ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
P80209 | VIRIPLHKFTSIRRTMSEAAGXVXXLIAKGPISKYATGEPAVRQGPIPELLKNYMDAQYYGEIGIGTPPQCFTVVFDTGSANLWVPSIHCKLLDIACWTHRKYNSDKSSTYVKNGTTFDIHYGSGSLSGYLSQDTVSVPCNPSSSSPGGVTVQRQTFGEAIKQPGVVFIAAKFDGILGMAYPRISVNNVLPVFDNLMQQKLVDKNVFSFFLNRDPKAQPGGELMLGGTDSKYYRGSLMFHNVTRQAYWQIHMDQLDVGSSLTVCKGGCEAIVDTGTSLIVGPVEEVRELQKAIGAVPLIQGEYMIPCEKVSSLPEVTVKL... | Function: Acid protease active in intracellular protein breakdown. Plays a role in APP processing following cleavage and activation by ADAM30 which leads to APP degradation.
PTM: N- and O-glycosylated.
Catalytic Activity: Specificity similar to, but narrower than, that of pepsin A. Does not cleave the 4-Gln-|-His-5 bon... |
Q05744 | MAPRGLLVLLLLALVGPCAALIRIPLTKFTSTRRMLTEVGSEIPDMNAITQFLKFKLGFADLAEPTPEILKNYMDAQYYGEIGIGTPPQKFTVVFDTGSSNLWVPSVHCHLLDIACLLHHKYDASKSSTYVENGTEFAIHYGTGSLSGFLSQDTVTLGNLKIKNQIFGEAVKQPGITFIAAKFDGILGMAFPRISVDKVTPFFDNVMQQKLIEKNIFSFYLNRDPTAQPGGELLLGGTDPKYYSGDFSWVNVTRKAYWQVHMDSVDVANGLTLCKGGCEAIVDTGTSLITGPTKEVKELQTAIGAKPLIKGQYVISCDKI... | Function: Acid protease active in intracellular protein breakdown. In chicken it is a key enzyme for yolk formation as it is capable of catalyzing intra oocytic break down of protein components of both vitellogenin and VLDL.
Catalytic Activity: Specificity similar to, but narrower than, that of pepsin A. Does not cleav... |
O93428 | MKMLLLCVFSALALTNDALVRIPLKKFRSIRRQLTDSGKRAEELLADHHSLKYNLSFPASNAPTPETLKNYLDAQYYGEIGLGTPPQPFTVVFDTGSSNLWVPSIHCSLLDIACLLHHKYNSGKSSTYVKNGTAFAIQYGSGSLSGYLSQDTCTIGDLAIDSQLFGEAIKQPGVAFIAAKFDGILGMAYPRISVDGVAPVFDNIMSQKKVEQNVFSFYLNRNPDTEPGGELLLGGTDPKYYTGDFNYVNVTRQAYWQIRVDSMAVGDQLSLCTGGCEAIVDSGTSLITGPSVEVKALQKAIGAFPLIQGEYMVNCDTVPS... | Function: Acid protease active in intracellular protein breakdown.
Catalytic Activity: Specificity similar to, but narrower than, that of pepsin A. Does not cleave the 4-Gln-|-His-5 bond in B chain of insulin.
Sequence Mass (Da): 42958
Sequence Length: 396
Subcellular Location: Lysosome
EC: 3.4.23.5
|
O76856 | MKLLILTLFLATIVLAQALTVPLNFHQASRESRRRVPQKWSNRLSALNAGTTIPISDFEDAQYYGAITIGTPGQAFKVVFDTGSSNLWIPSKKCPITVVACDLHNKYNSGASSTYVANGTDFTIQYGSGAMSGFVSQDSVTVGSLTVKDQLFAEATAEPGIAFDFAKFDGILGLAFQSISVNSIPPVFYNMLSQGLVSSTLFSFWLSRTPGANGGELSFGSIDNTKYTGDITYVPLTNETYWEFVMDDFAIDGQSAGFCGTTCHAICDSGTSLIAGPMADITALNEKLGAVILNGEGVFSDCSVINTLPNVTITVAGREF... | Function: Protease that may act during cell growth and/or development.
PTM: N-glycosylated on 2 out of the 3 potential sites. Glycans contain sulfated Mannose.
Catalytic Activity: Specificity similar to, but narrower than, that of pepsin A. Does not cleave the 4-Gln-|-His-5 bond in B chain of insulin.
Sequence Mass (Da... |
P07339 | MQPSSLLPLALCLLAAPASALVRIPLHKFTSIRRTMSEVGGSVEDLIAKGPVSKYSQAVPAVTEGPIPEVLKNYMDAQYYGEIGIGTPPQCFTVVFDTGSSNLWVPSIHCKLLDIACWIHHKYNSDKSSTYVKNGTSFDIHYGSGSLSGYLSQDTVSVPCQSASSASALGGVKVERQVFGEATKQPGITFIAAKFDGILGMAYPRISVNNVLPVFDNLMQQKLVDQNIFSFYLSRDPDAQPGGELMLGGTDSKYYKGSLSYLNVTRKAYWQVHLDQVEVASGLTLCKEGCEAIVDTGTSLMVGPVDEVRELQKAIGAVPL... | Function: Acid protease active in intracellular protein breakdown. Plays a role in APP processing following cleavage and activation by ADAM30 which leads to APP degradation . Involved in the pathogenesis of several diseases such as breast cancer and possibly Alzheimer disease.
PTM: N- and O-glycosylated.
Catalytic Acti... |
P18242 | MKTPGVLLLILGLLASSSFAIIRIPLRKFTSIRRTMTEVGGSVEDLILKGPITKYSMQSSPKTTEPVSELLKNYLDAQYYGDIGIGTPPQCFTVVFDTGSSNLWVPSIHCKILDIACWVHHKYNSDKSSTYVKNGTSFDIHYGSGSLSGYLSQDTVSVPCKSDQSKARGIKVEKQIFGEATKQPGIVFVAAKFDGILGMGYPHISVNNVLPVFDNLMQQKLVDKNIFSFYLNRDPEGQPGGELMLGGTDSKYYHGELSYLNVTRKAYWQVHMDQLEVGNELTLCKGGCEAIVDTGTSLLVGPVEEVKELQKAIGAVPLIQ... | Function: Acid protease active in intracellular protein breakdown. Plays a role in APP processing following cleavage and activation by ADAM30 which leads to APP degradation.
PTM: N- and O-glycosylated.
Catalytic Activity: Specificity similar to, but narrower than, that of pepsin A. Does not cleave the 4-Gln-|-His-5 bon... |
P22686 | MAFALISNRALTVKVEAAKKAAGTKQTKAAPAKSAGIEWYGPDRAKWLGPFSTNTPAYLTGEFPGDYGWDTAGLSADPETFKKYRELEVIHARWALLGALGILTPELLSTYAGVKFGEPVWFKAGAQIFSEGGLDYLGSPALIHAQNIVATLAVQVVLMGLIEGYRVNGGPAGEGLDPLYPGESFDPLGLADDPDTFAELKVKEIKNGRLAMFSCFGFFVQAIVTGKGPIQNLADHLADPGTNNAFAAATKFTPSA | Cofactor: Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and carotenoids such as lutein and neoxanthin.
Function: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.
PTM: Photoregulated by reversible phos... |
P14273 | MAFALASRKALQVTCKATGKKTAAKAAAPKSSGVEFYGPNRAKWLGPYSENATPAYLTGEFPGDYGWDTAGLSADPETFKRYRELELIHARWAMLGALGCQTPELLAKSGTKFGEAVWFKAGAQIFSEGGLDYLGNPSLVHAQNIVATSAVQVILMGLIEGYRVNGGPAGEGLDPLYPGESFDPLGLADDPDTFAELKVKEIKNGRLASFSMFGFFVQAIVTGKGPVQNLDDHLANPTVNNAFAFATKFTPSA | Cofactor: Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and carotenoids such as lutein and neoxanthin.
Function: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.
PTM: Photoregulated by reversible phos... |
P20865 | MQLSTPPEVPDMKNTYSNNECPAAEQELCSEQGGRAGKSTKKGAKAVSKSSSSANQFYGPDATSGWDLQHQHPRLPTGEFPGDYGWDTAGLSADPETFKRYRELELIHARCGLLGALGMVTPELLADEDGIKFGDAAIWFKAGAAIFQDGGLNYLGNPSLIHAQNIVATLAVQVVLMGLVEGYRVNGGPAGEGLDPLYPGEAFDPLGLADDPDTFAELKVKEIKNGRLAMFACLGFFVQAIVTGKGPIENLTDHLANPAENNAFAYATKFTPQ | Cofactor: Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and carotenoids such as lutein and neoxanthin.
Function: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.
PTM: Photoregulated by reversible phos... |
P27517 | MAALIARSGLKALNIRQTRQQRMATVPRAAVEFYGPDRAKFLGPFSENDTPEYLTGEFPGDYGWDTAGLSADPQTFARYREIELIHARWALLGALGILTPELLSQYAGVQFGEPVWFKAGAQIFADGGLNYLGNESLIHAQSIIATLAVQVVLMGLAEAYRANGGSEGFLDDLDTLYPGGPFDPLGLADDPDTFAELKVKEIKNGRLAMFSCLGFFVQAIVTGKGPVQNLTDHLADPTVNKAFASATKFTPGV | Cofactor: Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and carotenoids such as lutein and neoxanthin.
Function: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.
PTM: Photoregulated by reversible phos... |
P15773 | MYIPRLSVSICLHPLLIYKIAKPSKLNPISSTLIVTAGFTMLKHAAKSKVSSSTCDRRVKYLGPFSGEWPSYLTGEFPGDYGWDTAGLSAYPETFAKNRELEVIHSRCAMSAALGCIFPELLSVMGQGFGEAVWFKAGAQIFSEGGLDYLGNPSLVHAQSILAIWTTKVILMGAVEGYRIARGPLGEVTDPLYPGSFDSLGLAEDTEAFAELKVKELKNGRLAMFSMFGFFVQAIVSRKDRLENLADHLGWTVNNNALSNVTNFVPGN | Cofactor: Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and carotenoids such as lutein and neoxanthin.
Function: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.
PTM: Photoregulated by reversible phos... |
Q9S7M0 | MASTFTSSSSVLTPTTFLGQTKASSFNPLRDVVSLGSPKYTMGNDLWYGPDRVKYLGPFSVQTPSYLTGEFPGDYGWDTAGLSADPEAFAKNRALEVIHGRWAMLGAFGCITPEVLQKWVRVDFKEPVWFKAGSQIFSEGGLDYLGNPNLVHAQSILAVLGFQVILMGLVEGFRINGLDGVGEGNDLYPGGQYFDPLGLADDPVTFAELKVKEIKNGRLAMFSMFGFFVQAIVTGKGPLENLLDHLDNPVANNAWAFATKFAPGA | Cofactor: Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and carotenoids such as lutein and neoxanthin.
Function: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated . Modulates the rate of photosystem II ... |
Q9XF88 | MAATSTAAAASSIMGTRVVSDISSNSSRFTARFGFGTKKASPKKAKTVISDRPLWFPGAKSPEYLDGSLVGDYGFDPFGLGKPAEYLQFDLDSLDQNLAKNLYGEVIGTRTEAVDPKSTPFQPYSEVFGLQRFRECELIHGRWAMLATLGAITVEWLTGVTWQDAGKVELVDGSSYLGQPLPFSISTLIWIEVLVIGYIEFQRNAELDSEKRLYPGGKFFDPLGLASDPVKKAQLQLAEIKHARLAMVGFLGFAVQAAATGKGPLNNWATHLSDPLHTTIIDTFSSS | Cofactor: Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and carotenoids such as lutein and neoxanthin.
Function: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated.
PTM: Photoregulated by reversible phos... |
O87692 | MDFRTEFKPLTVQPQQIEGKSFEMITEELGPHPFTDEQYPIVQRVIHRSADFELGRSMLFHPDAIQAGIKAIRSGKQVVADVQMVQVGTNKQRIEKHGGEIKVYISDSDVMEEAKRLNTTRAIISMRKAIKEADGGIFAIGNAPTALLELIRLIKEGEAKPGLVIGLPVGFVSAAESKEELAKLYVPFITNIGRKGGSTVTVAALNAISILADSGVTYEGSAKRT | Function: Catalyzes the conversion of cobalt-precorrin-8 to cobyrinate.
Catalytic Activity: Co-precorrin-8X = cob(II)yrinate
Sequence Mass (Da): 24520
Sequence Length: 225
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 9/10.
EC: 5... |
Q05601 | MHYIQQPQTIEANSFTIISDIIRETRPDYRFASPLHEAIIKRVIHTTADFDWLDILWFSADALEQLCDALRHPCIIYTDTTMALSGINKRLLATFGGECRCYISDPRVVRAAQTQGITRSMAAVDIAIAEEEKNKLFVFGNAPTALFRLLEHNVTVSGVVGVPVGFVGAAESKEALTHSHFPAVAALGRKGGSNVAAAIVNALLYHLREA | Function: Catalyzes the conversion of cobalt-precorrin-8 to cobyrinate.
Catalytic Activity: Co-precorrin-8X = cob(II)yrinate
Sequence Mass (Da): 23034
Sequence Length: 210
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 9/10.
EC: 5... |
P74304 | MIPLEHPILLESFAHIDRSVGPHNLSSQEYAIARRVIHSTADFDFLHLLRFAPDLPQAEFDPDLPEHQAIARGIESLRHGQTIVVDVNMVKQGIQGLVQRTFNNPIQTAIDFATIADPGKTRTETGMDRCIAQFPEAIYVIGNAPTALLTLCQAIAAGKAKPALVIGVPVGFIGVLEAKKALSLLPCPQIRVEGNKGGSPVAAGIVNALLMLAWREG | Function: Catalyzes the conversion of cobalt-precorrin-8 to cobyrinate.
Catalytic Activity: Co-precorrin-8X = cob(II)yrinate
Sequence Mass (Da): 23363
Sequence Length: 217
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 9/10.
EC: 5... |
Q8UBQ6 | METDGKTLRRGWTTGTCAAAATKAACAALLTGEFPYPVDVELPSGARPAFSLATEEKGENFARAGVVKDAGDDPDVTHGALIESTVRRGEPGSGITFRAGKGVGIITRPGLPLPPGEPAINPVPRRMIETAIREVAGENADFEVEISVRDGEKLAEKTLNGRLGILGGISILGTTGVVIPFSCSAWIHSIWRGIDVARATGCTHVLGATGNTSEKAGQAVYDLPETALIDMGDFIGGMLKYLRSHPVERVTIAGGVAKMTKLAQGMLDVHSKKGLADLEALAVLAAEAGGDDNLAVAIRQANMVAHAFQLAESVGIDLGA... | Function: Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.
Catalytic Activity: Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine
Sequence Mass (Da): 39088
Sequence Length: 376
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II... |
A6TJE5 | MERYIIKDGKKLRYGYTTGSCATAASKAAAQMLLQPGEVHEVDIDTPKGWSLKLKVEDIQRSHGAVSCAIIKDAGDDPDVTNKLAIYSKLIWRQDTKIEIHGGEGVGTVTRPGLQIPVGKPAINPIPLQMIEREVREVIGPGRGVDIVISVPKGQEVAKKTFNPKLGIQGGISILGTSGIVEPMSEEAMKDSLALELPMAKAEKIKTFVFVPGNYGRDMAREKYKIHDKNMIKISNFVGFMMDQSVIQNVERILIIGHIGKLVKVAGGIFHTHSKVADGRREILAAHLAALGASQQLVLRVLESNTTEEAVGLIQEKGFD... | Function: Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.
Catalytic Activity: Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine
Sequence Mass (Da): 41119
Sequence Length: 377
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II... |
O29535 | MLIDPIELYRYPEKWIKDRDAEKKVRSGLYILTEDGYLRRGITTGTTASAAAVAAIASLKEKVEKVKVSTPAGVDVEVEVEAEKGFARVRKFSGDHEFDVTNGIIFEAEVCETSGIFFGRGVGVKAGEKAVSRSAKLQILENFIKASREFNFSGGVRISVPDGEEVAKKTGNEKVGIKGGISILGTTGFVEPWCKKLVETKLKIAMQYHRIAITTGRKAWLYARKKFPEYQPFVFGVHIDEALKHPGEKIIVGFPGLLKIWAGSRDRIEERAREEGVRVVVIEDDMDSWVWDVQGTDH | Function: Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.
Catalytic Activity: Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine
Sequence Mass (Da): 33163
Sequence Length: 298
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II... |
A6X049 | MNDETAPTNKSQEKAELRRGWTTGACATAATKAALTALITGEFPDPVGIILPKGEVPYFQLAYEGLGDGYAMAGIVKDAGDDPDVTHGATIISTVFPAPPGTGVVFRAGEGVGTVTRPGLQIPPGEAAINPVPRRMMTEICEQICAEYGLPADIVITISVPGGEEIAKKTWNPRLGIVGGISILGTTGVVHPFSCSAWIHSIHRGIDVARAAGQKHVLGATGSTSEDAAQALYDLPDFAILDMGDFAGGVLKYLREHPIDKLTIAGGFAKLTKLAQGALDLHSSRSQVDKSFLWTLAEKAGAPESMKDQILFANTALEVL... | Function: Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.
Catalytic Activity: Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine
Sequence Mass (Da): 38543
Sequence Length: 368
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II... |
Q8GDE1 | MDEADEGRSLRRGWTTGACATAALKAALEALVDRPFPDPVALTLPRGERPAFALATRETGPGWARAGVIKDAGDDPDVTHGALIEATARLLPKGSGLIFRAGSGVGTVTKPGLPLAVGEPAINPVPRAMMTEVATAAGLADLEISIAVAQGASIALRTWNPRLGILGGLSILGTTGVVVPYSCSAWIHSIRRGVDVARATGRAHVVGTTGATSERAALDHLGLDAEAVIDMGDFVGGLLKYLRDHPIPHLTIAGGFAKLSKLADGALDLHSKRAQVDIPALARRLAALGATQAVVSEAERANTALEVLTLAQAAGLPLAT... | Function: Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.
Catalytic Activity: Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine
Sequence Mass (Da): 36399
Sequence Length: 357
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II... |
Q1AYB7 | MPERRELREPPMPPSMARVRGRKLRTGWTTGTCAAAAAKAAARALASGEAQEMVEVRLPGRGEGRRVRFGVERCELGEGWAEAVVVKDAGDDPDVTHGAHLTARVSWREEPGVELDRGEGVGVVTKPGLGLPVGAPAINPVPRRMILYSLEEALDTRRRGVRVVISVPGGEEMARKTTNPRLGIVGGISILGTTGIVRPFSTAAWAASVVQAIDVVAAQGGDTFVLSTGGLTERAAMRLLPHLEEVCFIEVGDFTGQAVRRAAKRGLGRGFFVGMAGKLAKLASGVMMTHWTRSRVDTSLLAEITRKAGGSERLAEEVEG... | Function: Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.
Catalytic Activity: Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine
Sequence Mass (Da): 41209
Sequence Length: 388
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II... |
B8I0Q1 | MEEFIVKNGKRLKCGYTTGSCAAAAVKAGAVMLLGRTTIDEVIVNTPKGIRLNLQIGDIYKQKECISCSVKKDAGDDPDVTDGIKIFAKVEKLEKEILIEGGSGIGRVTKSGLQCAVGEAAINPVPRQMIQEVLKEVSETYGYKGGFSVVISAEDGEEIAKKTFNPRLGITGGISILGTSGIVEPMSEKALIETIHREINVKITQNNEYFLVTPGNFGRDFALKRFGLDIDKGVKCSNYIGETIDYAVYNNIKNILLIGHAGKLCKIAGGIMNTHSRTADGRCEIFAAHAALCGASKECINNIMQSMTTDEINVILREEG... | Function: Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.
Catalytic Activity: Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine
Sequence Mass (Da): 42002
Sequence Length: 384
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II... |
Q97WC6 | MIINSLKRFGITTGAAASAAAKAAVIGLLNKEKRSTVVIPTPIGLRLEIPVEKVEIDSEISCAEVKKFSGDNPDILDGLVIRCCAKLNENNEIVIIGERGVGKVTRSGLKATMGEMAISPTVREMIINAIREVTDKGIQITIEVPNGETIAEKTLNKMVGIVGGISILGTTGIETPVSDDDYLEHIRCELNVIRQSYDYVVIAPGNSAAKYAAELFDSNCIIKVGDRIGDSIKLASNLFKKVILAGLPAKLLKVYAGIFNTHYSQGDARLESLTHASVLAGLPYGTLTKISNALSVEEAFTYMTKEQRRKVMNIVAEKIL... | Function: Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.
Catalytic Activity: Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine
Sequence Mass (Da): 37755
Sequence Length: 349
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II... |
Q8Z5M8 | MSELSFDAPVWRHGKALRKGYTTGSCATAAAKVAELMVLRQHLIHQVSIVTPSGVTLCLNVESPHIEGQQAIAAIRKDGGDDVDATHGMLIFARVTLNDSGEITLTGGEGIGTVTRKGVGLPLGSAAINRTPRHTIESAVREAIGPARGADVEIFAPEGEVRAQKTYNSRLGILGGISIIGTTGIVTPMSEESWKRSLSLELEIKRASGLTRVILVPGNHGERFVREQMGVDTQAVVTMSNFVGYMIEEAVRLGFCQIVLVGHPGKLIKIAAGIFHTHSHIADARMETLVAHLALLGAPLELLTLVGDCDTTEAAMEHIE... | Function: Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.
Catalytic Activity: Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A + S-adenosyl-L-homocysteine
Sequence Mass (Da): 40861
Sequence Length: 379
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II... |
Q9HKE4 | MRMEGENWVYEVRGIPDEFFQRSEGIPMTKREIRIISLSDLRIRPGMRVMDIGCGSGSMTVEISNIIGENGSVTGLDVSGEAADLTMRNCRNLCRFSNYRIVISDVYKYDSDEEFDAVFVGGGTARIHDLFERIERMVHHASRVVVNAIQIHTAYLSLEEMNTRGYSGVNITQVMVSNGMRTSEGYAMIARNPVFIISGDAP | Function: Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7.
Catalytic Activity: Co-precorrin-6B + S-adenosyl-L-methionine = Co-precorrin-7 + CO2 + S-adenosyl-L-homocysteine
Sequence Mass (Da): 22628
Sequence Length: 202
Pathway: Cofactor biosynt... |
Q97A64 | MESEKSKFDYYIVTPDSLFERVDGIPMTKEEIRLISLNRLGVRNGGHFLDIGTGTGSVAVDMSRLAGPNGKIIALDRDEKAIKLARINLDRLSPYKNIQLVLADAYAYSPADSFDAIFIGGGTGDLPNLVSKYVPFLKSGARVVINAIQVKTLNDAVESLELNNFRNVSVIEVQISVGMKTGSSYAMIARNPIFVVSGEQP | Function: Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7.
Catalytic Activity: Co-precorrin-6B + S-adenosyl-L-methionine = Co-precorrin-7 + CO2 + S-adenosyl-L-homocysteine
Sequence Mass (Da): 21884
Sequence Length: 201
Pathway: Cofactor biosynt... |
O29537 | MRRGLVIVGHGSQLNHYREVMELHRKRIEESGAFDEVKIAFAARKRRPMPDEAIREMNCDIIYVVPLFISYGLHVTEDLPDLLGFPRGRGIKEGEFEGKKVVICEPIGEDYFVTYAILNSVFRIGRDGKGEE | Function: Catalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis.
Catalytic Activity: Co-sirohydrochlorin + 2 H(+) = Co(2+) + sirohydrochlorin
Sequence Mass (Da): 15109
Sequence Length: 132
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II... |
Q9HQM3 | MQALVIVGHGSHLNPGSSEPAYTHADTIRESGAFDEVREAFWKEEPSFRNVLRTLESDEVYVVPLFISEGYFTEQVIPRELRLDDFDPDDWDSDGTDADHVTLEADDVEKTIHYCGPVGTHDSMSEVIVQRASSVTGREEFGDDFGLAVVGHGTERNENSAKAIYYHADQIREMGVFGEVQAVFMDEDPEVDDVTDFFDTDDIVVVPLFVSDGFHTQEDIPEDMGLTDDYRTGYDIPTAVDGHDIWYSGAVGTEPLAADVVLERAADAGAPVGDAVDAVREQTRGANAAAGD | Function: Catalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis.
Catalytic Activity: Co-sirohydrochlorin + 2 H(+) = Co(2+) + sirohydrochlorin
Sequence Mass (Da): 31985
Sequence Length: 292
Domain: Seems to consist of two fused copies of the CbiX domain, resem... |
O87690 | MGGHYMKSVLFVGHGSRDPEGNDREFISTMKHDWDASILVETCFLEFERPNVSQGIDTCVAKGAQDVVVIPIMLLPAGHSKIHIPAAIDEAKEKYPHVNFVYGRPIGVHEEALEILKTRLQESGENLETPAEDTAVIVLGRGGSDPDANSDLYKITRLLWEKTNYKIVETSFMGVTAPLIDEGVERCLKLGAKKVVILPYFLFTGVLIKRLEEMVKQYKMQHENIEFKLAGYFGFHPKLQTILKERAEEGLEGEVKMNCDTCQYRLGIMEHIDHHHHHDHDHDHDHGHHHHDHHHDHHEDKVGELK | Cofactor: Binds 1 [4Fe-4S] cluster per dimer.
Function: Chelates cobalt to the cobalamin precursor as part of the anaerobic pathway to cobalamin biosynthesis.
Catalytic Activity: Co-sirohydrochlorin + 2 H(+) = Co(2+) + sirohydrochlorin
Sequence Mass (Da): 34882
Sequence Length: 306
Pathway: Cofactor biosynthesis; adeno... |
Q980A7 | MLGVLLVLHGSKIPEWKDVGIKYAEYLSKYFSLVEFGFLEFNKPTLSEALSNLLAKGADKIVVVPLLFATGTHFRRDIPRLLGIDNDEKKIRYMGREIEITIADPLGFDEKIGEVLVKRVNETYNKNY | Function: Catalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis.
Catalytic Activity: Co-sirohydrochlorin + 2 H(+) = Co(2+) + sirohydrochlorin
Sequence Mass (Da): 14606
Sequence Length: 128
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II... |
Q4JAI2 | MIGLLLVLHGSKIKEWQEIVINYAEELKRHFPLVEYGFIEINEPKIDEAAKKLVERGADTIVVVPLLFAAGMHFKRDIPNQLKETSNKAKIIIAEPIGFDKRIVDILKEKAEKALSVEGTSYQ | Function: Catalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis.
Catalytic Activity: Co-sirohydrochlorin + 2 H(+) = Co(2+) + sirohydrochlorin
Sequence Mass (Da): 13941
Sequence Length: 123
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II... |
Q55451 | MTLTSVPAPVSLFPELELPPLPYHRPLLMIGHGTRDEDGRQTFLDFVAQYQALDHSRPVIPCFLELTEPNIQAGVQQCVDQGFEEISALPILLFAARHNKFDVTNELDRSRQAHPQINFFYGRHFGITPAILDLWKARLNQLDSPEANPQGIDRQDTVLLFVGRGSSDPDANGDVYKMARMLWEGSGYQTVETCFIGISHPRLEEGFRRARLYQPKRIIVLPYFLFMGALVKKIFTITEEQRATFPEIEIQSLSEMGIQPELLALVREREIETQLGQVAMNCEACKFRLAFKNQGHGHDHGHGHHHHGHDHGHSHGEWVD... | Cofactor: Binds 1 [4Fe-4S] cluster per dimer.
Function: Chelates cobalt to the cobalamin precursor as part of the anaerobic pathway to cobalamin biosynthesis.
Catalytic Activity: Co-sirohydrochlorin + 2 H(+) = Co(2+) + sirohydrochlorin
Sequence Mass (Da): 38340
Sequence Length: 336
Pathway: Cofactor biosynthesis; adeno... |
Q9HPK9 | MFETTLHDGVLELAAPGARWLSTGWNGGDTRADRAYSITVPDDWAPDSTHEYVTDRLAAAGFAPRDDAPVLLTGVAQEHARIARCGPVAVAATAGLSNPAALPMDPDGGTLPDAKRAPPGTVNLVAATTRALDDAALSNLVAVAAEAKAATLLATAGFPGTTSDAVVVACDPGGETAPYSGSATPVGAATRACVREAVRASLDSRDAASPDSVESAAHGTTTDVQAAVFRP | Function: Converts adenosylcobinamide (AdoCbi) to adenosylcobyric acid (AdoCby), an intermediate of the de novo coenzyme B12 biosynthetic route.
Catalytic Activity: adenosylcob(III)inamide + H2O = (R)-1-aminopropan-2-ol + adenosylcob(III)yrate
Sequence Mass (Da): 23242
Sequence Length: 231
Pathway: Cofactor biosynthesi... |
Q8Q0G3 | MQYHIKDQTLIIKGDFEAVSTGLNGGRARVEYIFNKQVPRTFNPPSPEEFIREEARKDGIETASLGLLTAVNMEYLQVIEDDYMTAFITAGVSNCSEFRAKAGTINIILVSKARLSETALFGAIITATEAKGLALLEKGYNFLGTNTDAVIVAYETCSDSGPKSKTNQEIPYAGSSTEFGKKITEAVIKGIKAGLELRGE | Function: Converts adenosylcobinamide (AdoCbi) to adenosylcobyric acid (AdoCby), an intermediate of the de novo coenzyme B12 biosynthetic route.
Catalytic Activity: adenosylcob(III)inamide + H2O = (R)-1-aminopropan-2-ol + adenosylcob(III)yrate
Sequence Mass (Da): 21713
Sequence Length: 200
Pathway: Cofactor biosynthesi... |
Q9I589 | MKHYSATLALLPLTLALFLPQAAHAHGSMETPPSRVYGCFLEGPENPKSAACKAAVAAGGTQALYDWNGVNQGNANGNHQAVVPDGQLCGAGKALFKGLNLARSDWPSTAIAPDASGNFQFVYKASAPHATRYFDFYITKDGYNPEKPLAWSDLEPAPFCSITSVKLENGTYRMNCPLPQGKTGKHVIYNVWQRSDSPEAFYACIDVSFSGAVANPWQALGNLRAQQDLPAGATVTLRLFDAQGRDAQRHSLTLAQGANGAKQWPLALAQKVNQDSTLVNIGVLDAYGAVSPVASSQDNQVYVRQAGYRFQVDIELPVEG... | Function: Binds chitin but does not hydrolyze it, has no detectable protease or staphylolytic activity.
PTM: Can be detected in the extracellular supernatant as a 43 kDa protein and a 23 kDa protein, both proteins have the same N-terminus . Only the larger protein binds chitin, which may protect it from further process... |
O17754 | MLHAMRPVLLVAALLAVTAHAFLGFGSGSTHKDDAEWGHYHNQAQLEAKLGEINEKCPEITTLYEIGQSVEGRPLVVIQFSTTPGEHIPTKPEVKLIGNMHGNEPIGRELLLRFAETLCNGAINNDKEIVQLLNSTSIHILPSMNPDGFELALGTEPAQRQWLTGRSNINGVDLNRDFPDLDSIFYELQKIGVPKFDHLLSLFEDNVDRQPETIAVGQWTLSLPFVLSANFHEGDLVANYPFDAAIDENSQKTAYSASPDDGTFRWLAKSYADNHAHMSKNDHAPCDGTSQDAFARQGGITNGAKWYSVAGGMQDFNYLA... | Cofactor: Binds 1 zinc ion per subunit.
Function: During FMRFamide-like peptide (FaRPs or FLP) and neuropeptide-like protein (NLP) precursor processing, catalyzes the removal of Arg or Lys residues from the C-terminus following the initial endoprotease cleavage . By processing neuropeptides, modulates basal acetylcholi... |
P16870 | MAGRGGSALLALCGALAACGWLLGAEAQEPGAPAAGMRRRRRLQQEDGISFEYHRYPELREALVSVWLQCTAISRIYTVGRSFEGRELLVIELSDNPGVHEPGEPEFKYIGNMHGNEAVGRELLIFLAQYLCNEYQKGNETIVNLIHSTRIHIMPSLNPDGFEKAASQPGELKDWFVGRSNAQGIDLNRNFPDLDRIVYVNEKEGGPNNHLLKNMKKIVDQNTKLAPETKAVIHWIMDIPFVLSANLHGGDLVANYPYDETRSGSAHEYSSSPDDAIFQSLARAYSSFNPAMSDPNRPPCRKNDDDSSFVDGTTNGGAWY... | Cofactor: Binds 1 zinc ion per subunit.
Function: Sorting receptor that directs prohormones to the regulated secretory pathway. Acts also as a prohormone processing enzyme in neuro/endocrine cells, removing dibasic residues from the C-terminal end of peptide hormone precursors after initial endoprotease cleavage.
Catal... |
P37892 | MKQICSIVLLGAAVVSLVSAAGSDSEISFEYHRYEELRKALVSVWLQCPTIARIYTIGESFEGRELLVLEMSDNPGTHEPGEPEFKYIANMHGNEAVGRELLIYLAQYLCNQYQQGNETIIDLIHSTRIHLMPSMNPDGFEKAASQPGEIKDWFVGRSNAQGVDLNRNFPDLDRIIYTNEREGGANNHLLQNMKKAVDENTKLAPETKAVIHWIMEIPFVLSANLHGGDVVANYPYDETRTGSTHEYSASPDDVIFKSLAKAFSIYNPVMSDPQRPPCRKHDDDSSFKDGITNGGAWYSVPGGMQDFNYLSSNCFEITLE... | Cofactor: Binds 1 zinc ion per subunit.
Function: Removes residual C-terminal Arg or Lys remaining after initial endoprotease cleavage during prohormone processing.
Catalytic Activity: Release of C-terminal arginine or lysine residues from polypeptides.
Location Topology: Peripheral membrane protein
Sequence Mass (Da):... |
P15087 | MAGRGGRVLLALCAALVAGGWLLAAEAQEPGAPAAGMRRRRRLQQEDGISFEYHRYPELREALVSVWLQCTAISRIYTVGRSFEGRELLVIELSDNPGVHEPGEPEFKYIGNMHGNEAVGRELLIFLAQYLCNEYQRGNETIVNLIHSTRIHIMPSLNPDGFEKAASQPGELKDWFVGRSNAQGIDLNRNFPDLDRIVYVNEKEGGPNNHLLKNLKKIVDQNSKLAPETKAVIHWIMDIPFVLSANLHGGDLVANYPYDETRSGTAHEYSSCPDDAIFQSLARAYSSFNPVMSDPNRPPCRKNDDDSSFVDGTTNGGAWY... | Cofactor: Binds 1 zinc ion per subunit.
Function: Sorting receptor that directs prohormones to the regulated secretory pathway. Acts also as a prohormone processing enzyme in neuro/endocrine cells, removing dibasic residues from the C-terminal end of peptide hormone precursors after initial endoprotease cleavage.
Catal... |
P06621 | MRPSIHRTAIAAVLATAFVAGTALAQKRDNVLFQAATDEQPAVIKTLEKLVNIETGTGDAEGIAAAGNFLEAELKNLGFTVTRSKSAGLVVGDNIVGKIKGRGGKNLLLMSHMDTVYLKGILAKAPFRVEGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDYGTITVLFNTDEEKGSFGSRDLIQEEAKLADYVLSFEPTSAGDEKLSLGTSGIAYVQVNITGKASHAGAAPELGVNALVEASDLVLRTMNIDDKAKNLRFNWTIAKAGNVSNIIPASATLNADVRYARNEDFDAAMKTLEERAQQKKLPEADVKVIV... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the hydrolysis of reduced and non-reduced folates to pteroates and L-glutamate. This enzyme has a broad specificity.
Catalytic Activity: Release of C-terminal glutamate residues from a wide range of N-acylating moieties, including peptidyl, aminoacyl, benzo... |
Q7SIB1 | MKPPFQEALGIIQQLKQHGYDAYFVGGAVRDLLLGRPIGDVDIATSALPEDVMAIFPKTIDVGSKHGTVVVVHKGKAYEVTTFKTDGDYEDYRRPESVTFVRSLEEDLKRRDFTMNAIAMDEYGTIIDPFGGREAIRRRIIRTVGEAEKRFREDALRMMRAVRFVSELGFALAPDTEQAIVQNAPLLAHISVERMTMEMEKLLGGPFAARALPLLAETGLNAYLPGLAGKEKQLRLAAAYRWPWLAAREERWALLCHALGVQESRPFLRAWKLPNKVVDEAGAILTALADIPRPEAWTNEQLFSAGLERALSVETVRAAF... | Function: Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. tRNA 3'-terminal CCA addition i... |
P45269 | MKVYLVGGAVRDQLLGLPVKDRDWIVVGADPATLLSLGYQQVGKDFPVFLNPKTKEEYALARTERKSSAGYTGFICDFSPTITLEQDLIRRDLTINAMAQSEDGEIIDPYGGKQDLENRILRHISPAFSEDPLRVLRVARFAARYHSLGFKIASETLALMAELAQSGELQHLTAERIWLETEKALNEKNPEIYFETLHKTGALSVLFSEIDALYGVPNPVKHHPEVDSFIHTMLVLKQAVNLTENNPILNKSAVRFAAICHDLGKALTPQNILPHHYGHEQAGIKPTRSLCKRLKVPSYFQELAELTCEFHTHIHKAFEL... | Cofactor: Magnesium is required for nucleotidyltransferase activity.
Function: Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates a... |
B9LS95 | MDDLEAVLSRVRDRAVPEPAERDRLRTVAVELADRTREAIADLPVDADVVQVGSTARDTWVSGDRDIDLFVRFDAALDREQLEEYGLAVGHAVLPDGHEEYAEHPYVKGTYEGFDVDLVPCHDVETAGDLISAVDRTPFHDAYLSARLDEGLADDVVLAKAFLKGIGAYGSDLRTEGFSGYLTELLVLELGGFVPLVESARSWHPPVEFDPEGHAERTFDDPLVVVDPTDPTRNVAAVLSAENLARFQHYARELLAAPSEAPFEPVDPAPLDPTDVRDHLDRRETTPVAVVFDAPDLVDDQLWPQLRRSLDGIVRGLNDR... | Function: Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. tRNA 3'-terminal CCA addition i... |
Q5V030 | MSDEFDAVVGKVRARASPTDDERAQLQRVADAVMADAEAAIADLPVEAEVVQVGSTARGTWTAGDRDVDVFVCFPPSIDREALEEYGLAVGHDVLPDGREEYAEHPYVVGEREGYAVDLVPCYAVENATEIQSAVDRTPFHTRYLQERLDDNSAAEVRVAKQFLKGIGVYGSDLRTRGFSGYLTELLVLEFGGFRAFLEAVADWHPPVRLDPDDHGSETFDDPLVVIDPTDPERNVAAVLSETNVATLQHYARDLLAEPRVSLFTEDDPCPFEAADVEAAVSQRGTTPVALRFAAPDVVDDQLWPQLRKSLDGLCSELDR... | Function: Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. tRNA 3'-terminal CCA addition i... |
Q5QY23 | MDVYLVGGAVRDKLLKLPVHERDWVVVGARAEDLLKQGFLQVGKDFPVFLHPSTREEYALARTERKSGKGHTSFDVFASPDVTLEDDLARRDLTINAIAQSEDGEIVDPYNGVQDIKARKLRHVSEAFTEDPLRVLRVARFAARFAHLDFTVAEETQQMLQEMSASQELSHLVPERVWREWEKSLLTQTPTVFLTLLRDIQALSQVLPGITADDSQLQRLQRTSAYSDSVTLRFASLFIEQETPESLKQFCRQLAIPNHYRDSALLARNHEDFITTPELPEKAQLAALLKQIDYWRRPEKLEQLLQLRQAEYSESKQQKS... | Function: Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. tRNA 3'-terminal CCA addition i... |
Q88A53 | MQIYKVGGAVRDRLLGQPVTDIDWVVVGASTEDMLVKGYRPVGTDFPVFLHPLTNEEYALARTERKSGVGYGGFVFHASPDVTLEQDLIRRDLTINAMAEDKDGNLTDPYNGQQDLEARVLRHVSPAFAEDPLRVLRVARFAARYAGHGFTVAPETLELMRQLSESGELKALTAERSWKEISRALMEDQPQVFIQVLHDCGALSELMPEVEALFGVPQPAAHHPEIDTGVHVLSVLEQSAIHKHPLTVRWACLLHDLGKGLTPESEWPRHIAHEHTGLRLIKAVNERFRVPRDCQELALLVGQYHTHGHRALELKPSTLL... | Cofactor: Magnesium is required for nucleotidyltransferase activity.
Function: Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates a... |
Q9V2H1 | MLKMTLKEVLESIKPKDEERKKVKLIMDELRGIAQEVIEESGEEIEVKFVGSLAKDTYLSGDHDIDMFLAFPLSIPVEKLKSKGLEIAESIGKRLESYEISYAEHPYVRGVYKGYQVDIVPCYNVRDWREVRTAVDRSILHTEWVLKNIKGKNDEVRLLKRFLKGINAYGSEVYRRGFSGYLAEILVIKFGSFLKVLEKADFMLRQKIIDPENWLKREPEIAMKTVKREIEEDKPIIVIDPVDPRRNVAANLSWERYGLFYFKAREFLTKPSTELFFPRDKKGNYLEVLRRKGTHLVTLTFEPPNLVDDIIIPQVERTAK... | Function: Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. tRNA 3'-terminal CCA addition i... |
A1RS16 | MSTLEEVLREAYKLVTPSEEEERELKKVTEKVKALIADAINKYGIEAEIGVYGSSARSTWLPGQRDIDIFIVLTNRNINIKDVITLLSRYFSERGVTWSMRYAQHPYLSLLVDGYEVDVVPCYKISFGERPITAADRTPLHHKFLVEKLSEEQRRDVRLLKLFMKTIGVYGAEIKVEGFSGYLTELLVAYYGSFIDVLKAASRWRPYRTYITFSESRAKFKAPLVVVDPVDPERNVAAAVSLTSMSTFILASRRFLKNPSITYFQQRQGAVIKTNVVEVVFPYPNEPPDIVWGRYKRIGRSVFNWLKQCGFRVYRWGVES... | Function: Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. tRNA 3'-terminal CCA addition i... |
P77978 | MIEEEVLKIIKPTEEDKKGIEKVLEIIRERLNKLDFEVEGSFRKGTWLRQDTDVDVFVFYPKDVGKEYLERNALNDIINRIKDLDYTLAYAEHPYVIVNINNVEVDIVPALRVESGDRAITAVDRTPFHTKYVTSHLDERGKDEVRLLKRFMKGIGVYGAELKVQGFSGYATELLVIYYGSFRKVLEAASKWKHPIKIELTKPMRAFSEPLIIPDPVDPRRNVTAAVSLKNIATFSVAAKYYLKNPSMEFFFPSKKVEEKIKGDVLILRLNLDEKSSEDIIWGQIKRSVNKIERALKQSGFRVIDIQAWGDTSNIVIAVQ... | Function: Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template . Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate . tRNA 3'-terminal CCA addition... |
O65572 | MAEKLSDGSSIISVHPRPSKGFSSKLLDLLERLVVKLMHDASLPLHYLSGNFAPIRDETPPVKDLPVHGFLPECLNGEFVRVGPNPKFDAVAGYHWFDGDGMIHGVRIKDGKATYVSRYVKTSRLKQEEFFGAAKFMKIGDLKGFFGLLMVNVQQLRTKLKILDNTYGNGTANTALVYHHGKLLALQEADKPYVIKVLEDGDLQTLGIIDYDKRLTHSFTAHPKVDPVTGEMFTFGYSHTPPYLTYRVISKDGIMHDPVPITISEPIMMHDFAITETYAIFMDLPMHFRPKEMVKEKKMIYSFDPTKKARFGVLPRYAKD... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Cleaves a variety of carotenoids symmetrically at both the 9-10 and 9'-10' double bonds. Active on beta,beta-carotene, lutein, zeaxanthin, all-trans-violaxanthin, 9-cis-violaxanthin and 9'-cis-neoxanthin. With most substrates, the carotenoid is symmetrically cleaved. ... |
Q8LP17 | MGSEKKENGVILEVEPKPSNGFTSKAVDLLEKIIVKLFYDSSLPHHWLSGNFAPVKDETPPVKDLTVQGHLPDCLNGEFVRVGPNPKFSPVAGYHWFDGDGMIHGLRIKDGKASYVSRFVKTSRFKQEEYFNGSKFMKIGDLKGLFGLLMVNMQMLRAKLKILDVSYGHGTANTALVYHHQKLLALSEGDKPYAIKVFEDGDLQTLGMLDYDKRLGHNFTAHPKVDPFTGEMFTFGYSHTAPYVTYRVISKDGFMQDPVPITISDPVMMHDFAITENYSIFMDLPLYFRPKEMVKNKTLIFSFDSTKKARFGVLPRYAKD... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Cleaves a variety of carotenoids at the 9-10 and 9'-10' double bonds. Probably not involved in abscisic acid biosynthesis (By similarity).
Catalytic Activity: all-trans-zeaxanthin + 2 O2 = 2 (3R)-hydroxy-beta-ionone + 4,9-dimethyldodeca-2,4,6,8,10-pentaenedial
Sequenc... |
Q94IR2 | MGDDGKKNGAEGGLVKVDPKPTNGFSSKVIDLLEKLLVKFLYDSSLPHHYLTGNFGPVTETPPTKDLPVKGHLPDCLNGEFVRVGPNPKFAPVAGYHWFDGDGMIHGLRIKDGKATYVSRFVETSRLKQEEYFGRSKFMKIGDLKGLFGLLMVNIHMLRTKLKVLDLSYGGGTTNTALVYHHGKLLALSEADKPYAIKVFEDGDLQTLGMLDYDKRLGHSFTAHPKVDPFTGEMFSFGYAHTPPYITYRVISKDGYMHDPVPITISDPIMMHDFAITENYAVFMDLPLIFRPKEMVKNKTLIFSFDSTKKARFGVLPRYA... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Cleaves a variety of carotenoids at the 9-10 and 9'-10' double bonds. Probably not involved in abscisic acid biosynthesis.
Catalytic Activity: all-trans-zeaxanthin + 2 O2 = 2 (3R)-hydroxy-beta-ionone + 4,9-dimethyldodeca-2,4,6,8,10-pentaenedial
Sequence Mass (Da): 611... |
Q93VD5 | MATSLTLIATPCTAPRSSSSFALAPRLPPRCSNATAARRRAVRATTLQSDQEPAGSGDSGATTTKLSASTSVRQERWEGDLPIEGCLPPWLNGTYIRNGPGMWDVGEHAFHHLFDGYATLVRVSFRGGGGARATGAHRQIESEAYRAAVARGRPVLREFSHCPAPAKSLLHRFGDLVGLVTGAALTDNPNSAVLPLGDGRVMCLTETTKSSVLIDPDTLETVGRFRYTDRLGGMVQSAHPIVTDTEFLTLLPDLVRPGHLVVRMEAGSNERKVIGRMDCRGGPSPGWLHSFAVTEKYAVVPEMPLRYSSASLLASELAPF... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: May be involved in strigolactones biosynthesis.
Sequence Mass (Da): 59916
Sequence Length: 552
Subcellular Location: Plastid
EC: 1.13.11.-
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Q8LIY8 | MSPAMLQASSLCVSAALSGAASRPGRLASQGHQGKRAVAQPLAASAVTEAAPPAPVVAPPARPVDAPRRRGGRGGGGGGGELVAWKSVRQERWEGALEVDGELPLWLDGTYLRNGPGLWNLGDYGFRHLFDGYATLVRVSFRGGRAVGAHRQIESEAYKAARAHGKVCYREFSEVPKPDNFLSYVGQLATLFSGSSLTDNSNTGVVMLGDGRVLCLTETIKGSIQVDPDTLDTVGKFQYTDKLGGLIHSAHPIVTDTEFWTLIPDLIRPGYVVARMDAGSNERQFVGRVDCRGGPAPGWVHSFPVTEHYVVVPEMPLRYC... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Involved in strigolactones biosynthesis by cleaving the C(27) 9-cis-10'-apo-beta-carotenal produced by CCD7. Produces the C(19) carlactone and a C(8) hydroxyaldehyde. Also shows lower activity with all-trans-10'-apo-beta-carotenal producing a C(9) dialdehyde and the C... |
Q8VY26 | MASLITTKAMMSHHHVLSSTRITTLYSDNSIGDQQIKTKPQVPHRLFARRIFGVTRAVINSAAPSPLPEKEKVEGERRCHVAWTSVQQENWEGELTVQGKIPTWLNGTYLRNGPGLWNIGDHDFRHLFDGYSTLVKLQFDGGRIFAAHRLLESDAYKAAKKHNRLCYREFSETPKSVIINKNPFSGIGEIVRLFSGESLTDNANTGVIKLGDGRVMCLTETQKGSILVDHETLETIGKFEYDDVLSDHMIQSAHPIVTETEMWTLIPDLVKPGYRVVRMEAGSNKREVVGRVRCRSGSWGPGWVHSFAVTENYVVIPEMP... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Involved in strigolactones biosynthesis by cleaving the C(27) 9-cis-10'-apo-beta-carotenal produced by CCD7. Produces the C(19) carlactone and a C(8) hydroxyaldehyde. Also shows lower activity with all-trans-10'-apo-beta-carotenal producing a C(9) dialdehyde and the C... |
Q7Z6B0 | MDDDDFGGFEAAETFDGGSGETQTTSPAIPWAAFPAVSGVHLSPSSPEIVLDRDHSSSIGCLSSDAIISSPENTHAANSIVSQTIPKAQIQQSTHTHLDISLFPLGLTDEKSNGTIALVDDSEDPGANVSNIQLQQKISSLEIKLKVSEEEKQRIKQDVESLMEKHNVLEKGFLKEKEQEAISFQDRYKELQEKHKQELEDMRKAGHEALSIIVDEYKALLQSSVKQQVEAIEKQYISAIEKQAHKCEELLNAQHQRLLEMLDTEKELLKEKIKEALIQQSQEQKEILEKCLEEERQRNKEALVSAAKLEKEAVKDAVLK... | Function: Involved in the regulation of membrane traffic through the trans-Golgi network (TGN). Functions in close cooperation with the GGAs in the sorting of hydrolases to lysosomes.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 49971
Sequence Length: 441
Subcellular Location: Membrane
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Q53HC0 | MTSPHFSSYDEGPLDVSMAATNLENQLHSAQKNLLFLQREHASTLKGLHSEIRRLQQHCTDLTYELTVKSSEQTGDGTSKSSELKKRCEELEAQLKVKENENAELLKELEQKNAMITVLENTIKEREKKYLEELKAKSHKLTLLSSELEQRASTIAYLTSQLHAAKKKLMSSSGTSDASPSGSPVLASYKPAPPKDKLPETPRRRMKKSLSAPLHPEFEEVYRFGAESRKLLLREPVDAMPDPTPFLLARESAEVHLIKERPLVIPPIASDRSGEQHSPAREKPHKAHVGVAHRIHHATPPQAQPEVKTLAVDQVNGGKV... | Function: Interferon-stimulated protein that plays a role in innate immunity. Strongly inhibits ebolavirus transcription and replication. Forms a complex with viral RNA-bound nucleocapsid NP and thereby prevents the transport of NP to the cell surface.
PTM: Phosphorylated at Ser-209 by TTBK2.
Sequence Mass (Da): 36961
... |
Q8VDN4 | MAATNLENQLHSAQKNLLFLQREHASTLKGLHAEIRRLQQHCTDLTYELTLKSFELTGDSSSRTTELKRRCEELEAQLKAKEEENRKLLQELEQKNAAIAVLENTVREREKKYLEELKVKSHKLSMLSGELEQRASTVAYLTSQLHAAKKKLLSSSGTSDASPAGSPALASYKPTPPKDKLPETPRRRMKKSLSAPLHPEFEEVYRFGAESRKLLLREPVDAMPDPTPFLLARESAEVQLKERPLVIPPIASDRSATGQHSPARDKPHKTHVGVAHRIHHATPSQAQPEGEMRAVDQVNASKVVRKHSGTDRTV | Function: Interferon-stimulated protein that plays a role in innate immunity.
PTM: Phosphorylated at Ser-192 by TTBK2.
Sequence Mass (Da): 35207
Sequence Length: 314
Subcellular Location: Cytoplasm
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P78556 | MCCTKSLLLAALMSVLLLHLCGESEAASNFDCCLGYTDRILHPKFIVGFTRQLANEGCDINAIIFHTKKKLSVCANPKQTWVKYIVRLLSKKVKNM | Function: Acts as a ligand for C-C chemokine receptor CCR6. Signals through binding and activation of CCR6 and induces a strong chemotactic response and mobilization of intracellular calcium ions . The ligand-receptor pair CCL20-CCR6 is responsible for the chemotaxis of dendritic cells (DC), effector/memory T-cells and... |
Q5LL36 | MASLKKSRRVRLILFSGVALVSATALIGYAMRDGIQFFRTPTEVATDPPAANEVLRIGGMVEHGSLVRDGANFSFRVTDGETSFPISYVGIVPDLFREGEGTIATGSVIGGVFRATEILAKHDEVYMPSELAEMEALRD | Function: Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 15009
Sequence Length: 139
Subcellular Loc... |
Q3BSK6 | MNPQRRRRLWLVLALVLAGGLATTLVAMALQRNVAYLYTPSEVLRGDAGAHSRFRLGGMVEKGSFKRASGALEAQFRVTDGDAQLPVSYDRILPDLFREGQAVVATGRMQNGIFVAEDVLAKHDETYMPKEVADKMGSAHRKHDVPTAAGQAGELH | Function: Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 17029
Sequence Length: 156
Subcellular Loc... |
A5G2G1 | MMSRKKRRLWIVIACGIGLSTAVALMLFAFRSSLSFFMSPEQVAARHPPPGRVFRLGGIVQANTVVMGTRNGAPYTTFRITDGRASIPVVYTGVLPGLFRQGQGVVTIGAMAKGDSEFMASTVLAKHGADYMPRDVEMALRKAGKWNPKFGPPPNAGAWDDKSPAQIEASNNG | Function: Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 18598
Sequence Length: 173
Subcellular Loc... |
Q8EK44 | MNPRRKKRLTLAVALIGGVAAIASLLLYALNSNLNLFYTPSEIVNGKTDTGVKPEAGQRIRVGGMVTVGSMVRDPNSLHVQFAVHDSLGGEILVTYDDLLPDLFREGQGIVAQGVLGEDGKLAATEVLAKHDENYMPPEVAEAMGQKHEKLDYSQQKSATQ | Function: Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH (By similarity).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 17358
Sequence Length: 161... |
Q2KI22 | MAHQLLCCEMETIRRAYPDANLLNDRVLRAMLKAEETCAPSVSYFKCVQKEILPSMRKIVATWMLEVCEEQKCEEEVFPLAMNYLDRFLSLEPVKKSRLQLLGATCMFVASKMKETIPLTAEKLCIYTDNSIRPDELLHMELVLVNKLKWNLAAMTPHDFIEHFLSKMPVAEENKQIIRKHAQTFVALCATDVKFISNPPSMVAAGSVAAAAQGLHLGSANGFLSYHRLTRFLSKVIRCDPDCLRACQEQIEALLESSLRQAQQQNLDPKAAEEEEEEEEVDLACTPTDVRDVNI | Function: Regulatory component of the cyclin D1-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and... |
Q64HP0 | MAHQLLCCEVETIRRAYPDANLLNDRVLRAMLKAEETCAPSVSYFKCVQKEILPSMRKIVATWMLEVCEEQKCEEEVFPLAMNYLNRFLSLEPVKKSRLQLLGATCMFVASKMKETIPLTAEKLCIYTDNSIRPDELLQMELLLVNKLKWNLAAMTPHDFIEHFLSKMPVAEENKQIIRKHAQTFVALCATDVKFISNPPSMVAAGSVVAAVQGLHLGSSNSFLSYHRLTRFLSKVIKCDADCLRACQEQIEALLESSLRQAQQQSLDPKAAEEEEEEEEADLACTPTDVRDVNI | Function: Regulatory component of the cyclin D1-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and... |
P24385 | MEHQLLCCEVETIRRAYPDANLLNDRVLRAMLKAEETCAPSVSYFKCVQKEVLPSMRKIVATWMLEVCEEQKCEEEVFPLAMNYLDRFLSLEPVKKSRLQLLGATCMFVASKMKETIPLTAEKLCIYTDNSIRPEELLQMELLLVNKLKWNLAAMTPHDFIEHFLSKMPEAEENKQIIRKHAQTFVALCATDVKFISNPPSMVAAGSVVAAVQGLNLRSPNNFLSYYRLTRFLSRVIKCDPDCLRACQEQIEALLESSLRQAQQNMDPKAAEEEEEEEEEVDLACTPTDVRDVDI | Function: Regulatory component of the cyclin D1-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition . Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex an... |
P25322 | MEHQLLCCEVETIRRAYPDTNLLNDRVLRAMLKTEETCAPSVSYFKCVQKEIVPSMRKIVATWMLEVCEEQKCEEEVFPLAMNYLDRFLSLEPLKKSRLQLLGATCMFVASKMKETIPLTAEKLCIYTDNSIRPEELLQMELLLVNKLKWNLAAMTPHDFIEHFLSKMPEADENKQTIRKHAQTFVALCATDVKFISNPPSMVAAGSVVAAMQGLNLGSPNNFLSCYRTTHFLSRVIKCDPDCLRACQEQIEALLESSLRQAQQNVDPKATEEEGEVEEEAGLACTPTDVRDVDI | Function: Regulatory component of the cyclin D1-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and... |
Q6CW24 | MSTTFGNVFRRVNVKTLSFIVGAGALAGSATGTVMEYQDMRNYNNRNYNKQKLAALAAAHVAAKEKYDVAKYQKVYNDIALKIRDEDEYDDFIGYGPVLVRLAWHCAGTWDAKDNTGGPYGGTYRFAMETNDPSNNGLQNAAKFLEPIHEKYPWLSHGDLYSLAGVTAIQEMQGPTIPWRSGRVDQPEDTTPENGRLPDASKDAKYVRCFFHRLNFEDRQVVALLGAHALGKTHLKNSGFEGPWGAATNIFTNEFYNNLLNEKWDLITNDAGNKQYVNDKGWMMLPTDMALVQDPKYLPIVKEFANDQDTFFKEFTKAFV... | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 Fe(II)-[cytochrome c] + 2 H(+) + H2O2 = 2 Fe(III)-[cytochrome c] + 2 H2O
Sequence Mass (Da): 39041
Sequence L... |
Q7SDV9 | MAASRTATRTLRALRTSTRPALTAAPRAAFRQGGRRLYSSEPAKSGGSNIWAWAIGAGALGAGGLWYLNQDGASATPKVFAPKFDDYQAVYNEIASRLEEKDDYDDGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRFAPESDHGANAGLKAARDFLEPVKAKFPWITYSDLWILGGVCAIQEMLGPQIPYRPGRQDRDAAGCTPDGRLPDASQAQDHLRNIFYRMGFNDQEIVALSGAHALGRCHADRSGFDGPWTFSPTVLTNDYYKLLLDEKWQWKKWNGPKQYEDKKTKSLMMLPADMALIQDKKFKQWVEKYA... | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 Fe(II)-[cytochrome c] + 2 H(+) + H2O2 = 2 Fe(III)-[cytochrome c] + 2 H2O
Sequence Mass (Da): 39818
Sequence L... |
P55929 | MIKRTLTVSLLSLSLGAMFASAGVMAANEPIQPIKAVTPENADMAELGKMLFFDPRLSKSGFISCNSCHNLSMGGTDNITTSIGHKWQQGPINAPTVLNSSMNLAQFWDGRAKDLKEQAAGPIANPKEMASTHEIAEKVVASMPQYRERFKKVFGSDEVTIDRITTAIAQFEETLVTPGSKFDKWLEGDKNALNQDELEGYNLFKGSGCVQCHNGPAVGGSSYQKMGVFKPYETKNPAAGRMDVTGNEADRNVFKVPTLRNIELTYPYFHDGGAATLEQAVETMGRIQLNREFNKDEVSKIVAFLKTLTGDQPDFKLPIL... | PTM: Binds 2 heme c groups covalently per subunit.
Catalytic Activity: 2 Fe(II)-[cytochrome c] + 2 H(+) + H2O2 = 2 Fe(III)-[cytochrome c] + 2 H2O
Sequence Mass (Da): 36633
Sequence Length: 334
Subcellular Location: Periplasm
EC: 1.11.1.5
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P14532 | MQSSQLLPLGSLLLSFATPLAQADALHDQASALFKPIPEQVTELRGQPISEQQRELGKKLFFDPRLSRSHVLSCNTCHNVGTGGADNVPTSVGHGWQKGPRNSPTVFNAVFNAAQFWDGRAKDLGEQAKGPIQNSVEMHSTPQLVEQTLGSIPEYVDAFRKAFPKAGKPVSFDNMALAIEAYEATLVTPDSPFDLYLKGDDKALDAQQKKGLKAFMDSGCSACHNGINLGGQAYFPFGLVKKPDASVLPSGDKGRFAVTKTQSDEYVFRAAPLRNVALTAPYFHSGQVWELKDAVAIMGNAQLGKQLAPDDVENIVAFLH... | Cofactor: Binds 2 heme c groups covalently. Heme 1 is low-potential (-330 mV) with 2 His axial ligands and functions in the peroxidase reaction, while heme 2 is high potential (+320 mV) with His and Met axial ligands and functions to feed electrons from electron-shuttle proteins such as cytochrome c and azurin.
Functio... |
Q4PBY6 | MASLRTGLRVAQPLRASARNFATRPSIRSSVRHYSSPAPGSPPPPQPSSSSSTSKVLLTSVAIAAAAGGAFLAFGRDDKVSILGVGANGANKFQGSKGSVGPATTSAHSKADYQAVYNAIAEQLEANPDYDDGSYGPVLVRLAWHASGTYDKNSNTGGSNGATMRFAPESEHGANAGLGAARDFMEKIHQKFPWITYSDLWTLGGVAAIQELGGPKIPWRPGRKDATADKCTPDGRLPDGDKGPDHLRYIFYKMGFNDQEIVALSGAHALGRCHTDRSGFDGPWTFAPTSFTNEYFNLLMNEKWNIRKWNGPPQFEDKST... | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 Fe(II)-[cytochrome c] + 2 H(+) + H2O2 = 2 Fe(III)-[cytochrome c] + 2 H2O
Sequence Mass (Da): 43162
Sequence L... |
Q6C0Z6 | MRSFRAVRNFSTTAKRLSQAPKASTPNASSGNGFVLAFVAAAAGAGAYYYYANSPAAKVETFNATKADYQKVYDAIADKLIEDDDYDDGSYGPVLLRLAWHSSGTYNKSDNKFGSSGGTMRFKPEASHAANNGLVNARNFLKPIHEKFPWISTGDLYTLGGVTAVQELGGPIIPWKRGRVDEPESASPPDGSLPDASQGATHVRNVFNRQGFNDQEMVALIGAHALGRCHKQNSGFEGPWTFSPTMFTNDFYKLLLDDKWQWKKWDGNPQYEDVKTKSLMMLPTDMALATDKNFKKWATAYAKDQDLFFKDFSAAFSKML... | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 Fe(II)-[cytochrome c] + 2 H(+) + H2O2 = 2 Fe(III)-[cytochrome c] + 2 H2O
Sequence Mass (Da): 37646
Sequence L... |
P00431 | MTTAVRLLPSLGRTAHKRSLYLFSAAAAAAAAATFAYSQSQKRSSSSPGGGSNHGWNNWGKAAALASTTPLVHVASVEKGRSYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHTSGTWDKHDNTGGSYGGTYRFKKEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTPEDTTPDNGRLPDADKDADYVRTFFQRLNMNDREVVALMGAHALGKTHLKNSGYEGPWGAANNVFTNEFYLNLLNEDWKLEKNDANNEQWDSKSGYMMLPTDYSLIQDPKYLSIVKEYAN... | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 Fe(II)-[cytochrome c] + 2 H(+) + H2O2 = 2 Fe(III)-[cytochrome c] + 2 H2O
Sequence Mass (Da): 40353
Sequence L... |
P46092 | MGTEATEQVSWGHYSGDEEDAYSAEPLPELCYKADVQAFSRAFQPSVSLTVAALGLAGNGLVLATHLAARRAARSPTSAHLLQLALADLLLALTLPFAAAGALQGWSLGSATCRTISGLYSASFHAGFLFLACISADRYVAIARALPAGPRPSTPGRAHLVSVIVWLLSLLLALPALLFSQDGQREGQRRCRLIFPEGLTQTVKGASAVAQVALGFALPLGVMVACYALLGRTLLAARGPERRRALRVVVALVAAFVVLQLPYSLALLLDTADLLAARERSCPASKRKDVALLVTSGLALARCGLNPVLYAFLGLRFRQD... | Function: Receptor for chemokines SCYA27 and SCYA28. Subsequently transduces a signal by increasing the intracellular calcium ions level and stimulates chemotaxis in a pre-B cell line.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38416
Sequence Length: 362
Subcellular Location: Cell membrane
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Q9JL21 | MGTKPTEQVSWGLYSGYDEEAYSVGPLPELCYKADVQAFSRAFQPSVSLMVAVLGLAGNGLVLATHLAARRTTRSPTSVHLLQLALADLLLALTLPFAAAGALQGWNLGSTTCRAISGLYSASFHAGFLFLACISADRYVAIARALPAGQRPSTPSRAHLVSVFVWLLSLFLALPALLFSRDGPREGQRRCRLIFPESLTQTVKGASAVAQVVLGFALPLGVMAACYALLGRTLLAARGPERRRALRVVVALVVAFVVLQLPYSLALLLDTADLLAARERSCSSSKRKDLALLVTGGLTLVRCSLNPVLYAFLGLRFRRD... | Function: Receptor for chemokines SCYA27 and SCYA28. Subsequently transduces a signal by increasing the intracellular calcium ions level.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38900
Sequence Length: 362
Subcellular Location: Cell membrane
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P32246 | METPNTTEDYDTTTEFDYGDATPCQKVNERAFGAQLLPPLYSLVFVIGLVGNILVVLVLVQYKRLKNMTSIYLLNLAISDLLFLFTLPFWIDYKLKDDWVFGDAMCKILSGFYYTGLYSEIFFIILLTIDRYLAIVHAVFALRARTVTFGVITSIIIWALAILASMPGLYFSKTQWEFTHHTCSLHFPHESLREWKLFQALKLNLFGLVLPLLVMIICYTGIIKILLRRPNEKKSKAVRLIFVIMIIFFLFWTPYNLTILISVFQDFLFTHECEQSRHLDLAVQVTEVIAYTHCCVNPVIYAFVGERFRKYLRQLFHRRV... | Function: Receptor for a C-C type chemokine. Binds to MIP-1-alpha, MIP-1-delta, RANTES, and MCP-3 and, less efficiently, to MIP-1-beta or MCP-1 and subsequently transduces a signal by increasing the intracellular calcium ions level. Responsible for affecting stem cell proliferation.
Location Topology: Multi-pass membra... |
P0C8M8 | MDPKATSTSKTDNIDQITIIEEKVNKIGTEPTIRKYSKGRMLGKGGFAKCYEVTNLENKKVLAGKIICKASLTKSRAKQKLISEIKIHKSLRHSNIVEFEHVFEDQENVYILLELCPNQSLHDLIKRRKRLTEIEVQCYTLQLICGLKYLHSRRVIHRDLKLGNLLLNDKMELKICDFGLAAKLEFDGEKRKTVCGTPNYIAPEVIEGKGGHSYEVDTWSLGVIIYTLLVGRPPFETSDVKQTYKRIKACEYSFPDHVSVSDTAKNLVQKMLTLDPSKRPSLDEILQHPFLKNANNIPKFLPASTLACPPSTSYLNQFAS... | Function: May play a role in the division of some cell types.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 70234
Sequence Length: 626
EC: 2.7.11.21
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A0A072VDF2 | MPAATAAAAAESSSVSGETICVTGAGGFIASWMVKLLLEKGYTVRGTLRNPDDPKNGHLKKLEGAKERLTLVKVDLLDLNSVKEAVNGCHGVFHTASPVTDNPEEMVEPAVNGAKNVIIAGAEAKVRRVVFTSSIGAVYMDPNRSVDVEVDESCWSDLEFCKKTKNWYCYGKAVAEAAAWDVAKEKGVDLVVVNPVLVLGPLLQPTINASTIHILKYLTGSAKTYANATQAYVHVRDVALAHILVYEKPSASGRYLCAETSLHRGELVEILAKYFPEYPIPTKCSDEKNPRVKPHIFSNKKLKDLGLEFTPVSECLYETV... | Function: Involved in the latter stages of lignin biosynthesis . Catalyzes one of the last steps of monolignol biosynthesis, the conversion of cinnamoyl-CoAs into their corresponding cinnamaldehydes . Mediates the conversion of feruloyl-CoA to coniferylaldehyde . Also active, with a lower efficiency, toward coumaroyl-C... |
Q6K9A2 | MSSNFEANNNNNGEKQLVCVTGAGGFIGSWVVKELLIRGYHVRGTARDPADSKNAHLLELEGADERLSLCRADVLDAASLRAAFSGCHGVFHVASPVSNDPDLVPVAVEGTRNVINAAADMGVRRVVFTSSYGAVHMNPNRSPDAVLDETCWSDYEFCKQTDNLYCCAKMMAEMTATEEAAKRGLELAVVVPSMTMGPMLQQTLNFSTNHVARYLMGTKKSYPNAVAAYVDVRDVARAHVLVYERPEARGRYLCIGTVLHRAELLRMLRELFPRYPATAKCEDDGKPMAKPYKFSNQRLKDLGLEFTPLRKSLNEAVLCM... | Function: Involved in the latter stages of lignin biosynthesis. Catalyzes one of the last steps of monolignol biosynthesis, the conversion of cinnamoyl-CoAs into their corresponding cinnamaldehydes. Probably involved in the formation of lignin in defense responses.
Catalytic Activity: (E)-cinnamaldehyde + CoA + NADP(+)... |
A9L9E6 | MIFVTLEHILTHISFSIISVVIIIQLMTFFVHEIPALSDSLEKGMIATFLSITGLLIIRWIYSGHFPLSNLYESLMFLSWSFAIIHMIPKIWNHKNKNYLSAITIPSAIFTQAFATSGLSTEMHESGILVPALRSHWLMMHVSMMLLSYAALLVGSLFSIALLVITFRKNGKLVVENQNLLIGSSFFDQMDYLNFNENINVLENPSFSSSFKNYYKYQLVERLDYWSSRVISIGFSFLTIGILSGAVWANEAWGSYWNWDPKETWAFITWTIYAIYSHTRTTKNGQGANSAIVASIGFFIIWICYFGVNLLGIGLHSYGS... | Function: Required during biogenesis of c-type cytochromes (cytochrome c6 and cytochrome f) at the step of heme attachment.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36819
Sequence Length: 324
Subcellular Location: Plastid
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Q0G9H0 | MIFATLEHILTHISFSIISIVITIHLVTLLVHEIVGLCDPSEKGMIAAFFCITGLLVTRWIYSRHFPLSDLYESLMFLSWSFSIIHMVPKIWNHKNDLSAITAPSAIFTQGFATSGLSTEMHQSAILVPALQSQWLMMHVSMMLLSYAALLCGSLLSVALLVITFRKNIGIVGKSNHLLIGSFSFDEIHYLNEKRNVLQNTSFLSFRNYHRYQLTQRLDYWSYRVISLGFTFLTIGILSGAVWANEAWGSYWNWDPKETWAFITWTIFAIYLHTRTNRSLQGVNSAIVASMGFLIIWICYFGVNLLGIGLHSYGSFTLTS... | Function: Required during biogenesis of c-type cytochromes (cytochrome c6 and cytochrome f) at the step of heme attachment.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36455
Sequence Length: 321
Subcellular Location: Plastid
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P12214 | MPFITLERILAHTSFFLLFFVTFIYWGKFLYINIKPITILGEISMKIACFFITTFLLIRWSSSGHFPLSNLYESSMFLSWSFTLIHLILENKSKNTWLGIITAPSAMLTHGFATLSLPKEMQESVFLVPALQSHWLMMHVTMMMLSYSTLLCGSLLAITILIITLTKQKNLPILTSYFNFPFNSFIFKNLLQPMENEILSYKTQKVFSFINFRKWQLIKELDNWSYRVISLGFPLLTIGILSGAVWANEAWGSYWNWDPKETWALITWLIFAIYLHTRMIKGWQGKKPAIIASLGFFIVWICYLGVNLLGKGLHSYGWLI | Function: Required during biogenesis of c-type cytochromes (cytochrome c6 and cytochrome f) at the step of heme attachment.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37170
Sequence Length: 320
Subcellular Location: Plastid
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Q9MUM3 | MNLIEIETYLANASFALLLITMLIYGMKAIFTKNNILQLFGTLGILFSNFLVALLLSIRWFDSHHFPLSNMYESLMFLCWCFTFFHLLIEKYIQINFIGFITVPIAMLVNAFATFFLPLDMQHSTPLVPALKSNWLIMHVTIMMASYAALILGSLLSIAFLFLTYNKQIELQGNSIGNINDEMNSYITIDIEFQKNESIELAKLIDNLSYRTIGIGFPLLTIGIISGAVWANDAWGSYWSWDPKETWALITWIIFAIYLHTRITKGWQGRRPAIVAFIGFVIVWVCYLGVNLLGQGLHSYGWFTK | Function: Required during biogenesis of c-type cytochromes (cytochrome c6 and cytochrome f) at the step of heme attachment.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34891
Sequence Length: 305
Subcellular Location: Plastid
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Q8CII2 | MKKEHVSHCQFSAWYPLFRSLTIKSVILPLPQNVKDYLLDDGTLVVSGREDPPTCSQSDSGNEAEETQWSDDESTATLTAPEFPEFNTQVQEAINSLGGSVFPKLNWSAPRDAYWIAMNSSLKCKTLSDIFLLFKSSDFITHDFTQPFIHCTDDSPDPCIEYELVLRKWCELIPGAEFRCFVKENKLIGISQRDYTQYYDHISKQKEEICRCIQDFFKEHLQYKFLDEDFVFDIYRDSRGKVWLIDFNPFGEVTDSLLFTWEELTSENNLRGEVTEGDAQEQDSPAFRCTNSEVTVQPSPYLSFGLPKDFVDLSTGEDAH... | Function: Required for S phase entry of the cell cycle.
PTM: Phosphorylated.
Sequence Mass (Da): 38816
Sequence Length: 336
Subcellular Location: Cytoplasm
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Q62834 | MKKEHVSHCQFSAWYPLFRSLTIKSVILPLPQNVKDYLLDDGTLVVSGREDPPTCSQPDSGDEAEETQWSDDESTATLTAPEFPEFNTQVQEAINSLGGSVFPKLNWSAPRDAYWIAMNSSLKCKSLSDIFLLFKSSDFITHDFTQPFIHCNDDSPDPCIEYELVLRKWCELIPGAEFRCFVKENKLIGISQRDYTQYYDHISKQKEEICRCIQDFFKEHLQYKFLDEDFVFDIYRDSRGKVWLIDFNPFGEVTDSLLFTWEELTSENNLRGDVSEADALEQDSPAFRCTNSEVTVQPSPYLSYGLPKDFVDLSTGEDAH... | Function: Required for S phase entry of the cell cycle.
PTM: Phosphorylated.
Sequence Mass (Da): 38812
Sequence Length: 336
Subcellular Location: Cytoplasm
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Q95122 | MVCVPYLLLLLLPSLLRVSADTTEPCELDDDDFRCVCNFTDPKPDWSSAVQCMVAVEVEISAGGRSLEQFLKGADTNPKQYADTIKALRVRRLKLGAAQVPAQLLVAVLRALGYSRLKELTLEDLEVTGPTPPTPLEAAGPALTTLSLRNVSWTTGGAWLGELQQWLKPGLRVLNIAQAHSLAFPCAGLSTFEALTTLDLSDNPSLGDSGLMAALCPNKFPALQYLALRNAGMETPSGVCAALAAARVQPQSLDLSHNSLRVTAPGATRCVWPSALRSLNLSFAGLEQVPKGLPPKLSVLDLSCNKLSREPRRDELPEVN... | Function: Coreceptor for bacterial lipopolysaccharide. In concert with LBP, binds to monomeric lipopolysaccharide and delivers it to the LY96/TLR4 complex, thereby mediating the innate immune response to bacterial lipopolysaccharide (LPS). Acts via MyD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine secr... |
P08571 | MERASCLLLLLLPLVHVSATTPEPCELDDEDFRCVCNFSEPQPDWSEAFQCVSAVEVEIHAGGLNLEPFLKRVDADADPRQYADTVKALRVRRLTVGAAQVPAQLLVGALRVLAYSRLKELTLEDLKITGTMPPLPLEATGLALSSLRLRNVSWATGRSWLAELQQWLKPGLKVLSIAQAHSPAFSCEQVRAFPALTSLDLSDNPGLGERGLMAALCPHKFPAIQNLALRNTGMETPTGVCAALAAAGVQPHSLDLSHNSLRATVNPSAPRCMWSSALNSLNLSFAGLEQVPKGLPAKLRVLDLSCNRLNRAPQPDELPE... | Function: Coreceptor for bacterial lipopolysaccharide . In concert with LBP, binds to monomeric lipopolysaccharide and delivers it to the LY96/TLR4 complex, thereby mediating the innate immune response to bacterial lipopolysaccharide (LPS) . Acts via MyD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine se... |
P10810 | MERVLGLLLLLLVHASPAPPEPCELDEESCSCNFSDPKPDWSSAFNCLGAADVELYGGGRSLEYLLKRVDTEADLGQFTDIIKSLSLKRLTVRAARIPSRILFGALRVLGISGLQELTLENLEVTGTAPPPLLEATGPDLNILNLRNVSWATRDAWLAELQQWLKPGLKVLSIAQAHSLNFSCEQVRVFPALSTLDLSDNPELGERGLISALCPLKFPTLQVLALRNAGMETPSGVCSALAAARVQLQGLDLSHNSLRDAAGAPSCDWPSQLNSLNLSFTGLKQVPKGLPAKLSVLDLSYNRLDRNPSPDELPQVGNLSL... | Function: Coreceptor for bacterial lipopolysaccharide. In concert with LBP, binds to monomeric lipopolysaccharide and delivers it to the LY96/TLR4 complex, thereby mediating the innate immune response to bacterial lipopolysaccharide (LPS) . Acts via MyD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine sec... |
P29329 | MKWTALVIVAVLQTQFPVTAAQSFGLLDPKLCYLLDGILFIYGVIVTALFLRAKFSRSADAPAYQHGQNPVYNELNVGRREEYAVLDRRGGFDPEMGGKPQRKKNPHEVVYNELRKDKMAEAYSEIGMKSDNQRRRGKGHDGVYQGLSTATKDTYDALHMQALPPR | Function: Part of the TCR-CD3 complex present on T-lymphocyte cell surface that plays an essential role in adaptive immune response. When antigen presenting cells (APCs) activate T-cell receptor (TCR), TCR-mediated signals are transmitted across the cell membrane by the CD3 chains CD3D, CD3E, CD3G and CD3Z. All CD3 cha... |
Q9I8D8 | MNEAYSPAAPRPMGSTSPSTMKMFMCFLSVFMVVQTIGTVLFCLYLHMKMDKMEEVLSLNEDYIFLRKVQKCQTGEDQKSTLLDCEKVLKGFQDLQCKDRTASEELPKFEMHRGHEHPHLKSRNETSVAEEKRQPIATHLAGVKSNTTVRVLKWMTTSYAPTSSLISYHEGKLKVEKAGLYYIYSQVSFCTKAAASAPFTLYIYLYLPMEEDRLLMKGLDTHSTSTALCELQSIREGGVFELRQGDMVFVNVTDSTAVNVNPGNTYFGMFKL | Function: Cytokine that acts as a ligand to CD40/TNFRSF5 (By similarity). Costimulates T-cell proliferation and cytokine production (By similarity). Induces the activation of NF-kappa-B (By similarity). Mediates B-cell proliferation in the absence of co-stimulus as well as IgE production in the presence of IL4 (By simi... |
P29965 | MIETYNQTSPRSAATGLPISMKIFMYLLTVFLITQMIGSALFAVYLHRRLDKIEDERNLHEDFVFMKTIQRCNTGERSLSLLNCEEIKSQFEGFVKDIMLNKEETKKENSFEMQKGDQNPQIAAHVISEASSKTTSVLQWAEKGYYTMSNNLVTLENGKQLTVKRQGLYYIYAQVTFCSNREASSQAPFIASLCLKSPGRFERILLRAANTHSSAKPCGQQSIHLGGVFELQPGASVFVNVTDPSQVSHGTGFTSFGLLKL | Function: Cytokine that acts as a ligand to CD40/TNFRSF5 . Costimulates T-cell proliferation and cytokine production . Its cross-linking on T-cells generates a costimulatory signal which enhances the production of IL4 and IL10 in conjunction with the TCR/CD3 ligation and CD28 costimulation . Induces the activation of N... |
Q58DM3 | MGMSSLKLLKFVLFFFNLIFWFCGCCILGLGIYLLIHSKFGVLFHNLPSLTLGNVLVIVGSVIMVVAFLGCMGSIKENKCLLMSFFVLLLIILLAEVTLAILLFVYEQKLKEYVAEGLTESIQRYNSDNSTKAAWDSIQSFLQCCGVNGTSDWTSGPPASCPKGSAVKGCYIQAKQWFHSNFLYIGITTICVCVIQVLGMSFALTLNCQIDKTSQVLGL | Function: Required for efficient formation of myofibers in regenerating muscle at the level of cell fusion. May be involved in growth regulation in hematopoietic cells (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24103
Sequence Length: 219
Subcellular Location: Cell membrane
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P19397 | MGMSSLKLLKYVLFFFNLLFWICGCCILGFGIYLLIHNNFGVLFHNLPSLTLGNVFVIVGSIIMVVAFLGCMGSIKENKCLLMSFFILLLIILLAEVTLAILLFVYEQKLNEYVAKGLTDSIHRYHSDNSTKAAWDSIQSFLQCCGINGTSDWTSGPPASCPSDRKVEGCYAKARLWFHSNFLYIGIITICVCVIEVLGMSFALTLNCQIDKTSQTIGL | Function: Required for efficient formation of myofibers in regenerating muscle at the level of cell fusion. May be involved in growth regulation in hematopoietic cells (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24341
Sequence Length: 219
Subcellular Location: Cell membrane
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O55186 | MRAQRGLILLLLLLAVFCSTAVSLTCYHCFQPVVSSCNMNSTCSPDQDSCLYAVAGMQVYQRCWKQSDCHGEIIMDQLEETKLKFRCCQFNLCNKSDGSLGKTPLLGTSVLVAILNLCFLSHL | Function: Potent inhibitor of the complement membrane attack complex (MAC) action. Acts by binding to the C8 and/or C9 complements of the assembling MAC, thereby preventing incorporation of the multiple copies of C9 required for complete formation of the osmolytic pore (By similarity).
Location Topology: Lipid-anchor
S... |
P13987 | MGIQGGSVLFGLLLVLAVFCHSGHSLQCYNCPNPTADCKTAVNCSSDFDACLITKAGLQVYNKCWKFEHCNFNDVTTRLRENELTYYCCKKDLCNFNEQLENGGTSLSEKTVLLLVTPFLAAAWSLHP | Function: Potent inhibitor of the complement membrane attack complex (MAC) action. Acts by binding to the C8 and/or C9 complements of the assembling MAC, thereby preventing incorporation of the multiple copies of C9 required for complete formation of the osmolytic pore. This inhibitor appears to be species-specific. In... |
Q8SQ46 | MGIQGGSVLFGLLLVLAVFCHSGHSLQCYNCPNPTTDCKTAINCSSGFDTCLIARAGLQVYNQCWKFANCNYNDISTLLKESELRYFCCKKDLCNFNEQLESGGTSLSEKTVVLLVTPLLAAAWCLHP | Function: Potent inhibitor of the complement membrane attack complex (MAC) action. Acts by binding to the C8 and/or C9 complements of the assembling MAC, thereby preventing incorporation of the multiple copies of C9 required for complete formation of the osmolytic pore (By similarity).
PTM: N- and O-glycosylated.
Locat... |
O62680 | MGSKGGFILLWLLSILAVLCHLGHSLQCYNCINPAGSCTTAMNCSHNQDACIFVEAVPPKTYYQCWRFDECNFDFISRNLAEKKLKYNCCRKDLCNKSDATISSGKTALLVILLLVATWHFCL | Function: Potent inhibitor of the complement membrane attack complex (MAC) action. Acts by binding to the C8 and/or C9 complements of the assembling MAC, thereby preventing incorporation of the multiple copies of C9 required for complete formation of the osmolytic pore.
Location Topology: Lipid-anchor
Sequence Mass (Da... |
O77541 | MTSRGVHLLLRLLFLLAVFYSSDSSLMCYHCLLPSPNCSTVTNCTPNHDACLTAVSGPRVYRQCWRYEDCNFEFISNRLEENSLKYNCCRKDLCNGPEDDGTALTGRTVLLVAPLLAAARNLCL | Function: Potent inhibitor of the complement membrane attack complex (MAC) action. Acts by binding to the C8 and/or C9 complements of the assembling MAC, thereby preventing incorporation of the multiple copies of C9 required for complete formation of the osmolytic pore.
Location Topology: Lipid-anchor
Sequence Mass (Da... |
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