGKVDGAAKSAGETMHDNAATKIKAFTRGLQTGLVDFIGGTVLPILEKFKPALEGIGSTMATVGGFVSEHSTTFKVVAGIITAVLLPALIQWGVQSTINAGKAVVAWVTSSATAVIESTKQALAHAKVVAGWIASGVQAGLNAAKVVAGWVLMGAQSMIQGARMAAAWLLAMGPIPLIIAAIVGLVVLIVANWDKIWAYTKKVFQWLWDWVKKIFNWLEDLFLNFTGPGLLIKHWDKSRSATKNTFNNVKNFAKDALNAVVNFVKGLPGRILSAASSLLSAGKRIGGYVIDGIKNGLSKLGGFASSLASAVGRAAKGAINGVIDLLNWATPNKLGWGKLSIDLPDNPIPKIRAMGGPASGWTRVGERGPEDVFLPNGSTVRPNHALSGSGGVTVNVQTNADPFAIGREVAWALRTSPA
Serves as a base for tail tube protein polymerization and acts as a template for tail length determination.
Q9ZXB2
PORTL_BPPHC
Probable portal protein
MGFWSALFGRGHSPALDGIEARAWEPYDPSIYNLGAVAASGETVTPHDALQVSAVFASVRLLSETIATLPLSTYSKRGGSRKEIVTPEWLDYPNAEPGGMGRIDILSQTVLSLLLQGNAFLAVRWQGPNIVGLDVLDPTKIHVHMVMVDGLRRKVFEAYDIDADGNEVLLGWFTPRDVLHIPGMMLPGDFVGCSPISYARESIGLALAAQKYGSKFFANGAMPGAVVEVPGTMSEEGLARAREAWRAANSGVDNAHRVALLTEGAKFSKVAMSPDEAQFLQTRQFQVPEIARIFGVPPHLISDATNSTSWGSGLAEQNIAFTMFSLRPWLERIEAGFNRLLFAETADRFRFVKFNLDEIKRGAPKERMELWSLGLQNGIYSIDEVRAAEDMTPLPDGLGEKYRVPLNLGEVGEEPEPEPAPAPPAIEPPAEEPDEEPEPEGKPDDEGATEEDDEDDA
Forms the portal vertex of the capsid. This portal plays critical roles in head assembly, genome packaging, neck/tail attachment, and genome ejection. The portal protein multimerizes as a single ring-shaped homododecamer arranged around a central channel. Binds to the terminase subunits to form the packaging machine.
Q9ZXD8
VLYS_BPPH1
Probable holin (Lysis protein)
MWMNFESLQIARAYLFGEVKYLDLMLVLNIIDIITGVIKAWKFKELRSRSAWFGYVRKMLSFLVVIVANAIDTIMDLNGVLTFATVLFYIANEGLSITENLAQIGVKIPAVITDRLHVIESDNDQKTEKDDQAAG
Produces a lesion in the cytoplasmic membrane allowing the phage lysosyme to attack the peptidoglycan.
Q9ZXI0
CAPSH_BPAR1
Major capsid protein (Gene product 23) (Major head protein) (gp23) [Cleaved into: Mature major capsid protein (gp23*)]
MTIKTKAELLNKWKPLLEGEGLPEIANSKQAIIAKIFENQEKDFQTAPEYKDEKIAQAFGSFLTEAEIGGDHGYNATNIAAGQTSGAVTQIGPAVMGMVRRAIPNLIAFDICGVQPMNSPTGQVFALRAVYGKDPIASGAKEAFHPMYGPDAMFSGQGAAKKFAALKASDTLEVGTIYTHFFQDTGTVYLQATEVKQIDTSANDAAKLDAEIKKQMEAGVLVEIAEGMATSIAELQEGFNGSTDNPWNEMGFRIDKQVIEAKSRQLKAAYSIELAQDLRAVHGMDADAELSGILATEIMLEINREVVDWINYSAQVGKSGMTLTPGSKAGVFDFQDPIDIRGARWAGESFKALLFQIDKEAVEIARQTGRGEGNFIIASRNVVNVLASVDTGISYAAQGLATGFNTDTTKSVFAGVLGGKYRVYIDQYAKQDYFTVGYKGPNEMDAGIYYAPYVALTPLRGSDPKNFQPVMGFKTRYGIGINPFAESAAQAPASRIQSGMPSILNSLGKNAYFRRVYVKGI
Major capsid protein that self-associates to form hexamers, building most of the capsid in association with pentons made of the capsid vertex protein and one dodecamer of the portal protein. The major capsid protein self-associates to form 160 hexamers, building most of the T=13 laevo capsid. Folding of major capsid protein requires the assistance of two chaperones, the host chaperone groL acting with the phage encoded gp23-specific chaperone, gp31. The capsid also contains two nonessential outer capsid proteins, Hoc and Soc, which decorate the capsid surface. Through binding to adjacent gp23 subunits, Soc reinforces the capsid structure.
Q9ZXI1
SCAF_BPAR1
Capsid assembly scaffolding protein (Gene product 22) (gp22) (Head morphogenesis protein) (Major prohead-scaffolding core protein Gp22) (Scaffold protein) [Cleaved into: Internal peptide VII]
MLKEQLIAEAQKIDASVALDSIFESVNISPEAKETFGTVFEATVKQHAVKLAESHIAKIAEKAEEEVEKNKEEAEEKAEKKIAEQASKFLDHLAKEWLTENKLAVDKGIKAELFESMLGGLKELFVEHNVVVPEESVDVVAEMEEELQEHKEESARLFEELNKRDAYINYVQREVALSESTKDLTESQKEKVSALVEGIDYSDAFSSKLSAIVEMVKKSNKDESTITESINTPDTEEAGLNFVTEAVEDKSAQGAEDIVSVYAKVASRF
[Capsid assembly scaffolding protein]: Scaffolding protein involved in the icosahedric procapsid assembly. Coassembles with the capsid proteins to form the procapsid, in which the scaffolding protein is found within the external shell of icosahedrally arranged capsid protein subunits. In a subsequent step the scaffolding protein molecules are cleaved by the viral protease and released, except for the internal peptide VII.
Q9ZYM7
NU5M_RHISA
NADH-ubiquinone oxidoreductase chain 5 (EC 7.1.1.2) (NADH dehydrogenase subunit 5)
MFINWTMMLISFSIVFLYMFFMTFYFNIFFIFEYNLMSILSFEYKFYILLDWMSCMFSFTVLMISSMVLWYSHSYMSSDKNKTSFCWMVLMFILSMLLLVLMPNVFMLILGWDGLGLTSYCLVIFYQSSNSYNSGMMTIISNRVGDVMVIMMIIFAINFNSFELTSIKSFELIWGLLIIIAGLTKSAQIPFSAWLPAAMAAPTPVSALVHSSTLVTAGVYLLIRFDLLFNNNIFSAFLMKISLMTMIMSGMNAFFENDLKKIIAFSTLSQLSIMMLTLSLSLTNLSFFHLIVHAIFKSMLFLCAGFVIHNLMGNQDIRFLSDFFKFSPLILSCMMIGMFSLMGFPFIGGFYSKDVIMEFFFLKSNNMIEMNMFIVGIIFTFLYNFRLFYMLLLKGTLFNMMSKDSINIFMNYPIFNLTVYLLITSNLMSWLLLPEYTMIFLSFTQKLMLLFLVPFCTFMFMILLKFIKFFPYLKLNFLMTMWNLSELTSFIMLSNNKFLLKMSINDWTWLEMYGPLGIKSKIEHNYNFSMTKEINVITIAFSLTILMMIIVY
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Q9ZZ38
NU1M_TRIRU
NADH-ubiquinone oxidoreductase chain 1 (EC 7.1.1.2) (NADH dehydrogenase subunit 1)
MYTLISIIGKYISCLPALLIVAFLTISERKTMASMQRRLGQNIVGYYGLLQAFADALKLLLKEYVAPTQANIILLFLGPIITLIFSLLGYRVIPYGSGLFISDFNLGILYILAVSSLATYGILLAGWSANSKYAFLGSLRSTAQLISYELLLRFYILLVILFTGSLNLTTIIESQKVVYFILPLLPIFLIFFIGCIAETNRAPFDLAEAESELVSGFMTEHSAVIFMIFFFLAQYASIVLICILSSVLFLGGYLNILPLNTYNVCDFNSLFSDYLINGLSSLNLAIKTAFLIFVFIWVRASFPRIRFDQLMSVCWTILLPIIIAYVVLLPCIVIGLNSSILLI
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Q9ZZ43
NU6M_SQUAC
NADH-ubiquinone oxidoreductase chain 6 (EC 7.1.1.2) (NADH dehydrogenase subunit 6)
MVYFMFIMLVGLILGLMAVASNPSPYFAALGLVVAAGVGCGLLVGHGGSFLSLVLFLIYLGGMLVVFAYTAALAAEPYPETWGDWSVLLYVSVYLLGIFFVGKYFFKEWGGLGWVGVEEMSNLEMIRGDFGGVALLYANGGIMLVLGGWVLLLTLFVILELTRGLSYGTLRVV
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Q9ZZ47
NU3M_SQUAC
NADH-ubiquinone oxidoreductase chain 3 (EC 7.1.1.2) (NADH dehydrogenase subunit 3)
MNLIMSSVAATALISLILAFVAFWLPSLNPDNEKLSPYECGFDPLGSARLPFSLRFFLVAILFLLFDLEIALLLPLPWGNQLLTPSISLLWATSIIILLTLGLIYEWLQGGLEWAE
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Q9ZZ54
NU1M_SQUAC
NADH-ubiquinone oxidoreductase chain 1 (EC 7.1.1.2) (NADH dehydrogenase subunit 1)
MLQHILLYLINPLAYIVPILLATAFLTLVERKILGYMQFRKGPNIVGPYGLLQPIADGVKLFIKEPVRPSTSSPFLFLATPTLALTLALLMWMPLPLPHAIINLNLGLLFILAVSSLTVYTILGSGWASNSKYALMGALRAVAQTISYEVSLGLILLSMIIFTGGFTLHTFNLTQETVWLLVPGWPLAMMWYISTLAETNRAPFDLTEGESELVSGFNVEYAGGSFALFFLAEYTNILMMNTLSVILFMGSSYDPTMPQISTFYLMMKATLLTLIFLWIRASYPRFRYDQLMHLVWKNFLPLTLALILWHAALPIATASLPPLT
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Q9ZZM2
NU6M_SALSA
NADH-ubiquinone oxidoreductase chain 6 (EC 7.1.1.2) (NADH dehydrogenase subunit 6)
MTYIVSLFLLGLVLGLVAVASNPAPYFAALGLVVAAGVGCGVLVGYGGSFLSLVLFLIYLGGMLVVFAYSAALAAEPFPESWGDRSVLGYVVVYTVGVMLVAGWFWSGWYETSWVVVDEFKEFSVLRGDTSGVALMYSYGGGMLIVCAWVLLLTLFVVLELTRGLSRGALRAV
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Q9ZZX0
AI5B_YEAST
Intron-encoded DNA endonuclease aI5 beta (EC 3.1.-.-)
MLMLLMMILTNNKVFMETLYYYLMFNFQLMSPFGVPVPGPAPETKDIKNLYESIMNNYINILNKYTININKDNINKLKFLDNYTEEEKGYYLSGLFEGDGNIYTRCFSITFSLEDVLLANYLCTYFKIGHITAKYNFNKELTAVKWNIMKKKEQEVFMNYINGKLLTYKRYDQYFKYNFNNRLNIKLLKPKEFDLTLNPWLTGFNDADGYFYTGFQKHKNSQWLKFHLELSQKDSYILDIIKKYFKTGGILKRDYKSGATAYIYKAQSSKAMKPFIEYFNNYQPLSTRRYKQYLLLNIAYLLKLNKLHMLTNSLLMLKELMLLQSVKNMSLEMKNELNNRVKIIINKTHYNNIE
Mitochondrial DNA endonuclease involved in intron homing.
R1CW23
ALMA7_EMIHU
Dimethylsulfonioproprionate lyase 7 (DMSP lyase 7) (EC 4.4.1.3) (Dimethylpropiothetin dethiomethylase 7)
MAGKDRKTIEKNYPGAEVDEGGRFKPLPPADDDAKLLVCEYPSLGVIRLDYDYPPALGDIDHPGSFYYDVFYRVVPGLTFGMCQKGEMPDEIKQRFIDAIKWLDAQGVAGITSDCGFFMNFQDLARTVTDKPVFMSSLCQLPAVVCAYAAHEHIALFTANGESLKPMRDLIKKECGVDPEESRFIIVGCQDVPGFEAVANGDRVDVDSVMPHIVRLAKETVAKYADTAKPIRAILFECTELPPYSDAVRAATRLPVFDAITSCNSFLAALMDNPRFGVNNWHLSWDGSQTDYRYGDNLSADLKAKLVNAEHAENVAAAERKLAKDRQKPKPATGTGTAFDA
Mediates cleavage of dimethylsulfonioproprionate (DMSP) into dimethyl sulfide (DMS) and acrylate. DMS is the principal form by which sulfur is transported from oceans to the atmosphere and is a key component of the ocean sulfur cycle.
R1DS73
ALM2_EMIHU
Dimethylsulfonioproprionate lyase 2 (DMSP lyase 2) (EC 4.4.1.3) (Dimethylpropiothetin dethiomethylase 2)
MGSASSKTRKDKAKSSTIAACPTDTAAAKACPTRLDDGLAQVAMFAGLRQVTMGVLRIDYDYQTNLGDILDPRSFDFRLVSATVEGLTFKRAQEGEPLPCYVMSNLDGAVKKLIDAGADFIVGDCGFLVYWQVYVRDFAQQYAGGRACPVMLSSLVLSLPLLATIPVGGKIGILTASKGSLMKMQKKLASVIELQKEEARTRAVPAAVQPSGIEINFSDPRFKVVGLDTVNSFKTALADDSGVDDRRSIAIEIAKYCKQVACEDPAICAWLIECTEAGGFSWAIKLGTGLPVWDPVTIGRFLSLGFTSSLPSVALTLGETGQVALDPNETDVSKGRPTKAEHRFGPEFEEMLQ
Mediates cleavage of dimethylsulfonioproprionate (DMSP) into dimethyl sulfide (DMS) and acrylate. DMS is the principal form by which sulfur is transported from oceans to the atmosphere and is a key component of the ocean sulfur cycle.
R1ENF4
ALMA5_EMIHU
Dimethylsulfonioproprionate lyase 5 (DMSP lyase 5) (EC 4.4.1.3) (Dimethylpropiothetin dethiomethylase 5)
MPAQAVVGTNSYLFRTVHAEVKGLRYLDVRAGKELSVSQKKALKEAVKELDAEGVVAITGDCGSFVHYQTAVRRMTKTPAVLSPLLQAPLLATMYMKEETILVLTNDSSDYDQAALESNLVEIGLSQEDAARFVIQGLQHIEGFSTSEVADMSDERTWAMVDTSERLRLEIMSTIEAAKKANPSLRAILLESTLLPSFSDSMRQTRGVPVFDAITLADYLAAASTDNPRFGSNIDASVWSSAMERANVMDELSQRATPAIGILRIDYSYPPAPGDVDYPGSYYYRTVQEVAAGLTFEAAQEGRPLTAQQREAMEGAIRRLEAAKGVVGITGDCGFLMNYQVDARRMSHLPCFISAMMQCHMLAASFAADEEFLVLTANGKSLAPKFGEMLSLAHVTRPEDQARFHILGCEDVDGFDAVAKGEAVDVARVTPGIVALAKAAAARRPKVRAVLLECTELPPYADALRHALRIPVLDAITLVDFVHSASTDNPAFGVDFQKSSKVFV
Mediates cleavage of dimethylsulfonioproprionate (DMSP) into dimethyl sulfide (DMS) and acrylate. DMS is the principal form by which sulfur is transported from oceans to the atmosphere and is a key component of the ocean sulfur cycle.
R1ERP2
ALMA4_EMIHU
Dimethylsulfonioproprionate lyase 4 (DMSP lyase 4) (EC 4.4.1.3) (Dimethylpropiothetin dethiomethylase 4)
MGCTHSKEHSTANKPPAVGILRCHGARWMPAQAVVGTNSYLFRTVHAEVKGLRYLDVRAGKELSVSQKKALKEAVKELDAEGVVAITGDCGSFVHYQTAVRRMTKTPAVLSPLLQAPLLATMYMKEETILVLTNDSSDYDQAALESNLVEIGLSQEDAERFVIQGLQHIEGFSTSEVADMSDERTWAMVDTSERLRLEIMSTIEAAKKANPSLRAILLESTLLPSFSDSMRQTRGVPVFDAITLADYLAAASTDNPRFGSNIDASVWSSAMERANVMDELSQRATPAIGILRIDYSYPPAPGDVDYPGSYYYRTVQEVAAGLTFEAAQEGRPLTAQQREAMEGAIRRLEAAKGVVGITGDCGFLMNYQVDARRMSHLPCFISAMMQCHMLAASFAADEEFLVLTANGKSLAPKFGEMLSLAHVTRPEDQARFHILGCEDVDGFDAVAKGEAVDVARVTPGIVALAKAAAARRPKVRAVLLECTELPPYADALRHALRIPVLDAITLVDFVHSASTDNPAFGVDFQKSSKVFV
Mediates cleavage of dimethylsulfonioproprionate (DMSP) into dimethyl sulfide (DMS) and acrylate. DMS is the principal form by which sulfur is transported from oceans to the atmosphere and is a key component of the ocean sulfur cycle.
R1F493
ALMA6_EMIHU
Dimethylsulfonioproprionate lyase 6 (DMSP lyase 6) (EC 4.4.1.3) (Dimethylpropiothetin dethiomethylase 6)
MGCAGSTLRSGASFEDSRLAAIEDSRFHEVGHHAQFEDSRLAAIEDSRFHEVGHHAQFDEGGRFKQLPPANDDAKLLVADHPSLGVIRLDYDYPPALGDVDHPGSFYYDVFYRVVPGLTFELCQSGELPDDVKQRFIDAITWLDEQGVAGITGDCGFFMYFQALARSVTSKPVFMSSLCQLPAVVCAYAADEHIALFTANGESLKPMRELIKKECGVDPDDTRFVIVGCEDVPGFEAVANGDRVDVDSVLPHLVRLAEDTVAKHAGTAKPIRAILFECTELPPYSDAVRAATRLPVFDSITCCNSMLASLMDNPRFGVNNWHLSWDGAHTAHRFGDNVPPHLKGKLVNREHPENVARWNASLAERSSFSSAQQESIGRGSREL
Mediates cleavage of dimethylsulfonioproprionate (DMSP) into dimethyl sulfide (DMS) and acrylate. DMS is the principal form by which sulfur is transported from oceans to the atmosphere and is a key component of the ocean sulfur cycle.
R1F9H0
ALM1_EMIHU
Dimethylsulfonioproprionate lyase 1 (DMSP lyase 1) (EC 4.4.1.3) (Dimethylpropiothetin dethiomethylase 1)
MGNCTSHPHHEPQVHFDTVDGMATVKAFAGIRQVTMGVLRIDYEYQTNLGDILDPRSFDFRIISATAEGLTFAKAKAGDKLDATGKELLERAVRQLIDNGADFIVGDCGFLVYWQVMVRDYAQDYAQKKYGRKCPVMMSSLVLALPLLATIPSGGQIGILTASEKSLQAVQKKLPIVIEDQQKEDGGQRSRSVPAAEDPSGIMINFSDPRFKVVGLDEVKDFKHALDAQGADAVNDRRDIAVQIAAYCQKVQEKNPQIAAWLIECTEAGGFAWAIKVGTGLPVWDPITLGRFLSLGFTANVPNVALTLGQHGENPLDPSATTAGKGRCTGEEPGQIHALGAEFQAIREGTL
Mediates cleavage of dimethylsulfonioproprionate (DMSP) into dimethyl sulfide (DMS) and acrylate. DMS is the principal form by which sulfur is transported from oceans to the atmosphere and is a key component of the ocean sulfur cycle.
R1G6M4
ALMA3_EMIHU
Dimethylsulfonioproprionate lyase 3 (DMSP lyase 3) (EC 4.4.1.3) (Dimethylpropiothetin dethiomethylase 3)
MGCAGSTLRSGASFEDSRLAAIEDSRFHEVGHHAQFEDSRLAAIEDSRFHEVGHHAQFDEGGRFKQLPPANDDAKLLVADHPSLGVIRLDYDYPPALGDVDHPGSFYYDVFYRVVPGLTFELCQSGELPDDVKQRFIDAITWLDEQGVAGITGDCGFFMYFQALARSVTSKPVFMSSLCQLPAVVCAYAADEQIALFTANGESLKPMREIIKKECGVDPDDTRFVIVGCEDVPGFEAVANGDRVDVDSVVPHLVRLAEDTVAKHAGTAKPIRAILFECTELPPYSDAVRAATRLPVFDSITCCNSMLASLMDNPRFGVNNWHLSWDGAHTAHRFGDNVPPHLKGKLVNREHPENIARWNASLAERSSFSSAQQESIGRGSRKL
Mediates cleavage of dimethylsulfonioproprionate (DMSP) into dimethyl sulfide (DMS) and acrylate. DMS is the principal form by which sulfur is transported from oceans to the atmosphere and is a key component of the ocean sulfur cycle.
R4GUQ1
KA292_LYCMC
Potassium channel toxin alpha-KTx 29.2 (Neurotoxin KTx3) (Toxin LmKTx71)
MKSVCGVLIILVVLTTMLSISTFSTVGAEADCPISEAIKCVEKCKEKVEVCEPGVCKCSG
Weakly inhibits the Kv1.3/KCNA3 channel (1 uM of thetoxin inhibits currents by 13.2%) and Kv7.1/KCNQ1 channel (10 uM of the toxin inhibits currents by 27.7%).
R4LHX8
FLA_ACTS9
Fluorinase (EC 2.5.1.63)
MPANGNPIIAFMSDLGTTDDSVAQCKGLMLSICPGVTIVDVNHSMTPWDVEEGARYIVDLPRFFPEGTVFATTTYPATGTATRSVALRIKQAAQGGARGQWAGSGAGFERAEGSYIYIAPNNGLLTTVIEEHGYIEAYEVSNTKVIPAEPEPTFYSREMVAIPSAHLAAGFPLNEVGRALSDDEIVRFAKPKPSTVSGGVLSGVITNIDHPFGNLWTNIHRTDLEKAGIGYQTQLRLLLDGVLTFDLPLVPTFADAGQIGDPVIYINSRGYLALARNAAPLAYPYNLKAGLTVTVTKA
Catalyzes the formation of a C-F bond by combining S-adenosyl-L-methionine (SAM) and fluoride to generate 5'-fluoro-5'-deoxyadenosine (5'-FDA) and L-methionine.
R8NBR0
Y5631_BACCX
Probable CBASS effector molecule IK1_05631
MLEKQNSEENIELLRAMRYCYNKSKIFYAVRISISILIPILSISIYLFNRGSTGTSNTGVWFSVIGSIWLLIAYQIEKLEGGYIEKGAKIQEKFDINLFNIRWNNVLVGNQISPEDIRDFSSKFKGDEEKLKNWYGGLSSKHFYVNVILAQRSNLMWAISLKRNFSILLFTVSVLYLFLTIAFGFFVNMSMQEYIIKILLPSMSILIYGFKTSDELKKQSNKLEALGNSIISKFDTGNLSEINASACREYQDAIFVYNRIRSILIPEWLYWLRQQKDDEKMIQINIRLTKKSNLF
CBASS (cyclic oligonucleotide-based antiphage signaling system) provides immunity against bacteriophage. The CD-NTase protein synthesizes cyclic nucleotides in response to infection these serve as specific second messenger signals. The signals activate a diverse range of effectors, leading to bacterial cell death and thus abortive phage infection. A type I-B CBASS system. Protects B.subtilis against phage infection. When IK1_05630 and IK1_05631 are introduced in B.subtilis BEST7003 there is 1000-fold protection against phage SBSphiC. Both genes are required for protection. Activation leads to bacterial cell lysis and death, which occurs before the phage has finished its replication cycle, thus protecting non-infected bacteria by aborting the phage infection and preventing its propagation.
R9RZK8
MYG_BALMY
Myoglobin
MVLSDGEWQLVLNIWAKVEADVAGHGQDVLIRLFKGHPETLEKFDKFKHLKTEAEMKASEDLKKHGNTVLTALGGILKKKGHHEAELKPLAQSHATKHKIPIKYLEFISDAIIHVLHSRHPGDFGADAQGAMNKALELFRKDIAAKYKELGFQG
Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
S0AU91
FSDG_FUSHE
MFS transporter fsdG (Fusaridione A biosynthesis protein G)
MKGNEFRNQTQTTIKNELAEWSDNSNNSQVDYASNAPSGDHVLVDWDGPNDPKNPKNWPHSAFLIHTILVSMLCLAGNLATTMYAPGAAQLAVEFKTRDTTTIALTVSIYLLGFALAPMVTSPLSEVYGRLIVYHTSNIFFLGFNLACAFSSNIGMFIAFRFLAGCAGSAPMTVGGGTIADFAASPEKNNTALRLFALGPLLGPVIGPIVGGFVAENIGWRWTFRIMSIVIAVLSILSCIFLRETSAAAILGRRGARITKETGKPFMIPGPMPGMPPKPQQPTKEIVSRSLVRPMKMLIFLPQVLILSFYTAFVFGLIYLLFTTFPAVFEGQYGFSPGVSGLSYIGIGFGMVGALFLFNFINMKMSNRTDKHGQLIPESYLPLMTWFSPLLPIGFFWYGWSADKQTHWVVPILGTFFVGFGSFAIIMPTTAYLVYAQGPQGAASVLAASNMMRYVFAAFLPLAGQNMYDQLGLGWGNSLLGFLCVVLAPVPAIFQRYGHYLRERFPTEF
Efflux pump that might be required for efficient secretion of fusaridione A or other secondary metabolies produced by the fusaridione A gene cluster.
S0DRT4
EQXR_GIBF5
Trichosetin biosynthesis cluster transcription factor TF22
MSTRNSQSIRSSCDRCRSHKLKCTVSPEDSRSGPHKCTRCIRAQVTCVFGPRSQSKRTPNGKNKPEKPKPELEPPQKTSPPVCSSSLAGMDLGSPGAWTPWIDDLASQETEEPLPIDVNTAGDGSGPSDGDFWADLGMTQELNMLELAPTNTYQAQYLASFDYVAPPVAEVGHLMDISEPSEHTPPHAIVQLSTLVTKIHETSKALEESPWSNVPDAKQLQNYPIGRVLSLSQDFCSILGCIWGKVSISSDGQSSGSGSSPTPSADMLDYAEVLSSIKITQDPTASSSMAASVDMPTALLVLSCYTSLIKLYSLVFAHFENHLSHLPEIPSPYPSQAALASHRWGLQLGELPSADETCTKICTAVQVLLDAFQSVEDVFGLPRSFSAVRQRTCDMEGMDFSAELGRTSLWTDYMVHFVVRSNAIRADTEECEEMRELSTKVRSLKALIREKMNL
Transcription factor that regulates the expression of the gene cluster that mediates the biosynthesis of trichosetin, a trans-fused decalin-containing tetramic acid with antimicrobial activity. Directly activates expression of only the three biosynthetic genes PKS-NRPS1, DA and ER, while TF23 and MFS-T are induced by the final product trichosetin and not by TF22.
S0DRX0
FUB2_GIBF5
Fusaric acid biosynthesis protein 2
MATELKEYLVIIPDLPDVLAKRQVLLKPHNQDAAPLVKAGRVPFFGSTLAHHSAEGQQVAENGTVMIIKAESEEEIKEIIRKDIFTIEGVWDFGKLSIWPFKSK
Part of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties. L-aspartate is suggested as fusaric acid amino acid precursor that is activated and further processed to O-acetyl-L-homoserine by cluster enzymes aspartate kinase FUB3 and homoserine O-acetyltransferase FUB5, as well as enzymes of the primary metabolism. The polyketide synthase (PKS) FUB1 generates the triketide trans-2-hexenal which is presumptively released by the hydrolase FUB4 and linked to the NRPS-bound amino acid precursor by NAD(P)-dependent dehydrogenase FUB6. FUB1, FUB4, and the non-canonical NRPS Fub8 may form an enzyme complex. Further processing of the NRPS-bound intermediate might be carried out by FUB6 and the sulfhydrylase FUB7, enabling a spontaneous electrocyclization to close the carbon backbone of fusaric acid. Dihydrofusaric acid is likely to be released via reduction by the thioester reductase (TR) domain of FUB8 whereupon the final oxidation to fusaric acid may (also) be performed by the FMN-dependent dehydrogenase FUB9.
S0DRY0
FUB10_GIBF5
Fusaric acid cluster transcription factor FUB10 (Fusaric acid biosynthesis protein 10)
MAGDFSNRAPWKRSACDRCRAQKLRCHRDSGHSTDACLRCLKSGIECVTSKARPTGRPPSRQVQPTVVVEQGDTSSSSHTTDSSPSAGGTDMSNMMNFEYDLSLDNILDSIGMQHSDFIVNDNILVDISPLSSSQSTSQHSVAQAQAQTVDPSTIQSTASYQFNTLPSTSSMDSALPMRSDHVELLLSRLHSKLSAQLYSIRSSPWDVKGTLNLSLAHQGIGQDFENCESHPLVQVSQACTELERLLSGLRAPASAEHTPSTFSYTPAVPPRLRITQLLIALSCYIQIVSIYGIIFSKVFDYLLSTSKTSVGSYQSSPLTLYIGGLPIPPNETLSGNLLVHLIEHQLHQIEQLMGLPEHYRVSSRAKDTKDGELGLFGSQHSQSLLNAAIQLGEDRDGNHDDIRCVRALKIVMRQIKDF
Transcription factor that regulates the expression of the gene cluster that mediates the biosynthesis of fusaric acid, a mycotoxin with low to moderate toxicity to animals and humans, but with high phytotoxic properties.
S0DZI6
BIK4_GIBF5
Nitrogen metabolite regulation-like protein bik4 (Bikaverin biosynthesis protein 4)
MPSPHFSKVLVFGATGEVGSAVALEAHALGAHVSIALRDTTKHNEWISPSQEHAADLQRISADLTDPDSLKRAVHDTGAQAAFIYAVRSKDTLRGAITALRDAGIQYLVFLSTSQVRTAGTTKGDIRSIKPDHFIPWQHAQVEIALEELEVPHAAVRAGFFASNPLRIYLDRSSEPKQVNLLAPEVPHDPIDPKDIGRAAAAVLVNPRLYASGYQGEPKKDVVYLSGPALLSQTEQWEIINRELVAAGKPEVKVNHITVEQYLENLAKLHVPDVVAKSLAKSMVETRALYAPEDYEKSRGNVELLTGRKATAFDEFVKREIPRYFD
Nitrogen metabolite regulation-like protein involved in the regulation of the gene cluster that mediates the biosynthesis of bikaverin, a red pigment also considered as a mycotoxin.
S0E3H0
WOR1_GIBF5
Global transcription regulator sge1
MAGTMPLRPTYVGFVRDTTDALLIFEACLSGTLSHVPRRPHDRERQDLIKSGNIFVYEEHASGIKRWTDSISWSPSRILGNYLLYRELEKPFPPGEKKRARGRNGKSTTQSGGISKARQRNTVPFPQGLEHGNEYPSVPSDDERHLVGSLVDSYDFKEQGLVKKTISITYQGVPHHLVSYYNVEDVKAGLLSGPSDDPRLRGVVPRTELMNGQNFRAPVEEAMGGSYMPSMVASIGYPTLQHQSQMHQSQMHQPQMHQPQMHQSQMHQSQMHQPQMHQPQAHQPQVHQPQVHPPQVHQPQAHQPQYQSQTLHPTHGYQQTYAGQPNAPSSTWW
Global transcriptional regulator that acts as an activator of secondary metabolism. Required for expression of a yet uncharacterized secondary metabolism gene cluster containing a non-canonical non-ribosomal peptide synthetase. Not required for conidiogenesis nor for pathogenicity, but is involved in vegetative growth.
S0EBQ6
FUJ5_GIBF5
Fujikurins biosynthesis cluster transcription factor FFUJ_12243
MSHRQSCDRCRQQKVRCLRDESQGGAGNKARASFSRCERCTKASVDCVYSLKSRSNRPNAHQPIHNQVDADPQTLVGPSWFGQGLFCQAASGSLGPDYDDLAGQFADLDGAEFNGWDGNLDVIPSLSMSSLNTLAAPAAMVSQDISPTKDHHDNNHMQEPEADDDDESNNGHDQDAIQELSLQLTAISQRATRAKRRLHRAGCPPPTVSSPEVNEAFEDTNNLLRIANNITNACAHLCDEASSNSITLDYGLVFSALASHQHLLALFKAICHLIQRYLESMTSANQHRQQQQQRLHDGDIGPSSVAQFVMVLQLLTYLINRMDRNLAQVNGPHGHGLETSLGGQATPITPSTGYQDIVQSMLIHRGDKNNTTGSSQSLPIIGQVVLGAIPDEHKRLRQVIQELQTRIERSEIQ
Transcription factor that regulates the expression of the gene cluster that mediates the biosynthesis of fujikurins.
S0EBV2
FUJ3_GIBF5
Polyketide transferase FFUJ_12241 (EC 2.3.-.-) (Fujikurins biosynthesis cluster protein FFUJ_12241)
MSPVLPRHDIEFPTLDGITLRGWLYPATKRGPGMILSPGFNMPKDAIIPDICKWFQERDITCLAWDPRGIGASDGEPRNDIDPRQEAEHLHDAVTWLSKNPLVDVTKIALWGLCFGGNVTLAAAALEYVLNGSPFSSPPCFVVPSWADIDLTLSKRIAAMISVAPLIDSTGLPERRQPILELAMYDRAGRLEGDDPMYLPYVNEDGSVPNGLQLAADMMPALDRLGIPVENRVTVQTYYRALTWSVLNLVEYIAPTPAMMVTPEFDVSCPTKDQLKAYERMGEPKELDILKGKGHLDWIFGDVDIILNRQLDFLKRQMNF
Polyketide transferase part of the gene cluster that mediates the biosynthesis of fujikurins A-D, secondary metabolites playing a role during rice infection. The polyketide synthase PKS19 acts with the trans-enoyl reductase FFUJ_12240 and the polyketide transferase FFUJ_12241 to produce fujikurins, however, the biosynthesis pathway has not been identified yet.
S0ECK8
FUJ4_GIBF5
Fujikurins efflux protein FFUJ_12242
MATNVGGAVDNSRRSISDNRHDPEKPAELPDTLSGSETERPQDANPEAALDQQASDAAKAHDEGPPDGGTAAWMVVLGAWCCSFCSPGWINSMGSFQEYYQREPLKDYSSSEIAWIPSLEIFFLFGLGPIVGIIFDRYGPRPLIIGGTIFHVFGLMMASLAKTYYQFLLSQGVCSAIGVACLYSPALACISTWFLKRRGAAMGIMATGSSVGGVIFPIMITRMIERNGYPWALRTAAFLILGLQVIACLTVRPRQKPVPKKLPAGRLAAPFTEPAFALLLAGIFILTYGMYIPIDYLPLSGLQEAHMSVNMSQYLVAIMNAASLFGRLGAGYGADIIGRWNMFIIACGVTGISNLAVWIPATKSSITIGYAIMFGFASGAFVSLVGALPVSVSPIPELGYRMGIVFLVISIPALTMAPIGGAILQHASNGWVSLKVFAGVMCLVGSAIILGSRMLYTEKRLIKAF
Efflux pump that may be involved in the secretion of fujikurins.
S0EJ18
FUJ2_GIBF5
Trans-enoyl reductase FFUJ_12240 (EC 1.-.-.-) (Fujikurins biosynthesis cluster protein FFUJ_12240)
MQALVGAETGGYRLADNVEKPVLQPGSILCHVKAVALNPHDAKIVDYSNVPGALGGCDFAGVVVEIGNGVKRFKEGDRVFAVTFGMNASDKTAGAFTQYAVATEDLSCLIPEAMSFTEACSMGLAIATAGLALFQTPGLQLSMQGGNGEAVLVSGGATATGTMAIQFLRIAGYTPVVTCSPSNNALCESFGAEICFDYHSPTCGADIRVQTGNKLRHVLDCVVDISTMKMSYDAIGSSGGAYVALEAIPTNIKYTRRDICANWLMAPSILGTPVNKKGAYGRPSMPEHRQFGTYLFALAEKWLQDGSIKHHPIEIREGGLRSIREGIDDLRRGNVHAKKLVYPLSA
Trans-enoyl reductase part of the gene cluster that mediates the biosynthesis of fujikurins A-D, secondary metabolites playing a role during rice infection. The polyketide synthase PKS19 acts with the trans-enoyl reductase FFUJ_12240 and the polyketide transferase FFUJ_12241 to produce fujikurins, however, the biosynthesis pathway has not been identified yet.
S0EX56
UBACT_CHTCT
Prokaryotic ubiquitin-like protein UBact
MSDLFRMEERRQMPILPTEPARKEGDGGGPQKPDVKRPDTSDLLRRMKRVDPDAARRYRQRSGE
May function as a protein modifier covalently attached to lysine residues of substrate proteins. This may serve to target the modified proteins for degradation by proteasomes.
S0F1M4
TO1A_HADVN
Omega-hexatoxin-Hvn1a
MNTATGVIALLVLATVIGCIEAETRADLQGAFESYEGEAAEKIFRRSPTCIPSGQPCPYNENCCSKSCTYKEMKTATPVQRCD
Inhibits insect, but not mammalian, voltage-gated calcium channels (Cav).
S0F1M6
TOK1G_ATRRO
Omega/kappa-hexatoxin-Ar1g
MNTATGFIVLLVLATVLGGIEAGESHMRKDAMGRVRRQYCVPVDQPCSLNTQPCCDDATCTQELNENDNTVYYCRA
Toxin that may inhibit ion channels.
S0F1N0
TO1E_HADIN
Omega-hexatoxin-Hi1e
MNTATGFIVLLVLATVIGCISADFQGGFEPYEGEDAERIFRRSPTCIPTGQPCPYNENCCSQSCTYKANENGNQVKGCD
Inhibits insect, but not mammalian, voltage-gated calcium channels (Cav).
S0F1N6
TO1D_HADIN
Omega-hexatoxin-Hi1d
MNTATGFIVLLVLATVIGCISADFQGGFEPYEEEDAERIFRRSPTCIPTGQPCPYNENCCNQSCTYKANENGNQVKRCD
Inhibits insect, but not mammalian, voltage-gated calcium channels (Cav).
S0F1N7
TO1B_HADVN
Omega-hexatoxin-Hvn1b
MNTATGVIALLVLATVIGCIEAEETRADLQGAFESYEGEAADKIFRRSPTCIPSGQPCPYNENCCSKSCTYKENENGNTVQRCD
Inhibits insect, but not mammalian, voltage-gated calcium channels (Cav).
S0F204
TO1F_HADIN
Omega-hexatoxin-Hi1f
MNTATGFIVLLVLATVIGCISADFQGGFEPYEEEDAERIFRRSPTCIPTGQPCPYNENCCSQSCTYKTNENGNQVKGCD
Inhibits insect, but not mammalian, voltage-gated calcium channels (Cav).
S0F207
TOK1G_HADVE
Omega/kappa-hexatoxin-Hv1g
MNTATGFIVLLVLATVLGGIEAGESHMRKDAMGRVRRQYCVPVDQPCSLNTQPCCDDATCTQELNENDNTVYYCRA
Toxin that may inhibit ion channels.
S0F209
TOK1H_HADVE
Omega/Kappa-hexatoxin-Hv1h
MNTATGFIVLLVLATILGGIEAGESHMRKDAMGRVRRQYCVPVDQPCSLNTQPCCDDATCTQERNENGHTVYYCRA
Toxin that may inhibit ion channels.
S0F215
TO1G_HADIN
Omega-hexatoxin-Hi1g
MNTATGFIVLLVLATVIGCISADFQGSFEPYEEEDAERIFRRSTCTPTDQPCPYDESCCSGSCTYKANENGNQVKRCD
Inhibits insect, but not mammalian, voltage-gated calcium channels (Cav).
S2DJ52
L2HDH_INDAL
L-2-hydroxyglutarate dehydrogenase (EC 1.1.99.2)
MDFQVIIIGGGIVGLATGLKIKQRNPNIKVALLEKEEEVAKHQTGNNSGVIHSGLYYKPGSLKAKNCIEGYHELVRFCEEENIPFELTGKVVVATRKEQVPLLNSLLERGLQNGLKGTRSITLDELKHFEPYCAGVAAIHVPQTGIVDYKLVAEKYAEKFQILGGQVFLGHKVIKVETQNTASIIHTSKGSFSTNLLINCAGLYSDKVAQMNQKESLDVKIIPFRGEYYKIKKEREYLVKNLIYPVPDPNFPFLGVHFTRMMKGGVEAGPNAVLAFKREGYKKSQVNFSELAETLSWPGFQKVASKYWKTGMGELFRSFSKKAFTDALKELIPDIQESDLIEGGAGVRAQACDRTGGLLDDFCIREDQNAIHVLNAPSPAATSSLSIGGTVCEWALKRF
Catalyzes the dehydrogenation of L-2-hydroxyglutarate (L2HG or(S)-2-hydroxyglutarate) to 2-oxoglutarate (alpha-ketoglutarate). Active in vitro with the artificial electron acceptor 2,6-dichlorophenolindophenol (DCPIP). Also displays a very low oxidase activity in vitro on L-2-hydroxyglutarate with O2 as the electron acceptor, but this activity is most likely not physiological.
S3D778
GLOK_GLAL2
ABC transporter gloK (Pneumocandin biosynthesis cluster protein K)
MPENTAIASIFTAIVCFKFIILTLEAKEKSNLIRPEFKHPSPEQAAGILNRSFFWWFNPLLLTGSKQRLAVDDLFFNDDGLTFDAWRDIITRRWAKADISKPHALLKVMLATFKGLLLAGILPRLCLTGPETTTSNKVAYGLIAAYAIVYIGIAVMSTMSQHKNYRTIVAIRGSAVSLIYQHTLRLTSSSTSTSSSLTLINNDVERMGHGMREVHEIWASLIEIALSLWLLEVRLGVSVVAAVFVIIGNICTLLGCVFGFVKMGLLLGDRQKVWLEAIEKRTSSTIATLGSIRGIKSTGATDIVQRITTRLRLDEIRISLKYRELLVGIVTLSYVSTTMAPVFAFATYSIISNSRGTTPLLAASAYTSLTIFSLLGQAVSKWISSSVDIITTIACLERVRQYLATNLRVDPRTIESYIKPIDSSNSPRLRNSDISQTEMLDMGSVDQSQYHPNSVGEVLREVPLAKMMITIRDCSACWSKGSEMAISEINLTILKGSLAMVIGPIGSGKSTLLKVILGEMPHTTGTVIVGRSEAAFCGQSPWLTNVSVRNNIIGVSYLDANWYNTVVNACALDRDFEQLPDGDNTVIGSKGVLLSGGQKSRLALARALYARNDLVILDDVFSGLDAKTEQRVFESVLGSHGILRQGGTTTVLATNSVRNISLADHIVVMGSDGKITDQGTYQNLVFASSYLESLGTRQKTLNISDSEKSKDDTVSGLAVASAMHQPVDSDNRGDKDLTIYKYYIDTVGWVTWWVFVLLCSGFVFGLVFPQIWIQFWTEANARQANYRLAYYLSLYALWPLMAIVIFLGACAWLMIRMVSKAAIQFHGILLNSALSAPLVYFSTTDSGEVSNRFTQDLNLIDMELPTALIGTTVTFLSCIAQIGVIIYGSSYVAAAIPALIVFLYYIQLFYLRTSRQLRLLELEAKAPLLSHFMESIHGLVTIRAFGWTEKFTHQNHDLLERSQRPFYLLYCAQRWLNLTLELAVAFLAIILVSIALTTRESSGAKIGVALLSIVGFGLNLKTLVYTWTSLEIAMGAVSRIRHFAINTSSEDLPGEDRTLPPDWPHEGVIRFQSVSAAYSPTSHPVLNDLSFTVKAGTKVAICGRTGSGKSSTLAALLRLIDLRSGAITIDGIDISTVVRQDLRSKLITLPQEPFYYHASIRDNLDVRGQFSTEELLDILEVVGMREVIDKKGGLDAMANADVLSHGQSQLLCLARAILRPNKILILDEATSSVDKKTEEKMVDIIREKFQDRTVISVAHNLNTIMDYDEVIVLEAGRIIEQGKPLALALEPSFFASLLKAADGESEDALEEETISNIASPRSR
3-isopropylmalate dehydratase large subunit part of the gene cluster that mediates the biosynthesis of pneumocandins, lipohexapeptides of the echinocandin family that prevent fungal cell wall formation by non-competitive inhibition of beta-1,3-glucan synthase. Possibly secretes antifungal pneumocandins, thus avoiding of intracellular accumulation and ameliorating the toxicity to the producing cells.
S3DQQ3
GLOB_GLAL2
Pneumocandin biosynthesis cluster protein B
MDLFQSPGGDLIQDEDSVEVIEMLCIDFRDRLLVALSTTCQSDFREAKKVVEERLRDILETASSLSSTEVTSSPNASPLYNTDAPEDVVPTVGLDVGLDEPMADYSQNTPSITGGTASAEYQNSGDTNQMTLEDPACVDMFAAESQNTGHIPDSCLRDWSFEGVSMKSPSLFDWSSRNSNFPLTQEHENQFAEFLTLFEGEPNFDNWLSTMTWSSLESHSSPINGHSAGATPQLDQMHTVSNSRVARSVVSESTVTNTGSANSLNSGLLANTPSSSHSSVFERACSSVQEPTPEPTPVRGLQRKLRKQGPRQTTEATPCDQQIGPRASRATSQLPERRSMKMVRKEARDTPLTTSPANSTQINIEANTIPSDLSVEYAFGCFSDAKEVFETFYKRLSDDRKHLSSLLMRLFYAVGSPDALRQLRDALDLSRKNSMIASYHDSNDLAATVSVLDQLDATTTLSHILRRYHLVRLLDHRSKLESNHKAAKLAVKGTKRRLKYDCERIELMRRGENADCDANTRSAKERLKYRSKTRALTDLMQTLYPDLSPDSEGITTAGGCEYTRKLTKLRNRLACARNWYQFEETFPGAILALIPCATGDLSISIDHVEKLPSDVLKIFLDYLKERRGVFLSKMSRILSKDLYDVLMRRNVTKRYKLEQTNENSLTDGLHDDDRLLELCETV
Part of the gene cluster that mediates the biosynthesis of pneumocandins, lipohexapeptides of the echinocandin family that prevent fungal cell wall formation by non-competitive inhibition of beta-1,3-glucan synthase. The 10,12-dimethylmyristoyl side chain is synthesized by the reducing polyketide synthase gloL/GLPKS4. The thioesterase gloN/GLHYD exclusively interacts with gloL/GLPKS4 to maintain turnover of the polyketide side chain. The 10R,12S-dimethylmyristic acid is then transferred to the first thiolation domain of the nonribosomal peptide synthetase gloA/GLNRPS4 by the acyl-AMP ligase gloD/GLligase, followed by its acylation to L-ornithine to trigger elongation of the cyclic hexapeptide. L-ornithine, 4R-hydroxyl-L-proline (generated from L-proline by the dioxygenase gloF/GLOXY2), 3S-hydroxyl-L-homotyrosine (generated by gloG/GLHtyB, gloH/GLHtyA, gloI/GLHtyC, gloJ/GLHtyD and hydroxylated at C-3 by the dioxygenase gloM/GLOXY1), 3R-hydroxyl-L-glutamine (generated from L-glutamine probably by the dioxygenase gloE/GLOXY3) and 3S-hydroxyl-L-proline (generated from L-proline by the dioxygenase gloF/GLOXY2 to yield pneumocandin B0), or 3S-hydroxyl-4S-methyl-L-proline (generated from L-leucine by the dioxygenase gloC/GLOXY4 to yield pneumocandin A0) are sequentially added to the growing chain. The last C domain of gloA/GLNRPS4 is proposed to be responsible for cyclization by condensation to form the peptide bond between L-ornithine and 3S-hydroxyl-4S-methyl-L-proline (for pneumocandin A0) or 3S-hydroxyl-L-proline (for pneumocandin B0). Finally, the subsequent C-4 hydroxylation of 3S-hydroxyl-L-homotyrosine and L-ornithine dihydroxylation at C-4 and C-5 are performed by the cytochrome P450 monooxygenases gloP/GLP450-1 and gloO/GLP450-2, respectively.
S4R3P1
HMN13_HUMAN
Humanin-like 13 (HN13) (MT-RNR2-like protein 13)
MDTQGFSCLLLLISEIDLSVKRRI
Plays a role as a neuroprotective and antiapoptotic factor.
S4R3Y5
HMN11_HUMAN
Humanin-like 11 (HN11) (MT-RNR2-like protein 11)
MATRGFSCLLLVISEIDLSVKRWV
Plays a role as a neuroprotective and antiapoptotic factor.
S4S2C7
MAST_VESAF
Mastoparan-AF (MP-AF)
MKNTILILFTAFIALLGFFGMSAEADPIADPIADPISGPNAEADPEAINLKAIAALAKKLFG
Antimicrobial and mast cell degranulating peptide. Has broad spectrum antibacterial activity against both Gram-positive and Gram-negative bacteria (S.aureus MIC=16-32 ug/ml, S.xylosus MIC=1.5 ug/ml, S.alactolyticus MIC=8 ug/ml, C.koseri MIC=4 ug/ml, E.coli MIC=4-32 ug/ml, K.pneumoniae MIC=32 ug/ml, P.aerugiosa MIC=96 ug/ml, S.choleraesuis MIC=16 ug/ml, S.typhimurium MIC=32 ug/ml, V.parahamelytics MIC=16 ug/ml). Is also active on multi-antibiotic resistant hemolytic E.coli O157:H7. Acts by affecting membrane permeability. On E.coli O157:H7, acts through multiple membrane disruption patterns, including large perforations (full opening) at apical ends (hollow tubes), vesicle budding, forming dents, and membrane corrugation and invagination leading to irregular pits or pores. Exerts 40% lower membrane permeabilization activities on E.coli O157:H7 than on the non-pathogen E.coli BL21. Shows little hemolytic activities on sheep, chicken and human erythrocytes, but with a higher activity on chicken erythrocytes. Its mast cell degranulation activity may be related to the activation of G-protein coupled receptors in mast cells as well as interaction with other proteins located in cell endosomal membranes in the mast cells (By similarity).
S4S3E3
CTCQ_KITAU
Flavin reductase (NADH) (EC 1.5.1.36)
MPPEPLSLPLDLAPGLVDGDTFLSIMGALPTGVTVVTTLGPDGEPYGLTCSAACSVSKAPPLLLVCINRDSRVLKALLERGEFAVNVLRGGGESTSARFAAPVDDRFRDVRWEPGSAGGVPVMSADVVAHAECRVAAALDAGDHTIVIGAVVAGGPRPEVPSPLMYWRRSYARWPVEEDPRTAALTLAAEG
Catalyzes the reduction of flavin by NADH. Subsequently, the reduced flavins is transferred to the tetracycline 7-halogenase CtcP.
S4S3F6
MAST_VESVF
Mastoparan-V (MP-V)
MKNTILILFTAFIALLGFFGMSAEALADPVADPLAGPNAEADPEAINWKGIAAMAKKLLG
Antimicrobial and mast cell degranulating peptide. Has broad spectrum antibacterial activity against both Gram-positive and Gram-negative bacteria (S.aureus MIC=32-64 ug/ml, S.xylosus MIC=3 ug/ml, S.alactolyticus MIC=16 ug/ml, C.koseri MIC=4 ug/ml, E.coli MIC=8 ug/ml, K.pneumoniae MIC=64 ug/ml, P.aerugiosa MIC=256 ug/ml, S.choleraesuis MIC=32 ug/ml, S.typhimurium MIC=32 ug/ml, V.parahamelytics MIC=32 ug/ml). Affects membrane permeability of E.coli. Shows hemolytic activities on sheep, chicken and human erythrocytes. Its mast cell degranulation activity may be related to the activation of G-protein coupled receptors in mast cells as well as interaction with other proteins located in cell endosomal membranes in the mast cells (By similarity).
S4S3G3
MAST_VESDU
Mastoparan-D (MP-D)
MKNTILILFTAFIALLGFFGMSAEALADPIADPVAGPNPEADPEAINLKAIAAFAKKLLG
Antimicrobial and mast cell degranulating peptide. Has broad spectrum antibacterial activity against both Gram-positive and Gram-negative bacteria (S.aureus MIC=24-32 ug/ml, S.xylosus MIC=2 ug/ml, S.alactolyticus MIC=16 ug/ml, C.koseri MIC=4 ug/ml, E.coli MIC=8 ug/ml, K.pneumoniae MIC=32 ug/ml, P.aerugiosa MIC=128 ug/ml, S.choleraesuis MIC=16 ug/ml, S.typhimurium MIC=32 ug/ml, V.parahamelytics MIC=32 ug/ml). Affects membrane permeability of E.coli. Shows hemolytic activities on sheep, chicken and human erythrocytes. Its mast cell degranulation activity may be related to the activation of G-protein coupled receptors in mast cells as well as interaction with other proteins located in cell endosomal membranes in the mast cells (By similarity).
S4TDL2
TE2_HUMLU
Acyl-coenzyme A thioesterase 2, chloroplastic (Acyl-CoA thioesterase 2) (HlTE2) (EC 3.1.2.-) (Acyl-CoA thioester hydrolase 2)
MDLSSSPNHPITVVSTFASPFEGPPSVGDSNSSARKPISLWPGMYHSPVTNALWEARCKIFERLLDPPKDAPPQSELLTKTPSQSRTTILYNFSTDYILREQYRDPWNEVRIGKLLEDLDALAGTISVKHCSDDDSTTRPLLLVTASVDKIVLKKPISVDIDLKIVGAVIWVGRSSIEIQLEVSQSTKEGSNAADDVALSANFIFVARDSKTAKAAPVNRLSPETEQEKLLFDEAEARSSMRKRKRGDQERREFENGEANRLQTLLAEGRIFCDMPALADRDSILLRDTRQENSLICQPQQRNIHGRIFGGFLLHRAFELAFSTAYAFAGLVPYFLEIDHVDFXRPVDVGDFLRLKSCVLYTELHNPDQPLINIEVVAHVTRPELRSSEVSNTFYFTFTVRPEAKATKNGYRIRNVVPATEEEARRILERMDAEACI
Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH.
S4TE15
TE3_HUMLU
Acyl-acyl carrier protein thioesterase TE3, chloroplastic (HlTE3) (EC 3.1.2.-) (Acyl-ACP thioesterase TE3) (Acyl-lipid thioesterase 3)
MLQTFSPSYKPLHLPISSLSLSSSSSSSASSVAFPVTRLLIPPRLRVLPNPRRRCSALPFDIRGGKGMSEFYEVELKVRDYELDQYGVVNNAVYASYCQHGRHELLESFGLSCDAVARNGDALALSELSLKFLAPLRSGDKFVVKVRLSGSSAARLYFDHLIFKLPNQEPILDAKGTAVWLDKNYRPVRIPPEVRSKLVQFLRNEES
Acyl-ACP thioesterase involved in the production of fatty acids and beta-keto fatty acids (By similarity). May play a role in cuticular wax synthesis (By similarity).
S4TEF7
TE1_HUMLU
Acyl-acyl carrier protein thioesterase TE1, chloroplastic (HlTE1) (EC 3.1.2.-) (Acyl-ACP thioesterase TE1) (Acyl-lipid thioesterase 1)
MLQTISLLPAYNKPPVATLLHPHRSSSSSPLPCGHVSPVTHGGLIMNPQKRLRSFSANMKCSSTNSIIDDTIIRNGQRIMMSEYFDVQLKVRDYELDQYGVVNNAAYASYCQHGCIELMESIGVSGDRISRTGDALAISELSIKFLSPLRGGDKFVMKVRYCRISAVRTYFEHKIFKLPNREPILEAKATTIWLNKKYRPTRMPLEITSLLDKFFTR
Acyl-ACP thioesterase involved in the production of fatty acids and beta-keto fatty acids (By similarity). May play a role in cuticular wax synthesis (By similarity).
S4W177
EQXR_FUSHE
Equisetin cluster transcription factor eqxR (Equisetin biosynthesis protein R)
MSTQNNQSIRSSCDRCRSHKLKCTVAPENSRSGSNRCTRCIRAQVTCVFGHRSQSKRSTNVKKADIKSGTNSQETTSMQASTIVPGRVSVSPDLWVGRQEVEEGLPIGSDGGPSMGDGDLWAELGTNHDLNVFDLTPSSLPTYNSQQQFSATDFCSAPMVPHSDLSAINSQEWQFDVSEHPDQTTTAPHVIVQLSALVTNIHETSKSLGESFWASLAESSQLKNYPIGRVLSLSQDFTAILECIWMSKTMDYKQSSSFVTSESDGQDGISSFELEDVLDYGELLSTVGTSPGRSDFSTSTHSSVATAVDMPTMLLVLSCYTSLTKLYSLVFEHFESHLSHLPHSYTSPTSHTSPRWGLGLQLGELPSADETCTKVYTAVQILLDAFQSVEDVVGLPRSLSAVRQQTCGKEEEAESGDVFNRASLWTDFLAKSVFKATVKGTSEEDCEEIRQLSIKVKSLKALIRERMKL
Transcription factor that regulates the expression of the gene cluster that mediates the biosynthesis of Equisetin.
S4W288
EQXG_FUSHE
MFS transporter eqxG (Equisetin biosynthesis protein G)
MATTDPAIAAPDDSQLEAGRENIRANVGDALEKPSSSTGTMVDEPTDPNVVDWDGPHDPEHPLNWSKTQKNLHLVIVSLFTLAANLAATMFAPGAEELATEFSITNSTVTAMTVSLYVLGFALGPLLLAPLSELYGRLVIYYGCNFVYVVFTIGCAFSTNVAMFLVFRIICGCAASGPMSIGGGTVADLFPQEERGKAMALFTVGPLLGPSGLIGVATVIFMRETNYMVLLQRKAQRARKETGNDKLVPKLTRNETPKQMLARAIVRPLKLLIFSPIVLLISLYTGILFGLIFLLFTTFPSVFQDVYGFSPGTAGLAYLGLGIGMILGLVLFSVLSDKMLKQKSGAARPEDRLILMKWLGPITPLGLFIYGWTAKYAVHWIVPIIGTFVVGFGSLFVVIPGQIYLVDAFGAEAAASAMAANLLVRSPFGAFLDLTASPLYVSLGLGWGNSVLGFICLLFTPVPWLFYTYGERMRTHFKVDL
Efflux pump that might be required for efficient secretion of equisetin or other secondary metabolies produced by the equisetin gene cluster.
S4W775
EQXF_FUSHE
Equisetin cluster transcription factor eqxF (Equisetin biosynthesis protein F)
MADQVQDVHPMEWGPGKTPQGRARLPSSFDATVKDPVAAVHSENLVCRVPMHRIRHLESLVYDLMQNSSANVNQEQVGVTPSPGDQPHVPDYPTPSAAHAPSTNQEPASAAVSPADYGSMQSTGGGANYVGSAHWAAVLDGIAELKDHLDNEESHHSDSQGVDPPCLQVTGPQLLYGCPKPADKDEILSSIPARSVVDRLVSRYFNSFEMSPAVLHSVQFLKEYEEFWEDPQTTSPIWLGLLFTIMCLATQFEKSRLDPGVQSPAVLSMERELQEMVDTFRLRIPQCLVLGSYAKGGPFVLETLMLYIAAEIFLSNDAEIEIWILMGNTVQLALHMGYHRDPKHFKGLSPFTAEMRRRIWATIVEMDLGLSAQMGLPRMIKHWQTDTQEPSNFQDSDFDSATVEMPPSRLNTDLTPILYRLVKARLMTTIGYIWDFSADVRPYPYTEVQKMDDKLDQARKSIPECLKWHSMARNITDSPQHIMQKVILETVFYRAKIVLHRKYMFLPLAQSASSRRIVLESALKLLDYQHMLQEETQPFCQLYQERWRVSSLVNHDFLLATSILCYYLQHARGATPQLSESASFDETIMTSLSRSHDIWLQSSNSSKEARKVVRALAVILGRVNTPSADAAGESGLVFGLQSTYPPSTTNDYSQAPMITPTAEWQEMDGQSQWLPGPRVIQRLTYDMQRQQMRWGL
Transcription factor that regulates the expression of the gene cluster that mediates the biosynthesis of Equisetin.
S4W887
EQX3_FUSHE
Diels-Alderase fsa2 (EC 5.5.1.-) (Equisetin biosynthesis protein 3)
MSNVTVSVFTLDKSISEEPVLPSSFIPSSGNVFPKFTSAIPKTAWELWYFDGISKDDRSSIVIGVTRNAEGLKHGGFKVQVFVIWADERTWHRDLFFPESVVSIDESGATEGIWKHATSSSSISFSCAGDLSKASLVFDVPGIVQGDMHLEALPGDTGLDTDATLGPSVYYVRPLGRASVKAQLSLYSSDATAAEQFILGTSANGGMDRVWSPLSWPQVMTESYYLRAQVGPYAMQIMRIFPPKGSENSENQPSTMARLYREGQLICAPQHVVTRDDALITHDSLILSKQNTSDSGDAVTGEYRDKNTGYTVEFVGKGNEEQRWEFQVRHERIIWNTPTSRPGPDATGNTGFVERLYGGTIGESYEGVGTGGQCELS
Diels-Alderase part of the gene cluster that mediates the biosynthesis of equisetin, a trans-fused decalin-containing tetramic acid with antimicrobial activity. The PKS module of eqxS together with the enoylreductase eqxC catalyze the formation of the polyketide unit which is then conjugated to L-serine by the condensation domain of the eqxS NRPS module. Activity of the Dieckmann cyclase domain (RED) results in release of the Dieckmann product intermediate. Diels-Alderase eqx3 is involved in endo-selective Diels-Alder cycloaddition to form the decalin ring, leading to the production of N-desmethylequisetin also called trichosetin (By similarity). Subsequent N-methylation is carried out by eqxD to give equisetin.
S5ZYD3
OBP_PHOSU
Odorant-binding protein (Lipocalin) (allergen Phod s 1.0101)
NDYAELEGKWDTIAIAADNDAKIKEEGPLRLYVRELYCNEDCSEMEVTFYVNANNQCSKTTVIGYKQADGTYRTQFEGDNRFQPVYATPENIVFTSKNVDRAGQETNLIFVVGKSQPLTPEQHEKLVEFAHENNIPEENIHNVLATDTCPK
May act as a pheromone.
S6C8R9
DEPOL_BPK05
Probable tail spike protein (Depolymerase, capsule KN2-specific) [Cleaved into: Mature tail spike protein; Intramolecular chaperone]
MGYFQMTRNVEEIFGGVVVAPHQIPFKYTSTNGGETFLSLPFYPITGFVTINSGVQVPIDNFEIDGNTLNLGRELEPGDVVFCLFDKIMSPQDASNNAVRIYKFLSVGGETEFTPDFTAYGVQSLYIDGKYKTPGEDYNYFKTSGKVVLDTALPTGVWVVAEMSIKQNIPALAGNNGASEIGTNSGKSLAESLGTWIDTTIAIFEMTEAPSVIQTRGFYETNDGGAGVWVATGIISPSLAGTHVPSQAKVYNAGGVEYQLNVKSGFEISAKANGVKAVDDVNAETEDFVCLGEAINGITSRVKTMVNDEDLKTYLKVIIPSEYPLRIGKTSIKAYSRLKLDFQQASIYDRPSPSNRQEVTGVYMNAIERGIEDVRAISARFGGATSYSNMTLSDFHIEGGKFYGDHTTDKGVADCSTGTGLFTYNMENSSIRNTWFQGFACGRQYNRTGPGYYFDNLGNKVVGTLVPEVTSSGTGSYEGVKEWSVTAYGCRYLYLRVLSNWARFDNCKFGTYANWSSSPDGNQCEYFIENRGAGVVFSGGVIEANTAAANPTKGFVRDYARGCTFEGVYYENCLSAGWVIAIPEKSQYNRANGLFLTAIGSQFTLSSQGAPLVKFEEGYFGSYNPATGLYKTGGWETNYQYAGGVNTWAVGQPELDSGAFPHGGYDFKYGTYGIHYSGSVPDADSLRDTQEGNEFLSPYGLSVNSGILLFPTLSPAYQSNIVVWYKDLTGNFDPRNIVVGDFDNNNVSDGTSNALYRTNGFNYYDYGNGYKAAIVPYVNPRALDNRMTTSAGRKLKITVTSDAPIILKSIQAFVGGTPIFPPAIKDYVPRSQRDRIWGTMSAGSTDSGAYYGPLVGGGIFRPGDVVLPFVPFGNAALMNPASYTDNSSGFGASAETAVITGGATWGAGLAGATFTLTVESQDTINNWTTVSVPSAYLPYIFTGMPVYITANSSGGSTGLINTVRRVVNSDGTLSNKYVLYGALGAAGTTLTVSTTSSYTVRSGVSSTLTGVSGSFSASSWLGTASGDLRVGFGASGSGTRQTRYYYNGADVSAVVGSSGANALHLTGTGGITLNGSLLTSTSYSFGSASAYPANIYSQNAVTVVSDVHYKMDIVELNDAEIECAKACAKLYRRYKLKTAVAIKGEDGARYHVGTIAQLVMQAFTDAGLDWTKYGIITYESWEASDAVVETVGAVYDEEGNELVPETIMVVTPAKEAGEIYMVRYDEFNSFVMAGQEARLQALEEK
[Mature tail spike protein]: Functions as a receptor binding protein (RBP) and probably mediates the attachment to the host capsular exopolysaccharides (Probable). Displays a depolymerase activity that specifically degrades the KN2-type polysaccharides of Klebsiella pneumoniae capsule.