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O70492 | MAETVADTRRLITKPQNLNDAYGPPSNFLEIDVSNPQTVGVGRGRFTTYEIRVKTNLPIFKLKESTVRRRYSDFEWLRSELERESKVVVPPLPGKAFLRHVPFRGDDGIFDDNFIEERKQGLEQFINKVAGHPLAQNERCLHMFLQDEIIDKSYTPSKIRHA | Function: Phosphoinositide-binding protein required for multivesicular body formation. Specifically binds phosphatidylinositol 3-phosphate (PtdIns(P3)). Can also bind phosphatidylinositol 4-phosphate (PtdIns(P4)), phosphatidylinositol 5-phosphate (PtdIns(P5)) and phosphatidylinositol 3,5-biphosphate (PtdIns(3,5)P2) . Plays a role in protein transport between cellular compartments. Together with RAB7A facilitates endosome membrane association of the retromer cargo-selective subcomplex (CSC). May act in part as component of the SNX3-retromer complex which mediates the retrograde endosome-to-TGN transport of WLS distinct from the SNX-BAR retromer pathway (By similarity). Promotes stability and cell surface expression of epithelial sodium channel (ENAC) subunits SCNN1A and SCNN1G . Not involved in EGFR degradation. Involved in the regulation of phagocytosis in dendritic cells possibly by regulating EEA1 recruitment to the nascent phagosomes (By similarity). Involved in iron homeostasis through regulation of endocytic recycling of the transferrin receptor Tfrc presuambly by delivering the transferrin:transferrin receptor complex to recycling endosomes; the function may involve the CSC retromer subcomplex . Involved in regulation of neurite outgrowth in primary neurons .
PTM: Ubiquitinated, leading to its proteasomal degradation. Deubiquitinated by USP10.
Sequence Mass (Da): 18757
Sequence Length: 162
Domain: The PX domain mediates specific binding to phosphatidylinositol 3-phosphate (PtdIns(P3)).
Subcellular Location: Early endosome
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Q7SH92 | MQSLPDTRQQSFDEIYGPPENFLEIEVRNPRTHGIGRHMYTDYEIVCRTNIPAFKLRQSTVRRRYSDFEYFRDILERESARVTIPPLPGKVFTNRFSDDVIEGRRAGLEKFLKIVVGHPLLQTGSKVLAAFVQDPNWDRNAW | Function: Required for retention of late Golgi membrane proteins. Component of the retrieval machinery that functions by direct interaction with the cytosolic tails of certain TGN membrane proteins during the sorting/budding process at the prevacuolar compartment. Binds phosphatidylinositol 3-phosphate (PtdIns(P3)) (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 16642
Sequence Length: 142
Domain: The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization.
Subcellular Location: Cytoplasm
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O94291 | MDKLSRPEIRQQTTQQMYDVPENILEIDVINPQTHGIGRNMFTTYEIVCRTNMPYFRLHNSSVRRRYSEFEKFHDMLERESGRVSIPPLPGKIFTQRFRDDVIEERRQGLENFLRLVAGHPLIQTHSRVLSSFLQSPEFKPTP | Function: Required for retention of late Golgi membrane proteins. Component of the retrieval machinery that functions by direct interaction with the cytosolic tails of certain TGN membrane proteins during the sorting/budding process at the prevacuolar compartment. Binds phosphatidylinositol 3-phosphate (PtdIns(P3)) (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 16961
Sequence Length: 143
Domain: The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization.
Subcellular Location: Cytoplasm
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Q4P1V3 | MAFYSAGPLSPGYNSTSAWGGNDNAEEDPWAAPGSSSSAAPPTTSSGFAPSPPGGFASFSTQQQQQQQQQQQRQQAGYFGGAPAAGASLAQEADAYQDGLMETSFGVGSGAGQNRLGGAAATVNPQSPHNAHSSSSTYGSAISSTHSQPSTQSQQPQSHALPSSAAQAQAARAGAFPSGVSTSQYQPTSQGAQGASRFQSHTPSTLLPSEPAGFTSHTSSDYSATAPRQLAPGYPLPASNYTVPAYSPFARVDSLSTPRRETVEDMYGVPENFLEVEVRSPLTHGVGRKMYTDYEIVTRTNIPAFKLRYSSVRRRYSDFEYFRDILERESTRVNIPPLPGKVFTNRFTDEVIEARREGLERFLQVVAGHPLLQTGSKVMAAFLQDSGWSKDQWL | Function: Required for retention of late Golgi membrane proteins. Component of the retrieval machinery that functions by direct interaction with the cytosolic tails of certain TGN membrane proteins during the sorting/budding process at the prevacuolar compartment. Binds phosphatidylinositol 3-phosphate (PtdIns(P3)) (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 42068
Sequence Length: 394
Domain: The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization.
Subcellular Location: Cytoplasm
|
Q6C2S9 | MEASPKKPEALQRPDIKQQSFAEIYGVPENFLEIEVRSPQTHGIARKMYTDYEIVCRTNIPVFKLKSSVVRRRYSDFECFREILERESTRVSIPSLPGKVFTNRFSDEVIEARREGLEKFLQTVAGHPLLQTGSKVLCAFIQDPQWDKNQWI | Function: Required for retention of late Golgi membrane proteins. Component of the retrieval machinery that functions by direct interaction with the cytosolic tails of certain TGN membrane proteins during the sorting/budding process at the prevacuolar compartment. Binds phosphatidylinositol 3-phosphate (PtdIns(P3)) (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 17706
Sequence Length: 152
Domain: The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization.
Subcellular Location: Cytoplasm
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D4B5D4 | MIWKQPPRRMGEMGGSLSRRFGNAAASWAVWRVSRSCFSLLFFFYFFLFFSSSSLLPTTNNYQHLQLHSLIPTLNTTAHLPHQQASSASMKASLFLACSALGLALATPTQDAPETVNNPLGIVYQAKLPETSRTGIRGTINATAHSSGRGVVFNLDLWGFDNTEGPFRKLHTCFDQTNKQTNKIVKLTTTTAYHIHVDPVPTDGSCGPTKDHLDPFGRGQTPPCDDSLPQTCEPGDLSGKFGRLTTSSMEEHFNQTFHDLYTSTRPGLGTFFGNRSIVIHHRNSTRLTCANFTLVEQPGTSTTYVPRPTGTGIISSIFPTGTGAISTSGHAPTISATYTPTPTPSPPAQNNGAGRLVGFSLGAIMAALVPLAL | Cofactor: Binds 1 copper ion per subunit.
Function: Superoxide dismutases serve to convert damaging superoxide radicals, a key form of ROS, to less damaging hydrogen peroxide that can be converted into water by catalase action (By similarity). Degrades host-derived reactive oxygen species to escape innate immune surveillance (By similarity). Involved in the occurrence of miconazole-tolerant persisters in biofilms (By similarity). Persisters are cells that survive high doses of an antimicrobial agent. The unusual attributes of SOD5-like fungal proteins, including the absence of zinc and an open active site that readily captures extracellular copper, make these SODs well suited to meet challenges in zinc and copper availability at the host-pathogen interface (By similarity).
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer.
Location Topology: Lipid-anchor
Sequence Mass (Da): 40234
Sequence Length: 373
Subcellular Location: Secreted
EC: 1.15.1.1
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Q5AD07 | MKYLSIFLLATFALAGDAPISTDSKGSPSLIAKFEKTSKSNIEGTIKFTPANNGTVSVSVDLKGLPSDIGPFPYHVHEKPVPASKNCSATENHFNPYNGTVRAATPAAHEVGDLAGKHGNIMGESYKTEYDDSYISLNEKSRSYIGGLSIVIHANNGTRLNCANITLLDEGHGNANTTMSNSSSSSSQSAVNTSSSMASTAPQGNGAERAVVNGLLAAGVVGVIAALI | Cofactor: Binds 1 copper ion per subunit.
Function: Superoxide dismutases serve to convert damaging superoxide radicals, a key form of ROS, to less damaging hydrogen peroxide that can be converted into water by catalase action. Degrades host-derived reactive oxygen species to escape innate immune surveillance. Involved in the occurrence of miconazole-tolerant persisters in biofilms. Persisters are cells that survive high doses of an antimicrobial agent. The unusual attributes of SOD5-like fungal proteins, including the absence of zinc and an open active site that readily captures extracellular copper, make these SODs well suited to meet challenges in zinc and copper availability at the host-pathogen interface.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 23589
Sequence Length: 228
Subcellular Location: Secreted
EC: 1.15.1.1
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Q5ACV9 | MIFIPIIILIYLVSIAASDKSPKIKKNPRNVVAVADFPFGGDTQVKGNVVFSAKEGKHVNVHIDMTGLPKDEGPFFYHIHERSVPGNGNCEAVGLHFNPYNASPVCDEQKNDAYCQVGDLSGKHGCINTTCFELKYSDPYLSLNRKSKSYIIGKSVVFHYPNLTKIACADIEEANELRLQSLIDEYTQTDDAIQLKELNTPLETDYKFDEVEALSSEIYHSDTDSDPPQQELISTEKLYNKTDNVYSPEETRPSDQNKKSHRHSLLPLAKWKKNSPKNYSNISIHGISSDCLNDGMMVTGSVFGSLVLGIAAGIFV | Cofactor: Binds 1 copper ion per subunit.
Function: Superoxide dismutases serve to convert damaging superoxide radicals, a key form of ROS, to less damaging hydrogen peroxide that can be converted into water by catalase action. May be involved protection against extracellular stress.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 35110
Sequence Length: 316
Subcellular Location: Secreted
EC: 1.15.1.1
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P24704 | MAKGVAVLNSSEGVTGTIFFTQEGDGVTTVSGTVSGLKPGLHGFHVHALGDTTNGCMSTGPHFNPDGKTHGAPEDANRHAGDLGNITVGDDGTATFTITDCQIPLTGPNSIVGRAVVVHADPDDLGKGGHELSLATGNAGGRVACGIIGLQG | 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): 15098
Sequence Length: 152
Subcellular Location: Cytoplasm
EC: 1.15.1.1
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P80740 | MVKAVTVLNSSEGPHGIVYFAQEGDGPTTV | Cofactor: Binds 1 copper ion per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Probably involved in the protection against oxidative stress during pollen development.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 3104
Sequence Length: 30
Subcellular Location: Cytoplasm
EC: 1.15.1.1
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A2XGP6 | MVKAVVVLGSSEIVKGTIHFVQEGDGPTTVTGSVSGLKPGLHGFHIHALGDTTNGCMSTGPHYNPAGKEHGAPEDETRHAGDLGNVTAGEDGVANIHVVDSQIPLTGPNSIIGRAVVVHADPDDLGKGGHELSKTTGNAGGRVACGIIGLQG | 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): 15251
Sequence Length: 152
Subcellular Location: Cytoplasm
EC: 1.15.1.1
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E8XDJ8 | MKYTILSLVAGALISCSAMAENTLTVKMNDALSSGTGENIGEITVSETPYGLLFTPHLNGLTPGIHGFHVHTNPSCMPGMKDGKEVPALMAGGHLDPEKTGKHLGPYNDKGHLGDLPGLVVNADGTATYPLLAPRLKSLSELKGHSLMIHKGGDNYSDKPAPLGGGGARFACGVIEK | 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): 18370
Sequence Length: 177
Subcellular Location: Periplasm
EC: 1.15.1.1
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O66602 | MKKLSGVLAGSLLLISASFSQDLKAHAELINTEGEVIGKAELIETNSGVLIKLNAKGLPPNAELAFHIHERGECKPPTFKSAKGHFNPYGKKHGLLNPEGPHAGDMPNIYTDDKGNVRVQVLNPFVTLKKGEKNSLFKEGGTALVIHSGPDDYKSDPAGNAGKRIACGVIR | 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): 18231
Sequence Length: 171
EC: 1.15.1.1
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O78310 | MAATNTILAFSSPSRLLIPPSSNPSTLRSSFRGVSLNNNNLHRLQSVSFAVKAPSKALTVVSAAKKAVAVLKGTSDVEGVVTLTQDDSGPTTVNVRITGLTPGPHGFHLHEFGDTTNGCISTGPHFNPNNMTHGAPEDECRHAGDLGNINANADGVAETTIVDNQIPLTGPNSVVGRAFVVHELKDDLGKGGHELSLTTGNAGGRLACGVIGLTPL | Cofactor: Binds 1 copper ion per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Mediates tolerance to stress, including photo-oxidative stress.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 22244
Sequence Length: 216
Subcellular Location: Plastid
EC: 1.15.1.1
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P82902 | KAVAVLRGDSNVSGVVRFEQTHESEPTKIFIGQNSILALTVVVHAGTDDYGK | 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): 5555
Sequence Length: 52
Subcellular Location: Cytoplasm
EC: 1.15.1.1
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P24707 | QVEGVVTLSQEDNGPTTVKVRLTGLTPGKHGFHLHEFGDTTNGCMSTGSHFNPKKLTHGAPEDDVRHAGDLGNIVAGSDGVAEATIVDNQIPLSGPDSVIGRALVVHELEDDLGKGGHELSLTTGNAGGRLACGVVGLTPI | 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): 14435
Sequence Length: 141
Subcellular Location: Plastid
EC: 1.15.1.1
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P07505 | MAAHTILASAPSHTTFSLISPFSSTPTNALSSSLQSSSFNGLSFKLSPTTQSLSLSTSAASKPLTIVAATKKAVAVLKGTSNVEGVVTLTQEDDGPTTVNVRISGLAPGKHGFHLHEFGDTTNGCMSTGPHFNPDKKTHGAPEDEVRHAGDLGNIVANTDGVAEATIVDNQIPLTGPNSVVGRALVVHELEDDLGKGGHELSPTTGNAGGRLACGVVGLTPV | 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): 22567
Sequence Length: 222
Subcellular Location: Plastid
EC: 1.15.1.1
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O65175 | MACHSALAAVPSSRLHFYAPRPPLSTSVCPFQTALLGQPLRIYSSGASIAAAASPRSMVVVAATKKAVAVLKGTSQVDGVVTLVQEDDGPTTVNVRITGLTPGLHGFHLHEYGDTTNGCISTGSHFNPNKLTHGAPMDVVRHAGDLGNIVANVDGLAEATIVDDQIPLSGSNSVVGRAFVVHELEDDLGKGGHELSLTTGNAGGRLACGVVGLTPV | 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): 22075
Sequence Length: 216
Subcellular Location: Plastid
EC: 1.15.1.1
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P24702 | MKLTNLALAFTLFGASAVAFAHADHDHKKADNSSVEKLVVQVQQLDPVKGNKDVGTVEITESAYGLVFTPHLHGLAQGLHGFHIHQNPSCEPKEKDGKLVAGLGAGGHWDPKETKQHGYPWSDNAHLGDLPALFVEHDGSATNPVLAPRLKKLDEVKGHSLMIHEGGDNHSDHPAPLGGGGPRMACGVIK | 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): 20207
Sequence Length: 190
Subcellular Location: Periplasm
EC: 1.15.1.1
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Q12548 | NSSSVPLHGFHVHALGDTTNGCMSTGPHFNPTGKEHGAPQDENRHAGDLGNITAGADGVANVNVSDSQIPLTGAHSIIGRAVVVHADPDDLGKGGHELSKTTGNSNSSMDSCAHGIQGIL | 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): 12122
Sequence Length: 120
Subcellular Location: Cytoplasm
EC: 1.15.1.1
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P82205 | MPAKAVCVLRGDVSGTVFFDQQDEKSPVVVSGEVQGLTKGKHGFHVHEFGDNTNGCTSAGAHFNPEKQDHGGPSSAVRHVGDLGNIEAIEDSGVTKVSIQDSQISLHGPNSIIGRTLVVHADPDDLGLGGHELSKTTGNAGGRIACGVIGLAKI | 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): 15842
Sequence Length: 154
Subcellular Location: Cytoplasm
EC: 1.15.1.1
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Q7JR71 | MMQYLVVSLALCATICSAAQTRNMPIQAIAYLIGPVQSDNTQVKGNVTFTQNDCGQNVHVRVQLEGLKEGKHGFHIHEKGDLTNGCISMGAHYNPDKVDHGGPDHEVRHVGDLGNLEANSTGIIDVTYTDQVITLTGKLGIIGRGVVVHELEDDLGLGNHTDSKKTGNAGGRIACGVIGIK | Function: Protects the extracellular space from the toxic effects of reactive oxygen intermediates by converting superoxide radicals into hydrogen peroxide and oxygen.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 19221
Sequence Length: 181
Subcellular Location: Secreted
EC: 1.15.1.1
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P51547 | MTMLQQILLISVIIGTVHVHEVDCANEVLKARAYIFEAVKGGNPAKTVGIIDLVQTGTLVKMNGSVSGLQPGLHGFHIHEKGDLGNGCLAAGAHFNPHKMMHGAPEDSNRHVGDLGNIETPKTGDTPILISDSVISLTGQHNVIGRAIVIHADMDDLGRGTSELSKTTGNAGARVACGVIGIL | 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): 19078
Sequence Length: 183
Subcellular Location: Secreted
EC: 1.15.1.1
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P08294 | MLALLCSCLLLAAGASDAWTGEDSAEPNSDSAEWIRDMYAKVTEIWQEVMQRRDDDGALHAACQVQPSATLDAAQPRVTGVVLFRQLAPRAKLDAFFALEGFPTEPNSSSRAIHVHQFGDLSQGCESTGPHYNPLAVPHPQHPGDFGNFAVRDGSLWRYRAGLAASLAGPHSIVGRAVVVHAGEDDLGRGGNQASVENGNAGRRLACCVVGVCGPGLWERQAREHSERKKRRRESECKAA | Cofactor: Binds 1 copper ion per subunit.
Function: Protect the extracellular space from toxic effect of reactive oxygen intermediates by converting superoxide radicals into hydrogen peroxide and oxygen.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 25851
Sequence Length: 240
Subcellular Location: Secreted
EC: 1.15.1.1
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Q07449 | MINSFIVIFLSFLIFINYANLVCVEATHVYGRRSHSNGMHGNGARRAVAVLRGDAGVSGIIYFQQGSGGSITTISGSVSGLTPGLHGFHVHQYGDQTNGCTSAGDHYNPFGKTHGGPNDRIKHIGDLGNIVAGANGVAEVYINSYDIKLRGPLSVIGHSLVVHANTDDLGQGTGNMREESLKTGNAGSRLACGVIGIAAVS | Cofactor: Binds 1 copper ion per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems. May act in the parasite defense against phagocyte-generated reactive oxygen species.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 20904
Sequence Length: 201
Subcellular Location: Secreted
EC: 1.15.1.1
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Q08420 | MVAFLFCNLLLVACGSVTWTMSDTGESGVDLADRLDLVEKIGDTHSKDLEIWMELGKQREADAREMHAVCRVQPSAMLPPDQPQITGLVLFRQLGPSSRLEASFNLEGFPAEQNTSNHAIHVHEFGDLSQGCESTGPHYNPLGVPHPQHPGDFGNFVVRDGRLWKHRMGLATSLAGPHSILGRAVVVHAGEDDLGKGGNQASVQNGNAGRRLACCVVGTSNSEAWESQTKERKKRRRESECKTT | Cofactor: Binds 1 copper ion per subunit.
Function: Protect the extracellular space from toxic effect of reactive oxygen intermediates by converting superoxide radicals into hydrogen peroxide and oxygen.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 26620
Sequence Length: 244
Subcellular Location: Secreted
EC: 1.15.1.1
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P16026 | MTVYSYLVILFILLDNYCSAYGYGYSYYHRRHFDPAIASFTKEPYIGAVWFTQHGDYMYVNGSVAGLPPGKLLGTHVHRYGGLGNMCLEAGPHFNPFNQRHGPRHGYPRHAGDLGNIRVGRGGVAKFDFYVTIKGLGPFDGFIGRALVIHANRDDLGRNRDEGSRTTGNSGPRLACATIGFRAP | 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): 20346
Sequence Length: 184
Subcellular Location: Secreted
EC: 1.15.1.1
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P21276 | MAASSAVTANYVLKPPPFALDALEPHMSKQTLEFHWGKHHRAYVDNLKKQVLGTELEGKPLEHIIHSTYNNGDLLPAFNNAAQAWNHEFFWESMKPGGGGKPSGELLALLERDFTSYEKFYEEFNAAAATQFGAGWAWLAYSNEKLKVVKTPNAVNPLVLGSFPLLTIDVWEHAYYLDFQNRRPDYIKTFMTNLVSWEAVSARLEAAKAASA | Cofactor: Binds 1 Fe cation 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): 23791
Sequence Length: 212
Subcellular Location: Cell membrane
EC: 1.15.1.1
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Q5VRL3 | MAFATLVGVGGLSPALFSPSRPLSCSSSTSVSAPFILRAGGGGDARRHGLRRLVTPLRGSACRGESTNSRVLQCANEANVVTEDDIVNDGIDDETASDAEMDEDAEANGDESSGTDEDASVSWIEQQPLPYPSDALEPYISKETVEQHWGVHQNIHVERLNGMIGGSEWEGMSLGQMMLSSFNEGREAPHPPFFHAAQIWNHDFYWRSMQPGGGGKPPERLLKFINRDFGSYDGMIRQFMDAASTQFGSGWVWLCYKTSKLPHVKSRSPIPSDNYGRLVISKSPNAINPLVWGHSPLLAIDLWEHAYYLDYEDRRSDYVSTFLEKLVSWETVESRLKKAVQRAVERDEYVSTKHIRKQLLARAKSQIRAMPQQVNGDAREQTSGQEKSLGV | Cofactor: Binds 1 Fe cation 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): 43420
Sequence Length: 391
Subcellular Location: Plastid
EC: 1.15.1.1
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Q9LU64 | MMNVAVTATPSSLLYSPLLLPSQGPNRRMQWKRNGKRRLGTKVAVSGVITAGFELKPPPYPLDALEPHMSRETLDYHWGKHHKTYVENLNKQILGTDLDALSLEEVVLLSYNKGNMLPAFNNAAQAWNHEFFWESIQPGGGGKPTGELLRLIERDFGSFEEFLERFKSAAASNFGSGWTWLAYKANRLDVANAVNPLPKEEDKKLVIVKTPNAVNPLVWDYSPLLTIDTWEHAYYLDFENRRAEYINTFMEKLVSWETVSTRLESAIARAVQREQEGTETEDEENPDDEVPEVYLDSDIDVSEVD | Cofactor: Binds 1 Fe cation per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems (By similarity). Plays important role in chloroplast development, particularly in the maintenance of thylakoids membranes. Seems to act as a heterodimer with FSD3.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 34664
Sequence Length: 305
Subcellular Location: Plastid
EC: 1.15.1.1
|
Q5VSB7 | MAAFASALRVLPSPPAAVPRRLRSREQRQGCRSRRYSKVVAYYALTTPPYKLDALEPYISKRTVELHWGKHQQDYVDSLNKQLATSMFYGYTLEELIKEAYNNGNPLPEYNNAAQVWNHHFFWESMQPEGGGSPGRGVLQQIEKDFGSFTNFREEFIRSALSLLGSGWVWLVLKRKERKFSVVHTQNAISPLALGDIPLINLDLWEHAYYLDYKDDRRMYVTNFIDHLVSWDTVTLRMMRAEAFVNLGEPNIPVA | Cofactor: Binds 1 Fe cation 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): 29477
Sequence Length: 255
Subcellular Location: Plastid
EC: 1.15.1.1
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Q9FMX0 | MSSCVVTTSCFYTISDSSIRLKSPKLLNLSNQQRRRSLRSRGGLKVEAYYGLKTPPYPLDALEPYMSRRTLEVHWGKHHRGYVDNLNKQLGKDDRLYGYTMEELIKATYNNGNPLPEFNNAAQVYNHDFFWESMQPGGGDTPQKGVLEQIDKDFGSFTNFREKFTNAALTQFGSGWVWLVLKREERRLEVVKTSNAINPLVWDDIPIICVDVWEHSYYLDYKNDRAKYINTFLNHLVSWNAAMSRMARAEAFVNLGEPNIPIA | Cofactor: Binds 1 Fe cation per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems (By similarity). Plays important role in chloroplast development, particularly in the maintenance of thylakoids membranes. Seems to act as a heterodimer with FSD2.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 30360
Sequence Length: 263
Subcellular Location: Plastid
EC: 1.15.1.1
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Q9Y8H8 | MVSFKRYELPPLPYNYNALEPYIIEEIMKLHHQKHHNTYVKGANAALEKIEKHLKGEIQIDVRAVMRDFSFNYAGHIMHTIFWPNMAPPGKGGGTPGGRVADLIEKQFGGFEKFKALFSAAAKTVEGVGWGVLAFDPLTEELRILQVEKHNVLMTAGLVPILVIDVWEHAYYLQYKNDRGSYVENWWNVVNWDDVEKRLEQALNNAKPLYLLPQ | 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 ion at the active site.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 24577
Sequence Length: 214
EC: 1.15.1.1
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Q9X6W9 | MGVHKLEPKDHLKPQNLEGISNEQIEPHFEAHYKGYVAKYNEIQEKLADQNFADRSKANQNYSEYRELKVEETFNYMGVVLHELYFGMLTPGGKGEPSEALKKKIEEDIGGLDACTNELKAAAMAFRGWAILGLDIFSGRLVVNGLDAHNVYNLTGLIPLIVIDTYEHAYYVDYKNKRPPYIDAFFKNINWDVVNERFEKAMKAYEALKDFIK | Cofactor: Binds 1 Fe cation 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): 24475
Sequence Length: 213
EC: 1.15.1.1
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O15905 | MAFKLPALPYGMRELIPHISEETLSFHYGKHHAGYVNKLNSLIKGTPLESCTIEELILGQTGAVFNNAAQIWNHTFYWNSMGPNCGGEPTGPIRKKIEEKFGSFSAFKTDFSNLLAGHFGSGWGWLVLKDDGTADIVQTHDAGSPLKENLGRPLLCCDVWEHAYYIDYKNDRLSYINSWWNLVNWDFANKNLEAPFKWS | Cofactor: Binds 1 Fe cation 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): 22561
Sequence Length: 199
EC: 1.15.1.1
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P0C0I0 | MAIILPELPYAYDALEPQFDAETMTLHHDKHHATYVANTDAALEKHPEIGENLEELLADVPKIPEDIRQALINNGGGHLNHALFWELLSPEKQDVTPDVAQAIDDAFGSFDAFKEQFTAAATGRFGSGWAWLVVNKEGQLEITSTANQDTPISEGKKPILALDVWEHAYYLNYRNVRPNYIKAFFEIINWKKVSALYQAAK | 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): 22606
Sequence Length: 201
Subcellular Location: Secreted
EC: 1.15.1.1
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O33783 | YIDAETMTLHHDKHHATYVANANAALEKHPEIGEDLEALLADVEQIPADIRQALINNGGGHLNHALFWELLSPEKQEPTAEVAAAINEAFGSFEAFQEAFTAAATTRFGSGWAWLVVNDEGKLEVVSTANQDTPISDGKKPILAL | 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 ion at the active site.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 15700
Sequence Length: 145
EC: 1.15.1.1
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Q7SIC3 | AKFELPELPYAYDALEPTIDKETMNIHHTKHHNTYVTKLNGALEGHEDLKNKSLNDLISNLDAVPENIRTAVRNNGGGHANHSLFWKLMSPNGGGKPTGEVADKINDKYGSFEKFQEEFAAAAAGRFGSGWAWLVVNNGEIEIMSTPIQDNPLMEGKKPILGLDVWEHAYYLKYQNKRPDYISAFWNVVNWDEVAAQYSQAA | 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. Active only in homodimeric state.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 22661
Sequence Length: 202
Subcellular Location: Cytoplasm
EC: 1.15.1.1
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P00447 | MFAKTAAANLTKKGGLSLLSTTARRTKVTLPDLKWDFGALEPYISGQINELHYTKHHQTYVNGFNTAVDQFQELSDLLAKEPSPANARKMIAIQQNIKFHGGGFTNHCLFWENLAPESQGGGEPPTGALAKAIDEQFGSLDELIKLTNTKLAGVQGSGWAFIVKNLSNGGKLDVVQTYNQDTVTGPLVPLVAIDAWEHAYYLQYQNKKADYFKAIWNVVNWKEASRRFDAGKI | 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): 25774
Sequence Length: 233
Subcellular Location: Mitochondrion matrix
EC: 1.15.1.1
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P80735 | MLSRLFAPKVTVSAHCDLPCGVYDPAQARIEAESVKAVQEKMAGNDDPHFQTRATVIKEQRAELAKHHVSVLWSDYFKPPHFEKYPELHQLVNDTLKALSAAKGSKDPATGQKALDYIAQIDKIFWETKKA | Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 14703
Sequence Length: 131
Subcellular Location: Cytoplasm
EC: 1.15.1.1
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P80732 | HSDLPSGVYDPAQA | Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 1457
Sequence Length: 14
Subcellular Location: Cytoplasm
EC: 1.15.1.1
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P80734 | MLSRLFAPKVKVSAHCDLPCGVYDPAQARIEAESVKAIQEKMAANDDLHFQIRATVIKEQRAELAKHHLDVLWSDYFKPPHFESYPELHTLVNEAVKALSAAKASTDPATGQKALDYIAQIDKIFWETKKA | Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 14717
Sequence Length: 131
Subcellular Location: Cytoplasm
EC: 1.15.1.1
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D3RNN8 | MQDPASHSDSLVGRVEVKETTCYMCACRCGIRVHLRDGEVRYIDGNPNHPLNKGVICAKGSSGIMKQYSPGRLTQPLRRKAGAERGESAFEVISWDEAFAMLEERLAKLRAEDPKKFALFTGRDQMQALTGLFAKQYGTPNYAAHGGFCSVNMAAGLIYTIGGSFWEFGGPDLERAKLFVMIGTAEDHHSNPLKMAISEFKRRGGRFISVNPVRTGYSAVADEWVPIKPGTDGALLLAITREILDKGLFDRDFLVRYTNAAELVIDDPSRDDHGLFYRAEMHVEPDCFDPQNKLWWDRDIDGPISTHTPGADPRLMGRYVLPDGTPVKPSFQLLKERLEQYTPEWAAPITGIPADTIRRLAHEMGVMARDQKIELPIKWTDCWDDEHESVTGNPVAFHAMRGLAAHSNGFQTIRALGVLMTVLGTIDRPGGFRHKAPYPRPIPPCPKPPHGPEAVQPNTPLDGMPLGWPSKPEDLFVDAEGEAVRLDKAFSWEYPLSVHGLMHNVITNAWRGDPYPIDTLFLFMANMAWNSTMNTVEVRKMLVDKHPNGDYKIPFLVVCDTFASETVAFADLVLPDTSYLERHDVLSMLDRPISEFDGPVDSVRIPVLPPKGECKPFQEVLVELGSRLKLPAFTNADGSRKYRNYPDFIVNYETSPGSGIGFLAGWRGKGGDQFLKGEPNPHQWEMYAQNNCVYHHELPRSYQYMRNWNKGYLHWARAHGMIRYAEPITLHLYSEVLQRFRLAAQGKRPGRQPPERLRQRVETYFDPLPFYYEPLESRFTDTQRYPLNALTQRPMAMYHSWDSQNAWLRQIHSHNYLFLSPKVGLAQGFADGDWVWVESPHGKVRCMCRFSEAVEPGTVWTWNAIGKGAGAWGLAPNADEARKGFLLNHVIAEELPAHEAGEHLSNSDPVTGQAAWFDVRVRVYKAEAGEPEVTSPQFKPMPRLPGQEKKRGKWQAYVAGIFGKQAS | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Part of the SoeABC complex that catalyzes the oxidation of sulfite to sulfate.
Catalytic Activity: a quinone + H2O + sulfite = a quinol + sulfate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 108956
Sequence Length: 967
Subcellular Location: Cell inner membrane
EC: 1.8.5.6
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D3RNN7 | MTQLALVIDLNVCVGCHACVTSCKEWNTSGWAGPLVDQNPYEGSPTGTFFNRVQTFEIGTFPNTETVHFPKSCLHCEEPPCVPVCPTGASYKRPDNGVVLVDYDKCIGCKYCSWACPYGARELDAQQKVMKKCTLCIDRITDAKLSERDRKPSCVLACPANARLFGDVHDPDSEVSIAIRERGGYQLMPEWGTKPANHYLPRRKTRMHIDPEELTRVDNPWRKEDLTDYTGEETLDDVAW | Cofactor: Binds 3 [4Fe-4S] clusters.
Function: Part of the SoeABC complex that catalyzes the oxidation of sulfite to sulfate. SoeB is probably the electron transfer subunit.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 26995
Sequence Length: 240
Subcellular Location: Cell inner membrane
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D3RNN6 | MHPAFSVIFLTTLLGAGQGLYLAMVTGQLYAVARFLPAQADQFYAVGSLVALLLLIAGLGASFFHLGRPERAWRAAAMWRTSWLSREVIVLPIVMALVFAYGVAHWFEWTQPLFQVGAALQVDLTLLLGVLGTIASLALFVCTAMIYAAVRFLQEWHTPLTVSNFLFLGAASGFMLAAAYSAYIGNPLVTFYGTWAVILTLVGLASRLAHLRRNARLKHKSTVQTAIGVRHASVVQKAQGATGGSFNTREFFHGRSQSLLERLRTVYLVLVFPIPVLLIGLSYLIGSSNLPIIAFFVQFAGLLIERWSFFAEARHPQNLYYQSVA | Function: Part of the SoeABC complex that catalyzes the oxidation of sulfite to sulfate. SoeC probably anchors and stabilizes the catalytic subunits.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35715
Sequence Length: 325
Subcellular Location: Cell inner membrane
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Q8E9K5 | MEWQAEQAYNHLPPLPLDSKLAELAETLPILKACIPARAALAELKQAGELLPNQGLLINLLPLLEAQGSSEIENIVTTTDKLFQYAQEDSQADPMTKEALRYRTALYQGFTQLSNRPLCVTTALEICSTIKSVQMDVRKVPGTSLTNQATGEVIYTPPAGESVIRDLLSNWEAFLHNQDDVDPLIKMAMAHYQFEAIHPFIDGNGRTGRVLNILYLIDQQLLSAPILYLSRYIVAHKQDYYRLLLNVTTQQEWQPWIIFILNAVEQTAKWTTHKIAAARELIAHTTEYVRQQLPKIYSHELVQVIFEQPYCRIQNLVESGLAKRQTASVYLKQLCDIGVLEEVQSGKEKLFVHPKFVTLMTKDSNQFSRYAL | Function: Adenylyltransferase that mediates the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins.
Catalytic Activity: ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]
Sequence Mass (Da): 42225
Sequence Length: 372
EC: 2.7.7.108
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P39543 | MFSQIVLLLSAFIYVASATARRGTIKGRLDLAASNITGFVSTRTSFKLYQIGNFSTEYPYTSTTMFQDDEGNFEFANLPLNDGVNETTYYVMYPASMDFNLKPNRILIEFKNLENGTLQLNAFKNFFGREYFPSKDITYPEKLQSMKVHPYITVELLHKAPIRSYLQARNVSIFSTGIVGNILNSRWKLAGVITLIALVVFPIIVEKLDPETARAIREEAKRKQREKYAAVASK | Function: Involved in the export of PMA1, possibly through the monitoring or assisting of PMA1 folding and acquisition of competence to enter vesicles.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 26598
Sequence Length: 234
Subcellular Location: Endoplasmic reticulum membrane
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Q9S4P4 | MKISSGAINFSTIPNQVKKLITSIREHTKNGLASKITSVKNTHTSLNEKFKTGKDSPIEFALPQKIKDFFQPKDKNTLNKTLITVKNIKDTNNAGKKNISAEDVSKMNAAFMRKHIANQTCDYNYRMTGAAPLPGGVSVSANNRPTVSEGRTPPVSPSLSLQATSSPSSPADWAKKLTDAVLRQKAGETLTAADRDFSNADFRNITFSKILPPSFMERDGDIIKGFNFSNSKFTYSDISHLHFDECRFTYSTLSDVVCSNTKFSNSDMNEVVLQYSITTQQQPSFIHTTLKNTLIRHKANLSGVILNEPHNSSPPSVSGGGNFIRLGDIWLQMPLLWTENAVDGFLNHEHNNGKSILMTIDSLPDKYSQEKVQAMEDLVKSLRGGRLTEACIRPVESSLVSVLAHPPYTQSALIREWLGPVQERFFAHQCQTYNDVPLPTPDTYYQQRILPVLLDSFDRNSAAMTTHSGLFNQVILHCMTGVDCTDGTRQKAAALYEQYLAHPAVSPHIHNGLFGNYDGSSDWTTRAADNFLLLSSQDSDTAMMLSTDTLLTMLNPTPDTAWDNFYLQRAGENVSTAQISPVELFRHDFPVFLAAFNQQATQRRFGELIDIILSTEEHGELNQQFLAATNQKHSTVKLIDDASVSRLATIFDPLLPEGKLSPAHYQHILSAYHLTDATPQKQAETLFCLSTAFARYSSSAIFGTEHDSPPALRGYAEALMQKAWELSPAIFPTSEQFTDWSDRFHGLHGAFTCTCVVADSMQRHARKYFPSVLSSILPLSWA | Function: Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is an E3 ubiquitin ligase that interferes with host's ubiquitination pathway (By similarity). Required for inducing polymorphonuclear leukocytes migration across the intestinal epithelium.
PTM: Ubiquitinated in the presence of host E1 ubiquitin-activating enzyme, E2 ubiquitin-conjugating enzyme and ubiquitin.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 86885
Sequence Length: 782
Domain: Amino acids 100 to 347 are sufficient to target SopA to the mitochondria.
Subcellular Location: Secreted
EC: 2.3.2.26
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Q9AH19 | PAKEAYRLAAATFRDAQVKHLNSQPWQTIKNTLTHNGHQYTNMQLPAADMKIGTQDIFPSAYQGKGVCSWDTKNIHHANNLWMSTVSAHEDGKDKTLFCGIRHGVLSPYDVKDPLLRQTGAENEAKEVLTAALFSKPELLTRALEGEAVNLKLVSVGLLTASNVFGKEGTMVEDQMRAWQSLTQPGKMIHLKIRNKDGELQTVKIKPEIAAFNVGVNELALKLGFGLKTSDSYNVEALHQLLGNDLRPEAKPGGWVGDWLAQYPDNYEVVNILARQIKDIWKNNLHHKDGGEPYKLAQRLAMLANEIDAVPAWNCKSGKDRTGMMDSEIKREIICLHQTHTLNAPGSLPDRSGQEIFQKVLLNSGNLEIQKQNTGGAGNKVMKNLSPEVLNLSYQKRVGDENIWQSVKGISSLITS | Function: Converts phosphatidylinositol 3,4,5-trisphosphate (PtdIns 3,4,5-P3) to PtdIns 3-P and prevents the transition of PtdIns 3-P to PtdIns 3,5-P2. It is one of the known effectors injected by Salmonella into the host cell and is required for invasion and for an efficient generation and maintenance of Salmonella-containing vacuole (SVC). Alteration of the phosphoinositide composition of the plasma membrane causes membrane ruffling and actin cytoskeleton rearrangements. The persistence of PtdIns 3-P diverts the SCV from the endocytic pathway resulting in enlarged vesicles, which are essential to create a favorable environment where Salmonella can replicate and avoid immune defenses of the host cell (By similarity).
Sequence Mass (Da): 46118
Sequence Length: 416
Domain: Contains the consensus sequence Cys-X(5)-Arg characteristic of Mg-independent phosphatases.
Subcellular Location: Secreted
EC: 3.1.3.-
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P31122 | MTTNTVSRKVAWLRVVTLAVAAFIFNTTEFVPVGLLSDIAQSFHMQTAQVGIMLTIYAWVVALMSLPFMLMTSQVERRKLLICLFVVFIASHVLSFLSWSFTVLVISRIGVAFAHAIFWSITASLAIRMAPAGKRAQALSLIATGTALAMVLGLPLGRIVGQYFGWRMTFFAIGIGALITLLCLIKLLPLLPSEHSGSLKSLPLLFRRPALMSIYLLTVVVVTAHYTAYSYIEPFVQNIAGFSANFATALLLLLGGAGIIGSVIFGKLGNQYASALVSTAIALLLVCLALLLPAANSEIHLGVLSIFWGIAMMIIGLGMQVKVLALAPDATDVAMALFSGIFNIGIGAGALVGNQVSLHWSMSMIGYVGAVPAFAALIWSIIIFRRWPVTLEEQTQ | Function: Involved in the efflux of sugars. The physiological role may be the reduction of the intracellular concentration of toxic sugars or sugar metabolites. Transports L-arabinose and to a lesser extent IPTG. Seems to contribute to the control of the arabinose regulon.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42538
Sequence Length: 396
Subcellular Location: Cell inner membrane
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Q61473 | MSSPDAGYASDDQSQPRSAQPAVMAGLGPCPWAESLSPLGDVKVKGEVVASSGAPAGTSGRAKAESRIRRPMNAFMVWAKDERKRLAQQNPDLHNAELSKMLGKSWKALTLAEKRPFVEEAERLRVQHMQDHPNYKYRPRRRKQVKRMKRVEGGFLHALVEPQAGALGPEGGRVAMDGLGLPFPEPGYPAGPPLMSPHMGPHYRDCQGLGAPALDGYPLPTPDTSPLDGVEQDPAFFAAPLPGDCPAAGTYTYAPVSDYAVSVEPPAGPMRVGPDPSGPAMPGILAPPSALHLYYGAMGSPAASAGRGFHAQPQQPLQPQAPPPPPQQQHPAHGPGQPSPPPEALPCRDGTESNQPTELLGEVDRTEFEQYLPFVYKPEMGLPYQGHDCGVNLSDSHGAISSVVSDASSAVYYCNYPDI | Function: Acts as transcription regulator that binds target promoter DNA and bends the DNA . Binds to the sequences 5'-AACAAT-'3 or 5'-AACAAAG-3' . Modulates transcriptional regulation via WNT3A. Inhibits Wnt signaling. Promotes degradation of activated CTNNB1. Plays a key role in the regulation of embryonic development . Required for normal development of the definitive gut endoderm . Required for normal looping of the embryonic heart tube. Plays an important role in embryonic and postnatal vascular development, including development of arteries . Plays an important role in postnatal angiogenesis, where it is functionally redundant with SOX18 . Required for the generation and maintenance of fetal hematopoietic stem cells, and for fetal hematopoiesis . Probable transcriptional activator in the premeiotic germ cells.
Sequence Mass (Da): 44646
Sequence Length: 419
Domain: The 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.
Subcellular Location: Nucleus
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P35713 | MQRSPPGYGAQDDPPARRDCAWAPGHGAAADTRGLAAGPAALAAPAAPASPPSPQRSPPRSPEPGRYGLSPAGRGERQAADESRIRRPMNAFMVWAKDERKRLAQQNPDLHNAVLSKMLGKAWKELNAAEKRPFVEEAERLRVQHLRDHPNYKYRPRRKKQARKARRLEPGLLLPGLAPPQPPPEPFPAASGSARAFRELPPLGAEFDGLGLPTPERSPLDGLEPGEAAFFPPPAAPEDCALRPFRAPYAPTELSRDPGGCYGAPLAEALRTAPPAAPLAGLYYGTLGTPGPYPGPLSPPPEAPPLESAEPLGPAADLWADVDLTEFDQYLNCSRTRPDAPGLPYHVALAKLGPRAMSCPEESSLISALSDASSAVYYSACISG | Function: Transcriptional activator that binds to the consensus sequence 5'-AACAAAG-3' in the promoter of target genes and plays an essential role in embryonic cardiovascular development and lymphangiogenesis. Activates transcription of PROX1 and other genes coding for lymphatic endothelial markers. Plays an essential role in triggering the differentiation of lymph vessels, but is not required for the maintenance of differentiated lymphatic endothelial cells. Plays an important role in postnatal angiogenesis, where it is functionally redundant with SOX17. Interaction with MEF2C enhances transcriptional activation. Besides, required for normal hair development.
Sequence Mass (Da): 40891
Sequence Length: 384
Domain: Binds target DNA via the HMG box domain.
Subcellular Location: Nucleus
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P43680 | MQRSPPGYGAQDDPPSRRDCAWAPGIGAAAEARGLPVTNVSPTSPASPSSLPRSPPRSPESGRYGFGRGERQTADELRIRRPMNAFMVWAKDERKRLAQQNPDLHNAVLSKMLGKAWKELNTAEKRPFVEEAERLRVQHLRDHPNYKYRPRRKKQARKVRRLEPGLLLPGLVQPSAPPEAFAAASGSARSFRELPTLGAEFDGLGLPTPERSPLDGLEPGEASFFPPPLAPEDCALRAFRAPYAPELARDPSFCYGAPLAEALRTAPPAAPLAGLYYGTLGTPGPFPNPLSPPPESPSLEGTEQLEPTADLWADVDLTEFDQYLNCSRTRPDATTLPYHVALAKLGPRAMSCPEESSLISALSDASSAVYYSACISG | Function: Transcriptional activator that binds to the consensus sequence 5'-AACAAAG-3' in the promoter of target genes and plays an essential role in embryonic cardiovascular development and lymphangiogenesis . Activates transcription of PROX1 and other genes coding for lymphatic endothelial markers . Plays an essential role in triggering the differentiation of lymph vessels, but is not required for the maintenance of differentiated lymphatic endothelial cells . Plays an important role in postnatal angiogenesis, where it is functionally redundant with SOX17 . Interaction with MEF2C enhances transcriptional activation . Besides, required for normal hair development .
Sequence Mass (Da): 40898
Sequence Length: 377
Domain: Binds target DNA via the HMG box domain.
Subcellular Location: Nucleus
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Q6DGL6 | MYSMMMETDLHSPGPQTNTNPGQTGPNSGSKANQDRVKRPMNAFMVWSRGQRRKMAQENPKMHNSEISKRLGAEWKVMSEAEKRPFIDEAKRLRAMHMKEHPDYKYRPRRKTKTLLKKDKYSLAGGLLGGAGGGVGMSPAGVGQRLESPGGHGGSASAGYAHMNGWANGTYSGQVAAAAAAAAMMQEAQLAYSQHPGSGSHHHHAHHHHPHNPQPMHRYDMTALQYSPISNSQSYMSASPSGYGGISYTQHQNSSVATSAAIGTLSSLVKSEPNISPPVTTHSRGPCPGDLREMISMYLPTGESGDPSVQSRLHALPQHYQSTTAGVNGTVPLTHI | Function: Transcriptional activator.
Sequence Mass (Da): 36223
Sequence Length: 336
Domain: The 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.
Subcellular Location: Nucleus
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O57401 | MYSMMMETDLHSPGGAPAPGGGLSGQSGAGGGGGGGGGGGGKAGQDRVKRPMNAFMVWSRGQRRKMAQENPKMHNSEISKRLGAEWKVMSEAEKRPFIDEAKRLRALHMKEHPDYKYRPRRKTKTLLKKDKYSLAGGLLGAGPAAGGPPAVGVGMGVGVIPGGVGQRLESPGGAAGGGYAHMNGWANGAYPGSVAAAAAAAAMMQEAQLAYGQHPGGGGHPHHPHPHHPHHPHNPQPMHRYDMGALQYSPISNSQGYVSASPSGYGALPYGSQPHQNSAAAAAAAAAAAAASSGALGALGSLVKSEPSVSPPVTSHSRAPCPGDLREMISMYLPGGEGGDPAAAAAQSRLHSLPQHYQSASTGVNGTVPLTHI | Function: Transcriptional activator. May function as a switch in neuronal development. Keeps neural cells undifferentiated by counteracting the activity of proneural protein and suppresses neuronal differentiation.
Sequence Mass (Da): 37935
Sequence Length: 373
Domain: The 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.
Subcellular Location: Nucleus
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O00570 | MYSMMMETDLHSPGGAQAPTNLSGPAGAGGGGGGGGGGGGGGGAKANQDRVKRPMNAFMVWSRGQRRKMAQENPKMHNSEISKRLGAEWKVMSEAEKRPFIDEAKRLRALHMKEHPDYKYRPRRKTKTLLKKDKYSLAGGLLAAGAGGGGAAVAMGVGVGVGAAAVGQRLESPGGAAGGGYAHVNGWANGAYPGSVAAAAAAAAMMQEAQLAYGQHPGAGGAHPHAHPAHPHPHHPHAHPHNPQPMHRYDMGALQYSPISNSQGYMSASPSGYGGLPYGAAAAAAAAAGGAHQNSAVAAAAAAAAASSGALGALGSLVKSEPSGSPPAPAHSRAPCPGDLREMISMYLPAGEGGDPAAAAAAAAQSRLHSLPQHYQGAGAGVNGTVPLTHI | Function: Transcriptional activator. May function as a switch in neuronal development. Keeps neural cells undifferentiated by counteracting the activity of proneural proteins and suppresses neuronal differentiation (By similarity).
Sequence Mass (Da): 39023
Sequence Length: 391
Domain: The 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.
Subcellular Location: Nucleus
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P53783 | MYSMMMETDLHSPGGAQAPTNLSGPAGAGGGGGGGGGGGGGGGTKANQDRVKRPMNAFMVWSRGQRRKMAQENPKMHNSEISKRLGAEWKVMSEAEKRPFIDEAKRLRALHMKEHPDYKYRPRRKTKTLLKKDKYSLAGGLLAAGAGGGGAAVAMGVGVGVGAAAVGQRLESPGGAAGGGYAHVNGWANGAYPGSVAAAAAAAAMMQEAQLAYGQHPGAGGAHPHAHPAHPHPHHPHAHPHNPQPMHRYDMGALQYSPISNSQGYMSASPSGYGGIPYGAAAAAAAAAGGAHQNSAVAAAAAAAAASSGALGALGSLVKSEPSGSPPAPAHSRAPCPGDLREMISMYLPAGEGGDPAAAAAAAAQSRLHSLPQHYQGAGAGVNGTVPLTHI | Function: Transcriptional activator. May function as a switch in neuronal development. Keeps neural cells undifferentiated by counteracting the activity of proneural proteins and suppresses neuronal differentiation (By similarity).
Sequence Mass (Da): 39053
Sequence Length: 391
Domain: The 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.
Subcellular Location: Nucleus
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P48430 | MYNMMETELKPPAPQQTSGGGTGNSNSAANNQKNSPDRVKRPMNAFMVWSRGQRRKMAQENPKMHNSEISKRLGAEWKLLSEAEKRPFIDEAKRLRALHMKEHPDYKYRPRRKTKTLMKKDKYTLPGGLLAPGTNTMTTGVGVGATLGAGVNQRMDSYAHMNGWTNGGYGMMQEQLGYPQHPGLNAHNAAQMQPMHRYDVSALQYNSMTSSQTYMNGSPTYSMSYSQQGTPGMALGSMGSVVKTESSSSPPVVTSSSHSRAPCQAGDLRDMISMYLPGAEVPEPAAPSRLHMSQHYQSAPVPGTAINGTLPLSHM | Function: Transcriptional activator . Binds to the consensus DNA sequence 5'-TCATTGTTGTTG-3' . In cooperation with other transcription factors, binds to the promoter sequence of the crystallin gene to activate transcription in the lens . Downstream SRRT target that mediates the promotion of neural stem cell self-renewal (By similarity). Keeps neural cells undifferentiated by counteracting the activity of proneural proteins and suppresses neuronal differentiation . May function as a switch in neuronal development .
Sequence Mass (Da): 34511
Sequence Length: 315
Domain: The 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.
Subcellular Location: Nucleus
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P49785 | MLKKQTVWLLTMLSLVVVLSVYYIMSPESKNAVQMQSEKSASDSGEVATEKAPAKQDTKEKSGTETEKGKEDGTKGTKDSSADKETSAEASEKGTVVTETADDDLFTTYRLDLEDARSKEREELNAIVSSDDATAKEKSEAYDKMTALSEVEGTEKQLETLIKTQGYEDALVNAEGDKINITVKSDKHSKSKATAIIDLVAKEIKTMKDVAVTFEPSK | Function: Involved in forespore engulfment. Forms a channel with SpoIIIAH that is open on the forespore end and closed (or gated) on the mother cell end. This allows sigma-E-directed gene expression in the mother-cell compartment of the sporangium to trigger the activation of sigma-G forespore-specific gene expression by a pathway of intercellular signaling.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 23806
Sequence Length: 218
Subcellular Location: Cell membrane
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P21458 | MAKKKRKSRKKQAKQLNIKYELNGLLCIAISIIAILQLGVVGQTFIYLFRFFAGEWFILCLLGLLVLGVSLFWKKKTPSLLTRRKAGLYCIIASILLLSHVQLFKNLTHKGSIESASVVRNTWELFLMDMNGSSASPDLGGGMIGALLFAASHFLFASTGSQIMAIVMILIGMILVTGRSLQETLKKWMSPIGRFIKEQWLAFIDDMKSFKSNMQSSKKTKAPSKKQKPARKKQQMEPEPPDEEGDYETVSPLIHSEPIISSFSDRNEEEESPVIEKRAEPVSKPLQDIQPETGDQETVSAPPMTFTELENKDYEMPSLDLLADPKHTGQQADKKNIYENARKLERTFQSFGVKAKVTQVHLGPAVTKYEVYPDVGVKVSKIVNLSDDLALALAAKDIRIEAPIPGKSAIGIEVPNAEVAMVSLKEVLESKLNDRPDAKLLIGLGRNISGEAVLAELNKMPHLLVAGATGSGKSVCVNGIITSILMRAKPHEVKMMMIDPKMVELNVYNGIPHLLAPVVTDPKKASQALKKVVNEMERRYELFSHTGTRNIEGYNDYIKRANNEEGAKQPELPYIVVIVDELADLMMVASSDVEDSITRLSQMARAAGIHLIIATQRPSVDVITGVIKANIPSRIAFSVSSQTDSRTILDMGGAEKLLGRGDMLFLPVGANKPVRVQGAFLSDDEVEKVVDHVITQQKAQYQEEMIPEETTETHSEVTDELYDEAVELIVGMQTASVSMLQRRFRIGYTRAARLIDAMEERGVVGPYEGSKPREVLLSKEKYDELSS | Function: Plays an essential role during sporulation. Required for the translocation of the chromosomal DNA from mother cell into the forespore during polar septation, for the final steps of compartmentalization in the presence of trapped DNA, and for the final steps of engulfment. The N-terminus mediates localization to the division septum and is required for both septal membrane fusion and engulfment membrane fusion. May form DNA-conducting channels across the two lipid bilayers of the septum after cell division. The C-terminus functions as a DNA motor that exports DNA in an ATP-dependent manner from mother cell into the forespore. DNA-binding proteins are stripped off the chromosome during translocation, which may play a key role in reprogramming developmental gene expression in the forespore. The two arms of the chromosome are simultaneously pumped into the forespore, which suggests that the septum contains at least two channels, one for each arm. Required for separation of chromosome termini. Also required for optimal chromosome partitioning in vegetative cells, by actively moving chromosomal DNA trapped within the division septum into the daughter cells.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 87181
Sequence Length: 787
Domain: Consists of an N-terminal domain, followed by a linker domain, and a C-terminal domain, which forms the translocation motor involved in chromosome segregation. The C-terminal domain can be further subdivided into alpha, beta and gamma subdomains. Specific interactions between the gamma subdomain and specific SpoIIIE recognition sequences (SRS) regulate the compartment-specific activation of a mother-cell SpoIIIE complex. Interactions with nonpermissive SRS in the forespore lead to inactivation of the complex.
Subcellular Location: Cell membrane
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Q90WR8 | MTAPEQPVKQEEMAALDVDSSGHGEYLQHGNGNASASAAAAAPQDAQPSPLALLAATCSKIGPPSPEEDEAAAAAASHSAGATGDLASVQLAGTPNRWEVLSAAPATIKDEAGNIVQIPGAATVTSSGQYVLPIQSLQNQQIFSVAPGSDSSNGTVSNVQYQVIPQIQTADGQQVQLGFAASSDNSSINQETGQIQIIPGSNQTIIASGSPSANIQNILSQSGQVQVQGVAIGGSSFPGQAQVVANVPLGLPGNITFVPINSVDLDSLGLGSGSQTMTAGINADGHLINTGQAMDSSDNSERTGEQVSPEITETATDNDLFVPTSSSSQLPVTIDSSSILEQNANNLTTTSGQVHSSDLQGNYIQTSVSDDTQAQNIQVSTAQPIVQHIQLQESQQPTSQAQIVQGIAQQTIHGVQASQSISPQALQNLQLQLNPGTFLIQAQTVTPSGQITWQTFQVQGVQNLQNLQIQNAPGQQITLTPVQTLTLGQVAAGGALTSTPVSLSTAQLPNLQTVTVNSIDSAGIQLHQGENAGSPADIRIKEEEPDPEEWQLSGDSTLNTNDLTHLRVQVVDEEGDQPHQEGKRLRRVACTCPNCKEGGGRGSNLGKKKQHICHIPGCGKVYGKTSHLRAHLRWHSGERPFVCNWMFCGKRFTRSDELQRHRRTHTGEKKFVCPECSKRFMRSDHLAKHIKTHQNKKGIHSSSTVLASVEATSDDTLITAGGTTLILANIQQGSVSGIGTVNTSGTSNQDILTNTEIPLQLVTVSGNETME | Function: Transcriptional factor that can act as an activator or repressor depending on post-translational modifications. Binds to GT and GC boxes promoter elements. Competes with SP1 for the GC-box promoters. Weak activator of transcription (By similarity). Required for activation of SPARC transcription.
PTM: Acetylated by histone acetyltransferase p300, deacetylated by HDACs. Acetylation/deacetylation states regulate transcriptional activity. Acetylation appears to activate transcription. Alternate sumoylation and acetylation at Lys-541 also control transcriptional activity.
Sequence Mass (Da): 80950
Sequence Length: 771
Domain: The 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.
Subcellular Location: Nucleus
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Q02447 | MTAPEKPVKQEEMAALDVDSGGGGGGGGGHGEYLQQQQQHGNGAVAAAAAAQDTQPSPLALLAATCSKIGPPSPGDDEEEAAAAAGAPAAAGATGDLASAQLGGAPNRWEVLSATPTTIKDEAGNLVQIPSAATSSGQYVLPLQNLQNQQIFSVAPGSDSSNGTVSSVQYQVIPQIQSADGQQVQIGFTGSSDNGGINQESSQIQIIPGSNQTLLASGTPSANIQNLIPQTGQVQVQGVAIGGSSFPGQTQVVANVPLGLPGNITFVPINSVDLDSLGLSGSSQTMTAGINADGHLINTGQAMDSSDNSERTGERVSPDINETNTDTDLFVPTSSSSQLPVTIDSTGILQQNTNSLTTSSGQVHSSDLQGNYIQSPVSEETQAQNIQVSTAQPVVQHLQLQESQQPTSQAQIVQGITPQTIHGVQASGQNISQQALQNLQLQLNPGTFLIQAQTVTPSGQVTWQTFQVQGVQNLQNLQIQNTAAQQITLTPVQTLTLGQVAAGGAFTSTPVSLSTGQLPNLQTVTVNSIDSAGIQLHPGENADSPADIRIKEEEPDPEEWQLSGDSTLNTNDLTHLRVQVVDEEGDQQHQEGKRLRRVACTCPNCKEGGGRGTNLGKKKQHICHIPGCGKVYGKTSHLRAHLRWHSGERPFVCNWMYCGKRFTRSDELQRHRRTHTGEKKFVCPECSKRFMRSDHLAKHIKTHQNKKGIHSSSTVLASVEAARDDTLITAGGTTLILANIQQGSVSGIGTVNTSATSNQDILTNTEIPLQLVTVSGNETME | Function: Transcriptional factor that can act as an activator or repressor depending on isoform and/or post-translational modifications. Binds to GT and GC boxes promoter elements. Competes with SP1 for the GC-box promoters. Weak activator of transcription but can activate a number of genes involved in different processes such as cell-cycle regulation, hormone-induction and house-keeping.
PTM: Not glycosylated.
Sequence Mass (Da): 81925
Sequence Length: 781
Domain: The 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.
Subcellular Location: Nucleus
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O70494 | MTAPEKPVKQEEMAALDVDGGGGGGGHGEYLQQQQQQQQQHGNGAAAAAAQDTQPSPLALLAATCSKIGPPSPGDDDEEAAVAAAAGVPAAAAGATGDLASAQLGGAPNRWEVLSATPTTIKDEAGNLVQIPGAATSSGQYVLPLQNLQNQQIFSVAPGSDSSNGTVSNVQYQVIPQIQSTDAQQVQIGFTGSSDNGGINQENSQIQIIPGSNQTLLASGTPPANIQNLIPQTGQVQVQGVAIGGSSFPGQTQVVANVPLGLPGNITFVPINSVDLDSLGLSGSSQTMTAGINADGHLINTGQAMDSSDNSERTGERVSPDVNETNADTDLFVPTSSSSQLPVTIDSTGILQQNTNSLTTTSGQVHSSDLQGNYIQSPVSEETQAQNIQVSTAQPVVQHLQLQDSQQPTSQAQIVQGITPQTIHGVQASGQNISQQALQNLQLQLNPGTFLIQAQTVTPSGQITWQTFQVQGVQNLQNLQIQNTAAQQITLTPVQTLTLGQVAAGGALTSTPVSLSTGQLPNLQTVTVNSIDSTGIQLHPGENADSPADIRIKEEEPDPEEWQLSGDSTLNTNDLTHLRVQVVDEEGDQQHQEGKRLRRVACTCPNCKEGGGRGTNLGKKKQHICHIPGCGKVYGKTSHLRAHLRWHSGERPFICNWMFCGKRFTRSDELQRHRRTHTGEKKFVCPECSKRFMRSDHLAKHIKTHQNKKVIHSSSTVLASVEAGRDDALITAGGTTLILANIQQGSVSGIGTVNTSATSNQDILTNTEIPLQLVTVSGNETME | Function: Transcriptional factor that can act as an activator or repressor depending on isoform and/or post-translational modifications. Binds to GT and GC boxes promoter elements. Competes with SP1 for the GC-box promoters. Weak activator of transcription but can activate a number of genes involved in different processes such as cell-cycle regulation, hormone-induction and house-keeping (By similarity).
PTM: Acetylated by histone acetyltransferase p300, deacetylated by HDACs. Acetylation/deacetylation states regulate transcriptional activity. Acetylation appears to activate transcription. Alternate sumoylation and acetylation at Lys-553 also control transcriptional activity (By similarity).
Sequence Mass (Da): 82362
Sequence Length: 783
Domain: The 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.
Subcellular Location: Nucleus
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P35149 | MEKVDIFKDIAERTGGDIYLGVVGAVRTGKSTFIKKFMELVVLPNISNEADRARAQDELPQSAAGKTIMTTEPKFVPNQAMSVHVSDGLDVNIRLVDCVGYTVPGAKGYEDENGPRMINTPWYEEPIPFHEAAEIGTRKVIQEHSTIGVVITTDGTIGDIARSDYIEAEERVIEELKEVGKPFIMVINSVRPYHPETEAMRQDLSEKYDIPVLAMSVESMRESDVLSVLREALYEFPVLEVNVNLPSWVMVLKENHWLRESYQESVKETVKDIKRLRDVDRVVGQFSEFEFIESAGLAGIELGQGVAEIDLYAPDHLYDQILKEVVGVEIRGRDHLLELMQDFAHAKTEYDQVSDALKMVKQTGYGIAAPALADMSLDEPEIIRQGSRFGVRLKAVAPSIHMIKVDVESEFAPIIGTEKQSEELVRYLMQDFEDDPLSIWNSDIFGRSLSSIVREGIQAKLSLMPENARYKLKETLERIINEGSGGLIAIIL | Function: ATPase. Has a role at an early stage in the morphogenesis of the spore coat outer layers. Its ATP hydrolysis is required for proper assembly of the spore coat. Forms a basement layer around the outside surface of the forespore and self-assembles irreversibly into higher order structures by binding and hydrolyzing ATP thus creating a durable and stable platform upon which thereafter morphogenesis of the coat can take place. Required for proper localization of spore coat protein CotE and sporulation-specific proteins including SpoVM.
PTM: Seems to be cleaved by the YabG protease.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 55175
Sequence Length: 492
Domain: Extreme C-terminal region (AA 487-492) is required for its proper localization into a spherical shell around the developing forespore. N-terminus (AA 1-64) is functionally important although largely dispensable for proper localization.
Subcellular Location: Cytoplasm
EC: 3.6.1.-
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Q182W3 | MNNNIYEDISKRTQGDIYIGVVGPVRTGKSTFIRKFMEKLVIPNIDNEFKKDRTRDEIPQSGSGKTIMTVEPKFVPADGVEIKIKDTVSLKVRMVDCVGYIVEGALGHEEGGKQRLVSTPWSQEAMTFEKAAEIGTKKVIKDHSTIGIVVLTDGSVTGIDRKSYVEPEERVIQELKNLKKPFAVVLNTLSPKSEETSMLRSELEEKYEVPVLPMNVVEMEEEDIEEVMEAVLYDFPLTEIRINLPKWVEGLERNHWIKSSIITTLKQSIIDIGKIRDIEGIIQGFSELEFLEDTGVDNVELGEGVINIDLQTKQDLFYNVLEEKSGFKIEGDYQLLSLITRLSKVKNEYDKIESALIDAKIKGYGVVAPSLEELSLEEPEIMKQGKQYGIKLKANAPSLHIIKADISTEVSPIVGNQNQGEEMIKYLMEVFEEQPADLWESNMFGKSLHDLVKEQLQSKLYTMPEEIRVKMQKTLQKIVNEGSSNIITILL | Function: ATPase. Has a role at an early stage in the morphogenesis of the spore coat and is required for proper coat localization to the forespore.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 55517
Sequence Length: 491
Subcellular Location: Cytoplasm
EC: 3.6.1.-
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P17896 | MPDNIRKAVGLILLVSLLSVGLCKPLKEYLLIPTQMRVFETQTQAIETSLSVNAQTSESSEAFTVKKDPHEIKVTGKKSGESELVYDLAGFPIKKTKVHVLPDLKVIPGGQSIGVKLHSVGVLVVGFHQINTSEGKKSPGETAGIEAGDIIIEMNGQKIEKMNDVAPFIQKAGKTGESLDLLIKRDKQKIKTKLIPEKDEGEGKYRIGLYIRDSAAGIGTMTFYEPKTKKYGALGHVISDMDTKKPIVVENGEIVKSTVTSIEKGTGGNPGEKLARFSSERKTIGDINRNSPFGIFGTLHQPIQNNISDQALPVAFSTEVKKGPAEILTVIDDDKVEKFDIEIVSTTPQKFPATKGMVLKITDPRLLKETGGIVQGMSGSPIIQNGKVIGAVTHVFVNDPTSGYGVHIEWMLSEAGIDIYGKEKAS | Function: Plays a central role in the sigma-K checkpoint which coordinates gene expression during the later stages of spore formation. The protease is activated by trans cleavage of the zymogen precursor producing SpoIVB-45 kDa. This undergoes further trimming by cis cleavage to form SpoIVB-43 kDa and SpoIVB-42 kDa. The protease then cleaves the C-terminus of the SpoIVFA metalloprotease activating the latter.
Catalytic Activity: Self-cleaves 52-Val-|-Asn-53, 62-Ala-|-Phe-63 and 74-Val-|-Thr-75 at the N-terminus of SpoIVB.
Sequence Mass (Da): 46075
Sequence Length: 426
Subcellular Location: Forespore intermembrane space
EC: 3.4.21.116
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P26936 | MSHRADEIRKRLEKRRKQLSGSKRFSTQTVSEKQKPPSWVMVTDQEKHGTLPVYEDNMPTFNGKHPLVKTDSIILKCLLSACLVLVSAIAYKTNIGPVSQIKPAVAKTFETEFQFASASHWFETKFGNPLAFLAPEHKNKEQQIEVGKDLIAPASGKVQQDFQDNGEGIKVETSSDKIDSVKEGYVVEVSKDSQTGLTVKVQHADNTYSIYGELKDVDVALYDFVDKGKKLGSIKLDDHNKGVYYFAMKDGDKFIDPIQVISFE | Function: Implicated in the coupling of mother cell to forespore gene expression. Required for spore formation at 37 degrees Celsius, but not at 30 degrees Celsius. SpoIVFA plays a central role in both maintaining the SpoIVFA/BofA/SpoIVFB complex and anchoring it to the outer forespore membrane. SpoIVFA brings BofA into close proximity to SpoIVFB, allowing BofA to inhibit SpoIVFB. Increased accumulation of SpoIVFA seems to inhibit the activity of SpoIVFB and thus regulates the activation of sigma-K.
PTM: May be degraded by FtsH. It is stabilized by an ftsH disruption mutant, and in a probably independent fashion, by overexpression of BofA.
Sequence Mass (Da): 29607
Sequence Length: 264
Subcellular Location: Forespore outer membrane
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P26937 | MNKWLDLILKIHVHPFLWIIAALGLLTGHMKALLCLLLIVLIHELGHAALAVFFSWRIKRVFLLPFGGTVEVEEHGNRPLKEEFAVIIAGPLQHIWLQFAAWMLAEVSVIHQHTFELFTFYNLSILFVNLLPIWPLDGGKLLFLLFSKQLPFQKAHRLNLKTSLCFCLLLGCWVLFVIPLQISAWVLFVFLAVSLFEEYRQRHYIHVRFLLERYYGKNRELEKLLPLTVKAEDKVYHVMAEFKRGCKHPIIIEKSGQKLSQLDENEVLHAYFADKRTNSSMEELLLPY | Cofactor: Binds 1 zinc ion per subunit.
Function: Implicated in the coupling of mother cell to forespore gene expression. Required for spore formation. Processes the pro-sigma K factor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33640
Sequence Length: 288
Subcellular Location: Forespore outer membrane
EC: 3.4.24.-
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P0CH88 | VVGGKPAKLGAWPWMVALGF | PTM: Contains 3 disulfide bonds.
Sequence Mass (Da): 2085
Sequence Length: 20
Subcellular Location: Secreted
EC: 3.4.21.-
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Q02446 | MSDQKKEEEEEAAAAAAMATEGGKTSEPENNNKKPKTSGSQDSQPSPLALLAATCSKIGTPGENQATGQQQIIIDPSQGLVQLQNQPQQLELVTTQLAGNAWQLVASTPPASKENNVSQPASSSSSSSSSNNGSASPTKTKSGNSSTPGQFQVIQVQNPSGSVQYQVIPQLQTVEGQQIQINPTSSSSLQDLQGQIQLISAGNNQAILTAANRTASGNILAQNLANQTVPVQIRPGVSIPLQLQTLPGTQAQVVTTLPINIGGVTLALPVINNVAAGGGTGQVGQPAATADSGTSNGNQLVSTPTNTTTSASTMPESPSSSTTCTTTASTSLTSSDTLVSSADTGQYASTSASSSERTIEESQTPAATESEAQSSSQLQPNGMQNAQDQSNSLQQVQIVGQPILQQIQIQQPQQQIIQAIPPQSFQLQSGQTIQTIQQQPLQNVQLQAVNPTQVLIRAPTLTPSGQISWQTVQVQNIQSLSNLQVQNAGLSQQLTITPVSSSGGTTLAQIAPVAVAGAPITLNTAQLASVPNLQTVSVANLGAAGVQVQGVPVTITSVAGQQQGQDGVKVQQATIAPVTVAVGGIANATIGAVSPDQLTQVHLQQGQQTSDQEVQPGKRLRRVACSCPNCREGEGRGSNEPGKKKQHICHIEGCGKVYGKTSHLRAHLRWHTGERPFICNWMFCGKRFTRSDELQRHRRTHTGEKRFECPECSKRFMRSDHLSKHVKTHQNKKGGGTALAIVTSGELDSSVTEVLGSPRIVTVAAISQDSNPATPNVSTNMEEF | Function: Binds to GT and GC boxes promoters elements. Probable transcriptional activator.
Sequence Mass (Da): 81985
Sequence Length: 784
Domain: The 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors. In SP4, the motif is inactive.
Subcellular Location: Nucleus
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Q298L4 | MVRTKNQSSSSSASSSSHKSPIKSHGGSGSAAAGTAGHPVSRSSSSHRTSIDDRKSATNVSSSSNRRTTPGSSPDGDGDDDTTTTDDLTPTSTSAPRSAGGPSSVHKQNLYVVSFPIIFLFNVLRSLIYQLFCIFRYLYGASTKVIYRPHRRDCNIEIVVQNNSNNKDQKHQQLTSSQSLNYPLEVTSGEAASEQQVQQPLPQQRYRALQPLEMAGANRSGSGYSPGPGDPLLAKQKHHHRRAFEYISKALKIDEENEGHKELAIELYRKGIKELEDGIAVDCWSGRGDVWDRAQRLHDKMQTNLSMARDRLHFLALREEDFQMHRLSLKEEQKPNPSREQHQKPQKAREAADKPMLTNLTNDPVKLKTRSSGYGPKNGLTTPRISATATTPTSSSSLASGRKLTIGTKRPGNLAVAANKSQTLPRNLGSKTSVGAVRQPGKTAATPPAVRRQFSSGRNTPPQRSRTPINNNGASGSGSGASTPVVTVKGVEQKLVQLILDEIVEGGAKVEWTDIAGQEVAKQALQEMVILPSVRPELFTGLRAPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKLVRALFAVARHLQPSIIFIDEVDSLLSERSSGEHEASRRLKTEFLVEFDGLPGNPDGDRIVVLAATNRPQELDEAALRRFTKRVYVSLPDEQTRELLLNRLLQKQGSPLDTDALRRLSKITDGYSGSDLTALAKDAALEPIRELNVEQVKCLDINAMRHITEKDFHNSLKRIRRSVAQQSLSSYEKWSSDYGDITI | Function: ATP-dependent microtubule severing protein. Stimulates microtubule minus-end depolymerization and poleward microtubule flux in the mitotic spindle. Regulates microtubule stability in the neuromuscular junction synapse. Involved in lipid metabolism by regulating the size and distribution of lipid droplets. Involved in axon regeneration by regulating microtubule severing.
Catalytic Activity: n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 86084
Sequence Length: 788
Subcellular Location: Membrane
EC: 5.6.1.1
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Q9UBP0 | MNSPGGRGKKKGSGGASNPVPPRPPPPCLAPAPPAAGPAPPPESPHKRNLYYFSYPLFVGFALLRLVAFHLGLLFVWLCQRFSRALMAAKRSSGAAPAPASASAPAPVPGGEAERVRVFHKQAFEYISIALRIDEDEKAGQKEQAVEWYKKGIEELEKGIAVIVTGQGEQCERARRLQAKMMTNLVMAKDRLQLLEKMQPVLPFSKSQTDVYNDSTNLACRNGHLQSESGAVPKRKDPLTHTSNSLPRSKTVMKTGSAGLSGHHRAPSYSGLSMVSGVKQGSGPAPTTHKGTPKTNRTNKPSTPTTATRKKKDLKNFRNVDSNLANLIMNEIVDNGTAVKFDDIAGQDLAKQALQEIVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGDDRVLVMGATNRPQELDEAVLRRFIKRVYVSLPNEETRLLLLKNLLCKQGSPLTQKELAQLARMTDGYSGSDLTALAKDAALGPIRELKPEQVKNMSASEMRNIRLSDFTESLKKIKRSVSPQTLEAYIRWNKDFGDTTV | Function: ATP-dependent microtubule severing protein that specifically recognizes and cuts microtubules that are polyglutamylated . Preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold . Severing activity is not dependent on tubulin acetylation or detyrosination . Microtubule severing promotes reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. It is critical for the biogenesis and maintenance of complex microtubule arrays in axons, spindles and cilia. SPAST is involved in abscission step of cytokinesis and nuclear envelope reassembly during anaphase in cooperation with the ESCRT-III complex . Recruited at the midbody, probably by IST1, and participates in membrane fission during abscission together with the ESCRT-III complex . Recruited to the nuclear membrane by IST1 and mediates microtubule severing, promoting nuclear envelope sealing and mitotic spindle disassembly during late anaphase . Required for membrane traffic from the endoplasmic reticulum (ER) to the Golgi and endosome recycling . Recruited by IST1 to endosomes and regulates early endosomal tubulation and recycling by mediating microtubule severing . Probably plays a role in axon growth and the formation of axonal branches .
Catalytic Activity: n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 67197
Sequence Length: 616
Subcellular Location: Membrane
EC: 5.6.1.1
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B7PXE3 | MASTVALLRDSSDDRENFDDGETDCVQVGRKRKLTVFFYPLLLVFWLLRWVFYQFFLVLCFVCRGFVPRRHLATAETTTTMATAEEPDANLLIRQKQHHKKAFDFISKALKYDEENEDFKEMSIDLYRKGIEELQKGIAIDFSKGQGTTWERAHRLSDKMKVNLEMARDRLDFLESMVKIEHLGDHLPWHGGVAPAQRGQRRRAWQKAAPSAPSEPGTGPSWLKMAENGPAKGGPCPTSPRLQRSNTGVTLRRQQQQQLGGVSTVSRSQTLPRNSVPCPRMSARSPSRKAGNNEAVPTPNTARRRASQPQVPPVHPRGRQPTTRGGAAHRGGPPTVSQRSLLSSRVPPLKGVDSRLAHLILDEVVDGAPPVLFSDIAGQEVAKQALSEMVILPTDRPELFTGLRAPPKGLLLFGPPGNGKTMLAKAVAHESNSTFLNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLSERKDNEHEATRRLKTEFLVEFDGLHTGSEERVLVMGATNRPQELDDAALRRFTKRVYVTLPDHNTRVILLEKLLKKHNNPLSADKLKYLARLTEGYSGSDLTALAKDAALGPIRELNPEQVRCVDPKKMRNISLQDFLDSLKKVRRSVTPQSLDFFDRWNREFGDITV | Function: ATP-dependent microtubule severing protein. Microtubule severing may promote reorganization of cellular microtubule arrays and the release of microtubules from the microtubule organizing center following nucleation.
Catalytic Activity: n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 72474
Sequence Length: 648
Subcellular Location: Membrane
EC: 5.6.1.1
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A7T395 | MPNNDILRPLAIPAKYVGSFLVFLYNGLYFVFVVNLWSRLFGKATKTEVPPLPKIRKLGKDMASRAPPRRGQSSEDNEDGLPAEIFNVRRHHKQAYAYIARALEVDEGQGSLETKKRAVEFYNRGIEEMEAGLLIPCIDEGEEWDKARRLQEKMEANLENTRERMDELVIIFFIIVVALLVSAGMMDDQPLLSARKTSSEPSQAWDVSKPTGPSYKQSKSYKNSTTVTTKRSQASPSFSSSSSSVNSTAGSSRTKPAKPAPMAAPRRYNPQVRRTKSTKPAMMAKQSCVDEQKKKISHLKGIDPKLANIIMDEILESGPAVHFSDIAGVDNAKKALQEIVILPSLRPELWRGDPTLVLFQVLPYPPGSSHITLPRASTATSFTSCFFSISKRSSLVHPVVASFFVKSLEDLASILTTSLFTIDEVDSLLTERREGEHEHSRRLKTEFLVSFDGVVADPEERILVMGATNRPQELDDAALRRMVKRIHIPLPDKETRKVLLTKLLAKHHNPLSGAEIDRLARMTEHYSGSDLTALARDAALGPIRDLNSDQLKSMAANEVRNITFQDFVNSLQIIRPSVGPETLKAYDDWNRLYGSNA | Function: ATP-dependent microtubule severing protein. Microtubule severing may promote reorganization of cellular microtubule arrays and the release of microtubules from the microtubule organizing center following nucleation.
Catalytic Activity: n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 66629
Sequence Length: 597
Subcellular Location: Membrane
EC: 5.6.1.1
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B2RYN7 | MSSPAGRRKKKGSGGASPAPARPPPPAAVPAPAAGPAPAPGSPHKRNLYYFSYPLVVGFALLRLLACHLGLLFVWLCQRFSRALMAAKRSSGTAPAPASPSTPAPGPGGEAESVRVFHKQAFEYISIALRIDEEEKGQKEQAVEWYKKGIEELEKGIAVIVTGQGEQYERARRLQAKMMTNLVMAKDRLQLLESGAVPKKKDPLTHASNSLPRSKTVMKSGSTGLSGHHRAPSCSGLSMVSGARPGSGPAATTHKGTSKPNRTNKPSTPTTAVRKKKDLKNFRNVDSNLANLIMNEIVDNGTAVKFDDIAGQELAKQALQEIVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGDDRVLVMGATNRPQELDEAVLRRFIKRVYVSLPNEETRLLLLKNLLCKQGSPLTQKELAQLARMTDGYSGSDLTALAKDAALGPIRELKPEQVKNMSASEMRNIRLSDFTESLKKIKRSVSPQTLEAYIRWNKDFGDTTV | Function: ATP-dependent microtubule severing protein that specifically recognizes and cuts microtubules that are polyglutamylated. Preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold. Severing activity is not dependent on tubulin acetylation or detyrosination. Microtubule severing promotes reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. It is critical for the biogenesis and maintenance of complex microtubule arrays in axons, spindles and cilia. SPAST is involved in abscission step of cytokinesis and nuclear envelope reassembly during anaphase in cooperation with the ESCRT-III complex. Recruited at the midbody, probably by IST1, and participates in membrane fission during abscission together with the ESCRT-III complex. Recruited to the nuclear membrane by IST1 and mediates microtubule severing, promoting nuclear envelope sealing and mitotic spindle disassembly during late anaphase. Required for membrane traffic from the endoplasmic reticulum (ER) to the Golgi and endosome recycling. Recruited by IST1 to endosomes and regulates early endosomal tubulation and recycling by mediating microtubule severing (By similarity). Probably plays a role in axon growth and the formation of axonal branches .
Catalytic Activity: n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 63022
Sequence Length: 581
Subcellular Location: Membrane
EC: 5.6.1.1
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P40702 | MSSNKTEKPTKKRLEDSAKKGQSFKSKDLIIACLTLGGIAYLVSYGSFNEFMGIIKIIIADNFDQSMADYSLAVFGIGLKYLIPFMLLCLVCSALPALLQAGFVLATEALKPNLSALNPVEGAKKLFSMRTVKDTVKTLLYLSSFVVAAIICWKKYKVEIFSQLNGNIVGIAVIWRELLLALVLTCLACALIVLLLDAIAEYFLTMKDMKMDKEEVKREMKEQEGNPEVKSKRREVHMEILSEQVKSDIENSRLIVANPTHITIGIYFKPELMPIPMISVYETNQRALAVRAYAEKVGVPVIVDIKLARSLFKTHRRYDLVSLEEIDEVLRLLVWLEEVENAGKDVIQPQENEVRH | Function: Involved in a secretory pathway responsible for the surface presentation of determinants needed for the entry of Salmonella species into mammalian cells.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40093
Sequence Length: 356
Subcellular Location: Cell inner membrane
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P0A1M8 | MANKTEKPTPKKLKDAAKKGQSFKFKDLTTVVIILVGTFTIISFFSLSDVMLLYRYVIINDFEINEGKYFFAVVIVFFKIIGFPLFFCVLSAVLPTLVQTKFVLATKAIKIDFSVLNPVKGLKKIFSIKTIKEFFKSILLLIILALTTYFFWINDRKIIFSQVFSSVDGLYLIWGRLFKDIILFFLAFSILVIILDFVIEFILYMKDMMMDKQEIKREYIEQEGHFETKSRRRELHIEILSEQTKSDIRNSKLVVMNPTHIAIGIYFNPEIAPAPFISLIETNQCALAVRKYANEVGIPTVRDVKLARKLYKTHTKYSFVDFEHLDEVLRLIVWLEQVENTH | Function: Required for surface presentation of invasion plasmid antigens. Could play a role in preserving the translocation competence of the ipa antigens. Required for invasion and for secretion of the three ipa proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39852
Sequence Length: 342
Subcellular Location: Cell inner membrane
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Q5MJ68 | MLWAIPELGSPCPISISYEMSDSQDPTTSPVVTTQVELGGCSRQGGGNGFLRFRQHQEVQAFLSLLEDSFVQEFLSKDPCFQISDKYLLAMVLVYFQRAHLKLSEYTHSSLFLALYLANDMEEDLEGPKCEIFPWALGKDWCLRVGKFLHQRDKLWARMGFRAVVSRQCCEEVMAKEPFHWAWTRDRRPHHGGVQRVCPQVPVRLPRGPGLSPPHCSPCGLPQHCSSHLLKPVSSKCPSLTSECHRPPSQNYLSRVKNAWGGDFLIVLPPQMQLEPGTYSLRIFPKPPARPGH | Function: Promotes progression through the cell cycle via binding and activation of CDK1 and CDK2. Involved in the spindle-assembly checkpoint. Required for recruitment of MAD2L1, BUBR1 and BUB1 to kinetochores. Required for the correct localization of the active form of Aurora B in prometaphase.
Sequence Mass (Da): 33166
Sequence Length: 293
Domain: The C-terminus is required for CDK2-activation, but not CDK2-binding.
Subcellular Location: Cytoplasm
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P49726 | MPLVVRFPDVLKNRLETLQSAFDMAINSQGYEAHYQGVYPVKCNQDRFVVEDIVKFGSPYRFGLEAGSKPELLLAMNCLSKGSADALLVCNGFKDTEYISLALVARKLLLNSVIVLEQEEELDLVIDISRKMSVRPVIGLRAKLRTKHSGHFGSTSGEKGKFGLTTTQILRVVKKLDESGMLDCLQLLHFHIGSQIPTTELLADGVGEATQIYSELVRLGAGMKFIDIGGGLGIDYDGSKSSNSDVSVCYSIEEYASAVVQAVLYVCDRKGGKHPVICSESGRAIVSHHSILIFEAVSASTSHVSTQPSSGGLQSLVETLNEDARADYRNLSAAAVRGEYDTCLIYSDQLKQRCVEQFKDGSLDIEQLAAVDSICDWVSKAIGVADPVRTYHVNLSVFTSIPDFWGFSQLFPIVPIHRLDEKPTMRGILSDLTCDSDGKVDKFIGGESSLPLHEIGSGDGGRYYLGMFLGGAYEEALGGLHNLFGGPSVVRVMQSDSPHSFA | Catalytic Activity: H(+) + L-arginine = agmatine + CO2
Sequence Mass (Da): 54581
Sequence Length: 502
Pathway: Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1.
EC: 4.1.1.19
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O23141 | MPALACVDTSFVPPAYAFSDTAGDVFIPASSPTSAAVVVDRWSPSLSSSLYRIDGWGAPYFIANSSGNISVRPHGSETLPHQDIDLLKIVKKVTGPKSSGGLGLQLPLIVRFPDVLKNRLECLQSAFDYAIKSQGYDSHYQGVYPVKCNQDRFVVEDIVKFGSSFRFGLEAGSKPEILLAMSCLCKGSPDAFLVCNGFKDAEYISLALLGRKLALNTVIVLEQEEELDLVIELSQKMNVRPVIGLRAKLRTKHSGHFGSTSGEKGKFGLTTTQIVRVVRKLRQSGMLDCLQLLHFHIGSQIPSTSLLSDGVAEAAQLYCELVRLGAHMKVIDIGGGLGIDYDGSKSGESDLSVAYSLEEYAEAVVASVRVVCDRSSVKHPVICSESGRAIVSHHSVLIFEAVSADKPMVHQATPGDIQFLLEGNEEARANYEDLYAAVMRGDHESCLLYVDQLKQRCVEGFKEGVLSIEQLASVDGLCEWVLKAIGASDPVHTYNINLSVFTSIPDLWGIDQLFPIVPIHKLDQRPGARGILSDLTCDSDGKINKFIGGESSLPLHELDKNGSGGRYFLGMFLGGAYEEALGGVHNLFGGPSVVRVSQSDGPHSFAVTRAVPGQSSADVLRAMQHEPELMFQTLKHRAEEMMHTKGGSEGENEEEEEDDEFNNVAASLDRSFHNMPYLATEQASPSNSLSAAISNLGFYYCDEDVYDYISA | Function: Required for the biosynthesis of putrescine. Catalyzes the first step of polyamine (PA) biosynthesis to produce putrescine from arginine . Is a major contributor to basal arginine decarboxylase (ADC) activity and putrescine biosynthesis . Accumulation of putrescine plays a positive role in salt stress tolerance . Accumulation of putrescine plays a positive role in freezing tolerance . Production of PA is essential for normal seed development . Controls PA homeostasis which is crucial for normal plant growth and development .
Catalytic Activity: H(+) + L-arginine = agmatine + CO2
Sequence Mass (Da): 77219
Sequence Length: 711
Pathway: Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1.
Subcellular Location: Plastid
EC: 4.1.1.19
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O81160 | YQGVYPVKSNQDRFVVEDIVKFGSSFRFGLEAGSKPELLLAMSCLCKGNPEALLVCNGFKDAEYISLALLARKLALKHVIVLEQEEEVDMVIDISQKLSVRPVIGVRAKLRTKHSGHFGSTSGEKGKFGLTTTQVLRVVKKLQDSGMLDCLQLLHFHIGSQIPSTALLSDGVGEAAQIYSELVRLGARMKVVDFGGGLGIDYNGSKSGDSDLSVPYGLQEYAHVVNAIRFVCDRKSVKHPVICSESGRAIVSHHSILIFEAICLTAPATHNEPINIPFIMEGLSEDACADYWNLRDTAMRTGDGAFWFYADQWKQRCVEQFKEGTLGIEQLASVDGLCEWVLKAIGASDPVHTYNINLSVFTSIPDLWGIDQLFPIVPIHKLDQRPGARGILSDLTCDSDGKINKF | Catalytic Activity: H(+) + L-arginine = agmatine + CO2
Sequence Mass (Da): 44604
Sequence Length: 406
Pathway: Amine and polyamine biosynthesis; agmatine biosynthesis; agmatine from L-arginine: step 1/1.
EC: 4.1.1.19
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Q7N122 | MTISTLGNQQDDSLVSNAFGFLRFPLNFQPYSSDAEWVITGVPFDMATSGRAGSRHGPAAIRQVSTNLAWESRRWPWDFKLHNCLKVVDCGDVVFNFGDAQDMSDKLQAHAEKVLASGKRMLSFGGDHFITLPLLRAHAKHFGKMALVHFDAHADTYPNGSQFDHGTMFYHAPNEGLIDPHHSVQIGIRTEHGRDNGFTVLDADQVNDRSVDDLLAQIKETVGDMPVYLTFDIDCLDPAFAPGTGTPVIGGLTTDRALKLLRGLQPLNIVGMDVVEVAPAYDQSEITALAGATIALEMLYLQASKKR | Function: Catalyzes the formation of putrescine from agmatine.
Catalytic Activity: agmatine + H2O = putrescine + urea
Sequence Mass (Da): 33668
Sequence Length: 307
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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Q8FMF7 | MSGLEQPAELSRVWRWLLLVSVAICAASGLVYELALVSLSASLNGGGIVETSLIVAGYVAALGVGAILVKPFLRWPAQTFLAVETLLGLIGGLSALVLYMTFAVVGQNLWMLVLATALIGILVGAELPLLMTMIQRGRLADARTTGSLVATLNAADYLGALLGGLAWPFILLPWLGMMRGAAAAGMINLLAALFVGCVLLRHLLPRAQFIRAVVALLVAIAVLGTVLVRSDGIVATARQQLYRDPVIYAHQSDYQDIVVTQRGADRRLYLNGGLQYSTRDEHRYTESLVYPGLSDSARTALIIGGGDGLAARELLRFPDMRITQVELDPEVIEVANTILLPDNGGAMQDPRVTVITDDAFTWLRAGGDGGQRYDAIFVDLPDPNNDTMARLYSQEFYTLALARLNDGGRMVVQSSSAYTTPDVFWRIASTMSAAGCGAVIPYHVHVPTFGDWGFQLCGPEGTELGLRGDTPSLRFLTDEVLAAAGVFGADNQPRELEPSTLDHPRVVEDLRRGYRQAGE | 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 Topology: Multi-pass membrane protein
Sequence Mass (Da): 55796
Sequence Length: 519
Pathway: Amine and polyamine biosynthesis; spermidine biosynthesis; spermidine from putrescine: step 1/1.
Subcellular Location: Cell membrane
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B1I5Z0 | MHLWFTEKQNDNFAISYRVNETLHTETTPFQHLAVLDTVPFGRTLVLDGIVQTSVVDEYVYHEMITHVPLNTHPDPRRVLIVGGGDGGTLREVTKHPSVEKATLVEIDERVIAASKKYLPELACGFDSPKAEVVIGDGIKYVAEHKKTFDLVIVDSTDPIGPAVGLFSLEFYRSIYEALKDEGLFVAQTESPYFNTDLILRIYRDIAGIFPLARTYWACIPTYPGAMWSFTIGSKKHDPAQVAPEKIREHATRYYTPEIHRASFAMPRFLADRFR | 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 Mass (Da): 31161
Sequence Length: 275
Pathway: Amine and polyamine biosynthesis; spermidine biosynthesis; spermidine from putrescine: step 1/1.
Subcellular Location: Cytoplasm
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Q9XY92 | MDKIQNGWFSEISEFWPGNSFSLEVEKVLHHEKSEYQDFLVFKSKSFGNVLVLDGVIQATERDEFAYQEMITHIPLFSHPSPKRVLVVGGGDGGVLREVVKHPLVESVTLCEIDKGVIEASRNFLPNMRVGFDHPKVTLFIGDGMEFMRQRKGEFDVIITDSSDPIGPAQGLFERAYYELLKAALAPGGIVCSQCESMWLHLDTIKGLTTFCKELYPNVEYAYTSIPSYPGGSIGFILCSLGGSTKAPIREITPEVQSQMQYYNGEVHKASFVLPQFAAKKLNL | Function: Catalyzes the production of spermidine from putrescine and decarboxylated S-adenosylmethionine (dcSAM). Has a strong preference for putrescine as substrate (By similarity).
Catalytic Activity: putrescine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) + S-methyl-5'-thioadenosine + spermidine
Sequence Mass (Da): 31724
Sequence Length: 284
Pathway: Amine and polyamine biosynthesis; spermidine biosynthesis; spermidine from putrescine: step 1/1.
EC: 2.5.1.16
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P66834 | MAEKKQWHETLHDQFGQYFAVDNVLYHEKTDHQDLIIFENAAFGRVMALDGVVQTTERDEFIYHEMMTHVPLLAHGHAKHVLIIGGGDGAMLREVTRHKNVESITMVEIDAGVVSFCRQYLPNHNAGSYDDPRFKLVIDDGVNFVNQTSQTFDVIISDCTDPIGPGESLFTSAFYEGCKRCLNPGGIFVAQNGVCFLQQEEAIDSHRKLSHYFSDVGFYQAAIPTYYGGIMTFAWATDNDALRHLSTEIIQARFLASGLKCRYYNPAVHTAAFALPQYLQDALASQPS | 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 Mass (Da): 32307
Sequence Length: 288
Pathway: Amine and polyamine biosynthesis; spermidine biosynthesis; spermidine from putrescine: step 1/1.
Subcellular Location: Cytoplasm
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B1IFK1 | MKYSGYHLVIDLFGCNFDQLENTEYIIEMLKKLARALDTKIVAKAFHKFHPQGFSGALIISESHITIHTWPEDAYIGIDIFTCSKCFDSRKIVAYLKENLIFKKVEIKEILRGKID | 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 inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.
Catalytic Activity: H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-(methylsulfanyl)propylamine
Sequence Mass (Da): 13428
Sequence Length: 116
Pathway: Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1.
EC: 4.1.1.50
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A7HMP1 | MKSLGRHIIAEFYDCDKEMLDNIDAIEFHMKQAAYETGATIVNSSFHRFLPYGVSGVVVISESHLTIHTWPEYGYAAVDLFTCGDHVDPWKAFSYLKKIFKSQRAHVVEHLRGKYDEVGIPENAPHKAVEAEMAEIF | 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 inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.
Catalytic Activity: H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-(methylsulfanyl)propylamine
Sequence Mass (Da): 15605
Sequence Length: 137
Pathway: Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1.
EC: 4.1.1.50
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Q5KWC6 | MDTMGRHVISELWGCDFDKLNDIDFIEKTFVDAALKSGAEIREVAFHKFAPQGVSGVVIISESHLTIHTFPEHGYASIDVYTCGHLDPTIAADYIAEMLGAQTRETIELPRGMRPIEVKKAQAL | 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 inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.
Catalytic Activity: H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-(methylsulfanyl)propylamine
Sequence Mass (Da): 13746
Sequence Length: 124
Pathway: Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1.
EC: 4.1.1.50
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Q04NB1 | MNALGKHVIAEFYECDYETINNHELVEDIMLKSVDLSGATTIKSVFHRFSPYGVSGVVVVSESHFAIHTWPEYGYCAVDVFTCGDLIDNQAALDYLKEKFGSKNVSVVEMKRGVLNLGVDLHHKPVGN | 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 inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.
Catalytic Activity: H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-(methylsulfanyl)propylamine
Sequence Mass (Da): 14221
Sequence Length: 128
Pathway: Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1.
EC: 4.1.1.50
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Q57763 | MLKYLGKHLILELWGCDPKALDDIEGIEKMLVDSVKACGATLICVRTHKFSPQGATGVAVLAESHIAIHTYPEYGYAALDVFTCGEHTDPYKALEVIREFLKPKSIQIIDLKRGLMENGTFELK | 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 inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain.
Catalytic Activity: H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-(methylsulfanyl)propylamine
Sequence Mass (Da): 13792
Sequence Length: 124
Pathway: Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1.
EC: 4.1.1.50
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Q18425 | MFIVVVTIFENYTQWYSSLLTIFSLTIKRKLKTIRSMQDSTSKCTCTEHHMGGTICCCCRSDAEENEQLTSVILSRKPPPQEQCRGNLLVFINPNSGTGKSLETFANTVGPKLDKSLIRYEVVVTTGPNHARNVLMTKADLGKFNGVLILSGDGLVFEALNGILCREDAFRIFPTLPIGIVPSGSGNGLLCSVLSKYGTKMNEKSVMERALEIATSPTAKAESVALYSVKTDNQSYASFLSIGWGLMADIDIDSEKWRKSLGHHRFTVMGFIRSCNLRSYKGRLTYRPYKPKGFHPSSNVFSVYEKTTQQRIDDSKVKTNGSVSDSEEETMETKFQNWTLPDSDETLAVGSSDLEETVVIEDNFVNIYAVTLSHIAADGPFAPSAKLEDNRIHLSYILWKDIGTRVNIAKYLLAIEHETHLDLPFVKHVEVSSMKLEVISEGSHVVLDGEVVDTKTIEVASTKNHISVFSSTA | Function: Catalyzes the phosphorylation of sphingosine to form sphingosine 1-phosphate (SPP), a lipid mediator with both intra- and extracellular functions. Also acts on sphinganine (By similarity). Required for neurotransmitter release from neuromuscular junctions. Acts by recruiting the synaptic vesicle priming protein unc-13 to synapses (Probable).
Catalytic Activity: a sphingoid base + ATP = a sphingoid 1-phosphate + ADP + H(+)
Sequence Mass (Da): 52453
Sequence Length: 473
Pathway: Lipid metabolism; sphingolipid metabolism.
Subcellular Location: Presynaptic cell membrane
EC: 2.7.1.91
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Q9NYA1 | MDPAGGPRGVLPRPCRVLVLLNPRGGKGKALQLFRSHVQPLLAEAEISFTLMLTERRNHARELVRSEELGRWDALVVMSGDGLMHEVVNGLMERPDWETAIQKPLCSLPAGSGNALAASLNHYAGYEQVTNEDLLTNCTLLLCRRLLSPMNLLSLHTASGLRLFSVLSLAWGFIADVDLESEKYRRLGEMRFTLGTFLRLAALRTYRGRLAYLPVGRVGSKTPASPVVVQQGPVDAHLVPLEEPVPSHWTVVPDEDFVLVLALLHSHLGSEMFAAPMGRCAAGVMHLFYVRAGVSRAMLLRLFLAMEKGRHMEYECPYLVYVPVVAFRLEPKDGKGVFAVDGELMVSEAVQGQVHPNYFWMVSGCVEPPPSWKPQQMPPPEEPL | Function: Catalyzes the phosphorylation of sphingosine to form sphingosine 1-phosphate (SPP), a lipid mediator with both intra- and extracellular functions. Also acts on D-erythro-sphingosine and to a lesser extent sphinganine, but not other lipids, such as D,L-threo-dihydrosphingosine, N,N-dimethylsphingosine, diacylglycerol, ceramide, or phosphatidylinositol . In contrast to proapoptotic SPHK2, has a negative effect on intracellular ceramide levels, enhances cell growth and inhibits apoptosis . Involved in the regulation of inflammatory response and neuroinflammation. Via the product sphingosine 1-phosphate, stimulates TRAF2 E3 ubiquitin ligase activity, and promotes activation of NF-kappa-B in response to TNF signaling leading to IL17 secretion . In response to TNF and in parallel to NF-kappa-B activation, negatively regulates RANTES induction through p38 MAPK signaling pathway . Involved in endocytic membrane trafficking induced by sphingosine, recruited to dilate endosomes, also plays a role on later stages of endosomal maturation and membrane fusion independently of its kinase activity . In Purkinje cells, seems to be also involved in the regulation of autophagosome-lysosome fusion upon VEGFA .
Catalytic Activity: a sphingoid base + ATP = a sphingoid 1-phosphate + ADP + H(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 42518
Sequence Length: 384
Subcellular Location: Cytoplasm
EC: 2.7.1.91
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Q8CI15 | MEPVECPRGLLPRPCRVLVLLNPQGGKGKALQLFQSRVQPFLEEAEITFKLILTERKNHARELVCAEELGHWDALAVMSGDGLMHEVVNGLMERPDWETAIQKPLCSLPGGSGNALAASVNHYAGYEQVTNEDLLINCTLLLCRRRLSPMNLLSLHTASGLRLYSVLSLSWGFVADVDLESEKYRRLGEIRFTVGTFFRLASLRIYQGQLAYLPVGTVASKRPASTLVQKGPVDTHLVPLEEPVPSHWTVVPEQDFVLVLVLLHTHLSSELFAAPMGRCEAGVMHLFYVRAGVSRAALLRLFLAMQKGKHMELDCPYLVHVPVVAFRLEPRSQRGVFSVDGELMVCEAVQGQVHPNYLWMVCGSRDAPSGRDSRRGPPPEEP | Function: Catalyzes the phosphorylation of sphingosine to form sphingosine 1-phosphate (SPP), a lipid mediator with both intra- and extracellular functions . Also acts on D-erythro-sphingosine and to a lesser extent sphinganine, but not other lipids, such as D,L-threo-dihydrosphingosine, N,N-dimethylsphingosine, diacylglycerol, ceramide, or phosphatidylinositol . In contrast to proapoptotic SPHK2, has a negative effect on intracellular ceramide levels, enhances cell growth and inhibits apoptosis . Involved in the regulation of inflammatory response and neuroinflammation. Via the product sphingosine 1-phosphate, stimulates TRAF2 E3 ubiquitin ligase activity, and promotes activation of NF-kappa-B in response to TNF signaling (By similarity). In response to TNF and in parallel to NF-kappa-B activation, negatively regulates RANTES induction through p38 MAPK signaling pathway (By similarity). Involved in endocytic membrane trafficking induced by sphingosine, recruited to dilate endosomes, also plays a role on later stages of endosomal maturation and membrane fusion independently of its kinase activity . In Purkinje cells, seems to be also involved in the regulation of autophagosome-lysosome fusion upon VEGFA .
Catalytic Activity: a sphingoid base + ATP = a sphingoid 1-phosphate + ADP + H(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 42443
Sequence Length: 382
Subcellular Location: Cytoplasm
EC: 2.7.1.91
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Q9NRA0 | MNGHLEAEEQQDQRPDQELTGSWGHGPRSTLVRAKAMAPPPPPLAASTPLLHGEFGSYPARGPRFALTLTSQALHIQRLRPKPEARPRGGLVPLAEVSGCCTLRSRSPSDSAAYFCIYTYPRGRRGARRRATRTFRADGAATYEENRAEAQRWATALTCLLRGLPLPGDGEITPDLLPRPPRLLLLVNPFGGRGLAWQWCKNHVLPMISEAGLSFNLIQTERQNHARELVQGLSLSEWDGIVTVSGDGLLHEVLNGLLDRPDWEEAVKMPVGILPCGSGNALAGAVNQHGGFEPALGLDLLLNCSLLLCRGGGHPLDLLSVTLASGSRCFSFLSVAWGFVSDVDIQSERFRALGSARFTLGTVLGLATLHTYRGRLSYLPATVEPASPTPAHSLPRAKSELTLTPDPAPPMAHSPLHRSVSDLPLPLPQPALASPGSPEPLPILSLNGGGPELAGDWGGAGDAPLSPDPLLSSPPGSPKAALHSPVSEGAPVIPPSSGLPLPTPDARVGASTCGPPDHLLPPLGTPLPPDWVTLEGDFVLMLAISPSHLGADLVAAPHARFDDGLVHLCWVRSGISRAALLRLFLAMERGSHFSLGCPQLGYAAARAFRLEPLTPRGVLTVDGEQVEYGPLQAQMHPGIGTLLTGPPGCPGREP | Function: Catalyzes the phosphorylation of sphingosine to form sphingosine-1-phosphate (SPP), a lipid mediator with both intra- and extracellular functions. Also acts on D-erythro-dihydrosphingosine, D-erythro-sphingosine and L-threo-dihydrosphingosine. Binds phosphoinositides . In contrast to prosurvival SPHK1, has a positive effect on intracellular ceramide levels, inhibits cells growth and enhances apoptosis . In mitochondria, is important for cytochrome-c oxidase assembly and mitochondrial respiration. The SPP produced in mitochondria binds PHB2 and modulates the regulation via PHB2 of complex IV assembly and respiration . In nucleus, plays a role in epigenetic regulation of gene expression. Interacts with HDAC1 and HDAC2 and, through SPP production, inhibits their enzymatic activity, preventing the removal of acetyl groups from lysine residues with histones. Up-regulates acetylation of histone H3-K9, histone H4-K5 and histone H2B-K12 . In nucleus, may have an inhibitory effect on DNA synthesis and cell cycle . In mast cells, is the main regulator of SPP production which mediates calcium influx, NF-kappa-B activation, cytokine production, such as TNF and IL6, and degranulation of mast cells (By similarity). In dopaminergic neurons, is involved in promoting mitochondrial functions regulating ATP and ROS levels (By similarity). Also involved in the regulation of glucose and lipid metabolism (By similarity).
PTM: Phosphorylated by PKD on Ser-419 and Ser-421 upon PMA treatment. Phosphorylation induces export from the nucleus to the cytoplasm . Phosphorylated by MAPK1 and MAPK2 at Ser-387 and Thr-614, phosphorylation is induced by agonists such as EGF and PMA and increases kinase activity .
Catalytic Activity: a sphingoid base + ATP = a sphingoid 1-phosphate + ADP + H(+)
Sequence Mass (Da): 69217
Sequence Length: 654
Subcellular Location: Cytoplasm
EC: 2.7.1.91
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Q86KF9 | MSINSDYNKENNNISPLNTSSERRSSLRNSLNNSSNNNNNNVINTPTANSINSSGNFSPKEFVSNIDGEEIIYQNQSVEYKQRLCTIQIKQSTLIIKFNEKGGFTKYLVSDTIVGSEITNESTNEYTIYSCVMNTLDVTKETRRRKQFSLRFRDRFELNQFNDKFVEAFLDTLPMGNPRERRIRVILNPKSGKKMSDSIFKDINELFKDSKIFVKKTVTKGPDHAKKIGYKFNLKKYDTIVFISGDGLFHEFINGLLSRTDFEQARKIPLALIPGGTGNGIACSIGLQDPMSCALAVIRGFTKPLDVSVIQQGDKKWCSILSLTWGIVSDVDIESEKYRALGDVRLILGAALRILNLRIYRGKIWYLPALELNKTEIAKIPKCSYSCEICESDNPISTIENVISQQQQNNTTTNQLRRSSLNNSSNGFSPKLNTSGSISNGNDDELRSMFSKEENIKIENEIHDHQNDDVLPLLKSSSDQHFIVPPTKLPNQQFLKETKEELFAKGWKVLEGEFIGIVASTVSHLASDFIASPTAHLSDGLIDLVVINNNKKFSKAGLLSVLTESSTGAHVKSDLIDQYKVQAMILEPSNDREGIIAVDGELISYGRTSMECMRACINLICRTY | Function: Catalyzes the phosphorylation of sphingosine to form sphingosine-1-phosphate (S1P), which probably acts intracellularly as a second messenger perhaps by promoting cell proliferation. Overexpression of sgkA leads to increased growth rates on solid media and an increased resistance to the antitumor agents cisplatin and carboplatin.
Catalytic Activity: a sphingoid base + ATP = a sphingoid 1-phosphate + ADP + H(+)
Sequence Mass (Da): 70024
Sequence Length: 624
Subcellular Location: Cytoplasm
EC: 2.7.1.91
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P51688 | MSCPVPACCALLLVLGLCRARPRNALLLLADDGGFESGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQDVHHFNSFDKVRSLPLLLSQAGVRTGIIGKKHVGPETVYPFDFAYTEENGSVLQVGRNITRIKLLVRKFLQTQDDRPFFLYVAFHDPHRCGHSQPQYGTFCEKFGNGESGMGRIPDWTPQAYDPLDVLVPYFVPNTPAARADLAAQYTTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGIPFPSGRTNLYWPGTAEPLLVSSPEHPKRWGQVSEAYVSLLDLTPTILDWFSIPYPSYAIFGSKTIHLTGRSLLPALEAEPLWATVFGSQSHHEVTMSYPMRSVQHRHFRLVHNLNFKMPFPIDQDFYVSPTFQDLLNRTTAGQPTGWYKDLRHYYYRARWELYDRSRDPHETQNLATDPRFAQLLEMLRDQLAKWQWETHDPWVCAPDGVLEEKLSPQCQPLHNEL | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Catalyzes a step in lysosomal heparan sulfate degradation.
PTM: The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity.
Catalytic Activity: H2O + N-sulfo-D-glucosamine = D-glucosamine + sulfate
Sequence Mass (Da): 56695
Sequence Length: 502
Subcellular Location: Lysosome
EC: 3.10.1.1
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P39664 | MAAWEFALGLLTASLWRWARKWRSPVKVKPMLAAVSSLEPQLEQITTDLRDRDRLLEDLPVSFLLLDADNLVLEANRSARVLLALPPEDYCRPLLEVVRSYELDRLVARCRAANAPQTDRWTLTPVNPDPLQVVPQTPRPVQGQAIPLSNGQIGVLIEDRQELVDLAQQRNRWVSDVAHELKTPLTSIRLLAEALRDRLQDEPQVWVDRLLGETQRLGQLVQDLLELSRLEQGPSGLQKLEAVDLVALLTSVRNSLEPLAEPLRLGWAYQGPEQGFVRGDRQRLFRLWLNLVDNAIRHSPSGGCLYVELRQRGDTWICDLYDDGPGFADADLPYLFERFYRGDPSRVRPAAASSSSPGSGLGLAIARQVVEAHQGRISARNHPVTGGAWLRVQLPQEPSLTPALKIGTGRRSG | Function: Member of the two-component regulatory system SphR/SphS. Sensory kinase. Is involved in inducible production of alkaline phosphatase in response to phosphate limitation as it is directly involved in the regulation of phoA transcription in response to phosphate limitation. SphS functions as a protein kinase that phosphorylates SphR.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Mass (Da): 46216
Sequence Length: 413
Subcellular Location: Cytoplasm
EC: 2.7.13.3
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P39665 | MTTLKPALRRAAVLLPIAAVASSLFPIQEASAQRALVTADGSSTVFPISEAVAEEFQKRNKNINVTVGVSGTGGGFKRFCNGEIDIANASRPIKKEEVEACRKKGIRYIELPVAFDALTVVVNKSNPVNSITTAELAKIFGRDAEKKTTNWRQVKSSFPNLPLRVYAPGTDSGTYDYFNEAILNKKGTRGDLTASEDDNILVQGVSRDRGGIGFFGFSYYEENKGKLKALAVVNSNGKAVMPSVQNVLNGTYDPLARPVFIYVSEQAAKKANVRSFVNFYLQNAGKLSREVGFVPLPAKAYTAATQRFRSNKTGTVFAGKSLVGGSIEDLLKAEGIN | Function: May be involved in the system for phosphate transport across the cytoplasmic membrane.
PTM: The N-terminus is blocked.
Sequence Mass (Da): 36374
Sequence Length: 337
Subcellular Location: Cell inner membrane
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Q30HU9 | MDVVRTLILCVCLFGLTFAVPCIDGVCTSNELQCASGYVKGCHAGLCTCEHATTQSCTVVNNCLHLGTCSLHGRDGFWHCVDSVCKCFFF | Function: Slow-binding inhibitor of serine proteases. The inhibitor rapidly binds to the protease forming a weak enzyme-inhibitor complex, and this is followed by a slow isomerization forming a tight-binding enzyme-inhibitor complex. Active against subtilisin A, perkinsin and trypsin with dissociation constants of 0.29 nM, 13.7 nM and 17.7 nM respectively. Not active against thermolysin, papain or pepsin. Has antiparasitic activity against the protozoan P.marinus.
PTM: Contains 6 disulfide bonds.
Sequence Mass (Da): 9715
Sequence Length: 90
Subcellular Location: Secreted
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