ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q9Z0J5 | MAAIVAALRGSSGRFRPQTRVLTRGTRGAAGAASAAGGQQNFDLLVIGGGSGGLACAKEAAQLGRKVAVADYVEPSPRGTKWGLGGTCVNVGCIPKKLMHQAALLGGMIRDAQHYGWEVAQPVQHNWKAMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVNEHTVHGVDKAGKVTQLSAKHIVIATGGRPKYPTQVKGALEHGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTVMMRSVPLRGFDQQMASLVTEHMESHGTRFLKGCVPSLIRKLPTNQLQVTWEDLASGKEDVGTFDTVLWAIGRVPETRNLNLEKAGVNTNPKNQKIIVDAQEATSVPHIYAIGDVAEGRPELTPTAIKAGKLLAQRLFGKSSTLMNYSNVPTTVFTPLEYGCVGLSEEEAVALHGQEHIEVYHAYYKPLEFTVADRDASQCYIKMVCMREPPQLVLGLHFLGPNAGEVTQGFALGIQCGASYAQVMQTVGIHPTCSEEVVKLHISKRSGLDPTVTGCUG | Function: Involved in the control of reactive oxygen species levels and the regulation of mitochondrial redox homeostasis (By similarity). Maintains mitochondrial thioredoxin in a reduced state. May play a role in redox-regulated cell signaling.
Catalytic Activity: [thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide + H(+) + NADPH
Sequence Mass (Da): 56575
Sequence Length: 526
Subcellular Location: Mitochondrion
EC: 1.8.1.9
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Q86VQ6 | MERSPPQSPGPGKAGDAPNRRSGHVRGARVLSPPGRRARLSSPGPSRSSEAREELRRHLVGLIERSRVVIFSKSYCPHSTRVKELFSSLGVECNVLELDQVDDGARVQEVLSEITNQKTVPNIFVNKVHVGGCDQTFQAYQSGLLQKLLQEDLAYDYDLIIIGGGSGGLSCAKEAAILGKKVMVLDFVVPSPQGTSWGLGGTCVNVGCIPKKLMHQAALLGQALCDSRKFGWEYNQQVRHNWETMTKAIQNHISSLNWGYRLSLREKAVAYVNSYGEFVEHHKIKATNKKGQETYYTAAQFVIATGERPRYLGIQGDKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGFGLDVTVMVRSILLRGFDQEMAEKVGSYMEQHGVKFLRKFIPVMVQQLEKGSPGKLKVLAKSTEGTETIEGVYNTVLLAIGRDSCTRKIGLEKIGVKINEKSGKIPVNDVEQTNVPYVYAVGDILEDKPELTPVAIQSGKLLAQRLFGASLEKCDYINVPTTVFTPLEYGCCGLSEEKAIEVYKKENLEIYHTLFWPLEWTVAGRENNTCYAKIICNKFDHDRVIGFHILGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTLEITKSSGLDITQKGCUG | Cofactor: Binds 1 FAD per subunit.
Function: Displays thioredoxin reductase, glutaredoxin and glutathione reductase activities. Catalyzes disulfide bond isomerization. Promotes disulfide bond formation between GPX4 and various sperm proteins and may play a role in sperm maturation by promoting formation of sperm structural components (By similarity).
Catalytic Activity: [thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide + H(+) + NADPH
Sequence Mass (Da): 70683
Sequence Length: 643
Domain: The N-terminal glutaredoxin domain does not contain the C-X-X-C redox-active motif normally found in glutaredoxins but activity may be mediated through a single cysteine. The C-terminal Cys-Sec motif of one subunit of the homodimer may transfer electrons from the thiol-disulfide center to the glutaredoxin domain of the other subunit (By similarity).
Subcellular Location: Cytoplasm
EC: 1.8.1.9
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Q99MD6 | MEKPPSPPPPPRAQTSPGLGKVGVLPNRRLGAVRGGLMSSPPGRRARLASPGTSRPSSEAREELRRRLRDLIEGNRVMIFSKSYCPHSTRVKELFSSLGVVYNILELDQVDDGASVQEVLTEISNQKTVPNIFVNKVHVGGCDRTFQAHQNGLLQKLLQDDSAHDYDLIIIGGGSGGLSCAKEAANLGKKVMVLDFVVPSPQGTTWGLGGTCVNVGCIPKKLMHQAALLGHALQDAKKYGWEYNQQVKHNWEAMTEAIQSHIGSLNWGYRVTLREKGVTYVNSFGEFVDLHKIKATNKKGQETFYTASKFVIATGERPRYLGIQGDKEYCITSDDLFSLPYCPGCTLVVGASYVGLECAGFLAGLGLDVTVMVRSVLLRGFDQEMAEKVGSYLEQQGVKFQRKFTPILVQQLEKGLPGKLKVVAKSTEGPETVEGIYNTVLLAIGRDSCTRKIGLEKIGVKINEKNGKIPVNDVEQTNVPHVYAIGDILDGKPELTPVAIQAGKLLARRLFGVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAIEMYKKENLEVYHTLFWPLEWTVAGRDNNTCYAKIICNKFDNERVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTLEITKSSGLDITQKGCUG | Cofactor: Binds 1 FAD per subunit.
Function: Displays thioredoxin reductase, glutaredoxin and glutathione reductase activities. Catalyzes disulfide bond isomerization. Promotes disulfide bond formation between GPX4 and various sperm proteins and may play a role in sperm maturation by promoting formation of sperm structural components.
Catalytic Activity: [thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide + H(+) + NADPH
Sequence Mass (Da): 71319
Sequence Length: 652
Domain: The N-terminal glutaredoxin domain does not contain the C-X-X-C redox-active motif normally found in glutaredoxins but activity may be mediated through a single cysteine. The C-terminal Cys-Sec motif of one subunit of the homodimer may transfer electrons from the thiol-disulfide center to the glutaredoxin domain of the other subunit.
Subcellular Location: Cytoplasm
EC: 1.8.1.9
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D4APQ6 | MGVQRLALALIAFTSALTSVIAAPIVIEQPPLGPEHRYDAIVIGGGPSGLSALSSLGRVRRHVLLFDEGIYRNGATRHIHDMLTNDGVEPKVFRAKARQQISRYTSTSIKDVKVTKIKKVFEHGGRKYFFQVTDKTGAMYTASKVVLGTGVLDVLPGTPGLQENFGKGIYWCPWCDGWEHRDQPLGILGPLRHVMDSVYELETLNNDIIAFVNGTEHSVEDILYLNRKYPHWRQQLKHYNVQINNKMVSSIDRLQDGSKHQDKKTWQEFDKFRVNFNDGTSVERSVFITNFPTEQHSDLPDQLGLARDPIHKNKIKVNFKGMRASVPGVFVVGDANNDGSTNGNHAMFSGKRAAVALHVELEQERAEAALGKRDESFSAEQVENEALKLIGRDTEELEELWGRK | Cofactor: Binds 1 FAD per subunit.
Catalytic Activity: [thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide + H(+) + NADPH
Sequence Mass (Da): 45299
Sequence Length: 404
Subcellular Location: Secreted
EC: 1.8.1.9
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P61076 | MNNVISFIGNSSNKYFQINQLHFIRIINKNIHSKNNLINSNSSYNVFYNKYFIKNTFQNKNKLSSIYSKLNFSIKNMCKDKNEKKNYEHVNANEKNGYLASEKNELTKNKVEEHTYDYDYVVIGGGPGGMASAKEAAAHGARVLLFDYVKPSSQGTKWGIGGTCVNVGCVPKKLMHYAGHMGSIFKLDSKAYGWKFDNLKHDWKKLVTTVQSHIRSLNFSYMTGLRSSKVKYINGLAKLKDKNTVSYYLKGDLSKEETVTGKYILIATGCRPHIPDDVEGAKELSITSDDIFSLKKDPGKTLVVGASYVALECSGFLNSLGYDVTVAVRSIVLRGFDQQCAVKVKLYMEEQGVMFKNGILPKKLTKMDDKILVEFSDKTSELYDTVLYAIGRKGDIDGLNLESLNMNVNKSNNKIIADHLSCTNIPSIFAVGDVAENVPELAPVAIKAGEILARRLFKDSDEIMDYSYIPTSIYTPIEYGACGYSEEKAYELYGKSNVEVFLQEFNNLEISAVHRQKHIRAQKDEYDLDVSSTCLAKLVCLKNEDNRVIGFHYVGPNAGEVTQGMALALRLKVKKKDFDNCIGIHPTDAESFMNLFVTISSGLSYAAKGGCGGGKCG | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the transfer of electrons from NADPH to thioredoxins TRX1, TRX2 and TRX3, which in turn act as reductants of disulfide containing proteins . Able to reduce nitroglutathione (GSNO), a compound involved in the transport of nitric oxide (NO); however, TRX1 is more efficient in reducing GSNO . Has no catalytic activity towards oxidized glutathione (GSSG) .
Catalytic Activity: [thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide + H(+) + NADPH
Sequence Mass (Da): 68698
Sequence Length: 617
Subcellular Location: Mitochondrion
EC: 1.8.1.9
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P35035 | MSNKIAILLAVLVAVVACAEAQANQRHRLVRPSPSFSPRPRYAVGQRIVGGFEIDVSDAPYQVSLQYNKRHNCGGSVLSSKWVLTAAHCTAGASPSSLTVRLGTSRHASGGTVVRVARVVQHPKYDSSSIDFDYSLLELEDELTFSDSVQPVGLPKQDETVKDGTMTTVSGWGNTQSAAESNAVLRAANVPTVNQKECNKAYSEFGGVTDRMLCAGYQQGGKDACQGDSGGPLVADGKLVGVVSWGYGCAQAGYPGVYSRVAVVRDWVRENSGV | Function: Major function may be to aid in digestion of the blood meal.
Catalytic Activity: Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.
Sequence Mass (Da): 29057
Sequence Length: 274
Subcellular Location: Secreted
EC: 3.4.21.4
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P06871 | MKTFIFLALLGATVAFPIDDDDKIVGGYTCSRNSVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSRIQVRLGEYNIAVSEGGEQFINAAKIIRHPRYNANTIDNDIMLIKLSSPATLNSRVSAIALPKSCPAAGTQCLISGWGNTQSIGQNYPDVLQCLKAPILSDSVCRNAYPGQISSNMMCLGYMEGGKDSCQGDSGGPVVCNGELQGVVSWGAGCAQKGKPGVSPKVCKYVSWIQQTIAAN | Cofactor: Binds 1 Ca(2+) ion per subunit.
Catalytic Activity: Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.
Sequence Mass (Da): 26170
Sequence Length: 246
Subcellular Location: Secreted
EC: 3.4.21.4
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B9MKR8 | MLVLGIETSCDETSAAIVEDGRKILSNVIYSQIDIHYQFGGVVPEIASRKHVEKISYVVDMAFKQAGLTIDDIDGIAATYGPGLVGSLLVGLSFAKALSYAKRLPFVAVNHIEGHIYANFITYPQLTPPLIVLVVSGGHTNLIILKDFEEYEVVGKTRDDAAGEAFDKIARYLGLGYPGGPAIDKIAKQGDEDKYKYPVADVGGYNFSFSGLKSAVINHVHGLWQRGEEFKIEDVAASFQKTVVSILVEKTINLSLETNIRKIAVAGGVAANSKLRSEFYKKCAEHNIEFFVPEFKYCTDNAAMIASCGYFKLQKGIVSSYRENAVPYINLVSKKS | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
Catalytic Activity: adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA
Sequence Mass (Da): 36753
Sequence Length: 336
Subcellular Location: Cytoplasm
EC: 2.3.1.234
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Q8RC98 | MAKDIVILGIETSCDETAAGVVKNGKEVLSNVIYSQINVHKKYGGVVPEIASRKHIEAISFVVEEALNEAKLSLDEVDAIAATYGPGLVGPLLVGLSYGKALAYAKGKPFIGVNHIDGHIAANYIGGNLTPPFVCLVASGGHSHIVYVKDYGEYEVMGKTLDDAAGEAFDKVARALGLGYPGGPAIEKAAKLGNMEAIEFPKSFMEEGNFDFSFSGVKTAVLNYLNRQKQKGEEVNIYDVAASFQRNIVEVLVKKLVEAARFKNVSKVSIAGGVASNGFLRQKLEEDAKKFGLSVYYPEKIYCTDNGAMIAAAAYYDFVKGKFSGMDLNAIPYLKIGESDC | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
Catalytic Activity: adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA
Sequence Mass (Da): 36577
Sequence Length: 341
Subcellular Location: Cytoplasm
EC: 2.3.1.234
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A4XM18 | MLVLGIETSCDETAAAIVKDGREVLSNIVYSQIEIHNQFGGVVPEIASRKHVEKISYVADMALKEADIDIDKIDAVAATYGPGLVGSLLVGLSFAKALSYARKIPFIAINHIEGHIYANFITYPKLKPPLIVLVVSGGHTNLIILEDFDRYEVVGKTRDDAAGEAFDKIARYLGLGYPGGPAIDKVARHGDEEKYKYPLADVEGYNFSFSGLKSAVINHVHTLNQRRENFKVEDVAASFQKAVVDTLVEKTIKLSLESNIKRVAIAGGVAANSKLREELSKRCSEHQIEFYVPDFKYCTDNAAMIASAGYFKLIKGQTSSYSTNAVPYISLVSKKE | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
Catalytic Activity: adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA
Sequence Mass (Da): 36812
Sequence Length: 336
Subcellular Location: Cytoplasm
EC: 2.3.1.234
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A0RMI6 | MILGIESSCDDSSIALMDIDNFELKKYKKITQENEHSKFGGVVPELAARLHTAAIPNLIEDVKEFFTSIKAVAVTNEPGLSVSLISGVSAARALSLALGIPLIGVNHLIGHIYSLFLDKNVVLPLGVLLVSGGHTMVLNIDESGYIKLIATTSDDSFGESFDKVAKMMDLGYPGGAIIEKLALSGDKNRFNFTVPLKHDKRLEYSFSGLKNQVRTQISKFESLSLQDKSDIASSFQYTAISHITDKLEKIFSEYKFKNFGAIGGGSANQVLRSNLEQICEKFGSNLMFAPLKFCSDNAAMIARAGVCKYKNKCFTKPLDMSINPRCKLDGANLYF | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
Catalytic Activity: adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA
Sequence Mass (Da): 36645
Sequence Length: 335
Subcellular Location: Cytoplasm
EC: 2.3.1.234
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Q0P8R5 | MKNLILAIESSCDDSSIAIIDKNTLECKFHKKISQELDHSIYGGVVPELAARLHSEALPKMLKQCKEHFKNLCAIAVTNEPGLSVSLLSGISMAKTLASALNLPLIPINHLKGHIYSLFLEEKISLDMGILLVSGGHTMVLYLKDDASLELLASTNDDSFGESFDKVAKMMNLGYPGGVIIENLAKNAKLKNISFNTPLKHSKELAFSFSGLKNAVRLEILKHENLNEDTKAEIAYAFENTACDHIMDKLEKIFNLYKFKNFGVVGGASANLNLRSRLQNLCQKYNANLKLAPLKFCSDNALMIARAAVDAYEKKEFVSVEEDILSPKNKNFSRI | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
Catalytic Activity: adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA
Sequence Mass (Da): 37066
Sequence Length: 335
Subcellular Location: Cytoplasm
EC: 2.3.1.234
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Q6F0Y1 | MKILAIESSCDEFSISIIDDGKILTNIISSQIDQHVNFGGVVPELAARLHLENISWVIKSALESSNTKIEEIDHVAYTEKPGLIGSLIIGKLVAETIASYIDKPLMPLHHIEGHIYGASIENEFVYPVLAMVVSGGHTQIEIVNSPNEFEVIGATLDDAIGECYDKVARVMGLGYPGGPKIDKLAQKGNKEAFIFPISKNDDSYDFSYSGLKTAVINIIHNLTQKGEEIPVADIAASFQYAATKIVEKKLEKAIIQFKPKTLTVAGGVSANSEIRNIIMSLGKKYNITNTFVPKMEYCTDNAAMIAKLAYEKLKSSN | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
Catalytic Activity: adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA
Sequence Mass (Da): 34594
Sequence Length: 317
Subcellular Location: Cytoplasm
EC: 2.3.1.234
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Q5ZZQ1 | MKILGIETSHDDASVALFSENKVEILLTISQFELHEQFGGTVPELASREHSRNLAIILEKLLGKNIDFSTIDAIAYTKNPGLIGPLKIGFLFASALSLFFNKPLIPIDHLLGHFWSAAIENDLEFPVLSLLISGGHTQLIFAENKNNLEIIGSTVDDALGEIYDKIGRSLGCGYPGGPKIDLIWQQNNVRNMELIDFSLPKVLENPLDFSFSGLKTQVINYTNNLKENYLFSQKKVVEIAVSFQKTVIKYLKRQLDLALKTKKNVKTITLVGGVAANSEIRKLIKTYENKYKVVIPKKEFCTDNGAMIAKAAQIFLKFNEEK | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
Catalytic Activity: adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA
Sequence Mass (Da): 35961
Sequence Length: 322
Subcellular Location: Cytoplasm
EC: 2.3.1.234
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Q6KIG0 | MIILGIESSHDDTSIAILENKKVLFQLSLSQVKTHEKFGGTIPEIASREHVKNINILLTMLIEKFDLSKLDYIAYTEKPGLIGALQIGFLFASALSISLNKKLIPINHLEAHFFSSEITNEILYPAVGLVVSGGHSLIYYVKNVNSLEIIGETLDDAIGEVFDKISRKLNLGFPGGPIIDRISSEIVGDIKFTIPKTERDLDFSFSGIKTQVINYINNSKNLDINNVASSFQKTTIDYIEEKLKLAIKKHHPQSLVVGGGVSANTELRKRLSTLHANVLFPKKEYTTDNGAMIAITAFLKLNKSS | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
Catalytic Activity: adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA
Sequence Mass (Da): 33714
Sequence Length: 305
Subcellular Location: Cytoplasm
EC: 2.3.1.234
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Q602S1 | MLVLGIETSCDETGVALYDSSKGLLAHRLYSQVDEHAMYGGVVPEIASRDHLRKLLPLVREVLAAGGVRRTAIGGIAYTAGPGLIGALLVGAAVARSLAWAWSVPAIAVHHMEGHLLAPLLEPEPPEFPFVALLVSGGHTLLVEVRGIGVYQVLGESLDDAAGEAFDKTAKLLGLGYPGGPALARLAEKGRAERFHFPRPMTDRPGLDFSFSGLKTHALNVLAALPGTPQDKADIACAFQAAIVDTLVLKCRRAMRETGLGRLVVAGGVSANQAVRKGLQAMAESERYRVYFPRPEFCTDNGAMIAFAGCWRLRAGQFEPSAIEARARWAMETLTAV | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
Catalytic Activity: adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA
Sequence Mass (Da): 35901
Sequence Length: 337
Subcellular Location: Cytoplasm
EC: 2.3.1.234
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Q01TA4 | MQRILGIESSCDETAAAVVEDGERVLSSVVASQMSTHGRYGGVVPELASREHLRAIVPVVREALERSATRLEDLAAIAVTVGPGLVGSLLVGLTYAKSLSLASGVGLIGVNHIEGHIHAVILEARRDGTPVEFPALALVASGGHTHLFEVREDFTYRLLGKTRDDAAGEAFDKVGKLLGFGYPGGPVIDRLAPHGDPLAVRFTFAKMKGNALDFSFSGLKTAVLRWVEAHDMEAEIAARKALVRDNPSPDLDQWLAVTPKRTLDLAASFQHAVIHELLTRAAASAERIGARSLIVSGGVACNSGLRSAAYASRLPYAVHFPSFGLSTDNAAMIAAAAFPKLARREFSGLDIAAQANLTLA | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
Catalytic Activity: adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA
Sequence Mass (Da): 38057
Sequence Length: 360
Subcellular Location: Cytoplasm
EC: 2.3.1.234
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A9FDL0 | MRVLGIETSCDETAAAVVTEGGDVLSDVVRSQVALHAPYGGVVPEVAARDHARAVVPVVREALSRAGVSAADLDGIAVTSRPGLAGALLVGLQAAKGLAWAAGKPLVGVDHLVGHLLAVFLRRGGAPLSDERERPSFPYVALLASGGHTAIYRVDGPALGAIRELGATRDDAAGEAFDKVAKLLGLGYPGGPVVDRLAAGGDAAAAADAVPALMARKESLEFSFSGIKSSVARHVAKRGRPEGQALRDLCAAFQGAVVDALVQKTVRAARAEGIGRVVLGGGVAANQGLRAKMAAACERRGLALFVPPLASCTDNGAMIAYAGALRLAAGERDTLDLAPETRTALPRVTRKGGGAR | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
Catalytic Activity: adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA
Sequence Mass (Da): 36141
Sequence Length: 356
Subcellular Location: Cytoplasm
EC: 2.3.1.234
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Q9BZW7 | MMRSRSKSPRRPSPTARGANCDVELLKTTTRDREELKCMLEKYERHLAEIQGNVKVLKSERDKIFLLYEQAQEEITRLRREMMKSCKSPKSTTAHAILRRVETERDVAFTDLRRMTTERDSLRERLKIAQETAFNEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMKETISTVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGGTLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLDETNDELAQIARERDILAHDNDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLRKANEDAENWENKARQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVVKMEEELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQMANERISMQNLEALLVANRDKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRDVAQFRNVVTQLEADLDITKRQLGTERFERERAVQELRRQNYSSNAYHMSSTMKPNTKCHSPERAHHRSPDRGLDRSLEENLCYRDF | Function: Plays a role in spermatogenesis . When overexpressed, prevents nuclear localization of HIF1A (By similarity).
PTM: Processed into N-terminal 27-kDa and C-terminal 55-kDa fragments.
Sequence Mass (Da): 81421
Sequence Length: 698
Subcellular Location: Cytoplasm
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Q4R6W3 | MMRSRSKSPRRPSPTARGANCDVELLKTTTRDREELKCMLEKYERHLAEIQGNVKVLTSERDKTFLLYEQAQEEIARLRREMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGGTLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQSTEALIMCEQDISRMRRQLDETNDELAQIARERDILAHDNDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLRKANEDAENWENKARQSEADNNTLKLELITAEAEGNRLKEKVDSLSREVEQHLNAERSYKSQISTLHKSVVKMEEELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMMENELDSARSEIELLRSQMTNERISMQNLEALLVANRDKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRDVAQFRNVVTQLEADLDITKRQLGTERFERERAVQELRRQNYSSNAYHVSSTMKPNTKCHSPERAHHRSPDRGLDRSLEENLCYRDF | Function: Plays a role in spermatogenesis (By similarity). When overexpressed, prevents nuclear localization of HIF1A (By similarity).
PTM: Processed into N-terminal 27-kDa and C-terminal 55-kDa fragments.
Sequence Mass (Da): 69906
Sequence Length: 601
Subcellular Location: Cytoplasm
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Q6NY15 | MMRNRSKSPRRPSPTSRAANCDVELLKSTARDREELKCMLEKYERHLAEIQGNVKVLTSERDKTFLLYEQAQEEIARLRREMMKSCKSPKSTTAHAILRRVETERDVAFTDLRRMTTERDSLRERLKIAQETAFNEKAHLEQRIEELECTVHNLDDERMEQMANMTLMKETITTVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGATLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQSTEALIMCEQDISRMRRQLDETNDELGQIARERDILAHENDNLQEQFAKVKQENQALSKKLNDTHNELSDIKQKVQDTNLEVNKLKNILKSEESENRQIMEQLRKANEDAENWENKARQTEAENNTLKLELITAEAEGNRLKEKVDALNREVEQHLNAERSYKSQIATLHKSLVKMEEELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMMENELDSARSEIELLRSQMTNERISMQNLEALLVANRDKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRDVAQFRNVVTQLEADLDITKRQLGTERFERERAVQELRRQNYSSNAYNLGPMKPNTKCHSPERAHHRSPDRGLDRSLEENLCYRDF | Function: Plays a role in spermatogenesis . When overexpressed, prevents nuclear localization of HIF1A .
PTM: Processed into N-terminal 27-kDa and C-terminal 55-kDa fragments.
Sequence Mass (Da): 81262
Sequence Length: 697
Subcellular Location: Cytoplasm
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Q9Z220 | MMRNRSKSPRRPSPTSRAANCDVDLLKSTARDREELKCMLEKYERHLAEIQGNVKVLTSVRDKTFLLYEQAQEEIARLRREMMKSCQSPKSTTAHAILRRVETERDVAFTDLRRMTTARDSLRERLKIAQAFNEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMKETITIVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGATLNDLAKEKECLQTCLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQSTEALIMCEQDISRMRRQLDETNDELGQIARERDILAHENDNLQEQFAKVKQENQALSKKLNDTHNELSDIKQKVQDTNLEVNKLKNILKSEESTNLEVNKLKNILKSEESENRQIMEQLRKANEDAENWENKARQLEAENNTLKLELITAEAEGNRLKEKVDALNREVEQHLNAERSYKSQIATLHKSLVKMEEELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMMENELDSARSEIELLRSQMTNERISMQNLEALLVANRDKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRDVAQFRNVVTQLEADLDITKRQLGTERFERERAVQELRRQNYSSNAYHLGSMKPNTKCHSPERAHHRSPDRDLDRSLEENLCYRDF | Function: Plays a role in spermatogenesis (By similarity). When overexpressed, prevents nuclear localization of HIF1A (By similarity).
PTM: Processed into N-terminal 27-kDa and C-terminal 55-kDa fragments.
Sequence Mass (Da): 83012
Sequence Length: 712
Subcellular Location: Cytoplasm
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P98066 | MIILIYLFLLLWEDTQGWGFKDGIFHNSIWLERAAGVYHREARSGKYKLTYAEAKAVCEFEGGHLATYKQLEAARKIGFHVCAAGWMAKGRVGYPIVKPGPNCGFGKTGIIDYGIRLNRSERWDAYCYNPHAKECGGVFTDPKQIFKSPGFPNEYEDNQICYWHIRLKYGQRIHLSFLDFDLEDDPGCLADYVEIYDSYDDVHGFVGRYCGDELPDDIISTGNVMTLKFLSDASVTAGGFQIKYVAMDPVSKSSQGKNTSTTSTGNKNFLAGRFSHL | Function: Major regulator of extracellular matrix organization during tissue remodeling . Catalyzes the transfer of a heavy chain (HC) from inter-alpha-inhibitor (I-alpha-I) complex to hyaluronan. Cleaves the ester bond between the C-terminus of the HC and GalNAc residue of the chondroitin sulfate chain in I-alpha-I complex followed by transesterification of the HC to hyaluronan. In the process, potentiates the antiprotease function of I-alpha-I complex through release of free bikunin . Acts as a catalyst in the formation of hyaluronan-HC oligomers and hyaluronan-rich matrix surrounding the cumulus cell-oocyte complex, a necessary step for oocyte fertilization . Assembles hyaluronan in pericellular matrices that serve as platforms for receptor clustering and signaling. Enables binding of hyaluronan deposited on the surface of macrophages to LYVE1 on lymphatic endothelium and facilitates macrophage extravasation. Alters hyaluronan binding to functionally latent CD44 on vascular endothelium, switching CD44 into an active state that supports leukocyte rolling . Modulates the interaction of chemokines with extracellular matrix components and proteoglycans on endothelial cell surface, likely preventing chemokine gradient formation . In a negative feedback mechanism, may limit excessive neutrophil recruitment at inflammatory sites by antagonizing the association of CXCL8 with glycosaminoglycans on vascular endothelium . Has a role in osteogenesis and bone remodeling. Inhibits BMP2-dependent differentiation of mesenchymal stem cell to osteoblasts . Protects against bone erosion during inflammation by inhibiting TNFSF11/RANKL-dependent osteoclast activation .
PTM: N-glycosylated.
Sequence Mass (Da): 31203
Sequence Length: 277
Domain: The Link domain interacts with various extracellular matrix components, including heparin, heparan sulfates, hyaluronan and I-alpha-I complex . It is required for binding to various chemokines .
Subcellular Location: Secreted
EC: 3.1.1.-
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P41732 | MASRRMETKPVITCLKTLLIIYSFVFWITGVILLAVGVWGKLTLGTYISLIAENSTNAPYVLIGTGTTIVVFGLFGCFATCRGSPWMLKLYAMFLSLVFLAELVAGISGFVFRHEIKDTFLRTYTDAMQTYNGNDERSRAVDHVQRSLSCCGVQNYTNWSTSPYFLEHGIPPSCCMNETDCNPQDLHNLTVAATKVNQKGCYDLVTSFMETNMGIIAGVAFGIAFSQLIGMLLACCLSRFITANQYEMV | Function: May be involved in cell proliferation and cell motility.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27574
Sequence Length: 249
Subcellular Location: Membrane
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Q62283 | MASRRMETKPVITCLKTLLIIYSFVFWITGVILLAVGVWGKLTLGTYISLIAENSTNAPYVLIGTGTTIVVFGLFGCFATCRGSPWMLKLYAMFLSLVFLAELVAGISGFVFRHEIKDTFLRTYTDAMQNYNGNDERSRAVDHVQRSLSCCGVQNYTNWSSSPYFLDHGIPPSCCMNETDCNPLDLHNLTVAATKVNQKGCYDLVTSFMETNMGIIAGVAFGIAFSQLIGMLLACCLSRFITANQYEMV | Function: May be involved in cell proliferation and cell motility.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27544
Sequence Length: 249
Subcellular Location: Membrane
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O75954 | MARGCLCCLKYMMFLFNLIFWLCGCGLLGVGIWLSVSQGNFATFSPSFPSLSAANLVIAIGTIVMVTGFLGCLGAIKENKCLLLSFFIVLLVILLAELILLILFFVYMDKVNENAKKDLKEGLLLYHTENNVGLKNAWNIIQAEMRCCGVTDYTDWYPVLGENTVPDRCCMENSQGCGRNATTPLWRTGCYEKVKMWFDDNKHVLGTVGMCILIMQILGMAFSMTLFQHIHRTGKKYDA | PTM: Glycosylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26779
Sequence Length: 239
Subcellular Location: Membrane
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Q8BJU2 | MARGCLCCLKYTMFLFNLIFWLCGCGLLGVGIWLSVSQGNFATFSPSFPSLSAANLVIAIGTIVMVTGFLGCLGAIKENKCLLLSFFIVLLIILLAELILIILFFVYMDKVNENAKQDLKEGLLLYNTENNVGLKNAWNIIQAEMRCCGVTDYTDWYPVLGENTVPDRCCMENSQGCGRNSTTPLWRTGCYEKVKLWFDDNKHVLGTVGMCILIMQILGMAFSMTLFQHIHRTGKKYDA | PTM: Glycosylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26738
Sequence Length: 239
Subcellular Location: Membrane
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Q06AA5 | MARGCLCCLKYMMFLFNLIFWLCGCGLLGVGIWLSVSQGNFATFSPSFPSLSAANLVIAIGTIVMVTGFLGCLGAIKENRCLLLSFFIVLLIILLAELILIILFFVYMDKVNENARKDLKEGLLLYNSENNVGLKNAWNIIQAEMHCCGVTDYTDWYPVLGENTVPDRCCMENSQGCGRNSTTPLWKTGCYEKVKMWFDDNKHVLGTVGMCILIMQILGMAFSMTLFQHIHRTGKKYDA | PTM: Glycosylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26781
Sequence Length: 239
Subcellular Location: Membrane
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B3VSC2 | MARGCLCCLKYAMFLFNLIFWLCGCGLLGVGIWLSVSQGNFATFSPSFPSLSAANLVIAIGTIVMVTGFLGCLGAIKENRCLLLSFFIVLLIILLAELILIILFFVYMDKVNENAKKDLKEGLLLYNSENNVGLKNAWNIIQAEMHCCGVTDYRDWFLVLGENTVPDRCCMENSQGCGQNNTTLLWRTGCYEKVKQWFADNKHVLGTVGMCLLITQILGMAFSMTLFQHIHRTGKKYDA | PTM: Glycosylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26714
Sequence Length: 239
Subcellular Location: Membrane
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Q9BXA7 | MDDAAVLKRRGYLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETSHGKVYIVMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRMALSKTFCGSPAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRSKHLTGECKDLIYHMLQPDVNRRLHIDEILSHCWMQPKARGSPSVAINKEGESSRGTEPLWTPEPGSDKKSATKLEPEGEAQPQAQPETKPEGTAMQMSRQSEILGFPSKPSTMETEEGPPQQPPETRAQ | Function: Testis-specific serine/threonine-protein kinase required during spermatid development. Phosphorylates 'Ser-288' of TSKS. Involved in the late stages of spermatogenesis, during the reconstruction of the cytoplasm. During spermatogenesis, required for the transformation of a ring-shaped structure around the base of the flagellum originating from the chromatoid body.
PTM: Autophosphorylated.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 41618
Sequence Length: 367
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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Q96PF2 | MDDATVLRKKGYIVGINLGKGSYAKVKSAYSERLKFNVAVKIIDRKKTPTDFVERFLPREMDILATVNHGSIIKTYEIFETSDGRIYIIMELGVQGDLLEFIKCQGALHEDVARKMFRQLSSAVKYCHDLDIVHRDLKCENLLLDKDFNIKLSDFGFSKRCLRDSNGRIILSKTFCGSAAYAAPEVLQSIPYQPKVYDIWSLGVILYIMVCGSMPYDDSDIRKMLRIQKEHRVDFPRSKNLTCECKDLIYRMLQPDVSQRLHIDEILSHSWLQPPKPKATSSASFKREGEGKYRAECKLDTKTGLRPDHRPDHKLGAKTQHRLLVVPENENRMEDRLAETSRAKDHHISGAEVGKAST | Function: Testis-specific serine/threonine-protein kinase required during spermatid development. Phosphorylates TSKS at 'Ser-288' and SPAG16. Involved in the late stages of spermatogenesis, during the reconstruction of the cytoplasm. During spermatogenesis, required for the transformation of a ring-shaped structure around the base of the flagellum originating from the chromatoid body.
PTM: Autophosphorylated.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 40939
Sequence Length: 358
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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O54863 | MDDAAVLRKKGYIVGINLGKGSYAKVKSAYSERLKFNVAVKIIDRKKTPTDFVERFLPREMDILATVNHRSIIKTYEIFETSDGRIYIVMELGVQGDLLEFIKCRGALHEDVARKMFRQLSSAVKYCHDLDVVHRDLKCENLLLDKDFNIKLSDFGFSKRCLRDGSGRIVLSKTFCGSAAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPYDDSDIKKMLRIQKEHRVDFPRSKNLTGECKDLIYRILQPDVNRRLHIDEILSHSWLQPPKPKAMSSASFKREGEGKYRADCKLDTRPGSRPEHRPDHKLATKPQQRMLVTPENEDRMEDRLAETSRAKDHHISGAEVEKAST | Cofactor: Mg(2+) and Mn(2+) were both present in the kinase buffer but Mg(2+) is likely to be the in vivo cofactor.
Function: Testis-specific serine/threonine-protein kinase required during spermatid development. Phosphorylates 'Ser-281' of TSKS and SPAG16. Involved in the late stages of spermatogenesis, during the reconstruction of the cytoplasm. During spermatogenesis, required for the transformation of a ring-shaped structure around the base of the flagellum originating from the chromatoid body.
PTM: Autophosphorylated.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 41022
Sequence Length: 358
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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Q96PN8 | MEDFLLSNGYQLGKTIGEGTYSKVKEAFSKKHQRKVAIKVIDKMGGPEEFIQRFLPRELQIVRTLDHKNIIQVYEMLESADGKICLVMELAEGGDVFDCVLNGGPLPESRAKALFRQMVEAIRYCHGCGVAHRDLKCENALLQGFNLKLTDFGFAKVLPKSHRELSQTFCGSTAYAAPEVLQGIPHDSKKGDVWSMGVVLYVMLCASLPFDDTDIPKMLWQQQKGVSFPTHLSISADCQDLLKRLLEPDMILRPSIEEVSWHPWLAST | Function: May be involved in a signaling pathway during male germ cell development or mature sperm function.
PTM: Autophosphorylated.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 30102
Sequence Length: 268
EC: 2.7.11.1
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Q9D2E1 | MEDFLLSNGYQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIIDKMGGPEEFIQRFLPRELQIVRTLDHKNIIQVYEMLESADGKIYLVMELAEGGDVFDCVLNGGPLPESRAKALFRQMVEAIRYCHGCGVAHRDLKCENALLQGFNLKLTDFGFAKVLPKSRRELSQTFCGSTAYAAPEVLQGIPHDSKKGDVWSMGVVLYVMLCASLPFDDTDIPKMLWQQQKGVSFPTHLGISTECQDLLKRLLEPDMILRPSIEEVSWHPWLAST | Function: May be involved in a signaling pathway during male germ cell development or mature sperm function.
PTM: Autophosphorylated.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 30209
Sequence Length: 268
EC: 2.7.11.1
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Q9D411 | MGKGDTSETASATPAYRSVMEEYGYEVGKIIGHGSYGTVYEAYYTKQKVMVAVKIISKKKASEDYLNKFLPREIQVMKVLRHKYLINFYQAIETTSRVYIILELAQGGDVLEWIQRYGACAETLAGKWFSQMALGIAYLHSKGIVHRDLKLENLLLDKRENVKISDFGFAKMVPSSQPVHSSPSYRQMNSLSHLSQTYCGSFAYACPEILLGLPYNPFLSDTWSMGVILYTLVVARLPFDDTNLKKLLRETQKEVTFPANLTISQECKNLILQLLRQSTKRATILDVLRDPWMLKFQPEQPSNEIRLLEAMYQPTSSAKRHQSLEITT | Cofactor: Mg(2+) and Mn(2+) were both present in the kinase buffer but Mg(2+) is likely to be the in vivo cofactor.
Function: Serine/threonine kinase which is involved in male germ cell development and in mature sperm function . May be involved in the Cre/Creb signaling pathway . Phosphorylates CREB1 on 'Ser-133' in vitro and can stimulate Cre/Creb pathway in cells (By similarity). Phosphorylates CREM on 'Ser-116' in vitro . Phosphorylates ODF2 on 'Ser-95' .
PTM: Activated by autophosphorylation on Thr-197. ODF2 potentiates the autophosphorylation activity of TSSK4 at Thr-197.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 37377
Sequence Length: 328
Subcellular Location: Cytoplasmic vesicle
EC: 2.7.11.1
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Q8C1R0 | MRSSSWRKSDQRVFIEQVRECMNNGYLLSSKKIGSGAFSKVYLAYATRERMKHNPRLSSDLRGKRHTMVAIKIVSMAEAPAEYSRKFLPREILSLNATYKHMNIVQLYETYQNSQRSYLVLELAARGDLLEHINAVSDLRCCPGLEEEEARRLFWQLVSAVAHCHNVGIVHRDLKCENILLDDQGFIKLTDFGFANWVGLKNSLLSTFCGSVAYTAPEILMSKKYNGEQADLWSLGIILHAMVSGKLPFKEHQPHRMLNLIRRGPIFRPGLSPECRDLIRGLLQLHPCERLDLQQVAAHCWMLPAEHMLSSALGAPREQDHSWSTVAPDNTEPDRDTRHARSKGSSSSSGRTSPRRPSLAQLCNTWKPAPEQ | Function: May be involved in a signaling pathway during male germ cell development or mature sperm function.
PTM: Autophosphorylated.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 42234
Sequence Length: 372
EC: 2.7.11.1
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Q9BXA6 | MSGDKLLSELGYKLGRTIGEGSYSKVKVATSKKYKGTVAIKVVDRRRAPPDFVNKFLPRELSILRGVRHPHIVHVFEFIEVCNGKLYIVMEAAATDLLQAVQRNGRIPGVQARDLFAQIAGAVRYLHDHHLVHRDLKCENVLLSPDERRVKLTDFGFGRQAHGYPDLSTTYCGSAAYASPEVLLGIPYDPKKYDVWSMGVVLYVMVTGCMPFDDSDIAGLPRRQKRGVLYPEGLELSERCKALIAELLQFSPSARPSAGQVARNCWLRAGDSG | Function: Required for sperm production and function. Plays a role in DNA condensation during postmeiotic chromatin remodeling (By similarity).
PTM: Autophosphorylated.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 30331
Sequence Length: 273
EC: 2.7.11.1
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Q925K9 | MSGDKLLSELGYKLGRTIGEGSYSKVKVATSKKYKGTVAIKVVDRRRAPPDFVNKFLPRELSILRGVRHPHIVHVFEFIEVCNGKLYIVMEAAATDLLQAVQRNGRIPGSQARELFSQIAGAVRYLHDHHLVHRDLKCENVLLSPDERRVKITDFGFGRQAHGYPDLSTTYCGSAAYASPEVLLGIPYDPKKYDVWSLGVVLYVMVTGCMPFDDSDIAGLPRRQKRGVLYPDGLELSERCKSLIAELLQFSPSARPSAGQVARNGWLRAGDSG | Cofactor: Mg(2+) and Mn(2+) were both present in the kinase buffer but Mg(2+) is likely to be the in vivo cofactor.
Function: Required for sperm production and function. Plays a role in DNA condensation during postmeiotic chromatin remodeling.
PTM: Autophosphorylated.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 30287
Sequence Length: 273
EC: 2.7.11.1
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Q9NQE7 | MAVWLAQWLGPLLLVSLWGLLAPASLLRRLGEHIQQFQESSAQGLGLSLGPGAAALPKVGWLEQLLDPFNVSDRRSFLQRYWVNDQHWVGQDGPIFLHLGGEGSLGPGSVMRGHPAALAPAWGALVISLEHRFYGLSIPAGGLEMAQLRFLSSRLALADVVSARLALSRLFNISSSSPWICFGGSYAGSLAAWARLKFPHLIFASVASSAPVRAVLDFSEYNDVVSRSLMSTAIGGSLECRAAVSVAFAEVERRLRSGGAAQAALRTELSACGPLGRAENQAELLGALQALVGGVVQYDGQTGAPLSVRQLCGLLLGGGGNRSHSTPYCGLRRAVQIVLHSLGQKCLSFSRAETVAQLRSTEPQLSGVGDRQWLYQTCTEFGFYVTCENPRCPFSQLPALPSQLDLCEQVFGLSALSVAQAVAQTNSYYGGQTPGANKVLFVNGDTDPWHVLSVTQALGSSESTLLIRTGSHCLDMAPERPSDSPSLRLGRQNIFQQLQTWLKLAKESQIKGEV | Function: Protease that may play a role in T-cell development.
Sequence Mass (Da): 55049
Sequence Length: 514
Subcellular Location: Cytoplasmic vesicle
EC: 3.4.-.-
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Q9QXE5 | MAVKAPWLGFLLLVSLWGLSTPALLLRRLREHIQKFQESSSLHPGFGLGHGPGAVPKQGWLEQPLDPFNASDRRTFLQRYWVNDQHRTGQDVPVFLHIGGEGSLGPGSVMAGHPAALAPAWGALVISLEHRFYGLSMPAGGLDLALLRYLSSRHALADVASARQALSGLLNVSSSSPWICFGGSYAGSLATWARLKFPHLVFAAVASSAPLSAVVDFSAYNQVVARSLTQVAIGGSLECLAAASTAFTEVERLLRAGPAAQAVLREELGACGSLDLTEDQAELLGALQALVGGTVQYDGQAGAPLSVRQLCGLLLGKWGNRSRSTPYLGLRRAVQIVLRSMGQKCLSFSRAETVAQLSNTEPQVSGVGDRQWLYQTCTEFGFYVTCEGLQCPFSQLPALPFQLELCEQVFGLSPASVAQAVAQTNSYYGGQSPGATQVLFVNGDTDPWHVLSVTQDLGLSEPALLIPSASHCFDMAPMRPSDSPSLRLGRQKISQQLQDWLKDIKKSQS | Function: Protease that may play a role in T-cell development.
Sequence Mass (Da): 54523
Sequence Length: 509
Subcellular Location: Cytoplasmic vesicle
EC: 3.4.-.-
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Q11U13 | MRHTFTTEIMPLPTPEEKNINRLRKSFWEAVEEFDLIEPGDKIMVCLSGGKDSYTMLDMFIHAQTVRKNFEIIAVNLDQKQPDYPEHILPEYLTHLGVNFKIVEKDTYSIVIDKTPAGKTMCSLCSRLRRGSLYATAEELGVTKIALGHHREDVLETFFLNLFFSGKMEAMPAKYRTDDGKHVVIRPLVYCKENEIAEYSIYKKFPIIPCNLCGSQENMQRKITKKMLADWELQYPNRKEVIYNALKNISPSHLFDRDLYDFKELKHRVEELNEKDTPKVEEYIP | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster is chelated by three Cys residues, the fourth Fe has a free coordination site that may bind a sulfur atom transferred from the persulfide of IscS.
Function: Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system.
Catalytic Activity: AH2 + ATP + cytidine(32) in tRNA + S-sulfanyl-L-cysteinyl-[cysteine desulfurase] = 2-thiocytidine(32) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[cysteine desulfurase]
Sequence Mass (Da): 33320
Sequence Length: 285
Pathway: tRNA modification.
Subcellular Location: Cytoplasm
EC: 2.8.1.-
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P39414 | MKPSTEWWRYLAPLAVIAIIALLPVPAGLENHTWLYFAVFTGVIVGLILEPVPGAVVAMVGISIIAILSPWLLFSPEQLAQPGFKFTAKSLSWAVSGFSNSVIWLIFAAFMFGTGYEKTGLGRRIALILVKKMGHRTLFLGYAVMFSELILAPVTPSNSARGAGIIYPIIRNLPPLYQSQPNDSSSRSIGSYIMWMGIVADCVTSAIFLTAMAPNLLLIGLMKSASHATLSWGDWFLGMLPLSILLVLLVPWLAYVLYPPVLKSGDQVPRWAETELQAMGPLCSREKRMLGLMVGALVLWIFGGDYIDAAMVGYSVVALMLLLRIISWDDIVSNKAAWNVFFWLASLITLATGLNNTGFISWFGKLLAGSLSGYSPTMVMVALIVVFYLLRYFFASATAYTSALAPMMIAAALAMPEIPLPVFCLMVGAAIGLGSILTPYATGPSPIYYGSGYLPTADYWRLGAIFGLIFLVLLVITGLLWMPVVLL | Function: Catalyzes the uptake of tartrate in exchange for intracellular succinate. Essential for anaerobic L-tartrate fermentation.
Catalytic Activity: (2R,3R)-tartrate(out) + succinate(in) = (2R,3R)-tartrate(in) + succinate(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52906
Sequence Length: 487
Subcellular Location: Cell inner membrane
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Q9Z4S6 | MANLTRRQWLKVGLAVGGMVTFGLSYRDVAKRAIDGLLNGTSGKVTRDRIFGNALIPEAQAQTHWQQNPQQTIAMTQCFGCWTQCGIRARVNADGKVIRIAGNPYHPLSQEHPIDSSVPFSEAMEQLAGESGLDARSTACARGATLLESLYSPLRLLEPMKRVGKRGEGKWQRISFEQLIEEVVEGGDLFGEGHVDGLRAIHAPDTPIDAKHPSFGPKTNQLLVTNTSDEGRDAFLRRFALNSFGSKNFGAHGAYCGLAYRAGSGALMGDLDKNPHVKPDWENVEFALFMGTSPAQSGNPFKRQARQLASARLRENFQYVVVAPALPLSTVLADPRGRWQPVMPGSDSALAMGMIRWIMDNQRYNADYLAIPGVQAMQQAGEQSWTNATHLVIADELPTLAGQHLTLRHLTPDGEETPVVLNTDGELVDASTCRQARLFVTQYVTLADGQRVTVKSGLQRLKEAAEKLSLAQYSEQCGVPEAQIIALAETFTSHGRKAAVISHGGMMAGNGFYNAWSVMMLNALIGNLSLSGGVFVGGGKFNGVSDGPRYNMNSFAGKVKPSGLSIARSKTAYEASEEYRDKIAGGQSPYPAKAPWYPFVAGQLTELLTSALEGYPYPLKAWISNMSNPFYGVPGLRAVAEEKLKDPRRLPLFIAIDAFMNETTALADYIVPDTHNFESWGFTAPWGGVASKATTARWPVVAPATHRTADGQPVSMEAFCIAVAKRLHLPGFGDRAITDPQGNTFPLNRAEDFYLRVAANIAFMGKTPVALANQEDISLTGVSRILPAIQHTLKADEVGRVAFIYSRGGRFAPEDSGYTEQRLGNAWKKPLQIWNADVAAHRHAITGERFSGCPVWYPARLSDGRAIDDQFPIGQWPLKLISFKSNTMSSSTAVIPRLHHVKPANLVALNPQDGERYGLQHGDRVRIITPGGQVVAQISLLNGVMPGVIAIEHGYGHREMGATQHSLDGVPMPYDPQIRAGINLNDLGFADPTRTITNTWLDWVSGAAVRQGLPAKIERI | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Part of a membrane-bound tetrathionate reductase that catalyzes the reduction of tetrathionate to thiosulfate. TtrA is the catalytic subunit. During mice infection, the ability to use tetrathionate as an electron acceptor is a growth advantage for S.typhimurium over the competing microbiota in the lumen of the inflamed gut.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 110993
Sequence Length: 1020
Subcellular Location: Periplasm
EC: 1.8.-.-
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O30080 | MLISKTLIFYQVVNIVSQKGSGKRRWKMENGDRYVYVVDVSKCYGCLSCVAACAAENNVPVGYFRTWVERYAMNGRVAFVPKICNHCDNPSCVHACPVNATYKTEEGLVLIDDEICIGCGACIQACPYGARFRNPVKGTADKCTLCNHRIPERLPACVESCPTSARVYGKMSDKAVKEILSKKNAVVLKAYTGNEPHTYYVSLTGVE | Function: Part of a membrane-bound tetrathionate reductase that catalyzes the reduction of tetrathionate to thiosulfate. TtrB is probably involved in transfer of electrons from TtrC to TtrA (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 22871
Sequence Length: 207
Subcellular Location: Cell membrane
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Q7CQM9 | MWTGVNMDSSKRQFLQQLGVLTAGASLVPLAEAKFPFSPERHEGSPRHRYAMLIDLRRCIGCQSCTVSCTIENQTPQGAFRTTVNQYQVQREGSQEVTNVLLPRLCNHCDNPPCVPVCPVQATFQREDGIVVVDNKRCVGCAYCVQACPYDARFINHETQTADKCTFCVHRLEAGLLPACVESCVGGARIIGDIKDPHSRIATMLHQHRDAIKVLKPENGTSPHVFYLGLDDAFVTPLMGRAQPALWQEV | Function: Part of a membrane-bound tetrathionate reductase that catalyzes the reduction of tetrathionate to thiosulfate. TtrB is probably involved in transfer of electrons from TtrC to TtrA. During mice infection, the ability to use tetrathionate as an electron acceptor is a growth advantage for S.typhimurium over the competing microbiota in the lumen of the inflamed gut.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 27710
Sequence Length: 250
Subcellular Location: Periplasm
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O30079 | MLWSYPEGFAYFNEFAQSIIWEPVAFSYALLISGADLLLLAALALLSGYLRRAIPMFLILGLSFFSVILLGPLADLALPHRATEILTRPHLASTEMHPGISVMALYGGLLWPLTFIVALIFALLYFSYPMHKKGGTFSFLSFGVKSEESYERLKPAMKVLAAILVPLSALWTIYPGMLFFSQTWIYAWKNWGLMLPMFFGETFITATGTALILYYLERMEDERIRYPLLQIHGAAAIALAGVLILQMFIWGMWGNPNFAAVVPMMQAAAVIFLLTFILTLVSAKYEAITPIVPVLALFGVVVNKWNLIINGQLISRAGMGVLEPELAPNWLAEAVSPIALAILLLVILSYIFPMEVEEDAA | Function: Part of a membrane-bound tetrathionate reductase that catalyzes the reduction of tetrathionate to thiosulfate. TtrC probably anchors TtrA and TtrB to the external face of the cytoplasmic membrane. May transfer electrons from membrane quinol to TtrB (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40083
Sequence Length: 361
Subcellular Location: Cell membrane
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Q9Z4S7 | MTHSLIIEEVLAHPQDISWLPWAVQYFFFIGIAACAALFACYLHWRKKDAATEENRALLIAITCAITAPLALTADLHQTARVWHFYAWPTPWSWMPWGALFLPLFTGFLALWFLAQQIKRLFNKSYNVTKWLALASALCAVGLLIYTGREVSVVLARPIWFSYAFPVAMFLSALQAFFALMIVAARRDSVRLPKILWGQIWTLAALGLVVAMWVSGDTLSGTAIRQWITVALSAKYYAVGWVALWVCTLLFCSLALRHPLSQLRRVLLVLSALALCWLMRWTLLIQVQTVPKFNAQFNPYSLPGGTDGWLAILGTFGLWIALLIIIRETLNGLTRRLQHG | Function: Part of a membrane-bound tetrathionate reductase that catalyzes the reduction of tetrathionate to thiosulfate. TtrC probably anchors TtrA and TtrB to the periplasmic face of the cytoplasmic membrane. May transfer electrons from membrane quinol to TtrB. During mice infection, the ability to use tetrathionate as an electron acceptor is a growth advantage for S.typhimurium over the competing microbiota in the lumen of the inflamed gut.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38395
Sequence Length: 340
Subcellular Location: Cell inner membrane
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Q7CQM8 | MATIHLLDDDTAVTNACAFLLESLGYDVKCWTQGADFLAQASLYQAGVVLLDMRMPVLDGQGVHDALRQCGSTLAVVFLTGHGDVPMAVEQMKRGAVDFLQKPVSVKPLQAALERALTVSSAAVARREIILCYQQLTPKERELASLVAKGFMNREIAEAMNIAVRTVEVHRARVMEKMQAGSLAELIRRFEKMASPETRIRTTYEP | Function: Member of the two-component regulatory system TtrR/TtrS, which is required for synthesis of tetrathionate reductase. Positively regulates transcription of the ttrBCA operon. During mice infection, the ability to use tetrathionate as an electron acceptor is a growth advantage for S.typhimurium over the competing microbiota in the lumen of the inflamed gut.
PTM: Phosphorylated by TtrS.
Sequence Mass (Da): 22692
Sequence Length: 206
Subcellular Location: Cytoplasm
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Q8ZPP6 | MRGKTVRRLAVLAAVGLLCHGAWAGTWNIGILAMRGEASTRSHWQPLAKTLSQQLPGETFHIQPLDLHQMQEAVNQGTVQFVITNPAQFVQLNSHAPLRWLASLRSTRDGKAVSNVIGSVILTRRDSGITTAHDLIGKTVGAIDAQAFGGYLLGYKALSDAGLRPERDFHLRFTGFPGDALVYMLREKAVQAAIVPVCLLENMDQEGLINKKDFIALLSRPTPLPCLTSTPLYPDWSFAALPAVSDALADRVTRALFNAPAAASFHWGAPASTSQVEALLRDVRQHPQQRRLWLDVKSWLIQHQLMVGGVILAFLLLTLNYIWVMLLVRRRGKQLERNSVVLHQHERALETARQMSVLGEMTSGFAHELNQPLSAIRHYAQGCLIRLRAADEQHPLLPALEQIDQQAQRGADTLRNLRHWVSQAQGNPVLTEAWKAIAIREAIDHVWQLLRMAQQFPTVTLHTEVSAALRVTLPSVLLEQVLANIILNAAQAGATHLWIVAERTENGISIVLQDNAGGIDEALLRQAFQPFMTTRKEGMGLGLAICQRLVRYGRGDISIRNQTAPDGLSGTVVTIHFLHENGGRDGDNSSTG | Function: Member of the two-component regulatory system TtrR/TtrS, which is required for synthesis of tetrathionate reductase. Probably functions as a sensor protein kinase which is autophosphorylated at a histidine residue in response to tetrathionate, and transfers its phosphate group to TtrR. During mice infection, the ability to use tetrathionate as an electron acceptor is a growth advantage for S.typhimurium over the competing microbiota in the lumen of the inflamed gut.
PTM: Autophosphorylated.
Location Topology: Multi-pass membrane protein
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Mass (Da): 65239
Sequence Length: 592
Subcellular Location: Cell inner membrane
EC: 2.7.13.3
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Q9Y7Z5 | MEPKQRVVKPLKERVLPVVKNTQFVWFSGQVIVLISSVLYALQAIPFRSAPPFLFKSAAFGAIVAYAIVLYKTYSPNLTSRASWNKHFFARLMLDDNVQYFILALSMLIDRPILFSLAPYAIYATFHISTYLRSVLLPAIYPNISDAKTASYASRVSNLLNQYTRSQFQPAMQLVASLETFLLFRLFFGVFLRKNSISRLVGYIFFLRMRYTNSHFTRASIKAVSLRMDRLVADNRVPPVIKNAWHTFKTYVSKFGASPVGTAQSRPTASSSTTAPSST | Function: Required for the correct positioning of the cellular division plane by delimiting the actomyosin ring assembly at the cell equator.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31570
Sequence Length: 279
Subcellular Location: Golgi apparatus membrane
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O32274 | MSAEKSMNVSREFSVQQIHSFTLSEKTARYLAIKRVMDIWFALIGLAIALPMIAVFSILICLETPGPAIYTQERVGKGGKPFKLYKLRSMKIDAEKSGAVWAQKQDPRVTRIGAFIRRTRIDELPQLFNVLKGDMSMIGPRPERPVFTEKFQNEIPGFTQRLGSGERRLRYDAEGKADI | Function: Might mediate the very first reaction in teichuronic synthesis, i.e. the formation of lipid-linked N-acetylglucosamine.
Catalytic Activity: di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-D-galactosamine = N-acetyl-alpha-D-galactosaminyl-di-trans,octa-cis-undecaprenyl diphosphate + UMP
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 20323
Sequence Length: 179
Pathway: Cell wall biogenesis; teichuronic acid biosynthesis.
Subcellular Location: Cell membrane
EC: 2.7.8.40
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O32273 | MPSITKQIMSGAKWTSISTMCITIIQIVQFALLGNMMTLTEFGLVGMITTVTVFAQIVLDMGFGAALIQRDDATERQLSTLYWLNIMTGVLLFVLLYVSSPVIAGFYQREELVFLVRILAIMFLIAPIGQQYQYMLQKQLHFNTLSKIEIFSNVLSFGYLAIAVFMMDAILAYVISQVLLQSSKGILYWAVYRKKWHPAFVFDLRGMKDFFSFGAFQLSSRLVNRLGANIDMILIGRFIGAEALGIYNLAYQIVTIPVLKINPIVTRVAFPIFAKNKYENSVIREGFLNMTKMLALVSFPLLIGLVSVSDAFITAVFGEKWLAAVPILNVLAIVGILRVLMNPNGSVLLAKGRADLAFYWDSGVLLLYGLSLFAAVQTGSLLTVAWVYAIISVVNFLIGRWLLAYVIKLNLSAYFQSIMKPFLITAAMGIIAFGVSLSTEHFSMQAEMRLAISVAAGALCYLFLLVKAYPQTKSKLLRKGRLS | Function: Might be involved in the translocation of teichuronic acid repeating units from the inner to the outer surface of the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53720
Sequence Length: 483
Pathway: Cell wall biogenesis; teichuronic acid biosynthesis.
Subcellular Location: Cell membrane
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O32271 | MKKIAVIGTGYVGLVSGTCFAEIGNKVVCCDIDESKIRSLKNGVIPIYEPGLADLVEKNVLDQRLTFTNDIPSAIRASDIIYIAVGTPMSKTGEADLTYVKAAAKTIGEHLNGYKVIVNKSTVPVGTGKLVQSIVQKASKGRYSFDVVSNPEFLREGSAIHDTMNMERAVIGSTSHKAAAIIEELHQPFHAPVIKTNLESAEMIKYAANAFLATKISFINDIANICERVGADVSKVADGVGLDSRIGRKFLKAGIGFGGSCFPKDTTALLQIAKSAGYPFKLIEAVIETNEKQRVHIVDKLLTVMGSVKGRTISVLGLAFKPNTNDVRSAPALDIIPMLQQLGAHVKAYDPIAIPEASAILGEQVEYYTDVYAAMEDTDACLILTDWPEVKEMELVKVKTLLKQPVIIDGRNLFSLEEMQAAGYIYHSIGRPAVRGTEPSDKYFPGLPLEELAKDLGSVNL | Function: Catalyzes the conversion of UDP-glucose into UDP-glucuronate, one of the precursors of teichuronic acid.
PTM: Phosphorylated by YwqD and dephosphorylated by YwqE in vitro.
Catalytic Activity: H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-alpha-D-glucuronate
Sequence Mass (Da): 49816
Sequence Length: 461
Pathway: Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step 1/1.
Subcellular Location: Cytoplasm
EC: 1.1.1.22
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O32270 | MSIKRSAVHTLALLAAAIFGVVLLLGAIHKDIGFMQMAAVLAVLAIGLFLLTLATAFTTKERLFMAVIYILIACTFLNNAFFAIHLGFFSLFLYRLLLIAAGCLHIFGMVRNRTHIERWHGLQVKGILLFFAFWFIYGLVSLLWAKSVTVGLKYLALLAMGIFFIYLIVMYVQKMERLMIVYAIWLVMTVFLMIIGFYNHITHHHLASSTLYSGPEYKQHYPTSVFFNQNDFATFLSISFFFYITMMKNIKNGYIKAIGLVLSLCALYLIFATGSRASLLGIFAGIAVYIFIVLPPVLKRMAIWLSAAGIALFAVLFASKIYSKFWELFLAPQTLHSFHDRLPSNVARANLLKNAWHFFLDSYGFGVGAGNVSYYLEHYAVYDTDNVAEVHNWLVEILANFGLFIMLGYLSVYAYLIWVLYKFYERKLENQSKLITEGLITAMVSFLVSSISPSSVSNLFFHWVFMALVIAAVNVLRRSRQMPEPMYR | Function: Might be involved in the polymerization of teichuronic acid repeating units after their translocation to the outer surface of the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55536
Sequence Length: 488
Pathway: Cell wall biogenesis; teichuronic acid biosynthesis.
Subcellular Location: Cell membrane
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O32269 | MNDILIRIARRIKKNIIWIIAVPIILGAAGYILPSQIADQKSYTAEDTLAVGSYDHPVYNSTEEIPLLLKSDSFLKEALPDEKDEDVAEIKEKLTINTESKSLLTLSYSDEDKDRTESVLNAISSTFLKNDQKLYAEREAVIRSSIDALEGESVSEDSKVDKERFLYELKNTQLNLKAASVTDSETVSETAGGGMSPKKKAVLGVMIGLTIAFMFVVIPEFFRESF | Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25135
Sequence Length: 226
Pathway: Cell wall biogenesis; teichuronic acid biosynthesis.
Subcellular Location: Cell membrane
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P0DKN3 | MARLMMTVGCLIFIVVLLDMMVPVSNTCPGYFGECGDGPEEGECCGMYNYCCKGRCLMLASCQKRRDAGRLLRSLKKLKLTTH | Function: Acts as a neurotoxin by inhibiting voltage-gated potassium channels (Kv).
PTM: Contains 4 disulfide bonds.
Sequence Mass (Da): 9232
Sequence Length: 83
Domain: The cysteine framework is XI (C-C-CC-CC-C-C).
Subcellular Location: Secreted
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Q44470 | MNSDLETRVLRKITLRIVPFIMLLYFVAFLDRVNIGFAALTMNEDLGFSSTVFGIGAGIFFVGYFLFEVPSNLILNKVGARIWIARVMITWGIVSGLMAFVQGTTSFYALRFLLGVAEAGFFPGIILYLSFWFPARRRAAVTAIFMAAAPLSTVLGSPISGALMEMHGFLGLAGWQWMFLIEAAPAVILGVVVLFYLTDRPEKAKWLSEDERNWLVKTMNAEQAAKGKASHSILAGLADIRVIALALVYFGTSAGLYTLGIWAPQIIKEFGLSSLQVGFINAVPGIFAVAAMVLWARHSDKTGERTWHVVGACLLAAVGLAFATGATSVFTVLIALTLVNIGISCSKPPLWSMPTLFLSGPAAAAGIATINSIGNLGGFVGPSMIGWIKDTTGSFAGGLYFVAGLLVVSAIVTLVLSRTAPENGGKVAPVQHR | Function: Component of the tartrate utilization system and may allow entry of tartrate and tartrate dehydrogenase.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46253
Sequence Length: 433
Subcellular Location: Cell membrane
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P9WJ60 | MNLVSEKEFLDLPLVSVAEIVRCRGPKVSVFPFDGTRRWFHLECNPQYDDYQQAALRQSIRILKMLFEHGIETVISPIFSDDLLDRGDRYIVQALEGMALLANDEEILSFYKEHEVHVLFYGDYKKRLPSTAQGAAVVKSFDDLTISTSSNTEHRLCFGVFGNDAAESVAQFSISWNETHGKPPTRREIIEGYYGEYVDKADMFIGFGRFSTFDFPLLSSGKTSLYFTVAPSYYMTETTLRRILYDHIYLRHFRPKPDYSAMSADQLNVLRNRYRAQPDRVFGVGCVHDGIWFAEG | Function: Tuberculosinyl transferase that catalyzes the condensation of adenosine and tuberculosinyl diphosphate (TbPP) to generate 1-tuberculosinyladenosine (1-TbAd), which acts as an antiacid that directly protects M.tuberculosis from acid pH and physically remodels M.tuberculosis phagolysosomes. In addition, acts as a phosphatase that catalyzes the diphosphate-removal from TbPP to produce both tuberculosinol (TOH) and isotuberculosinol (iso-TOH).
Catalytic Activity: adenosine + H(+) + tuberculosinyl diphosphate = 1-tuberculosinyladenosine + diphosphate
Sequence Mass (Da): 34031
Sequence Length: 296
EC: 2.5.1.153
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B7NDV3 | MRFAIVVTGPAYGTQQASSAFQFAQALIAEGHELSSVFFYREGVYNANQLTSPASDEFDLVRGWQQLNAQHGVALNICVAAALRRGIVDETEAGRLGLASSNLQSGFTLSGLGALAEASLTCDRVVQF | Function: Part of a sulfur-relay system required for 2-thiolation of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions. Accepts sulfur from TusA and transfers it in turn to TusE.
Sequence Mass (Da): 13614
Sequence Length: 128
Subcellular Location: Cytoplasm
EC: 2.8.1.-
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A4WFD8 | MRFALMVTGPAYGTQQASSALQFAQAVLAEGHELSSVFFYREGVYNANQFTSPASDEYDLVRGWQALNETQGVELHICVAAALRRGVADETEAKRLGLSGANLQHGFTLSGLGALAQAALTCDRMVQF | Function: Part of a sulfur-relay system required for 2-thiolation of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions. Accepts sulfur from TusA and transfers it in turn to TusE.
Sequence Mass (Da): 13758
Sequence Length: 128
Subcellular Location: Cytoplasm
EC: 2.8.1.-
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P44762 | MRYVIAVKSPIYGKQGAFLAYQFAESLIKKEHEISQIFFFQDGVSNGNALVYPANDEVNLQKHWQMFSITYNVPLHLCVAASQRRGVVDNLTTPTTAHYNLAEGFTIAGLGEFIAASLNADRVITL | Function: Could be part of a sulfur-relay system.
Sequence Mass (Da): 13997
Sequence Length: 126
Subcellular Location: Cytoplasm
EC: 2.8.1.-
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A0A348G5W2 | MRRSYVLLAFAIVLIISIISAQVEADASSDAFADAVADAVADPIKGKKIMKNMGKAMKIAGKVAKAMAPIVVPLIVSAAGK | Function: Cationic amphipathic alpha-helical peptide with antimicrobial activities against E.coli (MIC=3.1), and S.aureus (MIC=3.1 uM). Also shows histamine-releasing activity (33.6% at 10 uM). Does not have activity against S.cerevisiae. Does not show hemolytic activity, even at 50 uM.
PTM: Truncated sequences of this peptide have also been found in the venom. It is possible they have been cleaved in the venom.
Sequence Mass (Da): 8342
Sequence Length: 81
Subcellular Location: Secreted
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Q75WH3 | MKVFSFTVVVVMILSLSAFVLAGDEGDVMKKIVAMEEAVEERACLAEYQKCEGSTVPCCPGLSCSAGRFRKTKLCTK | Function: Inhibits Kv11.1/KCNH2/ERG1, Kv1.1/KCNA1 and Kv1.3/KCNA3 voltage-gated potassium channels and Nav1.7/SCN9A voltage-gated sodium channels . In vivo, intracranial injection into mice causes lack of coordination for 10 min, followed by fast recovery.
Sequence Mass (Da): 8342
Sequence Length: 77
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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Q9Y6I9 | MSDLLLLGLIGGLTLLLLLTLLAFAGYSGLLAGVEVSAGSPPIRNVTVAYKFHMGLYGETGRLFTESCSISPKLRSIAVYYDNPHMVPPDKCRCAVGSILSEGEESPSPELIDLYQKFGFKVFSFPAPSHVVTATFPYTTILSIWLATRRVHPALDTYIKERKLCAYPRLEIYQEDQIHFMCPLARQGDFYVPEMKETEWKWRGLVEAIDTQVDGTGADTMSDTSSVSLEVSPGSRETSAATLSPGASSRGWDDGDTRSEHSYSESGASGSSFEELDLEGEGPLGESRLDPGTEPLGTTKWLWEPTAPEKGKE | Function: Major reticulophagy (also called ER-phagy) receptor that acts independently of other candidate reticulophagy receptors to remodel subdomains of the endoplasmic reticulum into autophagosomes upon nutrient stress, which then fuse with lysosomes for endoplasmic reticulum turnover . The ATG8-containing isolation membrane (IM) cradles a tubular segment of TEX264-positive ER near a three-way junction, allowing the formation of a synapse of 2 juxtaposed membranes with trans interaction between the TEX264 and ATG8 proteins . Expansion of the IM would extend the capture of ER, possibly through a 'zipper-like' process involving continued trans TEX264-ATG8 interactions, until poorly understood mechanisms lead to the fission of relevant membranes and, ultimately, autophagosomal membrane closure . Also involved in the repair of covalent DNA-protein cross-links (DPCs) during DNA synthesis: acts by bridging VCP/p97 to covalent DNA-protein cross-links (DPCs) and initiating resolution of DPCs by SPRTN .
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 34189
Sequence Length: 313
Domain: The LIR motif in the cytosol-facing C-terminal region is involved in the interaction with ATG8 proteins.
Subcellular Location: Endoplasmic reticulum membrane
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E9Q137 | MPDLLLLGLIGALTLLLLLTLLAFAGYSGLLTGVTVSAGSPPIRNITVAYKFHVGSYGDTGHLFTESCSISPKLRSIAVYYDNPHTVPPEKCRCAVGSILSEGEESPSPELIHLYQKFGFKIFSFPAPSHVVIATFPYTTPISIWLAARRVHPALDTYIKERKLCAHPRLEIYHQDKIHFMCPLARQGDFYVPEVKETERKCRELAEATDTQTDGTGADTSDASSVSLDVRPGSRETSATTLSPGAGNRGWDDGDNRSEHSYSESGASGSSFEELDLEGEGPLGEPRLNPEAKLLGPPRELSTPERGEE | Function: Major reticulophagy (also called ER-phagy) receptor that acts independently of other candidate reticulophagy receptors to remodel subdomains of the endoplasmic reticulum into autophagosomes upon nutrient stress, which then fuse with lysosomes for endoplasmic reticulum turnover. The ATG8-containing isolation membrane (IM) cradles a tubular segment of TEX264-positive ER near a three-way junction, allowing the formation of a synapse of 2 juxtaposed membranes with trans interaction between the TEX264 and ATG8 proteins. Expansion of the IM would extend the capture of ER, possibly through a 'zipper-like' process involving continued trans TEX264-ATG8 interactions, until poorly understood mechanisms lead to the fission of relevant membranes and, ultimately, autophagosomal membrane closure. Also involved in the repair of covalent DNA-protein cross-links (DPCs) during DNA synthesis: acts by bridging VCP/p97 to covalent DNA-protein cross-links (DPCs) and initiating resolution of DPCs by SPRTN.
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 33590
Sequence Length: 309
Domain: The LIR motif in the cytosol-facing C-terminal region is involved in the interaction with ATG8 proteins.
Subcellular Location: Endoplasmic reticulum membrane
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B3EWT3 | GLWIKGNYCLRGRCLPGGRKCCNGRPCECFAKICSCKPKLIGKLSALKKHT | PTM: Contains 4 disulfide bonds.
Sequence Mass (Da): 5611
Sequence Length: 51
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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P83996 | IACAPRFSLCNSDKECCKGLRCQSRIANMWPTFCSQ | Function: Neurotoxin. Causes spastic paralysis and death in mice. Moderate inhibitor of L-type calcium channels (Cav1/CACNA1).
Sequence Mass (Da): 4069
Sequence Length: 36
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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P85267 | GCVGHRKSCEHDKKNGCCYFMTCNCWHPMGQ | Function: Antagonist of L-type calcium channels (Cav1/CACNA1).
Sequence Mass (Da): 3561
Sequence Length: 31
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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P81694 | MKVLIISAVLFITIFSNISAEIEDDFLEDESFEAEDIIPFFENEQARSCIPKHEECTNDKHNCCRKGLFKLKCQCSTFDDESGQPTERCACGRPMGHQAIETGLNIFRGLFKGKKKNKKTKG | Function: Spider venom toxin that shows calcium channel blocking activity and exhibits cytolytic activity by affecting the outer leaflet curvature and/or pore formation across the membrane . It blocks L-type calcium channels (Cav1/CACNA1) in mammalian neurons at nanomolar concentrations. Furthermore, it produces a slow voltage-independent block of mid/low and high voltage-activated calcium channels in cockroach neurons . Potassium ions, histamine, M-ctenitoxin-Cs1a (AC P83619), CSTX-9 (AC P58604), and CSTX-13 (AC P83919) synergistically increase the insecticidal activity of this toxin . In vivo, it causes paralysis in blow flies and provokes death in drosophila .
Sequence Mass (Da): 13840
Sequence Length: 122
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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Q75WG6 | MKLTLFILIVFVVLANVYAAGISERNIIGGRVIKLCGGGAQKCCDREPRCDPCRKCVQSFHSGVYMCSDKKSNCS | Function: No toxicity is observed upon intracranial injection into mice and intrathorax injection into crickets.
PTM: Contains 4 disulfide bonds.
Sequence Mass (Da): 8203
Sequence Length: 75
Subcellular Location: Secreted
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Q75WG5 | MKILEKALLENDSAAEEESRNLRTKRCARKRAWCEKTENCCCPMKCIYAWYNGQSSCDHTISTIWTSCPK | Function: Inhibits tetrodotoxin-sensitive sodium channels (Nav) (By similarity). Intracranial injection into mice causes strong convulsions and death. Intrathorax injection into crickets causes paralysis prolonged for 2 min, followed by recovery.
Sequence Mass (Da): 8135
Sequence Length: 70
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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P0C2V1 | ECSKQLGESCKCNKQCCGATVICGTIYVGGKEENLCIEKTSNNAILNFFGKIAHVVENGLSFSCD | Function: Intrathorax injection into crickets causes paralysis prolonged for more than 60 min, followed by recovery.
PTM: Contains 4 disulfide bonds.
Sequence Mass (Da): 6951
Sequence Length: 65
Subcellular Location: Secreted
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P83557 | CMGYDIHCTDRLPCCFGLECVKTSGYWWYKKTYCRRKS | Function: Insecticidal neurotoxin. Shows competition for site 3 of insect voltage-gated sodium channels (Nav).
Sequence Mass (Da): 4602
Sequence Length: 38
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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P83558 | MMTLSPFLLLLIAAVVIGNASEGEVKNEFEERLKDEFKDPSRSEVAEVILLRELEVLEETLFGKEMTSDTEENRNSREKRCMGYDIECNENLPCCKHRKLECVETSGYWWYKRKYCRPIKG | Function: Insecticidal neurotoxin. Shows competition for site 3 of insect voltage-gated sodium channels (Nav). Induces flaccid paralysis when injected into lepidopteran larvae. Is not toxic to mice when injected intracranially at 20 pmol/g.
Sequence Mass (Da): 14188
Sequence Length: 121
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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P83560 | MKTLVIACVALVLVVVHGEVIEEVNEKQLQESVEEKYSLLQRLEKLDEAITAEENRNSRVRRCGSKRAWCKEKKDCCCGYNCVYAWYNQQSSCERKWKYLFTGEC | Function: Selectively slows channel inactivation of mammalian Nav1.1/SCN1A, Nav1.3/SCN3A, and Nav1.6/SCN8A and shows higher affinity for insect Nav1/para channels (site 3). Induces tonic repetitive firing of nerve impulses in insect neurons accompanied by plateau potentials.
Sequence Mass (Da): 12289
Sequence Length: 105
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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P83561 | MKAPATTLILVMSLISVLWATPDLEEGDLLAELGDLIATDDEYPMKPEERGCKLTFWKCKNKKECCGWNACALGICMPR | Function: Insect and vertebrate active toxin. Binds to site 4 of mammalian voltage-gated sodium channels and shifts the activation voltage of the mammalian Nav1.2a/SCN2A channel to more hyperpolarized voltages, whereas the insect channel, DmNav1 (para), is not affected. Competes for binding at site 3 of the insect sodium channel. Causes temporary paralysis when injected into lepidopteran larvae at 8.6 nmol/g. A low intracranial injection dose into mice causes lacrimation, closure of the eyes and sweating. A high injection dose causes extensive lacrimation and death.
Sequence Mass (Da): 8791
Sequence Length: 79
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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P83562 | MRTIVFLIVSILLLSSAVLMLAEGNAASHELQEYPIEESLEEQRKCVDGSCDPYSSDAPRCCGSQICQCIFFVPCYCKYRGK | Function: Induces flaccid paralysis when injected into lepidopteran larvae. Intracranial injection into mice causes awkwardness of movement and laboured respiration until death.
Sequence Mass (Da): 9159
Sequence Length: 82
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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Q75WH6 | MKVFSFTIGLVVIISLFAFALAYDEETDLMKKLVEMERAIEQRIICAPEGGPCVVGIGCCKGYSCAPGLLGLVGHCQ | Function: Intrathorax injection into crickets causes paralysis prolonged for more than 60 min, followed by recovery.
Sequence Mass (Da): 8255
Sequence Length: 77
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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Q75WH4 | MKFATFAFTLCVVISLSVLVLADEEEKDFLMNLIQPLKESEERQFCGTNGKPCVNGQCCGALRCVVTYHYADGVCLKMNP | Function: Inhibits Kv11.1/KCNH2/ERG1, Kv1.1/KCNA1, Kv1.2/KCNA2 voltage-gated potassium channels and Nav1.7/SCN9A voltage-gated sodium channels . In vivo, no toxicity is observed upon intracranial injection into mice and intrathorax injection into crickets.
PTM: Contains 3 disulfide bonds.
Sequence Mass (Da): 8882
Sequence Length: 80
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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A8X3V8 | MSSLTNPTTVMEEEEVPVAAPIRRGNKNPRRYSLVHQASCETQHHIGIRRQNTIQHRKQLTDQMREQKILQQLNDEGVEVIFAANDVSSIDFSVIVTSTDYISTFVSDILYNMKSAGVQICHVETRESKAVSGHDVLLDCRATKNQLIKAAELLTQNHVALTHFSIFSKKSVEKSQSMIWFPRHISELDQCSKCITKYEPTTDPRHPGHGDDEYIARRKFLNDQALEFKFGDEIGYVEYTEDEHATWKAVYEKLGGLHESHTCSVYRQNLKILQKEKVLTADRIPQIRDVNKFLQKKTGFELRPCSGLLSARDFLASLAFRVFQTTTYLRHHKSPHHSPEPDLIHELLGHVPMFSDPLLAQMSQDIGLMSLGASDEHIEKLATVYWFIVEFGLCKEDGKLKAIGAGLLSAYGELIHACSDAPEHKDFDPAVTAIQKYEDDDYQPLYFVADSIHDALAKLRKYASSMDRPFSVVYDPFTKSIETIQSSADLEKAFSRLSNDLSAITHAADRMKISITA | Function: Involved in the synthesis of catecholamines, such as dopamine. Has a role in serotonin signaling. Required for normal explorative and foraging behavior (By similarity).
Catalytic Activity: (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-tyrosine + O2 = (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + L-dopa
Sequence Mass (Da): 58573
Sequence Length: 517
Pathway: Catecholamine biosynthesis; dopamine biosynthesis; dopamine from L-tyrosine: step 1/2.
Subcellular Location: Cytoplasm
EC: 1.14.16.2
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P90986 | MSSLTNNTFMEEEPRGVTVIATKVAENSKNPRRYSLVHQASCETQHHKGIRRQNTIQHRKQLTDQMRCQKILQQLNDEGIEVIFTANDVTPIEFSIILTSTDPTLSNFVSDILQNMSSAKVQICHVETRGNEASHDVLLACKATKNQLIHSAELLTQNHVALTKFSIFAKKLSDEKNQSQIWFPRHISELDQCSKCITKYEPTTDPRHPGHGDVAYIARRKFLNDQALEFKFGDEIGYVDYTEEEHATWKAVYEKLGDLHLSHTCAVYRQNLKILQEEKVLTADRIPQIRDVNKFLQKKTGFELRPCSGLLSARDFLASLAFRVFQTTTYLRHHKSPHHSPEPDLIHELLGHVPMFSDPLLAQMSQDIGLMSLGASDEHIEKLSTVYWFIVEFGLCKEDGKLKAIGAGLLSAYGELMHACSDAPEHKDFDPAVTAVQKYEDDDYQPLYFVADSIHDALAKLRKYASSMDRPFSVVYDPFTKSIEAIESSADLEKAFSRLSNDLSAITHAADRMKISITM | Function: Involved in the synthesis of catecholamines, such as dopamine. Has a role in serotonin signaling. Required for normal explorative and foraging behavior. In response to food, involved in promoting the dopamine-mediated suppression of crh-1/CREB1 transcription factor activation in cholinergic SIA neurons . Modulates male mating behavior by controlling the protrusion of copulatory spicules from the tail of males during hermaphrodite vulval location .
Catalytic Activity: (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-tyrosine + O2 = (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + L-dopa
Sequence Mass (Da): 58828
Sequence Length: 519
Pathway: Catecholamine biosynthesis; dopamine biosynthesis; dopamine from L-tyrosine: step 1/2.
Subcellular Location: Cytoplasm
EC: 1.14.16.2
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P18459 | MMAVAAAQKNREMFAIKKSYSIENGYPSRRRSLVDDARFETLVVKQTKQTVLEEARSKANDDSLEDCIVQAQEHIPSEQDVELQDEHANLENLPLEEYVPVEEDVEFESVEQEQSESQSQEPEGNQQPTKNDYGLTEDEILLANAASESSDAEAAMQSAALVVRLKEGISSLGRILKAIETFHGTVQHVESRQSRVEGVDHDVLIKLDMTRGNLLQLIRSLRQSGSFSSMNLMADNNLNVKAPWFPKHASELDNCNHLMTKYEPDLDMNHPGFADKVYRQRRKEIAEIAFAYKYGDPIPFIDYSDVEVKTWRSVFKTVQDLAPKHACAEYRAAFQKLQDEQIFVETRLPQLQEMSDFLRKNTGFSLRPAAGLLTARDFLASLAFRIFQSTQYVRHVNSPYHTPEPDSIHELLGHMPLLADPSFAQFSQEIGLASLGASDEEIEKLSTVYWFTVEFGLCKEHGQIKAYGAGLLSSYGELLHAISDKCEHRAFEPASTAVQPYQDQEYQPIYYVAESFEDAKDKFRRWVSTMSRPFEVRFNPHTERVEVLDSVDKLETLVHQMNTEILHLTNAISKLRRPF | Function: Plays an important role in the physiology of adrenergic neurons.
Catalytic Activity: (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-tyrosine + O2 = (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + L-dopa
Sequence Mass (Da): 65996
Sequence Length: 579
Pathway: Catecholamine biosynthesis; dopamine biosynthesis; dopamine from L-tyrosine: step 1/2.
Subcellular Location: Cytoplasm
EC: 1.14.16.2
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P07101 | MPTPDATTPQAKGFRRAVSELDAKQAEAIMVRGQGAPGPSLTGSPWPGTAAPAASYTPTPRSPRFIGRRQSLIEDARKEREAAVAAAAAAVPSEPGDPLEAVAFEEKEGKAVLNLLFSPRATKPSALSRAVKVFETFEAKIHHLETRPAQRPRAGGPHLEYFVRLEVRRGDLAALLSGVRQVSEDVRSPAGPKVPWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQVYRQRRKLIAEIAFQYRHGDPIPRVEYTAEEIATWKEVYTTLKGLYATHACGEHLEAFALLERFSGYREDNIPQLEDVSRFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGASDEEIEKLSTLYWFTVEFGLCKQNGEVKAYGAGLLSSYGELLHCLSEEPEIRAFDPEAAAVQPYQDQTYQSVYFVSESFSDAKDKLRSYASRIQRPFSVKFDPYTLAIDVLDSPQAVRRSLEGVQDELDTLAHALSAIG | Function: Catalyzes the conversion of L-tyrosine to L-dihydroxyphenylalanine (L-Dopa), the rate-limiting step in the biosynthesis of cathecolamines, dopamine, noradrenaline, and adrenaline. Uses tetrahydrobiopterin and molecular oxygen to convert tyrosine to L-Dopa (PubMed:17391063, PubMed:1680128, PubMed:15287903, PubMed:8528210, Ref.18, PubMed:34922205, PubMed:24753243). In addition to tyrosine, is able to catalyze the hydroxylation of phenylalanine and tryptophan with lower specificity (By similarity). Positively regulates the regression of retinal hyaloid vessels during postnatal development (By similarity).
PTM: Phosphorylated on Ser-19, Ser-62 and Ser-71 by several protein kinases with different site specificities. Phosphorylation at Ser-62 and Ser-71 leads to an increase of TH activity . Phosphorylation at Ser-71 activates the enzyme and also counteracts the feedback inhibition of TH by catecholamines . Phosphorylation of Ser-19 and Ser-62 triggers the proteasomal degradation of TH through the ubiquitin-proteasome pathway (By similarity). Phosphorylation at Ser-62 facilitates transport of TH from the soma to the nerve terminals via the microtubule network . Phosphorylation at Ser-19 induces the high-affinity binding to the 14-3-3 protein YWHAG; this interaction may influence the phosphorylation and dephosphorylation of other sites . Ser-19 increases the phosphorylation at Ser-71 in a hierarchical manner, leading to increased activity (By similarity).
Catalytic Activity: (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-tyrosine + O2 = (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + L-dopa
Sequence Mass (Da): 58600
Sequence Length: 528
Pathway: Catecholamine biosynthesis; dopamine biosynthesis; dopamine from L-tyrosine: step 1/2.
Subcellular Location: Cytoplasm
EC: 1.14.16.2
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A0A060X6Z0 | MPISSSSSSSTKSMRRAASELERSDSVTSPRFIGRRQSLIEDARKEREAAAAAAEAAEATEQIVFEEEDGKALLNLFFTLRSSKTPALSRSLKVFETFEAKIHHLETRPCRKPRDSLEGLEYFVRCEVHLSDVSTLISSIKRIAEDVKTTKEVKFHWFPKKISELDRCHHLITKFDPDLDQEHPGFTDPVYRQRRKMIGDIAFRYKQGEPIPRVEYTEEEIGTWREVYSTLRDLYTTHACSEHLEAFNLLERHCGYSPENIPQLEDVSRFLRERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSPEPDCVHELLGHVPILADRVFAQFSQNIGLASLGASEEDIEKLSTLYWFTVEFGLCKQGGIVKAYGAGLLSSYGELVHALSDEPERREFDPEAAAIQPYQDQNYQSVYFVSESFTDAKEKLRSYVAGIKRPFSVRFDPYTYSIEVLDNPLKIRGGLESVKDELKMLTDALNVLA | Function: Plays an important role in the physiology of adrenergic neurons.
Catalytic Activity: (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-tyrosine + O2 = (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + L-dopa
Sequence Mass (Da): 55713
Sequence Length: 489
Pathway: Catecholamine biosynthesis; dopamine biosynthesis; dopamine from L-tyrosine: step 1/2.
Subcellular Location: Cytoplasm
EC: 1.14.16.2
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Q74PY8 | MFLAQEIIRKKRDGQPLSEEEIRFFINGIRDNVVSEGQIAALAMTIYFHDMSMPERVALTMAMRDSGTVLNWKSLNLNGPLVDKHSTGGVGDVTSLMLGPMVAACGGYVPMISGRGLGHTGGTLDKLEAIPGFDIFPDDNAFRKIIQNVGVAIIGQTSSLAPADKRFYATRDITATVDSIPLITASILAKKLAEGLDALVMDVKVGSGAFMPTYSLSADLAQAIVGVANGAGCKTTALLTDMNQVLASSAGNGVEVREAVRFLTGEYRNPRLLEVTMALCVEMLLSGGLAHDEADARAKLQAVLDNGKAAEVFGRMVAAQKGPADFVERYDSYLPVATLSKPVFAEQTGIITAMDTRALGMAVVALGGGRRRATDPIDYSVGLTEMARLGTRVDGQQPLAVIHANNEDDWQQEAEVVRAAITLGNNTPEETPVIYRRITE | Function: The enzymes which catalyze the reversible phosphorolysis of pyrimidine nucleosides are involved in the degradation of these compounds and in their utilization as carbon and energy sources, or in the rescue of pyrimidine bases for nucleotide synthesis.
Catalytic Activity: phosphate + thymidine = 2-deoxy-alpha-D-ribose 1-phosphate + thymine
Sequence Mass (Da): 46975
Sequence Length: 440
Pathway: Pyrimidine metabolism; dTMP biosynthesis via salvage pathway; dTMP from thymine: step 1/2.
EC: 2.4.2.4
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O60078 | MKETFQVGIIGFGDMGRLYAEYISKAGWRVNVCDRPENYESIQATYGNGGYTVLKDGFQVSRTSDYILYSVEAEHIDKVVALYGPATKVGAIVGGQTSCKAPEMNAFEKYLPEDVDIISCHSMHGPKVNPKSQPLVIIRHRASDEHFEIVNEILSCFKSSVVYLSAKEHDRITADTQAVTHAAFLTMGLAWHANNQYPWEINRWCGGIENIKMNLSMRIYSSKWHVYAGLAILNPEAQRQIQQYASSVTELFKLAISGKAKEYEDRIRNAGKFVFGENMDRNSSGLLLSDELLDQYSISNIPKDESKRNSHLSILAIVDSWSKLGIHPQNHMICSTPLFRLWVGVSEYVFRHPGLLDSCIYTATKHNDFSPDDLEFVVAVRSWSECVAAKDFTTYKKRFLETQEYFRPRFEEATRVGNAMISKLLENLQKM | Catalytic Activity: NADP(+) + prephenate = 3-(4-hydroxyphenyl)pyruvate + CO2 + NADPH
Sequence Mass (Da): 48906
Sequence Length: 431
Pathway: Amino-acid biosynthesis; L-tyrosine biosynthesis; (4-hydroxyphenyl)pyruvate from prephenate (NADP(+) route): step 1/1.
Subcellular Location: Cytoplasm
EC: 1.3.1.13
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P20049 | MVSEDKIEQWKATKVIGIIGLGDMGLLYANKFTDAGWGVICCDREEYYDELKEKYASAKFELVKNGHLVSRQSDYIIYSVEASNISKIVATYGPSSKVGTIVGGQTSCKLPEIEAFEKYLPKDCDIITVHSLHGPKVNTEGQPLVIINHRSQYPESFEFVNSVMACLKSKQVYLTYEEHDKITADTQAVTHAAFLSMGSAWAKIKIYPWTLGVNKWYGGLENVKVNISLRIYSNKWHVYAGLAITNPSAHQQILQYATSATELFSLMIDNKEQELTDRLLKAKQFVFGKHTGLLLLDDTILEKYSLSKSSIGNSNNCKPVPNSHLSLLAIVDSWFQLGIDPYDHMICSTPLFRIFLGVSEYLFLKPGLLEQTIDAAIHDKSFIKDDLEFVISAREWSSVVSFANFDIYKKQFQSVQKFFEPMLPEANLIGNEMIKTILSHSSDRSAAEKRNT | Catalytic Activity: NADP(+) + prephenate = 3-(4-hydroxyphenyl)pyruvate + CO2 + NADPH
Sequence Mass (Da): 50923
Sequence Length: 452
Pathway: Amino-acid biosynthesis; L-tyrosine biosynthesis; (4-hydroxyphenyl)pyruvate from prephenate (NADP(+) route): step 1/1.
EC: 1.3.1.13
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Q944B6 | MAETLITKPPLSLSFTSLSSMLPSLSLSTANRHLSVTDTIPLPNSNSNATPPLRIAIIGFGNYGQFLAETLISQGHILFAHSRSDHSSAARRLGVSYFTDLHDLCERHPDVVLLCTSILSIENILKTLPFQRLRRNTLFVDVLSVKEFAKTLLLQYLPEDFDILCTHPMFGPQSVSSNHGWRGLRFVYDKVRIGEERLRVSRCESFLEIFVREGCEMVEMSVTDHDKFAAESQFITHTLGRLLGMLKLISTPINTKGYEALLDLAENICGDSFDLYYGLFVYNNNSLEVLERIDLAFEALRKELFSRLHGVVRKQSFEGEAKKVHVFPNCGENDASLDMMRSEDVVVKYEYNSQVSGSVNDGSRLKIGIVGFGNFGQFLGKTMVKQGHTVLAYSRSDYTDEAAKLGVSYFSDLDDLFEEHPEVIILCTSILSTEKVLESLPFQRLKRSTLFVDVLSVKEFPRNLFLQTLPQDFDILCTHPMFGPESGKNGWNNLAFVFDKVRIGMDDRRKSRCNSFLDIFAREGCRMVEMSCAEHDWHAAGSQFITHTVGRLLEKLSLESTPIDTKGYETLLKLVENTAGDSFDLYYGLFLYNPNAMEQLERFHVAFESLKTQLFGRLHSQHSHELAKSSSPKTTKLLTS | Function: Involved in the biosynthesis of tyrosine. Has no prephenate dehydrogenase activity.
Catalytic Activity: L-arogenate + NADP(+) = CO2 + L-tyrosine + NADPH
Sequence Mass (Da): 72301
Sequence Length: 640
Pathway: Amino-acid biosynthesis; L-tyrosine biosynthesis; L-tyrosine from L-arogenate (NADP(+) route): step 1/1.
Subcellular Location: Plastid
EC: 1.3.1.78
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Q9LMR3 | MLLHFSPAKPLISPPNLRRNSPTFLISPPRSLRIRAIDAAQIFDYETQLKSEYRKSSALKIAVLGFGNFGQFLSKTLIRHGHDLITHSRSDYSDAANSIGARFFDNPHDLCEQHPDVVLLCTSILSTESVLRSFPFQRLRRSTLFVDVLSVKEFPKALFIKYLPKEFDILCTHPMFGPESGKHSWSGLPFVYDKVRIGDAASRQERCEKFLRIFENEGCKMVEMSCEKHDYYAAGSQFVTHTMGRVLEKYGVESSPINTKGYETLLDLVENTSSDSFELFYGLFMYNPNALEQLERLDMAFESVKKELFGRLHQQYRKQMFGGEVQSPKKTEQKLLNDGGVVPMNDISSSSSSSSSSS | Function: Involved in the biosynthesis of tyrosine. Has a weak prephenate dehydrogenase activity.
Catalytic Activity: L-arogenate + NADP(+) = CO2 + L-tyrosine + NADPH
Sequence Mass (Da): 40633
Sequence Length: 358
Pathway: Amino-acid biosynthesis; L-tyrosine biosynthesis; L-tyrosine from L-arogenate (NADP(+) route): step 1/1.
Subcellular Location: Plastid
EC: 1.3.1.78
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P20692 | MNQMKDTILLAGLGLIGGSIALAIKKNHPGKRIIGIDISDEQAVAALKLGVIDDRADSFISGVKEAATVIIATPVEQTLVMLEELAHSGIEHELLITDVGSTKQKVVDYADQVLPSRYQFVGGHPMAGSHKSGVAAAKEFLFENAFYILTPGQKTDKQAVEQLKNLLKGTNAHFVEMSPEEHDGVTSVISHFPHIVAASLVHQTHHSENLYPLVKRFAAGGFRDITRIASSSPAMWRDILLHNKDKILDRFDEWIREIDKIRTYVEQEDAENLFRYFKTAKDYRDGLPLRQKGAIPAFYDLYVDVPDHPGVISEITAILAAERISITNIRIIETREDINGILRISFQSDDDRKRAEQCIEARAEYETFYAD | Catalytic Activity: NAD(+) + prephenate = 3-(4-hydroxyphenyl)pyruvate + CO2 + NADH
Sequence Mass (Da): 41434
Sequence Length: 371
Pathway: Amino-acid biosynthesis; L-tyrosine biosynthesis; (4-hydroxyphenyl)pyruvate from prephenate (NAD(+) route): step 1/1.
EC: 1.3.1.12
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P07023 | MVAELTALRDQIDEVDKALLNLLAKRLELVAEVGEVKSRFGLPIYVPEREASMLASRRAEAEALGVPPDLIEDVLRRVMRESYSSENDKGFKTLCPSLRPVVIVGGGGQMGRLFEKMLTLSGYQVRILEQHDWDRAADIVADAGMVIVSVPIHVTEQVIGKLPPLPKDCILVDLASVKNGPLQAMLVAHDGPVLGLHPMFGPDSGSLAKQVVVWCDGRKPEAYQWFLEQIQVWGARLHRISAVEHDQNMAFIQALRHFATFAYGLHLAEENVQLEQLLALSSPIYRLELAMVGRLFAQDPQLYADIIMSSERNLALIKRYYKRFGEAIELLEQGDKQAFIDSFRKVEHWFGDYAQRFQSESRVLLRQANDNRQ | Catalytic Activity: chorismate = prephenate
Sequence Mass (Da): 42043
Sequence Length: 373
Pathway: Amino-acid biosynthesis; L-tyrosine biosynthesis; (4-hydroxyphenyl)pyruvate from prephenate (NAD(+) route): step 1/1.
Subcellular Location: Cytoplasm
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C1D070 | MQQYLDFMRHVLEHGTEKTDRTGTGTLSVFGHQMRFDLQEGFPLVTTKRTHLKSIIHELLWFLQGSSNVAYLREHGVTIWDEWADPDGELGPVYGVQWRSWPTPDGRHIDQIAQVVEQIRRTPDSRRLIVSAWNVGEIEQMALPPCHAFFQFYVADGRLSCQLYQRSADIFLGVPFNIASYALLTLMVAQVTGLKPGEFIWTGGDCHLYTNHLEQARKQLTREPRTLPVMRLNPDVRELDGFRFEDFTLEGYDPHPGIKAPVAV | Function: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP
Sequence Mass (Da): 30291
Sequence Length: 264
Pathway: Pyrimidine metabolism; dTTP biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.1.1.45
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O76511 | MVLTPTKDGPDQESMPLPADNGESPSKQQAPVNRDEMHYLDLLRHIIANGEQRMDRTEVGTLSVFGSQMRFDMRNSFPLLTTKRVFFRAVAEELLWFVAGKTDAKLLQAKNVHIWDGNSSREFLDKMGFTGRAVGDLGPVYGFQWRHFGAQYGTCDDDYSGKGIDQLRQVIDTIRNNPSDRRIIMSAWNPLDIPKMALPPCHCLAQFYVSEKRGELSCQLYQRSADMGLGVPFNIASYALLTHMIAHVTGLKPGDFVHTMGDTHVYLNHVEPLKEQLERTPRPFPKLIIKRQVQDIEDFRFEDFQIVDYNPHPKIQMDMAV | Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP
Sequence Mass (Da): 36657
Sequence Length: 321
Pathway: Pyrimidine metabolism; dTTP biosynthesis.
EC: 2.1.1.45
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A7HVX4 | MQQYLDLMRLARDTGVTKTDRTGTGTRSIFGHQMRFDLSEGFPLVTTKKLHLKSIIHELLWFIAGDTNTRYLKANGVSIWDDWADENGELGPVYGHQWRSWPTPDGGKIDQIRNLVEQIKTNPDSRRLIVSAWNVADVDSMALPPCHCLFQFYVAEGKLSCQLYQRSADIFLGVPFNIASYALLTMMVAQVTGLKPGEFIHTFGDAHLYLNHLEQADKQLAREPKKLPVMHINPDVKSLFDFTYDDFTLEGYEAHPHISAPVAV | Function: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP
Sequence Mass (Da): 29936
Sequence Length: 264
Pathway: Pyrimidine metabolism; dTTP biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.1.1.45
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Q7N8U4 | MKQYLDLMTRVLAEGTPKADRTGTGTLSIFGHQMRFNLQDGFPLVTTKRCHIRSIIHELLWFLNGDTNIKYLHENGVTIWDEWADENGDLGPVYGKQWRAWGTADGRQIDQLKTVLEQLKSDPDSRRIIVSAWNVGELDKMALAPCHAFFQFYVADGKLSCQLYQRSCDVFLGLPFNIASYALLVHMMAQQCDLEVGDFVWTGGDTHLYSNHMEQTKLQLSREPRSLPKLVIKRKPASLFDYKFDDFEIVDYDPHPGIKAPVAI | Function: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP
Sequence Mass (Da): 30184
Sequence Length: 264
Pathway: Pyrimidine metabolism; dTTP biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.1.1.45
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Q9Z671 | MSEHQYLRLVSDILEKGDQRHDRTGVGTLSLFGAMMRFDLSKGRIPILTTKKVSYRLAIREMLWFLSGDTNIRPLVEQGVSIWSDWPLARYQAETGALLSKKEFEAKILADTEFAKKWGDLGPVYGRQWRRWQGSDGQVYDQIATLIETLKSNPSSRRMLFHGWNVAELKDMALPPCHMVYQYHVTSDGRLNSLLYQRSADVFLGLPFNLVGAAALQAMLADQAGLALGDLVWTGGDVHIYRNHIDQMKEQLAREPRAFPRLELTRHPNSITDYKIEDFAITGYDPHPPIKGAVAV | Function: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP
Sequence Mass (Da): 33586
Sequence Length: 296
Pathway: Pyrimidine metabolism; dTTP biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.1.1.45
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P39040 | MSRAYDLVVIGAGSGGLEAGWNAASLHKKRVAVIDLQKHHGPPHYAALGGTCVNVGCVPKKLMVTGANYMDTIRESAGFGWELDRESVRPNWKALIAAKNKAVSGINDSYEGMFADTEGLTFHQGFGALQDNHTVLVRESADPNSAVLETLDTEYILLATGSWPQHLGIEGDDLCITSNEAFYLDEAPKRALCVGGGYISIEFAGIFNAYKARGGQVDLAYRGDMILRGFDSELRKQLTEQLRANGINVRTHENPAKVTKNADGTRHVVFESGAEADYDVVMLAIGRVPRSQTLQLDKAGVEVAKNGAIKVDAYSKTNVDNIYAIGDVTDRVMLTPVAINEGAAFVDTVFANKPRATDHTKVACAVFSIPPMGVCGYVEEDAAKKYDQVAVYESSFTPLMHNISGSTYKKFMVRIVTNHADGEVLGVHMLGDSSPEIIQSVAICLKMGAKISDFYNTIGVHPTSAEELCSMRTPAYFYQKGKRVEKIDSNL | Cofactor: Binds 1 FAD per subunit.
Function: Trypanothione is the parasite analog of glutathione; this enzyme is the equivalent of glutathione reductase.
PTM: The N-terminus is blocked.
Catalytic Activity: NADP(+) + trypanothione = H(+) + NADPH + trypanothione disulfide
Sequence Mass (Da): 53229
Sequence Length: 491
Subcellular Location: Cytoplasm
EC: 1.8.1.12
|
Q6NUM6 | MDPSADTWDLSSPLISLWINRFYIYLGFAVSISLWICVQIVIEMQGFATVLAEAVTSLDLPVAIINLKEYDPDDHLIEEVTSKNVCVFLVATYTDGLPTESAEWFCKWLEEASIDFRFGKTYLKGMRDAVFGLGNSAYASHFNKVGKNVDKWLWMLGVHRVMSRGEGDCDVVKSKHGSIEANFRAWKTKFISQLQALQKGERKKSCGGHCKKGKCESHQHGSEEREEGSQEQDELHHRDTKEEEPFESSSEEEFGGEDHQSLNSIVDVEDLGKIMDHVKKEKREKEQQEEKSGLFRNMGRNEDGERRAMITPALREALTKQVDAPRERSLLQTHILWNESHRCMETTPSLACANKCVFCWWHHNNPVGTEWLWKMDQPEMILKEAIENHQNMIKQFKGVPGVKAERFEEGMTVKHCALSLVGEPIMYPEINRFLKLLHQCKISSFLVTNAQFPAEIRNLEPVTQLYVSVDASTKDSLKKIDRPLFKDFWQQFLDSLKALAVKQQRTVYRLMLVKAWNVDELQAYAQLVSLGNPDFIEVKGVTYCRESSASSLTMAHVPWHEEVVQFVRELVDLIPEYEIACEHEHSNCLLIAHRKFKIGGEWWTWIDYNRFQELIQEYEDSGGSKTFSAKDYMARTPHWALFGANERSFDPKDTRHQRKNKSKAISGC | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Probable component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes the condensation of N-methylguanine with 2 carbon atoms from pyruvate to form the tricyclic 4-demethylwyosine, an intermediate in wybutosine biosynthesis (By similarity).
Catalytic Activity: N(1)-methylguanosine(37) in tRNA(Phe) + pyruvate + S-adenosyl-L-methionine = 4-demethylwyosine(37) in tRNA(Phe) + 5'-deoxyadenosine + CO2 + H2O + L-methionine
Sequence Mass (Da): 76946
Sequence Length: 668
Pathway: tRNA modification; wybutosine-tRNA(Phe) biosynthesis.
EC: 4.1.3.44
|
Q8RXN5 | MSTTSSVRVRLAFVALLSATTFYCIHKYRRLKHLKNLSLNPSSTLKASRGKIFFISQTGTAKALAQRLHELCASNDIAFDIVDPHSYEPEDLPKETLVLFIASTWDGGKPPKNGEFLVNWLGESAEDFRVGSLLLSDCKFAVFGVGSRAYGESYNAVAKELSSRMIGLGGLEMIPVGEGDVDDGELDRAFQDWCDGVIRVLKGGSAQETNGVSQQIGAVEDDLEYYDSTDEEDEDNDADGGIVDLEDIAGKAPSKRNGVVKVTKVDGKKEMVTPVIRASLTKQGYKIIGSHSGVKICRWTKSQLRGRGGCYKHSFYGIESHRCMETTPSLACANKCVFCWRHHTNPVGKSWQWKMDEPSVIVKGALDLHKNMIKQMKGVPGVTPEKLQEGLNPRHCALSLVGEPIMYPEINALVDELHGRRISTFLVTNAQFPEKILMMKPITQLYVSVDAATKESLKAIDRPLFADFWERFIDSLKALQEKQQRTVYRLTLVKGWNTEELDAYFNLFSIGKPDFIEIKGVTYCGSSATSKLTMENVPWHTDVKAFSEALSLKSNGEYEVACEHAHSCCVLLGRTEKFKVDGKWFTWIDYEKFHDLVASGEPFTSTDYMAQTPSWAVYGAQEGGFDPGQLRYKKERNHPPKPQAVLA | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Probable component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes the condensation of N-methylguanine with 2 carbon atoms from pyruvate to form the tricyclic 4-demethylwyosine, an intermediate in wybutosine biosynthesis (By similarity).
Catalytic Activity: N(1)-methylguanosine(37) in tRNA(Phe) + pyruvate + S-adenosyl-L-methionine = 4-demethylwyosine(37) in tRNA(Phe) + 5'-deoxyadenosine + CO2 + H2O + L-methionine
Sequence Mass (Da): 72080
Sequence Length: 647
Pathway: tRNA modification; wybutosine-tRNA(Phe) biosynthesis.
EC: 4.1.3.44
|
Q08C92 | MSGVLNDVRDYTEGYLQVLWQNRLYVYSTAAVLIGVWFTVNMLFKKKKMVHPVSPLASKSVKKQEPASEAKKVIYVSGVKVFYGSQTGTAKGFAKELAEDVIAQGIQCEVIDMKDFDPEDRLAEECTSKIICVFLVATYTDGQPTESAEWFCKWLEEASTDFRYGKTYLKGMRYAVFGLGNSVYVGHFNTVSKSIDKWLWMLSAARIMTRGEGDCNVVKSRHGSVQADFQVWKGKFLNRLQALAKGEKKACSGNCKKASCKNKKKHKEEAEDNHSLAEKNNSEEELMESSSDEESSSEDEKSHGSVIDMEDLGNVMNHMKKAKQRMEEDEEDSQRVKQNGERKSECEEERREMITPALRDSLTKQGYKLIGSHSGVKLRRWTKSMLRGRGGCYKHTFYGIESHRCMETTPSLACANKCVFCWRHHTNPVGTEWRWKMDPAEKIIQEAMENHRNMIRQFRGVPGVRPERFEEGLTVKHCALSLVGEPIMYPEINSFLKLLHQQNISSFLVTNAQFPEEIRSLVPVTQLYVSVDASTKDSLKKIDRPLFKDFWQRFLDSLRALGEKQQRTVYRLTLVKAWNVDELKAYADLIALGQPDFIEVKGVTYCGESSASSLTMANVPWHEEVIYFVQQLANLLPDYEIACEHEHSNCLLLANHKFKVDGEWWTWIDYERFQELIQQYEESGGTKNFSAMDYMAKTPSWAVFGAGERGFDPTDTRFQRKNKTKDISGC | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Probable component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes the condensation of N-methylguanine with 2 carbon atoms from pyruvate to form the tricyclic 4-demethylwyosine, an intermediate in wybutosine biosynthesis (By similarity).
Catalytic Activity: N(1)-methylguanosine(37) in tRNA(Phe) + pyruvate + S-adenosyl-L-methionine = 4-demethylwyosine(37) in tRNA(Phe) + 5'-deoxyadenosine + CO2 + H2O + L-methionine
Sequence Mass (Da): 83549
Sequence Length: 730
Pathway: tRNA modification; wybutosine-tRNA(Phe) biosynthesis.
EC: 4.1.3.44
|
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