ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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Q8N5C8 | MAQSSPQLDIQVLHDLRQRFPEIPEGVVSQCMLQNNNNLEACCRALSQESSKYLYMEYHSPDDNRMNRNRLLHINLGIHSPSSYHPGDGAQLNGGRTLVHSSSDGHIDPQHAAGKQLICLVQEPHSAPAVVAATPNYNPFFMNEQNRSAATPPSQPPQQPSSMQTGMNPSAMQGPSPPPPPPSYMHIPRYSTNPITVTVSQNLPSGQTVPRALQILPQIPSNLYGSPGSIYIRQTSQSSSGRQTPQSTPWQSSPQGPVPHYSQRPLPVYPHQQNYQPSQYSPKQQQIPQSAYHSPPPSQCPSPFSSPQHQVQPSQLGHIFMPPSPSTTPPHPYQQGPPSYQKQGSHSVAYLPYTASSLSKGSMKKIEITVEPSQRPGTAINRSPSPISNQPSPRNQHSLYTATTPPSSSPSRGISSQPKPPFSVNPVYITYTQPTGPSCTPSPSPRVIPNPTTVFKITVGRATTENLLNLVDQEERSAAPEPIQPISVIPGSGGEKGSHKYQRSSSSGSDDYAYTQALLLHQRARMERLAKQLKLEKEELERLKSEVNGMEHDLMQRRLRRVSCTTAIPTPEEMTRLRSMNRQLQINVDCTLKEVDLLQSRGNFDPKAMNNFYDNIEPGPVVPPKPSKKDSSDPCTIERKARRISVTSKVQADIHDTQAAAADEHRTGSTQSPRTQPRDEDYEGAPWNCDSCTFLNHPALNRCEQCEMPRYT | Function: Adapter required to activate the JNK and NF-kappa-B signaling pathways through the specific recognition of 'Lys-63'-linked polyubiquitin chains by its RanBP2-type zinc finger (NZF) . Acts as an adapter linking MAP3K7/TAK1 and TRAF6 to 'Lys-63'-linked polyubiquitin chains . The RanBP2-type zinc finger (NZF) specifically recognizes Lys-63'-linked polyubiquitin chains unanchored or anchored to the substrate proteins such as RIPK1/RIP1 and RIPK2: this acts as a scaffold to organize a large signaling complex to promote autophosphorylation of MAP3K7/TAK1, and subsequent activation of I-kappa-B-kinase (IKK) core complex by MAP3K7/TAK1 .
PTM: Ubiquitinated; following IL1 stimulation or TRAF6 overexpression . Ubiquitinated by AMFR via 'Lys-27'-linked polyubiquitination; leading to TAK1/MAP3K7 activation .
Sequence Mass (Da): 78653
Sequence Length: 712
Domain: The RanBP2-type zinc finger (NZF) mediates binding to two consecutive 'Lys-63'-linked ubiquitins.
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Q7Z7C8 | MADAAATAGAGGSGTRSGSKQSTNPADNYHLARRRTLQVVVSSLLTEAGFESAEKASVETLTEMLQSYISEIGRSAKSYCEHTARTQPTLSDIVVTLVEMGFNVDTLPAYAKRSQRMVITAPPVTNQPVTPKALTAGQNRPHPPHIPSHFPEFPDPHTYIKTPTYREPVSDYQVLREKAASQRRDVERALTRFMAKTGETQSLFKDDVSTFPLIAARPFTIPYLTALLPSELEMQQMEETDSSEQDEQTDTENLALHISMEDSGAEKENTSVLQQNPSLSGSRNGEENIIDNPYLRPVKKPKIRRKKSLS | Function: The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription . TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC) . The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 . The TFIID complex structure can be divided into 3 modules TFIID-A, TFIID-B, and TFIID-C . TAF8 is involved in forming the TFIID-B module, together with TAF5 . Mediates both basal and activator-dependent transcription . Plays a role in the differentiation of preadipocyte fibroblasts to adipocytes, however, does not seem to play a role in differentiation of myoblasts . Required for the integration of TAF10 in the TAF complex . May be important for survival of cells of the inner cell mass which constitute the pluripotent cell population of the early embryo (By similarity).
Sequence Mass (Da): 34262
Sequence Length: 310
Domain: Ectopic expression of the histone fold domain acts as a dominant-negative mutant resulting in differentiation inhibition.
Subcellular Location: Nucleus
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P86071 | GVTSNPAIFQKAISTSNAYNDQFR | Function: Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Catalytic Activity: D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = beta-D-fructose 6-phosphate + D-erythrose 4-phosphate
Sequence Mass (Da): 2630
Sequence Length: 24
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage): step 2/3.
Subcellular Location: Cytoplasm
EC: 2.2.1.2
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P80427 | KYKPTDATTNPSLILQAKFLEELQNSKKIYNYYKKESVVEHLSESSAKKLEMTEANFRWEMNEDKFAVDAVKLEK | Function: Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. May play a role in the conversion of sterols into ecdysteroids via NADPH.
PTM: Phosphorylated.
Catalytic Activity: D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = beta-D-fructose 6-phosphate + D-erythrose 4-phosphate
Sequence Mass (Da): 8818
Sequence Length: 75
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage): step 2/3.
Subcellular Location: Cytoplasm
EC: 2.2.1.2
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Q9W1G0 | MGSDRTLKKQKMSVLQELKKITTIVADTGDFEAINIYKPTDATTNPSLILSASSMERYQPLVQKAVEYAKGKKGSVSEQVAEAMDYLCVLFGTEILKVVPGRVSTEIDARLSFDTKKSVEKALKLIALYKSLGVDKERILIKLASTWEGIKAAEILENEHGVHCNLTLLFSFAQAVACAEAGVTLISPFVGRILDWYVANTDTKKFEALKDPGVISVTNIYNYYKKFGYKTLVMGASFRNVGEIKALAGCDLLTISPALLKELENETESVVTYLSVSNAKLQDIEKITVDESRFRWLLNEDAMATDKLSEGIRKFAVDTVKLENLIKTYLK | Function: Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Catalytic Activity: D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = beta-D-fructose 6-phosphate + D-erythrose 4-phosphate
Sequence Mass (Da): 36734
Sequence Length: 331
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage): step 2/3.
Subcellular Location: Cytoplasm
EC: 2.2.1.2
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P37837 | MSSSPVKRQRMESALDQLKQFTTVVADTGDFHAIDEYKPQDATTNPSLILAAAQMPAYQELVEEAIAYGRKLGGSQEDQIKNAIDKLFVLFGAEILKKIPGRVSTEVDARLSFDKDAMVARARRLIELYKEAGISKDRILIKLSSTWEGIQAGKELEEQHGIHCNMTLLFSFAQAVACAEAGVTLISPFVGRILDWHVANTDKKSYEPLEDPGVKSVTKIYNYYKKFSYKTIVMGASFRNTGEIKALAGCDFLTISPKLLGELLQDNAKLVPVLSAKAAQASDLEKIHLDEKSFRWLHNEDQMAVEKLSDGIRKFAADAVKLERMLTERMFNAENGK | Function: Catalyzes the rate-limiting step of the non-oxidative phase in the pentose phosphate pathway. Catalyzes the reversible conversion of sedheptulose-7-phosphate and D-glyceraldehyde 3-phosphate into erythrose-4-phosphate and beta-D-fructose 6-phosphate . Not only acts as a pentose phosphate pathway enzyme, but also affects other metabolite pathways by altering its subcellular localization between the nucleus and the cytoplasm (By similarity).
Catalytic Activity: D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = beta-D-fructose 6-phosphate + D-erythrose 4-phosphate
Sequence Mass (Da): 37540
Sequence Length: 337
Domain: The first 10 amino acids are essential for nuclear localization.
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage): step 2/3.
Subcellular Location: Nucleus
EC: 2.2.1.2
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Q93092 | MSGSPVKRQRMESALDQLKQFTTVVADTGDFNAIDEYKPQDATTNPSLILAAAQMPAYQELVEEAIAYGKKLGGPQEEQIKNAIDKLFVLFGAEILKKIPGRVSTEVDARLSFDKDAMVARARRLIELYKEAGVGKDRILIKLSSTWEGIQAGKELEEQHGIHCNMTLLFSFAQAVACAEAGVTLISPFVGRILDWHVANTDKKSYEPQEDPGVKSVTKIYNYYKKFGYKTIVMGASFRNTGEIKALAGCDFLTISPKLLGELLKDNSKLAPALSVKAAQTSDSEKIHLDEKAFRWLHNEDQMAVEKLSDGIRKFAADAIKLERMLTERMFSAENGK | Function: Catalyzes the rate-limiting step of the non-oxidative phase in the pentose phosphate pathway. Catalyzes the reversible conversion of sedheptulose-7-phosphate and D-glyceraldehyde 3-phosphate into erythrose-4-phosphate and beta-D-fructose 6-phosphate . Not only acts as a pentose phosphate pathway enzyme, but also affects other metabolite pathways by altering its subcellular localization between the nucleus and the cytoplasm .
Catalytic Activity: D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = beta-D-fructose 6-phosphate + D-erythrose 4-phosphate
Sequence Mass (Da): 37387
Sequence Length: 337
Domain: The first 10 amino acids are essential for nuclear localization.
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage): step 2/3.
Subcellular Location: Nucleus
EC: 2.2.1.2
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Q9EQS0 | MSGSPVKRQRMESALDQLKQFTTVVADTGDFNAIDEYKPQDATTNPSLILAAAQMPAYQELVEEAIAYGKKLGGPQEEQIKNAIDKLFVLFGAEILKKIPGRVSTEVDARLSFDKDAMVARARRIIELYKEAGISKDRILIKLSSTWEGIQAGKELEEQHGIHCNMTLLFSFAQAVACAEAGVTLISPFVGRILDWHVANTDKKSYEPQEDPGVKSVTKIYNYYKKFGYKTIVMGASFRNTGEIKALAGCDFLTISPKLLGELLKDSSKLAPTLSVKAAQTSDLEKIHLDEKAFRWLHNEDQMAVEKLSDGIRKFAADAIKLERMLTERMFSAENGK | Function: Catalyzes the rate-limiting step of the non-oxidative phase in the pentose phosphate pathway. Catalyzes the reversible conversion of sedheptulose-7-phosphate and D-glyceraldehyde 3-phosphate into erythrose-4-phosphate and beta-D-fructose 6-phosphate.
Catalytic Activity: D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = beta-D-fructose 6-phosphate + D-erythrose 4-phosphate
Sequence Mass (Da): 37460
Sequence Length: 337
Domain: The first 10 amino acids are essential for nuclear localization.
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage): step 2/3.
Subcellular Location: Nucleus
EC: 2.2.1.2
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Q3YBN2 | MSWLLSTMCLVHVCGNIFCLFETTTNPEAYMKVSKIVNHWGYTSEEYEAVTEDGYILPLNRIPHGKNNINSTAPKKVVLCQHGLFSTAGVWVSNPPSNSLAFILADAGFDVWMGNSRGSTWAKKHLYLDPNSKEFWAFSFDEMIKYDLPATINFILKKTGQKQIYYIGHSQGALIALGAFSTNQKLAEKIKLCFLLAPIATLKHVEGIVSLLPYFYPTAFKVVFSEKEFLSAVAFSKLHGYSCNAKVINDGCVAIFLSMTGYVPQHLNKSRVDVYIRHSLAGTSVQTLLHYRQAIKKGVFEAYDWGSQSLNMLHYNQTTPPLYNVEDMKIPTAMWSGGKDSLADTKDVAHLVPKISNLIYHKITADFSHLDFTVGKNAYYVSNDILKLLDKSETENLH | Function: Female-specific protein which lacks detectable lipase activity against a range of substrates. Binds the hydrophobic lipid 1-aminoanthracene with high affinity.
PTM: N-glycosylated.
Sequence Mass (Da): 44666
Sequence Length: 398
Subcellular Location: Secreted
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Q3IWB0 | MLAMSPPKPAVELDRHIDLDQAHAVASGGARIVLAPPARDRCRASEARLGAVIREARHVYGLTTGFGPLANRLISGENVRTLQANLVHHLASGVGPVLDWTTARAMVLARLVSIAQGASGASEGTIARLIDLLNSELAPAVPSRGTVGASGDLTPLAHMVLCLQGRGDFLDRDGTRLDGAEGLRRGRLQPLDLSHRDALALVNGTSAMTGIALVNAHACRHLGNWAVALTALLAECLRGRTEAWAAALSDLRPHPGQKDAAARLRARVDGSARVVRHVIAERRLDAGDIGTEPEAGQDAYSLRCAPQVLGAGFDTLAWHDRVLTIELNAVTDNPVFPPDGSVPALHGGNFMGQHVALTSDALATAVTVLAGLAERQIARLTDERLNRGLPPFLHRGPAGLNSGFMGAQVTATALLAEMRATGPASIHSISTNAANQDVVSLGTIAARLCREKIDRWAEILAILALCLAQAAELRCGSGLDGVSPAGKKLVQALREQFPPLETDRPLGQEIAALATHLLQQSPV | Function: Catalyzes the non-oxidative deamination of L-tyrosine. Has very low phenylalanine ammonia-lyase activity (in vitro).
PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly.
Catalytic Activity: L-tyrosine = (E)-4-coumarate + NH4(+)
Sequence Mass (Da): 54914
Sequence Length: 523
EC: 4.3.1.23
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Q6MAI4 | MEKNKLDQLKSMTTIVIDTGDIEAIKEYSPTDATTNPSLILSAVEKPAYKPLMEEAYHYSQKAKSSGEQISLFLDKLFVNVGCEILKLIPGRVSTEVDARLSFDVEGSIQKAQSLIALYKEMGIEKERILIKLASTWEGGLAAKQLEKMGIHCNMTLLFSMPQAIHCAEAQATLISPFVGRILDWYKKHDNVPGYAPAEDPGVKSVTTIYHYFKKFSYKTQIMGASFRNKEEILELAGCDLLTISPHFLQELHDASGNVEQKLDAAKSKQLNIEPIKMNEKAFRLALNDDAMATEKLSEGIRNFAKDAQKLEKMLRTTYKIG | Function: Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Catalytic Activity: D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = beta-D-fructose 6-phosphate + D-erythrose 4-phosphate
Sequence Mass (Da): 36045
Sequence Length: 322
Pathway: Carbohydrate degradation; pentose phosphate pathway; D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage): step 2/3.
Subcellular Location: Cytoplasm
EC: 2.2.1.2
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B1LXF6 | MADWNPALYTRFEDERTRPAAELLARVPLEAPRLAIDLGCGPGNSTALIAARFPDAEVIGLDTSPAMLESARARLPRLAFALADAATWTPERAPDLIYANAVLQWLPDHATLLPRLFGLLAPGGVLAVQMPDNLAEPTHRLMRAVAASGPWAAAIGDPAVAGRLGRMLEPAAYYDLLAPAAAEVDVWRTAYHHRMADAAAIVDWVRATGLRPFLDPLDPEHRAGFLDAYTRAIDGAYPPRSDGRRLLAFPRVFVVARKAS | Function: Catalyzes the S-adenosylmethionine monomethyl esterification of trans-aconitate.
Catalytic Activity: S-adenosyl-L-methionine + trans-aconitate = (E)-3-(methoxycarbonyl)pent-2-enedioate + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28139
Sequence Length: 260
Subcellular Location: Cytoplasm
EC: 2.1.1.144
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B0UPF4 | MADWNAAQYLKFADERTRPAADLLARVPLESPARVIDLGCGPGNSTALLCARFPRAAVTGLDSSPDMLATARERLPAVRFVEADLAGFTPAEPPDLLFANAVLQWLPDHAGLLARLARMLAPGGCLAVQMPDNLEEPSHRLMRRVAGEAPFAERLAQAAAARTRLGSFRDYDAWLSAAGCTVDLWRTTYVHPLAGHRGIVEWVRGTGLRPFLDPLDPADQAAFLARYEAALAEAYPPQADGRVLLPFPRLFLVARRR | Function: Catalyzes the S-adenosylmethionine monomethyl esterification of trans-aconitate.
Catalytic Activity: S-adenosyl-L-methionine + trans-aconitate = (E)-3-(methoxycarbonyl)pent-2-enedioate + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28029
Sequence Length: 257
Subcellular Location: Cytoplasm
EC: 2.1.1.144
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A4T0W0 | MWNPAVYLTYADHRGRPYYDLLSRVDAREPRRIVDLGCGPGNLTRTLTQRWPGAVVEAWDSSEEMVTAARERGVDARVGDVRDWAPLPDTDVVVSNATLHWVPEHPDLLLRWAGQLRAGSWIAFQVPGNFDAPSHRAVRDLVSSARWAHLLRDFPFEKSEVVRPAAGYAELLTDAGCTVDAWETTYVHELTGEKPVLEWIGGTALRPVRAALPDHDWQEFRAELIPLLDAAYPRRADGITFFPFRRIFVVARVKN | Function: Catalyzes the S-adenosylmethionine monomethyl esterification of trans-aconitate.
Catalytic Activity: S-adenosyl-L-methionine + trans-aconitate = (E)-3-(methoxycarbonyl)pent-2-enedioate + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28848
Sequence Length: 255
Subcellular Location: Cytoplasm
EC: 2.1.1.144
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B2HNX5 | MWDPDVYLAFADHRGRPFYDLVSRIGAKRARRVVDLGCGPGNLTRYLARRWPEAIIEAWDSSPQMVAAARERGIDATTGDLRTWKPKPDTDVVISSAALHWVPEHADLMVQWATELPHGSWIAVQVPGNFETPSHAVVRALARREPYAKLMRDIPFRVGAVVGSPASYAGLLMDAGCKVDAWETTYLHQLTGKNPVLEWITGTALVPVRERLDDVSWEQFRQELIPLLDDAYPPRSDGTTMFPFRRLFIVAEVGGARRSADVS | Function: Catalyzes the S-adenosylmethionine monomethyl esterification of trans-aconitate.
Catalytic Activity: S-adenosyl-L-methionine + trans-aconitate = (E)-3-(methoxycarbonyl)pent-2-enedioate + S-adenosyl-L-homocysteine
Sequence Mass (Da): 29431
Sequence Length: 263
Subcellular Location: Cytoplasm
EC: 2.1.1.144
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Q0DKE8 | MAAMGSKDGGGGGGGMAAQAGRLGVVASVAFNLAALAFYLRRRYFGGDDAAAVRKKAEAEVAPSSGKPPVTKDSIINLDHGDPTMYEAFWRGGAGERATIVIPGWQTMSYFSDVGSLCWFLEPGLEREVRRLHRLVGNAVADGYHVLVGTGSTQLFQAALYALSPPGPSAPMNVVSPAPYYSSYPAVTDFLKSGLYRWAGDAKMFDGDTYVELVCSPSNPDGGIREAVLKSGDGVAVHDLAYYWPQYTPITSAAAHDIMLFTVSKCTGHAGTRLGWALVKDRAVAQKMSKFIELNTIGVSKDSQLRAAKILKAITDGYDRAPAAGDDDDDSSRLFHFARRKMVSRWAKLRAAVAASGIFTLPDELPGHCTFANETVSAYPPFAWLRCGKEGVDDLEGYLRERKIISRGGGKFGADGRVVRISMLDTDEAFAIFVDRLAAMN | Function: Probable tryptophan aminotransferase that may be involved in the regulation of auxin production in developing rice grains.
Catalytic Activity: 2-oxoglutarate + L-tryptophan = indole-3-pyruvate + L-glutamate
Sequence Mass (Da): 47349
Sequence Length: 441
Pathway: Plant hormone metabolism; auxin biosynthesis.
EC: 2.6.1.27
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Q94A02 | MGQIPRFLSWRNMLVLSLAINFSLILKILKGDRERGDSWDRTAYVSIWPVVSTTASESSSLSSASCNYSKIEEDDDRIINLKFGDPTVYERYWQENGEVTTMVIPGWQSLSYFSDENNLCWFLEPELAKEIVRVHKVVGNAVTQDRFIVVGTGSTQLYQAALYALSPHDDSGPINVVSATPYYSTYPLITDCLKSGLYRWGGDAKTYKEDGPYIELVTSPNNPDGFLRESVVNSTEGILIHDLAYYWPQYTPITSPADHDVMLFTASKSTGHAGIRIGWALVKDRETARKMIEYIELNTIGVSKDSQLRVAKVLKVVSDSCGNVTGKSFFDHSYDAMYERWKLLKQAAKDTKRFSVPDFVSQRCNFFGRVFEPQPAFAWFKCEEGIVDCEKFLREEKKILTKSGKYFGDELSNVRISMLDRDTNFNIFLHRITSSFNSTL | Function: Involved in auxin production. Both TAA1 and TAR2 are required for maintaining proper auxin levels in roots, while TAA1, TAR1 and TAR2 are required for proper embryo patterning. Involved in the maintenance of the root stem cell niches.
Catalytic Activity: 2-oxoglutarate + L-tryptophan = indole-3-pyruvate + L-glutamate
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 50007
Sequence Length: 440
Pathway: Plant hormone metabolism; auxin biosynthesis.
Subcellular Location: Membrane
EC: 2.6.1.27
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Q5VQG8 | MAALRVGTRAVEGRFQASNGGGGGGGGMAPSSRLVAAHREAKPRSSHSAAPWKLPRRRAGAMPLWRVAVFASVALNVATLALLLHHYATSPPPHHHHHDAGLATRSSDAAVHRRARTASSMAPSTGKPAVTTDSVINLDHGDPTMFEEFWRETGDAAEVVIPGWQTMSYFSDVTNVCWFLEPELDRQVRRLHRVVGNAAVDGYHVLVGTGSTQLFMAALYALAPDAAAAAAGEPISVVSTAPYYSSYPAVTDFLRSGLFRWAGDADAFKGDSYIELVCSPNNPDGAIREAVLDPKTGNGRTVHDLAYYWPQYTPITKRASHDIMLFTVSKSTGHAGTRIGWALVKDRAIARKMTKFVELNTIGVSKDSQMRAAKVLAAVSDGYERRPEQTKETMTTPLRLFDFGRRKMVERWSMLRAAAAASGIFSLPEETSGFCNFTKETAATNPAFAWLRCDREDVEDCAGFLRGHKILTRSGAQFGADARYVRVSMLDRDDAFDIFINRLSSLK | Function: Probable tryptophan aminotransferase involved in auxin (IAA) biosynthesis . Required for auxin production to initiate multiple change in growth in response to environmental and developmental cues . Functions upstream of YUCCA1 in auxin biosynthesis . Required for polar auxin transport .
Catalytic Activity: 2-oxoglutarate + L-tryptophan = indole-3-pyruvate + L-glutamate
Sequence Mass (Da): 55260
Sequence Length: 507
Pathway: Plant hormone metabolism; auxin biosynthesis.
EC: 2.6.1.27
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Q9FE98 | MIHNKLLIAGSIILNLVFTIHILYNNTSTWSPTWTNRAALEAEAAASVSCSGHGRSYVDGLGVLDGHKPCECHDCYTGKDCSVLLKDCPVDANSGDPLFLEPFWIRKAEESAVVESGWHRMSYTFNGYGLFMSAELEKIIRKLHNVVGNAVTDNRFIIFGAGATQLLAASVHALSQTNSLSPSRLVTSVPYYNLYKQQADFFNSTNLKFEGDASAWKRSERNDDIKQVIEIVTSPNNPDGKLKRAVLDGPNVKYIHDYAYYWPYFSPITRQADEDLSLFSLSKTTGHAGSRFGWALVKEKTVYEKMKIYISLSSMGVSRDTQLRALQLLKVVIGDGGNEIFRFGYGTLKKRWEILNKIFSMSTRFSLETIKPEYCNYFKKVREFTPSYAWVKCERPEDTDCYEIFKAAKITGRNGEMFGSDERFVRLSLIRSQDDFDQLIAMLKKFVSKEAVVVDSI | Function: Probable aminotransferase.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 51654
Sequence Length: 457
Subcellular Location: Membrane
EC: 2.6.1.-
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Q2G2L3 | MTVEERSNTAKVDILGVDFDNTTMLQMVENIKTFFANQSTNNLFIVTANPEIVNYATTHQAYLELINQASYIVADGTGVVKASHRLKQPLAHRIPGIELMDECLKIAHVNHQKVFLLGATNEVVEAAQYALQQRYPNISFAHHHGYIDLEDETVVKRIKLFKPDYIFVGMGFPKQEEWIMTHENQFESTVMMGVGGSLEVFAGAKKRAPYIFRKLNIEWIYRALIDWKRIGRLKSIPIFMYKIAKAKRKIKKAK | Function: Catalyzes the conversion of GlcNAc-PP-undecaprenol into ManNAc-GlcNAc-PP-undecaprenol, the first committed lipid intermediate in the de novo synthesis of teichoic acid.
Catalytic Activity: N-acetyl-alpha-D-glucosaminyl-di-trans,octa-cis-undecaprenyl diphosphate + UDP-N-acetyl-alpha-D-mannosamine = H(+) + N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl di-trans,octa-cis-undecaprenyl diphosphate + UDP
Sequence Mass (Da): 29133
Sequence Length: 254
Pathway: Cell wall biogenesis; poly(ribitol phosphate) teichoic acid biosynthesis.
EC: 2.4.1.187
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Q2G2X4 | MNVLIKKFYHLVVRILSKMITPQVIDKPHIVFMMTFPEDIKPIIKALNNSSYQKTVLTTPKQAPYLSELSDDVDVIEMTNRTLVKQIKALKSAQMIIIDNYYLLLGGYNKTSNQHIVQTWHASGALKNFGLTDHQVDVSDKAMVQQYRKVYQATDFYLVGCEQMSQCFKQSLGATEEQMLYFGLPRINKYYTADRATVKAELKDKYGITNKLVLYVPTYREDKADNRAIDKAYFEKCLPGYTLINKLHPSIEDSDIDDVSSIDTSTLMLMSDIIISDYSSLPIEASLLDIPTIFYVYDEGTYDQVRGLNQFYKAIPDSYKVYTEEDLIMTIQEKEHLLSPLFKDWHKYNTDKSLHQLTEYIDKMVTK | Function: Catalyzes the addition of a single glycerol phosphate residue to the prenoldiphosphate-linked disaccharide.
Catalytic Activity: CDP-glycerol + N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl di-trans,octa-cis-undecaprenyl diphosphate = 4-O-[(2R)-glycerylphospho]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl di-trans,octa-cis-undecaprenyl diphosphate + CMP + H(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 42436
Sequence Length: 367
Pathway: Cell wall biogenesis; poly(ribitol phosphate) teichoic acid biosynthesis.
Subcellular Location: Cell membrane
EC: 2.7.8.44
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Q89KZ7 | MGSLSIWHWILVIAVVLLLFGRGKISDLMGDVAQGIKAFKKGMQDDDKPADKPEPAKSIEHNAAPTAARSDVGSKAV | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 8200
Sequence Length: 77
Subcellular Location: Cell inner membrane
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B2S5B5 | MGSFSIWHWLIVLAVVLLLFGRGKIPELMGDVAKGIKNFKQGMADEDAKEDPRTIDAKAEEPVKDVKKTTKS | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 7999
Sequence Length: 72
Subcellular Location: Cell inner membrane
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A6X1F5 | MGSFSIWHWLIVLAVVLLLFGRGKIPELMGDVAKGIKNFKQGMSDEDAKDDARDSGRTIDAKADETVNDVKKTTKS | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 8367
Sequence Length: 76
Subcellular Location: Cell inner membrane
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Q5YUY0 | MSGTFSWTHLLIIALLFVVLFGAKRLPDAARGLGRSLRIFKSEVNQMQHETPQANAAPVQQPAQQLPPAQPAQAPAQPVNQAEQKSA | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 9411
Sequence Length: 87
Subcellular Location: Cell membrane
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Q2G9D4 | MGGLSLPHLIVLALVVLILFGRGRISEMMGDFGKGIKSFKQGMNDEDSKPVTPPPAQIPPASLQQTPPPAQPAPQPTSTDQAQ | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 8744
Sequence Length: 83
Subcellular Location: Cell inner membrane
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Q30ZC2 | MFGIGIPELLVIFVLILLVFGAKRLPEIGGGLGRAIKNFKKATTEPDEIDVTPSSEKKHKDE | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 6778
Sequence Length: 62
Subcellular Location: Cell inner membrane
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B2JHX4 | MGSLSIWHWLIVLLIVALVFGTKKLRNIGSDLGGAVKGFKEGMKDGETPEGQQRDQLSRTNTVDVDAKEKAPHSGDSR | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 8492
Sequence Length: 78
Subcellular Location: Cell inner membrane
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B2SZ54 | MGSLSIWHWLIVLLIVALVFGTKKLRNIGGDLGGAVKGFKEGMKEADAPAAEAQQRELPRNGAVDVEAKEKTPRSGDYR | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 8563
Sequence Length: 79
Subcellular Location: Cell inner membrane
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Q13TR5 | MGSLSIWHWLIVLLIVALVFGTKKLRNIGTDLGGAVKGFKEGMKEAETPAGEAQQRELPRNGAVDVDAKEKAPRSGDYR | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 8593
Sequence Length: 79
Subcellular Location: Cell inner membrane
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Q9CKD3 | MGGISITQLLIIVAIVVLLFGTKKLRTLGSDLGESVKGFKKAMADDNKEKDAEFKSLSDDSETTAKTEKAKDKEQA | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 8203
Sequence Length: 76
Subcellular Location: Cell inner membrane
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Q9XH46 | MEITLSISSSSVIPTRLPNSSCYSNLSFLSSNSNTSSLLLKKARIKTRTTKGFTCNAFFGLGVPELVVIAGVAALVFGPKKLPEVGRSIGQTVKSFQQAAKEFETELKKEPNPTEEISVASEQEKQEIKVSSTKDNV | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across the thylakoid membrane. Involved in delta pH-dependent protein transport required for chloroplast development, especially thylakoid membrane formation. TATC and TATB mediate precursor recognition, whereas TATA facilitates translocation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 14799
Sequence Length: 137
Subcellular Location: Plastid
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Q4FM05 | MSIGIWQIAIVVILVVLLFGRGKISSLMGDVAKGIKSFKKGMATDITDEPEPKNVSENNQDSKDKE | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 7191
Sequence Length: 66
Subcellular Location: Cell inner membrane
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B4RDI4 | MGSFSIWHWLIVLVVVALLFGGRGRLSGIMGDAAKGIRAFRDGLKGESEQAEDETAKPLPKERDKDSARG | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 7599
Sequence Length: 70
Subcellular Location: Cell inner membrane
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Q7MZ84 | MGGISIWQLLIIAVIVVLLFGTNKLRTLGSDLGASIKGFKKAIGDDNQPQQAQKTSSDADFETKNITEKQSVAQSETSESKNKEQV | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 9296
Sequence Length: 86
Subcellular Location: Cell inner membrane
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Q6LVW7 | MGGISIWQLLIIALIIVLLFGTKKLRSLGGDLGSAVKGFKKAIGDEELTVKKDNTEADADFEQKTLSKEEQQSEDPVQKSQKDKEQV | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 9576
Sequence Length: 87
Subcellular Location: Cell inner membrane
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A1VK47 | MGGFSIWHWLIVLLIVVMVFGTKKLRNMGSDLGGAVKGFKDGMKDGGQSPADEKPVVPASQVTNAQAADKAERNTIDVEARQKS | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 9000
Sequence Length: 84
Subcellular Location: Cell inner membrane
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Q9A6T1 | MLPDIGGTELLIIAAVALIVVGPKDLPALLRKVGQFVGRMRGMASEFRASFDEMARQSELDELRREVQAMRSGQFTNPVQDAADAARDVQVDQVFADIDASLSSGAMQAHPYAAGETHNSILPTAEPSAEIVEAKPKRAPRKKAVAEPVAAEPVLVEPVKAPRKRASQKQEITVEAPKAVRAPRKRASKAGDSTASDIVS | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 21372
Sequence Length: 200
Subcellular Location: Cell inner membrane
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A3PIZ4 | MFDIGWSELLVIGVVALVVVGPKDLPEMFRTLGRVTAKARNMAREFQRAMEAAADETGVKDVVKDVKNVTSPRSMGLDAMKQAADRFEKWDPMKPQQGAPKPAAPASSIPAAKAQQGAGAAAVTAPPASEPAAPVPQAPAAAAPEAASPAPAEPKSNA | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 16249
Sequence Length: 158
Subcellular Location: Cell inner membrane
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Q11HC6 | MLDLGWSEILVIAVVLIVVVGPKDLPRVLRSFGRTTAKMRAMAGDFRRQFDEALREAELDDMKGLVDDVRKLDPRSEIRKHLSPLEEAGKEIRSGLSEAAKAKPAASSLPAADSKPAEPLKNGATSLGPEAPPPVTGETAAPKVSEKAEVGAVAASPGTSAKQAAPKAKAAAAAKAPTKNTASAPAKKPSPRRKKTAGTAP | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 20840
Sequence Length: 201
Subcellular Location: Cell inner membrane
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Q1R004 | MFDMGFLELMLIGVVALLVLGPERLPTAARTVGLWVGKIKRTVSGMQREISAQLEAEELRQKLNEQQRKLDAGLGKVRDEVERHGDAPSSRGGQPPPSRTTPTAARSADDTDETPPSTAASRETPEPPAAPSAKDSNAP | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 14881
Sequence Length: 139
Subcellular Location: Cell inner membrane
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Q6NHY4 | MFSSIGWPEIFTVLILGLIIIGPERLPKVIEDVRAAIYAAKKAINNAKEELNGNLGAEFDEFREPINKIASIQRMGPKAVLTKALFDEDENFMDNFDPKKIMASGTEGEAYRERGINPQPAGDSASPQTPSNKESQPKAGFSWDDIT | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 16199
Sequence Length: 147
Subcellular Location: Cell membrane
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Q8FQD9 | MFSNVGWGEILLLFIVGLIVIGPERLPRLMEDLKAAIVAARTAINNAKQNLDTDFGEEFDEIRKPMAQIAQIRSMSPKTAITRALFDGDDSFLDSFDPKKIMADDTAGQAHRQQVAKTGTTPEHAEVVERPADRIDPTQSPNTPGKNNDGGKPPAGGGYTWTDLI | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 17975
Sequence Length: 165
Subcellular Location: Cell membrane
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Q4JUF6 | MFSNVGWGEVLVLLIVALFLIGPERLPGLIKEVRAMLLAVRNAISQAKEQIDGELGEDFREFSKPLQELNSVRQMGAKGFITKTLLDGDDSFLTSFNETKQDVKDTVDTVRKPNLRESLKADKTKKSAQPQPSLASGSADNGGIAVTQQSNAGESRSSHDSPVADAAEQLTGDVGSASEPKEKPSAPGYGWEDVT | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 20931
Sequence Length: 195
Subcellular Location: Cell membrane
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A5EVU3 | MFEIGFWELVLVAIIGIVVVGPKRLPEVVRTLGLLLRKMRRTISSVRADIERELDLEEMRKLMSDVDEPLKKHVDQLNQSIWQAEYDLRQGGKNLLKMIDEPPYQEPPPAAHSVQTDAEAYRDTGIEPADKSSSPEHHHDDAAR | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 16434
Sequence Length: 144
Subcellular Location: Cell inner membrane
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P69426 | MFDIGFSELLLVFIIGLVVLGPQRLPVAVKTVAGWIRALRSLATTVQNELTQELKLQEFQDSLKKVEKASLTNLTPELKASMDELRQAAESMKRSYVANDPEKASDEAHTIHNPVVKDNEAAHEGVTPAAAQTQASSPEQKPETTPEPVVKPAADAEPKTAAPSPSSSDKP | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 18421
Sequence Length: 171
Subcellular Location: Cell inner membrane
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Q6DAQ1 | MFDIGVNLTSSQFEKDREQVVIRAKLAGVSGILITGTNAQESHQAMLLAQAYPDYCWSTAGVHPHDASQWNDAIAEQLHQMANAACVVSIGECGLDFNRNFSTPEEQEQAFSAQLAIAAELSMPVFLHCRDAHPRFISLLTPWLSQLPAAVVHCFTGNRHELDECLAAGLMIGITGWVCDERRGLELRALLPHIPADRLLVETDAPYLLPRDLRPKPASRRNEPCYLPHIIRQIAEWRGEDATWLGQTTDENARRVFRLA | Function: 3'-5' exonuclease that prefers single-stranded DNA and RNA. May play a role in the H(2)O(2)-induced DNA damage repair.
Sequence Mass (Da): 29032
Sequence Length: 260
Subcellular Location: Cytoplasm
EC: 3.1.11.-
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C6CQJ7 | MEGISIAKLLVIGALIVLLFGTNKLRSLGGDLGAAIKGFKKAMNDDQPAAKSSAQDEHPAAISETRPKE | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatE shares overlapping functions with TatA.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 7204
Sequence Length: 69
Subcellular Location: Cell inner membrane
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Q86VP1 | MTSFQEVPLQTSNFAHVIFQNVAKSYLPNAHLECHYTLTPYIHPHPKDWVGIFKVGWSTARDYYTFLWSPMPEHYVEGSTVNCVLAFQGYYLPNDDGEFYQFCYVTHKGEIRGASTPFQFRASSPVEELLTMEDEGNSDMLVVTTKAGLLELKIEKTMKEKEELLKLIAVLEKETAQLREQVGRMERELNHEKERCDQLQAEQKGLTEVTQSLKMENEEFKKRFSDATSKAHQLEEDIVSVTHKAIEKETELDSLKDKLKKAQHEREQLECQLKTEKDEKELYKVHLKNTEIENTKLMSEVQTLKNLDGNKESVITHFKEEIGRLQLCLAEKENLQRTFLLTTSSKEDTCFLKEQLRKAEEQVQATRQEVVFLAKELSDAVNVRDRTMADLHTARLENEKVKKQLADAVAELKLNAMKKDQDKTDTLEHELRREVEDLKLRLQMAADHYKEKFKECQRLQKQINKLSDQSANNNNVFTKKTGNQQKVNDASVNTDPATSASTVDVKPSPSAAEADFDIVTKGQVCEMTKEIADKTEKYNKCKQLLQDEKAKCNKYADELAKMELKWKEQVKIAENVKLELAEVQDNYKELKRSLENPAERKMEGQNSQSPQCFKTCSEQNGYVLTLSNAQPVLQYGNPYASQETRDGADGAFYPDEIQRPPVRVPSWGLEDNVVCSQPARNFSRPDGLEDSEDSKEDENVPTAPDPPSQHLRGHGTGFCFDSSFDVHKKCPLCELMFPPNYDQSKFEEHVESHWKVCPMCSEQFPPDYDQQVFERHVQTHFDQNVLNFD | Function: Ubiquitin-binding adapter that participates in inflammatory, antiviral and innate immune processes as well as selective autophagy regulation . Plays a key role in the negative regulation of NF-kappa-B and IRF3 signalings by acting as an adapter for the ubiquitin-editing enzyme A20/TNFAIP3 to bind and inactivate its substrates . Disrupts the interactions between the E3 ubiquitin ligase TRAF3 and TBK1/IKBKE to attenuate 'Lys63'-linked polyubiquitination of TBK1 and thereby IFN-beta production . Recruits also A20/TNFAIP3 to ubiquitinated signaling proteins TRAF6 and RIPK1, leading to their deubiquitination and disruption of IL-1 and TNF-induced NF-kappa-B signaling pathways . Inhibits virus-induced apoptosis by inducing the 'Lys-48'-linked polyubiquitination and degradation of MAVS via recruitment of the E3 ligase ITCH, thereby attenuating MAVS-mediated apoptosis signaling . As a macroautophagy/autophagy receptor, facilitates the xenophagic clearance of pathogenic bacteria such as Salmonella typhimurium and Mycobacterium tuberculosis . Upon NBR1 recruitment to the SQSTM1-ubiquitin condensates, acts as the major recruiter of RB1CC1 to these ubiquitin condensates to promote their autophagic degradation .
PTM: Phosphorylated in the C-terminal region by CHUK/IKKA leading to NF-kappa-B signaling down-regulation.
Sequence Mass (Da): 90877
Sequence Length: 789
Domain: The C-terminal UBZ-type zinc fingers function as ubiquitin-binding domains.
Subcellular Location: Cytoplasm
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P14079 | MAHFPGFGQSLLFGYPVYVFGDCVQGDWCPISGGLCSARLHRHALLATCPEHQITWDPIDGRVIGSALQFLIPRLPSFPTQRTSKTLKVLTPPITHTTPNIPPSFLQAMRKYSPFRNGYMEPTLGQHLPTLSFPDPGLRPQNLYTLWGGSVVCMYLYQLSPPITWPLLPHVIFCHPGQLGAFLTNVPYKRIEKLLYKISLTTGALIILPEDCLPTTLFQPARAPVTLTAWQNGLLPFHSTLTTPGLIWTFTDGTPMISGPCPKDGQPSLVLQSSSFIFHKFQTKAYHPSFLLSHGLIQYSSFHNLHLLFEEYTNIPISLLFNEKEADDNDHEPQISPGGLEPLSEKHFRETEV | Function: Transcriptional activator that governs the viral transcription from the 5'LTR via the recruitment of dimers of host phosphorylated CREB1. Together they bind cAMP response elements within the viral promoter and mediate high-level viral transcription. Increases host CREB1 O-GlcNAcylation to further increase 5'LTR transactivation. Modulates also the expression of cellular genes leading to the deregulation of T-cell proliferation, perturbing the integrity of cell cycle checkpoints, the DNA damage response and apopototic pathways. Acts as an ubiquitin E3 ligase and stimulates host IKK complex by catalyzing the assembly of free mixed-linkage polyubiquitin chains, resulting in constitutive activation of the transcription factor NF-kappa-B. Inhibits the host nonsense-mediated mRNA decay (NMD), a cellular process that can actively degrade mRNAs by interacting with host UPF1.
PTM: Phosphorylation at Thr-48 results in the loss of NF-kappa-B activation function. Phosphorylation at Thr-215 results in loss of CREB and NF-B responsive promoters activation. Phosphorylation at Thr-184 and Ser-336 have no effect on these Tax functions. Phosphorylation of either Ser-300 or Ser-301 is necessary for localization to nuclear bodies. Thr-48, Thr-184, Thr-215 and Ser-336 are highly phosphorylated, whereas Ser-300 or Ser-301 are only rarely phosphorylated (By similarity).
Sequence Mass (Da): 39513
Sequence Length: 353
Domain: The 48 N-terminal residues contain a non-canonical functional nuclear localization signal (NLS).
Subcellular Location: Host nucleus
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Q6C9I6 | MSHFGDHVGIDPAIMKQYSEHHNGSHDNDDKDKEDKEKQNTEAVAAAAVQLDASLLASGILDDFEKAKKEEEEANGNNNASNDQQNASDRHVGDMLEQHSQQHQQSQEHDTSYINTYIEDKVPLTSVLIPGDRRVSDREASDRIAATTRRVRLRWTQEETADLMEGCKVHGVGNWKKILTDPRFRFNNRTAVDLKDRFRTCFPEDYRRLYPNARSRKFGKKTNVMAVNDDLVKVNRKERRVFTPEEDERLLNGFMKHGPSWSNIQRDNELGLFERRSTDLRDRFRNAFPLEYAAAGFKARGPKRRPVVEATHGNTLQTIFSASDGSEMSPRKYHRVQEQMDRQPVMRVHPQAPMDQGVDRDHMTQQFTQELQPQAHSRKQQGGDGLKEEVFAAAQNQSYNNYYYQK | Function: Telomere-binding protein that mediates telomere clustering by promoting formation of head-to-head dimers of DNA molecules through the telomeric tracts. Binds specifically 5'-TTAGTCAGGG-3' repeats in subtelomeric regions.
Sequence Mass (Da): 46861
Sequence Length: 406
Domain: The presence of both Myb domains is required for high affinity telomeric DNA-binding.
Subcellular Location: Nucleus
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Q0CS99 | MPWIETKPGLWQRPIGDNEKFIKFIGDRSHQVGREHWSVTAGAAFTLNRDWSLSDLSSHCLNAWCAFRFDHPSIACTVEGDTVSYQTPSNEELASWANETFHIHDLSTTSDDLIAALKPSRYLTAHLLPGENRVILHAAHWRTDGYGALQLVHAFLDTLCKAVGCHSKAIQWGEEWRRLTPSIEEVLDLPLTATPEILEATKECLKTLAHTRGAVGTAPSGDKLAAPAGTRSAHLSLTTADTSAVMAACAERKISLLSAVHASCAALTWLEASSNDRDKHYTSTMRFSLRPHLPPPYSGPAYAAGLYTGGYMFPVPASQSWIENAKQYEKEYNTGITEDFLKCRRQYAVELIGILQRGAPPPDPPPSEVDISSVGDAEALVSPRFTHNGTILEVQSVDIGVETLTRQTYCFLWTFRGRLELHLVYNEAFYEPERAERMVRILAKTLQTELGLA | Function: Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of azaterrilone A and other azaphilones, a class of fungal metabolites characterized by a highly oxygenated pyrano-quinone bicyclic core and exhibiting a broad range of bioactivities . The first step of the pathway begins with the non-reducing polyketide synthase tazA that assembles one acetyl-CoA starter unit, five malonyl-CoA units, and catalyzes a series of Claisen condensations, methylation, PT-mediated cyclization, and finally releases the first hexaketide precursor through the R-domain. The tazA product then undergoes reduction on its terminal ketone and the following pyran-ring formation by yet undetermined enzyme(s). Dehydration and enoyl reduction, possibly involving the trans-enoyl reductase tazE leads to the next intermediate. TazD is predicted as an acetyltransferase and might catalyze the acetylation steps leading to the synthesis of azaterrilone A. Azaterrilone A is not the final product of the taz pathway and both the highly reducing polyketide synthase tazB and the dual enzyme tazHJ catalyze late steps of the pathway, leading to the production of the 2 final stereoisomers that contain additional polyketide modification whose structures have still to be determined (Probable).
Sequence Mass (Da): 50202
Sequence Length: 453
Pathway: Secondary metabolite biosynthesis.
EC: 2.3.2.-
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Q0CS94 | MTAEHDAAILPKPGGPLAVGKRATPEPGPNDVLIEVKAVALNPCDYYQRDYGMPPVPIYPAVIGGDAAGVVAKLGSSVTGGPVPGPGSRVIAFASSFYQNGSPDHGAFQKYALAQSEAVIPLPDNLSFEEGAVFPLAVLTALTAWTTIGIPLDTRYTPADKQAVLIWGASSSVGSFAVQSAKTLGFTVYATASPKHHELVKKLGADAVFDYKDSDVVSKIVDAVKKDGVYLHTAHCVVDGALQPTLDILKETKGDAFAKVAHSPVLPECHPTLDNTQITFNFPSMDEVVRTRISKLRRAVSRE | Function: Trans-enoyl reductase; part of the gene cluster that mediates the biosynthesis of azaterrilone A and other azaphilones, a class of fungal metabolites characterized by a highly oxygenated pyrano-quinone bicyclic core and exhibiting a broad range of bioactivities . The first step of the pathway begins with the non-reducing polyketide synthase tazA that assembles one acetyl-CoA starter unit, five malonyl-CoA units, and catalyzes a series of Claisen condensations, methylation, PT-mediated cyclization, and finally releases the first hexaketide precursor through the R-domain. The tazA product then undergoes reduction on its terminal ketone and the following pyran-ring formation by yet undetermined enzyme(s). Dehydration and enoyl reduction, possibly involving the trans-enoyl reductase tazE leads to the next intermediate. TazD is predicted as an acetyltransferase and might catalyze the acetylation steps leading to the synthesis of azaterrilone A. Azaterrilone A is not the final product of the taz pathway and both the highly reducing polyketide synthase tazB and the dual enzyme tazHJ catalyze late steps of the pathway, leading to the production of the 2 final stereoisomers that contain additional polyketide modification whose structures have still to be determined (Probable).
Sequence Mass (Da): 32019
Sequence Length: 303
Pathway: Secondary metabolite biosynthesis.
EC: 1.-.-.-
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Q0CSA3 | MPSNESTCLGSDRNMQTAWKLNASTPGFTPKKLRVVCIGAGLSGLTLAYKLKHERPMDFVDLRIYEKNHEVGGTWLDNVYPGVGCDIPSPSYVFPFEPNPDWSKFYVGGAEIQQYILRTTAKYGLKERIVFNTRLLKAEWNEDSAKWKLQLEQDGRVFDDETDVLINGTGCLSQWKWPDIEGLDCFKGKLLHSARWDPEYNWEGKRIAVIGNGSSALQLVPSLQPKAAKLVNYIRHPTWVSVNFCPDLTRDGMGSNFEFTEEEKQQFRDDPEMFFQYRKKVEHGVNTVLQMMISGSGEHKFLHETVEGLMRQRLADRPDLIDKMIPNYEIGCRRLSPGDGYLEALQAANARPSFANINRITPTGFETDEGEEEFDLIACATGFNTSYIPPFKMTGRGGRRLDVEWKDKPAAYFATCAAGFPNYFIFAGPNAPIGHGSVNRMIWFQADYMLNWVEKIATEDIRSVAVKDSAVRDFNEFAKENLKRFVWSKGCHAWYSKKTDGEDNIVTAMYPGSLLHFKVYLDKIRGEHFDIQYNTSNMFGFLGNGELALEREKDGDMAFYM | Cofactor: Binds 1 FAD per subunit.
Function: FAD-binding monooxygenase; part of the gene cluster that mediates the biosynthesis of azaterrilone A and other azaphilones, a class of fungal metabolites characterized by a highly oxygenated pyrano-quinone bicyclic core and exhibiting a broad range of bioactivities . The first step of the pathway begins with the non-reducing polyketide synthase tazA that assembles one acetyl-CoA starter unit, five malonyl-CoA units, and catalyzes a series of Claisen condensations, methylation, PT-mediated cyclization, and finally releases the first hexaketide precursor through the R-domain. The tazA product then undergoes reduction on its terminal ketone and the following pyran-ring formation by yet undetermined enzyme(s). Dehydration and enoyl reduction, possibly involving the trans-enoyl reductase tazE leads to the next intermediate. TazD is predicted as an acetyltransferase and might catalyze the acetylation steps leading to the synthesis of azaterrilone A. Azaterrilone A is not the final product of the taz pathway and both the highly reducing polyketide synthase tazB and the dual enzyme tazHJ catalyze late steps of the pathway, leading to the production of the 2 final stereoisomers that contain additional polyketide modification whose structures have still to be determined (Probable).
Sequence Mass (Da): 63906
Sequence Length: 561
Pathway: Secondary metabolite biosynthesis.
EC: 1.14.13.-
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Q8WQ47 | MRECISVHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGTGDDSFNTFFSETGSGKHVPRAVYVDLEPTVVDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIVDLVLDRIRKLADQCTGLQGFLIFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFAVYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLVTYAPVISSEKAYHEQLTVSEITNTCFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIAAIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGLDSTEADDTAGEEF | Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin tyrosine ligase (TTL), respectively.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 50038
Sequence Length: 450
Subcellular Location: Cytoplasm
EC: 3.6.5.-
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P10489 | MREAICIHIGQAGYQIGNACSQLFC | Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 2727
Sequence Length: 25
Subcellular Location: Cytoplasm
EC: 3.6.5.-
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P24635 | ICKRNLDIERPSYTNLNRLISQVVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLVTYAPIISAEKAYHEQLAVAEVTSACFEPANQMVKCDPRHGKYMACCMLYRGDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVLGGDLAKVQRAVCMLSNTTAVAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGLDTFEAEEEEGGDEY | Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin tyrosine ligase (TTL), respectively.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 26962
Sequence Length: 240
Subcellular Location: Cytoplasm
EC: 3.6.5.-
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P33628 | CWELYWLEHGIQPDGMMPSDTTVGVGDDAFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGAYRQLFHPEQLISGKEDAANNFARGHYTVGEEIVDLCLDRVRKLADNCTGL | Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 12573
Sequence Length: 113
Subcellular Location: Cytoplasm
EC: 3.6.5.-
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P14642 | MREVISIHVGQAGIQVGNACWELFCLEHGIQPDGQMPSDKASRANDDAFNTFFSETGAGKHVPRCVFVDLEPTVVDEVRTGTYRQLFHPEQLISGKEDAANNFARGHYTIGKEVIDVCLDRIRKLADNCTGLQGFLMFSAVGGGTGSGFGCLMLERLSVDYGKKSKLNFCCWPSPQVSTAVVEPYNSVLSTHSLLEHTDVAIMLDNEAIYDICRRNLDIERPTYTNLNRLIAQVISSLTASLRFDGALNVDVTEFQTNLVPYPRIHFMLSSYAPVVSAEKAYHEQLSVSEITNSAFEPANMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAVATIKTKRTIQFVDWCPTGFKCGINYQPPTVVPGGDLAKVMRAVCMISNSTAIAEVFSRMDQKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGIESNEAEGEDEGYEADY | Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin tyrosine ligase (TTL), respectively.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 50297
Sequence Length: 453
Subcellular Location: Cytoplasm
EC: 3.6.5.-
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P84549 | AIFVDLEPTVIDEVRSLDIERPTYTNLNRFDGAINVDVTEFQTNLVPYPR | Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 5767
Sequence Length: 50
Subcellular Location: Cytoplasm
EC: 3.6.5.-
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P10872 | MREVISIHVGQGGIQVGNACWELFCLEHGIQPDGQMPSDKTIGGGDDAFNTFFSETGAGKHVPRAVFLDLEPTVIDEVRTGTYRQLFHPEQLISGKEDAANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFNSVGGGTGSGLGSLLLERLSVDYGKKSKLGFTIYPSPQVSTAVVEPYNSILSTHSLLEHTDVAVMLDNEAIYDICRRNLDIERPTYTNLNRLIAQVISSLTASLRFDGALNVDITEFQTNLVPYPRIHFMLSSYAPIISAEKAYHEQLSVAEITNSAFEPANMMAKCDPRHGKYMACSMMYRGDVVPKDVNASIATIKTKRTIQFVDWCPTGFKVGINYQPSTVVPGGDLAKVMRAVCMISNSTAIAEVFSRLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGIETAEGEGEEEGY | Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin tyrosine ligase (TTL), respectively.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 49577
Sequence Length: 449
Subcellular Location: Cytoplasm
EC: 3.6.5.-
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P41351 | MREVISIHVGQGGIQVGNACWELFCLEHGIQPDGQMPSDKTIGGGDDAFNTFFSETGAGKHVPRAVFLDLEPTVIDEVRTGTYRQLFHPEQLISGKEDAANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFNSVGGGTGSGLGSLLLERLSVDYGKKSKLGFTIYPSPQVSTAVVEPYNSILSTHSLLEHTDVAVMLDNEAIYDICRRNLDIERPTYTNLNRLIAQVISSLTASLRFDGALNVDITEFQTNLVPYPRIHFMLSSYAPIISAEKAYHEQLSVAEITNSAFEPANMMAKCDPRHGKYMACSMMYRGDVVPKDVNASIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVMRAVCMISNSTAIAEVFSRLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGIETAEGEGEEEGY | Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin tyrosine ligase (TTL), respectively.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Sequence Mass (Da): 49587
Sequence Length: 449
Subcellular Location: Cytoplasm
EC: 3.6.5.-
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P13602 | MREIVHLQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEATGNKFVPRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDSKNMMAACDPRHGRYLTVAAIFRGRMSMKEVDEQMLNVQNKSSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATADEQGEFEEEEDEA | Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
PTM: Some glutamate residues at the C-terminus are polyglycylated, resulting in polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. The precise function of polyglycylation is still unclear.
Sequence Mass (Da): 49724
Sequence Length: 443
Domain: The MREI motif is common among all beta-tubulin isoforms and may be critical for tubulin autoregulation.
Subcellular Location: Cytoplasm
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Q9HA65 | MEGAGYRVVFEKGGVYLHTSAKKYQDRDSLIAGVIRVVEKDNDVLLHWAPVEEAGDSTQILFSKKDSSGGDSCASEEEPTFDPGYEPDWAVISTVRPQLCHSEPTRGAEPSCPQGSWAFSVSLGELKSIRRSKPGLSWAYLVLVTQAGGSLPALHFHRGGTRALLRVLSRYLLLASSPQDSRLYLVFPHDSSALSNSFHHLQLFDQDSSNVVSRFLQDPYSTTFSSFSRVTNFFRGALQPQPEGAASDLPPPPDDEPEPGFEVISCVELGPRPTVERGPPVTEEEWARHVGPEGRLQQVPELKNRIFSGGLSPSLRREAWKFLLGYLSWEGTAEEHKAHIRKKTDEYFRMKLQWKSVSPEQERRNSLLHGYRSLIERDVSRTDRTNKFYEGPENPGLGLLNDILLTYCMYHFDLGYVQGMSDLLSPILYVIQNEVDAFWCFCGFMELVQGNFEESQETMKRQLGRLLLLLRVLDPLLCDFLDSQDSGSLCFCFRWLLIWFKREFPFPDVLRLWEVLWTGLPGPNLHLLVACAILDMERDTLMLSGFGSNEILKHINELTMKLSVEDVLTRAEALHRQLTACPELPHNVQEILGLAPPAEPHSPSPTASPLPLSPTRAPPTPPPSTDTAPQPDSSLEILPEEEDEGADS | Function: Probable RAB GTPase-activating protein that inhibits RAB8A/B function. Reduces Rab8 recruitment to tubules emanating from the endocytic recycling compartment (ERC) and inhibits Rab8-mediated endocytic trafficking, such as that of transferrin receptor (TfR) . Involved in regulation of autophagy.
Sequence Mass (Da): 72670
Sequence Length: 648
Domain: The arginine and glutamine fingers are critical for the GTPase-activating mechanism, they pull out Rab's 'switch 2' glutamine and insert in Rab's active site.
Subcellular Location: Cytoplasmic vesicle
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Q2T9Q1 | MALRSARGDGPTSGRWDGGAEKGDFNAKRKKKVAEIYQALNSEPTDVAALRRMAISEGGLLTDEIRRKVWPKLLNVNTNDPPPISGKNLRQMSKDYQQVLLDVRRSLRRFPPGMPEEQREGLQEELIDIILLILERNPQLHYYQGYHDIVVTFLLVLGERLATSLVEKLSTHHLRDFMDPTMDNTKHILNYLMPIIDQVNPELHDFMQSAEVGTIFALSWLITWFGHVLSDFRHVVRLYDFFLACHPLMPIYFAAVIVLYREQEVLDCDCDMASVHHLLSQIPQDLPYETLISRAGDLFVQFPPSELAREAAAQPQAEKTAASTFKDFELASAQQRPDMVLRQRFRGLLRPDERTKDVLTKPRTNRFVKLAVMGLTVALGAAALAVVKSALEWAPKFQLQLFP | Function: GTPase-activating protein specific for Rab1 and Rab2 small GTPase families for which it can accelerate the intrinsic GTP hydrolysis rate by more than five orders of magnitude (By similarity). Involved in maintaining endoplasmic reticulum structure (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45913
Sequence Length: 403
Domain: The arginine and glutamine fingers are critical for the GTPase-activating mechanism, they pull out Rab's 'switch 2' glutamine and insert in Rab's active site.
Subcellular Location: Membrane
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Q96BZ9 | MALRSAQGDGPTSGHWDGGAEKADFNAKRKKKVAEIHQALNSDPTDVAALRRMAISEGGLLTDEIRRKVWPKLLNVNANDPPPISGKNLRQMSKDYQQVLLDVRRSLRRFPPGMPEEQREGLQEELIDIILLILERNPQLHYYQGYHDIVVTFLLVVGERLATSLVEKLSTHHLRDFMDPTMDNTKHILNYLMPIIDQVNPELHDFMQSAEVGTIFALSWLITWFGHVLSDFRHVVRLYDFFLACHPLMPIYFAAVIVLYREQEVLDCDCDMASVHHLLSQIPQDLPYETLISRAGDLFVQFPPSELAREAAAQQQAERTAASTFKDFELASAQQRPDMVLRQRFRGLLRPEDRTKDVLTKPRTNRFVKLAVMGLTVALGAAALAVVKSALEWAPKFQLQLFP | Function: GTPase-activating protein specific for Rab1 and Rab2 small GTPase families for which it can accelerate the intrinsic GTP hydrolysis rate by more than five orders of magnitude . Involved in maintaining endoplasmic reticulum structure .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45855
Sequence Length: 403
Domain: The arginine and glutamine fingers are critical for the GTPase-activating mechanism, they pull out Rab's 'switch 2' glutamine and insert in Rab's active site.
Subcellular Location: Membrane
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Q9D9I4 | MALRPSKGDGSAGRWDRGAGKADFNAKRKKKVAEIHQALNSDPIDLAALRRMAISEGGLLTDEIRCQVWPKLLNVNTSEPPPVSRKDLRDMSKDYQQVLLDVRRSLRRFPPGMPDEQREGLQEELIDIILLVLDRNPQLHYYQGYHDIVVTFLLVVGERLATSLVEKLSTHHLRDFMDPTMDNTKHILNYLMPIIDQVSPELHDFMQSAEVGTIFALSWLITWFGHVLMDFRHVVRLYDFFLACHPLMPIYFAAVIVLYREQEVLDCDCDMASVHHLLSQIPQDLPYETLISRAGDLFVQFPPSELAREAAAQQEAERTAASTFKDFELASTQQRPDMVLRQRFRGLLRPEARTKDVLTKPRTNRFVKLAVMGLTVALGAAALAVVKSALEWAPKFQLQLFP | Function: GTPase-activating protein specific for Rab1 and Rab2 small GTPase families for which it can accelerate the intrinsic GTP hydrolysis rate by more than five orders of magnitude (By similarity). Involved in maintaining endoplasmic reticulum structure (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45825
Sequence Length: 402
Domain: The arginine and glutamine fingers are critical for the GTPase-activating mechanism, they pull out Rab's 'switch 2' glutamine and insert in Rab's active site.
Subcellular Location: Membrane
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Q8IYX1 | MTTLSPENSLSARQSASFILVKRKPPIDKTEWDSFFDESGHLAKSRDFICVNILERGLHPFVRTEAWKFLTGYFSWQSSQDERLTVDSMRRKNYKALCQMYEKIQPLLENLHRNFTETRNNIARDIQKIYDKDPLGNVLIDKKRLEKILLLSYVCNTQAEYQQGFHEMMMLFQLMVEHDHETFWLFQFFLQKTEHSCVINIGVAKNLDMLSTLITFLDPVFAEHLKGKGAGAVQSLFPWFCFCFQRAFKSFDDVWRLWEVLLTGKPCRNFQVLVAYSMLQMVREQVLQESMGGDDILLACNNLIDLDADELISAACVVYAELIQKDVPQTLKDFFL | Function: Acts as a GTPase-activating protein for Rab family protein(s) . Essential for the establishment of male fertility, and is required for both the production of normal sperm number and sperm function (By similarity). Plays an important role in the formation of intact mitochondria, outer dense fibers and axoneme within the sperm tail (By similarity). Essential for sperm mitochondrial sheath formation and for the interactions of ARMC12 with VDAC2 and VDAC3 (By similarity). May be involved in acrosome formation and cytoskeletal reorganization during spermiogenesis, possibly by regulating RAB3A activity .
Sequence Mass (Da): 39221
Sequence Length: 336
Domain: The arginine and glutamine fingers are critical for the GTPase-activating mechanism, they pull out Rab's 'switch 2' glutamine and insert in Rab's active site.
Subcellular Location: Cytoplasmic vesicle
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Q9XTQ6 | MEPTASQGIQYLRGGVEWILKLLNLHILNVKHENKPLLFRLIDLKVYIPSSVSTVRWSSGASSYVILGEYRKMRSAVALLFLLVAYCGGVVHAGEIVAELYHTNVTVKWHTDYERQLVDFSIWFGASTPDVLFLGFSDFGDTNNSDVLMYYNSKKEIKDAYTNRDFKITSDLQQDFQLLRKRKDHIVVRRKLTTCDSRDYAFLPGTTQFYIAASWGSTNLVDIRDKRWVVDKKFGKVIEGPTDQPNIEEEPAALEKDVKVVIVNSNSPDPIPNVETTYKCIIRKMPFDTVNNMYHVVRMEPYVTPGNEHLVHHMEIFMCRDEVEEWSGSCNDPKKPPKSKSCSHVIAAWAMGEGPIHYPKEAGLPIGGKGKNAYVMVEIHYNNPELHKGVIDSSGFQFFVTGQLRKYDAGIMELGLIYSDANSVPPNQKAWAMNGYCPSQCTKNLPEEGINIFASQLHAHLTGRKLFTSQYRSGVRIGDVNRDEHYSPHWQHLQQLRPVVKVMPGDTLVTTCVYDTRKRSKVTFGGYRIVDEMCVNYIYYYPASDVEVCKSAISNSTLRAYFSERHGMDGKRMQISDMYSNVKDWGNGVDEEFYNVLNVGNMNMNCLKSNGEPFEFESKDSRQSWENMARPTFVSGSFITTRDRFQCPAINDMINFE | Cofactor: Binds 2 copper ions per subunit.
Function: Required for the conversion of tyramine to octopamine, a precursor of octapamine but probably itself a neurotransmitter . Involved in the regulation of egg laying, which is inhibited by tyramine . Due to its involvement in octopamine biosynthesis, also required for crtc-1-dependent regulation of AMPK-mediated longevity .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 74963
Sequence Length: 657
Subcellular Location: Membrane
EC: 1.14.17.-
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Q86B61 | MLKIPLQLSSQDGIWPARFARRLHHHHQLAYHHHKQEQQQQQQQQQQQQAKQKQKQNGVQQGRSPTFMPVMLLLLMATLLTRPLSAFSNRLSDTKLHEIYLDDKEIKLSWMVDWYKQEVLFHLQNAFNEQHRWFYLGFSKRGGLADADICFFENQNGFFNAVTDTYTSPDGQWVRRDYQQDCEVFKMDEFTLAFRRKFDTCDPLDLRLHEGTMYVVWARGETELALEDHQFALPNVTAPHEAGVKMLQLLRADKILIPETELDHMEITLQEAPIPSQETTYWCHVQRLEGNLRRRHHIVQFEPLIRTPGIVHHMEVFHCEAGEHEEIPLYNGDCEQLPPRAKICSKVMVLWAMGAGTFTYPPEAGLPIGGPGFNPYVRLEVHFNNPEKQSGLVDNSGFRIKMSKTLRQYDAAVMELGLEYTDKMAIPPGQTAFPLSGYCVADCTRAALPATGIIIFGSQLHTHLRGVRVLTRHFRGEQELREVNRDDYYSNHFQEMRTLHYKPRVLPGDALVTTCYYNTKDDKTAALGGFSISDEMCVNYIHYYPATKLEVCKSSVSEETLENYFIYMKRTEHQHGVHLNGARSSNYRSIEWTQPRIDQLYTMYMQEPLSMQCNRSDGTRFEGRSSWEGVAATPVQIRIPIHRKLCPNYNPLWLKPLEKGDCDLLGECIY | Cofactor: Binds 2 copper ions per subunit.
Function: Converts tyramine into octopamine, a neurotransmitter involved in ovulation and locomotion . Functions in an amine-mediated Bacc-dependent signaling pathway that negatively regulates acute ethanol sensitivity .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 77729
Sequence Length: 670
Subcellular Location: Membrane
EC: 1.14.17.-
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Q9UHD2 | MQSTSNHLWLLSDILGQGATANVFRGRHKKTGDLFAIKVFNNISFLRPVDVQMREFEVLKKLNHKNIVKLFAIEEETTTRHKVLIMEFCPCGSLYTVLEEPSNAYGLPESEFLIVLRDVVGGMNHLRENGIVHRDIKPGNIMRVIGEDGQSVYKLTDFGAARELEDDEQFVSLYGTEEYLHPDMYERAVLRKDHQKKYGATVDLWSIGVTFYHAATGSLPFRPFEGPRRNKEVMYKIITGKPSGAISGVQKAENGPIDWSGDMPVSCSLSRGLQVLLTPVLANILEADQEKCWGFDQFFAETSDILHRMVIHVFSLQQMTAHKIYIHSYNTATIFHELVYKQTKIISSNQELIYEGRRLVLEPGRLAQHFPKTTEENPIFVVSREPLNTIGLIYEKISLPKVHPRYDLDGDASMAKAITGVVCYACRIASTLLLYQELMRKGIRWLIELIKDDYNETVHKKTEVVITLDFCIRNIEKTVKVYEKLMKINLEAAELGEISDIHTKLLRLSSSQGTIETSLQDIDSRLSPGGSLADAWAHQEGTHPKDRNVEKLQVLLNCMTEIYYQFKKDKAERRLAYNEEQIHKFDKQKLYYHATKAMTHFTDECVKKYEAFLNKSEEWIRKMLHLRKQLLSLTNQCFDIEEEVSKYQEYTNELQETLPQKMFTASSGIKHTMTPIYPSSNTLVEMTLGMKKLKEEMEGVVKELAENNHILERFGSLTMDGGLRNVDCL | Function: Serine/threonine kinase that plays an essential role in regulating inflammatory responses to foreign agents . Following activation of toll-like receptors by viral or bacterial components, associates with TRAF3 and TANK and phosphorylates interferon regulatory factors (IRFs) IRF3 and IRF7 as well as DDX3X . This activity allows subsequent homodimerization and nuclear translocation of the IRFs leading to transcriptional activation of pro-inflammatory and antiviral genes including IFNA and IFNB . In order to establish such an antiviral state, TBK1 form several different complexes whose composition depends on the type of cell and cellular stimuli . Plays a key role in IRF3 activation: acts by first phosphorylating innate adapter proteins MAVS, STING1 and TICAM1 on their pLxIS motif, leading to recruitment of IRF3, thereby licensing IRF3 for phosphorylation by TBK1 . Phosphorylated IRF3 dissociates from the adapter proteins, dimerizes, and then enters the nucleus to induce expression of interferons . Thus, several scaffolding molecules including FADD, TRADD, MAVS, AZI2, TANK or TBKBP1/SINTBAD can be recruited to the TBK1-containing-complexes . Under particular conditions, functions as a NF-kappa-B effector by phosphorylating NF-kappa-B inhibitor alpha/NFKBIA, IKBKB or RELA to translocate NF-Kappa-B to the nucleus . Restricts bacterial proliferation by phosphorylating the autophagy receptor OPTN/Optineurin on 'Ser-177', thus enhancing LC3 binding affinity and antibacterial autophagy . Phosphorylates SMCR8 component of the C9orf72-SMCR8 complex, promoting autophagosome maturation . Phosphorylates ATG8 proteins MAP1LC3C and GABARAPL2, thereby preventing their delipidation and premature removal from nascent autophagosomes . Phosphorylates and activates AKT1 . Seems to play a role in energy balance regulation by sustaining a state of chronic, low-grade inflammation in obesity, wich leads to a negative impact on insulin sensitivity (By similarity). Attenuates retroviral budding by phosphorylating the endosomal sorting complex required for transport-I (ESCRT-I) subunit VPS37C . Phosphorylates Borna disease virus (BDV) P protein . Plays an essential role in the TLR3- and IFN-dependent control of herpes virus HSV-1 and HSV-2 infections in the central nervous system . Acts both as a positive and negative regulator of the mTORC1 complex, depending on the context: activates mTORC1 in response to growth factors by catalyzing phosphorylation of MTOR, while it limits the mTORC1 complex by promoting phosphorylation of RPTOR .
PTM: Autophosphorylation at Ser-172 activates the kinase, and is an essential step for virus-triggered signaling. Phosphorylated by IKBKB/IKKB at Ser-172. Phosphorylation requires homodimerization and ubiquitination at Lys-30 and Lys-401. Dephosphorylated at Ser-172 by PPM1B and this negatively regulates its role in mediating antiviral response.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 83642
Sequence Length: 729
Domain: Comprises A N-terminal kinase domain, a ubiquitin-like domain and a C-terminal coiled-coil region mediating homodimerization.
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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Q9LDG2 | MSKNSNVEENGGAKPICEALRRFKRSRLVFEPSLGVLGFFLVGVCLVCSFFFFDYRSVAKSYGLSDKSERFVWLKFDNISSSSSSSSNSSKRVGFLEESGSGCDVFDGDWVWDESYPLYQSKDCRFLDEGFRCSDFGRSDLFYTQWRWQPRHCNLPRFDAKLMLEKLRDKRLVFVGDSIGRNQWESLLCLLSSAVKNESLIYEINGSPITKHKGFLVFKFEEYNCTVEYYRSPFLVPQSRPPIGSPGKVKTSLKLDTMDWTSSKWRDADVLVLNTGHWWNEGKTTRTGCYFQEGEEVKLKMNVDDAYKRALNTVVKWIHTELDSNKTQVFFRTFAPVHFRGGDWKTGGTCHMETLPEIGTSLASSETWEQLKILRDVLSHNSNRSETVKVKLLNITAMAAQRKDGHPSLYYLGPHGPAPLHRQDCSHWCLPGVPDTWNELFYALFMKQEAPSSSKRVEEANSTGNVTMS | Function: 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).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 53649
Sequence Length: 469
Subcellular Location: Membrane
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Q9FGE9 | MELGSRRIYTTMPSKLRSSSSLLPRILLLSLLLLLFYSLILRRPITSNIASPPPCDLFSGRWVFNPETPKPLYDETCPFHRNAWNCLRNKRDNMDVINSWRWEPNGCGLSRIDPTRFLGMMRNKNVGFVGDSLNENFLVSFLCILRVADPSAIKWKKKKAWRGAYFPKFNVTVAYHRAVLLAKYQWQARSSAEANQDGVKGTYRVDVDVPANEWINVTSFYDVLIFNSGHWWGYDKFPKETPLVFYRKGKPINPPLDILPGFELVLQNMVSYIQREVPAKTLKFWRLQSPRHFYGGDWNQNGSCLLDKPLEENQLDLWFDPRNNGVNKEARKINQIIKNELQTTKIKLLDLTHLSEFRADAHPAIWLGKQDAVAIWGQDCMHWCLPGVPDTWVDILAELILTNLKTE | Function: 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).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 47142
Sequence Length: 407
Subcellular Location: Membrane
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Q9ZQR5 | MATTSHNKPSLFPLLSLLCFISIFLLLSLSKRASLSSPKTHRSATVFPPKPDGSLSPLSATCDFSEGSWIYDPNPRSTRYTSSCKEIFKGWNCIRNNKTNGFEISNWRWKPKHCDLPSFDPLKFLQSHRNTNIGFVGDSLNRNMFVSLFCMLKSVTGELKKWRPAGADRGFTFSQYNLTIAYHRTNLLARYGRWSANAKGGELESLGFKEGYRVDVDIPDSSWAKASSFHDILILNTGHWWWAPSKFDPVKSPMLFFEGGRPILPPIPPATGLDRVLNNMVNFVEKTKRPGGIIFFRTQSPRHFEGGDWDQGGTCQRLQPLLPGKVEEFFSVGNNGTNVEVRLVNQHLYNSLKSRSAFHVLDITRMSEYRADAHPAAAGGKNHDDCMHWCLPGLTDTWNDLFVATLHTIKAL | Function: 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).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 46462
Sequence Length: 412
Subcellular Location: Membrane
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Q0WPS0 | MFGGKSHILRGSVSLALIVLILLVIILLVSEENPLRDSLFEVKRQFSSSSSSSSSVCNFAKGKWVEDRKRPLYSGFECKQWLSSMWSCRIMGRPDFSFEGYRWQPEGCNMPQFDRFTFLTRMQNKTIAFIGDSLGRQQFQSLMCMASGGEDSPEVQNVGWEYGLVKAKGALRPDGWAYRFPTTNTTILYYWSASLSDLVPMNNTDPPSLTAMHLDRPPAFMRNYLHRFDVLVLNTGHHWNRGKIEGNHWVMHVNGTQVEGEYLKDIRNAKDFTIHSVAKWLDAQLPLHPRLKAFFRTISPRHFKNGDWNTGGNCNNTVPLSRGSEITGDDGSIDATVESAVNGTRIKILDITALSELRDEAHISGSKLKPRKPKKASNVTSTPTINDCLHWCLPGIPDTWNELFIAQI | Function: 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).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 46105
Sequence Length: 408
Subcellular Location: Membrane
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O80940 | MVQIVPHVANAHMVKTSRKGLLALVVVGVEECCPTRRCDLRDPNLVVDSNCLLSRSTHQSSLVEDSIIINHFRILNFNNRASIFLCLRIGVICSTQSKMYGGKSYILKGSVSLSLIILILLVTTLLVSAKNQPRISLIEVKTCNLAKGEWVEDKKRPLYSGFECKQWLSNIFSCRVMGRPDFSFEGYRWQPEGCNIPEFNRVNFLRRMQNKTIAFIGDSLGREQFQSLMCMATGGKESPEVQNVGSEYGLVIPKGAPRPGGWAYRFPTTNTTVLSYWSASLTDLVPMNNTDPPHLIAMHLDRPPAFIRNYLHRFHVLVLNTGHHWSRDKIEKNHWVMHVNGTRVEGGYFKNVENAKIFTIHSLVKWLDAQLPLHPRLKAFFTTISPRHEKCNNTIPLSRGSKITGEGGSLDTIVESAVNGTRVKILDITALSKLRDEAHIAGCKLKPKKASNVTSAPTFNDCLHWCLPGIPDTWNELLIAQL | Function: 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).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 54168
Sequence Length: 482
Subcellular Location: Membrane
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F4K5L5 | MNETFSATPRSMTIHRYRMKRGALRRRARDISVMLVVLVCATVVIWTWDRTPTSAFLPPESHYLKLQSEEKVEKLPTALNTETKDSYSSAIPFVNKEESKEDSSDNKDTEEEEEKQVEEVTVSNTNRGKIPTIEEKKGEHEVIASEPKYRKTPTREDFKLEKVKHEVAVGEGEATETTHIKETNSDPKSNILATDEERTDGTSTARITNQACNYAKGKWVVDNHRPLYSGSQCKQWLASMWACRLMQRTDFAFESLRWQPKDCSMEEFEGSKFLRRMKNKTLAFVGDSLGRQQFQSMMCMISGGKERLDVLDVGPEFGFITPEGGARPGGWAYRFPETNTTVLYHWSSTLCDIEPLNITDPATEHAMHLDRPPAFLRQYLQKIDVLVMNTGHHWNRGKLNGNKWVMHVNGVPNTNRKLAALGNAKNFTIHSTVSWVNSQLPLHPGLKAFYRSLSPRHFVGGEWNTGGSCNNTTPMSIGKEVLQEESSDYSAGRAVKGTGVKLLDITALSHIRDEGHISRFSISASRGVQDCLHWCLPGVPDTWNEILFAMI | Function: 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).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 62316
Sequence Length: 551
Subcellular Location: Membrane
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Q9FHM0 | MTLASPRVSNSKTTVLLFPRKVSSIAFAIGGLTSFVIFASLLLFTYPIGSSVTDYFYRTETTQNVQFHHSIHDPDRNPSPVSSSESPPVLTQDSDDKVLPKGSHDSNDVRLGEETNSGKSSNVSIDEEATQDHVETECDLYHGNWFYDPMGPLYTNNSCPLLTQMQNCQGNGRPDKGYENWRWKPSQCDLPRFDAKKFLELMRGKTLAFIGDSVARNQMESMMCLLWQVETPVNRGNRKMQRWYFRSSSVMIARMWSSWLVHQFNEPFGFATDGVTKLKLDQPDERIIEALPNFDVVVLSSGHWFAKQSVYILNDQIVGGQLWWPDKSKPEKINNVEAFGISVETIIKAMAKHPNYTGLTILRTWSPDHYEGGAWNTGGSCTGKVEPLPPGNLVTNGFTEIMHEKQATGFHRAVADDKLGNRSKKLKLMDITEAFGYRHDGHPGPYRSPDPKKITKRGPDGQPPPQDCLHWCMPGPVDTWNEMVLEIIRRDFEGRQSSPSS | Function: 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).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 56526
Sequence Length: 501
Subcellular Location: Membrane
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Q15170 | MDKPRKENEEEPQSAPKTDEERPPVEHSPEKQSPEEQSSEEQSSEEEFFPEELLPELLPEMLLSEERPPQEGLSRKDLFEGRPPMEQPPCGVGKHKLEEGSFKERLARSRPQFRGDIHGRNLSNEEMIQAADELEEMKRVRNKLMIMHWKAKRSRPYPI | Function: May be involved in transcriptional regulation. Modulates various viral and cellular promoters in a promoter context-dependent manner. For example, transcription from the FOS promoter is increased, while Rous sarcoma virus (RSV) long terminal repeat (LTR) promoter activity is repressed. Does not bind DNA directly.
PTM: Phosphorylation of Ser-38 and Ser-39 is critical for transcriptional repression.
Sequence Mass (Da): 18641
Sequence Length: 159
Subcellular Location: Nucleus
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Q3ZAB8 | MSEKYHSTVTRRDFMKRLGLAGAGAGALGAAVLAENNLPHEFKDVDDLLSAGKALEGDHANKVNNHPWWVTTRDHEDPTCNIDWSLIKRYSGWNNQGAYFLPEDYLSPTYTGRRHTIVDSKLEIELQGKKYRDSAFIKSGIDWMKENIDPDYDPGELGYGDRREDALIYAATNGSHNCWENPLYGRYEGSRPYLSMRTMNGINGLHEFGHADIKTTNYPKWEGTPEENLLIMRTAARYFGASSVGAIKITDNVKKIFYAKVQPFCLGPWYTITNMAEYIEYPVPVDNYAIPIVFEDIPADQGHYSYKRFGGDDKIAVPNALDNIFTYTIMLPEKRFKYAHSIPMDPCSCIAYPLFTEVEARIQQFIAGLGYNSMGGGVEAWGPGSAFGNLSGLGEQSRVSSIIEPRYGSNTKGSLRMLTDLPLAPTKPIDAGIREFCKTCGICAEHCPTQAISHEGPRYDSPHWDCVSGYEGWHLDYHKCINCTICEAVCPFFTMSNNSWVHNLVKSTVATTPVFNGFFKNMEGAFGYGPRYSPSRDEWWASENPIRGASVDIF | Cofactor: Binds 2 [4Fe-4S] clusters.
Function: Catalyzes the reductive dechlorination of trichloroethene (TCE) to cis-1,2-dichloroethene (DCE) and of cis-1,2-dichloroethene to chloroethene . The substrate specificity is broad, and the enzyme can dehalogenate various substrates, including 1,1-dichloroethene (1,1-DCE), 1,2-dichloroethane and 1,2-dibromoethane . A variety of other haloalkanes and haloalkenes containing three to five carbon atoms are dehalogenated at lower rates . Trans-1,2-dichloroethene (trans-DCE) and chloroethene are degraded at rates which are approximately 2 orders of magnitude lower . Titanium(III) citrate and methyl viologen can be used as reductants .
Catalytic Activity: AH2 + trichloroethene = (Z)-1,2-dichloroethene + A + chloride + H(+)
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 62156
Sequence Length: 554
Subcellular Location: Cell membrane
EC: 1.21.99.-
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D0ZE09 | MSSTDSVVAGQAKVTTWRKTDTRWVLGLFGTAIGAGVLFFPISAGIGGLLPIIFMLILAFPIAFFCHRALARLCLSGRSISDNITDTVDQHFGHVGGVVITFLYFFAICPLLWIYGVTITNTFIAFWQHQLLLPAINRGVVALAILLVMAFFIYFGKDLMVKVMGYLVFPFITCLVLISLSLIPYWTGDIFTSFDMHSLSLFGSHGILVTVWLGIAIMVFSFNFSPIVSSFVVSKREEYEADFGREYTEQKCAKIISRASVLMVVVVMFFAFSCLFTLSPQDMAQAKQQNIPILSYLANHFSSLGSGKSTYATVLEYGASIIALVAIFKSFFGHYLGTLEGLNGLIIKFGYHGEKSQAPMKKLNMISMVIIMGSTWVIAYINPNILDLIGAMGAPIIAALLCLLPMYAVWRVPALAKYKGKASNYFVTIIGLLTILNIVYQLM | Function: Involved in the import of threonine and serine into the cell, with the concomitant import of a proton (symport system).
Catalytic Activity: H(+)(in) + L-threonine(in) = H(+)(out) + L-threonine(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48853
Sequence Length: 443
Subcellular Location: Cell inner membrane
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Q8E8J1 | MKALSKLKAEKGIWLVDAPKPEMGHNDLLIKIKKTAICGTDMHIYNWDEWSQKTIPVPMVVGHEYVGEVVDIGQEVRGFNIGDRVSGEGHITCGHCRNCRAGRTHLCRNTSGVGVNREGSFAEYLVIPAFNAFKIPDDISDDLASIFDPFGNAVHTALSFDLVGEDVLITGAGPIGIMAAAVCRHVGARHVVITDVNEYRLELARKMGATRAVNVAQENLKDVMKELGMTEGFDVGLEMSGVPSAFRAMLDTMNHGGKIAMLGIPGGEMAIDWSKVIFKGLVIKGIYGREMFETWYKMASLIQSGLDISPIITHHYKIDDFQKGFDAMGSGQSGKVILSWD | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-amino-3-ketobutyrate.
Catalytic Activity: L-threonine + NAD(+) = (2S)-2-amino-3-oxobutanoate + H(+) + NADH
Sequence Mass (Da): 37255
Sequence Length: 341
Pathway: Amino-acid degradation; L-threonine degradation via oxydo-reductase pathway; glycine from L-threonine: step 1/2.
Subcellular Location: Cytoplasm
EC: 1.1.1.103
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P31212 | PFDAPGVIKGQGTIGTEINRQLKDIHAVFVPVGGGGLISGVAAYFTQVAPHTKIIGVEPYGAASMTLSLYEGHRVKLENVDTFADGVAVALVGEYTFAKCQELIDGMVLVRNDGISAAIKDVYDEGRNILETSGAVAIAGAAAYCEFYNIKNENIVAIASGANMDFSKLHKVTELAELGSDNEALLATFMIEQPGSFKTFAKLVGSMNITEVTYRFTSERKEALVLYRVDVDEKSDLEEMIKKLNSSNMKTFNFSHNELVAEHIKHLVGGSASISDEIFGEFIFPEKAGTLSTFLEAFSPRWNITLCRYRDQGDINGNVLVGFQVPQSEMDEFKSQADGLGYPYELDNSNEAFNIVVAE | Catalytic Activity: L-threonine = 2-oxobutanoate + NH4(+)
Sequence Mass (Da): 39088
Sequence Length: 359
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-oxobutanoate from L-threonine: step 1/1.
Subcellular Location: Plastid
EC: 4.3.1.19
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S4TEF7 | MLQTISLLPAYNKPPVATLLHPHRSSSSSPLPCGHVSPVTHGGLIMNPQKRLRSFSANMKCSSTNSIIDDTIIRNGQRIMMSEYFDVQLKVRDYELDQYGVVNNAAYASYCQHGCIELMESIGVSGDRISRTGDALAISELSIKFLSPLRGGDKFVMKVRYCRISAVRTYFEHKIFKLPNREPILEAKATTIWLNKKYRPTRMPLEITSLLDKFFTR | Function: 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).
Sequence Mass (Da): 24589
Sequence Length: 217
Subcellular Location: Plastid
EC: 3.1.2.-
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P0DN60 | MALEAQMTLRMFVLVAMASTVHVLSSSFSEDLGTVPLSKVFRSETRFTLIQSLRALLSRQLEAEVHQPEIGHPGFSDETSSRTGKRGGLGRCIHNCMNSRGGLNFIQCKTMCS | PTM: Contains 2 disulfide bonds.
Sequence Mass (Da): 12433
Sequence Length: 113
Domain: The cysteine framework is XIV (C-C-C-C).
Subcellular Location: Secreted
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P0CI09 | SCSSGCSDCNSDSCQCTLNQFTNSDSCCC | PTM: Contains 4 disulfide bonds.
Sequence Mass (Da): 3003
Sequence Length: 29
Domain: The cysteine framework is C-C-C-C-C-CCC.
Subcellular Location: Secreted
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S4TDL2 | MDLSSSPNHPITVVSTFASPFEGPPSVGDSNSSARKPISLWPGMYHSPVTNALWEARCKIFERLLDPPKDAPPQSELLTKTPSQSRTTILYNFSTDYILREQYRDPWNEVRIGKLLEDLDALAGTISVKHCSDDDSTTRPLLLVTASVDKIVLKKPISVDIDLKIVGAVIWVGRSSIEIQLEVSQSTKEGSNAADDVALSANFIFVARDSKTAKAAPVNRLSPETEQEKLLFDEAEARSSMRKRKRGDQERREFENGEANRLQTLLAEGRIFCDMPALADRDSILLRDTRQENSLICQPQQRNIHGRIFGGFLLHRAFELAFSTAYAFAGLVPYFLEIDHVDFXRPVDVGDFLRLKSCVLYTELHNPDQPLINIEVVAHVTRPELRSSEVSNTFYFTFTVRPEAKATKNGYRIRNVVPATEEEARRILERMDAEACI | Function: 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.
Sequence Mass (Da): 49163
Sequence Length: 437
Subcellular Location: Plastid
EC: 3.1.2.-
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S4TE15 | MLQTFSPSYKPLHLPISSLSLSSSSSSSASSVAFPVTRLLIPPRLRVLPNPRRRCSALPFDIRGGKGMSEFYEVELKVRDYELDQYGVVNNAVYASYCQHGRHELLESFGLSCDAVARNGDALALSELSLKFLAPLRSGDKFVVKVRLSGSSAARLYFDHLIFKLPNQEPILDAKGTAVWLDKNYRPVRIPPEVRSKLVQFLRNEES | Function: 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).
Sequence Mass (Da): 23158
Sequence Length: 207
Subcellular Location: Plastid
EC: 3.1.2.-
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S4TF94 | MMTPIGIRIRKQIPLSYHYSSIQALLSRFTPTPYNPISNSSSSTQTIPTQFHESQCTNPISRPTVFLFDPPPIRFTHTKSFSTDPSSLDFPSNQPPVVSTISSHHNISQPIDAGSSIRKPISLWPGMFNSPVTNALWEARSNMFEKYGEPTADPPSQSELVTKSPAQSRTSILYNLSSDYALREHYRNPWNMIRIGKLLEDLDALAGTIAFKHCTNEDGMSRPLLLVTASVDKMVLKKPISIDTDLSIVGAVTWVGRSSMEIQLQVLQTTHESSDPSDSVSLVANFTFVARDSKTGKSAVINQISPETGEEKLLWREADERNKMRKMKRKIQKDLELEKQYIERLNALLAEGRVFCDLPALADRNSILMKDTCLENSFICQPQQRNIYGRIFGGFLMRRAVELAFSTTYSFAGVVTHFLEVDHVDFLRPVDVGDFLRLKSCVLYTELQNPTEPLINVEVVAHVTRPELRSSEVSNKFYFTFSVGPEAVKDGLLVRNVVPATEEEARRVLERMDAETPHPHSQYENEI | Function: 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 . Active on acyl CoAs with short chains (propanoyl-CoA and butanoyl-CoA), branched short chains (2-methylpropanoyl-CoA, 2-methylbutanoyl-CoA and 3-methylbutanoyl-CoA) and medium chains (octanoyl-CoA) .
Catalytic Activity: 2-methylpropanoyl-CoA + H2O = 2-methylpropanoate + CoA + H(+)
Sequence Mass (Da): 59414
Sequence Length: 527
Subcellular Location: Mitochondrion
EC: 3.1.2.-
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P0CI21 | GLSQSGCQAFTGRWCVGCERLRSRVVWECSPKRVVNSI | PTM: Contains 2 disulfide bonds.
Sequence Mass (Da): 4256
Sequence Length: 38
Domain: The cysteine framework is XIV (C-C-C-C).
Subcellular Location: Secreted
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Q6UDH5 | MGESFDAFSLDEDMPMETNEKRKDGRDRGTRAQSAVVVQPVAASRHK | Function: Plays an important role in the cytoplasmic envelopment of tegument proteins and capsids during the assembly and egress processes. Participates also in viral entry at the fusion step probably by regulating the core fusion machinery.
Location Topology: Lipid-anchor
Sequence Mass (Da): 5252
Sequence Length: 47
Subcellular Location: Virion tegument
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Q9E6Q3 | MFAVSAMRRRRRRILAECRTREAVYKERTLELLSQGVETDDPEFIEVFTSARNAHSDYKAQLRSNMRLEATDRKTKIIQRHIDEQLDRRLILDINRKLLNPKLQLQLDQTEEAILEKEDILAQTIDDITLNDSITNTDELDEESEALLTKWILNQKTKKRPTVAKTAIAPTAHGLQTKVSRNVFITGKDDLVQPTDLGQPSTHEVITCTSRERIIHPDGIHTEIYTTEDVSPTILDDVSDSCV | Function: Contributes to the nuclear transport of the viral transcriptional activator VP16 homolog during the early phase of infection. Therefore, participates indirectly in the regulation of the immediate-early gene expression. Additionally, seems to be important for efficient nuclear targeting of capsids (By similarity).
PTM: Phosphorylated.
Sequence Mass (Da): 27861
Sequence Length: 243
Subcellular Location: Virion tegument
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P04291 | MDRDAAHAALRRRLAETHLRAEIYKDQTLQLHREGVSTQDPRFVGAFMAAKAAHLELEARLKSRARLEMMRQRATCVKIRVEEQAARRDFLTAHRRYLDPALGERLDAVDDRLADQEEQLEEAATNASLWGDGDLAEGWMSPADSDLLVMWQLTSAPKVHANGPSRIGSHPTYTPTPTGPPGAPAAPLSRTPPSPAPPTGPATDPASASGFARDYPDGE | Function: Contributes to the nuclear transport of the viral transcriptional activator VP16 during the early phase of infection. Therefore, participates indirectly in the regulation of the immediate-early gene expression. Additionally, seems to be important for efficient nuclear targeting of capsids. The UL51-UL14 complex regulates final viral envelopment for efficient viral replication .
PTM: Phosphorylated.
Sequence Mass (Da): 23934
Sequence Length: 219
Subcellular Location: Virion tegument
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P89437 | MSRDASHAALRRRLAETHLRAEVYRDQTLQLHREGVSTQDPRFVGAFMAAKAAHLELEARLKSRARLEMMRQRATCVKIRVEEQAARRDFLTAHRRYLDPALSERLDAADDRLADQEEQLEEAAANASLWGDGDLADGWMSPGDSDLLVMWQLTSAPKVHTDAPSRPGSRPTYTPSAAGRPDAQAAPPPETAPSPEPAPGPAADPASGSGFARDCPDGE | Function: Contributes to the nuclear transport of the viral transcriptional activator VP16 during the early phase of infection. Therefore, participates indirectly in the regulation of the immediate-early gene expression. Additionally, seems to be important for efficient nuclear targeting of capsids (By similarity).
PTM: Phosphorylated.
Sequence Mass (Da): 23871
Sequence Length: 219
Subcellular Location: Virion tegument
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P36338 | MDAARDGRPERRRAVSGTYRTHPFQRPSARRSAGRPARCGRRGRGAPRVRRPRPYFQRPPDEDTSEDENVYDYIDGDSSDSADDYDSDYFTANRGPNHGAGDAMDTDAPPERAPEGGAPQDYLTAHLRAIEVLPESAPHRSLLERTARTVYAQQFPPRDLSAGSKAPAQRARRSLRGFPRGGGGGQEPGPDDEGDDAADLREDLVPDEAYAHLERDERLSEGPPLLNMEAAAAAAGERSVVEELFTYAPAQPQVEVPLPRILEGRVRPSAFFAQMSLDALCRTPPNDQRVARERRAWEMAGTPHGLLITTWSTVDPEFSIGGMYVGAPEGTRPRLVWRRAMKQAMALQYRLGVGGLCRAVDGAACRPLRRCSFWRDALLRECATAIFCRGRGARAAPRRLPRPAVGLLAATQFTPPDASPHATLFRGSMGSLIYWHELRVMLTAVPALCARYAGAGLQSAELYLLALRHSEAPGYTANERYALSAYLTLFVALAERGLRWLYLAGAHLLGPHPTAAAFREVRAKIPYERLPLGSATLHDAEVETVDSATFQEALAFSALAHVYGEAYVAVRTATTLLMAEYAVHAERRDVRQMTAAFLGVGLIAQRLMGSLNLLLNCVAGAAVYGGRRVTVREGTLARYSLLADAALPLVRPVFLVEFREARDGVMRELRLRPVASPPLAGKRRVMELYLSLDSIEALVGREPLGSRPVLGPLVDIAEALADHPHLVTGDGRGPRLGGR | Function: Tegument protein that can bind to various RNA transcripts. Plays a role in the attenuation of selective viral and cellular mRNA degradation by modulating the activity of host shutoff RNase UL41/VHS. Also plays a role in the primary envelopement of virions in the perinuclear space, probably by interacting with two nuclear egress proteins UL31 and UL34.
PTM: Monoubiquitinated.
Sequence Mass (Da): 80757
Sequence Length: 739
Domain: The nuclear export signal is CRM1-dependent.
Subcellular Location: Virion tegument
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Q9Y4R8 | MEPAPSEVRLAVREAIHALSSSEDGGHIFCTLESLKRYLGEMEPPALPREKEEFASAHFSPVLRCLASRLSPAWLELLPHGRLEELWASFFLEGPADQAFLVLMETIEGAAGPSFRLMKMARLLARFLREGRLAVLMEAQCRQQTQPGFILLRETLLGKVVALPDHLGNRLQQENLAEFFPQNYFRLLGEEVVRVLQAVVDSLQGGLDSSVSFVSQVLGKACVHGRQQEILGVLVPRLAALTQGSYLHQRVCWRLVEQVPDRAMEAVLTGLVEAALGPEVLSRLLGNLVVKNKKAQFVMTQKLLFLQSRLTTPMLQSLLGHLAMDSQRRPLLLQVLKELLETWGSSSAIRHTPLPQQRHVSKAVLICLAQLGEPELRDSRDELLASMMAGVKCRLDSSLPPVRRLGMIVAEVVSARIHPEGPPLKFQYEEDELSLELLALASPQPAGDGASEAGTSLVPATAEPPAETPAEIVDGGVPQAQLAGSDSDLDSDDEFVPYDMSGDRELKSSKAPAYVRDCVEALTTSEDIERWEAALRALEGLVYRSPTATREVSVELAKVLLHLEEKTCVVGFAGLRQRALVAVTVTDPAPVADYLTSQFYALNYSLRQRMDILDVLTLAAQELSRPGCLGRTPQPGSPSPNTPCLPEAAVSQPGSAVASDWRVVVEERIRSKTQRLSKGGPRQGPAGSPSRFNSVAGHFFFPLLQRFDRPLVTFDLLGEDQLVLGRLAHTLGALMCLAVNTTVAVAMGKALLEFVWALRFHIDAYVRQGLLSAVSSVLLSLPAARLLEDLMDELLEARSWLADVAEKDPDEDCRTLALRALLLLQRLKNRLLPPASP | Function: Regulator of the DNA damage response (DDR). Part of the TTT complex that is required to stabilize protein levels of the phosphatidylinositol 3-kinase-related protein kinase (PIKK) family proteins. The TTT complex is involved in the cellular resistance to DNA damage stresses, like ionizing radiation (IR), ultraviolet (UV) and mitomycin C (MMC). Together with the TTT complex and HSP90 may participate in the proper folding of newly synthesized PIKKs. Promotes assembly, stabilizes and maintains the activity of mTORC1 and mTORC2 complexes, which regulate cell growth and survival in response to nutrient and hormonal signals. May be involved in telomere length regulation.
PTM: Hydroxylation by PHD3 is required for a proper interaction with ATR, and activation of the ATR/CHK1/p53 pathway following DNA damage.
Sequence Mass (Da): 91747
Sequence Length: 837
Subcellular Location: Cytoplasm
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P03707 | MEVNKKQLADIFGASIRTIQNWQEQGMPVLRGGGKGNEVLYDSAAVIKWYAERDAEIENEKLRREVEELRQASEADLQPGTIEYERHRLTRAQADAQELKNARDSAEVVETAFCTFVLSRIAGEIASILDGLPLSVQRRFPELENRHVDFLKRDIIKAMNKAAALDELIPGLLSEYIEQSG | Function: The small subunit is responsible for the binding to multiple recognition elements within the packaging initiation site cos . The terminase lies at a unique vertex of the procapsid and is composed of two subunits, a small terminase subunit involved in viral DNA recognition (binding to packaging sequence cos), and a large terminase subunit possessing endonucleolytic, ATPase and helicase activities (DNA maturation and packaging) (Probable). The terminase binds, cooperatively with the host factor IHFA/IHFB, to the cos site at the junction of adjacent viral genomes in the concatemeric DNA . The endonuclease and helicase activities of the large subunit cleave the viral DNA generating 5'overhangs of 12 bp in length (Probable). The terminase remains bound to the left end of the genome to be packaged, forming a stable DNA-terminase complex (Probable). In a reaction facilitated by the viral assembly catalyst gpFI, the DNA-terminase complex binds to the portal of the procapsid and the terminase packages the viral DNA into the procapsid until the next cos site on the concatemer reaches the complex (Probable). The downstream cos site is then cut generating the mature right end of the genome, the heterotrimer undocks from the DNA-filled head and remains bound to the left end of concatemer's next genome (Probable).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 20441
Sequence Length: 181
Domain: The N-terminus contains a winged helix-turn-helix (wHTH) that binds the viral DNA (Probable). The N-terminus also contains an ATPase site that regulates DNA binding activity . The central part contains a region for the self-interaction . the C-terminus contains region of interaction with the terminase large subunit (Probable).
Subcellular Location: Host cytoplasm
EC: 3.6.4.-
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A0A0C3FBR2 | MPSQSLTIRLPKFEETFSVFPDNGLNPHYANSRAESRAWINQYHHAVCGPNMRTFMDKCNFELAGALFYPYANEAGLRATMDLVNLLWLYDELTDTKTETEAVNAAHIVACALREPDFDDGTWICSMIKDFNQRHISKAGPNTAYRFIYNFCNYVEAVGTEAGLRAKNEILDITTYISFRRETSALRLTFDLVQYCLGIDLPQYVHDDPVFASGYNAAMDLVCWTNDLFSYNREQAKGHAGANVVTVIMKSKGVDIQSAVDFVGGYCEALTSQLVEARRILLSRSHRVYSKDAVRILEAFGDFVRGNDQWSFASERYFGQKNKVVKESRIVEIITPFSDLIAINE | Function: Terpene cyclase that catalyzes the cyclization of farnesyl diphosphate (FPP) to various sesquiterpenes, including beta-elemene, viridiflorene and gamma-cadinene . Gamma-cadinene is the major product of PILCRDRAFT_825684 .
Catalytic Activity: (2E,6E)-farnesyl diphosphate = diphosphate + viridiflorene
Sequence Mass (Da): 39099
Sequence Length: 345
Domain: The DDXXD motif is important for the catalytic activity, presumably through binding to Mg(2+).
EC: 4.2.3.-
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P56587 | ALCNCNRIIIPHMCWKKCGKK | Function: Presynaptic neurotoxin that blocks the inwardly rectifying Kir1.1/KCNJ1 and Kir3.1/3.4 (KCNJ3/KCNJ5) potassium channels with high affinity by binding to the M1-M2 linker region of these channels in a 1:1 stoichiometry. It may block the potassium channel pore by occluding its alpha helix into the channel vestibule. Tertiapin-Q also inhibits calcium-activated large conductance BK-type (KCNMA) potassium channels in a concentration-, and voltage-dependent manner, in addition to inhibiting Kir3.1/3.2 (KCNJ3/KCNJ6) heteromultimers potassium channels. It can prevent dose-dependently acetylcholine(ACh)-induced atrioventricular blocks in mammalian hearts, as KCNJ3/KCNJ5 channels (also named I(KACh), because these channels are activated by ACh) are found in mammalian myocytes. Interacts specifically with calmodulin in the presence of calcium.
PTM: Oxidation of Met-13 results in the loss of biological activity.
Sequence Mass (Da): 2460
Sequence Length: 21
Subcellular Location: Secreted
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Q3U132 | MEASVLSPTSWEKRRAWLRQSRNWQTQVLEEEAAAALQDALDPEPSSLDDVFQEGNPINKIEDWLQGCGCRDTEEGLSEESGQSNYSGYSSHGTSFEDDLSLGAEATLLSTNGNLFSRNFLQTPRLCQLLDLGSSLASSSMTGGTNKTSSSISEILDQVQEDAEDILFSLGFGHENHKDTSRIPARFFSNPSQAKGINFQLFLKSQVQRMEMEDPCLMLASRFKQVQTLAVTADAFFCLYSYVSKTPVQKFTPSNMFWNFDPTDVPSIRILAPEPEPYSPRERLRRAISKMCLYTGSRDRLSSSYNNPKKNSLDQIVWEVMDRVKGEKIQQDPEHRQALGEESVPPIQNTNPSTSSLPCVSYPKEETQGDMCHAHALARPGPQYHINSTQVRRQLWVLQDINEKPRSAENESPWERKSKARKNLFQRVPVDKNIKSLNLPTIQQKQNQGQARHELTNL | Function: May play a role in the regulation of inositol 1,4,5-trisphosphate receptor-mediated Ca(2+) release and mitochondrial Ca(2+) uptake via the mitochondria-associated endoplasmic reticulum membrane (MAM) compartment (By similarity). Required for the development and maturation of T-cells, its function being essential for the late stages of thymocyte development. Plays a role in T-cell antigen receptor (TCR)-mediated activation of the ERK and NFAT signaling pathways, possibly by serving as a scaffolding protein that promotes the assembly of the LAT signalosome in thymocytes.
PTM: May be phosphorylated in response to store-operated Ca(+2) entry.
Sequence Mass (Da): 51768
Sequence Length: 458
Subcellular Location: Cytoplasm
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