ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q7Z614 | MASPEHPGSPGCMGPITQCTARTQQEAPATGPDLPHPGPDGHLDTHSGLSSNSSMTTRELQQYWQNQKCRWKHVKLLFEIASARIEERKVSKFVVYQIIVIQTGSFDNNKAVLERRYSDFAKLQKALLKTFREEIEDVEFPRKHLTGNFAEEMICERRRALQEYLGLLYAIRCVRRSREFLDFLTRPELREAFGCLRAGQYPRALELLLRVLPLQEKLTAHCPAAAVPALCAVLLCHRDLDRPAEAFAAGERALQRLQAREGHRYYAPLLDAMVRLAYALGKDFVTLQERLEESQLRRPTPRGITLKELTVREYLH | Function: May play a role in cellular vesicle trafficking. Has been proposed to function as a sorting protein that targets SELPLG into endosomes, but has no effect on SELPLG internalization from the cell surface, or on SELPLG-mediated cell-cell adhesion.
Location Topology: Peripheral membrane protein
Sequence Mass (Da)... |
Q9D2Y5 | MASPEHPGSPGWRGPINQCRTRTRQEVLPPGPDLPCPGPEEAQDGPSSNSSMTTRELQEHWQKEKSRWKHVRLLFEIASARIEERKVSKFVMYQVVVIQTGSFDSDKAVVERRYSDFERLQKALLKRFGPELEDVTFPRKRLTGNLSAETICERRRELREYLRLLYAVRAVRRSREFLDFLTRPELREAFGCLRAGQYARALELLGRALPLQEKLTAHCPSAAVPALCAALVCLRDLERPAEAFAVGERALRCLRTRENHRYYAPLLDAMVRLAYALGKDFAALQSRLDENQLRRPTHRDATLKELTVREYLS | Function: May play a role in cellular vesicle trafficking . Has been proposed to function as a sorting protein that targets SELPLG into endosomes, but has no effect on SELPLG internalization from the cell surface, nor on SELPLG-mediated cell-cell adhesion .
Location Topology: Peripheral membrane protein
Sequence Mass (... |
Q3UR97 | MASRLLHRLRHALASDGPGEAAAGPEAEQFPESSELEDDDAEGLSSRLSGTLSFTSAEDDPDDEDEDDEAGLDSPPSGDGASGEDAERSPPPDGQRSSQLLARQLQDFWKKSRNTLVPQRLLFEVTSANVVKDPPSKYVLYTLAVMGPGPPDRQPAQISRRYSDFERLHRNLQRQFRGPMSAISFPRKRLRRNFTAETIARRSRAFEQFLGHLQAVPELRQAPDLQDFFVLPELRRAQSLTCTGLYREALALWANAWQLQTQLGTPSGPDRPLLTLAGLAVCHQELEDPGEARACSEKALQLLGDKRPHPFLAPFLEAHV... | Function: Binds to membranes enriched in phosphatidylinositol 3-phosphate (PtdIns(P3)) and phosphatidylinositol 4,5-bisphosphate . May be involved in several stages of intracellular trafficking.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 40308
Sequence Length: 363
Domain: The PX domain mediates ... |
Q96L94 | MLEVHIPSVGPEAEGPRQSPEKSHMVFRVEVLCSGRRHTVPRRYSEFHALHKRIKKLYKVPDFPSKRLPNWRTRGLEQRRQGLEAYIQGILYLNQEVPKELLEFLRLRHFPTDPKASNWGTLREFLPGDSSSQQHQRPVLSFHVDPYVCNPSPESLPNVVVNGVLQGLYSFSISPDKAQPKAACHPAPLPPMP | Function: May be involved in several stages of intracellular trafficking (By similarity). Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)) .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 22068
Sequence Length: 193
Domain: The PX domain mediates specific binding to m... |
Q17QS1 | MEVYIPSFRYEESDLERGYTVFKIEVLMNGRKHFVEKRYSEFHALHKKLKKCIKTPEIPSKHVRNWVPKVLEQRRQGLETYLQAVILENEELPKLFLDFLNVRHLPSLPKTESYGSFDETESEESSKLSHQPVLLFLRDPYVLPAASDFPNVVIEGVLHGIFYPHLQPR | Function: May be involved in several stages of intracellular trafficking.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 19908
Sequence Length: 169
Domain: The PX domain mediates specific binding to membranes enriched in phosphatidylinositol 3-phosphate (PtdIns(P3)).
Subcellular Location: Cytoplasmi... |
Q9Y343 | MEVYIPSFRYEESDLERGYTVFKIEVLMNGRKHFVEKRYSEFHALHKKLKKCIKTPEIPSKHVRNWVPKVLEQRRQGLETYLQAVILENEELPKLFLDFLNVRHLPSLPKAESCGSFDETESEESSKLSHQPVLLFLRDPYVLPAASDFPNVVIEGVLHGIFYPHLQPR | Function: May be involved in several stages of intracellular trafficking.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 19818
Sequence Length: 169
Domain: The PX domain mediates specific binding to membranes enriched in phosphatidylinositol 3-phosphate (PtdIns(P3)).
Subcellular Location: Cytoplasmi... |
Q9CRB0 | MEVYIPSFRHEDSDLERGYTVFKIEVLMNGRKHFVEKRYSEFHALHKKLKKCIKTPEIPSKHVRNWVPKVLEQRRQGLETYLQAVILENEELPKLFLDFLNVRHLPSLPKAESCGSFDETESEESSKLSHQPVLLFLGDPYVLPAASDFPNVVIEGVLHGIFFSHLQPR | Function: May be involved in several stages of intracellular trafficking.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 19653
Sequence Length: 169
Domain: The PX domain mediates specific binding to membranes enriched in phosphatidylinositol 3-phosphate (PtdIns(P3)).
Subcellular Location: Cytoplasmi... |
Q9H3E2 | MDKALKEVFDYSYRDYILSWYGNLSRDEGQLYHLLLEDFWEIARQLHHRLSHVDVVKVVCNDVVRTLLTHFCDLKAANARHEEQPRPFVLHACLRNSDDEVRFLQTCSRVLVFCLLPSKDVQSLSLRIMLAEILTTKVLKPVVELLSNPDYINQMLLAQLAYREQMNEHHKRAYTYAPSYEDFIKLINSNSDVEFLKQLRYQIVVEIIQATTISSFPQLKRHKGKETAAMKADLLRARNMKRYINQLTVAKKQCEKRIRILGGPAYDQQEDGALDEGEGPQSQKILQFEDILANTFYREHFGMYMERMDKRALISFWESV... | Function: May be involved in several stages of intracellular trafficking.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 97945
Sequence Length: 840
Subcellular Location: Endosome membrane
|
Q96L92 | MADEDGEGIHPSAPHRNGGGGGGGGSGLHCAGNGGGGGGGPRVVRIVKSESGYGFNVRGQVSEGGQLRSINGELYAPLQHVSAVLPGGAADRAGVRKGDRILEVNHVNVEGATHKQVVDLIRAGEKELILTVLSVPPHEADNLDPSDDSLGQSFYDYTEKQAVPISVPRYKHVEQNGEKFVVYNVYMAGRQLCSKRYREFAILHQNLKREFANFTFPRLPGKWPFSLSEQQLDARRRGLEEYLEKVCSIRVIGESDIMQEFLSESDENYNGVSDVELRVALPDGTTVTVRVKKNSTTDQVYQAIAAKVGMDSTTVNYFAL... | Function: Involved in the retrograde transport from endosome to plasma membrane, a trafficking pathway that promotes the recycling of internalized transmembrane proteins. Following internalization, endocytosed transmembrane proteins are delivered to early endosomes and recycled to the plasma membrane instead of being d... |
Q8K4V4 | MADEDGEGIHPSTPHRNGGGGGGSGLHCAGNGGGGGGGPRVVRIVKSESGYGFNVRGQVSEGGQLRSINGELYAPLQHVSAVLPGGAADRAGVRKGDRILEVNGVNVEGATHKQVVDLIRAGEKELILTVLSVPPHEADNLDPSDDSLGQSFYDYTEKQAVPISVPTYKHVEQNGEKFVVYNVYMAGRQLCSKRYREFAILHQNLKREFANFTFPRLPGKWPFSLSEQQLDARRRGLEEYLEKVCSIRVIGESDIMQEFLSESDENYNGVSDVELRVALPDGATVTVRVKKNSTTDQVYQAIAAKVGMDSTTVNYFALFE... | Function: Involved in the retrograde transport from endosome to plasma membrane, a trafficking pathway that promotes the recycling of internalized transmembrane proteins. Following internalization, endocytosed transmembrane proteins are delivered to early endosomes and recycled to the plasma membrane instead of being d... |
P00442 | MATKAVCVLKGDGPVQGTIHFEAKGDTVVVTGSITGLTEGDHGFHVHQFGDNTQGCTSAGPHFNPLSKKHGGPKDEERHVGDLGNVTADKNGVAIVDIVDPLISLSGEYSIIGRTMVVHEKPDDLGRGGNEESTKTGNAGSRLACGVIGIAK | Cofactor: Binds 1 copper ion per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
PTM: Palmitoylation helps nuclear targeting and decreases catalytic activity.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 15683
Sequ... |
P66826 | MMKSLFIASTMVLMAFPAFAESTTVKMYEALPTGPGKEVGTVVISEAPGGLHFKVNMEKLTPGYHGFHVHENPSCAPGEKDGKIVPALAAGGHYDPGNTHHHLGPEGDGHMGDLPRLSANADGKVSETVVAPHLKKLAEIKQRSLMVHVGGDNYSDKPEPLGGGGARFACGVIE | Cofactor: Binds 1 copper ion per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 18262
Sequence Length: 174
Subcellular Location: Periplasm
EC: 1.15.1.1
|
P41962 | MSANRIAVLRGDNVSGIIRFKQEKEGSPTTISGEIKGLTPGLHGFHVHQYGDTTNGCISAGPHFNPYNKTHGGPTDEMRHVGDLGNIVAGADGTAHIDISDKHVQLLGPNSIIGRSLVVHADQDDLGKGVGDKKDESLKTGNAGARVACGIVAVSAAS | Cofactor: Binds 1 copper ion per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 16341
Sequence Length: 158
Subcellular Location: Cytoplasm
EC: 1.15.1.1
|
P34697 | MFMNLLTQVSNAIFPQVEAAQKMSNRAVAVLRGETVTGTIWITQKSENDQAVIEGEIKGLTPGLHGFHVHQYGDSTNGCISAGPHFNPFGKTHGGPKSEIRHVGDLGNVEAGADGVAKIKLTDTLVTLYGPNTVVGRSMVVHAGQDDLGEGVGDKAEESKKTGNAGARAACGVIALAAPQ | Cofactor: Binds 1 copper ion per subunit.
Function: Protects cells against oxidative stress by converting superoxide radicals to hydrogen peroxide . Required for normal brood size . May be involved in regulating mpk-1 phosphorylation downstream of phosphatase ptp-2 during oocyte maturation .
Catalytic Activity: 2 H(+) ... |
H6BDU4 | MALKAVCVLKGDGQVQGTIHFEQKENGPVMVSGSISGLAEGDHGFHVHQFGDNTQGCTSAGPHFNPLSKKHGGPKDQERHVGDLGNVTAGKDGVAIVSIEDPVISLSGDHSIIGRTMVVHEKPDDLGKGGNEESTKTGNAGSRLACGVIGIAQ | Cofactor: Binds 1 copper ion per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
PTM: Palmitoylation helps nuclear targeting and decreases catalytic activity.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 15743
Sequ... |
Q6FWL5 | MVKAVAVLRGSAGVSGVVTLEQASEQDPTTITYEIAGNDPNAERGFHIHEFGDVTNGCVSAGPHFNPFKKTHGAPQDENRHVGDLGNIKTDAQGVAKGVITDSLVKLIGPTSVVGRSVVVHAGTDDLGKGGNEESLKTGNAGPRPACGVIGLTN | Cofactor: Binds 1 copper ion per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 15750
Sequence Length: 154
Subcellular Location: Cytoplasm
EC: 1.15.1.1
|
Q8WNN6 | MEMKAVCVLKGQGPVEGTIHFVQKGSGPVVVSGTITGLTEGEHGFHVHQFEDXTQGCTSAGPHFNPLSKKHGGPKDQERHVGDLGNVTAGKDGVAIVSIEDSLIALSGDYSIIGRTMVVHEKRDDLGKGDNEESTQTGNAGSRLACGVIGIAQ | Cofactor: Binds 1 copper ion per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
PTM: Palmitoylation helps nuclear targeting and decreases catalytic activity.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 15913
Sequ... |
O22373 | MVKAVAVLSSSECVSGTILFSQDGDAPTTVTGNVSGLKPGLHGFHVHALGDTTNGCMSTGPHYNPAGKEHGAPEDENRHAGDLGNITVGEDGTASFTITDEQIPLTGPQSIIGRGVVVHADPDDLGKGGHELTKTTGNAGGRVACGIIGLQG | Cofactor: Binds 1 copper ion per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 15279
Sequence Length: 152
Subcellular Location: Cytoplasm
EC: 1.15.1.1
|
P80174 | MATVKAVCVLKGEDPVKEPVKGPVKEPVKGIIYFEQQGNGPVTLSGSITGLTEGKHGFHVHEFGDNTNGCTSAGAHFNPPGKNHGGPQDNERHVGDLGNVIANKEGVAEVCIKDSLISLTGSQSIIGRTMVVHEKEDDLGKGGNDESLKTGNAGSRLACGVVGIAKL | Cofactor: Binds 1 copper ion per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 17277
Sequence Length: 167
Subcellular Location: Cytoplasm
EC: 1.15.1.1
|
P20379 | MIRLSAAAALGLAAALAASPALAQTSATAVVKAGDGKDAGAVTVTEAPHGVLLKLELKGLTPGWHAAHFHEKGDCGTPDFKSAGAHVHTAATTVHGLLNPDANDSGDLPNIFAAADGAATAEIYSPLVSLKGAGGRPALLDADGSSIVVHANPDDHKTQPIGGAGARVACGVIK | Cofactor: Binds 1 copper ion per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems (By similarity). May function against extracytoplasmic toxic oxygen species.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 17100
Sequen... |
P33431 | MATKAVCVLKGDGPVQGIIHFEQKANGPVVVKGRITGLVEGKHGFHVHEFGDNTQGCTSAGPHFNPLSKKHGGPQDEERHVGDLGNVTAGADGVANVSIEDSLISLSGANSIIGRTMVVHEKPDDLGKGGNEESTKTGNAGSRLACGVIGIAQ | Cofactor: Binds 1 copper ion per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
PTM: Palmitoylation helps nuclear targeting and decreases catalytic activity.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 15670
Sequ... |
O81235 | MAIRCVASRKTLAGLKETSSRLLRIRGIQTFTLPDLPYDYGALEPAISGEIMQIHHQKHHQAYVTNYNNALEQLDQAVNKGDASTVVKLQSAIKFNGGGHVNHSIFWKNLAPSSEGGGEPPKGSLGSAIDAHFGSLEGLVKKMSAEGAAVQGSGWVWLGLDKELKKLVVDTTANQDPLVTKGGSLVPLVGIDVWEHAYYLQYKNVRPEYLKNVWKVINWKYASEVYEKENN | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 25444
Sequence Length: 231
Subcellular Location: Mitochondrion matrix
E... |
P09737 | MSEYELPPLPYDYDALEPHISEQVLTWHHDTHHQGYVNGWNDAEETLAENRETGDHASTAGALGDVTHNGSGHILHTLFWQSMSPAGGDEPSGALADRIAADFGSYENWRAEFEAAASAASGWALLVYDSHSNTLRNVAVDNHDEGALWGSHPILALDVWEHSYYYDYGPDRGSFVDAFFEVVDWDEPTERFEQAAERFE | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 22385
Sequence Length: 200
EC: 1.15.1.1
|
Q03300 | MSDYELDPLPYEYDALEPHISEQVLTWHHDTHHQGYVNGWNAAEETLAENREAGEFGSSAGALRNVTHNGSGHILHDLFWQNMSPEGGDEPEGALAERIAEDFGSYEAWKGEFEAAAGAAGGWALLVYDSFSNQLRNVVVDKHDQGALWGSHPILALDVWEHSYYHDYGPARGDFVSAFFEVVDWDEPAARYEQAVELFE | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 22412
Sequence Length: 200
EC: 1.15.1.1
|
P50058 | MQTTFRRILILFVGLLVPLFFACQSNSQVDAAPSAAPQLSASPAKLDPLPYDYAALEPYIDAQTMRLHHDKHHATYVNNINETLKAYPDLQKQSVDSLIQNLNQVPEAIRTKIRNNGGGHVNHTMFWQIMAPKAGGTPTGAVAKAIDQTFGSFDAFKQQFNKAGADRFGSGWAWLVSDRQGKLSITSTANQDNPLMSNPNAYPILGNDVWEHAYYLKYQNRRAEYLTNWWNVVNWQAVNQRYAQAQRK | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 27956
Sequence Length: 248
EC: 1.15.1.1
|
P09233 | MALRTLASKKVLSFPFGGAGRPLAAAASARGVTTVTLPDLSYDFGALEPAISGEIMRLHHQKHHATYVANYNKALEQLETAVSKGDASAVVQLQAAIKFNGGGHVNHSIFWKNLKPISEGGGEPPHGKLGWAIDEDFGSFEALVKKMNAEGAALQGSGWVWLALDKEAKKVSVETTANQDPLVTKGASLVPLLGIDVWEHAYYLQYKNVRPDYLNNIWKVMNWKYAGEVYENVLA | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 25545
Sequence Length: 235
Subcellular Location: Mitochondrion matrix
E... |
Q9K4V3 | MAFELPNLPYGFDALEPHIDQQTMEIHHGKHHNTYVTKLNAAVEGTDLESKSIEEIVANLDSVPENIQTAVRNNGGGHLNHSLFWELLTPNSEEKGTVVDKIKEQWGSLDAFKEEFADKAAARFGSGWAWLVVNNGNLEIVTTPNQDNPITEGKTPILGLDVWEHAYYLKYQNKRPDYISAFWNVVNWEKVDELYNAAK | Cofactor: Binds 1 Mn(2+) or Fe(3+) ion per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. Catalyzes the dismutation of superoxide anion radicals into O2 and H2O2 by successive reduction and oxidation of the transition metal i... |
P80733 | ATYTLPEPPYDYAAL | Cofactor: Binds 1 Fe(2+) or Zn(2+) ion per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 1685
Sequence Length: 15
EC: 1.15.1.1
|
O54233 | QFDQETMTLHHDKHHATYVANANAALEKHPEIGENLEELLANVESIPADIRQALINNGGGHLNHALFWELLSPEKTEVTKEVASAIDQAFGSFDAFKEQFAAAATGRFGSGWAWLVVTKEGSLEITSTANQDTPISEGKKPILAL | Cofactor: Binds 1 Mn(2+) or Fe(3+) ion per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. Catalyzes the dismutation of superoxide anion radicals into O2 and H2O2 by successive reduction and oxidation of the transition metal i... |
P09738 | MAILLPDLPYAYDALEPYIDAETMTLHHDKHHATYVANANAALEKHPEIGENLEVLLADVEQIPADIRQSLINNGGGHLNHALFWELLSPEKTKVTAEVAAAINEAFGSFDDFKAAFTAAATTRFGSGWAWLVVDKEGKLEVTSTANQDTPISQGLKPILALDVWEHAYYLNYRNVRPNYIKAFFEVINWNTVARLYAEALTK | Cofactor: Binds 1 Mn(2+) or Fe(3+) ion per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. Catalyzes the dismutation of superoxide anion radicals into O2 and H2O2 by successive reduction and oxidation of the transition metal i... |
O33756 | YIDEETMHLHHDKHHQTYVNNVNAALEKHPEIGEDLESLLADVESIPADIRQAVINNGGGHLNHALFWELMTPEQTAPSAELAAAIDATFGSFEDFKAAFTAAATTRFGSGWAWSVVNKEGKLEVTSTANQDTPLSEGKTPILGL | Cofactor: Binds 1 Mn(2+) or Fe(3+) ion per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. Catalyzes the dismutation of superoxide anion radicals into O2 and H2O2 by successive reduction and oxidation of the transition metal i... |
P0A4J6 | MAIILPELPYAYDALEPYIDAETMHLHHDKHHQTYVNNANAALEKHPEIGEDLEALLADVESIPADIRQALINNGGGHLNHALFWELMTPEKTAPSAELAAAIDATFGSFEEFQAAFTAAATTRFGSGWAWLVVNKEGKLEVTSTANQDTPISEGKKPILGLDVWEHAYYVKYRNVRPDYIKAFFSVINWNKVDELYAAAK | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. May play a critical role against oxidative stress, affecting both the survival and the virulence of S.pneumoniae.
Catalytic Activity: 2 H(+) + 2 ... |
P87219 | MSEEIISFTNPALGPLPTKAPQLPSNVLDLFSLKGKVASVTGSSGGIGWAVAEAFAQAGADVAIWYNSKPADAKAEYLTEKYGVKAKAYKCNVTDPNDVSKVINEIEKDFGTIDIFVANAGVAWTDGPEIDVQGYDQWKKIVDCDLNGVYYCAHTVGQIFKKNKSGSLIITSSMSGTIVNIPQLQAPYNAAKAACTHLAKSLSVEWASFGARVNSISPGYILTDIADFADPEMKKKWWQLTPLGREGLPQELVGAYLYLASNASTYTTGSNIAVDGGYTCP | Function: Catalyzes the NADP dependent reduction of L-sorbose to D-glucitol. Can also convert fructose to mannitol, but less efficiently.
Catalytic Activity: D-sorbitol + NADP(+) = H(+) + keto-L-sorbose + NADPH
Sequence Mass (Da): 30038
Sequence Length: 281
Pathway: Carbohydrate degradation; L-sorbose degradation.
EC: ... |
Q9Y6Z9 | MTSMFSLKGKTTLITGGSGGIGFSIAKAFAAAGSNVGLLYGRNKKALEYAAELRDKHGVQAKAYSCPIENRSAVIETTNQAVEELGGRLDVMIANAGIAIPHLSLEDKNEDIWTKVVGINLNGAYYTAQAAGHHFKKQGKGSLIFTASMSGHIANWPQQWASYHATKAAVKHLARALAVEWAPFARVNSVSPGYIDTDLTLYADENLRKKWKEYTPQARIGLPDELPGAYLYLASDASSYCTGSDIIVDGGYCSR | Function: Catalyzes the NADP dependent reduction of L-sorbose to D-glucitol.
Catalytic Activity: D-sorbitol + NADP(+) = H(+) + keto-L-sorbose + NADPH
Sequence Mass (Da): 27437
Sequence Length: 255
EC: 1.1.1.289
|
P56693 | MAEEQDLSEVELSPVGSEEPRCLSPGSAPSLGPDGGGGGSGLRASPGPGELGKVKKEQQDGEADDDKFPVCIREAVSQVLSGYDWTLVPMPVRVNGASKSKPHVKRPMNAFMVWAQAARRKLADQYPHLHNAELSKTLGKLWRLLNESDKRPFIEEAERLRMQHKKDHPDYKYQPRRRKNGKAAQGEAECPGGEAEQGGTAAIQAHYKSAHLDHRHPGEGSPMSDGNPEHPSGQSHGPPTPPTTPKTELQSGKADPKRDGRSMGEGGKPHIDFGNVDIGEISHEVMSNMETFDVAELDQYLPPNGHPGHVSSYSAAGYGL... | Function: Transcription factor that plays a central role in developing and mature glia (By similarity). Specifically activates expression of myelin genes, during oligodendrocyte (OL) maturation, such as DUSP15 and MYRF, thereby playing a central role in oligodendrocyte maturation and CNS myelination (By similarity). On... |
Q04888 | MAEEQDLSEVELSPVGSEEPRCLSPGSAPSLGPDGGGGGSGLRASPGPGELGKVKKEQQDGEADDDKFPVCIREAVSQVLSGYDWTLVPMPVRVNGASKSKPHVKRPMNAFMVWAQAARRKLADQYPHLHNAELSKTLGKLWRLLNESDKRPFIEEAERLRMQHKKDHPDYKYQPRRRKNGKAAQGEAECPGGEAEQGGAAAIQAHYKSAHLDHRHPEEGSPMSDGNPEHPSGQSHGPPTPPTTPKTELQSGKADPKRDGRSLGEGGKPHIDFGNVDIGEISHEVMSNMETFDVTELDQYLPPNGHPGHVGSYSAAGYGL... | Function: Transcription factor that plays a central role in developing and mature glia . Specifically activates expression of myelin genes, during oligodendrocyte (OL) maturation, such as DUSP15 and MYRF, thereby playing a central role in oligodendrocyte maturation and CNS myelination . Once induced, MYRF cooperates wi... |
Q8AXX8 | MSDDQSLSEVEMSPVGSEDPSLTPDPLPPHAHSSPDDDDDDDEEEEEETKVKKEQDSEDERFPVCIREAVSQVLNGYDWTLVPMPVRVNGGSKSKPHVKRPMNAFMVWAQAARRKLADQYPHLHNAELSKTLGKLWRLLNENDKRPFIEEAERLRMQHKKDHPDYKYQPRRRKNGKPSPGEGDGSSEAEGGAASIQAHYKNSHLDHRHGSPMSDGNSEHSTGQSHGPPTPPTTPKTELQAGKSDGKRDGSHALREGGKPQIDFGNVDIGEISHDVMSNMETFDVNEFDQYLPPNGHAGHPSHIGGYTSSYGLTGALAAGP... | Function: Acts early in neural crest formation, functioning redundantly with the other group E Sox factors sox8 and sox9 to induce neural crest progenitors. Acts downstream of wnt-signaling at the neural plate border. Involved in the specification of neural crest progenitors fated to form the pigment cell lineage.
PTM:... |
Q15506 | MSIPFSNTHYRIPQGFGNLLEGLTREILREQPDNIPAFAAAYFESLLEKREKTNFDPAEWGSKVEDRFYNNHAFEEQEPPEKSDPKQEESQISGKEEETSVTILDSSEEDKEKEEVAAVKIQAAFRGHIAREEAKKMKTNSLQNEEKEENK | Function: Sperm surface zona pellucida binding protein. Helps to bind spermatozoa to the zona pellucida with high affinity. Might function in binding zona pellucida and carbohydrates (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 17406
Sequence Length: 151
Subcellular Location: Memb... |
Q62252 | MSIPFSNTHYRIPQGFGNLLEGLTREILREQPDNIPAFAAAYFENLLEKREKTSFDPAEWGAKVEDRFYNNHAFKEQEQVEKCEQELAKSSGREETPVTPFEESTEEEREQEEAAALKIQSLFRGHVAREEVKKMKSDKNENLKEEADN | Function: Sperm surface zona pellucida binding protein. Helps to bind spermatozoa to the zona pellucida with high affinity. Might function in binding zona pellucida and carbohydrates (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 17296
Sequence Length: 149
Subcellular Location: Memb... |
P36425 | MSIPFSNTHYRIPQGFGNLLEGLTREILREQPDNIPAFAAAYFENLLEKREKTNFDPAEWGAKVDDRFYNNHAFQEHESEKCEAEEKSQSVTEEETPVLTIDSEDDKDKEEMAALKIQAAFRGHLAREDVKKIRTNKAEEETEENN | Function: Sperm surface zona pellucida binding protein. Helps to bind spermatozoa to the zona pellucida with high affinity. Might function in binding zona pellucida and carbohydrates.
PTM: The N-terminus is blocked.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 16892
Sequence Length: 146
Subcellula... |
Q8L7N4 | MIPWGGVTCCLSAAALYLLGRSSGRDAEVLETVTRVNQLKELAQLLELDSKILPFIVAVSGRVGSETPIKCEHSGIRGVIVEETAEQHFLKHNETGSWVQDSALMLSMSKEVPWFLDDGTSRVHVMGARGATGFALTVGSEVFEESGRSLVRGTLDYLQGLKMLGVKRIERVLPTGIPLTIVGEAVKDDIGEFRIQKPDRGPFYVSSKSLDQLISNLGKWSRLYKYASMGFTVLGVFLITKHVIDSVLERRRRRQLQKRVLDAAAKRAELESEGSNGTRESISDSTKKEDAVPDLCVICLEQEYNAVFVPCGHMCCCTAC... | Function: E3 ubiquitin-protein ligase involved in the regulation of protein import in the chloroplast. Associates with TOC complexes and mediates ubiquitination of TOC components, promoting their degradation via the ubiquitin-proteasome system (UPS). Plays a role in the reorganization of the TOC machinery. Involved in ... |
Q9JHX2 | MAAVAVLRNDSLQAFLQDRTPSASPDLGKHSPLALLAATCSRIGQPGAAAAPDFLQVPYDPALGSPSRLFHPWTADMPAHSPGALPPPHPSLGLTPQKTHLQPSFGAAHELPLTPPADPSYPYEFSPVKMLPSSMAALPASCAPAYVPYAAQAALPPGYSNLLPPPPPPPPPPTCRQLSPAPAPDDLPWWSIPQSGAGPGSSGVPGTSLSSACAGPPHAPRFPASAAAAAAAAAALQRGLVLGPSDFAQYQSQIAALLQTKAPLAATARRCRRCRCPNCQAAGGAPEAEPGKKKQHVCHVPGCGKVYGKTSHLKAHLRWH... | Function: Binds to GC boxes promoters elements. Probable transcriptional activator that has a role in the coordination of changes in transcription required to generate pattern in the developing embryo.
Sequence Mass (Da): 42052
Sequence Length: 398
Domain: The 9aaTAD motif is a transactivation domain present in a large... |
Q9NAX4 | MKVLLLLVCLVFAYVNASYDACYNVVCPSNYQCRAEGDQAYCVPEHHEYGCDRHSCGRGYECVERWDSFCCKPIHHRPHPHPRPPHPHPRPTNCDYTSCPREFDCHVINRNVTACLPDNHVCRDFQCPVGTHCFNGERGPHCVSDTHYPNLCRVTKCSYDFTCKMVRGNPTCLRNHDGISTHSPTHTPTHSPTTSPTHCPSCTELAPFCHSAGLVCRTILNPSCVSAVRGIINTRSCCTYIAVCASNSTSTTGATTGATTPTSTTGAATTAAATTTTATSTTGAATTAPATTTTTSTTGAATTAPATTTTSTTGAATTAP... | Function: Forms a triad with cellulose and pspB that is essential for spore outer layer formation.
Sequence Mass (Da): 47250
Sequence Length: 464
Domain: The N-terminal part (18-235) contains the information required for insertion into the coat.
Subcellular Location: Spore wall
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Q3SY56 | MLTAVCGSLGSQHTEAPHASPPRLDLQPLQTYQGHTSPEAGDYPSPLQPGELQSLPLGPEVDFSQGYELPGASSRVTCEDLESDSPLAPGPFSKLLQPDMSHHYESWFRPTHPGAEDGSWWDLHPGTSWMDLPHTQGALTSPGHPGALQAGLGGYVGDHQLCAPPPHPHAHHLLPAAGGQHLLGPPDGAKALEVAAPESQGLDSSLDGAARPKGSRRSVPRSSGQTVCRCPNCLEAERLGAPCGPDGGKKKHLHNCHIPGCGKAYAKTSHLKAHLRWHSGDRPFVCNWLFCGKRFTRSDELQRHLQTHTGTKKFPCAVCS... | Function: Promotes cell proliferation (By similarity). Plays a role in tooth germ growth (By similarity). Plays a role in the control of enamel mineralization. Binds the AMBN promoter .
Sequence Mass (Da): 39840
Sequence Length: 376
Domain: The 9aaTAD motif is a transactivation domain present in a large number of yeast... |
Q8VI67 | MASSLLEEEAHYGSSPLAMLTAACSKFGGSSPLRDSTTLGKGGTKKPYADLSAPKTMGDAYPAPFSSTNGLLSPAGSPPAPASGYANDYPPFPHSFPGPTGAQDPGLLVPKGHSSSDCLPSVYTSLDMTHPYGSWYKAGIHAGISPGPGNTPTPWWDMHPGGNWLGGGQGQGDGLQGTLSTGPAQPPLNPQLPTYPSDFAPLNPAPYPAPHLLQPGPQHVLPQDVYKPKAVGNSGQLEGSGAAKPPRGAGTGGSGGYAGSGAGRSTCDCPNCQELERLGAAAAGLRKKPIHSCHIPGCGKVYGKASHLKAHLRWHTGERP... | Function: Transcriptional activator essential for osteoblast differentiation . Binds to SP1 and EKLF consensus sequences and to other G/C-rich sequences .
PTM: Propionylated . Depropionylation at Lys-368 by SIRT7 activates transcription factor activity and positively regulates bone formation by osteoblasts .
Sequence M... |
P54704 | MRLLSVLLIGFLCLAGTYAQKYQLSPAYNDPYLTDDKTGTHDFWVQNASLPVFYGFHDWNFQDNSGIMEINGDEMHITGKIYPTVNMGDCHRYNVDLVFKKDKSGNVMPKKELRESAYVPHGPIDPATWKYYTFVQGKWTGFGCDPQNVVFSGAEGGMPLQLGYGANGKNGDNGISVWLIYGYTIVDINCNIRPIITQSPTQPPTQPPTYPPTQPPTQPPTQPPTYPPTYPPTYPPTYPPTYPPTHPPTYPPTYPPTQPPTQPPVQDCSTLECPEGFHCEIVNNRRTCVCDTTVPPTHPPTQSPTYPPTQPPTQPPTYPP... | Function: Required for incorporation of cotE into the spore coat and for the formation of the outer layer. Has a cross-bridging function between cellulose and other coat proteins.
PTM: O-glycosylated.
Sequence Mass (Da): 59506
Sequence Length: 532
Domain: The N-terminal part (1-200) directs accumulation in prespore ves... |
P54643 | MLFLKNIGVFFMIFLVSKSYATDCNKITNEEECHKSSECIVINYTPCCGEQKWACSKGTFDTCTYENSCYRNSSNNQVVEVSNKCFNLDGFIKITTPTEYSCSDAKIKECALLGKSCSFQKNSCSNPTSCCPGESICEGLSSGSSTSGGGSSGGTSGGSSSGGTSGGSSSGGTSGSSSSGSSSGGVSSCSTTHCPEGYHCSMVNDVATCLASTTGGTGLPGTSSSTAGVSSCLTTLCPIGHICVEDSNGVNCVPNGGGTSGGSSSTGTSGGHPDPCRDVDCPDGFHCECKDGKTAKCVPSPTTGSSSTSGGHPDPCKDVT... | Function: May contribute to the structure of the coat at the interface between the middle, cellulosic layer and the outer, electron-dense, proteinaceous layer.
PTM: Disulfide bonding is important for associating SP87 with the coat.
Sequence Mass (Da): 71805
Sequence Length: 677
Subcellular Location: Cytoplasmic vesicle... |
Q64HY5 | MLAATCNKIGSPSPSPSALSDSASSFGKGFHPWKRSSSSSSASAGSCGAVGSGLPGFGVAGAARNGSSAAAAAAAAAAAALVSDSFSCGGSPGSSAFSLTSSGAAAASSPFANDYSVFQAPGSAGGGGGGGGGGGGAAGQEAAHQPVFISKVHASVEGLQGIYPRVGMAHPYESWFKPSHPGLAAGEVGSAGASSWWDVGAGWIDVQSPNGAAALPGSLHPAAGGLQSSLHSPLGGYNSDYSGLGHSAFGGGASSHLLSPAGQHLMDGFKPVLPGSYPDSAPSPLAGAGGSMLGGGPAAPLSASPRSSARRYSGRATCDC... | Function: Transcription factor which plays a key role in limb development. Positively regulates FGF8 expression in the apical ectodermal ridge (AER) and contributes to limb outgrowth in embryos.
Sequence Mass (Da): 47402
Sequence Length: 480
Domain: The 9aaTAD motif is a transactivation domain present in a large number... |
Q8IXZ3 | MLAATCNKIGSPSPSPSSLSDSSSSFGKGFHPWKRSSSSSSASCNVVGSSLSSFGVSGASRNGGSSSAAAAAAAAAAAAAALVSDSFSCGGSPGSSAFSLTSSSAAAAAAAAAAAASSSPFANDYSVFQAPGVSGGSGGGGGGGGGGSSAHSQDGSHQPVFISKVHTSVDGLQGIYPRVGMAHPYESWFKPSHPGLGAAGEVGSAGASSWWDVGAGWIDVQNPNSAAALPGSLHPAAGGLQTSLHSPLGGYNSDYSGLSHSAFSSGASSHLLSPAGQHLMDGFKPVLPGSYPDSAPSPLAGAGGSMLSAGPSAPLGGSPR... | Function: Transcription factor which plays a key role in limb development. Positively regulates FGF8 expression in the apical ectodermal ridge (AER) and contributes to limb outgrowth in embryos (By similarity).
Sequence Mass (Da): 48674
Sequence Length: 490
Domain: The 9aaTAD motif is a transactivation domain present i... |
Q5B8F4 | MAPKPPSGTSSRAWDAVNPPLSEWVLDAVSSMGFTRMTPVQASAIPLFMAHKDVVVEAVTGSGKTLSFLIPVVEKLLRLEEPIKKHHVGAIIVSPTRELASQIYNVLTSLLAFHPASAAVINTSETEDVPRPKHSSSVLRVVPQLLLGGSTSPAEDLSTFLKRSPNLLVATPGRLLELLSSPHVYCPQSSFEMLVLDEADRLLDLGFKETLQNILRRLPKQRRTGLFSASVSEAVDQIVRVGLRNPVKVVVKVKGASGVDDKRTPASLQMTYLTQPPTGKFPALKHILNSVQPTPSKSIFFVSTCSGVDYLSVILPLILG... | Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits. Binds 90S pre-ribosomal particles and dissociates from pre-60S ribosomal particles after processing of 27SB pre-rRNA. Required for the normal formation of 18S rRNA through the processing of pre-rRNAs at sites A0, A1 and A2, and the... |
Q8SR49 | MGCKGIEDVAMNGRLKKEIEENGFGKMTEVQLKCIPEVLKGKDVVVQSPTGTGKTMAFLAPILSCIYDGKGRGRPGVTAVVITPTRELALQIREVAGLFDVKCECFIGGMSIEEDYKRMKEEFSIAVGTPGRLLEIVGKETKKFSSLSHLVLDEADKLLGFGFEEKLMQLLAKLPRNRVTGLFSATRNDSVDKLSRVFLRNPVSINVGNNEMPVALEYIVVSPMEKLLVLMDIVTGRRCIVFFATCSEVDFFSGLVSRAGFGNICKIHGKISQDERNRVYEEFFQRDGLLFCTDVAARGIDFRGVDLVVHFDVPKEYSSI... | Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits. Binds 90S pre-ribosomal particles and dissociates from pre-60S ribosomal particles after processing of 27SB pre-rRNA. Required for the normal formation of 18S rRNA through the processing of pre-rRNAs at sites A0, A1 and A2, and the... |
Q873H9 | MAPTQPQTKVRKPPRSWDALTPPLAQWILDYLSSMGFTQPTPVQKSCLELFRGNKDVVVEAVTGSGKTLAFLIPVVEKLLRGEEPAKRNHVQGIIISPTRELATQIYNVLVSLVKFHEPSAEAISHAKSDEKRPTATQPVVVPQLLVGGTTKAAEDLGTFLRLSPNLLIGTPGRLAELLSSAYVKAPASTFEVLIMDEADRLLDMGFANELNRILGYLPKQRRTGLFSASLSDAVERLITVGLLYPHKITVRVKSLKDGGIIQERKTPMSLQMSYLVTPASQKMPAIVQLLEKLEPRPQRSIIFFSSCMAVKYFSRILGA... | Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits. Binds 90S pre-ribosomal particles and dissociates from pre-60S ribosomal particles after processing of 27SB pre-rRNA. Required for the normal formation of 18S rRNA through the processing of pre-rRNAs at sites A0, A1 and A2, and the... |
O74764 | MSFQSINIDKWLKNAVAAQGFKKMTPVQANAIPLFLKNKDLVVEAVTGSGKTLAYLLPCFDKVTRRDTDETGLGALIVAPTRELATQIFNVTKELLAYQPDSLDGGKKLVADMYIGGKGTLTNDLASFREKNPSVVIGTPGRLNEMLSHISSKHLEILILDEADTLIDMGFQRTLQSIISQLPKQRRTGLFSATMNDTVSSFLKIAGLRNSVRVSVTVTSKKIDTRTPSSLAIQSLVIPPIYKVQCMIHLLCTIEYEKAIVFFSSCASVEYFNSLFLTYKLPFEIVALHGQQVQSNRSRNFEKFKKSNKKTVLFTTDIAS... | Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits. Binds 90S pre-ribosomal particles and dissociates from pre-60S ribosomal particles after processing of 27SB pre-rRNA. Required for the normal formation of 18S rRNA through the processing of pre-rRNAs at sites A0, A1 and A2, and the... |
Q4P9E5 | MSAEPSVQTTSSSGPTELRSAPSYAGSWTKLTPPLTPWVVSLLSDLGFGQMTPVQASTIPLFVSHKDVVVEAVTGSGKTLAFVIPVLEMLARRTTRLKKDEVGALIVSPTRELAEQIYKVLVMFLDAQNHAHVQAQQQQDQDEQDEQDEQEAQSDSDTDPDASTALNNKRKSSNHLVARKNMISGAQLVVGGSKCTPLDDYRQLRDSGADILVGTPGRLEELLSKKGVKKSSLEVLVLDEADRLLDLGFTENLRRILSLLPKQRRTGLFSATMTDALSELVRIGLRNPVRVVVKVEAKHKTSSSIDDSRRTPATLQNLYQ... | Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits. Binds 90S pre-ribosomal particles and dissociates from pre-60S ribosomal particles after processing of 27SB pre-rRNA. Required for the normal formation of 18S rRNA through the processing of pre-rRNAs at sites A0, A1 and A2, and the... |
Q6C193 | MSTDWKDLPVAPWLIDTMEQFGFTDMTPVQASVIPMFAGNKDVIVEAVTGSGKTIAFLVPLIQRMLNLLKEGPAVSGRVYSVVVSPTRELARQTYEVLQSILEMGCPEADASDKITLEKKKKGKAAPTMPKKIRGQLIMGGDLPSHMDLKNFLRDKPQIIVATPGRLLELLRAPQIKTSAFDSLVLDEADRLLDLGFGRDITSIINILPKQRRTGLFSATITDAIQNLVKIGLRNPVKIVVKVGGKKEQKTPLSLGLSYVVLEPREKLAYALNLLSIYPYRKAIVYLPTCAAVTYYQQMFSHLNEGREEPYEIYGLHGKL... | Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits. Required for the normal formation of 18S rRNA through the processing of pre-rRNAs at sites A0, A1 and A2, and the normal formation of 25S and 5.8S rRNAs through the processing of pre-rRNAs at sites C1 and C2 (By similarity).
Sequen... |
Q9XWW1 | MTDEPVKVVNKWDGPTVKNALDEVVKKILNDKVGWTESHNLMNLRLLISFIGVAFSAFACGYDYYEPFPKSKIVLAVCSVSYFICMGILQMYQWYVEKDCIYEATEVDGKQSRKWAWSSEIKAHDDKYTLSAEFKKEGRSGQGKITKSIGAYIDNDGEIIVPLVKKEVDDLYNRLIRSEQ | Function: Component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (By similarity). Enhances the enzymatic activity of SPC and facilitates the interactions between different comp... |
Q5BJI9 | MAARNGKNSILEKWRIDEKPVKIDKWDGAAVKNSLDDAAKKVLIEKYGYLESFNLVDGRLFICTVSCLFTIVALIWDYLHPFPESKPVLACCVVSYFIMMGILTLYTSYKEKNIFLVAMQKDPAGMDPDHSWCLSSSLKRFDDQYTLRMSFTDGKTKQSRETEFTKSVSVFFDENGTLVMDQYEKYVSKLHDTLATEKKTK | Function: Component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (By similarity). Enhances the enzymatic activity of SPC and facilitates the interactions between different comp... |
Q55E35 | MSTTTTTTTTEKPIQVTLYDSNTIKQTLDDSIVKYVTSALSYTQNQKLNYTKVLFGLIGCTLAAIAQFYPIPFPKNKPVLILCVALYVVISLILYYINIFIQKDYILQASKSNDEIKVATVLQKYDPNYQVKIENAKNSSINVPFSKSIDLYFDTKGTFLESNFHNDLSVQFKKFAKLNVKDK | Function: Component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (By similarity). Enhances the enzymatic activity of SPC and facilitates the interactions between different comp... |
Q9VYY2 | MGKKDEKSQQGEELVKVNKWDGSAVKHALDDAVKTCLLGDRPQLKEQFGLVNTRLALCALAVSVAIMAHAWDFTHPFPESRPVLLFSVLAYFALLGILTLHSSFREKGTFAVALQKDKERERLWEASSDMRKYDDKYLLTLSVRDTKNGKRREQSSNKSCAAFIDQNGIVLDNLVANEVNRLFNALAADKKNASSLSSN | Function: Component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (By similarity). Enhances the enzymatic activity of SPC and facilitates the interactions between different comp... |
Q15005 | MAAAAVQGGRSGGSGGCSGAGGASNCGTGSGRSGLLDKWKIDDKPVKIDKWDGSAVKNSLDDSAKKVLLEKYKYVENFGLIDGRLTICTISCFFAIVALIWDYMHPFPESKPVLALCVISYFVMMGILTIYTSYKEKSIFLVAHRKDPTGMDPDDIWQLSSSLKRFDDKYTLKLTFISGRTKQQREAEFTKSIAKFFDHSGTLVMDAYEPEISRLHDSLAIERKIK | Function: Component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum . Enhances the enzymatic activity of SPC and facilitates the interactions between different components of the t... |
Q9CYN2 | MAASASQGGRSGGGGGSSGAGGGPSCGTSSSRSGLLDKWKIDDKPVKIDKWDGSAVKNSLDDSAKKVLLEKYKYVENFGLIDGRLTICTISCFFAIVALIWDYMHPFPESKPVLALCVISYFVMMGILTIYTSYKEKSIFLVAHRKDPTGMDPDDIWQLSSSLKRFDDKYTLKLTFISGRTKQQREAEFTKSIAKFFDHSGTLVMDAYEPEISRLHDSLATERKIK | Function: Component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (By similarity). Enhances the enzymatic activity of SPC and facilitates the interactions between different comp... |
Q9NFA0 | MSGNNVQEEDSTFHVSNLYSETEIKKITQDFISEKIREQNFEEIVKYSNIRIFLSLVLIVIGTYCSIFVQYKKNPVIMIQLLVAFFVVSTTLIIFEYFFFDDVFMILRSNNGSLVKLYCRLDVKKSTLILAYKLNKNVFETSFELKRLYNENGYLMKPYAKNVVMNFLSAHGRTLKLKN | Function: Component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum . Enhances the enzymatic activity of SPC and facilitates the interactions between different components of the t... |
Q5M8Y1 | MAARGGKNGLLEKWKIDDKPVKIDKWDGSAVKNSLDDAAKKVLLEKYRYVENFCLIDGRLIICTISCVFAIVALVWDYLHPFPESKPVLAICVISYFLMMGILTIYTSYKEKSIFLVAHRKDPAGMDPDDIWHLSSSLKRFDDKYTLKVTYISGKTKAQRDAEFTKSIARFFDDNGTLVMDLFEPEVSKLHDSLAMEKKTK | Function: Component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (By similarity). Enhances the enzymatic activity of SPC and facilitates the interactions between different comp... |
Q60MW2 | MHNLLSRANSLLAFTLWVMAAVTAACFLSTVFLDYTVSNHLEVNDIKIRNVRDYATDDKQADLATLAFNLKVDFSRLFNWNVKQLFVYLVAEYKSAENAVNQVVIWDRIVERAERVVMDEIGVKTKYYFLDDGAHLLKHDNVTFVLRYNVIPNAGYLRLVQSTNQLVVPFPTTYTTTRRS | Function: Essential component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (By similarity). Essential for the SPC catalytic activity, possibly by stabilizing and positioning th... |
B0G180 | MHSLSQRANTIVCFGGIVLVGVLLLNVLSRAFFSDHVDVDIKLNEIHRFNTQRNFEYSFISIDLDANLEPLFNWNTKMLFLYVTAEYRTKQNVLSQVVVWDHILTEKSKANIHEKRLSKYPIINQGLGLKNNTIKLTFNYNVVPISGILTRHQVGTSEFKFPTTYMKEAY | Function: Essential component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (By similarity). Essential for the SPC catalytic activity, possibly by stabilizing and positioning th... |
Q9VCA9 | MHTVLTRGNATVAYTLSVLACLTFSCFLSTVFLDYRTDANINTVRVLVKNVPDYGASREKHDLGFVTFDLQTNLTGIFNWNVKQLFLYLTAEYQTPANQLNQVVLWDKIILRGDNAVLDFKNMNTKYYFWDDGNGLKDNRNVSLYLSWNIIPNAGLLPSVQATGKHLFKFPADYATSSI | Function: Essential component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (By similarity). Essential for the SPC catalytic activity, possibly by stabilizing and positioning th... |
P61009 | MNTVLSRANSLFAFSLSVMAALTFGCFITTAFKDRSVPVRLHVSRIMLKNVEDFTGPRERSDLGFITFDITADLENIFDWNVKQLFLYLSAEYSTKNNALNQVVLWDKIVLRGDNPKLLLKDMKTKYFFFDDGNGLKGNRNVTLTLSWNVVPNAGILPLVTGSGHVSVPFPDTYEITKSY | Function: Essential component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum . Essential for the SPC catalytic activity, possibly by stabilizing and positioning the active center... |
P70999 | MRFDEAYSGKVFIASRPEWEEADAILYGMPMDWTVSYRPGSRFGPSRIREVSIGLEEYSPYLDRDLADLNFFDAGDIPLPFGNPQRSLDMIEEYVDSILEKGKFPMGMGGEHLVSWPVIKAMYKKYPDLAIIHFDAHTDLRVDYEGEPLSHSTPIRKAAELIGPHNVYSFGIRSGMKEEFEWAKENGMHISKFEVLEPLKEVLPKLAGRPVYVTIDIDVLDPAHAPGTGTVDAGGITSKELLASVHEIARSEVNVKGADLVEVAPVYDHSEQTANTASKIIREMLLGFVK | Function: Catalyzes the formation of putrescine from agmatine.
Catalytic Activity: agmatine + H2O = putrescine + urea
Sequence Mass (Da): 32417
Sequence Length: 290
Pathway: Amine and polyamine biosynthesis; putrescine biosynthesis via agmatine pathway; putrescine from agmatine: step 1/1.
EC: 3.5.3.11
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Q7VRG4 | MCTLMHKHDDSLFSNSFGFLRLPLEFYPYTRHNDWVITGVPFDIATSGRSGSRFGPASIRKASINLAWENCRWPWNFDIRQKLKIIDCGDLIYKSGNVQDFTNILQKHIENLLRFRKKILLLGGDHYITLPVLRAYSKFFGTISIIHFDAHADYYDNNNQYDHGAVILYALHEKLINPNRSVQIGIRTEYDKNFGFTVLDAEYVNTTAVHVLINQIVSVIQNRPVYLTFDIDCLDPSVAPGTGTPVIGGLTTSCALQIIRGFQKLNIIGIDIVEVAPVYDCAQITALAAATLGLEMLYTQVKF | Function: Catalyzes the formation of putrescine from agmatine.
Catalytic Activity: agmatine + H2O = putrescine + urea
Sequence Mass (Da): 34254
Sequence Length: 303
EC: 3.5.3.11
|
Q90XD2 | MICLLRTARLSARLLFASAAAPCRRASRFNVPPSAEFVARPVGVCSMLRLPVQTSAEGLDAAFVGVPLDTGTSNRPGARFGPQQIRAESVMVRRYNASTGAAPFDSLLVADVGDVNVNLYNLPDSCRRIRESYQKIVASGCVPLTLGGDHSITYPILQAVAEKHGPVGLVHVDAHTDTSDMALGEKIYHGTPFRRCVDEGLLDCSRVVQIGIRGSSYAPNPYKYCWDQGFRVVPAEECWMKSLVPLMGEVRQQMGDGPVYISFDIDGLDPAYAPGTGTPEIAGLTPMQALEIIRGCKGLNIVGCDLVEVAPIYDVSGNTA... | Catalytic Activity: agmatine + H2O = putrescine + urea
Sequence Mass (Da): 36488
Sequence Length: 340
Pathway: Amine and polyamine biosynthesis; putrescine biosynthesis via agmatine pathway; putrescine from agmatine: step 1/1.
Subcellular Location: Mitochondrion
EC: 3.5.3.11
|
Q7P0S6 | MSDEMIYGDGAIRRQGLYGSSIENTYAGVLSFMRRNYSRDLEGVDVAVSGIPLDLSVTFRSGARMGPQAIRAASVQLAELKPYPWGFDPFEDLAVVDYGDCWFDAHNPLTIKPSIIEHARTILASGAKMLTFGGDHYVTYPLLIAHAEKYGKPLALLHFDAHCDTWPDDSPDSLNHGTMFYKAVKEGLIDPKKSVQVGIRTWNDDFMGLNVLGAPWVHDNGVDATIAEIKKTIGDAPVYVTFDIDCLDPSAAPGTGTPVPGGLTTAQALKIIRNLGDLNIVGMDVVEVAPSYDQSEITAIAAAHIACDMLCLMRNKKVAG... | Function: Catalyzes the formation of putrescine from agmatine.
Catalytic Activity: agmatine + H2O = putrescine + urea
Sequence Mass (Da): 34861
Sequence Length: 322
Pathway: Amine and polyamine biosynthesis; putrescine biosynthesis via agmatine pathway; putrescine from agmatine: step 1/1.
EC: 3.5.3.11
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A8APF8 | MSTLGHQYDNSLVSNAFGFLRLPLNFQPYDSDADWVITGVPFDMATSGRAGGRHGPAAIRQVSTNLAWEHNRFPWNFDMRERLNVVDCGDLVYAFGDAREMSEKLQAHAEKLLSAGKRMLSFGGDHFVTLPLLRAHAKHFGKMALVHFDAHTDTYANGCEFDHGTMFYTAPKEGLIDPNHSVQIGIRTEFDKDNGFTVLDACQVNDRGVDDIIAQVNQIVGDMPVYLTFDIDCLDPAFAPGTGTPVIGGLTSDRAIKLVRGLKDLNIVGMDVVEVAPAYDQSEITALAAATLALEMLYIQAAKKGE | Function: Catalyzes the formation of putrescine from agmatine.
Catalytic Activity: agmatine + H2O = putrescine + urea
Sequence Mass (Da): 33525
Sequence Length: 306
Pathway: Amine and polyamine biosynthesis; putrescine biosynthesis via agmatine pathway; putrescine from agmatine: step 1/1.
EC: 3.5.3.11
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Q815E8 | MPKHRKQSKIKIYRITSYKKDKRSELDSDKFELEQQDKHDIQDKQDKQDEQNKQDKQVQSENVTIVPTDSHSLDVWDEISLKEIQAGEHTSLFEEKSNYQNINLVQVNDVRLYLDKQLQFSSVDEQIYHEALVHPIMAKVIDPKRVLILGGGDGLALREVLKYETVLHVDLVDLDEAMINMARNVPEIVSLNKNAFFDNRVNVHVCDAKEFLNSPSSLYDVIIIDFPDPATELLSTLYTSELFARIATFLTEDGAFVCQSNSPADAPLVYWSIGNTIEHAGLTVKSYHTIVPSFGTDWGFHLATNSAHVLDQIEQLYVVP... | Function: Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine.
Catalytic Activity: putrescine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) + S-methyl-5'-thioadenosine + spermidine
Sequence ... |
Q8R977 | MILKLEVGVGLKNLNGKWGLDSSKEFYWEPDVEGGYRVYKVKSVIIEHQSLYQKIDIVELETWGKSLFLDGSLQSTESDEFIYHELLVHPAMRVHPSPKRVLICGVGEGKSVREVLKYPTVKEVIGVDIDKEVVALCQKHLGKTPIDDKRVRLVYQDVAEFIKNYRGEPFDVAIVDVTDDLDGPARSVHQLDFYKRLYEILGEKATVVVQGTSAFSKVKNVGFCHIYEILKEVFPFVIPYADYIPSFSDLWTFFVALKGIKDLTPRHEIPRDLKYYDEYTNERIFTLAKPLREKLGV | Function: Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine.
Catalytic Activity: putrescine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) + S-methyl-5'-thioadenosine + spermidine
Sequence ... |
A2BJU2 | MAQRLPWRFVAEWTSEGEMVLREVKRIYAAGATRYQEYMIAELAGIGKALVLDGKVQSSILDEHWYHEALVHPILLAHQCPRKVLVIGGGEGATVREVLRHSCVEHVTMVDIDEELVELAKKHLAEWHQGAFSSDKLELVIGDGRRYVENCHRKYDAIILDLVDPMEGGPAARLYTLEFYRAVKGCLRPGGAVVTQATSPTLSPRVYAVIRNTLAKVFTIVRPYVSYVRSYNGLWGFVAASDTVDPAKLSAKEVDELIAARIRGQLRFYDGETHEWMFRLPLPVRQVLSETRDYATDEKPVYVPV | Function: Involved in the biosynthesis of polyamines which are thought to support the growth of thermophilic microorganisms under high-temperature conditions. It seems that long-chain and branched-chain of polyamines effectively stabilize DNA and RNA, respectively. Catalyzes the irreversible transfer of a propylamine g... |
Q8EXA3 | MELWLDEALELKNGRALKIKVKEFLHSRTTPFQKIDVFESVGFGRMFTLDGVVMMTEADEFAYHEMIVHVPMMSHPNPEKVLVIGGGDGGTVREVLKHPSVKEVHLCEIDKGVIDVCYEYFPEIANAMKDPRVKHAYEDGAKYVKDYQNYFDCIMVDSSDPVGPAEVLFKRPFYETMANCLKEGGICTTQGESFYYHGSIIRELFNFIPEIFKHCGYYYTVVPTYPSGIIGFTYCSKGPDPYTVVPDPQRVPQGLKYYSAEMHKAAFVLPQFAQKHIVRK | Function: Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine.
Catalytic Activity: putrescine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) + S-methyl-5'-thioadenosine + spermidine
Sequence ... |
Q9HV34 | MPAEVAAGLPPLPPNHFYFYPPDPLLEGDGAITAIEDSDPFDQYVYRLRRVLYQGRTRWQNVLIADTYNYDRVLMLDGAIQSAESDESLYHELLVQPAMLAHDEPRDVLIIGGGEGATLREVLSHASVRRAVMVDLDRELVELCREHLFQWHQGAFDDPRCELLAEDGRAYLERDPSLYDVVIIDVVDMLDNGPAQALYTRQFYELLHSRLRPGGVVAVQGLEFSHSDDKPHAALARTLRSVFSQVHSYRATVPSFLSSWGFLLASDWLDTNHWQAEDIDRRIERKLGPLWLDHLDGDYLKACFVMDRETRFLLAQPGPV... | Function: Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine.
Catalytic Activity: putrescine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) + S-methyl-5'-thioadenosine + spermidine
Sequence ... |
Q9X8S2 | MIEPHAPAPPGSPPSWGGPCGPEAPARLPVRPAVGRFLVLAGVFVCAACGLVYELELVALASYLIGDSVTQASVVLSVMVFAMGLGSLAAKRLRGLAAAGFGALEAALALVGGSSAMLLYAVFAWTGGWGGLWADGPRILLVAFSLAIGVLIGAEVPLLMELIQRVRRQDPGGAVADLFAADYVGALVGGLAFPFVLLPFLGQLTGALLTGTVNAVVGAALVLGLFRRDLTRRARWLLLTANAVVLALLATATVLADDFERAARHAVYGQDVRVAVRTGVQEVVLTGDADGRPLDLFLDGRLRVRGSDERSYHEALVHPA... | Function: Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine.
Catalytic Activity: putrescine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) + S-methyl-5'-thioadenosine + spermidine
Location ... |
Q9YE02 | MAGGSEKSVFLKWSWFLEWLTPDRATLKHIEDVIFQGRSRFQEIAVVRVSGEGKVLVLDGKTQSSESDEFMYHEALVHPAMILHGSPRKVLILGGGEGATLREVLKHRSVEKAVMVDIDETVVNVAREHLREWHRGAFDDPRAEVVIDDAWNYVASKAETGFDVVIADLVDPLEAGPATRLYSEEYYRMVKDVMNPGGVFVTQAVSISHLTEYHAIIRNTVARVFKHVESYGVYVPSFDSMWGFVVASDDKDPRILGDRGFFETRLSHQLQGAELRFLDYASMLHMLNIPKMYREAIAREKRYATLDNQVFLPA | Function: Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine.
Catalytic Activity: putrescine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) + S-methyl-5'-thioadenosine + spermidine
Sequence ... |
O27950 | MVWFFEYYDGCGLAIKVKKKLYEAEGVQKVEIYETESMGKMLVIDGKIQLTELDEPFYHEMLVHVPMLSHENPRKVAVIGGGDGGALREVLKHNVERAVLVDIDRNVIDLSRKFLKIDHGAFEDERVEIAIMDGKEFLRDCEIFDVIIVDSTDPVGVSDTLFDREFFELARQKCDVISLQSQSPLIQKEYFRTLLVNSAPFERRDVYLSCVPTYPLALWSFIIGGEYDFSNLEERFERIKGKTVHYNPDVHRAAFALPEWLKKEVEACI | Function: Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine.
Catalytic Activity: putrescine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) + S-methyl-5'-thioadenosine + spermidine
Sequence ... |
P70998 | MSELWYTEKQTKNFGITMKVNKTLHTEQTEFQHLEMVETEEFGNMLFLDGMVMTSEKDEFVYHEMVAHVPLFTHPNPEHVLVVGGGDGGVIREILKHPSVKKATLVDIDGKVIEYSKKFLPSIAGKLDDPRVDVQVDDGFMHIAKSENQYDVIMVDSTEPVGPAVNLFTKGFYAGIAKALKEDGIFVAQTDNPWFTPELITNVQRDVKEIFPITKLYTANIPTYPSGLWTFTIGSKKYDPLAVEDSRFFDIETKYYTKDIHKAAFVLPKFVSDLIK | Function: Involved in the cell growth and proliferation. Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine (Probable).
Catalytic Activity: putrescine + S-adenosyl 3-(methylsulfanyl)propylamine... |
Q9KDW4 | MLELHDCDATLLNDMQQIKTIMCEAACKAKAMIVTEHFHYFLPFGVSGVVIIQESHLTIHTWPEHGYAAIDVFTCNSKLALQAAVQYITQQFNAGNVTQHYLHRG | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine.
PTM: Is synthesized initially as an ina... |
Q81X04 | MEYSTFGKHIIVDLWGVDFSLLDDMYFLEHHLIHAADLSGAHVLNVSTKEFDPHGVTVLVLLSESHLSIHTYPEQNFAAIDCYTCGTTVEPQIAIDYIVSILKPNEMHIRRLIRGIGEIVNTD | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine.
PTM: Is synthesized initially as an ina... |
Q815E7 | MEYSTFGKHIIVDLWGVDFSLLDDMHFLEYHLVTAADYSGAHVLNVSKKEFQPYGVTVLVLLSESHLSIHTYPEQNFAAIDCYTCGTTVEPQIAIDYIVNILKPERMHIKRLIRGIGEIVTAD | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine.
PTM: Is synthesized initially as an ina... |
A3DDC1 | MNALGRHILAEIYGCDAAILNNRNLIEKIMVESALEAGAEVREVAFHKFSPQGVSGVVVISESHLAIHTWPELGYAAVDVFTCGEKVNPWDACNYLTERFKAKHMTATEVKRGVFEEPVKVANL | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine.
PTM: Is synthesized initially as an ina... |
B7J3Q3 | MRSLGHQIVADFYHCDGSTLSDVDFVTDAMLEAARRANCTIVTQTFHHFSPYGVSGAVIVAESHLAIHTWPEYGYAAVDVFTCGDIIQPEDALNYLKEAFGAGQVSTMEMKRGQVDMMGVPAHELRVKPALCA | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine.
PTM: Is synthesized initially as an ina... |
Q01892 | MLALEAAQLDGPHFSCLYPDGVFYDLDSCKHSSYPDSEGAPDSLWDWTVAPPVPATPYEAFDPAAAAFSHPQAAQLCYEPPTYSPAGNLELAPSLEAPGPGLPAYPTENFASQTLVPPAYAPYPSPVLSEEEDLPLDSPALEVSDSESDEALVAGPEGKGSEAGTRKKLRLYQFLLGLLTRGDMRECVWWVEPGAGVFQFSSKHKELLARRWGQQKGNRKRMTYQKLARALRNYAKTGEIRKVKRKLTYQFDSALLPAVRRA | Function: Sequence specific transcriptional activator which binds to the PU-box, a purine-rich DNA sequence (5'-GAGGAA-3') that can act as a lymphoid-specific enhancer. Promotes development of plasmacytoid dendritic cells (pDCs), also known as type 2 DC precursors (pre-DC2) or natural interferon (IFN)-producing cells. ... |
P18047 | MKRARFEDDFNPVYPYEHYNPLDIPFITPPFASSNGLQEKPPGVLSLKYTDPLTTKNGALTLKLGTGLNIDKNGDLSSDASVEVSAPITKTNKIVGLNYTKPLALQNNALTLSYNAPFNVVNNNLALNMSQPVTINANNELSLLIDAPLNADTGTLRLRSDAPLGLVDKTLKVLFSSPLYLDNNFLTLAIERPLALSSNRAVALKYSPPLKIENENLTLSTGGPFTVSGGNLNLATSAPLSVQNNSLSLGVNPPFLITDSGLAMDLGDGLALGGSKLIINLGPGLQMSNGAITLALDAALPLQYKNNQLQLRIGSASALI... | Function: Forms spikes that protrude from each vertex of the icosahedral capsid. Interacts with host receptor CXCAR to provide virion initial attachment to target cell. Fiber proteins are shed during virus entry, when virus is still at the cell surface (By similarity).
Sequence Mass (Da): 59113
Sequence Length: 547
Dom... |
Q9S840 | MECNAKPPFQWELENLISFGTSTAEVPRKLKPMEWEIDGFDCTSLYSSSFAYAGSSGSDIAHAFSKSSKSTSISSSSAEVRTHNFTSETGESLPGEFAKGIDTSPSLELSFGSGDPVLGLKLGKRTYFEDFWEVENAKGLGLPVTLASSSVSPVKKSKSIPQRLQTPHCQVEGCNLDLSSAKDYHRKHRICENHSKFPKVVVSGVERRFCQQCSRFHCLSEFDEKKRSCRRRLSDHNARRRKPNPGRTYDGKPQVDFVWNRFALIHPRSEEKFIWPSSKHVPSRVLMPQPAKTEISDTEHNRFGLLDPKTKTARAELFSK... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Trans-acting factor that binds specifically to the consensus nucleotide sequence 5'-TNCGTACAA-3'.
Sequence Mass (Da): 46860
Sequence Length: 419
Domain: The SBP-type zinc finger is required for the binding to DNA.
Subcellular Location: Nucleus
|
Q8SS86 | MFFVGVAVLAALQSVWGNGGLETNEVAGMDRLGVESQKENPPGILLRKDDGMCEARKPMDMSPGEVQTETKTVVKEIVVEIEEPREGIQEVLPVVQYEGQAKVSAGNDLLKPSCGVSSGFTSSAERCYVLTKDAHDGDTSKMISLVESLSGRVKRQYTKNITGVSFCSSHSDVLRKVDDAGMHVEEDKIYTVSMLQNNIPNYMYLMRHYENTIFNNYFYDNWIFRVLQIKRVMTKFLGSYEYYHTGKGVNIFLLDTAISSMDGACNLSGRLEACNAHGNVMAELLVGKTNGFAKDSRLSVLDVVDCDGKVALSEMIHGLE... | Function: May be involved in the degradation of proteins for nutrient acquisition or possess a regulatory function by proteolytic activation of proproteins.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 58673
Sequence Length: 535
Subcellular Location: Membrane
EC: 3.4.21.-
|
Q0JGI1 | MDWDAKMPSWDLGTVVGPSGGGGGGGGGGGALDLKLGAPTSWKTTTTVSAASAAPAAVAPPPPPPASSSSSAAAAGKRARAGQGQQAAVPACSVEGCAADLSKCVRDYHRRHKVCEAHSKTAVVTVAGQQQRFCQQCSRFHLLGEFDEEKRSCRKRLDGHNKRRRKPQPDPLNPGNLFANHHGAARFTSYPQIFSTAASMSPQETKWPANVVKTEAADVFQEPYYHALHLNGAGAAAAASIFHHGGNKARKHHFPFLTADHGGGAAAASPLFGCQPFTITPSSESRSSSSSRHSNGKMFAHDGGLDNCALSLLSDNPTPT... | Function: Trans-acting factor that binds specifically to the consensus nucleotide sequence 5'-TNCGTACAA-3' (By similarity). May be involved in panicle development.
Sequence Mass (Da): 42654
Sequence Length: 412
Domain: The SBP-type zinc finger is required for the binding to DNA.
Subcellular Location: Nucleus
|
P93015 | MSMRRSKAEGKRSLRELSEEEEEEEETEDEDTFEEEEALEKKQKGKATSSSGVCQVESCTADMSKAKQYHKRHKVCQFHAKAPHVRISGLHQRFCQQCSRFHALSEFDEAKRSCRRRLAGHNERRRKSTTD | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Trans-acting factor that binds specifically to the consensus nucleotide sequence 5'-TNCGTACAA-3' of AP1 promoter. Binds specifically to the 5'-GTAC-3' core sequence. Promotes both vegetative phase change and flowering. Regulates phase-specific patterns of leaf epider... |
A2X0Q6 | MGSFGMDWNQKSSVLWDWENMPPIGNSANENPKNVMLAESKLAGVGVDIGHESGHSSGGTFSSSSEIGYGSSKSSISASIDSPSKVGNTIELNFASAEEHDKNMDKGKSKVDDTGTSRSPVVAANRVEPLIGLKLGKRTYFEDVCGGQNVKSSPSGVSVATPSPGLAKKVKVAQQNTQNPHCQVEGCNVDLSSAKPYHRKHRVCEPHSKTLKVIVAGLERRFCQQCSRFHGLAEFDQKKRSCRRRLHDHNARRRKPQPEAISLSSSRLSTLLYGDARQQASFLFGQAPYGQMGSCASSWDNPVPGGFKFTATKAPWSRPT... | Function: Trans-acting factor that binds specifically to the consensus nucleotide sequence 5'-TNCGTACAA-3' (By similarity). May be involved in panicle development.
Sequence Mass (Da): 50265
Sequence Length: 469
Domain: The SBP-type zinc finger is required for the binding to DNA.
Subcellular Location: Nucleus
|
Q9S7A9 | MEGKRSQGQGYMKKKSYLVEEDMETDTDEEEEVGRDRVRGSRGSINRGGSLRLCQVDRCTADMKEAKLYHRRHKVCEVHAKASSVFLSGLNQRFCQQCSRFHDLQEFDEAKRSCRRRLAGHNERRRKSSGESTYGEGSGRRGINGQVVMQNQERSRVEMTLPMPNSSFKRPQIR | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Trans-acting factor that binds specifically to the consensus nucleotide sequence 5'-TNCGTACAA-3' of AP1 promoter. Promotes both vegetative phase change and flowering.
Sequence Mass (Da): 20120
Sequence Length: 174
Domain: The SBP-type zinc finger is required for the ... |
Q6H509 | MDWMPPPKPTSPRSPPLLWDWADAAVPGSSSGEVSAAAAAAAAHPGRRRKEKRGRAEEGGGGGGEVRCQVEGCGVELVGVKDYHRKHRVCEAHSKFPRVVVAGQERRFCQQCSRFHALSEFDQKKRSCRRRLYDHNARRRKPQTDVFSYASARPPSSLLFDDNRQISFVWNKAPLSHVRPFAISPWESSSEVGTTDGHIYLDKSHISKSLPAFNTDIDELLPMKDFSAATIWMFFGVLFIRTAQESCMSFH | Function: Trans-acting factor that binds specifically to the consensus nucleotide sequence 5'-TNCGTACAA-3' (By similarity). May be involved in panicle development.
Sequence Mass (Da): 28158
Sequence Length: 251
Domain: The SBP-type zinc finger is required for the binding to DNA.
Subcellular Location: Nucleus
|
Q9S758 | MEGQRTQRRGYLKDKATVSNLVEEEMENGMDGEEEDGGDEDKRKKVMERVRGPSTDRVPSRLCQVDRCTVNLTEAKQYYRRHRVCEVHAKASAATVAGVRQRFCQQCSRFHELPEFDEAKRSCRRRLAGHNERRRKISGDSFGEGSGRRGFSGQLIQTQERNRVDRKLPMTNSSFKRPQIR | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Trans-acting factor that binds specifically to the consensus nucleotide sequence 5'-TNCGTACAA-3' of AP1 promoter. Promotes both vegetative phase change and flowering.
Sequence Mass (Da): 20992
Sequence Length: 181
Domain: The SBP-type zinc finger is required for the ... |
Q0E3F8 | MMSSRLNAGAMAVPAAAVAADVVDFGYAAPMPPPYVGFDPAGMGGERQLFQHGGACHGLYDGGLDFSAAAAFQEAATLGVGLPGGNLLQSLAPPAAAAATPSSLQMPMMMSLPGLPATAADVYPFGGGGFVKREDGPVLDVVGGGGGGRIGLNLGRRTYFSPADVLAVDRLLLRSRLGGMGMEMGMGMGVLGLGLAAAAHHHQPPRCQAEGCKADLSAAKHYHRRHKVCDFHAKAAAVLAAGKQQRFCQQCSRFHVLAEFDEAKRSCRKRLTEHNRRRRKPTAGGQSSKDSPPPPPSKKGTDASIASSYTSCDHHKAAAS... | Function: Trans-acting factor that binds specifically to the consensus nucleotide sequence 5'-TNCGTACAA-3'.
Sequence Mass (Da): 49132
Sequence Length: 468
Domain: The SBP-type zinc finger is required for the binding to DNA.
Subcellular Location: Nucleus
|
Q94JW8 | MDSWSYGRSVFMSNETLLPCDTFAKNRRFEQRLSNNDDVLISDMAGNSNGFSAVSITKVVPEEEDEENISSSSKFSSQELNRIDFKLRSFLDLGNDDDDTSSRGFALPSKKSRASNLCSQNPLCQVYGCSKDLSSSKDYHKRHRVCEAHSKTSVVIVNGLEQRFCQQCSRFHFLSEFDDGKRSCRRRLAGHNERRRKPAFYFLPGKRHKLLRTSQDVVGNKFLENSSLVLPESFPGSLLYRVIDEDDHRTSRLVSFKDEPTCSMFPTNEQNSSRTYESKPAIYSTEVSSIWDLHETAASRSTRALSLLSAQSQQHLSKFP... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Trans-acting factor that binds specifically to the consensus nucleotide sequence 5'-TNCGTACAA-3'.
Sequence Mass (Da): 45953
Sequence Length: 405
Domain: The SBP-type zinc finger is required for the binding to DNA.
Subcellular Location: Nucleus
|
Q75LH6 | MEAARVGAQSRHLYGGGLGEPDMDRRDKRLFGWDLNDWRWDSDRFVATPVPAAEASGLALNSSPSSSEEAGAASVRNVNARGDSDKRKRVVVIDDDDVEDDELVENGGGSLSLRIGGDAVAHGAGVGGGADEEDRNGKKIRVQGGSPSGPACQVEGCTADLTGVRDYHRRHKVCEMHAKATTAVVGNTVQRFCQQCSRFHPLQEFDEGKRSCRRRLAGHNRRRRKTRPEVAVGGSAFTEDKISSYLLLGLLGVCANLNADNAEHLRGQELISGLLRNLGAVAKSLDPKELCKLLEACQSMQDGSNAGTSETANALVNTAV... | Function: Trans-acting factor that binds specifically to the consensus nucleotide sequence 5'-TNCGTACAA-3'.
Sequence Mass (Da): 105604
Sequence Length: 969
Domain: The SBP-type zinc finger is required for the binding to DNA.
Subcellular Location: Nucleus
|
Q8S9G8 | MSSLSQSPPPPEMDIQPPALVNDDPSTYSSALWDWGDLLDFAADERLLVDQIHFPPVLSPPLPPLIPTQTPAESELDPSPEESGSGSDRVRKRDPRLICSNFIEGMLPCSCPELDQKLEDAELPKKKRVRGGSGVARCQVPDCEADISELKGYHKRHRVCLRCATASFVVLDGENKRYCQQCGKFHLLPDFDEGKRSCRRKLERHNNRRKRKPVDKGGVAAEQQQVLSQNDNSVIDVEDGKDITCSSDQRAEEEPSLIFEDRHITTQGSVPFTRSINADNFVSVTGSGEAQPDEGMNDTKFERSPSNGDNKSAYSTVCPT... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Transcription factor that participates in reprogramming global gene expression during copper deficiency in order to improve the metal uptake and prioritize its distribution to copper proteins of major importance (Probable). Binds directly to 5'-GTAC-3' motifs in the ... |
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