ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q9Z0J5 | MAAIVAALRGSSGRFRPQTRVLTRGTRGAAGAASAAGGQQNFDLLVIGGGSGGLACAKEAAQLGRKVAVADYVEPSPRGTKWGLGGTCVNVGCIPKKLMHQAALLGGMIRDAQHYGWEVAQPVQHNWKAMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVNEHTVHGVDKAGKVTQLSAKHIVIATGGRPKYPTQVKGALEHGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTVMMRSVPLRGFDQQMASLVTEHMESHGTRFLKGCVPSLIRKLPTNQLQVTWEDLASGKEDVGTFDTVLWAIGR... | 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]-disulf... |
Q86VQ6 | MERSPPQSPGPGKAGDAPNRRSGHVRGARVLSPPGRRARLSSPGPSRSSEAREELRRHLVGLIERSRVVIFSKSYCPHSTRVKELFSSLGVECNVLELDQVDDGARVQEVLSEITNQKTVPNIFVNKVHVGGCDQTFQAYQSGLLQKLLQEDLAYDYDLIIIGGGSGGLSCAKEAAILGKKVMVLDFVVPSPQGTSWGLGGTCVNVGCIPKKLMHQAALLGQALCDSRKFGWEYNQQVRHNWETMTKAIQNHISSLNWGYRLSLREKAVAYVNSYGEFVEHHKIKATNKKGQETYYTAAQFVIATGERPRYLGIQGDKEY... | 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 struct... |
Q99MD6 | MEKPPSPPPPPRAQTSPGLGKVGVLPNRRLGAVRGGLMSSPPGRRARLASPGTSRPSSEAREELRRRLRDLIEGNRVMIFSKSYCPHSTRVKELFSSLGVVYNILELDQVDDGASVQEVLTEISNQKTVPNIFVNKVHVGGCDRTFQAHQNGLLQKLLQDDSAHDYDLIIIGGGSGGLSCAKEAANLGKKVMVLDFVVPSPQGTTWGLGGTCVNVGCIPKKLMHQAALLGHALQDAKKYGWEYNQQVKHNWEAMTEAIQSHIGSLNWGYRVTLREKGVTYVNSFGEFVDLHKIKATNKKGQETFYTASKFVIATGERPRY... | 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 struct... |
D4APQ6 | MGVQRLALALIAFTSALTSVIAAPIVIEQPPLGPEHRYDAIVIGGGPSGLSALSSLGRVRRHVLLFDEGIYRNGATRHIHDMLTNDGVEPKVFRAKARQQISRYTSTSIKDVKVTKIKKVFEHGGRKYFFQVTDKTGAMYTASKVVLGTGVLDVLPGTPGLQENFGKGIYWCPWCDGWEHRDQPLGILGPLRHVMDSVYELETLNNDIIAFVNGTEHSVEDILYLNRKYPHWRQQLKHYNVQINNKMVSSIDRLQDGSKHQDKKTWQEFDKFRVNFNDGTSVERSVFITNFPTEQHSDLPDQLGLARDPIHKNKIKVNFK... | 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 | MNNVISFIGNSSNKYFQINQLHFIRIINKNIHSKNNLINSNSSYNVFYNKYFIKNTFQNKNKLSSIYSKLNFSIKNMCKDKNEKKNYEHVNANEKNGYLASEKNELTKNKVEEHTYDYDYVVIGGGPGGMASAKEAAAHGARVLLFDYVKPSSQGTKWGIGGTCVNVGCVPKKLMHYAGHMGSIFKLDSKAYGWKFDNLKHDWKKLVTTVQSHIRSLNFSYMTGLRSSKVKYINGLAKLKDKNTVSYYLKGDLSKEETVTGKYILIATGCRPHIPDDVEGAKELSITSDDIFSLKKDPGKTLVVGASYVALECSGFLNSL... | 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 eff... |
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 | MLVLGIETSCDETSAAIVEDGRKILSNVIYSQIDIHYQFGGVVPEIASRKHVEKISYVVDMAFKQAGLTIDDIDGIAATYGPGLVGSLLVGLSFAKALSYAKRLPFVAVNHIEGHIYANFITYPQLTPPLIVLVVSGGHTNLIILKDFEEYEVVGKTRDDAAGEAFDKIARYLGLGYPGGPAIDKIAKQGDEDKYKYPVADVGGYNFSFSGLKSAVINHVHGLWQRGEEFKIEDVAASFQKTVVSILVEKTINLSLETNIRKIAVAGGVAANSKLRSEFYKKCAEHNIEFFVPEFKYCTDNAAMIASCGYFKLQKGIVSS... | 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, togeth... |
Q8RC98 | MAKDIVILGIETSCDETAAGVVKNGKEVLSNVIYSQINVHKKYGGVVPEIASRKHIEAISFVVEEALNEAKLSLDEVDAIAATYGPGLVGPLLVGLSYGKALAYAKGKPFIGVNHIDGHIAANYIGGNLTPPFVCLVASGGHSHIVYVKDYGEYEVMGKTLDDAAGEAFDKVARALGLGYPGGPAIEKAAKLGNMEAIEFPKSFMEEGNFDFSFSGVKTAVLNYLNRQKQKGEEVNIYDVAASFQRNIVEVLVKKLVEAARFKNVSKVSIAGGVASNGFLRQKLEEDAKKFGLSVYYPEKIYCTDNGAMIAAAAYYDFVK... | 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, togeth... |
A4XM18 | MLVLGIETSCDETAAAIVKDGREVLSNIVYSQIEIHNQFGGVVPEIASRKHVEKISYVADMALKEADIDIDKIDAVAATYGPGLVGSLLVGLSFAKALSYARKIPFIAINHIEGHIYANFITYPKLKPPLIVLVVSGGHTNLIILEDFDRYEVVGKTRDDAAGEAFDKIARYLGLGYPGGPAIDKVARHGDEEKYKYPLADVEGYNFSFSGLKSAVINHVHTLNQRRENFKVEDVAASFQKAVVDTLVEKTIKLSLESNIKRVAIAGGVAANSKLREELSKRCSEHQIEFYVPDFKYCTDNAAMIASAGYFKLIKGQTSS... | 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, togeth... |
A0RMI6 | MILGIESSCDDSSIALMDIDNFELKKYKKITQENEHSKFGGVVPELAARLHTAAIPNLIEDVKEFFTSIKAVAVTNEPGLSVSLISGVSAARALSLALGIPLIGVNHLIGHIYSLFLDKNVVLPLGVLLVSGGHTMVLNIDESGYIKLIATTSDDSFGESFDKVAKMMDLGYPGGAIIEKLALSGDKNRFNFTVPLKHDKRLEYSFSGLKNQVRTQISKFESLSLQDKSDIASSFQYTAISHITDKLEKIFSEYKFKNFGAIGGGSANQVLRSNLEQICEKFGSNLMFAPLKFCSDNAAMIARAGVCKYKNKCFTKPLDM... | 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, togeth... |
Q0P8R5 | MKNLILAIESSCDDSSIAIIDKNTLECKFHKKISQELDHSIYGGVVPELAARLHSEALPKMLKQCKEHFKNLCAIAVTNEPGLSVSLLSGISMAKTLASALNLPLIPINHLKGHIYSLFLEEKISLDMGILLVSGGHTMVLYLKDDASLELLASTNDDSFGESFDKVAKMMNLGYPGGVIIENLAKNAKLKNISFNTPLKHSKELAFSFSGLKNAVRLEILKHENLNEDTKAEIAYAFENTACDHIMDKLEKIFNLYKFKNFGVVGGASANLNLRSRLQNLCQKYNANLKLAPLKFCSDNALMIARAAVDAYEKKEFVSV... | 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, togeth... |
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, togeth... |
Q5ZZQ1 | MKILGIETSHDDASVALFSENKVEILLTISQFELHEQFGGTVPELASREHSRNLAIILEKLLGKNIDFSTIDAIAYTKNPGLIGPLKIGFLFASALSLFFNKPLIPIDHLLGHFWSAAIENDLEFPVLSLLISGGHTQLIFAENKNNLEIIGSTVDDALGEIYDKIGRSLGCGYPGGPKIDLIWQQNNVRNMELIDFSLPKVLENPLDFSFSGLKTQVINYTNNLKENYLFSQKKVVEIAVSFQKTVIKYLKRQLDLALKTKKNVKTITLVGGVAANSEIRKLIKTYENKYKVVIPKKEFCTDNGAMIAKAAQIFLKFNE... | 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, togeth... |
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, togeth... |
Q602S1 | MLVLGIETSCDETGVALYDSSKGLLAHRLYSQVDEHAMYGGVVPEIASRDHLRKLLPLVREVLAAGGVRRTAIGGIAYTAGPGLIGALLVGAAVARSLAWAWSVPAIAVHHMEGHLLAPLLEPEPPEFPFVALLVSGGHTLLVEVRGIGVYQVLGESLDDAAGEAFDKTAKLLGLGYPGGPALARLAEKGRAERFHFPRPMTDRPGLDFSFSGLKTHALNVLAALPGTPQDKADIACAFQAAIVDTLVLKCRRAMRETGLGRLVVAGGVSANQAVRKGLQAMAESERYRVYFPRPEFCTDNGAMIAFAGCWRLRAGQFEP... | 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, togeth... |
Q01TA4 | MQRILGIESSCDETAAAVVEDGERVLSSVVASQMSTHGRYGGVVPELASREHLRAIVPVVREALERSATRLEDLAAIAVTVGPGLVGSLLVGLTYAKSLSLASGVGLIGVNHIEGHIHAVILEARRDGTPVEFPALALVASGGHTHLFEVREDFTYRLLGKTRDDAAGEAFDKVGKLLGFGYPGGPVIDRLAPHGDPLAVRFTFAKMKGNALDFSFSGLKTAVLRWVEAHDMEAEIAARKALVRDNPSPDLDQWLAVTPKRTLDLAASFQHAVIHELLTRAAASAERIGARSLIVSGGVACNSGLRSAAYASRLPYAVHF... | 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, togeth... |
A9FDL0 | MRVLGIETSCDETAAAVVTEGGDVLSDVVRSQVALHAPYGGVVPEVAARDHARAVVPVVREALSRAGVSAADLDGIAVTSRPGLAGALLVGLQAAKGLAWAAGKPLVGVDHLVGHLLAVFLRRGGAPLSDERERPSFPYVALLASGGHTAIYRVDGPALGAIRELGATRDDAAGEAFDKVAKLLGLGYPGGPVVDRLAAGGDAAAAADAVPALMARKESLEFSFSGIKSSVARHVAKRGRPEGQALRDLCAAFQGAVVDALVQKTVRAARAEGIGRVVLGGGVAANQGLRAKMAAACERRGLALFVPPLASCTDNGAMIA... | 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, togeth... |
Q9BZW7 | MMRSRSKSPRRPSPTARGANCDVELLKTTTRDREELKCMLEKYERHLAEIQGNVKVLKSERDKIFLLYEQAQEEITRLRREMMKSCKSPKSTTAHAILRRVETERDVAFTDLRRMTTERDSLRERLKIAQETAFNEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMKETISTVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGGTLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALI... | 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 | MMRSRSKSPRRPSPTARGANCDVELLKTTTRDREELKCMLEKYERHLAEIQGNVKVLTSERDKTFLLYEQAQEEIARLRREMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGGTLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQSTEALIMCEQDISRMRRQLDETNDELAQIARERDILAHDNDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQL... | 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 | MMRNRSKSPRRPSPTSRAANCDVELLKSTARDREELKCMLEKYERHLAEIQGNVKVLTSERDKTFLLYEQAQEEIARLRREMMKSCKSPKSTTAHAILRRVETERDVAFTDLRRMTTERDSLRERLKIAQETAFNEKAHLEQRIEELECTVHNLDDERMEQMANMTLMKETITTVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGATLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQSTEALI... | 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 | MMRNRSKSPRRPSPTSRAANCDVDLLKSTARDREELKCMLEKYERHLAEIQGNVKVLTSVRDKTFLLYEQAQEEIARLRREMMKSCQSPKSTTAHAILRRVETERDVAFTDLRRMTTARDSLRERLKIAQAFNEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMKETITIVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGATLNDLAKEKECLQTCLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQSTEALIMC... | 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 co... |
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 | MDDAAVLKRRGYLLGINLGEGSYAKVKSAYSERLKFNVAIKIIDRKKAPADFLEKFLPREIEILAMLNHCSIIKTYEIFETSHGKVYIVMELAVQGDLLELIKTRGALHEDEARKKFHQLSLAIKYCHDLDVVHRDLKCDNLLLDKDFNIKLSDFSFSKRCLRDDSGRMALSKTFCGSPAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPYDDSNIKKMLRIQKEHRVNFPRSKHLTGECKDLIYHMLQPDVNRRLHIDEILSHCWMQPKARGSPSVAINKEGESSRGTEPLWTPEPGSDKKSATKLEPEGEAQP... | 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 bas... |
Q96PF2 | MDDATVLRKKGYIVGINLGKGSYAKVKSAYSERLKFNVAVKIIDRKKTPTDFVERFLPREMDILATVNHGSIIKTYEIFETSDGRIYIIMELGVQGDLLEFIKCQGALHEDVARKMFRQLSSAVKYCHDLDIVHRDLKCENLLLDKDFNIKLSDFGFSKRCLRDSNGRIILSKTFCGSAAYAAPEVLQSIPYQPKVYDIWSLGVILYIMVCGSMPYDDSDIRKMLRIQKEHRVDFPRSKNLTCECKDLIYRMLQPDVSQRLHIDEILSHSWLQPPKPKATSSASFKREGEGKYRAECKLDTKTGLRPDHRPDHKLGAKTQ... | 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 aro... |
O54863 | MDDAAVLRKKGYIVGINLGKGSYAKVKSAYSERLKFNVAVKIIDRKKTPTDFVERFLPREMDILATVNHRSIIKTYEIFETSDGRIYIVMELGVQGDLLEFIKCRGALHEDVARKMFRQLSSAVKYCHDLDVVHRDLKCENLLLDKDFNIKLSDFGFSKRCLRDGSGRIVLSKTFCGSAAYAAPEVLQGIPYQPKVYDIWSLGVILYIMVCGSMPYDDSDIKKMLRIQKEHRVDFPRSKNLTGECKDLIYRILQPDVNRRLHIDEILSHSWLQPPKPKAMSSASFKREGEGKYRADCKLDTRPGSRPEHRPDHKLATKPQ... | 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 rec... |
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 | MGKGDTSETASATPAYRSVMEEYGYEVGKIIGHGSYGTVYEAYYTKQKVMVAVKIISKKKASEDYLNKFLPREIQVMKVLRHKYLINFYQAIETTSRVYIILELAQGGDVLEWIQRYGACAETLAGKWFSQMALGIAYLHSKGIVHRDLKLENLLLDKRENVKISDFGFAKMVPSSQPVHSSPSYRQMNSLSHLSQTYCGSFAYACPEILLGLPYNPFLSDTWSMGVILYTLVVARLPFDDTNLKKLLRETQKEVTFPANLTISQECKNLILQLLRQSTKRATILDVLRDPWMLKFQPEQPSNEIRLLEAMYQPTSSAKR... | 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 vi... |
Q8C1R0 | MRSSSWRKSDQRVFIEQVRECMNNGYLLSSKKIGSGAFSKVYLAYATRERMKHNPRLSSDLRGKRHTMVAIKIVSMAEAPAEYSRKFLPREILSLNATYKHMNIVQLYETYQNSQRSYLVLELAARGDLLEHINAVSDLRCCPGLEEEEARRLFWQLVSAVAHCHNVGIVHRDLKCENILLDDQGFIKLTDFGFANWVGLKNSLLSTFCGSVAYTAPEILMSKKYNGEQADLWSLGIILHAMVSGKLPFKEHQPHRMLNLIRRGPIFRPGLSPECRDLIRGLLQLHPCERLDLQQVAAHCWMLPAEHMLSSALGAPREQD... | 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 +... |
Q9NQE7 | MAVWLAQWLGPLLLVSLWGLLAPASLLRRLGEHIQQFQESSAQGLGLSLGPGAAALPKVGWLEQLLDPFNVSDRRSFLQRYWVNDQHWVGQDGPIFLHLGGEGSLGPGSVMRGHPAALAPAWGALVISLEHRFYGLSIPAGGLEMAQLRFLSSRLALADVVSARLALSRLFNISSSSPWICFGGSYAGSLAAWARLKFPHLIFASVASSAPVRAVLDFSEYNDVVSRSLMSTAIGGSLECRAAVSVAFAEVERRLRSGGAAQAALRTELSACGPLGRAENQAELLGALQALVGGVVQYDGQTGAPLSVRQLCGLLLGGGG... | 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 | MAVKAPWLGFLLLVSLWGLSTPALLLRRLREHIQKFQESSSLHPGFGLGHGPGAVPKQGWLEQPLDPFNASDRRTFLQRYWVNDQHRTGQDVPVFLHIGGEGSLGPGSVMAGHPAALAPAWGALVISLEHRFYGLSMPAGGLDLALLRYLSSRHALADVASARQALSGLLNVSSSSPWICFGGSYAGSLATWARLKFPHLVFAAVASSAPLSAVVDFSAYNQVVARSLTQVAIGGSLECLAAASTAFTEVERLLRAGPAAQAVLREELGACGSLDLTEDQAELLGALQALVGGTVQYDGQAGAPLSVRQLCGLLLGKWGN... | 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(... |
P39414 | MKPSTEWWRYLAPLAVIAIIALLPVPAGLENHTWLYFAVFTGVIVGLILEPVPGAVVAMVGISIIAILSPWLLFSPEQLAQPGFKFTAKSLSWAVSGFSNSVIWLIFAAFMFGTGYEKTGLGRRIALILVKKMGHRTLFLGYAVMFSELILAPVTPSNSARGAGIIYPIIRNLPPLYQSQPNDSSSRSIGSYIMWMGIVADCVTSAIFLTAMAPNLLLIGLMKSASHATLSWGDWFLGMLPLSILLVLLVPWLAYVLYPPVLKSGDQVPRWAETELQAMGPLCSREKRMLGLMVGALVLWIFGGDYIDAAMVGYSVVALM... | 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:... |
Q9Z4S6 | MANLTRRQWLKVGLAVGGMVTFGLSYRDVAKRAIDGLLNGTSGKVTRDRIFGNALIPEAQAQTHWQQNPQQTIAMTQCFGCWTQCGIRARVNADGKVIRIAGNPYHPLSQEHPIDSSVPFSEAMEQLAGESGLDARSTACARGATLLESLYSPLRLLEPMKRVGKRGEGKWQRISFEQLIEEVVEGGDLFGEGHVDGLRAIHAPDTPIDAKHPSFGPKTNQLLVTNTSDEGRDAFLRRFALNSFGSKNFGAHGAYCGLAYRAGSGALMGDLDKNPHVKPDWENVEFALFMGTSPAQSGNPFKRQARQLASARLRENFQYV... | 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 com... |
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 Locatio... |
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 ... |
O30079 | MLWSYPEGFAYFNEFAQSIIWEPVAFSYALLISGADLLLLAALALLSGYLRRAIPMFLILGLSFFSVILLGPLADLALPHRATEILTRPHLASTEMHPGISVMALYGGLLWPLTFIVALIFALLYFSYPMHKKGGTFSFLSFGVKSEESYERLKPAMKVLAAILVPLSALWTIYPGMLFFSQTWIYAWKNWGLMLPMFFGETFITATGTALILYYLERMEDERIRYPLLQIHGAAAIALAGVLILQMFIWGMWGNPNFAAVVPMMQAAAVIFLLTFILTLVSAKYEAITPIVPVLALFGVVVNKWNLIINGQLISRAGMG... | 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 prote... |
Q9Z4S7 | MTHSLIIEEVLAHPQDISWLPWAVQYFFFIGIAACAALFACYLHWRKKDAATEENRALLIAITCAITAPLALTADLHQTARVWHFYAWPTPWSWMPWGALFLPLFTGFLALWFLAQQIKRLFNKSYNVTKWLALASALCAVGLLIYTGREVSVVLARPIWFSYAFPVAMFLSALQAFFALMIVAARRDSVRLPKILWGQIWTLAALGLVVAMWVSGDTLSGTAIRQWITVALSAKYYAVGWVALWVCTLLFCSLALRHPLSQLRRVLLVLSALALCWLMRWTLLIQVQTVPKFNAQFNPYSLPGGTDGWLAILGTFGLWI... | 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 a... |
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 competi... |
Q8ZPP6 | MRGKTVRRLAVLAAVGLLCHGAWAGTWNIGILAMRGEASTRSHWQPLAKTLSQQLPGETFHIQPLDLHQMQEAVNQGTVQFVITNPAQFVQLNSHAPLRWLASLRSTRDGKAVSNVIGSVILTRRDSGITTAHDLIGKTVGAIDAQAFGGYLLGYKALSDAGLRPERDFHLRFTGFPGDALVYMLREKAVQAAIVPVCLLENMDQEGLINKKDFIALLSRPTPLPCLTSTPLYPDWSFAALPAVSDALADRVTRALFNAPAAASFHWGAPASTSQVEALLRDVRQHPQQRRLWLDVKSWLIQHQLMVGGVILAFLLLTLN... | 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, ... |
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 ... |
O32273 | MPSITKQIMSGAKWTSISTMCITIIQIVQFALLGNMMTLTEFGLVGMITTVTVFAQIVLDMGFGAALIQRDDATERQLSTLYWLNIMTGVLLFVLLYVSSPVIAGFYQREELVFLVRILAIMFLIAPIGQQYQYMLQKQLHFNTLSKIEIFSNVLSFGYLAIAVFMMDAILAYVISQVLLQSSKGILYWAVYRKKWHPAFVFDLRGMKDFFSFGAFQLSSRLVNRLGANIDMILIGRFIGAEALGIYNLAYQIVTIPVLKINPIVTRVAFPIFAKNKYENSVIREGFLNMTKMLALVSFPLLIGLVSVSDAFITAVFGEK... | 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... |
O32271 | MKKIAVIGTGYVGLVSGTCFAEIGNKVVCCDIDESKIRSLKNGVIPIYEPGLADLVEKNVLDQRLTFTNDIPSAIRASDIIYIAVGTPMSKTGEADLTYVKAAAKTIGEHLNGYKVIVNKSTVPVGTGKLVQSIVQKASKGRYSFDVVSNPEFLREGSAIHDTMNMERAVIGSTSHKAAAIIEELHQPFHAPVIKTNLESAEMIKYAANAFLATKISFINDIANICERVGADVSKVADGVGLDSRIGRKFLKAGIGFGGSCFPKDTTALLQIAKSAGYPFKLIEAVIETNEKQRVHIVDKLLTVMGSVKGRTISVLGLAF... | 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 Le... |
O32270 | MSIKRSAVHTLALLAAAIFGVVLLLGAIHKDIGFMQMAAVLAVLAIGLFLLTLATAFTTKERLFMAVIYILIACTFLNNAFFAIHLGFFSLFLYRLLLIAAGCLHIFGMVRNRTHIERWHGLQVKGILLFFAFWFIYGLVSLLWAKSVTVGLKYLALLAMGIFFIYLIVMYVQKMERLMIVYAIWLVMTVFLMIIGFYNHITHHHLASSTLYSGPEYKQHYPTSVFFNQNDFATFLSISFFFYITMMKNIKNGYIKAIGLVLSLCALYLIFATGSRASLLGIFAGIAVYIFIVLPPVLKRMAIWLSAAGIALFAVLFASK... | 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 Lo... |
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 | MNSDLETRVLRKITLRIVPFIMLLYFVAFLDRVNIGFAALTMNEDLGFSSTVFGIGAGIFFVGYFLFEVPSNLILNKVGARIWIARVMITWGIVSGLMAFVQGTTSFYALRFLLGVAEAGFFPGIILYLSFWFPARRRAAVTAIFMAAAPLSTVLGSPISGALMEMHGFLGLAGWQWMFLIEAAPAVILGVVVLFYLTDRPEKAKWLSEDERNWLVKTMNAEQAAKGKASHSILAGLADIRVIALALVYFGTSAGLYTLGIWAPQIIKEFGLSSLQVGFINAVPGIFAVAAMVLWARHSDKTGERTWHVVGACLLAAVGL... | 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... |
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... |
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 presen... |
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 ... |
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 m... |
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
|
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
|
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... |
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
|
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 'd... |
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
|
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 'disul... |
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: 1... |
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 sodi... |
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... |
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
|
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
Seque... |
A8X3V8 | MSSLTNPTTVMEEEEVPVAAPIRRGNKNPRRYSLVHQASCETQHHIGIRRQNTIQHRKQLTDQMREQKILQQLNDEGVEVIFAANDVSSIDFSVIVTSTDYISTFVSDILYNMKSAGVQICHVETRESKAVSGHDVLLDCRATKNQLIKAAELLTQNHVALTHFSIFSKKSVEKSQSMIWFPRHISELDQCSKCITKYEPTTDPRHPGHGDDEYIARRKFLNDQALEFKFGDEIGYVEYTEDEHATWKAVYEKLGGLHESHTCSVYRQNLKILQKEKVLTADRIPQIRDVNKFLQKKTGFELRPCSGLLSARDFLASLAF... | 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 ... |
P90986 | MSSLTNNTFMEEEPRGVTVIATKVAENSKNPRRYSLVHQASCETQHHKGIRRQNTIQHRKQLTDQMRCQKILQQLNDEGIEVIFTANDVTPIEFSIILTSTDPTLSNFVSDILQNMSSAKVQICHVETRGNEASHDVLLACKATKNQLIHSAELLTQNHVALTKFSIFAKKLSDEKNQSQIWFPRHISELDQCSKCITKYEPTTDPRHPGHGDVAYIARRKFLNDQALEFKFGDEIGYVDYTEEEHATWKAVYEKLGDLHLSHTCAVYRQNLKILQEEKVLTADRIPQIRDVNKFLQKKTGFELRPCSGLLSARDFLASL... | 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 . Modu... |
P18459 | MMAVAAAQKNREMFAIKKSYSIENGYPSRRRSLVDDARFETLVVKQTKQTVLEEARSKANDDSLEDCIVQAQEHIPSEQDVELQDEHANLENLPLEEYVPVEEDVEFESVEQEQSESQSQEPEGNQQPTKNDYGLTEDEILLANAASESSDAEAAMQSAALVVRLKEGISSLGRILKAIETFHGTVQHVESRQSRVEGVDHDVLIKLDMTRGNLLQLIRSLRQSGSFSSMNLMADNNLNVKAPWFPKHASELDNCNHLMTKYEPDLDMNHPGFADKVYRQRRKEIAEIAFAYKYGDPIPFIDYSDVEVKTWRSVFKTVQD... | 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 bi... |
P07101 | MPTPDATTPQAKGFRRAVSELDAKQAEAIMVRGQGAPGPSLTGSPWPGTAAPAASYTPTPRSPRFIGRRQSLIEDARKEREAAVAAAAAAVPSEPGDPLEAVAFEEKEGKAVLNLLFSPRATKPSALSRAVKVFETFEAKIHHLETRPAQRPRAGGPHLEYFVRLEVRRGDLAALLSGVRQVSEDVRSPAGPKVPWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQVYRQRRKLIAEIAFQYRHGDPIPRVEYTAEEIATWKEVYTTLKGLYATHACGEHLEAFALLERFSGYREDNIPQLEDVSRFLKERTGFQLRP... | 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, Pub... |
A0A060X6Z0 | MPISSSSSSSTKSMRRAASELERSDSVTSPRFIGRRQSLIEDARKEREAAAAAAEAAEATEQIVFEEEDGKALLNLFFTLRSSKTPALSRSLKVFETFEAKIHHLETRPCRKPRDSLEGLEYFVRCEVHLSDVSTLISSIKRIAEDVKTTKEVKFHWFPKKISELDRCHHLITKFDPDLDQEHPGFTDPVYRQRRKMIGDIAFRYKQGEPIPRVEYTEEEIGTWREVYSTLRDLYTTHACSEHLEAFNLLERHCGYSPENIPQLEDVSRFLRERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSPEPDC... | 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 bi... |
Q74PY8 | MFLAQEIIRKKRDGQPLSEEEIRFFINGIRDNVVSEGQIAALAMTIYFHDMSMPERVALTMAMRDSGTVLNWKSLNLNGPLVDKHSTGGVGDVTSLMLGPMVAACGGYVPMISGRGLGHTGGTLDKLEAIPGFDIFPDDNAFRKIIQNVGVAIIGQTSSLAPADKRFYATRDITATVDSIPLITASILAKKLAEGLDALVMDVKVGSGAFMPTYSLSADLAQAIVGVANGAGCKTTALLTDMNQVLASSAGNGVEVREAVRFLTGEYRNPRLLEVTMALCVEMLLSGGLAHDEADARAKLQAVLDNGKAAEVFGRMVAAQ... | 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-... |
O60078 | MKETFQVGIIGFGDMGRLYAEYISKAGWRVNVCDRPENYESIQATYGNGGYTVLKDGFQVSRTSDYILYSVEAEHIDKVVALYGPATKVGAIVGGQTSCKAPEMNAFEKYLPEDVDIISCHSMHGPKVNPKSQPLVIIRHRASDEHFEIVNEILSCFKSSVVYLSAKEHDRITADTQAVTHAAFLTMGLAWHANNQYPWEINRWCGGIENIKMNLSMRIYSSKWHVYAGLAILNPEAQRQIQQYASSVTELFKLAISGKAKEYEDRIRNAGKFVFGENMDRNSSGLLLSDELLDQYSISNIPKDESKRNSHLSILAIVDS... | 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
|
P20049 | MVSEDKIEQWKATKVIGIIGLGDMGLLYANKFTDAGWGVICCDREEYYDELKEKYASAKFELVKNGHLVSRQSDYIIYSVEASNISKIVATYGPSSKVGTIVGGQTSCKLPEIEAFEKYLPKDCDIITVHSLHGPKVNTEGQPLVIINHRSQYPESFEFVNSVMACLKSKQVYLTYEEHDKITADTQAVTHAAFLSMGSAWAKIKIYPWTLGVNKWYGGLENVKVNISLRIYSNKWHVYAGLAITNPSAHQQILQYATSATELFSLMIDNKEQELTDRLLKAKQFVFGKHTGLLLLDDTILEKYSLSKSSIGNSNNCKPV... | 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
|
Q944B6 | MAETLITKPPLSLSFTSLSSMLPSLSLSTANRHLSVTDTIPLPNSNSNATPPLRIAIIGFGNYGQFLAETLISQGHILFAHSRSDHSSAARRLGVSYFTDLHDLCERHPDVVLLCTSILSIENILKTLPFQRLRRNTLFVDVLSVKEFAKTLLLQYLPEDFDILCTHPMFGPQSVSSNHGWRGLRFVYDKVRIGEERLRVSRCESFLEIFVREGCEMVEMSVTDHDKFAAESQFITHTLGRLLGMLKLISTPINTKGYEALLDLAENICGDSFDLYYGLFVYNNNSLEVLERIDLAFEALRKELFSRLHGVVRKQSFEGE... | 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... |
Q9LMR3 | MLLHFSPAKPLISPPNLRRNSPTFLISPPRSLRIRAIDAAQIFDYETQLKSEYRKSSALKIAVLGFGNFGQFLSKTLIRHGHDLITHSRSDYSDAANSIGARFFDNPHDLCEQHPDVVLLCTSILSTESVLRSFPFQRLRRSTLFVDVLSVKEFPKALFIKYLPKEFDILCTHPMFGPESGKHSWSGLPFVYDKVRIGDAASRQERCEKFLRIFENEGCKMVEMSCEKHDYYAAGSQFVTHTMGRVLEKYGVESSPINTKGYETLLDLVENTSSDSFELFYGLFMYNPNALEQLERLDMAFESVKKELFGRLHQQYRKQM... | 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): st... |
P20692 | MNQMKDTILLAGLGLIGGSIALAIKKNHPGKRIIGIDISDEQAVAALKLGVIDDRADSFISGVKEAATVIIATPVEQTLVMLEELAHSGIEHELLITDVGSTKQKVVDYADQVLPSRYQFVGGHPMAGSHKSGVAAAKEFLFENAFYILTPGQKTDKQAVEQLKNLLKGTNAHFVEMSPEEHDGVTSVISHFPHIVAASLVHQTHHSENLYPLVKRFAAGGFRDITRIASSSPAMWRDILLHNKDKILDRFDEWIREIDKIRTYVEQEDAENLFRYFKTAKDYRDGLPLRQKGAIPAFYDLYVDVPDHPGVISEITAILA... | 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
|
P07023 | MVAELTALRDQIDEVDKALLNLLAKRLELVAEVGEVKSRFGLPIYVPEREASMLASRRAEAEALGVPPDLIEDVLRRVMRESYSSENDKGFKTLCPSLRPVVIVGGGGQMGRLFEKMLTLSGYQVRILEQHDWDRAADIVADAGMVIVSVPIHVTEQVIGKLPPLPKDCILVDLASVKNGPLQAMLVAHDGPVLGLHPMFGPDSGSLAKQVVVWCDGRKPEAYQWFLEQIQVWGARLHRISAVEHDQNMAFIQALRHFATFAYGLHLAEENVQLEQLLALSSPIYRLELAMVGRLFAQDPQLYADIIMSSERNLALIKRY... | 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
|
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... |
O76511 | MVLTPTKDGPDQESMPLPADNGESPSKQQAPVNRDEMHYLDLLRHIIANGEQRMDRTEVGTLSVFGSQMRFDMRNSFPLLTTKRVFFRAVAEELLWFVAGKTDAKLLQAKNVHIWDGNSSREFLDKMGFTGRAVGDLGPVYGFQWRHFGAQYGTCDDDYSGKGIDQLRQVIDTIRNNPSDRRIIMSAWNPLDIPKMALPPCHCLAQFYVSEKRGELSCQLYQRSADMGLGVPFNIASYALLTHMIAHVTGLKPGDFVHTMGDTHVYLNHVEPLKEQLERTPRPFPKLIIKRQVQDIEDFRFEDFQIVDYNPHPKIQMDMA... | 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
|
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... |
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... |
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... |
P39040 | MSRAYDLVVIGAGSGGLEAGWNAASLHKKRVAVIDLQKHHGPPHYAALGGTCVNVGCVPKKLMVTGANYMDTIRESAGFGWELDRESVRPNWKALIAAKNKAVSGINDSYEGMFADTEGLTFHQGFGALQDNHTVLVRESADPNSAVLETLDTEYILLATGSWPQHLGIEGDDLCITSNEAFYLDEAPKRALCVGGGYISIEFAGIFNAYKARGGQVDLAYRGDMILRGFDSELRKQLTEQLRANGINVRTHENPAKVTKNADGTRHVVFESGAEADYDVVMLAIGRVPRSQTLQLDKAGVEVAKNGAIKVDAYSKTNVD... | 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
Su... |
Q6NUM6 | MDPSADTWDLSSPLISLWINRFYIYLGFAVSISLWICVQIVIEMQGFATVLAEAVTSLDLPVAIINLKEYDPDDHLIEEVTSKNVCVFLVATYTDGLPTESAEWFCKWLEEASIDFRFGKTYLKGMRDAVFGLGNSAYASHFNKVGKNVDKWLWMLGVHRVMSRGEGDCDVVKSKHGSIEANFRAWKTKFISQLQALQKGERKKSCGGHCKKGKCESHQHGSEEREEGSQEQDELHHRDTKEEEPFESSSEEEFGGEDHQSLNSIVDVEDLGKIMDHVKKEKREKEQQEEKSGLFRNMGRNEDGERRAMITPALREALTK... | 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 eukaryoti... |
Q8RXN5 | MSTTSSVRVRLAFVALLSATTFYCIHKYRRLKHLKNLSLNPSSTLKASRGKIFFISQTGTAKALAQRLHELCASNDIAFDIVDPHSYEPEDLPKETLVLFIASTWDGGKPPKNGEFLVNWLGESAEDFRVGSLLLSDCKFAVFGVGSRAYGESYNAVAKELSSRMIGLGGLEMIPVGEGDVDDGELDRAFQDWCDGVIRVLKGGSAQETNGVSQQIGAVEDDLEYYDSTDEEDEDNDADGGIVDLEDIAGKAPSKRNGVVKVTKVDGKKEMVTPVIRASLTKQGYKIIGSHSGVKICRWTKSQLRGRGGCYKHSFYGIES... | 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 eukaryoti... |
Q08C92 | MSGVLNDVRDYTEGYLQVLWQNRLYVYSTAAVLIGVWFTVNMLFKKKKMVHPVSPLASKSVKKQEPASEAKKVIYVSGVKVFYGSQTGTAKGFAKELAEDVIAQGIQCEVIDMKDFDPEDRLAEECTSKIICVFLVATYTDGQPTESAEWFCKWLEEASTDFRYGKTYLKGMRYAVFGLGNSVYVGHFNTVSKSIDKWLWMLSAARIMTRGEGDCNVVKSRHGSVQADFQVWKGKFLNRLQALAKGEKKACSGNCKKASCKNKKKHKEEAEDNHSLAEKNNSEEELMESSSDEESSSEDEKSHGSVIDMEDLGNVMNHMK... | 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 eukaryoti... |
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