ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
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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.-
|
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.-
|
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.-
|
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.-
|
Q55167 | MTSDDAAAGLVRVLDAAQGAFLALDSYGGNDRSRAVLAMAEALERSFAQILEANTLDLVVSREMSVADCLCEWLKLTPERLQNTVTILKRLASLPDPLQRVMASPYQFNLAQTYCQLMPLGVVALVYESFPELAAIAAGFCLKTGNSLVLRSCGASSHSTAAICEILREGLLDADLPVDSVSHIPSETSPNVQDLVGNASQLNLVIPYGRPSFVEQISQQCTPPVLKAAMGNCYLYWSSKGDLEMVRQMIIDSHVGHPDPVNAIEKVLVSPGQNPAPLVRLLNNLQAKGFKLRGDAELCEQFPDHLTLAKENEWGKAYLDRTVAFRTTQNLKTAIAWINSHSSGHGDCIATDSYQESRQFSMGVDSALVYVNIPPYFCRNPRHGESLFLGVSSQKGQRRGLIGLEAFMTPKQIVQGESRS | 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
Sequence Mass (Da): 45772
Sequence Length: 420
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2.
Subcellular Location: Cytoplasm
EC: 1.2.1.41
|
Q39JM2 | MDIDQYMTDLGRRARHASRAMARASTAAKNAALDAVARAIERDAQVLKDANARDVARAREKGLDAAFVDRLTLSDKALNTMVEGLRQVASLADPIGEISNLKYRPSGIQVGQMRVPLGVIGIIYESRPNVTIDAAALCLKSGNATILRGGSEALESNTALAKLIGEGLEAAGLPQDAVQVVATADRAAVGKLITMTEYVDVIVPRGGKSLIERLINEARVPMIKHLDGICHVYVDDRADLAKALTVCDNAKTHRYGTCNTMETLLVSSGVAAKLLPPLGKLYRDKQVELRVDAAARTVLADAGVGPLVDATEEDWHTEYLAPVLAIKVVDGLDAAIEHINHYGSHHTDAIVTEDHDRAMRFLREVDSASVMVNASTRFADGFEFGLGAEIGISNDKLHARGPVGLEGLTSLKYVVLGHGEGRQ | 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
Sequence Mass (Da): 45279
Sequence Length: 423
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2.
Subcellular Location: Cytoplasm
EC: 1.2.1.41
|
Q2SZ88 | MDIDQYMTDVGRRARRASRSIARASTAAKNAALEAVARAIERDAGALKAANARDVARAKDKGLDAAFVDRLTLSDKALKTMVEGLRQVATLPDPIGEMSNLKYRPSGIQVGQMRVPLGVIGIIYESRPNVTIDAAALCLKSGNATILRGGSEALESNTALAKLIGEGLAEAGLPQDTVQVVETADRAAVGRLITMTEYVDVIVPRGGKSLIERLINEARVPMIKHLDGICHVYVDDRASVTKALTVCDNAKTHRYGTCNTMETLLVARGIAPAVLSPLGRLYREKGVELRVDADARAVLEAAGVGPLVDATDEDWRTEYLAPVLAIKIVDGIDAAIEHINEYGSHHTDAIVTEDHDRAMRFLREVDSASVMVNASTRFADGFEFGLGAEIGISNDKLHARGPVGLEGLTSLKYVVLGHGEGRQ | 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
Sequence Mass (Da): 45309
Sequence Length: 423
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2.
Subcellular Location: Cytoplasm
EC: 1.2.1.41
|
A4XK60 | MSDLIQKAQKVKEASKKLMNLSESQKNLALSCISKKILDNMEYILVENKKDMENAQNKGIKGALLDRLKLTEDRIRQICKGIEDVIKLPDPVGEVISMWKRPNGLIIGQKRVPIGAIGIIYEARPNVTVDAAVLCLKAGNSVLLRGGSEAINSNVALVKTMKEGLIEAGIDEGSIEIVEDTSRETAVAMMKLNEYLDLLIPRGGANLIKTVVQNATVPVIETGVGNCHVFVDESADFEMAEKIVINAKTQRPGVCNAAEKLLVHKNIAESFLPMIVKKLMTKGVEIRGCSKTVEICKQNGIEVKEATEDDWYTEYLDLIIGVKVVDSIDAAIEHINKYGSKHSEAIVTRDYFNAQKFLDFVDAAACYVNASTRFTDGFEFGFGAEIGISTQKLHARGPMGLKELTTIKYIILGSGQVRE | 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
Sequence Mass (Da): 46002
Sequence Length: 419
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2.
Subcellular Location: Cytoplasm
EC: 1.2.1.41
|
A7GVZ7 | MSEILNIAKAAKASCEQLLNLSAQAKSQILNAVADELVRQKEAIKAANLLDLKAGENAGLSAALLDRLELTDARIEAMANGVREVAKFDEVVGEVLGGWRHPNGMQITKIRVPLGVLGIIYESRPNVSIDAAALALKSGNAVILRGSAAAISSNKFLVNLFNETGAKFGLPKGAVALVESTDKEAVGEMIKMHEFIDVLIPRGGKNLKDFIIQNATIPVIETGAGVCHIFVDESADVREAVEIIKNAKTQRPSTCNSVECVLLHERVAVKVLTSLARELDGVQLRVHEDLWAKFGENLGEISGDLDANLSGLKAEVKIGESSNGAQLVKADESDFGTEFLSLVLAVKCVSGVAEAVSYINSHSTHHSDAILSRDYANIERFLNAVDSAVVYANASTRFSDGGEFGFGGEIGISTQKLHARGPMGVRELTTSKYVVRGDGQIR | 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
Sequence Mass (Da): 47155
Sequence Length: 442
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2.
Subcellular Location: Cytoplasm
EC: 1.2.1.41
|
P53000 | MRNLLENIKKNSQKLLNLTPKDKEKIILKLAQILRENFKIILEANKKDMANFTKSGAMKDRLLLDEKRILALCEGLEKIAYIEDPIGKISKGWKNYAGLSIQKMSIPLGLICVIYEARPSLSAEIAALMIKSSNACVFKGGSEAKFTNEAIFTLVNKVLKEFDLQDCFAMFTQRDEILQILAFDDLIDVIIPRGSSNMIQEIANNTKIPLIKQNKGLCHAFVDQSANLDMALKIILNAKCQRVSVCNALETLLIHEKIAKNFISLLIPEFEKFKVKIHAHENALAYFNNSNLKIFKANENTFDTEWLDFALSVKLVKDCDEAIEHINKHSSLHSETIISNDASNIAKFQRLINSSCIYANASTRFSDGGEFGFGGEVGISTSKLHARGPMGIEDICTYKYIINGEGQIRE | 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
Sequence Mass (Da): 46000
Sequence Length: 410
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2.
Subcellular Location: Cytoplasm
EC: 1.2.1.41
|
Q3AF39 | MDEVLNLAKKAKEASKKLAQLSTEQKNRALLKIAQYLEENMEKILTENQKDLAEAKKGGLSPAFIERLTLNEKRILDMAEGVRQVAKLPDPVGEVLGMTRRPNGLVIGQVRVPLGVVGIIYESRPNVTVDAAALCLKAGNAVILRGGKEAFNSNLALVTLMEEALRSEEIPEGAVGMIKTTSRDAANYLMRLNGYLDVLIPRGGAGLIKTVVENSTVPVIETGVGNCHVYVEEDADLEMAERIIINAKCQRPAVCNAMETLLVHEKIAPVFLPQIGKALKENGVEIRGCEVTRRYIPDALPATEEDYYTEFLDLILAVRVVRDLDEAIAHITKYGSGHSEAIVTRDYFKARRFTEEVDAAAVYVNASTRFTDGFEFGFGAEIGISTQKLHARGPMGLKELTTTKYVIYGTGQIRG | 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
Sequence Mass (Da): 45489
Sequence Length: 415
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2.
Subcellular Location: Cytoplasm
EC: 1.2.1.41
|
Q3IP72 | MTETTEAKVDAAQTAALELANESDEARQENLQAIADAIDERRAEVLEANEKDVEAAEEMLEAGEYSQALVDRLKLSDAKLDSIIEMVRSVAGQEDPLGKTLTARELDDGLDLYKVSVPIGVIGTVFESRPDALVQIAALSLRSGNAVILKGGSEASHSNRVLYEIIREATADLPDGWAQLIEAREDVDRLLGMDDSVDLLMPRGSSAFVSYIQDNTSIPVLGHTEGVCHVYVDDAADLDMATDIAYDAKVQYPAVCNAVETLLVHEDVAEEYLPDIAARYAEADVEMRGDEATRSVLDRDIEAATDDDWTSEYGDLIVAIKVVDSLESAIDHINTNGSKHTESIVTEDDGRASTFMRRLDSASVFHNASTRFSDGYRFGLGAEVGISTGKIHARGPVGLKGLTTYKYHLEGDGHLVATYAGEDAKPFSHEEFDGEWSP | 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
Sequence Mass (Da): 47559
Sequence Length: 438
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2.
Subcellular Location: Cytoplasm
EC: 1.2.1.41
|
Q9JZG3 | MSNTQKQLALAKAAKKSVNTADTEEKNRALLAMADSLEAATADILAANRQDLEAAAGNIPESMTDRLLLDGKRICAMADGIRAVAALPNPVGEILETSTLPNGLEIVKKRVAMGVIGIIYESRPNVTSDAAALALKSGSAVVLRSGKDAFQSARAIVAALKTGLAQTRIDPDALQLIEDTGRESSYEMMRAKDYLDLLIPRGGAGLIRAVVENAVVPVIETGTGIVHIYIDKDADWDKALRIVYNAKTSRPSVCNSMEVLLVHEDIAADFLPKLERLLVRDRIEAGLPPIRFRLDPQAARHIGGEAAGADDFDTEFLDYILAVKTVASVEEAVWHIETHSTHHSDGIVTENRHAADYFTTHIDSAAVYVNASTRFTDGGEFGLGCEMGISTQKLHARGPMGLKELTSYKYIVQGTGQVRE | 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
Sequence Mass (Da): 45257
Sequence Length: 420
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2.
Subcellular Location: Cytoplasm
EC: 1.2.1.41
|
Q820I7 | MEKTEKIQADMQALGRAARAAARIVAKADTAVKNHALIAMARAIRCHEASLLAANAADVAQARNKGLEPAMIDRLTLTPKGIASMAAGLEQIAALSDPIGAVTDLDYRPSGIQVGRMRVPLGVIAIIYEARPNVTADAAGLCLKAGNAAILRGGSEAIQSNQAIAACVQEGLRSAGLPEHAVQVVETTDRAAVGELITMSEYVDMVVPRGGKGLIERIANEARVPVIKHLDGVCHVYVDLSADLEKAVRVADNAKTQRYGTCNTMETLLVHAGIAERFLPRICKILLEKGVELRGDEAARALVAGIKPAVEEDWYAEYLAPVLSVRIVEDIDQAITHIATYGSQHTDAIVTEDYSRARQFLREVDSSSVMINASTRFADGFEYGLGAEIGISTDKLHARGPVGLEGLTSQKFIVLGDGHIRE | 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
Sequence Mass (Da): 45013
Sequence Length: 422
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2.
Subcellular Location: Cytoplasm
EC: 1.2.1.41
|
A1SHP5 | MSTQHDEHDAAGATGVADQVVAAAERARAASHGLALATRAEKDAALQAMAEALLTREPEVLAANGEDVARAEANGTPPNIVDRLRLTQERVAAMAQGLRDVAALPDPVGEVLRGSTLANGLEMRQVRVPFGVVGMIYEARPNVTADAAGICLKSGNAVLLRGSSSARSSNAAIVAALRDAIAGTGLDPDVVQQVPGDSHDSVKALMRARGHVDVLIPRGGAGLIRSVVEESTVPVIETGVGNCHVYVDRAADLDKALAIVLNAKTHRTSVCNAAESLLVHADLADTFVPRVVAALQEAGVTVHGDERFQAEDGVLPATDEDYGQEYLSLDISAAVVPDLDGAIAHIRRWSSQHTEAIVTEDLAAARRFTAAVDSAAVLVNASTRFTDGGEFGFGAEIGISTQKLHARGPMGLTEMTSTKYVVTGDGHVR | 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
Sequence Mass (Da): 44694
Sequence Length: 429
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2.
Subcellular Location: Cytoplasm
EC: 1.2.1.41
|
Q9PEM3 | MSHIRHLAQQCRDAARRLATLSTDAKRRLLETMATALNTDAATILAANAADLDAARTQQVGTAMLDRLALDPQRLAAMADALRDIAALPDPVGQVTRDDQRPNGIHVQKIRVPLGVIAMIYEARPNVTADAAALCIKAGNGIILRGGSEAIRSNIAIATALQRALRLASLPETALILVQDMARHTMLELLQLSDLIDLVIPRGGEGLIRFVAEHARIPVIKHYKGVCHQFVDASADIEMAIRLLIDGKTTRPAACNALETLLVHTDIAPRFLPAAAAALRPYGVQLRGDHATCTLLPDVVLATDADYAAEYLDLILAIRIVPNVDAALEHIRRYGSDHTEVIVTADPAHADTFVQQLYSAVVMVNASSRFSDGGALGLGAEIGISTTRLHAYGPMGLDALTVERFVVRGQGQVRH | 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
Sequence Mass (Da): 44553
Sequence Length: 415
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2.
Subcellular Location: Cytoplasm
EC: 1.2.1.41
|
P54885 | MSSSQQIAKNARKAGNILKTISNEGRSDILYKIHDALKANAHAIEEANKIDLAVAKETGLADSLLKRLDLFKGDKFEVMLQGIKDVAELEDPVGKVKMARELDDGLTLYQVTAPVGVLLVIFESRPEVIANITALSIKSGNAAILKGGKESVNTFREMAKIVNDTIAQFQSETGVPVGSVQLIETRQDVSDLLDQDEYIDLVVPRGSNALVRKIKDTTKIPVLGHADGICSIYLDEDADLIKAKRISLDAKTNYPAGCNAMETLLINPKFSKWWEVLENLTLEGGVTIHATKDLKTAYFDKLNELGKLTEAIQCKTVDADEEQDFDKEFLSLDLAAKFVTSTESAIQHINTHSSRHTDAIVTENKANAEKFMKGVDSSGVYWNASTRFADGFRYGFGAEVGISTSKIHARGPVGLDGLVSYQYQIRGDGQVASDYLGAGGNKAFVHKDLDIKTVTL | 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
Sequence Mass (Da): 49740
Sequence Length: 456
Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2.
EC: 1.2.1.41
|
Q2VZU1 | MSPLAAAKRLIVKIGSSLLVDDSTGQVRRGWLETLAADIAACKARGQEVIVVSSGAVAVGRRKLGLVPPLKLEEKQAAAATGQIRLAHAWQDALAHHQITVAQVLLTLDDSENRRRYLNARSTLETLLKLGAVPVINENDTVATAEIRVGDNDRLAARVAQMVSADALVLFSDIDGLYTADPRKDPDARFIPEVHELTPEIEAMAGDPGSAYGSGGMVTKLVAARICLSAGCRMAITRGEPMHPLKTIEDGGRCTWFLPNSEPRTARKQWIFGSMKPTGTLVLDAGAARALAQGRSLLPAGITEVSGAFERGDCVLVKDGSGKVLGRGLVAYSADDSRAIMGRKSGEIEAILGFRGRDELIHRDDLVMEG | 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: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.7.2.11
|
Q9ZG98 | MHGRLPLTAQTHRRLVVKVGSAVLSGPQGRQHQLAIAAQVAALRAEGREVVLVSSGAQATGMQKLGLTEKPKSMPGKQALAAVGQPTLMLLWEQAFSWYDLKVAQVLLTAEDLAHRHRYLNARQTLETLLEWGIVPIINENDTVMVEEIKFGDNDQLSALIASLVGADLLILLSDIEALYEADPRTHPEAQPIPYVERVDAGVLRMAGDSPNRVGTGGMKSKLLAAEKAQAAGIPHLLLPGTRPQSIAEALQGAPVGTLFAGGQRRYSGRKLWLYQLPKPQGEVVVDAGAAKALRQGGASLLPAGILEVRGQFGVGEAVRCLDEQGNLIGVGLVNYSAAELARIKRRKTREIEALLGYKNTDEAIHRDYFALASELE | 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: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.7.2.11
|
Q46F79 | MTDRNEFLNDINKIVIKIGTSSLTKQNCDSTKENCSIDPTFIENIAAQVSELRKLGKEVIVVSSGAIGVGLYELGIAPKPREIPIRQAAAAVGQSILMQYWSEAFSKHGIKVAQILLTYEFYSDRVSYLNLRNSISTLLEYGVVPIINENDCTCTNEIEAIFGDNDKLSAMVASKIDADLLIILSDIDGLFDKNPKIHEDARLISLVEKITPEIESYGGDPTSFKGVGGMRTKIKAAKICSMAGCYVLIANSEIEDVLLKVLSGKEIGTLFLAERHIQKNRARWIILSRASGTIRVDAGAKAAVLGKNSLLSAGVVDVEGNFDRGDVVRLECEGRVFAKGITDYTSEELMKIKGAHTDEIEGILGYNNYSNVIKKENIGIMEN | 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: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.7.2.11
|
Q12TG0 | MTNRKEIIGDAEKIVIKIGTTSISREDGSLNNEFMDTIASQVSELHRAGKQIILVSSGSIGIGIEILDLGCRPKEIPVRQAAAAVGQGVLMQHWTEAFQKYGLNVAQILLTYDSFTNRLTYLNLRNSISTLLSYGVIPIINENDPICVHEIEATLGDNDKLSAMVASKMEADLLILFTDIDGLYDKNPKRHDDAVLLRTVEEITPTIESYGGNPTSMKGVGGMRTKIDAAKICNISGCYMVIANSNVDDGIRRILDGEELGTLFLTNQFVHKNRIRWIILARSSGSIVVDTGAKEALAKRMSLLPSGVLGVAGTFDRGDIVKLECDGVVFGKGITDYTSEELKAIKGKQTNEIADILGYKNYDHVVQKDNIGLFK | 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: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.7.2.11
|
B0JFY2 | MNQTIVIKIGTSSLTDNETGQLSLSTIAALVEVLTRLRAAGHRVVLVSSGAVGVGCRRLGIQERPKKIALKQAIAAVGQGRLMRIYDDLFTSLGQPIAQILLTRPELMERTCYVNAYNTFQALFELGVIAIVNENDTVAIDELKFGDNDTLSALVASLIEADWLFILTDVDRLYSADPRLFPEAAAIARVSPAELAQLSIDAGSSGSQWGTGGMATKLAAARIATSAGVEMAITRGRQPGNILKIMAGEAIGTRFEAQKRSDNARKRWIAYGLLPMGKIYLDAGAIQAICQGGKSLLAAGITKVEGEFSASESVQLCDQEGRELARGIVNYSSEEIDRVKGQHSERIASLLGYMAAETIIHRDNLVILSASSTTSTNKG | 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: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.7.2.11
|
Q1GQZ4 | MSLFPPASCPRLIVKIGSALLVDPGGAVRRDWLTGIAADIAERARAGQQVAVVSSGAIALGARRLGLAKGGRASLEDAQAAAATGQIALSQVWAEVLGAEGLTAAQMLVTLGDLEHRRRYLNAAATLDRLLSLGVVPIINENDSVATEEIRFGDNDRLAARVAQAAAARGVILLSDIDGLYDRNPAQPGAVHIERIERIDAAIEAMADTGSASGMGSGGMVSKIAAARIANAAGAHLAIASGRIDRPLSTAARHSLFVAERGASARKAWLAGGLTAEGRLTIDAGAVKALVGGASLLAAGVTAVSGSFARGDILDIVGPDGRVVARGLSEYPAADAAAIVGLGRDAQEAALGYAPRSAIVHRDHMVLL | 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: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.7.2.11
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Q9RDJ9 | MAGARQAVGEARRIVVKVGSSSLTTAAGGLDADRVDALVDVLAKMRGADKEVVLVSSGAIAAGLAPLGLPRRPRDLARQQAAASVGQGLLVARYTASFARYGVRVGQVLLTSDDMSRRAHHRNASRTLDKLLAMGAFPIVNENDTVATDEIRFGDNDRLAALVAHLVRADLLVLLSDVDGVYDGDPSRPGTSRLAEVRDMGDLAGVDIGSAGKAGVGTGGMVTKVEAARIAAAAGIPVVLTSAVHAADALAGGDTGTYFHATGRRSADRLLWLQHASAPQGALVLDDGAVRAVVEGRKSLLPAGIAGVEGDFAAGDPVELRDGTGRAVARGLVNFDAKEMPRLIGRSTRELARELGPAYEREVVHRDDLVILHP | 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: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.7.2.11
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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
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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 kinases.
Sequence Mass (Da): 14114
Sequence Length: 131
Subcellular Location: Cytoplasm
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O14011 | MFCSISGETPKEPVISRVSGNVYEKRLIEQVIRETSKDPVTQQECTLEDLVPVKVPDFVRPRPPSATSLPALLSLFQEEWDSVALEQFELRRNLTETKQELSTALYSLDAALRVISRLTKERDEAREALAKFSDNIGTVSSKTIEVQEVEMGESDDQLKTSLRSTVEKTFQELSSKRKRTKLQPKWATDDAVSQLLQATPSTILENLETESTTSFFPSPENSSFVLCLHKDELLCLDIQSNSTLKIFEGSALACCWLTSSKIAVATADAISIFEFPVSSSGLQSVGEPTSSIPIDEKVNFLQAHPSGEYLLAASNEKCYIFSLKSQVYNITVAQHITSLAVHPDGNLFVAGLENGELRFFETSSGNELTKFGPHSSPVKTLQFGENGYWLVVTTNDDSDIFIWDLRKSELVQKIPLQTKVAAVSLDITSQLLVSSDGETLYVHIYVKSSKSWRCMSQTHVSSISNLVWLNELHQLLFSTSNGAILRLG | 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-[acceptor protein]-L-lysine.
Sequence Mass (Da): 54191
Sequence Length: 488
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
EC: 2.3.2.27
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P32523 | MLCAISGKVPRRPVLSPKSRTIFEKSLLEQYVKDTGNDPITNEPLSIEEIVEIVPSAQQASLTESTNSATLKANYSIPNLLTSLQNEWDAIMLENFKLRSTLDSLTKKLSTVMYERDAAKLVAAQLLMEKNEDSKDLPKSSQQAVAITREEFLQGLLQSSRDFVARGKLKAPKWPILKNLELLQAQNYSRNIKTFPYKELNKSMYYDKWVCMCRCEDGALHFTQLKDSKTITTITTPNPRTGGEHPAIISRGPCNRLLLLYPGNQITILDSKTNKVLREIEVDSANEIIYMYGHNEVNTEYFIWADNRGTIGFQSYEDDSQYIVHSAKSDVEYSSGVLHKDSLLLALYSPDGILDVYNLSSPDQASSRFPVDEEAKIKEVKFADNGYWMVVECDQTVVCFDLRKDVGTLAYPTYTIPEFKTGTVTYDIDDSGKNMIAYSNESNSLTIYKFDKKTKNWTKDEESALCLQSDTADFTDMDVVCGDGGIAAILKTNDSFNIVALTP | 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 spliceosome maturation. It is also probably involved in DNA repair.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 56570
Sequence Length: 503
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
EC: 2.3.2.27
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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-phosphorylated substrates.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 25274
Sequence Length: 218
EC: 3.1.3.16
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O44249 | MTDAKNNLLYFFDRPNEPCFMQKGEDKVVFEIPDHYYPDKYKSLSNTLSNRFGNEATKRIPIRNITLPNLEVPMQLPYNDQFSLFVPKHRTMAAKLIDIFMGMRDVEDLQSVCSYCQLRINPYMFNYCLSVAILHRPDTKGLSIPTFAETFPDKFMDSKVFLRAREVSNVVISGSRMPVNVPINYTANTTEPEQRVAYFREDIGINLHHWHWHLVYPFDSADRSIVNKDRRGELFYYMHQQIIGRYNVERMCNGLPQVKPFSDFSAPIEEGYFPKLDSQVASRTWPPRFAGSVFRNLDRTVDQVKIDVRKLFTWRDQFLEAIQKMAIKMPNGRELPLDEVTGIDMLGNLMESSIISPNRGYYGDLHNMGHVFAAYTHDPDHRHLEQFGVMGDSATAMRDPFFYRWHRFVDDVFNIYKEKLTPYTNERLDFPGVRVSSVGIEGARPNTLRTLWQQSTVELGRGLDFTPRGSVLARFTHLQHDEFQYVIEVNNTTGGNLMGTVRIFMAPKVDDNGQPMSFNKQRRLMIELDKFSQALRPGTNTIRRRSVDSSVTIPYERTFRNQSERPGDPGTAGAAEFDFCGCGWPHHMLIPKGTAQGYPVVLFVMISNWNNDRIEQDLVGSCNDAASYCGIRDRKYPDKQAMGYPFDRKMANDAATLSDFLRPNMAVRDCSIQFSDTTVERGQQG | 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. Binds to the surface of hemocytes and is involved in hemocyte melanization.
PTM: The N-terminus is blocked.
Catalytic Activity: 2 L-dopa + O2 = 2 H2O + 2 L-dopaquinone
Sequence Mass (Da): 78966
Sequence Length: 685
Subcellular Location: Secreted
EC: 1.14.18.1
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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.
Catalytic Activity: 2 L-dopa + O2 = 2 H2O + 2 L-dopaquinone
Sequence Mass (Da): 22867
Sequence Length: 195
Subcellular Location: Secreted
EC: 1.14.18.1
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F4IE66 | MPSMAQGELKSFVQNSRPNPKSPTVSPFSMRQKIAEHRRSLPIASVEKRLVEEVQKNDILIIVGETGSGKTTQLPQFLYNAGFCREGKMIGITQPRRIAAVTVAKRVAEECEVQLGQKVGYSIRFDDTTSGSTRLKYMTDGLLLREALLDPHLSRYSVIIVDEAHDRSVHTDVLLALLKKIQRTRSQPVSEKTEFGNVASQVQTTTRDANGPQQNGVLKGYQGRKLSPLKLIIMSASLDARVFSEYFGGAKAVHVQGRQFPVDILYTVHPESDYVDATLVTIFQIHFEEKPGDILVFLTGQDEIESVERLVQERLQNIPEDKRKLLPLAIFSALPSEQQMKVFAPAPTGFRKVILATNIAETSITIPGIRYVIDPGFVKARSYDPSKGMESLDVVPASKAQTLQRSGRAGREGPGKSFRLYPEREFEKLEDSTKPEIKRCNLSNIILQLKALGIDDIVGFDFIDKPSRGAIIKALAELHSLGALADDGKLENPVGYQMSRLPLEPVYSKALILANQFNCLEEMLITVAVLSVESIFYDPREKREEARTSKNHFASVEGDHLTYLSVYRESDEFLEKRKAAGSGNNIDKIMKKWCKENYVNSRSLKHARDIYRQIREHVEQIGFNVSSCGNDMLAFRRCLAASFFLKAAQRQLDGTYRALESGEVVHIHPTSVLFRAKPECVIFNELMQTSKKYIKNLTIIDSLWLSELAPHHFQTAE | 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 germination by controlling expression of genes coding for GerA and GerK receptors.
Catalytic Activity: H2O + P(1),P(4)-bis(5'-guanosyl) tetraphosphate = GMP + GTP + 2 H(+)
Sequence Mass (Da): 27463
Sequence Length: 244
Subcellular Location: Forespore
EC: 3.6.1.17
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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 | MSFSEFYQRSINEPEAFWAEQARRIDWRQPFTQTLDHSRPPFARWFCGGTTNLCHNAVDRWRDKQPEALALIAVSSETDEERTFTFSQLHDEVNIVAAMLLSLGVQRGDRVLVYMPMIAEAQITLLACARIGAIHSVVFGGFASHSVAARIDDARPALIVSADAGARGGKILPYKKLLDDAIAQAQHQPKHVLLVDRGLAKMAWVDGRDLDFATLRQQHLGASVPVAWLESNETSCILYTSGTTGKPKGVQRDVGGYAVALATSMDTIFGGKAGGVFFCASDIGWVVGHSYIVYAPLLAGMATIVYEGLPTYPDCGVWWKIVEKYQVNRMFSAPTAIRVLKKFPTAQIRNHDLSSLEALYLAGEPLDEPTASWVTETLGVPVIDNYWQTESGWPIMALARALDDRPSRLGSPGVPMYGYNVQLLNEVTGEPCGINEKGMLVIEGPLPPGCIQTIWGDDARFVKTYWSLFNRQVYATFDWGIRDAEGYYFILGRTDDVINIAGHRLGTREIEESISSYPNVAEVAVVGIKDALKGQVAVAFVIPKQSDTLADREAARDEENAIMALVDNQIGHFGRPAHVWFVSQLPKTRSGKMLRRTIQAICEGRDPGDLTTIDDPASLQQIRQAIEE | 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 degradation.
EC: 6.2.1.17
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P28708 | MDEYSSIYSQPKTPRLKQEGFPDSIGDQHEKALIDENGEEDKKMASTEGTTGDSRSTPLTVSIPTFENVQALPTPMTYTPLSPGNLSMSPIDQSSLNIPKRRSHARLLDDMLSVTQPNQRVVSELIAPANLSPQRVVSLPTVTEEALVNDSVDSDNYTKEPYFPESSSSTEKCDDDIFQGFLLDHWDRPLLWKKVRPIGSGNFSTVLLYELMDQSNPKLKQVAVKRLKYPEELSNVEQINTSLRYKETLSRLENSLTRELQVLKSLNHPCIVKLLGINNPIFVTSKKPLCDLIIKTPRALPPCDMIMSYCPAGDLLAAVMARNGRLEAWLIQRIFTEVVLAVKYLHENSIIHRDLKLENILLKYSFDDINSFRDSPIYCKQNFIELADFGLCKKIENNEMCTARCGSEDYVSPEILMGVPYDGHLSDTWALGVILYSLFEDRLPFDPPPNASARQRSRATSHRIARFDWRWYRLSDYKTNVGKQIVENTLTRKNQRWSINEIYESPFVKTIADTLSFS | 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]
Sequence Mass (Da): 58956
Sequence Length: 518
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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Q12310 | MSLSRILRYNQRNNKTTASLTAEHAYSDNWAYSVSLGDPTSVGVNMAAKTGEALNKSYDSVFSSLPVADSVPRTDFTASSRDDENTDVQKLTTSWMEKIDTKMPENISKIDSNIISSPMVSKVEARFIVPKGRLRKNSTDFTSSFSNSLSLPKSYGKLIFFTSKKNSSSTKKNLANDISDNKHNNNSSNTIGHNIPVTTATATCDEIACTSTEHEYNVYEEERMFTTRVYSLEDSVSSLSTNPLDDTYSEAVQVNTRHIEDTESTAHIRKHSYTTSLSSIKRLFKITSFSNNNSNSCDHQESTVADDCAISSSLKETTSSPVSTGSFSLMIENEDSDRDQIIQALYSNIEASTDLVSRKYRDLDVVLGEGSGGKVKLVQRVLDNKVFALKEYRSKKKRESERKYIKNIISEYCIASTLKNPNICETLEILYEKGKIFQILEYCEYDLFSLVMSEKMHYEEICCLFKQLINGVKYLHDIGLSHRDLKLDNCVVTRRGILKLIDFGASSVFHYPLSSQMIEANGIVGSDPYLSPEVFYFNEYDPRALDVWSVGIIFFCMITRRFPWKYPKVKDVQFKAFCSGRGVSSFKDLVTRPATDDSNNYDNDGYEEGVIDMGPNFILHRLPEETHKIMRRILEVSPFRRITINGILQDGWIKEIETCQVVGAASPNEASLRIINKGNHIHTNIDQRYAHIGGLHQRT | 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]
Sequence Mass (Da): 78939
Sequence Length: 699
EC: 2.7.11.1
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P33297 | MATLEELDAQTLPGDDELDQEILNLSTQELQTRAKLLDNEIRIFRSELQRLSHENNVMLEKIKDNKEKIKNNRQLPYLVANVVEVMDMNEIEDKENSESTTQGGNVNLDNTAVGKAAVVKTSSRQTVFLPMVGLVDPDKLKPNDLVGVNKDSYLILDTLPSEFDSRVKAMEVDEKPTETYSDVGGLDKQIEELVEAIVLPMKRADKFKDMGIRAPKGALMYGPPGTGKTLLARACAAQTNATFLKLAAPQLVQMYIGEGAKLVRDAFALAKEKAPTIIFIDELDAIGTKRFDSEKSGDREVQRTMLELLNQLDGFSSDDRVKVLAATNRVDVLDPALLRSGRLDRKIEFPLPSEDSRAQILQIHSRKMTTDDDINWQELARSTDEFNGAQLKAVTVEAGMIALRNGQSSVKHEDFVEGISEVQARKSKSVSFYA | 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: Cytoplasm
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P33298 | MEELGIVTPVEKAVEEKPAVKSYASLLAQLNGTVNNNSALSNVNSDIYFKLKKLEKEYELLTLQEDYIKDEQRHLKRELKRAQEEVKRIQSVPLVIGQFLEPIDQNTGIVSSTTGMSYVVRILSTLDRELLKPSMSVALHRHSNALVDILPPDSDSSISVMGENEKPDVTYADVGGLDMQKQEIREAVELPLVQADLYEQIGIDPPRGVLLYGPPGTGKTMLVKAVANSTKAAFIRVNGSEFVHKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGSDREVQRILIELLTQMDGFDQSTNVKVIMATNRADTLDPALLRPGRLDRKIEFPSLRDRRERRLIFGTIASKMSLAPEADLDSLIIRNDSLSGAVIAAIMQEAGLRAVRKNRYVILQSDLEEAYATQVKTDNTVDKFDFYK | 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: Cytoplasm
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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 activity but no trypsin-like activity.
PTM: Acetylated. The acetylated form at Met-1 was shown to be in 100-fold excess of the unacetylated form with the initiator methionine removed in whole cells and purified 20S proteasomes.
Sequence Mass (Da): 27613
Sequence Length: 252
Subcellular Location: Cytoplasm
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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 participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex).
PTM: C-terminal extension is partially cleaved off by limited proteolysis leading to a conversion of the proteasome from its latent into its active form.
Sequence Mass (Da): 29547
Sequence Length: 263
Subcellular Location: Cytoplasm
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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 activity but no caspase-like activity.
PTM: The N-terminus is blocked.
Sequence Mass (Da): 28312
Sequence Length: 259
Pathway: Protein degradation; proteasomal Pup-dependent pathway.
Subcellular Location: Cytoplasm
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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 (Da): 19943
Sequence Length: 186
Subcellular Location: Plastid
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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 conjugated to a prokaryotic ubiquitin-like protein (Pup). Identified substrates of the M.smegmatis proteasome are the pupylated SodA and Ino1 proteins . The Pup-proteasome system (PPS) is essential for survival under starvation; PPS likely functions to recycle amino acids under nitrogen starvation, thereby enabling the cell to maintain basal metabolic activities .
PTM: Pupylated at an undetermined lysine residue by the prokaryotic ubiquitin-like protein Pup with the help of the ligase PafA, which leads to its degradation by the proteasome and thereby constitutes a negative auto-regulation.
Sequence Mass (Da): 26915
Sequence Length: 246
Pathway: Protein degradation; proteasomal Pup-dependent pathway.
Subcellular Location: Cytoplasm
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B7EA73 | MDLPKEIFLKEYKKPDYLFDSVNLEFQLGEDKTIVTSKIAVSPGTEGTSSPLTLHGRDLKLLSIKVNGKDLKSEDYMVDSRHLTVSRPPGGTFNLEIVTEIYPQLNTSLEGLYKSTGNFCTQCEAEGFRKITYFQDRPDVMATYTCRIEADKTLYPVLLSNGNLIEQGDLEGGKHYALWEDPFKKPSYLFALVAGQLDCREDSFTTCSGRKVTLRIWTPGQDLAKTAHAMYSLKAAMKWDEEVFGLEYDLDLFNIVVVPDFNMGAMENKSLNIFQSRLVLASPETATDGDYAAILGVVGHEYFHNWTGNRVTCRDWFQLTLKEGLTVFRDQEFSSDLGCRTVKRIADVSKLRTYQFPQDAGPMAHPIRPHSYIKMDNFYTVTVYEKGAEVVRMYKTMFGASGFRKGMDLYFQRHDGQAVTCEDFYAAMCDANNTQLPNFLQWYSQAGTPTVKVSSSYDASSQTFSLKFSQEVPPTPGQPVKEPMFIPIAVGLVDSTGKDMPLTSIYSDGMLQSLTSDGQPVFTTVLQFNKKEEEFIFNNIPEKPVPSLLRGYSAPVRLDSDLTESDLFFLLANDSDEFNRWEAGQVLSRKLMLSLVADFQQQKTLALNPKFVDGLRSILRNTSLDKEFIAKAITLPGQGEIMDMMPVADPDAVHAVRTFIKKELALQLKDDLLSTVTNNRSSEAYTFNHDSMARRALKNTCLAYLASLNEPDTTELAFVEYKSATNMTEQFAALAALSQNPGQVRDDTLLDFYNKWQHDYLVVSKWFALQATSDIPGNVANVQKLLGHPAFDMRNPNKVYSLIGGFCGSPVNFHAKDGSGYKFLGEVVLQLDKINPQVASRMVSAFSRWRRYDESRQALAKAQLEMIVSANGLSENVYEIASKSLAA | 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 | MTTTLQQRESASLWEQFCQWVTSTNNRIYVGWFGTLMIPTLLTATTCFIIAFIAAPPVDIDGIREPVAGSLLYGNNIISGAVVPSSNAIGLHFYPIWEAASLDEWLYNGGPYQLVVFHFLIGIFCYMGRQWELSYRLGMRPWICVAYSAPVSAATAVFLIYPIGQGSFSDGMPLGISGTFNFMIVFQAEHNILMHPFHMLGVAGVFGGSLFSAMHGSLVTSSLVRETTEVESQNYGYKFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLGAWPVIGIWFTAMGVSTMAFNLNGFNFNQSILDSQGRVIGTWADVLNRANIGFEVMHERNAHNFPLDLASGEQAPVALTAPAVNG | 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 oxygen-evolving complex (OEC). There is also a Cl(-1) ion associated with D1 and D2, which is required for oxygen evolution. The PSII complex binds additional chlorophylls, carotenoids and specific lipids.
Function: Photosystem II (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 photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbD) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors.
Catalytic Activity: 2 a plastoquinone + 2 H2O + 4 hnu = 2 a plastoquinol + O2
PTM: C-terminally processed by CtpA; processing is essential to allow assembly of the oxygen-evolving complex and photosynthetic growth.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39721
Sequence Length: 360
Subcellular Location: Cellular thylakoid membrane
EC: 1.10.3.9
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Q3M5L6 | MSTIVQRQKEFNFFDLWDSFCAWITSTENRIYIGWFGVLSIPTLLAATTCFVLAFIAAPSVDMDGIREPIMGSLMDGNNLITAAVVPTSAAIGLHFYPIWEAASMDEWLYNGGPYQLIVLHFLIGIWCLLGRFWELSYRLGMRPWIAVAYSAPVIAATSVLLVYPIGQGSFSDGLPLGIAGTFHFMLAFQGDHNILMHPFHMLGVAGVFGGALLSSLHGSLVASTLIRNTDENESINGGYKLGQQQVTYKYLAGHNSFLGRLLIPTFASRNHRAFHFLLAALPTIGIWFAAMGVCSMAFNLNGLNFNHSILDSRGNVIRSDADILNRANIGLSVMHAPNVHNFPLVLSSGQPIPVS | 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 oxygen-evolving complex (OEC). There is also a Cl(-1) ion associated with D1 and D2, which is required for oxygen evolution. The PSII complex binds additional chlorophylls, carotenoids and specific lipids.
Function: Photosystem II (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 photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbD) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors.
Catalytic Activity: 2 a plastoquinone + 2 H2O + 4 hnu = 2 a plastoquinol + O2
PTM: Tyr-164 forms a radical intermediate that is referred to as redox-active TyrZ, YZ or Y-Z.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38955
Sequence Length: 356
Subcellular Location: Cellular thylakoid membrane
EC: 1.10.3.9
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P06007 | MTIAIGTYQEKRTWFDDADDWLRQDRFVFVGWSGLLLFPCAYFALGGWLTGTTFVTSWYTHGLATSYLEGCNFLTAAVSTPANSMAHSLLFVWGPEAQGDFTRWCQLGGLWAFVALHGAFGLIGFMLRQFEIARSVNLRPYNAIAFSAPIAVFVSVFLIYPLGQSGWFFAPSFGVAAIFRFILFFQGFHNWTLNPFHMMGVAGVLGAALLCAIHGATVENTLFEDGDGANTFRAFNPTQAEETYSMVTANRFWSQIFGVAFSNKRWLHFFMLLVPVTGLWMSAIGVVGLALNLRAYDFVSQEIRAAEDPEFETFYTKNILLNEGIRAWMAAQDQPHERLVFPEEVLPRGNAL | 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 required for oxygen evolution. The PSII complex binds additional chlorophylls, carotenoids and specific lipids.
Function: Photosystem II (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 photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbD) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors. D2 is needed for assembly of a stable PSII complex.
Catalytic Activity: 2 a plastoquinone + 2 H2O + 4 hnu = 2 a plastoquinol + O2
PTM: Phosphorylated in vitro .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39447
Sequence Length: 352
Subcellular Location: Plastid
EC: 1.10.3.9
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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 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 photons, and an electron transfer chain that converts photonic excitation into a charge separation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 9415
Sequence Length: 83
Subcellular Location: Plastid
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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 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 photons, and an electron transfer chain that converts photonic excitation into a charge separation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 9500
Sequence Length: 84
Subcellular Location: Plastid
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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 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 photons, and an electron transfer chain that converts photonic excitation into a charge separation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 4389
Sequence Length: 38
Subcellular Location: Plastid
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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 consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 4154
Sequence Length: 36
Subcellular Location: Plastid
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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 consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 4091
Sequence Length: 36
Subcellular Location: Plastid membrane
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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 consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 4168
Sequence Length: 36
Subcellular Location: Plastid
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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 consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 4233
Sequence Length: 37
Subcellular Location: Plastid
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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 photons, and an electron transfer chain that converts photonic excitation into a charge separation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 4250
Sequence Length: 42
Subcellular Location: Plastid
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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 photons, and an electron transfer chain that converts photonic excitation into a charge separation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 5060
Sequence Length: 45
Subcellular Location: Cellular thylakoid membrane
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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 photons, and an electron transfer chain that converts photonic excitation into a charge separation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 6982
Sequence Length: 61
Subcellular Location: Plastid
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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 photons, and an electron transfer chain that converts photonic excitation into a charge separation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 5284
Sequence Length: 47
Subcellular Location: Cellular thylakoid membrane
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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 photons, and an electron transfer chain that converts photonic excitation into a charge separation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 5126
Sequence Length: 46
Subcellular Location: Plastid
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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 photons, and an electron transfer chain that converts photonic excitation into a charge separation. This subunit is found at the monomer-monomer interface.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3902
Sequence Length: 37
Subcellular Location: Plastid
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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 photons, and an electron transfer chain that converts photonic excitation into a charge separation. This subunit is found at the monomer-monomer interface.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3871
Sequence Length: 37
Subcellular Location: Plastid
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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
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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 activation of LHCSR3-dependent quenching in the antenna of photosystem II (PSII) .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26133
Sequence Length: 245
Subcellular Location: Plastid
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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 Topology: Multi-pass membrane protein
Sequence Mass (Da): 26950
Sequence Length: 254
Subcellular Location: Plastid
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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 photosynthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28008
Sequence Length: 265
Subcellular Location: Plastid
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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
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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
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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
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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
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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
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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
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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
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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
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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 oxidoreductase, using light energy to abstract electrons from H(2)O, generating a proton gradient subsequently used for ATP formation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 6764
Sequence Length: 62
Subcellular Location: Cellular thylakoid membrane
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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
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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.
Subcellular Location: Cytoplasm
EC: 3.4.25.1
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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 an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 33606
Sequence Length: 295
Pathway: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2.
Subcellular Location: Cell membrane
EC: 4.1.1.65
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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 an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 32614
Sequence Length: 297
Pathway: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2.
Subcellular Location: Cell membrane
EC: 4.1.1.65
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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 an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 25240
Sequence Length: 232
Pathway: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2.
Subcellular Location: Cell membrane
EC: 4.1.1.65
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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 an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 31093
Sequence Length: 280
Pathway: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2.
Subcellular Location: Cell membrane
EC: 4.1.1.65
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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 an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 25826
Sequence Length: 232
Pathway: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2.
Subcellular Location: Cell membrane
EC: 4.1.1.65
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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 an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 23407
Sequence Length: 214
Pathway: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2.
Subcellular Location: Cell membrane
EC: 4.1.1.65
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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 an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 23900
Sequence Length: 217
Pathway: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2.
Subcellular Location: Cell membrane
EC: 4.1.1.65
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P36081 | MRFHDSILIFFSLASLYQHVHGARQVVRPKEKMTTSEEVKPWLRTVYGSQKELVTPTVIAGVTFSEKPEETPNPLKPWVSLEHDGRPKTIKPEINKGRTKKGRPDYSTYFKTVSSHTYSYEELKAHNMGPNEVFVEEEYIDEDDTYVSLNPIVRCTPNLYFNKGLAKDIRSEPFCTPYENSRWKVDKTYFVTWYTRFFTDENSGKVADKVRVHLSYVKENPVEKGNYKRDIPATFFSSEWIDNDNGLMPVEVRDEWLQDQFDRRIVVSVQPIYISDEDFDPLQYGILLYITKGSKVFKPTKEQLALDDAGITNDQWYYVALSIPTVVVVFFVFMYFFLYVNGKNRDFTDVTRKALNKKRRVLGKFSEMKKFKNMKNHKYTELPSYKKTSKQN | 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 role in PMA1 maturation or quality control in the Golgi . PSG1 might also couple PMA1 sorting and maturation in the early secretory pathway with the glycosylation machinery (Probable).
PTM: The precursor protein is cleaved into two polypeptide chains, PSG1-N' and PSG1-C'. The cleavage is performed in the Golgi apparatus by Ca(+)-dependent serine protease KEX2 between Arg-229 and Asp-230.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 46036
Sequence Length: 392
Subcellular Location: Golgi apparatus lumen
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Q9VWU1 | MPLKWSLLLGTFVLISCSSVEAAVTVGRACKVTDTMPGICRTSSDCEPLIDGYIKSGVLTLNDVPSCGLGAWGEIFCCPTKPCCDNSTITSVSTSSTTSTKAPMTSGRVDVPTFGSGDRPAVAACKKIRERKQQRSGNQLVIHIVGGYPVDPGVYPHMAAIGYITFGTDFRCGGSLIASRFVLTAAHCVNTDANTPAFVRLGAVNIENPDHSYQDIVIRSVKIHPQYVGNKYNDIAILELERDVVETDNIRPACLHTDATDPPSNSKFFVAGWGVLNVTTRARSKILLRAGLELVPLDQCNISYAEQPGSIRLLKQGVIDSLLCAIDQKLIADACKGDSGGPLIHELNVEDGMYTIMGVISSGFGCATVTPGLYTRVSSYLDFIEGIVWPDNRV | 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 Length: 394
Domain: The clip domain consists of 35-55 residues which are 'knitted' together usually by 3 conserved disulfide bonds forming a clip-like compact structure.
Subcellular Location: Secreted
EC: 3.4.21.-
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