ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q1IZP1 | MTTETLTVRDLGLRARAAARVLRSLPTARKAAALHAIARELQAREGVILAANARDVAAAEAARLPAHMVARLRLDAASLAAIADDVAAVAQLPDPVGETTPERILPSGIRVSQRRVPLGVLGVIYESRPNVTVDVAALALMSGNAVILRGGKETVNSNAALEGAIRAALASENIPEDAVQVIRDPARERMLELLRLDDLVDAIIPRGGAGLHRFCVENATVPVIVGGIGVVHIYLDESFTRDPADVARAVNLIRNAKVQKPSACNALDTLLIHVRALPVLPAIARDLTAHGVTLRADPPALAALQTAGLEAQAATDADYG... | Function: Catalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.
Catalytic Activity: L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + L-glutamyl 5-phosphate + NADPH
Sequ... |
Q7VJ31 | MQKPRIVLKIGSSNLCNGKIIDKTQIKALAQIISELKMRFDVILVSSGAVASGHTTLHIDRNTLQNKQALASIGQPLLMESYREALKDYAIPTAQLLLVWRDFDSRKNTTFAKDTIDTLLAHNALPIINENDTIATDEMVFGDNDRLGAYVTYYFGAKLLIILSDIDGYFDKNPHQYDDAQILPIVHSIPSQALEQTHSPHGDFATGGIVTKLIAADFLLQRKCMMFLSHGRKLDVLRDFLLHNKQSSGTLFCPADSQGIKTLI | Function: Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.
Catalytic Activity: ATP + L-glutamate = ADP + L-glutamyl 5-phosphate
Sequence Mass (Da): 29369
Sequence Length: 264
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: s... |
Q6AFY0 | MTIDDRGQIRSARRIVVKVGSSSISGENAGQIGPLVDALAEAHGRGSQVVLVSSGAIATGIPYLALTERPKDLATQQAAAAVGQNVLIYRYQDSLDRYGIVAGQVLLTARDVENPTHRSNAKRAMERLLDLRILPIVNENDTVATHEIRFGDNDRLAALVAKLVEADLLVLLSDVDALYTKPPQESGAERIAHVGWNDQLEGVEIGSAGPSGVGTGGALTKVSAARQAAEHGTAVVLTATSLVVDALRGEPVGTWFAPAQETAVESAPAS | Function: Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.
Catalytic Activity: ATP + L-glutamate = ADP + L-glutamyl 5-phosphate
Sequence Mass (Da): 28254
Sequence Length: 270
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: s... |
Q72NQ8 | MKPERNSLSEKIRNAEKIVIKVGSARLSGLPSEVNDFLFQLVSDIRHLRDLGKKVILVSSGAIARGRLLLSELPSTISSGDSLAEKQALAAMGQNRLVNLYDSFFSKVNLSIAQILFGVLDLESKEGYKNLKNTFTQLVEWGILPVVNENDSVATEEVKFGDNDMLSALVSLIVEADLLIILTGVDGFLKEEKVVPFLEKISKEDLGLAGGPSGPGTGGMFTKLKSAGLLSEAGIPTAILNGKKMHVIREFLEKNSIGTLVAPSGNRVFSEEDVKEIIRKNRNGNGGNSL | Function: Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.
Catalytic Activity: ATP + L-glutamate = ADP + L-glutamyl 5-phosphate
Sequence Mass (Da): 31307
Sequence Length: 290
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: s... |
Q9WYD0 | MIMKVVVKVGSNLLVGSSGLRKSYIAELCREVARLKSQGHEISIITSGARAAGFTYLGKGKRTQDLHIKQALCAVGQVQLMKVYENAFDFYGIKIAQILLTRDTFSNRKRYLNLRNTLIGLSEFDVVPIVNENDTVATEEITLGDNDTLAAMFSIAWDADFLVLFTTVDGVIDENGKLVERFDESVKLKDMGKSSWGTGGIRSKIESALMASRCGVKATICSGNDVSNLTRFVKGEPVGTVFEPQGRLKAKKAWIAFLSEPAGKIYVNKGAEEALKSGNSLLPVGVTGVEGTFDVGDVVEIVNEEGELVGRGIVNYSSSD... | Function: Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.
Catalytic Activity: ATP + L-glutamate = ADP + L-glutamyl 5-phosphate
Sequence Mass (Da): 38320
Sequence Length: 353
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: s... |
Q60050 | MRPGLSAKRLVVKVGSAVLTGERGLDLEAMAEIARQVAALREEGREVVLVSSGAVAAGMRRLGLKERPKDMPKKQALAALGQPLLMAFWQEAFAPFGLPVAQVLLTAEDLSSRSRYLNAKATLRALLDLGAIPVINENDTVAFEEIRFGDNDQLSARVAALVEAGLLALLSDVDALYEEDPKKNPQARPIPEVESVEAVLAHAGEENPLGSGGMKSKLLAARIAGRVGIPTLLLPGKRPGVLLQALSGAPLGTYFHARRRYRGEKAWLFGLLRPKGELVLDRGAVRALKERGASLLPAGVKEVRGRFSRGEAVRLLSEEG... | Function: Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.
Catalytic Activity: ATP + L-glutamate = ADP + L-glutamyl 5-phosphate
Sequence Mass (Da): 39890
Sequence Length: 370
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: s... |
P74936 | MIRALFAAAKKIVIKIGSNTLAQADGTPDEEFLAECARACAALMRDGKQIVVVSSGAQVAGISALHCLSSPPQGAGLERHESRGVIPGDGASCKQALCAVGQAELISRWRSAFAAHQQCVGQFLCTKEDFTDSDRAAQVRYTLSFLLERRVVPILNENDALCCSDVPSVPADRRVSLSPQKRIGDNDSLSAFVALLWQADLLLLLSDIDGVYDKDPKAHTDAQHVPLVTDVSALVGKTSMGSSNVFGTGGIATKLDAARLVTRAGIPLVLANGRHLDPILSLMRGDARGTLFVPVS | Function: Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.
Catalytic Activity: ATP + L-glutamate = ADP + L-glutamyl 5-phosphate
Sequence Mass (Da): 31315
Sequence Length: 296
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: s... |
B3E610 | MRRGLLQQVRRVVIKVGSRVLTVEGGGLDYDAISRLCDEMAGLRQQGIEVILVSSGAVAAGRDALRSADTTLTIPQKQAAAAVGQPLLMQAYQQACTRHGLVTAQILLTAEDLANRNRFLNARTTLEALLTAGALPVINENDSVAVAEIKFGDNDNLSALVTSLAEADLLLILTDIEGLYSANPASDPDAELIPLVRSITREIERMAGGSGSNVGTGGMATKVTAAKKAARFGVPTILAPGKQPGVITAAVSGQEIGTLFLPATDGLNRRKHWIAYTLRPAGKVLVDAGAQKALVEKGTSLLPSGITGVEGRFERGRCVR... | Function: Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.
Catalytic Activity: ATP + L-glutamate = ADP + L-glutamyl 5-phosphate
Sequence Mass (Da): 39666
Sequence Length: 376
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: s... |
P98118 | GHASQVLVRKRRANSMLEETKKGNLERECIEELCNKEEAREVFENDPETDYFYPKYLGCLGSFRAKLFTATRRSANGYPDLRSCVNAIPDQCNPLPCSEEGYLNCKDGQATFTCICKPGWQGEKCEIDINECKDPTNINGGCSQICDNTAGSYHCSCKSGFVMLANEKDCKDMDECSVKPSVCGTAVCKNTPGDFECECSEGYRYNPTAKSCEDIDECSENMCAQLCVNYPGGYSCYCDGKKGFKLAQDKKSCEAVPVCLPLDLDKNYQLLYLAEQFVGAVLYLKFHLPEITRFSAEFDFRTYDSEGVILYAESLDHSTW... | Function: Anticoagulant plasma protein; it is a cofactor to activated protein C in the degradation of coagulation factors Va and VIIIa. It helps to prevent coagulation and stimulating fibrinolysis.
PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF do... |
P53813 | MRVLSVRFRVLLACLALVLPNSETNFLSKERASQVLVRKRRANTLLEETKKGNLERECIEELCNKEEAREVFENNPETDYFYPKYLGCLGAFRVGAFSAARQSANAYPDLRSCVNAIPDQCDPMPCNEDGYLSCKDGQGAFTCICKPGWQGDKCQFDINECKDPSNINGGCSQTCDNTPGSYHCSCKIGFAMLTNKKDCKDVDECSLKPSVCGTAVCKNIPGDFECECPNGYRYDPSSKSCKDVDECSENTCAQLCVNYPGGYSCYCDGKKGFKLAQDQRSCEGIPVCLSLDLDKNYELLYLAEQFAGVVLYLKFRLPDI... | Function: Anticoagulant plasma protein; it is a cofactor to activated protein C in the degradation of coagulation factors Va and VIIIa. It helps to prevent coagulation and stimulating fibrinolysis.
PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF do... |
P92961 | MTATEAKNRKINVGDGDDVVDIEIPDTAHQISSDSWFQVAFVLTTGINSAYVLGYSGTIMVPLGWIGGVVGLLIATAISLYANTLIAKLHEFGGRRHIRYRDLAGFIYGRKAYHLTWGLQYVNLFMINCGFIILAGSALKAVYVLFRDDHTMKLPHFIAIAGLICAIFAIGIPHLSALGVWLGVSTFLSLIYIVVAIVLSVRDGVKTPSRDYEIQGSSLSKLFTITGAAANLVFAFNTGMLPEIQATVRQPVVKNMMKALYFQFTAGVLPMYAVTFIGYWAYGSSTSTYLLNSVNGPLWVKALANVSAILQSVISLHIFA... | Function: Proline transporter that mediates proline and glycine betaine transport. May be involved in long-distance transport of proline and required for phloem loading, retrieval of proline leaking from the phloem, or in xylem-to-phloem transfer. When expressed in a heterologous system (yeast), imports D- and L-prolin... |
P92962 | MDTSEARNRKVVAVEQFDLEVPETAHQISSDSWFQVAFVLTTGINSAYVLGYSGTVMVPLGWIGGVVGLILATAISLYANTLIAKLHEFGGKRHIRYRDLAGFIYGKKMYRVTWGLQYVNLFMINCGFIILAGSALKAVYVLFRDDSLMKLPHFIAIAGVVCAIFAIGIPHLSALGIWLGVSTILSIIYIIVAIVLSAKDGVNKPERDYNIQGSSINKLFTITGAAANLVFAFNTGMLPEIQATVKQPVVKNMMKALYFQFTVGVLPMYAVTFIGYWAYGSSTSTYLLNSVSGPVWVKALANISAFLQSVISLHIFASPT... | Function: Proline transporter that mediates proline and glycine betaine transport. May be involved in the uptake of compatible solutes from the soil into the roots, or in retrieval of apoplastic amino acids delivered to the roots via the phloem. May be involved in delivery of proline to wounding sites. When expressed i... |
A0A0S2DN74 | MVAVVQADYSRAEALAAWTRLSDEFIGNCYVSVRPRHAPAWEVVVASAAGSLRLEAFKRAHDHDFLDRLAVAIGNWEQKAQRPDHEIAQMLDQVGDYGLMQGMTNPDKGFMHADILLPLLQARDACAIVVRTEPVFQQLGTAFLVRPDLILTAAHVVMDVDAATGRWASTLKNGLAFHFREKPNQREHPTLAIRPAAVALISHALPHGRPPNLLERSLAAPADTCLDYALIRLAQRVSHLRPVEVVDTAAVKQGKPCWAFGFPGGNALMMDVDLVTDIDPGSGRWLHRANVAAGMSGGCCINHEGQVAGLHEGTLDSEDD... | Function: Possibly a dedicated protease for substrate gasdermin bGSDM; cleaves the bGSDM precursor, releasing the pore-forming moiety, which integrates into the membrane and triggers cell death. Involved in defense against bacteriophages. When this probable 4 gene operon (bGSDM-FE772_23060-FE772_23065-FE772_23070) is i... |
A2QIL2 | MDGIMTNGSSEAHPPMPPPEPIERPPTPPPPPPEDSALPPPPPDTSAPPPPPEDLPPAPPPETEPKKKKVGWGTKRPAPTPLSVEELVRKKREADAAAAKPKFLSKKEREKLALEKRAQEVAATRRLKSEHASNGVDRSATHSPSVSSEGPNGDARSIPTGPRAMRNSDAAPTAPAAMRHSQSHNKNYDLAPPPPPKSMSFGLTSGKGDSRFVDEDEAAAQAALVKQRYMGADQTSNFSAKKKRKRTTDRKFNFEWNAEEDTSGDYNPLYQHRHETNFFGRGRLAGFGDDVAESVAHKYARALEDRDREAGSIRAREILE... | Function: ATP-dependent RNA helicase involved in mRNA splicing. May destabilize the U1/5'-splice site duplex to permit an effective competition for the 5'-splice site by the U6 snRNA, resulting in the switch between U1 and U6 at the 5'-splice site. May also act to unwind the U4/U6 base-pairing interaction in the U4/U6/... |
A6RJA2 | MASNGYSNSADAVPPPPSDNDGRPPSPPPPPPDSFVPPPPPSSLAPPPPPSSDLPPPPPSELLPPPPEPKKKKGWGAPKPGPLSIEDILKKKKEADEAAAKAKFLSKAAREKLALETRAKEVEEQKRKREAEQDNRISIGSVNGNGNGYGSAANGPDGYERSYQQENGRRESSFVPTGPRAMRNSQQSRSSSDKPNDMEPPPKPAKSAAAGTGKASVAGEKRPANAEDLQAALIKTRYMGAETNQSTFSAKKKRRRTTEKKFNFEWNAEEDTSPDYNPIYQNRAEAGLYGRGRLGGFAEDEGATLKYAKALEERDAEAGG... | Function: ATP-dependent RNA helicase involved in mRNA splicing. May destabilize the U1/5' splice site duplex to permit an effective competition for the 5' splice site by the U6 snRNA, resulting in the switch between U1 and U6 at the 5' splice site. May also act to unwind the U4/U6 base-pairing interaction in the U4/U6/... |
Q6FM43 | MLVLRKFRWRKWTAETLESTKMTRPIDVHQLLKSRSAGPKYMSVEERERVVIEHSNDEVDLGVEYAKKRNVDEVAEDSARESKKKSKRLDFDWDPADNTLEGYQPIVNPVILERIRQQEDQGDDLEAQYLGKSWREKLLVEMDERDWRIMREEFNITSKGKGAVKHPLRNWSETNVIPTDLVRALTEGMGFDEPTAIQRITIPNAISSNKSVPRDILGIASTGSGKTLAFSIPILARLDALPARPVNLKTLDGPLALVLVPTRELAQQISQEINRLLSAWENKKNLNAVSIVGGHSMSDISHTLRNGCDILIATPGRLLD... | Function: ATP-dependent RNA helicase involved in mRNA splicing. May destabilize the U1/5'-splice site duplex to permit an effective competition for the 5'-splice site by the U6 snRNA, resulting in the switch between U1 and U6 at the 5'-splice site. May also act to unwind the U4/U6 base-pairing interaction in the U4/U6/... |
Q1DMX8 | MDGMLTEGTSAIPPPQPPLEPIERPPTPPPLPPDESALPPPPTDPAPPPPPPDSLAPPPPPEDVPRSTYTVPVVVKKKKVGWGSSKSTTPLSVEELLRKKKEADEAASRPKFLTKSQREKLALEKRAKEIEHERRIRAASTNGSMMSDSNGGGGNSNGRASPTTRYDNVNGSSRTSIPTAPRALRGEIPTAPAAMRSSQAKNNDPRPGNKVPSDSAATGEKRTAPEDAQALLTRQRYMGADQTSSFSAKKKRRRTTERKFNFEWNADEDTSPDYNPLYQNRSEMNFFGRGRLAGFSDDVVDSAAKRYAKALEDRDLEAGS... | Function: ATP-dependent RNA helicase involved in mRNA splicing. May destabilize the U1/5'-splice site duplex to permit an effective competition for the 5'-splice site by the U6 snRNA, resulting in the switch between U1 and U6 at the 5'-splice site. May also act to unwind the U4/U6 base-pairing interaction in the U4/U6/... |
P0CQ89 | MAGPLSVEDMLAKQKAEKEAAAKPKFLSKAERQKIALEKRQSEVREQQEREDAERRQREEFDRAAEEERRRHEQERYGYNAGPSGRNDRDGYGRDGYGRDNRRGFGDRRDGSGPAIPSGPRGAALPVGPRSMQSRNGGGLPYDGFAQGSPSQLSSTPVAGSASPGPASTTASGDAVPPSQAELEALRARYLGKRTDGKKPRLRKAQDKKIIFDWNEQDDTSAADQSSWTREVRELVPGGTMFGGRLAGMDGAKKNETRSDNHADPLERRRAVKGKDDDRHWSDKPLDEMKERDWRIFREDFSIAARGGGIPHPLRNWRES... | Function: ATP-dependent RNA helicase involved in mRNA splicing. May destabilize the U1/5'-splice site duplex to permit an effective competition for the 5'-splice site by the U6 snRNA, resulting in the switch between U1 and U6 at the 5'-splice site. May also act to unwind the U4/U6 base-pairing interaction in the U4/U6/... |
Q6BLU9 | MSKRPISVEELIGKSQSAEVISKPKFLSKSERQKLSLQRNQEIQDKKRQQSTVNNGAKKRYNNSIEDNPEPKKINKKLKKGRNFNFDWDEEEDTSNNYQPLVRYDNRTNPPDLGLSDMHWSEKQIDDMTTRDWRIFKEDYNITSKGGDIENPLRCWAESKLPAKLLNILIKNLGYDSPTPIQRASIPLALNGRDIVGIAETGSGKTLAFLLPLFSYILSVDSNYLLYEHQQESNFNKPLGLILAPTRELALQITKEAKLFGDKLNLNVVTIIGGHQYEETVHSVRNGVHIVVATPGRLIDSLERGIINLSNCYFFTMDEA... | Function: ATP-dependent RNA helicase involved in mRNA splicing. May destabilize the U1/5'-splice site duplex to permit an effective competition for the 5'-splice site by the U6 snRNA, resulting in the switch between U1 and U6 at the 5'-splice site. May also act to unwind the U4/U6 base-pairing interaction in the U4/U6/... |
Q6CT49 | MLRPVSIDDLISDTVPAKKPRFLIKKRTFPQPEEEEASKALSHTVIKRKDNYRNLDEDELYEEQVSNEPDDLLFLARKSADLLKKRQNEDESIVDNYLGKHWSEKKYEEMSTRDWRILSEDFNISSKGGTVEKPLRNWHELKLIPEDLLNIITNDLHYNEPTSIQRSTIPNVINNRDFIGVASTGSGKTLAFLLPILIKLHGIPPLNSITKHDGPLALVLAPTRELAQQIQHEGQSITKLWKRPCNIVSIVGGHSLEEISANLRDGCDILVATPGRLLDCLDSHLLFLKQVNTLVLDEADKMIDFGFEDQLTTILAKTET... | Function: ATP-dependent RNA helicase involved in mRNA splicing. May destabilize the U1/5'-splice site duplex to permit an effective competition for the 5'-splice site by the U6 snRNA, resulting in the switch between U1 and U6 at the 5'-splice site. May also act to unwind the U4/U6 base-pairing interaction in the U4/U6/... |
A5DU73 | MSKRPIPIDDLLKEDAIVPKYIPKSKRAKSSNGPGEDGANTTLKLQYPQSSVNHGSAVSRSTQFSAHQKSSTRPTTSLQPPSKLRHKKFQFDWDDIDDPHYNPQPLYSFELDQLGVENGDNYNDNKNNNDDDDNFDFQDPLLHDDRNSGHWSTKLLSEMTDRDWRIFNEDYGITTKGKKIPHATRSWDESGLDPKILASLKSFGFRQPTPVQRASIPISLELRDVVGVAETGSGKTLAFLLPLLHYLSRVDGNYLNYEKVRNEPLALVLAPTRELALQITQEAEKFGKQLGFNVLSIIGGRQYQETMDQIDNMIVGRGVH... | Function: ATP-dependent RNA helicase involved in mRNA splicing. May destabilize the U1/5'-splice site duplex to permit an effective competition for the 5'-splice site by the U6 snRNA, resulting in the switch between U1 and U6 at the 5'-splice site. May also act to unwind the U4/U6 base-pairing interaction in the U4/U6/... |
A4RK80 | MAPLDLEEILKKHKAAKAEAAKPRFIPRGQRKKMEEEKKLKVEEEQKRQQEELQKTRSELQKAREELAGLQRVRRQEQSRSRESDHSVPTGPRAMRSYDDDSFNGNGNGSNSNRNNNNNQRDRQDASTKTNGSRTAEEVQEEKKYLERYTGPPAKVSTFSANKKRRRTTDQKFNFDWDPKDDTSQPWRYEETGAHERSANGATEQVRRKKATRDYNDPRLVPWQDKELSQMTTRDWRLFKVNLEIVTKGNNIPNPMRFWEESNLPHVLKDTIKQVGYTEPTPVQRAAIPIALQCRDLIGISKTGSGKTAAFVLPMLSYIE... | Function: ATP-dependent RNA helicase involved in mRNA splicing. May destabilize the U1/5'-splice site duplex to permit an effective competition for the 5'-splice site by the U6 snRNA, resulting in the switch between U1 and U6 at the 5'-splice site. May also act to unwind the U4/U6 base-pairing interaction in the U4/U6/... |
Q7SEL0 | MSTTSRREPPDLAALLRKKKEEEAAAAKPRFIPKKERERLEAEKKAKEEEERKRKEEAKPQPNGTNHNGNRMDGIQSHHNHNPQRNIPTGPKAMRYDDDRGPNGMSNGRDYRDNRDNRDNRDRNQRGAKRGAPNDDEEKRAKMERNDEAELRARYMGPVVNQSTFSAKKKRRRTAANKFNFDWDADDDTSRPFDPIYAERQEPLVRLGGYEMTEEMVMRKAEAIRRGDPETGEERARQYLEQHRRIKEMEQRKNLGKHWSEKKLEDMKERDWRIFKENFGIATKGGAIPNPMRSWEESTLPRRLLDIVKNVGYDEPTPIQ... | Function: ATP-dependent RNA helicase involved in mRNA splicing. May destabilize the U1/5'-splice site duplex to permit an effective competition for the 5'-splice site by the U6 snRNA, resulting in the switch between U1 and U6 at the 5'-splice site. May also act to unwind the U4/U6 base-pairing interaction in the U4/U6/... |
Q0UWC8 | MTDTTLPPPPPPPPPPADKMPPPPPTDVPPPPPPQEEELGPVLVPSKKAKKGWASQRKQPPSIDDILKAKREQEAAAAKPKFLSKAERERIALEKRRKEVEEAQRRREGSNSSTNGASHKGHYDASSSIPTGPRAMRPEAPSGPPSRQQRSNGDMAPPPLPDKKTGKRPPPEDAEAAMIRQRYMGAEQNQSTFSAKKKRKRTTEKKFNFEWNEEEDTSYDYNPIYQQKAEAGFFGRGRLGGFTEDVTEQGTQKFIEAMIERDPVSGRERAERILDMERRRKEEGGRAQLDKHWSEKKLEHMRERDWRIFKEDFNIATKGG... | Function: ATP-dependent RNA helicase involved in mRNA splicing. May destabilize the U1/5'-splice site duplex to permit an effective competition for the 5'-splice site by the U6 snRNA, resulting in the switch between U1 and U6 at the 5'-splice site. May also act to unwind the U4/U6 base-pairing interaction in the U4/U6/... |
Q56062 | MSLHSPGQAFRAALAKENPLQIVGAINANHALLAQRAGYQAIYLSGGGVAAGSLGLPDLGISTLDDVLTDIRRITDVCPLPLLVDADIGFGSSAFNVARTVKSIAKAGAAALHIEDQVGAKRCGHRPNKAIVSKEEMVDRIRAAVDARTDPNFVIMARTDALAVEGLEAALDRAQAYVDAGADMLFPEAITELSMYRRFADVAQVPILANITEFGATPLFTTDELRSAHVAMALYPLSAFRAMNRAAEKVYTVLRQEGTQKNVIDIMQTRNELYESINYYQFEEKLDALYRNKKS | Function: Involved in the catabolism of short chain fatty acids (SCFA) via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the thermodynamically favored C-C bond cleavage of (2R,3S)-2-methylisocitrate to yield pyruvate and succinate via an alpha-carboxy-carbanion intermediate.
Catalytic Activity: ... |
Q8EJW1 | MTQSAGLRFRQALANSKPLQIVGTTNAYFALMAEQTGFQALYLSGAGVANASYGLPDLGMTSMNDVLIDAGRITSATQLPLLVDIDTGWGGAFNIARTIKEFEKIGVAAVHMEDQVSQKRCGHRPNKAVVSTEEMVDRIKAAVDARTDPNFVIMARTDAVAVEGLEAGIERAKAYIAAGADMIFAEALTELDQYRHFKAQVKAPILANMTEFGQTQLFNKEELAQAGADMVLYPLGTFRAANQAALKVMQALMNDGHQRNVLDTMQTRADLYKYLGYHAFEDKLDQLFSQDK | Function: Involved in the catabolism of short chain fatty acids (SCFA) via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the thermodynamically favored C-C bond cleavage of (2R,3S)-2-methylisocitrate to yield pyruvate and succinate via an alpha-carboxy-carbanion intermediate.
Catalytic Activity: ... |
Q8NSL1 | MSSATTTDVRKGLYGVIADYTAVSKVMPETNSLTYRGYAVEDLVENCSFEEVFYLLWHGELPTAQQLAEFNERGRSYRSLDAGLISLIHSLPKEAHPMDVMRTAVSYMGTKDSEYFTTDSEHIRKVGHTLLAQLPMVLAMDIRRRKGLDIIAPDSSKSVAENLLSMVFGTGPESPASNPADVRDFEKSLILYAEHSFNASTFTARVITSTKSDVYSAITGAIGALKGPLHGGANEFVMHTMLAIDDPNKAAAWINNALDNKNVVMGFGHRVYKRGDSRVPSMEKSFRELAARHDGEKWVAMYENMRDAMDARTGIKPNLD... | Function: Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the Claisen condensation of propionyl-CoA and oxaloacetate (OAA) to yield 2-methylcitrate (2-MC) and CoA. Also c... |
O34002 | MTEPTIHKGLAGVTADVTAISKVNSDTNSLLYRGYPVQELAAKCSFEQVAYLLWNSELPNDSELKAFVNFERSHRKLDENVKGAIDLLSTACHPMDVARTAVSVLGANHARAQDSSPEANLEKAMSLLATFPSVVAYDQRRRRGEELIEPREDLDYSANFLWMTFGEEAAPEVVEAFNVSMILYAEHSFNASTFTARVITSTLADLHSAVTGAIGALKGPLHGGANEAVMHTFEEIGIRKDESLDEAATRSKAWMVDALAQKKKVMGFGHRVYKNGDSRVPTMKSALDAMIKHYDRPEMLGLYNGLEAAMEEAKQIKPNL... | Function: Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the Claisen condensation of propionyl-CoA and oxaloacetate (OAA) to yield 2-methylcitrate (2-MC) and CoA. Also c... |
B0YD89 | MAMTMRSTRHASKLAQTARLALTNSRRYSTAEPDLKTALKAVIPAKRELFKQVKERSDEVIGEVKVANVIGGMRGLKSMLWEGSVLDPEEGIRFHGKTIKDCQKELPKGTSGTEMLPEAMFWLLLTGQVPSTNQVRAFSRELAEQSHLPQHILDLIKSFPRSMHPMTQLSIAVAALNTESKFAKAYEKGLSKADYWEPTFDDSISLLAKIPRVAALVFRPDEVDQVGTQALDASQDWSYNFAELLGKGGKENQDFHDLLRLYLALHGDHEGGNVSAHATHLVGSALSDPFLSYSAGLLGLAGPLHGLAAQEVLRWILAMQ... | Function: Component of the methylcitrate cycle that catalyzes the synthesis of (2S,3S)-2-methylcitrate from propionyl-CoA and oxaloacetate. Plays an important role in detoxification of propionyl-CoA, an inhibitor of both primary and secondary metabolism. Has also citrate synthase activity using as substrates acetyl-CoA... |
O34779 | MLTALKTDTGKIRQHNEDDAGIFKGKDEFILAVVADGMGGHLAGDVASKMAVKAMGEKWNEAETIPTAPSECEKWLIEQILSVNSKIYDHAQAHEECQGMGTTIVCALFTGKTVSVAHIGDSRCYLLQDDDFVQVTEDHSLVNELVRTGEISREDAEHHPRKNVLTKALGTDQLVSIDTRSFDIEPGDKLLLCSDGLTNKVEGTELKDILQSDSAPQEKVNLLVDKANQNGGEDNITAVLLELALQVEEGEDQC | Cofactor: Binds 2 manganese ions per subunit.
Function: Protein phosphatase that dephosphorylates PrkC and EF-G (elongation factor G, fusA). prpC and prkC are cotranscribed, which suggests that they form a functional couple in vivo, PrpC's primary role being possibly to counter the action of PrkC. May be involved in sp... |
Q9TEM3 | MALPLRTARHASRLAQTIGRRGYATAEPDLKSALKAVIPAKRELLAEVKKQGDEVIGEVKVSNVIGGMRGLKSMLWEGSVLDADEGIRFHGKTIKDCQKELPKGPTGTEMLPEAMFWLLLTGEVPSTSQVRAFSKQLAEESHLPDHILDLAKSFPKHMHPMTQISIITAALNTESKFAKLYEKGINKADYWEPTFDDAISLLAKIPRVAALVFRPNEIDVVGRQKLDPAQDWSYNFAELLGKGGANNADFHDLLRLYLALHGDHEGGNVSAHATHLVGSALSDPFLSYSAGLLGLAGPLHGLAAQEVLRWILAMQEKIGT... | Function: Catalyzes the synthesis of (2S,3S)-2-methylcitrate from propionyl-CoA and oxaloacetate and also from acetyl-CoA and oxaloacetate with a greater efficiency. Also has citrate synthase activity and can substitute for the loss of citA activity.
Catalytic Activity: H2O + oxaloacetate + propanoyl-CoA = (2S,3S)-2-me... |
P02810 | MLLILLSVALLAFSSAQDLDEDVSQEDVPLVISDGGDSEQFIDEERQGPPLGGQQSQPSAGDGNQNDGPQQGPPQQGGQQQQGPPPPQGKPQGPPQQGGHPPPPQGRPQGPPQQGGHPRPPRGRPQGPPQQGGHQQGPPPPPPGKPQGPPPQGGRPQGPPQGQSPQ | Function: PRP's act as highly potent inhibitors of crystal growth of calcium phosphates. They provide a protective and reparative environment for dental enamel which is important for the integrity of the teeth.
PTM: Proteolytically cleaved; PRP-2, PRP-1, PIF-S and Db-S yield PRP-4, PRP-3 (protein A), PIF-F and Db-F, re... |
H8F0D7 | MTGPLAAARSVAATKSMTAPTVDERPDIKKGLAGVVVDTTAISKVVPQTNSLTYRGYPVQDLAARCSFEQVAFLLWRGELPTDAELALFSQRERASRRVDRSMLSLLAKLPDNCHPMDVVRTAISYLGAEDPDEDDAAANRAKAMRMMAVLPTIVAIDMRRRRGLPPIAPHSGLGYAQNFLHMCFGEVPETAVVSAFEQSMILYAEHGFNASTFAARVVTSTQSDIYSAVTGAIGALKGRLHGGANEAVMHDMIEIGDPANAREWLRAKLARKEKIMGFGHRVYRHGDSRVPTMKRALERVGTVRDGQRWLDIYQVLAAE... | Function: Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the Claisen condensation of propionyl-CoA and oxaloacetate (OAA) to yield 2-methylcitrate (2-MC) and CoA. Also c... |
Q56063 | MTDTTILQNNTHVIKPKKSVALSGVPAGNTALCTVGKSGNDLHYRGYDILDLAEHCEFEEVAHLLIHGKLPTRDELNAYKSKLKALRGLPANVRTVLEALPAASHPMDVMRTGVSALGCTLPEKEGHTVSGARDIADKLLASLSSILLYWYHYSHNGERIQPETDDDSIGGHFLHLLHGEKPTQSWEKAMHISLVLYAEHEFNASTFTSRVIAGTGSDVYSAIIGAIGALRGPKHGGANEVSLEIQQRYETPDEAEADIRKRVENKEVVIGFGHPVYTIADPRHQVIKRVAKQLSEEGGSLKMYHIADRLETVMWETKKM... | Function: Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the Claisen condensation of propionyl-CoA and oxaloacetate (OAA) to yield 2-methylcitrate (2-MC) and CoA. Also c... |
Q8EJW2 | MSDAKKLTGAGLRGQSAGETALSTVGVSGSGLTYRGYDVKDLAENATFEEVAYLILYGELPTTAQLAAYKTKLKGMRGLPQALKEVLERIPADAHPMDVMRTGCSMLGNLEAEHSFSEQSQIADRLLAAFPSIICYWYRFSHDGVRIDTETDDDQIGAHFLHLLHGKAPSALHTKVMDVSLILYAEHEFNASTFTARVCASTLSDMHSCVTGAIGSLRGPLHGGANEAAMELIQDMKDEADARDVLMGKLERKEKIMGFGHAIYRDSDPRNAIIKEWSEKLAADYGDDRLYRVSVACEALMWEQKKLFCNADFFHASAYH... | Function: Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and via the 2-methylcitrate cycle II (propionate degradation route). Catalyzes the Claisen condensation of propionyl-CoA and oxaloacetate (OAA) to yield 2-methylcitrate (2-MC) and CoA . Cata... |
Q6C793 | MISAIRPAVRSSVRVAPMANTAFRAYSTQDGLKERFAELIPENVEKIKKLRKEKGNTVIGEVILDQAYGGMRGIKGLVWEGSVLDPEEGIRFRGLTIPDLQKQLPHAPGGKEPLPEGLFWLLLTGEIPTDAQVKGLSADWASRAEIPKHVEELIDRCPPTLHPMAQLGIAVNALESESQFTKAYEKGVNKKEYWQYTYEDSMNLIAKLPVIASRIYRNLFKDGKIVGSIDNSLDYSANFASLLGFGDNKEFIELLRLYLTIHADHEGGNVSAHTTKLVGSALSSPFLSLSAGLNGLAGPLHGRANQEVLEWILEMKSKIG... | Function: Component of the methylcitrate cycle that catalyzes the synthesis of (2S,3S)-2-methylcitrate from propionyl-CoA and oxaloacetate. Plays an important role in detoxification of propionyl-CoA, an inhibitor of both primary and secondary metabolism. Has also citrate synthase activity using as substrates acetyl-CoA... |
A6H6T1 | MCGIRAKKSGLGGYGAGLLAALLGVSFLSQHAQTAEHVTNAANNTTIQIMKSTLSLSEVCGKTKFQGKIYGGQIAGAERWPWQASLRLYGRHICGAVLIDKNWVLSAAHCFQRSQEPSDYHVMLGYTDLNSPTRYSRTMSVQKVIVHKDYNRFHTQGSDIVLLQLRSSVEYSSHILPACVPEENIKIPKEKACWASGWGYLREDVRIPLPNELYEAELIIMSNDQCKGFFPPPVPGSGRSYYIYDDMVCAADYDMSKSICAGDSGGPLVCLLEGSWYVVGLTSWSSTCEEPIVSPSVFARVSYFDKWIKDNKKSSSNSKP... | Function: May play an important role in the sperm/egg interaction; released during the acrosome reaction.
Sequence Mass (Da): 40146
Sequence Length: 365
Subcellular Location: Cytoplasmic vesicle
EC: 3.4.21.-
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Q6AXZ6 | MWGSRAQQSGPDRGRTCLLAVLLLSFSLFQLHAQDYKPSQTPPPTSDALLKPMGRVQKEICGKTKFQGKIYGGSIAKAERWPWQASLIFRGRHICGAVLIDKNWVASAAHCFKRSLKPSDYRILLGYNELSNPSNYSRQMTLSKVIVHEDYNKLHSQEKDIVLIQLHLPVRYSSHIFPVCVPDQTTKEPSDESCWISGWGMVTDDKFLQAPFPLLDSEVFLMNDQECEAFFQTPQISITEYDAIKDDMICAGDITNQKSTCRGDSGGPLVCLLDSYWYLVGLASWSGACLEPIHSPSIFTRVSHFSDWIEKKKADTPDVD... | Function: May play an important role in the sperm/egg interaction; released during the acrosome reaction.
Sequence Mass (Da): 41448
Sequence Length: 369
Subcellular Location: Cytoplasmic vesicle
EC: 3.4.21.-
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Q7RTY9 | MGARGALLLALLLARAGLGKPGELGALQAGPGAARRPGGGGREEACGHREIHALVAGGVESARGRWPWQASLRLRRRHRCGGSLLSRRWVLSAAHCFQKHYYPSEWTVQLGELTSRPTPWNLRAYSSRYKVQDIIVNPDALGVLRNDIALLRLASSVTYNAYIQPICIESSTFNFVHRPDCWVTGWGLISPSGTPLPPPYNLREAQVTILNNTRCNYLFEQPSSRSMIWDSMFCAGAEDGSVDTCKGDSGGPLVCDKDGLWYQVGIVSWGMDCGQPNRPGVYTNISVYFHWIRRVMSHSTPRPNPSQLLLLLALLWAP | PTM: N-glycosylated.
Location Topology: Lipid-anchor
Sequence Mass (Da): 35078
Sequence Length: 318
Subcellular Location: Cell membrane
EC: 3.4.21.-
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Q920S2 | MGIQGPVLLLLLLCVMLGKPGSREESQAADLKSTDIKLLSMPCGRRNDTRSRIVGGIESMQGRWPWQASLRLKKSHRCGGSLLSRRWVLTAAHCFRKYLDPEKWTVQLGQLTSKPSYWNRKAYSGRYRVKDIIVNSEDKLKSHDLALLRLASSVTYNKDIQPVCVQPSTFTSQHQPRCWVTGWGVLQEDLKPLPPPYHLREVQVSILNNSRCQELFEIFSLHHLITKDVFCAGAEDGSADTCSGDSGGPLVCNMDGLWYQIGIVSWGIGCGRPNLPGIYTNVSHYYNWIETMMILNGAVRRDLALPLLSITLLQAPWLLR... | PTM: N-glycosylated.
Location Topology: Lipid-anchor
Sequence Mass (Da): 36218
Sequence Length: 322
Subcellular Location: Cell membrane
EC: 3.4.21.-
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Q7Z5A4 | MSSGGGSRGLLAWLLLLQPWPGQNWAGMAAPRLPSPLLSEEGGENPEASPAPGPEAGPPLNLFTSFPGDSLLCGRTPLRIVGGVDAEEGRWPWQVSVRTKGRHICGGTLVTATWVLTAGHCISSRFHYSVKMGDRSVYNENTSVVVSVQRAFVHPKFSTVTTIRNDLALLQLQHPVNFTSNIQPICIPQENFQVEGRTRCWVTGWGKTPEREKLASEILQDVDQYIMCYEECNKIIQKALSSTKDVIIKGMVCGYKEQGKDSCQGDSGGRLACEYNDTWVQVGIVSWGIGCGR | Function: Plays a role in spermatogenesis. Involved in germ cell survival during meiosis.
Location Topology: Lipid-anchor
Sequence Mass (Da): 32006
Sequence Length: 293
Subcellular Location: Cytoplasm
EC: 3.4.21.-
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Q8VIF2 | MASGGGSLGLIVFLLLLQPKPCEAWAAASVLSTSGFPSGFSEAPRDNPPPPTRVRMSKATTRSPFMNFSLVCGQPFMKIMGGVDAEEGKWPWQVSVRVRHMHVCGGSLINSQWVLTAAHCIYSRIQYNVKVGDRSVYRQNTSLVIPIKTIFVHPKFSTTIVVKNDIALLKLQHPVNFTTNIYPVCIPSESFPVKAGTKCWVTGWGKLVPGAPDVPTEILQEVDQNVILYEECNEMLKKATSSSVDLVKRGMVCGYKERGKDACQGDSGGPMSCEFENKWVQVGVVSWGISCGRKGYPGVYTDVAFYSKWLIAVVNQADCL... | Function: Plays a role in spermatogenesis. Involved in germ cell survival during meiosis. Lacks protease activity in vitro.
Location Topology: Lipid-anchor
Sequence Mass (Da): 36683
Sequence Length: 335
Subcellular Location: Cytoplasm
EC: 3.4.21.-
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Q76HL1 | MGGFCGADRGGFLALLVWLQLLQPLFSGTYKPREDSGVMHRPQRPRRPRSDPEAPAQQSRLKSLSISHPSGVPVSVDRTEIPGSGSPSGTTTKITLENRRSSLGGPFFTDTCGHRITEVDPGSLSAGRKWPWQVSLQSQNEHVCGGSLISHRWVLTAAHCIYEQEEYMVMLGDDMLHSESESVTLVPVQDIIFPSNFDIQTMRNDIALALLYFPVNYSSLIQPVCLPEEPFRVKNGTVCWVTGWGQQNEIDAGFASILLQEVQQRILLQKHCNTLFQRQLGTSKNLVIKGMICGLQDSGQSLCWGDSGNPLVCESDNTWT... | Function: Plays a role in spermatogenesis. Involved in germ cell survival during meiosis. Lacks protease activity in vitro.
Location Topology: Lipid-anchor
Sequence Mass (Da): 42203
Sequence Length: 382
Subcellular Location: Cell membrane
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Q402U7 | MAFQGCDCFGLLVWLLLLQTRLGKARMVPGTPSLSPLPSENGLDDSGVNPQERPLTGMPETSLPRKPGDSTRPLDSMAFTPGQSFSTMSLSRQPFPTWVPPTSACGHRTARIVGGRPAPARKWPWQVSLQVHKQHICGGSLISKWWVITAAHCVYGHLDYAVFMGDADLWSKRPVRIPVQDIIVHQDFSMMRTVVHDIALVLLAFPVNYSVNIQPVCIPEKSFLVQPGTLCWVTGWGKVLEQGRSSRILQEIELNIIRHEKCNQILKDIMGNIFTLVQEGGVCGYNEKGGDACQGDSGGPLVCEFNKTWVQVGIVSWGLG... | Function: Lacks protease activity in vitro.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 41073
Sequence Length: 372
Subcellular Location: Membrane
EC: 3.4.21.-
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Q5M8S2 | MACGSVDPHGLLSSPLASARLNSLPYMEGPWIWSCGQTNITCKVVNGKAVEVGKWPWQVSILFLGMYICSGSLIHHHWILTAAHCLQRSKNPAKYTVKVGVQTLPDNSTSELLVTRIVIHENFINRMSDDIAILKLKYPVTWSPLVQPICLPSFNLKPSIGTMCWVVGWGLEKAEGHPKTPYSVQGLAVRIVNNEICNHRYQFLLLKNQKKFIGNDMLCTSSEWGLDTCQDTSGSSLVCQMNKTWVQMGVVSWNFDCGRRQFPSVYTSTSHFTQWIKRQIGDLKFTSMAVPSFLSPFILTGYILLVSLGSLWLL | Location Topology: Single-pass membrane protein
Sequence Mass (Da): 35185
Sequence Length: 314
Subcellular Location: Membrane
EC: 3.4.21.-
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Q16651 | MAQKGVLGPGQLGAVAILLYLGLLRSGTGAEGAEAPCGVAPQARITGGSSAVAGQWPWQVSITYEGVHVCGGSLVSEQWVLSAAHCFPSEHHKEAYEVKLGAHQLDSYSEDAKVSTLKDIIPHPSYLQEGSQGDIALLQLSRPITFSRYIRPICLPAANASFPNGLHCTVTGWGHVAPSVSLLTPKPLQQLEVPLISRETCNCLYNIDAKPEEPHFVQEDMVCAGYVEGGKDACQGDSGGPLSCPVEGLWYLTGIVSWGDACGARNRPGVYTLASSYASWIQSKVTELQPRVVPQTQESQPDSNLCGSHLAFSSAPAQGL... | Function: Possesses a trypsin-like cleavage specificity with a preference for poly-basic substrates. Stimulates epithelial sodium channel (ENaC) activity through activating cleavage of the gamma subunits (SCNN1G).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 36431
Sequence Length: 343
Subcellular... |
Q9ES87 | MALRVGLGLGQLEALFVLLLIGLLQSRIGADGTEASCGAVIQPRITGGGSAKPGQWPWQVSITYNGVHVCGGSLVSNQWVVSAAHCFPREHSKEEYEVKLGAHQLDSFSNDIVVHTVAQIISHSSYREEGSQGDIALIRLSSPVTFSRYIRPICLPAANASFPNGLHCTVTGWGHVAPSVSLQTPRPLQQLEVPLISRETCSCLYNINAVPEEPHTIQQDMLCAGYVKGGKDACQGDSGGPLSCPIDGLWYLAGIVSWGDACGAPNRPGVYTLTSTYASWIHHHVAELQPRVVPQTQESQPDGHLCNHHPVFNLAAAQKL... | Function: Possesses a trypsin-like cleavage specificity with a preference for poly-basic substrates. Stimulates epithelial sodium channel (ENaC) activity through activating cleavage of the gamma subunits (SCNN1G) (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 36857
Sequence Length:... |
Q5WGV5 | MVSLVLAALAPAMALFSYVYLRDVYSKAKMFLVLRIFIIGALLVVPILVIQFAFTEENVFPHPAAKAFLLYGFLEEGLKWLMLFVFAYQHGQLQRPGDGILFGVSVSLGFATVENGLYMIAYGLEAAIPRTVLPTTAHAVYGIVMGYYIGQAKYKEDHKKMFLLLGAILPILLHGGYDFILSSFGHYVLYAMIPFMVILWLLAIWKLKKASRFTV | Function: Involved in the degradation of specific anti-sigma factors. Responsible for Site-1 cleavage of the RsiW anti-sigma factor. This results, after two other proteolytic steps catalyzed by the RasP and ClpXP proteases, in the release of SigW and the transcription activation of the genes under the control of the si... |
P50738 | MFAIISAGIAPGIALLSYFYLKDQYDNEPVHMVLRSFFLGVVLVFPIMFIQYVLEKENVGGGSFFVSFLSSGFLEESLKWFILMISVYPHAHFDEHYDGIVYGASVSLGFATLENILYLIGHGVEHAFVRALLPVSCHALIGVIMGFYLGKARFSADKARVKWLTLSLVVPSLLHGSYDFILTALSNWIYYMLPFMVFLWWFGLRKAKKARSVNMMQV | Function: Involved in the degradation of anti-sigma-W factor RsiW. Responsible for Site-1 cleavage of the RsiW anti-sigma factor. This results, after two other proteolytic steps catalyzed by the RasP and ClpXP proteases, in the release of SigW and the transcription activation of the genes under the control of the sigma... |
Q188Z4 | MKLDLFLLAIIPILIGMFWIRSKDRYCREPLIHLIKFFLIGAFLSVIIILLENLLMKFNVFEGYSELIYVSFVVAGLVEEGVKALILIPALIKEKHFTEKLDGIIYSVFLALGFATIENMVYIFSESRNLALQVGINRAVISIPAHVMFAITMGYYISKYKFEGNKNKRREYLFMAVLIPILLHGVFDFILMIEYRWAIILLIVYVIILWKINLDKLEKYMNHSKKVFFGNLRKKKKK | Function: Involved in the degradation of specific anti-sigma factors, specifically RsiT. Involved in the regulation of extracytoplasmic function sigma factors expression. Seems to play a role in the resistance to antimicrobial peptides. Required for colonization or survival in the host cecum.
Location Topology: Multi-p... |
Q5KXR9 | MFSLISAGVAPGVALLSYFYLKDEYEAEPLSFVLRMFLFGVLLVFPIMFIQYVLAAEGIVASPAAEAFLSAALLEEFVKWFVVYFFVYDHDEFDEPYDGIVYSASVSLGFATLENILYLLANGVETAIARALLPVSSHALFSVIMGFYFGKAKFAVKKRRYYLWASFLLPFFLHGVYDWLLLAKERWGYYMGLFMLALWWAALRKVKQAKGYARPQAVPPVKSQA | Function: Involved in the degradation of specific anti-sigma factors. Responsible for Site-1 cleavage of the RsiW anti-sigma factor. This results, after two other proteolytic steps catalyzed by the RasP and ClpXP proteases, in the release of SigW and the transcription activation of the genes under the control of the si... |
Q8EQA1 | MLSILSAGIAPALALLSYIYLKDKITEPIWLIIRMFILGALLVLPIMFIQYAISSEFNYDSIFIEAFFQIALLEEFFKWFVFMFVIYQHEEFDNHYDGIVYASSLSLGFASIENILYLITNGIEYAFLRAVFPVSSHALFGIIMGYYLGKAKTHTNYKKKNLTLAFLLPFLLHGIYNFILKGFSSFTLILTPFMVLLWIIALYRLKRANENTIIN | Function: Involved in the degradation of specific anti-sigma factors. Responsible for Site-1 cleavage of the RsiW anti-sigma factor. This results, after two other proteolytic steps catalyzed by the RasP and ClpXP proteases, in the release of SigW and the transcription activation of the genes under the control of the si... |
C0HLY5 | LKDGPCPSYMDTCCLSPDRR | Function: Binds the A.niger cell wall component alpha-1,3-glucan, a fungal pathogen-associated molecular pattern (PAMP) that activates the host immune response.
Sequence Mass (Da): 2258
Sequence Length: 20
Subcellular Location: Secreted
EC: 3.4.21.-
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B4FSG1 | MGALPVAHSLALTAAFLPCRRPAAHGRCRRRRYRAVVAYMEPNPNSPAAIAGRLVGALPIVGLVARILNDEGGVGGDIIDFAEFRRRVSKKCTVMDSKAFYDFNQRRGKPGDPFYVLLCCWLAAIGAGLLKTEEILEGVARLRISNDIEFEEETFIDMMRAAKEKRAKLKAPAPQIPMETRAEKALEAIYVCCFGQDMVEDEDEKLLRAILNAVFPSVGRAAVERMVASMAKQVASGERKRDGRTVSKEVQQRQLKDLEFLKQNKLESS | Function: Nuclear genome-encoded factor required for the accumulation of photosystem I (PSI). Functions as PSI biogenesis factor. Cooperates with PYG7 to promote the stable assembly of PSI in the thylakoid membrane. May target primarily the PsaC subunit. Does not seem to be required for the expression of chloroplast ge... |
P10098 | MSHSVKIYDTCIGCTQCVRACPTDVLEMIPWDGCKAKQIASAPRTEDCVGCKRCESACPTDFLSVRVYLWHETTRSMGLGY | Cofactor: Binds 2 [4Fe-4S] clusters. Cluster 2 is most probably the spectroscopically characterized electron acceptor FA and cluster 1 is most probably FB.
Function: Apoprotein for the two 4Fe-4S centers FA and FB of photosystem I (PSI); essential for photochemical activity. FB is the terminal electron acceptor of PSI,... |
Q06SI8 | MSHIVKIYDTCIGCTQCVRACPLDVLEMVPWDGCKAEQMASAPRTEDCVGCKRCESACPTDFLSVRVYTSSESTRSMGLAY | Cofactor: Binds 2 [4Fe-4S] clusters. Cluster 2 is most probably the spectroscopically characterized electron acceptor FA and cluster 1 is most probably FB.
Function: Apoprotein for the two 4Fe-4S centers FA and FB of photosystem I (PSI); essential for photochemical activity. FB is the terminal electron acceptor of PSI,... |
P31087 | MSHSVKIYDTCIGCTQCVRACPLDVLEMVPWDGCKAGQIASSPRTEDCVGCKRCETACPTDFLSIRVYLGAETTRSMGLAY | Cofactor: Binds 2 [4Fe-4S] clusters. Cluster 2 is most probably the spectroscopically characterized electron acceptor FA and cluster 1 is most probably FB.
Function: Apoprotein for the two 4Fe-4S centers FA and FB of photosystem I (PSI); essential for photochemical activity. FB is the terminal electron acceptor of PSI,... |
P17227 | MINLPSLFVPLVGLLFPAVAMASLFLHVEKRLLFSTKKIN | Function: May help in the organization of the PsaL subunit.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 4470
Sequence Length: 40
Subcellular Location: Plastid
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O47040 | MIIPNLPSFFVPLVGLLLPAITMVIFHLYIQNDDIF | Function: May help in the organization of the PsaL subunit.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 4116
Sequence Length: 36
Subcellular Location: Plastid
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P52768 | MIIPNLLPNLLSNLLSNLLPILPSILVPLVGLLLPAITMVLSHLYIQKDEIL | Function: May help in the organization of the PsaL subunit.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 5711
Sequence Length: 52
Subcellular Location: Plastid
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O87786 | MSSEFAATWLPAVFVPLIGLVTPAVFIVLIGRYITATD | Function: May help in the organization of the PsaL subunit.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 4081
Sequence Length: 38
Subcellular Location: Cellular thylakoid membrane
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P23993 | MATAYAPPMASQVMKSGLACSKPRGMSGASLTRRPRFVVKAVKSDKPTYQVVQPINGDPFIGSLETPVTSSPLVAWYLSNLPAYRTAVSPLLRGIEVGLAHGYLLVGPFALTGPLRNTPVHGQAGTLGAIGLVSILSVCLTMYGVASFNEGEPSTAPVLTLTGRKKEADKLQTAEGWSQFTGGFFFGGVSGAVWAYFLLYVLDLPYFFK | PTM: The N-terminus is blocked.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22211
Sequence Length: 209
Subcellular Location: Plastid
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A6NEC2 | MWLAAAAPSLARRLLFLGPPPPPLLLLVFSRSSRRRLHSLGLAAMPEKRPFERLPADVSPINCSLCLKPDLLDFTFEGKLEAAAQVRQATNQIVMNCADIDIITASYAPEGDEEIHATGFNYQNEDEKVTLSFPSTLQTGTGTLKIDFVGELNDKMKGFYRSKYTTPSGEVRYAAVTQFEATDARRAFPCWDERAIKATFDISLVVPKDRVALSNMNVIDRKPYPDDENLVEVKFARTPVTSTYLVAFVVGEYDFVETRSKDGVCVCVYTPVGKAEQGKFALEVAAKTLPFYKDYFNVPYPLPKIDLIAIADFAAGAMEN... | Cofactor: Binds 1 zinc ion per subunit.
Function: Aminopeptidase with broad substrate specificity to several peptides.
Sequence Mass (Da): 53747
Sequence Length: 478
EC: 3.4.11.-
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P58577 | MAQAVDASKNLPSDPRNREVVFPAGRDPQWGNLETPVNASPLVKWFINNLPAYRPGLTPFRRGLEVGMAHGYFLFGPFAKLGPLRDAANANLAGLLGAIGLVVLFTLALSLYANSNPPTALASVTVPNPPDAFQSKEGWNNFASAFLIGGIGGAVVAYFLTSNLALIQGLVG | PTM: Two stable N-terminal degradation products have been sequenced at the protein level.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18119
Sequence Length: 172
Subcellular Location: Cellular thylakoid membrane
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A5LHX3 | MALQDVCKWQSPDTQGPSPHLPRAGGWAVPRGCDPQTFLQIHGPRLAHGTTTLAFRFRHGVIAAADTRSSCGSYVACPASCKVIPVHQHLLGTTSGTSADCATWYRVLQRELRLRELREGQLPSVASAAKLLSAMMSQYRGLDLCVATALCGWDRSGPELFYVYSDGTRLQGDIFSVGSGSPYAYGVLDRGYRYDMSTQEAYALARCAVAHATHRDAYSGGSVDLFHVRESGWEHVSRSDACVLYVELQKLLEPEPEEDASHAHPEPATAHRAAEDRELSVGPGEVTPGDSRMPAGTETV | Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. Incorporated instead of PSMB5 or PSMB8, this ... |
Q8BG41 | MALQDVCKWQTPDTPRPSIHLPQAGGWAVPRGCDPQTFLQIHGPRLAHGTTTLAFRFRHGVIAAADTRSSCGSYVACPASRKVIPVHQRLLGTTSGTSADCATWYRVLRRELRLRELREGQLPSVAGTAKLLAAMMSCYRGLDLCVATALCGWDHSGPALFYVYSDGTCLQGDIFSVGSGSPYAYGVLDRGYHYDMTIQEAYTLARCAVAHATHRDAYSGGSVDLFHVRESGWEYVSRSDACVLYRELQKARSLEQELEAKACGIYPEPATPQGARECKELFVEQEEVTPEDCAIIMKTETM | Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. Incorporated instead of PSMB5 or PSMB8, this ... |
Q9YES4 | MSFAGATALGIRVEDGVVLAADKRMSYGGFILSRNFKKIFVINDRIGIAFAGLYGDMGGLVRIVEGQMRLASLETGKPATVRNVAKFLSSLLYSYKFFPFNVEAIVGGIDPGGEPKLYVLDPLGSIIEEDYVAAGTGATTAFGLLEHVYKRGMSLEEAKKAAVEALRASMARDAGTGDGIDVLVLPVSGKPSLETIKFRLVEG | Function: Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.
Catalytic Activity: Cleavage of peptide bonds with very broad specificity.
Sequence Mass (Da): 21586
Sequence Length: 203
Subcellular Location: Cytoplasm
EC: 3.4.25.1
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B8D673 | MGEVVLPGTAIGLKTSEGVVLASEKRLTYDGFVLSRNARKIHMITNHIGVGFAGLMGDVNFLVKVLRLEAKNYELQHGREIKTRSLAKLLSVILYSYKLAPMLTEVVVGGYDEEGPSLYILDPVGSVIEEKYVAVGSGAQLALGYIEPRYNPGLGLKEAEELAVNAVKTVIERDVLSGDGIDLVVIDKNGYQSKEIIFKMTG | Function: Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.
Catalytic Activity: Cleavage of peptide bonds with very broad specificity.
Sequence Mass (Da): 21927
Sequence Length: 202
Subcellular Location: Cytoplasm
EC: 3.4.25.1
|
Q8SR11 | MMSNEKEMTGTTIIAIKYDDGVLIGADSRTSMGAYVSSRVTDKLTQITDKIFVCRSGSSADTQMISSYLRMYLSMYSQLEDSIPQVQRAAALASKIIYENPSLLAGLIVAGYDDKPRVFNISLGGSLTERDWAIGGSGSAFIYGYCDVNWRSGMSLEEGIRFVRNAVSCAINRDNASGGCIRMSAISRTGVQRYFYPGDKVLQ | Function: The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe... |
Q7HP56 | MTSLIRSNSWGSFVQTITSSSNRLYIGWFGLLVFPLLSLATVAYITAFFLAPAVDIDGIREPVAGSLIYGNNIISGAVIPSSNAIGVHFYPLWESLGLDEWLYNGGTYQFVVFHFFLGVCGWMGREWEFSYRLGMRPWIFVAFSAPIAAAAAVFIIYPIGQGSFSDGMPLGIQGTFNFMLVFQAEHKILMHPFHILGVAGVFGGSLFSAMHGSLVSSSLLAETAGSESLNNGYVFGQEDETYSISAAHAYFGRLIFQYASFNNSRSLHFFLAAWPVIGIWFTSLGVATMAFNLNGFNFNQSILDESGHYINSWADILNRA... | Cofactor: The D1/D2 heterodimer binds P680, chlorophylls that are the primary electron donor of PSII, and subsequent electron acceptors. It shares a non-heme iron and each subunit binds pheophytin, quinone, additional chlorophylls, carotenoids and lipids. D1 provides most of the ligands for the Mn4-Ca-O5 cluster of the... |
P83755 | MTAILERRESESLWGRFCNWITSTENRLYIGWFGVLMIPTLLTATSVFIIAFIAAPPVDIDGIREPVSGSLLYGNNIISGAIIPTSAAIGLHFYPIWEAASVDEWLYNGGPYELIVLHFLLGVACYMGREWELSFRLGMRPWIAVAYSAPVAAATAVFLIYPIGQGSFSDGMPLGISGTFNFMIVFQAEHNILMHPFHMLGVAGVFGGSLFSAMHGSLVTSSLIRETTENESANEGYRFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLAAWPVVGIWFTALGISTMAFNLNGFNFNQSVVDSQGRVINTWADI... | Cofactor: The D1/D2 heterodimer binds P680, chlorophylls that are the primary electron donor of PSII, and subsequent electron acceptors. It shares a non-heme iron and each subunit binds pheophytin, quinone, additional chlorophylls, carotenoids and lipids. D1 provides most of the ligands for the Mn4-Ca-O5 cluster of the... |
Q7NMA9 | MTTSSNRPTPGGPTQPVSYPVFTVRWLAVHALTVPTIFFLGALAAMQFIQR | Cofactor: With its partner (PsbE) binds heme. PSII binds additional chlorophylls, carotenoids and specific lipids.
Function: This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electr... |
Q3BAK8 | MATKTIESSSRSGPRRTGVGSLLKPLNSEYGKVAPGWGTTPLMGVAMALFAIFLSIILEIYNSSVLLDGISIN | Function: One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consi... |
P31095 | MGQKTALSNFLKPFNSNAGKVVPGWGTTPLMGLFMGLLFVFLLIILQIYNSTIVLDAFSVNVGG | Function: One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consi... |
A0T0M2 | MLTLKILVYTTIIFFVSLFIFGLLSSDPSRNPNRKDFE | Function: One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consi... |
Q85X70 | MLTLKLFVYAVVVFFISLFIFGFLSNDPGRNPGRKE | Function: One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consi... |
Q2THQ0 | MADTTGRIPLWLVGTVTGIPVIGLIGVFFYGSYSGLGSSL | Function: One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures ... |
P32974 | MARPNPNKQVVELNRTSLYWGLLLIFVLAVLFSSYIFN | Function: One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures ... |
P62113 | METATLVAIFISGLLVSFTGYALYTAFGQPSQQLRDPFEEHGD | Function: May play a role in photosystem I and II biogenesis.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 4722
Sequence Length: 43
Subcellular Location: Plastid
|
Q31RR3 | MMEASPGLSIAITFAVILLALTGFSIYTSFGPPSKQLEDPFEDHED | Function: May play a role in photosystem I and II biogenesis.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 4988
Sequence Length: 46
Subcellular Location: Cellular thylakoid membrane
|
P26286 | MESATVLSITFAVILIAITGLAVYTSFGPPSAELGDPFDDHED | Function: May play a role in photosystem I and II biogenesis.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 4512
Sequence Length: 43
Subcellular Location: Cellular thylakoid membrane
|
Q6ENE7 | MEALVYTFLLVSTLGIIFFAIFFREPPKVPTKKVK | Function: Seems to play a role in the dimerization of PSII.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 4045
Sequence Length: 35
Subcellular Location: Plastid
|
Q31LM3 | MTPTLSAFIWSLVLGGVIVVIPLTVALIFISQTDKVRRS | Function: Involved in the binding and/or turnover of quinones at the Q(B) site of Photosystem II.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 4243
Sequence Length: 39
Subcellular Location: Cellular thylakoid membrane
|
P72575 | MTPSLANFLWSLVLGAAIVLIPATVGLIFISQKDKITRS | Function: Involved in the binding and/or turnover of quinones at the Q(B) site of Photosystem II.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 4186
Sequence Length: 39
Subcellular Location: Cellular thylakoid membrane
|
A0T0N4 | MTTSLANFIASLTAGALVLSAIGIALIIISKNDRVQRS | Function: Involved in the binding and/or turnover of quinones at the Q(B) site of Photosystem II.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3931
Sequence Length: 38
Subcellular Location: Plastid
|
Q9F1R6 | MTITPSLKGFFIGLLSGAVVLGLTFAVLIAISQIDKVQRSL | Cofactor: PSII binds multiple chlorophylls, carotenoids and specific lipids.
Function: Involved in the binding and/or turnover of quinones at the Q(B) site of Photosystem II. PSII is a light-driven water plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subs... |
O49347 | MAAAMATATKCMSLNPSPPKLQNQTKSKPFISLPTPPKPNVSLAVTSTALAGAVFSSLSYSEPALAIQQIAQLAAANASSDNRGLALLLPIVPAIAWVLYNILQPAINQVNKMRESKGIVVGLGIGGGLAASGLLTPPPEAYAAAEAAAASSDSRGQLLLIVVTPALLWVLYNILQPALNQINKMRSGD | Function: PSBY-1 and -2 are manganese-binding polypeptides with L-arginine metabolizing enzyme activity. They are a component of the core of photosystem II.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 19465
Sequence Length: 189
Subcellular Location: Plastid
|
Q85G61 | MDTRLLIVLLPIIAAASWAIYNIGKILLLQLTKRS | Function: Manganese-binding polypeptide with L-arginine metabolizing enzyme activity. Component of the core of photosystem II.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3923
Sequence Length: 35
Subcellular Location: Plastid
|
Q4G385 | MDTRLLVVLLPVATAAAWALFNIGRLALQQLKRMS | Function: Manganese-binding polypeptide with L-arginine metabolizing enzyme activity. Component of the core of photosystem II.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3882
Sequence Length: 35
Subcellular Location: Plastid
|
D3E0A3 | MSNKNTFEGTTTVGITCKDGVVFASERRASMGNLVAHKVAEKIFKIDNHIAATIAGSVADAQTLMKVISAETSLYRLRNGKDISLEAAAAVSSNILHSSPAYVQTLIGGVDDTGASIYSLDAAGGMIKDTFISTGSGSTFAYGVLEDRFYEDITVEEATEVAIRAIKAATERDTFSGNGFLVANVTKDGFKMLEKEEVDAIIEKINS | Function: Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.
Catalytic Activity: Cleavage of peptide bonds with very broad specificity.
Sequence Mass (Da): 21975
Sequence Length: 207
Subcellular Location: Cytoplasm
EC: 3.4.25.1
|
A5UM14 | MDDKILEGTTTVGITCKDGVVFASERRASMGNLVAHKVAEKIFKINDHIVTTIAGSVGDAQNLMKIIEAEVSLYQMRNNDKISVKAAASVTANILRSGPMYVQTLLGGMDGDKPSLYSLDPAGGMIEDTYISTGSGSIVAYGVLEDRYHEEITTDEGLEIAVRAIKAASERDTFSGNGYLVAKVTKDGFEMLDKEKVNDIVAKI | Function: Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.
Catalytic Activity: Cleavage of peptide bonds with very broad specificity.
Sequence Mass (Da): 21928
Sequence Length: 204
Subcellular Location: Cytoplasm
EC: 3.4.25.1
|
O27270 | MNDKNTLKGTTTVGITCKDGVVFATERRASMGNLIAHKATDKIFKIDEHIAATIAGSVADAQSLMKYLKAEAALYRMRNSEKISIEAAAALAANILHSSRFYPFIVQTLLGGVDENGAKIYSLDPSGGMIPDKFVSTGSGSPVAYGVLEDRYSDELYVDEAVDVAIRAIKSAMERDTYSGNGILVATVTEEEGFRMLSEEEIQKRIENLN | Function: Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.
Catalytic Activity: Cleavage of peptide bonds with very broad specificity.
Sequence Mass (Da): 22765
Sequence Length: 210
Subcellular Location: Cytoplasm
EC: 3.4.25.1
|
Q730J7 | MRRTLYRLMIELTNGRFTSYILRKFAQSRLSSIIIPSYAKVFQINQDEMEKGLKEYRTLHELFTRKLKEGKRSIDTDASSIVSPVDGVFADHGPIEETKTFDIKGKRYSIVDMLGNEERAQRYAGGTYMVIYLSPSHYHRIHSPLSGSVTERFVLGRKSYPVNAAGMEYGKEPLSKNYRSVTEVNSDGEHMALVKVGAMFVNSIELLHERDTVQKGEEMAYFTFGSTVVLLFEKDMIEVVQELKSGQELRLGEKIATRLAHK | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2
PTM: Is synthesized initially as a... |
P39822 | MFNTAVKILYRSLIELTNHRLSSYLIKGFCESKISKPVIPLFSKHFRLNWDDVDGTAADYGSLSELFIRQINLERRPVSKEAHAVVSPVDGVVQTVGIINPNQTFTVKGKDYSFAELTGCKSADHQYNGGYFVVLYLSPRHYHRFHSPISCRYQKLAELGNRSYPVNQLGLKYGKDVLSKNYRFVYELNSGSRNVLMIPVGAMNINSIVQTNTRTELEIGEELGYFSFGSTVILVFEKDAFQPSAHLAEGQEVQVGELIGYEE | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2
PTM: Is synthesized initially as a... |
Q8A5K8 | MGRLKKLKKIRIHREGTHILWASFLLLLLINAALYWGIDCKIPFYVVAVASIAVYLLMVNFFRCPIRLFGKDTEKIVVAPADGKIVVIEEVDENEYFHDRRLMISIFMSIVNVHANWYPVDGTIKKVAHHNGNFMKAWLPKASTENERSTVVIETPEGVEVLTRQIAGAVARRIVTYAEVGEECYIDEHMGFIKFGSRVDVYLPLGTEVCVNMGQLTTGNQTVIAKLK | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2
PTM: Is synthesized initially as a... |
Q1D614 | MNDQTFMKLMQVLPKSALSTVVGMATRLPVPAPVHQAAMRAFAKAYNVDMEEAEHSFEHYPTFAQFFTRGLKPGLRPVDAGEKVVVSPVDGRVSQVGYSDYGRCLQAKGIEYTVDELLGDSEAAKPFYGGAWTTIYLSPRDYHRIHAPLGGTITGYAYIPGEFWPVNPASVKNKQSLFCVNERLVTYLDTVAGKCAVVKVGATCVSRIKAAYDEVTTHTGQPGKVHRYGSAMPVEKGGELGRFEMGSTVILLFEPKRVTWDDSLQEEAVVRLGKRIGVIT | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2
PTM: Is synthesized initially as a... |
Q9JZP0 | MNRLYPHPIIAREGWPIIGGGLALSLLVSICCGWWSLPFWVFTVFALQFFRDPAREIPLNPEAVLSPVDGRIVVVERARDPYRDVDALKISIFMNVFNVHSQKSPADCTVTKVVYNKGKFVNADLDKASTENERNAVLATTASGREITFVQVAGLVARRILCYTQAGAKLSRGERYGFIRFGSRVDMYLPVDAQAQVAIGDKVTGVSTVLARLPLTAPQTESEPESEPALQTAPVETAANPSAEQRQIEAAAAKIQAAVQDVLKD | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2
PTM: Is synthesized initially as a... |
Q2GEF4 | MTKFSLHKEGLLTIGFTLACTAVAFFFVPALGLCGICVAALVTYFFRDPQRAIAISKDFVLSPADGLICKIENALPPQSSELVEEMQKISVYLSPLNVHVNRIPVDGIVRKLHYVPGKNLRADYDSSEDENERQESTIEMADGRNVVVVQQTGFLARRVVCDLRKDQQVSAGKRFGIIKFGSRVTVYIPKDMPLLVSEGQTVVAGETILALLSETASLVTERFLD | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2
PTM: Is synthesized initially as a... |
O25130 | MKEFAYSEPCLDKEDKKAVLEVLNSKQLTQGKRSLLFEEALCEFLGVKHALVFNSATSALLTLYRNFSEFSADRNEIITTPISFVATANMLLESGYTPVFAGIKNDGNIDELALEKLINERTKAIVSVDYAGKSVEVESVQKLCKKHSLSFLSDSSHALGSEYQNKKVGGFALASVFSFHAIKPITTAEGGAVVTNDSELHEKMKLFRSHGMLKKDFFEGEVKSIGHNFRLNEIQSALGLSQLKKAPFLMQKREEAALTYDRIFKDNPYFTPLHPLLKDKSSNHLYPILMHQKFFTCKKLILESLHKRGILAQVHYKPIY... | Function: Catalyzes the second step in the biosynthesis of pseudaminic acid, a sialic-acid-like sugar that is used to modify flagellin. Uses UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose as substrate producing UDP-4-amino-4,6-dideoxy-beta-L-AltNAc.
Catalytic Activity: 2-oxoglutarate + UDP-4-amino-4,6-dideoxy-N-... |
O25093 | MRAIAIVLARSSSKRIKNKNIIDFFNKPMLAYPIEVALNSKLFEKVFISSDSMEYVNLAKNYGASFLNLRPKILADDRATTLEVMAYHMEELELKDEDIACCLYGASALLQEKHLKNAFETLNKNQNTDYVFTCSPFSASPYRSFSLENGVQMAFKEHSNTRTQDLKTLYHDAGLLYMGKAQAFKEMRPIFSQNSIALELSPLEVQDIAHFRRFRISQAQIQPFEKRMPVKILCDCFLTSGLGHVRRCEKILSFIEKLGVEASLYLHKQNNISAFLEGVGGNDFLITDSYCLNSKDFYLLKEKAKSLMVIEDTEHAKGFY... | Cofactor: Mg(2+) is required for pseudaminic acid cytidylyltransferase activity.
Function: Catalyzes the fourth and sixth steps in the biosynthesis of pseudaminic acid, a sialic-acid-like sugar that is used to modify flagellin. The C-terminus mediates the fourth step of the pathway and catalyzes the removal of UDP from... |
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