ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q49Y20 | MNWTEVAIVANHEVSPIITNLLEDYGSNGVVIEDSEDLTHDFEDKYGEIYALNAEDYPTQGVRVKAYFNEIKYTKDFQEKLIQSLKDIESLDLDLFSFDEQTIREQDWENEWKHYFHPFRASEKFTIVPSWETYQQEDDSELCIELDPGMAFGTGDHPTTSMCLKAIEAYVKSSDSVIDVGTGSGILSIAAHLLGVKRIKALDVDEMAVRVAKENFQKNNCEYAIEAVPGNLLKEETEKFDVVIANILAHIIEEMIDDAYNTLNKDGYFITSGIIEEKHEAIVEHMKRSGFEIVSINHDNSWVCIVGQKVSD | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 35480
Sequence Length: 312
Subcellular Location: Cytoplasm
EC: 2.1.1.-
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P60095 | MGEFYHELTLSPSSYLELFSDFLLEATGEGIEEEGNSIIVRSDQDLSWLIEALQEFCQTLSARVSEEVNFSHSLTWKRNEDWIERYRQSIQPIECAPFYVRPSWHPPKPDLIDLLIDPALAFGSGHHGTTNGCLACLGALELEGKRVLDVGCGSGILAIASAKKGAIVEMCDTDELAVGEALKNASLNQVIASKVWIGSVGDAEGEYDLIIANILAAILIMLSPWLKERLKPGARLILSGILGPYKEDVLRKFGGFTLEKELLCEEWVTLQLRKN | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 30422
Sequence Length: 275
Subcellular Location: Cytoplasm
EC: 2.1.1.-
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Q8PQ06 | MPFLELTLSCSEVTLPRFQNALDDVGALAVTMLDADADTSNERAILEPGVGEMPLWDRLTMTALFDGDSDALVVLAALEAFDPGLDWSQVAFRMVEDSDWERAWMDLFKPMQFGERTFIVPWNHALPEAADTPEAAVVRLDPGLAFGSGTHQTTALCLRWLDSLAGSGELQGRSVLDFGCGSGILAVAALKLGATHAVGVDNDPQALLATADNAQRNGVDAQLAVYMPQDEPVQTYQVVVANILASALDALADTLAARVAPGGRIALSGILHGQEDDLLKRYAPWFEQLRCERDEDWMRIDGVRRG | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 33124
Sequence Length: 306
Subcellular Location: Cytoplasm
EC: 2.1.1.-
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Q9PBE3 | MAFLEVSVQCQGRSQARYEEVLESFGALAVTLLDADADTVRERGVFEPGVGETVLWDVVVLSALFPVETDALGLLAGLEGAEPGLDWGGVRFRVVVDEDWERVWMDQFQPMRFGERTFIVPWNQAVPVEASGMDAAVVRLDPGLAFGSGTHPTTGLCLRWLDRLGGDGVLGGGEVLDFGCGSGILALAALKLGAVYAVGVDNDPQALLASRENALRNGVAERLEVYLPAEAPVRRYPVVVANILASTLVALAERLAGCVAPGGRLALSGILRGEEKEVLRCYAVWLDVLGCEEEDGWIRIDGVRRC | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 32838
Sequence Length: 306
Subcellular Location: Cytoplasm
EC: 2.1.1.-
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Q55167 | MTSDDAAAGLVRVLDAAQGAFLALDSYGGNDRSRAVLAMAEALERSFAQILEANTLDLVVSREMSVADCLCEWLKLTPERLQNTVTILKRLASLPDPLQRVMASPYQFNLAQTYCQLMPLGVVALVYESFPELAAIAAGFCLKTGNSLVLRSCGASSHSTAAICEILREGLLDADLPVDSVSHIPSETSPNVQDLVGNASQLNLVIPYGRPSFVEQISQQCTPPVLKAAMGNCYLYWSSKGDLEMVRQMIIDSHVGHPDPVNAIEKVLVSPGQNPAPLVRLLNNLQAKGFKLRGDAELCEQFPDHLTLAKENEWGKAYLD... | 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... |
Q39JM2 | MDIDQYMTDLGRRARHASRAMARASTAAKNAALDAVARAIERDAQVLKDANARDVARAREKGLDAAFVDRLTLSDKALNTMVEGLRQVASLADPIGEISNLKYRPSGIQVGQMRVPLGVIGIIYESRPNVTIDAAALCLKSGNATILRGGSEALESNTALAKLIGEGLEAAGLPQDAVQVVATADRAAVGKLITMTEYVDVIVPRGGKSLIERLINEARVPMIKHLDGICHVYVDDRADLAKALTVCDNAKTHRYGTCNTMETLLVSSGVAAKLLPPLGKLYRDKQVELRVDAAARTVLADAGVGPLVDATEEDWHTEYL... | 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... |
Q2SZ88 | MDIDQYMTDVGRRARRASRSIARASTAAKNAALEAVARAIERDAGALKAANARDVARAKDKGLDAAFVDRLTLSDKALKTMVEGLRQVATLPDPIGEMSNLKYRPSGIQVGQMRVPLGVIGIIYESRPNVTIDAAALCLKSGNATILRGGSEALESNTALAKLIGEGLAEAGLPQDTVQVVETADRAAVGRLITMTEYVDVIVPRGGKSLIERLINEARVPMIKHLDGICHVYVDDRASVTKALTVCDNAKTHRYGTCNTMETLLVARGIAPAVLSPLGRLYREKGVELRVDADARAVLEAAGVGPLVDATDEDWRTEYL... | 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... |
A4XK60 | MSDLIQKAQKVKEASKKLMNLSESQKNLALSCISKKILDNMEYILVENKKDMENAQNKGIKGALLDRLKLTEDRIRQICKGIEDVIKLPDPVGEVISMWKRPNGLIIGQKRVPIGAIGIIYEARPNVTVDAAVLCLKAGNSVLLRGGSEAINSNVALVKTMKEGLIEAGIDEGSIEIVEDTSRETAVAMMKLNEYLDLLIPRGGANLIKTVVQNATVPVIETGVGNCHVFVDESADFEMAEKIVINAKTQRPGVCNAAEKLLVHKNIAESFLPMIVKKLMTKGVEIRGCSKTVEICKQNGIEVKEATEDDWYTEYLDLII... | 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... |
A7GVZ7 | MSEILNIAKAAKASCEQLLNLSAQAKSQILNAVADELVRQKEAIKAANLLDLKAGENAGLSAALLDRLELTDARIEAMANGVREVAKFDEVVGEVLGGWRHPNGMQITKIRVPLGVLGIIYESRPNVSIDAAALALKSGNAVILRGSAAAISSNKFLVNLFNETGAKFGLPKGAVALVESTDKEAVGEMIKMHEFIDVLIPRGGKNLKDFIIQNATIPVIETGAGVCHIFVDESADVREAVEIIKNAKTQRPSTCNSVECVLLHERVAVKVLTSLARELDGVQLRVHEDLWAKFGENLGEISGDLDANLSGLKAEVKIGE... | 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... |
P53000 | MRNLLENIKKNSQKLLNLTPKDKEKIILKLAQILRENFKIILEANKKDMANFTKSGAMKDRLLLDEKRILALCEGLEKIAYIEDPIGKISKGWKNYAGLSIQKMSIPLGLICVIYEARPSLSAEIAALMIKSSNACVFKGGSEAKFTNEAIFTLVNKVLKEFDLQDCFAMFTQRDEILQILAFDDLIDVIIPRGSSNMIQEIANNTKIPLIKQNKGLCHAFVDQSANLDMALKIILNAKCQRVSVCNALETLLIHEKIAKNFISLLIPEFEKFKVKIHAHENALAYFNNSNLKIFKANENTFDTEWLDFALSVKLVKDCD... | 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... |
Q3AF39 | MDEVLNLAKKAKEASKKLAQLSTEQKNRALLKIAQYLEENMEKILTENQKDLAEAKKGGLSPAFIERLTLNEKRILDMAEGVRQVAKLPDPVGEVLGMTRRPNGLVIGQVRVPLGVVGIIYESRPNVTVDAAALCLKAGNAVILRGGKEAFNSNLALVTLMEEALRSEEIPEGAVGMIKTTSRDAANYLMRLNGYLDVLIPRGGAGLIKTVVENSTVPVIETGVGNCHVYVEEDADLEMAERIIINAKCQRPAVCNAMETLLVHEKIAPVFLPQIGKALKENGVEIRGCEVTRRYIPDALPATEEDYYTEFLDLILAVRV... | 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... |
Q3IP72 | MTETTEAKVDAAQTAALELANESDEARQENLQAIADAIDERRAEVLEANEKDVEAAEEMLEAGEYSQALVDRLKLSDAKLDSIIEMVRSVAGQEDPLGKTLTARELDDGLDLYKVSVPIGVIGTVFESRPDALVQIAALSLRSGNAVILKGGSEASHSNRVLYEIIREATADLPDGWAQLIEAREDVDRLLGMDDSVDLLMPRGSSAFVSYIQDNTSIPVLGHTEGVCHVYVDDAADLDMATDIAYDAKVQYPAVCNAVETLLVHEDVAEEYLPDIAARYAEADVEMRGDEATRSVLDRDIEAATDDDWTSEYGDLIVAI... | 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... |
Q9JZG3 | MSNTQKQLALAKAAKKSVNTADTEEKNRALLAMADSLEAATADILAANRQDLEAAAGNIPESMTDRLLLDGKRICAMADGIRAVAALPNPVGEILETSTLPNGLEIVKKRVAMGVIGIIYESRPNVTSDAAALALKSGSAVVLRSGKDAFQSARAIVAALKTGLAQTRIDPDALQLIEDTGRESSYEMMRAKDYLDLLIPRGGAGLIRAVVENAVVPVIETGTGIVHIYIDKDADWDKALRIVYNAKTSRPSVCNSMEVLLVHEDIAADFLPKLERLLVRDRIEAGLPPIRFRLDPQAARHIGGEAAGADDFDTEFLDYI... | 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... |
Q820I7 | MEKTEKIQADMQALGRAARAAARIVAKADTAVKNHALIAMARAIRCHEASLLAANAADVAQARNKGLEPAMIDRLTLTPKGIASMAAGLEQIAALSDPIGAVTDLDYRPSGIQVGRMRVPLGVIAIIYEARPNVTADAAGLCLKAGNAAILRGGSEAIQSNQAIAACVQEGLRSAGLPEHAVQVVETTDRAAVGELITMSEYVDMVVPRGGKGLIERIANEARVPVIKHLDGVCHVYVDLSADLEKAVRVADNAKTQRYGTCNTMETLLVHAGIAERFLPRICKILLEKGVELRGDEAARALVAGIKPAVEEDWYAEYLA... | 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... |
A1SHP5 | MSTQHDEHDAAGATGVADQVVAAAERARAASHGLALATRAEKDAALQAMAEALLTREPEVLAANGEDVARAEANGTPPNIVDRLRLTQERVAAMAQGLRDVAALPDPVGEVLRGSTLANGLEMRQVRVPFGVVGMIYEARPNVTADAAGICLKSGNAVLLRGSSSARSSNAAIVAALRDAIAGTGLDPDVVQQVPGDSHDSVKALMRARGHVDVLIPRGGAGLIRSVVEESTVPVIETGVGNCHVYVDRAADLDKALAIVLNAKTHRTSVCNAAESLLVHADLADTFVPRVVAALQEAGVTVHGDERFQAEDGVLPATDE... | 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... |
Q9PEM3 | MSHIRHLAQQCRDAARRLATLSTDAKRRLLETMATALNTDAATILAANAADLDAARTQQVGTAMLDRLALDPQRLAAMADALRDIAALPDPVGQVTRDDQRPNGIHVQKIRVPLGVIAMIYEARPNVTADAAALCIKAGNGIILRGGSEAIRSNIAIATALQRALRLASLPETALILVQDMARHTMLELLQLSDLIDLVIPRGGEGLIRFVAEHARIPVIKHYKGVCHQFVDASADIEMAIRLLIDGKTTRPAACNALETLLVHTDIAPRFLPAAAAALRPYGVQLRGDHATCTLLPDVVLATDADYAAEYLDLILAIRI... | 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... |
P54885 | MSSSQQIAKNARKAGNILKTISNEGRSDILYKIHDALKANAHAIEEANKIDLAVAKETGLADSLLKRLDLFKGDKFEVMLQGIKDVAELEDPVGKVKMARELDDGLTLYQVTAPVGVLLVIFESRPEVIANITALSIKSGNAAILKGGKESVNTFREMAKIVNDTIAQFQSETGVPVGSVQLIETRQDVSDLLDQDEYIDLVVPRGSNALVRKIKDTTKIPVLGHADGICSIYLDEDADLIKAKRISLDAKTNYPAGCNAMETLLINPKFSKWWEVLENLTLEGGVTIHATKDLKTAYFDKLNELGKLTEAIQCKTVDAD... | Function: Catalyzes the NADPH dependent reduction of L-gamma-glutamyl 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... |
Q2VZU1 | MSPLAAAKRLIVKIGSSLLVDDSTGQVRRGWLETLAADIAACKARGQEVIVVSSGAVAVGRRKLGLVPPLKLEEKQAAAATGQIRLAHAWQDALAHHQITVAQVLLTLDDSENRRRYLNARSTLETLLKLGAVPVINENDTVATAEIRVGDNDRLAARVAQMVSADALVLFSDIDGLYTADPRKDPDARFIPEVHELTPEIEAMAGDPGSAYGSGGMVTKLVAARICLSAGCRMAITRGEPMHPLKTIEDGGRCTWFLPNSEPRTARKQWIFGSMKPTGTLVLDAGAARALAQGRSLLPAGITEVSGAFERGDCVLVKDG... | 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): 39445
Sequence Length: 370
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: s... |
Q9ZG98 | MHGRLPLTAQTHRRLVVKVGSAVLSGPQGRQHQLAIAAQVAALRAEGREVVLVSSGAQATGMQKLGLTEKPKSMPGKQALAAVGQPTLMLLWEQAFSWYDLKVAQVLLTAEDLAHRHRYLNARQTLETLLEWGIVPIINENDTVMVEEIKFGDNDQLSALIASLVGADLLILLSDIEALYEADPRTHPEAQPIPYVERVDAGVLRMAGDSPNRVGTGGMKSKLLAAEKAQAAGIPHLLLPGTRPQSIAEALQGAPVGTLFAGGQRRYSGRKLWLYQLPKPQGEVVVDAGAAKALRQGGASLLPAGILEVRGQFGVGEAVR... | 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): 40592
Sequence Length: 377
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: s... |
Q46F79 | MTDRNEFLNDINKIVIKIGTSSLTKQNCDSTKENCSIDPTFIENIAAQVSELRKLGKEVIVVSSGAIGVGLYELGIAPKPREIPIRQAAAAVGQSILMQYWSEAFSKHGIKVAQILLTYEFYSDRVSYLNLRNSISTLLEYGVVPIINENDCTCTNEIEAIFGDNDKLSAMVASKIDADLLIILSDIDGLFDKNPKIHEDARLISLVEKITPEIESYGGDPTSFKGVGGMRTKIKAAKICSMAGCYVLIANSEIEDVLLKVLSGKEIGTLFLAERHIQKNRARWIILSRASGTIRVDAGAKAAVLGKNSLLSAGVVDVEG... | 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): 41888
Sequence Length: 383
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: s... |
Q12TG0 | MTNRKEIIGDAEKIVIKIGTTSISREDGSLNNEFMDTIASQVSELHRAGKQIILVSSGSIGIGIEILDLGCRPKEIPVRQAAAAVGQGVLMQHWTEAFQKYGLNVAQILLTYDSFTNRLTYLNLRNSISTLLSYGVIPIINENDPICVHEIEATLGDNDKLSAMVASKMEADLLILFTDIDGLYDKNPKRHDDAVLLRTVEEITPTIESYGGNPTSMKGVGGMRTKIDAAKICNISGCYMVIANSNVDDGIRRILDGEELGTLFLTNQFVHKNRIRWIILARSSGSIVVDTGAKEALAKRMSLLPSGVLGVAGTFDRGDI... | 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): 40967
Sequence Length: 375
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: s... |
B0JFY2 | MNQTIVIKIGTSSLTDNETGQLSLSTIAALVEVLTRLRAAGHRVVLVSSGAVGVGCRRLGIQERPKKIALKQAIAAVGQGRLMRIYDDLFTSLGQPIAQILLTRPELMERTCYVNAYNTFQALFELGVIAIVNENDTVAIDELKFGDNDTLSALVASLIEADWLFILTDVDRLYSADPRLFPEAAAIARVSPAELAQLSIDAGSSGSQWGTGGMATKLAAARIATSAGVEMAITRGRQPGNILKIMAGEAIGTRFEAQKRSDNARKRWIAYGLLPMGKIYLDAGAIQAICQGGKSLLAAGITKVEGEFSASESVQLCDQE... | 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): 40526
Sequence Length: 379
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: s... |
Q1GQZ4 | MSLFPPASCPRLIVKIGSALLVDPGGAVRRDWLTGIAADIAERARAGQQVAVVSSGAIALGARRLGLAKGGRASLEDAQAAAATGQIALSQVWAEVLGAEGLTAAQMLVTLGDLEHRRRYLNAAATLDRLLSLGVVPIINENDSVATEEIRFGDNDRLAARVAQAAAARGVILLSDIDGLYDRNPAQPGAVHIERIERIDAAIEAMADTGSASGMGSGGMVSKIAAARIANAAGAHLAIASGRIDRPLSTAARHSLFVAERGASARKAWLAGGLTAEGRLTIDAGAVKALVGGASLLAAGVTAVSGSFARGDILDIVGPD... | 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): 37406
Sequence Length: 368
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: s... |
Q9RDJ9 | MAGARQAVGEARRIVVKVGSSSLTTAAGGLDADRVDALVDVLAKMRGADKEVVLVSSGAIAAGLAPLGLPRRPRDLARQQAAASVGQGLLVARYTASFARYGVRVGQVLLTSDDMSRRAHHRNASRTLDKLLAMGAFPIVNENDTVATDEIRFGDNDRLAALVAHLVRADLLVLLSDVDGVYDGDPSRPGTSRLAEVRDMGDLAGVDIGSAGKAGVGTGGMVTKVEAARIAAAAGIPVVLTSAVHAADALAGGDTGTYFHATGRRSADRLLWLQHASAPQGALVLDDGAVRAVVEGRKSLLPAGIAGVEGDFAAGDPVEL... | 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): 38840
Sequence Length: 374
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: s... |
A4KA41 | MSWQAYVDEHLMCEIDGHHLSAAAIIGHDGSVWAQSSTFPQFKPEEIAAIIKDFDEPGSLAPTGLHLGGIKYMVIQGESGAVIRGKKGAGGITVKKTSQALIFGIYDEPLTPGQCNMIVERLGDYLLKQGL | Function: Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations (By similarity).
PTM: Phosphorylated by MAP kinases.
Sequence Mass (Da): 14083
Sequence Length: 131
Subcellular Location: Cytoplasm
|
Q9FR39 | MSWQAYVDDHLLCDIEGQHLSAAAIVGHDGSVWAQSENFPELKPEEVAGMIKDFDEPGTLAPTGLFVGGTKYMVIQGEPGVVIRGKKGTGGITIKKTGMSLIIGIYDEPMTPGQCNMVVERLGDYLIEQGF | Function: Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG. Has a high affinity for poly-proline.
PTM: Phosphorylated by MAP kinas... |
O14011 | MFCSISGETPKEPVISRVSGNVYEKRLIEQVIRETSKDPVTQQECTLEDLVPVKVPDFVRPRPPSATSLPALLSLFQEEWDSVALEQFELRRNLTETKQELSTALYSLDAALRVISRLTKERDEAREALAKFSDNIGTVSSKTIEVQEVEMGESDDQLKTSLRSTVEKTFQELSSKRKRTKLQPKWATDDAVSQLLQATPSTILENLETESTTSFFPSPENSSFVLCLHKDELLCLDIQSNSTLKIFEGSALACCWLTSSKIAVATADAISIFEFPVSSSGLQSVGEPTSSIPIDEKVNFLQAHPSGEYLLAASNEKCYI... | Function: Probable ubiquitin-protein ligase involved in pre-mRNA splicing (By similarity). May also function in DNA repair (By similarity).
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acce... |
P32523 | MLCAISGKVPRRPVLSPKSRTIFEKSLLEQYVKDTGNDPITNEPLSIEEIVEIVPSAQQASLTESTNSATLKANYSIPNLLTSLQNEWDAIMLENFKLRSTLDSLTKKLSTVMYERDAAKLVAAQLLMEKNEDSKDLPKSSQQAVAITREEFLQGLLQSSRDFVARGKLKAPKWPILKNLELLQAQNYSRNIKTFPYKELNKSMYYDKWVCMCRCEDGALHFTQLKDSKTITTITTPNPRTGGEHPAIISRGPCNRLLLLYPGNQITILDSKTNKVLREIEVDSANEIIYMYGHNEVNTEYFIWADNRGTIGFQSYEDDS... | Function: Probable ubiquitin-protein ligase involved in pre-mRNA splicing. Acts as a central component of the NTC complex (or PRP19-associated complex) that associates to the spliceosome to mediate conformational rearrangement or to stabilize the structure of the spliceosome after U4 snRNA dissociation, which leads to ... |
P55798 | MKQPAPVYQRIAGHQWRHIWLSGDIHGCLEQLRRKLWHCRFDPWRDLLISVGDVIDRGPQSLRCLQLLEQHWVCAVRGNHEQMAMDALASQQMSLWLMNGGDWFIALADNQQKQAKTALEKCQHLPFILEVHSRTGKHVIAHADYPDDVYEWQKDVDLHQVLWSRSRLGERQKGQGITGADHFWFGHTPLRHRVDIGNLHYIDTGAVFGGELTLVQLQ | Cofactor: Binds 2 manganese ions per subunit.
Function: Plays a key role in signaling protein misfolding via the CpxR/CPXA transducing system. It also modulates the phosphorylated status of many phosphoproteins in E.coli, some of which acting as major chaperones. Has been shown, in vitro, to act on Ser, Thr and Tyr-pho... |
O44249 | MTDAKNNLLYFFDRPNEPCFMQKGEDKVVFEIPDHYYPDKYKSLSNTLSNRFGNEATKRIPIRNITLPNLEVPMQLPYNDQFSLFVPKHRTMAAKLIDIFMGMRDVEDLQSVCSYCQLRINPYMFNYCLSVAILHRPDTKGLSIPTFAETFPDKFMDSKVFLRAREVSNVVISGSRMPVNVPINYTANTTEPEQRVAYFREDIGINLHHWHWHLVYPFDSADRSIVNKDRRGELFYYMHQQIIGRYNVERMCNGLPQVKPFSDFSAPIEEGYFPKLDSQVASRTWPPRFAGSVFRNLDRTVDQVKIDVRKLFTWRDQFLE... | Cofactor: Binds 2 copper ions per subunit.
Function: This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the rate-limiting conversions of tyrosine to DOPA, DOPA to DOPA-quinone and possibly 5,6 dihydroxyindole to indole-5'6 quinone... |
Q8ZNY9 | MMRPEEIYQRIEAKNWRHVWVVGDIHGCFSMLMKRLRECRFDPQQDLLVSVGDLIDRGPDSLGCLALLRESWMTAVRGNHEQMALDARASSQSTLWLMNGGDWFTRLTAEHAAQAEALFILCQRLPWILEVRCRHSTHVIAHADYPASTYQWQKKVDLHQVLWSRERLINKRGGISGADHFWFGHTPLRRRMDFANVHYIDTGAVFGGQLTLARIQ | Function: Can hydrolyze phosphorylated Ser-, Thr- or Tyr-substrates in vitro. The natural substrate is unknown.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 25037
Sequence Length: 216
EC: 3.1.3.16
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P85046 | MRDPFFYRWHSYIDDIFQEHKERLRPYTEAQLNFNGITVTGVQVAPERGPTNTFQTSWQQSDVDLSRGMDFVAPRGNVTARFTHLNHTPFTYSIQVNNSSGAQRMGMVRIFLAPKTDERGNEMLFRDQRLMMIEMDKFVVSMRPGQNTIRRRSTESTVTIPFERTFRSLEESRPDQTTDAQQQFNFCGCGWPHHM | Cofactor: Binds 2 copper ions per subunit.
Function: This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the rate-limiting conversions of tyrosine to DOPA, DOPA to DOPA-quinone and possibly 5,6 dihydroxyindole to indole-5'6 quinone... |
F4IE66 | MPSMAQGELKSFVQNSRPNPKSPTVSPFSMRQKIAEHRRSLPIASVEKRLVEEVQKNDILIIVGETGSGKTTQLPQFLYNAGFCREGKMIGITQPRRIAAVTVAKRVAEECEVQLGQKVGYSIRFDDTTSGSTRLKYMTDGLLLREALLDPHLSRYSVIIVDEAHDRSVHTDVLLALLKKIQRTRSQPVSEKTEFGNVASQVQTTTRDANGPQQNGVLKGYQGRKLSPLKLIIMSASLDARVFSEYFGGAKAVHVQGRQFPVDILYTVHPESDYVDATLVTIFQIHFEEKPGDILVFLTGQDEIESVERLVQERLQNIPE... | Function: Involved in pre-mRNA splicing. Plays a role during development in processes such as meristem maintenance, leaf morphogenesis and root morphogenesis.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 80515
Sequence Length: 717
Subcellular Location: Nucleus
EC: 3.6.4.13
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Q81GJ7 | MKYDIIGDIHGCFQEFQNLTEKLGYNWSSGLPVHPDQRKLAFVGDITDRGPHSLRMIEIVWELVIHKKEAYYAPGNHCNKLYRFFLGRNVTVAHGLETTVAEYEALPSHKQNIIKEKFITLYEQSPLYHILDEKRVIVCHAGIRQDYIGRRDKKVQTFVLYGDITGEKHADGSPVRRDWAQEYKGQAWIVYGHTPVAEPRFVNQTVNIDTGAVFGGKLTGLRYPEMETISVPSSLPFVAEKFRPIS | Function: Asymmetrically hydrolyzes Ap4p to yield AMP and ATP.
Catalytic Activity: H2O + P(1),P(4)-bis(5'-guanosyl) tetraphosphate = GMP + GTP + 2 H(+)
Sequence Mass (Da): 28192
Sequence Length: 246
EC: 3.6.1.17
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O31614 | MAYDIISDIHGCYDEMTALIQKLGYTIKNGVPVHEEGRVLVFAGDLTDRGPKSIEVIRFVAGAYEKGAVRYVPGNHCNKLYRYLKGNPVKVMHGLETTAAELEELSKDEKKSVSEQFMKLYETAPLYDILHNGELVVAHAGIRADDIGKYTRRVKDFVLYGDVTGETYPDGRPIRRDWAAAYNGKAWVVYGHTPVKEPRKVNRTINIDTGCVFGNQLTGFRFPEIETVSVPSSLPYDESRFRPI | Cofactor: Nickel. 100-fold less efficiency with manganese.
Function: Asymmetrically hydrolyzes Ap4p to yield AMP and ATP. Does not hydrolyze Ap2a or Ap6A. Also has an ATPase activity. Was shown to dephosphorylate phosphotyrosine but not phosphoserine or phosphothreonine from phosphorylated peptides. Involved in spore g... |
Q5L1R3 | MQVDIIGDIHGCFREFAALTETLGYHWDEGVPIHPDGRKLGFVGDLTDRGPESLNMIEIVCALVERNLAYYVPGNHCNKLYRFFLGRNVQIAHGLETTVAEYRTLPPSEQEMIRRKFIRLYEQAPLYAVLDEGRLVIAHAGIRHDYIGRTDKKVKTFVLYGDITGEMNQDGTPVRRDWAKRYHGSAWVVYGHTPVEKPRFVGRTVNIDTGCVFGGALTALRYPEMETVSVPSSMPFVPEKFRTFS | Function: Asymmetrically hydrolyzes Ap4p to yield AMP and ATP.
Catalytic Activity: H2O + P(1),P(4)-bis(5'-guanosyl) tetraphosphate = GMP + GTP + 2 H(+)
Sequence Mass (Da): 27839
Sequence Length: 245
EC: 3.6.1.17
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Q9K907 | MQFDIIGDVHGCYDELMELIDKLGYEYKRGSYDHPDGRLLAFVGDLTDRGPHSLEVIRLVSHMVKKKTAYYVPGNHCNKLYRYMIGRKVQVKHGLETTVAELNALSEEERIEVIAQFKELYEQAPLYHSFPEDKLVITHAGIREDDIGSYGKRVETFVLYGDITGETNPDGTPVRRDWAATYQGDWWIVYGHTPVRRPRIIHRTVNIDTGCVFGGALTALRFPEIEFVSIPSRQPLVSEKFRNFPG | Function: Asymmetrically hydrolyzes Ap4p to yield AMP and ATP.
Catalytic Activity: H2O + P(1),P(4)-bis(5'-guanosyl) tetraphosphate = GMP + GTP + 2 H(+)
Sequence Mass (Da): 28191
Sequence Length: 246
EC: 3.6.1.17
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P55912 | MSFSEFYQRSINEPEAFWAEQARRIDWRQPFTQTLDHSRPPFARWFCGGTTNLCHNAVDRWRDKQPEALALIAVSSETDEERTFTFSQLHDEVNIVAAMLLSLGVQRGDRVLVYMPMIAEAQITLLACARIGAIHSVVFGGFASHSVAARIDDARPALIVSADAGARGGKILPYKKLLDDAIAQAQHQPKHVLLVDRGLAKMAWVDGRDLDFATLRQQHLGASVPVAWLESNETSCILYTSGTTGKPKGVQRDVGGYAVALATSMDTIFGGKAGGVFFCASDIGWVVGHSYIVYAPLLAGMATIVYEGLPTYPDCGVWWK... | Function: Catalyzes the synthesis of propionyl-CoA from propionate and CoA. Also converts acetate to acetyl-CoA but with a lower specific activity.
Catalytic Activity: ATP + CoA + propanoate = AMP + diphosphate + propanoyl-CoA
Sequence Mass (Da): 69334
Sequence Length: 628
Pathway: Organic acid metabolism; propanoate d... |
P28708 | MDEYSSIYSQPKTPRLKQEGFPDSIGDQHEKALIDENGEEDKKMASTEGTTGDSRSTPLTVSIPTFENVQALPTPMTYTPLSPGNLSMSPIDQSSLNIPKRRSHARLLDDMLSVTQPNQRVVSELIAPANLSPQRVVSLPTVTEEALVNDSVDSDNYTKEPYFPESSSSTEKCDDDIFQGFLLDHWDRPLLWKKVRPIGSGNFSTVLLYELMDQSNPKLKQVAVKRLKYPEELSNVEQINTSLRYKETLSRLENSLTRELQVLKSLNHPCIVKLLGINNPIFVTSKKPLCDLIIKTPRALPPCDMIMSYCPAGDLLAAVM... | Function: Protein kinase that functions as regulator in the pheromone-induced mating pathway downstream of mitogen-activated protein kinase (MAPK) FUS3. Diminishes transcriptional induction of genes in response to pheromone signaling.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein... |
Q12310 | MSLSRILRYNQRNNKTTASLTAEHAYSDNWAYSVSLGDPTSVGVNMAAKTGEALNKSYDSVFSSLPVADSVPRTDFTASSRDDENTDVQKLTTSWMEKIDTKMPENISKIDSNIISSPMVSKVEARFIVPKGRLRKNSTDFTSSFSNSLSLPKSYGKLIFFTSKKNSSSTKKNLANDISDNKHNNNSSNTIGHNIPVTTATATCDEIACTSTEHEYNVYEEERMFTTRVYSLEDSVSSLSTNPLDDTYSEAVQVNTRHIEDTESTAHIRKHSYTTSLSSIKRLFKITSFSNNNSNSCDHQESTVADDCAISSSLKETTSS... | Function: Protein kinase that functions as regulator in the pheromone-induced mating pathway downstream of mitogen-activated protein kinase (MAPK) FUS3. Diminishes transcriptional induction of genes in response to pheromone signaling.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein... |
P33297 | MATLEELDAQTLPGDDELDQEILNLSTQELQTRAKLLDNEIRIFRSELQRLSHENNVMLEKIKDNKEKIKNNRQLPYLVANVVEVMDMNEIEDKENSESTTQGGNVNLDNTAVGKAAVVKTSSRQTVFLPMVGLVDPDKLKPNDLVGVNKDSYLILDTLPSEFDSRVKAMEVDEKPTETYSDVGGLDKQIEELVEAIVLPMKRADKFKDMGIRAPKGALMYGPPGTGKTLLARACAAQTNATFLKLAAPQLVQMYIGEGAKLVRDAFALAKEKAPTIIFIDELDAIGTKRFDSEKSGDREVQRTMLELLNQLDGFSSDDR... | Function: The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity).
PTM: N-acetylated by NAT1.
Sequence Mass (Da): 48256
Sequence Length: 434
Subcellular Location: Cyt... |
P33298 | MEELGIVTPVEKAVEEKPAVKSYASLLAQLNGTVNNNSALSNVNSDIYFKLKKLEKEYELLTLQEDYIKDEQRHLKRELKRAQEEVKRIQSVPLVIGQFLEPIDQNTGIVSSTTGMSYVVRILSTLDRELLKPSMSVALHRHSNALVDILPPDSDSSISVMGENEKPDVTYADVGGLDMQKQEIREAVELPLVQADLYEQIGIDPPRGVLLYGPPGTGKTMLVKAVANSTKAAFIRVNGSEFVHKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGSDREVQRILIELLTQMDGFDQSTNVKVIMATNR... | Function: The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity).
PTM: N-acetylated by NAT3.
Sequence Mass (Da): 47894
Sequence Length: 428
Subcellular Location: Cyt... |
Q9V2V6 | MQGQAQQQAYDRGITIFSPDGRLYQVEYAREAVKRGTASIGVRTPEGVVLAADKRSRSPLMEPTSVEKIHKADDHIGIASAGHVADARQLIDFARRQSQVNRLRYGEPIGIETLTKEVTDHIQQYTQVGGARPFGVALLIGGVENGTPRLYETDPSGTPYEWKAVSIGADRGDHQEHLEENFRDDLTLDEGIELALEAIASTSDEGTAPDGVDVATVSAETERFVELSNDEIESYLEANDLLATEDDEQTEE | Function: Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The H.volcanii alpha1-beta proteasome is able to cleave oligopeptides after Phe, Tyr and Trp, poorly after Glu but not after Arg. Thus, displays chymotrypsin-like activity, low caspase-like activ... |
Q9R1P4 | MFRNQYDNDVTVWSPQGRIHQIEYAMEAVKQGSATVGLKSKTHAVLVALKRAQSELAAHQKKILHVDNHIGISIAGLTADARLLCNFMRQECLDSRFVFDRPLPVSRLVSLIGSKTQIPTQRYGRRPYGVGLLIAGYDDMGPHIFQTCPSANYFDCRAMSIGARSQSARTYLERHMSEFMECNLDELVKHGLRALRETLPAEQDLTTKNVSIGIVGKDLEFTIYDDDDVSPFLDGLEERPQRKAQPSQAAEEPAEKADEPMEH | Function: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus p... |
Q53080 | MTMPYYASAEQIMRDRSELARKGIARGRSVVVLTFRDGVLFVAENPSTALHKVSELYDRLGFAAVGKYNEFENLRRAGIVHADMRGYSYDRRDVTGRSLANAYAQTLGTIFTEQPKPYEVEICVAEVGRVGSPKAPQLYRITYDGSIVDEQHFVVMGGTTEPIATAMRESYRADLDLEAAVGIAVNALRQGGAGEGEKRNVDVASLEVAVLDQSRPRRAFRRIAGTALEQLVPAEPAAASESAPEPKPDTETKPADTQD | Function: Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The R.erythropolis proteasomes are able to cleave oligopeptides after Tyr, Phe and Leu, very poorly after Arg but not after Glu. Thus, displays chymotrypsin-like activity, low trypsin-like activi... |
O64750 | MAASSSHLFALPSPASPFLSAPNRNRVRVLAKSCPENQSFDSNDSDSSSETTHKAQGDQKSVSRRQWMTACVCASAALISNSYTFVSVQSAAALDKKPGGSCRNCQGSGAVLCDMCGGTGKWKALNRKRAKDVYEFTECPNCYGRGKLVCPVCLGTGLPNNKGLLRRPGARELLEKMYNGRLLPDS | Cofactor: Binds 2 Zn(2+) ions per monomer.
Function: Involved in female gametophyte development. Required for embryo sac development . Nuclear genome-encoded factor required for the accumulation of photosystem I (PSI) during plant development . Required for light acclimation and chloroplast development .
Sequence Mass ... |
P58575 | MVQRGSKVRILRPESYWFQDVGTVASVDQSGIKYPVIVRFDKVNYAGINTNNFAVDELIEVEAPKAKAKK | Function: Stabilizes the interaction between PsaC and the PSI core, assists the docking of the ferredoxin to PSI and interacts with ferredoxin-NADP oxidoreductase.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 7886
Sequence Length: 70
Subcellular Location: Cellular thylakoid membrane
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Q9WWP1 | MVQRGSKVRILRPESYWFQDVGTVASVDQSGIKYPVIVRFEKVNYSGINTNNFAEDELVEVEAPKAKPKK | Function: Stabilizes the interaction between PsaC and the PSI core, assists the docking of the ferredoxin to PSI and interacts with ferredoxin-NADP oxidoreductase.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 7958
Sequence Length: 70
Subcellular Location: Cellular thylakoid membrane
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P69403 | MERGSKVKILRKESYWYQEIGTVAAMDKSGIKYPVLVRFEKVNYNNVNTNSFADNELIDLGK | Function: Stabilizes the interaction between PsaC and the PSI core, assists the docking of the ferredoxin to PSI and interacts with ferredoxin-NADP oxidoreductase.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 7172
Sequence Length: 62
Subcellular Location: Plastid
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Q7V8Y4 | MAISKGDKVRIRREESYWHNEVGTVASVDTTGKYGVLVRFEKTNYFGMQGTDNGNLTNSFAESELDRA | Function: Stabilizes the interaction between PsaC and the PSI core, assists the docking of the ferredoxin to PSI and interacts with ferredoxin-NADP oxidoreductase.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 7648
Sequence Length: 68
Subcellular Location: Cellular thylakoid membrane
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P12354 | MASIASSVAVRLGLTQVLPNKNFSSPRSTRLVVRAAEEAAAAPAAASPEGEAPKAAAKPPPIGPKRGSKVRIMRKESYWYKGVGSVVAVDQDPKTRYPVVVRFNKVNYANVSTNNYALDEIQEVA | Function: Stabilizes the interaction between PsaC and the PSI core, assists the docking of the ferredoxin to PSI and interacts with ferredoxin-NADP oxidoreductase.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 13367
Sequence Length: 125
Subcellular Location: Plastid
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Q85FK2 | MQHVKIYLSTAPVVATIWFGLLAGLLIEINRFFPDALLFPFP | Function: May help in the organization of the PsaE and PsaF subunits.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 4761
Sequence Length: 42
Subcellular Location: Plastid
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P56769 | MRDLKTYLSVAPVLSTLWFGSLAGLLIEINRLFPDALTFPFFSF | Function: May help in the organization of the PsaE and PsaF subunits.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 5009
Sequence Length: 44
Subcellular Location: Plastid
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A0QZ46 | MSFPYFISPEQAMRERSELARKGIARGRSVVALAYSEGVLFVAENPSRSLQKVSELYDRVGFAAVGRFNEFDNLRRGGIQFADTRGYAYDRRDVTGRQLANVYAQTLGTIFTEQAKPYEVELCVAEVAHYGETKAPELYRITYDGSIADEPHFVVMGGTTEPIIAALNESYTENASLQDAVEIAVKALSASAEGAEPRSLGPSTLEVAILDAGRPRRAFRRITGAALEALLPEQPQQADSGDKPTE | Function: Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The M.smegmatis proteasome is able to cleave oligopeptides after hydrophobic residues, thus displaying chymotrypsin-like activity. In complex with the ATPase Mpa, degrades protein targets conjuga... |
B7EA73 | MDLPKEIFLKEYKKPDYLFDSVNLEFQLGEDKTIVTSKIAVSPGTEGTSSPLTLHGRDLKLLSIKVNGKDLKSEDYMVDSRHLTVSRPPGGTFNLEIVTEIYPQLNTSLEGLYKSTGNFCTQCEAEGFRKITYFQDRPDVMATYTCRIEADKTLYPVLLSNGNLIEQGDLEGGKHYALWEDPFKKPSYLFALVAGQLDCREDSFTTCSGRKVTLRIWTPGQDLAKTAHAMYSLKAAMKWDEEVFGLEYDLDLFNIVVVPDFNMGAMENKSLNIFQSRLVLASPETATDGDYAAILGVVGHEYFHNWTGNRVTCRDWFQLT... | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: Release of an N-terminal amino acid, preferentially alanine, from a wide range of peptides, amides and arylamides.
Sequence Mass (Da): 99524
Sequence Length: 887
EC: 3.4.11.14
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Q9YER0 | MAEWIAGGLEGPAGRGLDERVVRSGTTTVGLIASDHVILAADKRATAGFLIASRRVKKIVMLSNYVAMTVSGLVADAQILSDVLREEIRLYEMTNKVKPSVRFVASLLSNILFSSKFFPYIVQLIVGGYDTQPRLYTLDLFGSITEDKYTATGSGSPIAYGVLEERYREDLSVEEAIKVATTAIRSAVLRDAASGDGADVVVIGPQGYEEKFIPYNSLV | 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): 23702
Sequence Length: 219
Subcellular Location: Cytoplasm
EC: 3.4.25.1
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A8M8R5 | MSDQLELMTGTTVGIKAKDGVVLAAEKRVSYGFYLMSKSGKKVYPITNRIGLASSGILADIQTITKVIRANIANMEIEMKRPVSVRAAAKLLSIMLFQNKYMPYIAETMVGGIDEEGPKLFILDSWGSLIEDDFAALGNGARTAIGLIETGYSSSITVKEAKELAIKAIKEAIARDPTSGDGIDTLVITGNGYLEDSIKL | 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): 21484
Sequence Length: 200
Subcellular Location: Cytoplasm
EC: 3.4.25.1
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A0RXV1 | MSNNVEEKILHGTTTVGIKATDGVVLCADMRASAGYFIANNNTMKIQRIDDHAGLTLAGGVADAQNIVDVLRYHASLHRIRKQGPIPIKSLARLTSLIFHQNRGYPFMADILMGGFDAVGPALYNIDMFGSVEEKSYVTTGSGSPVAYGTLEEEYRADLTADEAKGVALRAVKAAITRNIGTGDGINVAVINGNGFELLTREQKKAVIAL | 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): 22452
Sequence Length: 210
Subcellular Location: Cytoplasm
EC: 3.4.25.1
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B8D683 | MREAVSKTTTVGLVTGDYVVLAADKRATAGPMVYHKAVKKISKITDYAALTISGLVADAQYIVENARYIAREYEIEMGGPIPIKALASRISLILSVYLRYSPFIVQLLLGGRDSTGASLYYMDLYGSVTREKYMATGSGSPVAFGILEKNYRSDLSLEEAKKLAFNAVSSAIMRDGFSGEGVDIVVIGPGIYSEETIPLKKTIESS | 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): 22270
Sequence Length: 206
Subcellular Location: Cytoplasm
EC: 3.4.25.1
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P16033 | MTTTLQQRESASLWEQFCQWVTSTNNRIYVGWFGTLMIPTLLTATTCFIIAFIAAPPVDIDGIREPVAGSLLYGNNIISGAVVPSSNAIGLHFYPIWEAASLDEWLYNGGPYQLVVFHFLIGIFCYMGRQWELSYRLGMRPWICVAYSAPVSAATAVFLIYPIGQGSFSDGMPLGISGTFNFMIVFQAEHNILMHPFHMLGVAGVFGGSLFSAMHGSLVTSSLVRETTEVESQNYGYKFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLGAWPVIGIWFTAMGVSTMAFNLNGFNFNQSILDSQGRVIGTWADV... | 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... |
Q3M5L6 | MSTIVQRQKEFNFFDLWDSFCAWITSTENRIYIGWFGVLSIPTLLAATTCFVLAFIAAPSVDMDGIREPIMGSLMDGNNLITAAVVPTSAAIGLHFYPIWEAASMDEWLYNGGPYQLIVLHFLIGIWCLLGRFWELSYRLGMRPWIAVAYSAPVIAATSVLLVYPIGQGSFSDGLPLGIAGTFHFMLAFQGDHNILMHPFHMLGVAGVFGGALLSSLHGSLVASTLIRNTDENESINGGYKLGQQQVTYKYLAGHNSFLGRLLIPTFASRNHRAFHFLLAALPTIGIWFAAMGVCSMAFNLNGLNFNHSILDSRGNVIRS... | 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... |
P06007 | MTIAIGTYQEKRTWFDDADDWLRQDRFVFVGWSGLLLFPCAYFALGGWLTGTTFVTSWYTHGLATSYLEGCNFLTAAVSTPANSMAHSLLFVWGPEAQGDFTRWCQLGGLWAFVALHGAFGLIGFMLRQFEIARSVNLRPYNAIAFSAPIAVFVSVFLIYPLGQSGWFFAPSFGVAAIFRFILFFQGFHNWTLNPFHMMGVAGVLGAALLCAIHGATVENTLFEDGDGANTFRAFNPTQAEETYSMVTANRFWSQIFGVAFSNKRWLHFFMLLVPVTGLWMSAIGVVGLALNLRAYDFVSQEIRAAEDPEFETFYTKNIL... | 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. There is also a Cl(-1) ion associated with D1 and D2, which is r... |
P13554 | MSGSTGERSFADIITSIRYWIIHSITIPSLFIAGWLFVSTGLAYDVFGSPRPNEYFTETRQGIPLITGRFDSLEQLDEFSRSF | Cofactor: With its partner (PsbF) 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... |
A0T0A3 | MSGGSTGERPFSDIITSVRYWIIHSITIPSLFVSGWLFVSTGLAYDVFGTPRPNEYFTQDRQQIPLVNDRFSAKQELEDLTKGL | Cofactor: With its partner (PsbF) 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... |
Q0P3N7 | MSVKTYPIFTFRWLAVHALAVPTVFFLGSITAMQFIQR | 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... |
Q70Y13 | MLTLKLFVYTVVIFFVSLFIFGFLSNDPGRNPGRDE | 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... |
B0YPM8 | MPTLKLFVYAIVIFFVSPFVFGFLSNDPGRNPGRKD | 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... |
P62100 | MLTLKLFVYTVVIFFVSLFIFGFLSNDPGRNPGREE | 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... |
Q06J30 | MLILKSFVYTVVASFVSLFIFGFLSNDPGRRPGRKRI | 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... |
P56338 | MSNTGTTGRIPLWLVGTVAGTAALTLVAVFFYGSYVGLGSSL | 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 ... |
Q8YYG5 | MEAALLLAKLPEAYQIFDPLVDVLPIIPVFFLLLAFVWQAAVGFR | 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 ... |
Q6ENJ4 | MPNILSLTCICFNSVIYPTSFFFAKLPEAYAIFNPIVDFMPVIPVLFFLLAFVWQAAVSFR | 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 ... |
Q7U9L1 | MASFTLDLLAQLPEAYQAFSPLIDILPLIPVFFLLLAFVWQASVGFR | 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 ... |
P28642 | MLNIFSLVCICINSALYSSSFFLGKLPEAYAFLNPIVDFMPVIPLL | 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 ... |
Q85X47 | MEVNNLGFIAVLMFLAIPTAFLLIPYVKTASASSGSN | 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 ... |
P41608 | MEVNTLAFIAVLLFLAVPTAFLLIPYVKTASASSGSN | 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 ... |
Q1XDG2 | METATVLSIFISSLLLGITGYSIYTAFGPASKDLRDPFEEHEE | Function: May play a role in photosystem I and II biogenesis.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 4750
Sequence Length: 43
Subcellular Location: Plastid
|
A8HPM2 | MAMTLSTKAFAQRGVSARKNTVRVYAASTKVNPKLASKTEVERFKQATGLPAPAINGKQFPLKLGFTKTNELFVGRLAMVGFSASLIGEILTGKGALAQFGYETGLNGIEVDGLVIGLIAFNLIAAVLPTSQTFVPEEQDTISERPAGPLQDPRITLLEPKKFFGVQGFGFTKENELFVGRAAQLGFAFSLIGEAVTGKGALAQFDIETGLSLRDTEFGLVVFILFLLFAAINEGSGKFVDEESA | Function: Required for non-photochemical quenching (NPQ), a mechanism that converts and dissipates the harmful excess absorbed light energy into heat and protect the photosynthetic apparatus from photo-oxidative damage . Seems involved in the activation of NPQ, possibly by promoting conformational changes required for ... |
Q0J8R9 | MALQQSMAMPMMVVSDLGTAPRSSPMVQLQRMKKHLVVVAAFKSRTKASPKVDKSNKNKSIVEDGIFGTSGGIGFTKENELFVGRVAMLGFAASLLGEAVTGKGILAQLNLETGIPIYEAEPLLLFFILFTLLGAIGALGDRGRFVDDATGLERAVIPPGKGFRAALGLSEGGPLFGFTKANELFVGRLAQLGIAFSLIGEIITGKGALAQLNIETGVPINEIEPLLLFNILFFFFAAINPGTGKFVTDDNDDQ | Function: Involved in high light-mediated energy-dependent nonphotochemical quenching (NPQ, qE) and thermal dissipation (TD) thus regulating energy conversion in photosystem II and protecting from photoinhibition . Seems also to regulate quantum yield of electron transport in fluctuating light conditions .
Location Top... |
Q9XF91 | MAQTMLLTSGVTAGHFLRNKSPLAQPKVHHLFLSGNSPVALPSRRQSFVPLALFKPKTKAAPKKVEKPKSKVEDGIFGTSGGIGFTKANELFVGRVAMIGFAASLLGEALTGKGILAQLNLETGIPIYEAEPLLLFFILFTLLGAIGALGDRGKFVDDPPTGLEKAVIPPGKNVRSALGLKEQGPLFGFTKANELFVGRLAQLGIAFSLIGEIITGKGALAQLNIETGIPIQDIEPLVLLNVAFFFFAAINPGNGKFITDDGEES | Function: Plays an important role in non-photochemical quenching, a process maintains the balance between dissipation and utilization of light energy to minimize generation of oxidizing molecules, thereby protecting the plant against photo-oxidative damage. Is not necessary for efficient light harvesting and photosynth... |
Q85FJ6 | MEALVYTFLLVATLGIIFFAIFFREPPKVPNRGK | Function: Seems to play a role in the dimerization of PSII.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3900
Sequence Length: 34
Subcellular Location: Plastid
|
Q67I71 | MEALVYTFLLVSTLGIIFFAIFFREPPKVPTKKMK | Function: Seems to play a role in the dimerization of PSII.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 4077
Sequence Length: 35
Subcellular Location: Plastid
|
B2J1B5 | MDIDYRIAIVLAPVVIAASWAVFNIGAAALRQIQGFLDREA | 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): 4459
Sequence Length: 41
Subcellular Location: Cellular thylakoid membrane
|
P59908 | MLGIDARLFLVVAPILAAVSWAAFNIGRAAVGQLQLLIKRSRA | 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): 4592
Sequence Length: 43
Subcellular Location: Cellular thylakoid membrane
|
Q7VD03 | MLNLLVITLPILAAIGWVTLNIQKPAREQWDRQFGDNKPF | 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): 4621
Sequence Length: 40
Subcellular Location: Cellular thylakoid membrane
|
P59909 | MILIVLLPILLAATWAFINIRGAALKQQGLGLVSKNKG | 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): 4046
Sequence Length: 38
Subcellular Location: Cellular thylakoid membrane
|
Q31KZ4 | MVILFQLALLLLVVMSFVLIVGVPVLYATNGDRVQSNRLILVGGLAWTALVVLVGVLNYFVV | Function: Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 6714
Sequence Length: 62
Subcellular Location: Cellular thylakoid membrane
|
Q2JXZ7 | MMLIFQIALLVLVLYSLLLVVAVPVLFSSASDWSRAKNVILVGSLLWVLMVIGVGVLSFFK | Function: Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 6694
Sequence Length: 61
Subcellular Location: Cellular thylakoid membrane
|
Q8DHJ2 | MTILFQLALAALVILSFVMVIGVPVAYASPQDWDRSKQLIFLGSGLWIALVLVVGVLNFFVV | Cofactor: PSII binds multiple chlorophylls, carotenoids and specific lipids.
Function: Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna. May also aid in binding of PsbK, Ycf12 and the oxygen-evolving complex to PSII, at least in vitro. PSII is a light-driven water plastoquinone ... |
P49528 | MITALVALLVFISLGLVITVPVALATPGEWEASKSTFTRAFQAWVGLVIVIAAADGISSAI | Function: Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 6271
Sequence Length: 61
Subcellular Location: Plastid
|
C7LYP7 | MRKDGARLALPLFDPRHDPGPDFAALVSRDAARTVPTSGDGSLGAQVPHGTTIAALRFAGGVVIAGDRRATEGNFIANRTIEKVFPADRFSGVGIAGAAGPAVEMVRIFQVQLEHYEKVEGKALSLEGKANQLAQMIRQNLPLAMQGLVVMPLFAGWDAERSEGRIFTFDVAGGRYEEVAYYAIGSGGRDARATLKLGWRPGLDEAGAVHLAVQALYEAAQEDAATGGPDALRGIFPVVAVIDREGYRRIDDARLEEIAVELDQAVRERGARR | 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): 29247
Sequence Length: 273
Pathway: Protein degradation; proteasomal Pup-dependent pathway.
Subcellu... |
Q493W4 | MLEKIQILLQYLLPKYWITYLVGLGASWKGGWITRYAILLFIHIYKIDMKESDKPNLTDYATFNAFFTRKLHKNARPIDTNPSTLIIPADGIITQIGKINQTNIFRVKNAPYHLDGLLAGHDNIIDYFINGSFVIIYIPPQNCHRIYMPCTGTLREVLYIPGNLFSVHPKITKNMPNIFSRNERVICLFETDFGYMAQILIGAIIVGSIETTWLGTITPPREGIVRHWRYSSNNTNTDADDSIILQKGHEMGLFKLGSTVINLFGDKKVILNNLLQPYDIARIGMPLAHGHSQKK | 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... |
Q7W6I5 | MPFKDQLFLASQYLAPHHLVSRLMGRVADCRAPEIKNRMIARFVRRYNVDMSEALVEDPLAYASFNDFFTRALKPDARPLDDEPGAALCPADGAISQIGAIDNGRIFQAKGHSFGLTDLLGGDAERAAPFAGGQFATIYLSPRDYHRVHMPLAGTLREMVHVPGRLFSVNPLTARSVPELFARNERVACLFDTEHGPMALVLVGAMIVASIETVWAGLVTPHKRQVRSVRYDAAARAPIHLDKGAEMGRFKLGSTVIVLFGPKRLRWLDLPSVRGPVRMGETLALPASTAISFPESE | 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... |
Q89NP2 | MSILDSIQRQIPPIHKEGYPFIGGFALASLILFWLWSPLGWIGTILTVWCALFFRDPVRVTPVREGLVVSPADGRVSMITMALPPAELGLGDRPLPRISVFMSVFNCHVNRSPIAGRVDRIAYRPGLFINAELDKASEDNERNSLVITTPTARIGVVQIAGLIAKRIVCFVREGQAIGAGERFGLIRFGSRLDVYLPVGTKALVSEGQTAIAGETILADLAGDDPSRAYRAN | 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... |
C0Z4E2 | MGKKLLPGLIHRLPQNAMSRTMGKITATPFSRLAIQRYIKHYQIDTSIIEKPASEYRTLKEFFSRRLKPAARPIAPGPDTIVSPVDGTVSQLGDICEGTLIQAKGKDFSVSELLGGSEEEAKRYYGGKFITIYLSPRDYHRIHMPVTGDLSSYCYLPGRLYPVNKLGIENVDRLFARNERLVTHIKTDSLGDMALVKVGALFVGSVKVCYNTATTNIKHGRQTHEKIAGTPRYEKGSELGWFEFGSTVILLLESNELEWATGVEKGKSLLMGQALATKKA | 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... |
Q8YFM9 | MSLTDTIRNTFVPIHREGYPFIAGFFVVSLMLGWLWDPLFWIGMVLTVWCIYFYRDPERVTPMDDDLVISPADGKVSFVGLAVPPAELDLGYEPMTRVSVFMNVFSVHINRSPVRGKIDKVVHRPGKFLNAELDKASTENERNSVLIESPHGKIGVVQIAGLVARRIVCWSNQDDELSVGERFGLIRFGSRVDVYLPSDATVRVAVGQTAIAGETVLADYGTERGEPVVRIA | 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... |
Q6AJI0 | MLQPQVPVAREGVPFIGFAAFLTLVSAASECEILTFIFLLATAFTLYFFRDPERFVPDDPSALISPADGKIIVIEKTDKQDFIEGEALKISIFMNVFNVHVNRAPIAGKVDKIIYTPGKFYSADSSQGAEYNENCGIVLTTNSGKKIAFVQVAGLIARRIVCWLEPNDTIQSGRRVGLIRFGSRVDLYLPTDTALSVSVGDKVRAGETILGQII | 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... |
Q726X7 | MRNPSISITPEGLPAIGLCTLATLTFALIGCWVMAVIFLLLTWFCCHFFRDPERVTPTGAGLAVSPADGRVIRVEPVTDPITGEKRTCVCIFMNVFNVHVNRMPVAGTIRNIVYHPGKFFNAAWDKAATDNERCDYLIEDAEGGKWTMVQIAGLIARRIVCRVDEGDTLTRGERYGMIRFGSRVDLYLPDGYCPTVSVGEHVFAGQTIVARKSPEGA | 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... |
P36081 | MRFHDSILIFFSLASLYQHVHGARQVVRPKEKMTTSEEVKPWLRTVYGSQKELVTPTVIAGVTFSEKPEETPNPLKPWVSLEHDGRPKTIKPEINKGRTKKGRPDYSTYFKTVSSHTYSYEELKAHNMGPNEVFVEEEYIDEDDTYVSLNPIVRCTPNLYFNKGLAKDIRSEPFCTPYENSRWKVDKTYFVTWYTRFFTDENSGKVADKVRVHLSYVKENPVEKGNYKRDIPATFFSSEWIDNDNGLMPVEVRDEWLQDQFDRRIVVSVQPIYISDEDFDPLQYGILLYITKGSKVFKPTKEQLALDDAGITNDQWYYVA... | Function: With EXP1, the specific cargo receptor protein for the plasma membrane ATPase PMA1, is involved in the transport and/or maturation of PMA1 . EXP1 and PSG1 probably act sequentially to promote PMA1 sorting between the ER and the Golgi, with EXP1 promoting PMA1 export from the ER to the Golgi while PSG1 has a r... |
Q9VWU1 | MPLKWSLLLGTFVLISCSSVEAAVTVGRACKVTDTMPGICRTSSDCEPLIDGYIKSGVLTLNDVPSCGLGAWGEIFCCPTKPCCDNSTITSVSTSSTTSTKAPMTSGRVDVPTFGSGDRPAVAACKKIRERKQQRSGNQLVIHIVGGYPVDPGVYPHMAAIGYITFGTDFRCGGSLIASRFVLTAAHCVNTDANTPAFVRLGAVNIENPDHSYQDIVIRSVKIHPQYVGNKYNDIAILELERDVVETDNIRPACLHTDATDPPSNSKFFVAGWGVLNVTTRARSKILLRAGLELVPLDQCNISYAEQPGSIRLLKQGVID... | Function: Serine protease that plays a key role in innate immunity in response to Gram-positive bacterial and fungal proteases . Acts as a component of the Toll pathway upstream of protease spz processing enzyme SPE and Tl ligand spz . Nec regulates the cascade by inhibiting psh .
Sequence Mass (Da): 42228
Sequence Len... |
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