ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
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) . P... |
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... |
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... |
Q4P1V3 | MAFYSAGPLSPGYNSTSAWGGNDNAEEDPWAAPGSSSSAAPPTTSSGFAPSPPGGFASFSTQQQQQQQQQQQRQQAGYFGGAPAAGASLAQEADAYQDGLMETSFGVGSGAGQNRLGGAAATVNPQSPHNAHSSSSTYGSAISSTHSQPSTQSQQPQSHALPSSAAQAQAARAGAFPSGVSTSQYQPTSQGAQGASRFQSHTPSTLLPSEPAGFTSHTSSDYSATAPRQLAPGYPLPASNYTVPAYSPFARVDSLSTPRRETVEDMYGVPENFLEVEVRSPLTHGVGRKMYTDYEIVTRTNIPAFKLRYSSVRRRYSDFE... | 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... |
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... |
D4B5D4 | MIWKQPPRRMGEMGGSLSRRFGNAAASWAVWRVSRSCFSLLFFFYFFLFFSSSSLLPTTNNYQHLQLHSLIPTLNTTAHLPHQQASSASMKASLFLACSALGLALATPTQDAPETVNNPLGIVYQAKLPETSRTGIRGTINATAHSSGRGVVFNLDLWGFDNTEGPFRKLHTCFDQTNKQTNKIVKLTTTTAYHIHVDPVPTDGSCGPTKDHLDPFGRGQTPPCDDSLPQTCEPGDLSGKFGRLTTSSMEEHFNQTFHDLYTSTRPGLGTFFGNRSIVIHHRNSTRLTCANFTLVEQPGTSTTYVPRPTGTGIISSIFPT... | 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 survei... |
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... |
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 supe... |
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
|
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): ... |
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
|
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
|
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
|
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: 2... |
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
|
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
|
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
|
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
|
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
|
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
|
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
|
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
|
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
|
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 Loc... |
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): 209... |
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 Loc... |
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
|
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.... |
Q5VRL3 | MAFATLVGVGGLSPALFSPSRPLSCSSSTSVSAPFILRAGGGGDARRHGLRRLVTPLRGSACRGESTNSRVLQCANEANVVTEDDIVNDGIDDETASDAEMDEDAEANGDESSGTDEDASVSWIEQQPLPYPSDALEPYISKETVEQHWGVHQNIHVERLNGMIGGSEWEGMSLGQMMLSSFNEGREAPHPPFFHAAQIWNHDFYWRSMQPGGGGKPPERLLKFINRDFGSYDGMIRQFMDAASTQFGSGWVWLCYKTSKLPHVKSRSPIPSDNYGRLVISKSPNAINPLVWGHSPLLAIDLWEHAYYLDYEDRRSDYVS... | 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
|
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 hetero... |
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
|
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 hetero... |
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 i... |
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
|
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
|
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
|
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 i... |
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
Subcellula... |
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
E... |
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
|
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
|
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
|
D3RNN8 | MQDPASHSDSLVGRVEVKETTCYMCACRCGIRVHLRDGEVRYIDGNPNHPLNKGVICAKGSSGIMKQYSPGRLTQPLRRKAGAERGESAFEVISWDEAFAMLEERLAKLRAEDPKKFALFTGRDQMQALTGLFAKQYGTPNYAAHGGFCSVNMAAGLIYTIGGSFWEFGGPDLERAKLFVMIGTAEDHHSNPLKMAISEFKRRGGRFISVNPVRTGYSAVADEWVPIKPGTDGALLLAITREILDKGLFDRDFLVRYTNAAELVIDDPSRDDHGLFYRAEMHVEPDCFDPQNKLWWDRDIDGPISTHTPGADPRLMGRYV... | 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 ... |
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
|
D3RNN6 | MHPAFSVIFLTTLLGAGQGLYLAMVTGQLYAVARFLPAQADQFYAVGSLVALLLLIAGLGASFFHLGRPERAWRAAAMWRTSWLSREVIVLPIVMALVFAYGVAHWFEWTQPLFQVGAALQVDLTLLLGVLGTIASLALFVCTAMIYAAVRFLQEWHTPLTVSNFLFLGAASGFMLAAAYSAYIGNPLVTFYGTWAVILTLVGLASRLAHLRRNARLKHKSTVQTAIGVRHASVVQKAQGATGGSFNTREFFHGRSQSLLERLRTVYLVLVFPIPVLLIGLSYLIGSSNLPIIAFFVQFAGLLIERWSFFAEARHPQNLY... | 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
|
Q8E9K5 | MEWQAEQAYNHLPPLPLDSKLAELAETLPILKACIPARAALAELKQAGELLPNQGLLINLLPLLEAQGSSEIENIVTTTDKLFQYAQEDSQADPMTKEALRYRTALYQGFTQLSNRPLCVTTALEICSTIKSVQMDVRKVPGTSLTNQATGEVIYTPPAGESVIRDLLSNWEAFLHNQDDVDPLIKMAMAHYQFEAIHPFIDGNGRTGRVLNILYLIDQQLLSAPILYLSRYIVAHKQDYYRLLLNVTTQQEWQPWIIFILNAVEQTAKWTTHKIAAARELIAHTTEYVRQQLPKIYSHELVQVIFEQPYCRIQNLVESG... | 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
|
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
|
Q9S4P4 | MKISSGAINFSTIPNQVKKLITSIREHTKNGLASKITSVKNTHTSLNEKFKTGKDSPIEFALPQKIKDFFQPKDKNTLNKTLITVKNIKDTNNAGKKNISAEDVSKMNAAFMRKHIANQTCDYNYRMTGAAPLPGGVSVSANNRPTVSEGRTPPVSPSLSLQATSSPSSPADWAKKLTDAVLRQKAGETLTAADRDFSNADFRNITFSKILPPSFMERDGDIIKGFNFSNSKFTYSDISHLHFDECRFTYSTLSDVVCSNTKFSNSDMNEVVLQYSITTQQQPSFIHTTLKNTLIRHKANLSGVILNEPHNSSPPSVSGG... | 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... |
Q9AH19 | PAKEAYRLAAATFRDAQVKHLNSQPWQTIKNTLTHNGHQYTNMQLPAADMKIGTQDIFPSAYQGKGVCSWDTKNIHHANNLWMSTVSAHEDGKDKTLFCGIRHGVLSPYDVKDPLLRQTGAENEAKEVLTAALFSKPELLTRALEGEAVNLKLVSVGLLTASNVFGKEGTMVEDQMRAWQSLTQPGKMIHLKIRNKDGELQTVKIKPEIAAFNVGVNELALKLGFGLKTSDSYNVEALHQLLGNDLRPEAKPGGWVGDWLAQYPDNYEVVNILARQIKDIWKNNLHHKDGGEPYKLAQRLAMLANEIDAVPAWNCKSGKD... | 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-co... |
P31122 | MTTNTVSRKVAWLRVVTLAVAAFIFNTTEFVPVGLLSDIAQSFHMQTAQVGIMLTIYAWVVALMSLPFMLMTSQVERRKLLICLFVVFIASHVLSFLSWSFTVLVISRIGVAFAHAIFWSITASLAIRMAPAGKRAQALSLIATGTALAMVLGLPLGRIVGQYFGWRMTFFAIGIGALITLLCLIKLLPLLPSEHSGSLKSLPLLFRRPALMSIYLLTVVVVTAHYTAYSYIEPFVQNIAGFSANFATALLLLLGGAGIIGSVIFGKLGNQYASALVSTAIALLLVCLALLLPAANSEIHLGVLSIFWGIAMMIIGLGMQ... | 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... |
Q61473 | MSSPDAGYASDDQSQPRSAQPAVMAGLGPCPWAESLSPLGDVKVKGEVVASSGAPAGTSGRAKAESRIRRPMNAFMVWAKDERKRLAQQNPDLHNAELSKMLGKSWKALTLAEKRPFVEEAERLRVQHMQDHPNYKYRPRRRKQVKRMKRVEGGFLHALVEPQAGALGPEGGRVAMDGLGLPFPEPGYPAGPPLMSPHMGPHYRDCQGLGAPALDGYPLPTPDTSPLDGVEQDPAFFAAPLPGDCPAAGTYTYAPVSDYAVSVEPPAGPMRVGPDPSGPAMPGILAPPSALHLYYGAMGSPAASAGRGFHAQPQQPLQPQ... | 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 developmen... |
P35713 | MQRSPPGYGAQDDPPARRDCAWAPGHGAAADTRGLAAGPAALAAPAAPASPPSPQRSPPRSPEPGRYGLSPAGRGERQAADESRIRRPMNAFMVWAKDERKRLAQQNPDLHNAVLSKMLGKAWKELNAAEKRPFVEEAERLRVQHLRDHPNYKYRPRRKKQARKARRLEPGLLLPGLAPPQPPPEPFPAASGSARAFRELPPLGAEFDGLGLPTPERSPLDGLEPGEAAFFPPPAAPEDCALRPFRAPYAPTELSRDPGGCYGAPLAEALRTAPPAAPLAGLYYGTLGTPGPYPGPLSPPPEAPPLESAEPLGPAADLWA... | 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 ... |
P43680 | MQRSPPGYGAQDDPPSRRDCAWAPGIGAAAEARGLPVTNVSPTSPASPSSLPRSPPRSPESGRYGFGRGERQTADELRIRRPMNAFMVWAKDERKRLAQQNPDLHNAVLSKMLGKAWKELNTAEKRPFVEEAERLRVQHLRDHPNYKYRPRRKKQARKVRRLEPGLLLPGLVQPSAPPEAFAAASGSARSFRELPTLGAEFDGLGLPTPERSPLDGLEPGEASFFPPPLAPEDCALRAFRAPYAPELARDPSFCYGAPLAEALRTAPPAAPLAGLYYGTLGTPGPFPNPLSPPPESPSLEGTEQLEPTADLWADVDLTEF... | 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 essentia... |
Q6DGL6 | MYSMMMETDLHSPGPQTNTNPGQTGPNSGSKANQDRVKRPMNAFMVWSRGQRRKMAQENPKMHNSEISKRLGAEWKVMSEAEKRPFIDEAKRLRAMHMKEHPDYKYRPRRKTKTLLKKDKYSLAGGLLGGAGGGVGMSPAGVGQRLESPGGHGGSASAGYAHMNGWANGTYSGQVAAAAAAAAMMQEAQLAYSQHPGSGSHHHHAHHHHPHNPQPMHRYDMTALQYSPISNSQSYMSASPSGYGGISYTQHQNSSVATSAAIGTLSSLVKSEPNISPPVTTHSRGPCPGDLREMISMYLPTGESGDPSVQSRLHALPQHY... | 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
|
O57401 | MYSMMMETDLHSPGGAPAPGGGLSGQSGAGGGGGGGGGGGGKAGQDRVKRPMNAFMVWSRGQRRKMAQENPKMHNSEISKRLGAEWKVMSEAEKRPFIDEAKRLRALHMKEHPDYKYRPRRKTKTLLKKDKYSLAGGLLGAGPAAGGPPAVGVGMGVGVIPGGVGQRLESPGGAAGGGYAHMNGWANGAYPGSVAAAAAAAAMMQEAQLAYGQHPGGGGHPHHPHPHHPHHPHNPQPMHRYDMGALQYSPISNSQGYVSASPSGYGALPYGSQPHQNSAAAAAAAAAAAAASSGALGALGSLVKSEPSVSPPVTSHSRAP... | 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 prese... |
O00570 | MYSMMMETDLHSPGGAQAPTNLSGPAGAGGGGGGGGGGGGGGGAKANQDRVKRPMNAFMVWSRGQRRKMAQENPKMHNSEISKRLGAEWKVMSEAEKRPFIDEAKRLRALHMKEHPDYKYRPRRKTKTLLKKDKYSLAGGLLAAGAGGGGAAVAMGVGVGVGAAAVGQRLESPGGAAGGGYAHVNGWANGAYPGSVAAAAAAAAMMQEAQLAYGQHPGAGGAHPHAHPAHPHPHHPHAHPHNPQPMHRYDMGALQYSPISNSQGYMSASPSGYGGLPYGAAAAAAAAAGGAHQNSAVAAAAAAAAASSGALGALGSLVKS... | 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 transactiva... |
P53783 | MYSMMMETDLHSPGGAQAPTNLSGPAGAGGGGGGGGGGGGGGGTKANQDRVKRPMNAFMVWSRGQRRKMAQENPKMHNSEISKRLGAEWKVMSEAEKRPFIDEAKRLRALHMKEHPDYKYRPRRKTKTLLKKDKYSLAGGLLAAGAGGGGAAVAMGVGVGVGAAAVGQRLESPGGAAGGGYAHVNGWANGAYPGSVAAAAAAAAMMQEAQLAYGQHPGAGGAHPHAHPAHPHPHHPHAHPHNPQPMHRYDMGALQYSPISNSQGYMSASPSGYGGIPYGAAAAAAAAAGGAHQNSAVAAAAAAAAASSGALGALGSLVKS... | 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 transactiva... |
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-renewa... |
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 ... |
P21458 | MAKKKRKSRKKQAKQLNIKYELNGLLCIAISIIAILQLGVVGQTFIYLFRFFAGEWFILCLLGLLVLGVSLFWKKKTPSLLTRRKAGLYCIIASILLLSHVQLFKNLTHKGSIESASVVRNTWELFLMDMNGSSASPDLGGGMIGALLFAASHFLFASTGSQIMAIVMILIGMILVTGRSLQETLKKWMSPIGRFIKEQWLAFIDDMKSFKSNMQSSKKTKAPSKKQKPARKKQQMEPEPPDEEGDYETVSPLIHSEPIISSFSDRNEEEESPVIEKRAEPVSKPLQDIQPETGDQETVSAPPMTFTELENKDYEMPSLD... | 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 ... |
Q90WR8 | MTAPEQPVKQEEMAALDVDSSGHGEYLQHGNGNASASAAAAAPQDAQPSPLALLAATCSKIGPPSPEEDEAAAAAASHSAGATGDLASVQLAGTPNRWEVLSAAPATIKDEAGNIVQIPGAATVTSSGQYVLPIQSLQNQQIFSVAPGSDSSNGTVSNVQYQVIPQIQTADGQQVQLGFAASSDNSSINQETGQIQIIPGSNQTIIASGSPSANIQNILSQSGQVQVQGVAIGGSSFPGQAQVVANVPLGLPGNITFVPINSVDLDSLGLGSGSQTMTAGINADGHLINTGQAMDSSDNSERTGEQVSPEITETATDNDL... | 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: Acetylat... |
Q02447 | MTAPEKPVKQEEMAALDVDSGGGGGGGGGHGEYLQQQQQHGNGAVAAAAAAQDTQPSPLALLAATCSKIGPPSPGDDEEEAAAAAGAPAAAGATGDLASAQLGGAPNRWEVLSATPTTIKDEAGNLVQIPSAATSSGQYVLPLQNLQNQQIFSVAPGSDSSNGTVSSVQYQVIPQIQSADGQQVQIGFTGSSDNGGINQESSQIQIIPGSNQTLLASGTPSANIQNLIPQTGQVQVQGVAIGGSSFPGQTQVVANVPLGLPGNITFVPINSVDLDSLGLSGSSQTMTAGINADGHLINTGQAMDSSDNSERTGERVSPDI... | 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 proces... |
O70494 | MTAPEKPVKQEEMAALDVDGGGGGGGHGEYLQQQQQQQQQHGNGAAAAAAQDTQPSPLALLAATCSKIGPPSPGDDDEEAAVAAAAGVPAAAAGATGDLASAQLGGAPNRWEVLSATPTTIKDEAGNLVQIPGAATSSGQYVLPLQNLQNQQIFSVAPGSDSSNGTVSNVQYQVIPQIQSTDAQQVQIGFTGSSDNGGINQENSQIQIIPGSNQTLLASGTPPANIQNLIPQTGQVQVQGVAIGGSSFPGQTQVVANVPLGLPGNITFVPINSVDLDSLGLSGSSQTMTAGINADGHLINTGQAMDSSDNSERTGERVSP... | 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 proces... |
P35149 | MEKVDIFKDIAERTGGDIYLGVVGAVRTGKSTFIKKFMELVVLPNISNEADRARAQDELPQSAAGKTIMTTEPKFVPNQAMSVHVSDGLDVNIRLVDCVGYTVPGAKGYEDENGPRMINTPWYEEPIPFHEAAEIGTRKVIQEHSTIGVVITTDGTIGDIARSDYIEAEERVIEELKEVGKPFIMVINSVRPYHPETEAMRQDLSEKYDIPVLAMSVESMRESDVLSVLREALYEFPVLEVNVNLPSWVMVLKENHWLRESYQESVKETVKDIKRLRDVDRVVGQFSEFEFIESAGLAGIELGQGVAEIDLYAPDHLYDQ... | 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 hydroly... |
Q182W3 | MNNNIYEDISKRTQGDIYIGVVGPVRTGKSTFIRKFMEKLVIPNIDNEFKKDRTRDEIPQSGSGKTIMTVEPKFVPADGVEIKIKDTVSLKVRMVDCVGYIVEGALGHEEGGKQRLVSTPWSQEAMTFEKAAEIGTKKVIKDHSTIGIVVLTDGSVTGIDRKSYVEPEERVIQELKNLKKPFAVVLNTLSPKSEETSMLRSELEEKYEVPVLPMNVVEMEEEDIEEVMEAVLYDFPLTEIRINLPKWVEGLERNHWIKSSIITTLKQSIIDIGKIRDIEGIIQGFSELEFLEDTGVDNVELGEGVINIDLQTKQDLFYNV... | 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.-
|
P17896 | MPDNIRKAVGLILLVSLLSVGLCKPLKEYLLIPTQMRVFETQTQAIETSLSVNAQTSESSEAFTVKKDPHEIKVTGKKSGESELVYDLAGFPIKKTKVHVLPDLKVIPGGQSIGVKLHSVGVLVVGFHQINTSEGKKSPGETAGIEAGDIIIEMNGQKIEKMNDVAPFIQKAGKTGESLDLLIKRDKQKIKTKLIPEKDEGEGKYRIGLYIRDSAAGIGTMTFYEPKTKKYGALGHVISDMDTKKPIVVENGEIVKSTVTSIEKGTGGNPGEKLARFSSERKTIGDINRNSPFGIFGTLHQPIQNNISDQALPVAFSTEV... | 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. Th... |
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 int... |
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 me... |
P0CH88 | VVGGKPAKLGAWPWMVALGF | PTM: Contains 3 disulfide bonds.
Sequence Mass (Da): 2085
Sequence Length: 20
Subcellular Location: Secreted
EC: 3.4.21.-
|
Q02446 | MSDQKKEEEEEAAAAAAMATEGGKTSEPENNNKKPKTSGSQDSQPSPLALLAATCSKIGTPGENQATGQQQIIIDPSQGLVQLQNQPQQLELVTTQLAGNAWQLVASTPPASKENNVSQPASSSSSSSSSNNGSASPTKTKSGNSSTPGQFQVIQVQNPSGSVQYQVIPQLQTVEGQQIQINPTSSSSLQDLQGQIQLISAGNNQAILTAANRTASGNILAQNLANQTVPVQIRPGVSIPLQLQTLPGTQAQVVTTLPINIGGVTLALPVINNVAAGGGTGQVGQPAATADSGTSNGNQLVSTPTNTTTSASTMPESPSS... | 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... |
Q298L4 | MVRTKNQSSSSSASSSSHKSPIKSHGGSGSAAAGTAGHPVSRSSSSHRTSIDDRKSATNVSSSSNRRTTPGSSPDGDGDDDTTTTDDLTPTSTSAPRSAGGPSSVHKQNLYVVSFPIIFLFNVLRSLIYQLFCIFRYLYGASTKVIYRPHRRDCNIEIVVQNNSNNKDQKHQQLTSSQSLNYPLEVTSGEAASEQQVQQPLPQQRYRALQPLEMAGANRSGSGYSPGPGDPLLAKQKHHHRRAFEYISKALKIDEENEGHKELAIELYRKGIKELEDGIAVDCWSGRGDVWDRAQRLHDKMQTNLSMARDRLHFLALREE... | 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. Inv... |
Q9UBP0 | MNSPGGRGKKKGSGGASNPVPPRPPPPCLAPAPPAAGPAPPPESPHKRNLYYFSYPLFVGFALLRLVAFHLGLLFVWLCQRFSRALMAAKRSSGAAPAPASASAPAPVPGGEAERVRVFHKQAFEYISIALRIDEDEKAGQKEQAVEWYKKGIEELEKGIAVIVTGQGEQCERARRLQAKMMTNLVMAKDRLQLLEKMQPVLPFSKSQTDVYNDSTNLACRNGHLQSESGAVPKRKDPLTHTSNSLPRSKTVMKTGSAGLSGHHRAPSYSGLSMVSGVKQGSGPAPTTHKGTPKTNRTNKPSTPTTATRKKKDLKNFRNV... | 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, bu... |
B7PXE3 | MASTVALLRDSSDDRENFDDGETDCVQVGRKRKLTVFFYPLLLVFWLLRWVFYQFFLVLCFVCRGFVPRRHLATAETTTTMATAEEPDANLLIRQKQHHKKAFDFISKALKYDEENEDFKEMSIDLYRKGIEELQKGIAIDFSKGQGTTWERAHRLSDKMKVNLEMARDRLDFLESMVKIEHLGDHLPWHGGVAPAQRGQRRRAWQKAAPSAPSEPGTGPSWLKMAENGPAKGGPCPTSPRLQRSNTGVTLRRQQQQQLGGVSTVSRSQTLPRNSVPCPRMSARSPSRKAGNNEAVPTPNTARRRASQPQVPPVHPRGRQ... | 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 tub... |
A7T395 | MPNNDILRPLAIPAKYVGSFLVFLYNGLYFVFVVNLWSRLFGKATKTEVPPLPKIRKLGKDMASRAPPRRGQSSEDNEDGLPAEIFNVRRHHKQAYAYIARALEVDEGQGSLETKKRAVEFYNRGIEEMEAGLLIPCIDEGEEWDKARRLQEKMEANLENTRERMDELVIIFFIIVVALLVSAGMMDDQPLLSARKTSSEPSQAWDVSKPTGPSYKQSKSYKNSTTVTTKRSQASPSFSSSSSSVNSTAGSSRTKPAKPAPMAAPRRYNPQVRRTKSTKPAMMAKQSCVDEQKKKISHLKGIDPKLANIIMDEILESGPA... | 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 tub... |
B2RYN7 | MSSPAGRRKKKGSGGASPAPARPPPPAAVPAPAAGPAPAPGSPHKRNLYYFSYPLVVGFALLRLLACHLGLLFVWLCQRFSRALMAAKRSSGTAPAPASPSTPAPGPGGEAESVRVFHKQAFEYISIALRIDEEEKGQKEQAVEWYKKGIEELEKGIAVIVTGQGEQYERARRLQAKMMTNLVMAKDRLQLLESGAVPKKKDPLTHASNSLPRSKTVMKSGSTGLSGHHRAPSCSGLSMVSGARPGSGPAATTHKGTSKPNRTNKPSTPTTAVRKKKDLKNFRNVDSNLANLIMNEIVDNGTAVKFDDIAGQELAKQALQ... | 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... |
P40702 | MSSNKTEKPTKKRLEDSAKKGQSFKSKDLIIACLTLGGIAYLVSYGSFNEFMGIIKIIIADNFDQSMADYSLAVFGIGLKYLIPFMLLCLVCSALPALLQAGFVLATEALKPNLSALNPVEGAKKLFSMRTVKDTVKTLLYLSSFVVAAIICWKKYKVEIFSQLNGNIVGIAVIWRELLLALVLTCLACALIVLLLDAIAEYFLTMKDMKMDKEEVKREMKEQEGNPEVKSKRREVHMEILSEQVKSDIENSRLIVANPTHITIGIYFKPELMPIPMISVYETNQRALAVRAYAEKVGVPVIVDIKLARSLFKTHRRYDL... | 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
|
P0A1M8 | MANKTEKPTPKKLKDAAKKGQSFKFKDLTTVVIILVGTFTIISFFSLSDVMLLYRYVIINDFEINEGKYFFAVVIVFFKIIGFPLFFCVLSAVLPTLVQTKFVLATKAIKIDFSVLNPVKGLKKIFSIKTIKEFFKSILLLIILALTTYFFWINDRKIIFSQVFSSVDGLYLIWGRLFKDIILFFLAFSILVIILDFVIEFILYMKDMMMDKQEIKREYIEQEGHFETKSRRRELHIEILSEQTKSDIRNSKLVVMNPTHIAIGIYFNPEIAPAPFISLIETNQCALAVRKYANEVGIPTVRDVKLARKLYKTHTKYSFV... | 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
Sub... |
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): 33... |
P49726 | MPLVVRFPDVLKNRLETLQSAFDMAINSQGYEAHYQGVYPVKCNQDRFVVEDIVKFGSPYRFGLEAGSKPELLLAMNCLSKGSADALLVCNGFKDTEYISLALVARKLLLNSVIVLEQEEELDLVIDISRKMSVRPVIGLRAKLRTKHSGHFGSTSGEKGKFGLTTTQILRVVKKLDESGMLDCLQLLHFHIGSQIPTTELLADGVGEATQIYSELVRLGAGMKFIDIGGGLGIDYDGSKSSNSDVSVCYSIEEYASAVVQAVLYVCDRKGGKHPVICSESGRAIVSHHSILIFEAVSASTSHVSTQPSSGGLQSLVETL... | 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
|
O23141 | MPALACVDTSFVPPAYAFSDTAGDVFIPASSPTSAAVVVDRWSPSLSSSLYRIDGWGAPYFIANSSGNISVRPHGSETLPHQDIDLLKIVKKVTGPKSSGGLGLQLPLIVRFPDVLKNRLECLQSAFDYAIKSQGYDSHYQGVYPVKCNQDRFVVEDIVKFGSSFRFGLEAGSKPEILLAMSCLCKGSPDAFLVCNGFKDAEYISLALLGRKLALNTVIVLEQEEELDLVIELSQKMNVRPVIGLRAKLRTKHSGHFGSTSGEKGKFGLTTTQIVRVVRKLRQSGMLDCLQLLHFHIGSQIPSTSLLSDGVAEAAQLYCE... | 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 toleran... |
O81160 | YQGVYPVKSNQDRFVVEDIVKFGSSFRFGLEAGSKPELLLAMSCLCKGNPEALLVCNGFKDAEYISLALLARKLALKHVIVLEQEEEVDMVIDISQKLSVRPVIGVRAKLRTKHSGHFGSTSGEKGKFGLTTTQVLRVVKKLQDSGMLDCLQLLHFHIGSQIPSTALLSDGVGEAAQIYSELVRLGARMKVVDFGGGLGIDYNGSKSGDSDLSVPYGLQEYAHVVNAIRFVCDRKSVKHPVICSESGRAIVSHHSILIFEAICLTAPATHNEPINIPFIMEGLSEDACADYWNLRDTAMRTGDGAFWFYADQWKQRCVEQ... | 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
|
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
|
Q8FMF7 | MSGLEQPAELSRVWRWLLLVSVAICAASGLVYELALVSLSASLNGGGIVETSLIVAGYVAALGVGAILVKPFLRWPAQTFLAVETLLGLIGGLSALVLYMTFAVVGQNLWMLVLATALIGILVGAELPLLMTMIQRGRLADARTTGSLVATLNAADYLGALLGGLAWPFILLPWLGMMRGAAAAGMINLLAALFVGCVLLRHLLPRAQFIRAVVALLVAIAVLGTVLVRSDGIVATARQQLYRDPVIYAHQSDYQDIVVTQRGADRRLYLNGGLQYSTRDEHRYTESLVYPGLSDSARTALIIGGGDGLAARELLRFPDM... | 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 ... |
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 ... |
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 (... |
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 ... |
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 ina... |
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 ina... |
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 ina... |
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 ina... |
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 ina... |
Q18425 | MFIVVVTIFENYTQWYSSLLTIFSLTIKRKLKTIRSMQDSTSKCTCTEHHMGGTICCCCRSDAEENEQLTSVILSRKPPPQEQCRGNLLVFINPNSGTGKSLETFANTVGPKLDKSLIRYEVVVTTGPNHARNVLMTKADLGKFNGVLILSGDGLVFEALNGILCREDAFRIFPTLPIGIVPSGSGNGLLCSVLSKYGTKMNEKSVMERALEIATSPTAKAESVALYSVKTDNQSYASFLSIGWGLMADIDIDSEKWRKSLGHHRFTVMGFIRSCNLRSYKGRLTYRPYKPKGFHPSSNVFSVYEKTTQQRIDDSKVKTN... | 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 prote... |
Q9NYA1 | MDPAGGPRGVLPRPCRVLVLLNPRGGKGKALQLFRSHVQPLLAEAEISFTLMLTERRNHARELVRSEELGRWDALVVMSGDGLMHEVVNGLMERPDWETAIQKPLCSLPAGSGNALAASLNHYAGYEQVTNEDLLTNCTLLLCRRLLSPMNLLSLHTASGLRLFSVLSLAWGFIADVDLESEKYRRLGEMRFTLGTFLRLAALRTYRGRLAYLPVGRVGSKTPASPVVVQQGPVDAHLVPLEEPVPSHWTVVPDEDFVLVLALLHSHLGSEMFAAPMGRCAAGVMHLFYVRAGVSRAMLLRLFLAMEKGRHMEYECPYLV... | 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, diacylg... |
Q8CI15 | MEPVECPRGLLPRPCRVLVLLNPQGGKGKALQLFQSRVQPFLEEAEITFKLILTERKNHARELVCAEELGHWDALAVMSGDGLMHEVVNGLMERPDWETAIQKPLCSLPGGSGNALAASVNHYAGYEQVTNEDLLINCTLLLCRRRLSPMNLLSLHTASGLRLYSVLSLSWGFVADVDLESEKYRRLGEIRFTVGTFFRLASLRIYQGQLAYLPVGTVASKRPASTLVQKGPVDTHLVPLEEPVPSHWTVVPEQDFVLVLVLLHTHLSSELFAAPMGRCEAGVMHLFYVRAGVSRAALLRLFLAMQKGKHMELDCPYLVH... | 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, diacyl... |
Q9NRA0 | MNGHLEAEEQQDQRPDQELTGSWGHGPRSTLVRAKAMAPPPPPLAASTPLLHGEFGSYPARGPRFALTLTSQALHIQRLRPKPEARPRGGLVPLAEVSGCCTLRSRSPSDSAAYFCIYTYPRGRRGARRRATRTFRADGAATYEENRAEAQRWATALTCLLRGLPLPGDGEITPDLLPRPPRLLLLVNPFGGRGLAWQWCKNHVLPMISEAGLSFNLIQTERQNHARELVQGLSLSEWDGIVTVSGDGLLHEVLNGLLDRPDWEEAVKMPVGILPCGSGNALAGAVNQHGGFEPALGLDLLLNCSLLLCRGGGHPLDLLS... | 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 ... |
Q86KF9 | MSINSDYNKENNNISPLNTSSERRSSLRNSLNNSSNNNNNNVINTPTANSINSSGNFSPKEFVSNIDGEEIIYQNQSVEYKQRLCTIQIKQSTLIIKFNEKGGFTKYLVSDTIVGSEITNESTNEYTIYSCVMNTLDVTKETRRRKQFSLRFRDRFELNQFNDKFVEAFLDTLPMGNPRERRIRVILNPKSGKKMSDSIFKDINELFKDSKIFVKKTVTKGPDHAKKIGYKFNLKKYDTIVFISGDGLFHEFINGLLSRTDFEQARKIPLALIPGGTGNGIACSIGLQDPMSCALAVIRGFTKPLDVSVIQQGDKKWCSI... | 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 cispl... |
P51688 | MSCPVPACCALLLVLGLCRARPRNALLLLADDGGFESGAYNNSAIATPHLDALARRSLLFRNAFTSVSSCSPSRASLLTGLPQHQNGMYGLHQDVHHFNSFDKVRSLPLLLSQAGVRTGIIGKKHVGPETVYPFDFAYTEENGSVLQVGRNITRIKLLVRKFLQTQDDRPFFLYVAFHDPHRCGHSQPQYGTFCEKFGNGESGMGRIPDWTPQAYDPLDVLVPYFVPNTPAARADLAAQYTTVGRMDQGVGLVLQELRDAGVLNDTLVIFTSDNGIPFPSGRTNLYWPGTAEPLLVSSPEHPKRWGQVSEAYVSLLDLTP... | 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 ... |
P39664 | MAAWEFALGLLTASLWRWARKWRSPVKVKPMLAAVSSLEPQLEQITTDLRDRDRLLEDLPVSFLLLDADNLVLEANRSARVLLALPPEDYCRPLLEVVRSYELDRLVARCRAANAPQTDRWTLTPVNPDPLQVVPQTPRPVQGQAIPLSNGQIGVLIEDRQELVDLAQQRNRWVSDVAHELKTPLTSIRLLAEALRDRLQDEPQVWVDRLLGETQRLGQLVQDLLELSRLEQGPSGLQKLEAVDLVALLTSVRNSLEPLAEPLRLGWAYQGPEQGFVRGDRQRLFRLWLNLVDNAIRHSPSGGCLYVELRQRGDTWICDL... | 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 th... |
P39665 | MTTLKPALRRAAVLLPIAAVASSLFPIQEASAQRALVTADGSSTVFPISEAVAEEFQKRNKNINVTVGVSGTGGGFKRFCNGEIDIANASRPIKKEEVEACRKKGIRYIELPVAFDALTVVVNKSNPVNSITTAELAKIFGRDAEKKTTNWRQVKSSFPNLPLRVYAPGTDSGTYDYFNEAILNKKGTRGDLTASEDDNILVQGVSRDRGGIGFFGFSYYEENKGKLKALAVVNSNGKAVMPSVQNVLNGTYDPLARPVFIYVSEQAAKKANVRSFVNFYLQNAGKLSREVGFVPLPAKAYTAATQRFRSNKTGTVFAGK... | 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
|
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... |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.