ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q3SZB8 | MARTKRTAYKSTGGKVPRKQLVIEAAGKSAPSTSGMTKPHRYRPGTVALREIRPYQKSTHFLIRKLPFQRLVREIAQDFKTDLKFQSAAIRTLQEASEAYLVVFLESKQHSNLARMYSQNKSFPWLEGKRRQPQPM | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
Q6NXT2 | MARTKQTARKSTGGKAPRKQLATKAARKSTPSTCGVKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFNTDLRFQSAAVGALQEASEAYLVGLLEDTNLCAIHAKRVTIMPKDIQLARRIRGERA | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
P02301 | MALTKQTARKSTGGKAPRKQLATKATRKSAPSTGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSAAIGALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
P02302 | MARTKQTARKSTGGKAPRKQLVTKAAKKCAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQRSAVMALQEASEAYLVALFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
A0A3G9K5C8 | MASFENSLSVLIVGAGLGGLAAAIALRRQGHVVKIYDSSSFKAELGAGLAVPPNTLRSLQQLGCNTENLNGVDNLCFTAMGYDGSVGMMNNMTDYREAYGTSWIMVHRVDLHNELMRVALDPGGLGPPATLHLNHRVTFCDVDACTVTFTNGTTQSADLIVGADGIRSTIRRFVLEEDVTVPASGIVGFRWLVQADALDPYPELDWIVKKPPLGARLISTPQNPQSGVGLADRRTIIIYACRGGTMVNVLAVHDDERDQNTADWSVPASKDDLFRVFHDYHPRFRRLLELAQDINLWQMRVVPVLKKWVNKRVCLLGDAA... | Function: Hispidin-3-hydroxylase; part of the gene cluster that mediates the fungal bioluminescence cycle . Hydroxylates hispidin in order to produce the fungal luciferin 3-hydroxyhispidin . The fungal bioluminescence cycle begins with the hispidin synthetase that catalyzes the formation of hispidin which is further hy... |
P08898 | MARTKQTARKSTGGKAPRKQLATKAARKSAPASGGVKKPHRYRPGTVALREIRRYQKSTELLIRRAPFQRLVREIAQDFKTDLRFQSSAVMALQEACEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
Q6DL03 | MARTKQTARKSTGGKAPRKQLASKAARKSAPSTGGVKKPHRYKPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKSDLRFQSSAIGALQESVESYLVSLFEDTNLCAIHAKRVTIQSKDIQLARRLRGERN | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
P0CO05 | MARTKQTARKSTGGKAPRKQLATKAARKQAPSQVSGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAIGALQEASEAYLVSLFEDTNLAAIHAKRVTIQPKDLQLARRLRGERS | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
P69071 | MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTELRFQSSAVMALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
P09322 | MSGRGKGGKGLGKGGAKRHRKILRDNIQGITKPAIRRLARRGGVKRISALVYEETRAVLKLFLENVIRDAVTYTEHAKRKTVTSLDVVYSLKRQGRTIYGFGG | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
P69152 | MAGGKGGKGMGKVGAKRHSRKSNKASIEGITKPAIRRLARRGGVKRISSFIYDDSRQVLKSFLENVVRDAVTYTEHARRKTVTAMDVVYALKRQGRTLYGFGG | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
P01899 | MGAMAPRTLLLLLAAALAPTQTRAGPHSMRYFETAVSRPGLEEPRYISVGYVDNKEFVRFDSDAENPRYEPRAPWMEQEGPEYWERETQKAKGQEQWFRVSLRNLLGYYNQSAGGSHTLQQMSGCDLGSDWRLLRGYLQFAYEGRDYIALNEDLKTWTAADMAAQITRRKWEQSGAAEHYKAYLEGECVEWLHRYLKNGNATLLRTDSPKAHVTHHPRSKGEVTLRCWALGFYPADITLTWQLNGEELTQDMELVETRPAGDGTFQKWASVVVPLGKEQNYTCRVYHEGLPEPLTLRWEPPPSTDSYMVIVAVLGVLGAM... | Function: Involved in the presentation of foreign antigens to the immune system.
PTM: Polyubiquitinated in case of infection by murid herpesvirus 4, by the viral E3 ligase K3 (mK3). This modification causes the protein to be targeted for rapid degradation by the endoplasmic reticulum-associated degradation (ERAD) syste... |
P14426 | MGAMVPRTLLLLLAAALAPAQTRAGPHSLRYFETVVSRPGLGEPRFISVGYVDNTEFVRFDSDAENPRDEPRVRWMEQEGPEYWERETQIAKGNEQSFRVDLRTLLRYYNQSEGGSHTIQRLSGCDVGSDWRLLRGYEQFAYDGCDYIALNEDLKTWTAADMAALITKHKWEQAGAAERDRAYLEGTCVEWLRRYLELGNATLLHTDSPKAHVTHHPRSKVEVTLRCWALGFYPADITLTWQLNGEELTQDMELVETRPAGDGTFQKWASVVVPLGKEQNYTCHVYHEGLPEPLTLRWEPPPSTDSYMVIVAVLGVLGAV... | Function: Involved in the presentation of foreign antigens to the immune system.
PTM: Polyubiquitinated in case of infection by murid herpesvirus 4, by the viral E3 ligase K3 (mK3), leading to target the protein for rapid degradation by the endoplasmic reticulum-associated degradation (ERAD) system. Ubiquitination take... |
P13753 | MRVMRVMRPRTLLLLLSGVLVLTETLAGSHSLRYFYTGVSRPGLGEPRFIAVGYVDDTQFVRFDSDAPNPREEPRVPWMEQEGPEYWDRNTRIYKDTAQIFRVDLNTLRGYYNQSETGSHNIQAMYGCDVGPDGRLLRGFWQFGYDGRDYIALNEELRSWTAADTAAQITKRKWEAAGAAETWRNYLEGECVEWLRRYLENGKDTLLRADPPKAHVTHHSISDREVTLRCWALGFYPEEISLTWQREGEDQTQDMELVETRPSGDGTFQKWAALVVPSGEEQRYTCRVQHEGLQEPLTLRWEPPQTSFLIMGIIVGLVLL... | Function: Involved in the presentation of foreign antigens to the immune system.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 41513
Sequence Length: 364
Subcellular Location: Membrane
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P01901 | MVPCTLLLLLAAALAPTQTRAGPHSLRYFVTAVSRPGLGEPRYMEVGYVDDTEFVRFDSDAENPRYEPRARWMEQEGPEYWERETQKAKGNEQSFRVDLRTLLGYYNQSKGGSHTIQVISGCEVGSDGRLLRGYQQYAYDGCDYIALNEDLKTWTAADMAALITKHKWEQAGEAERLRAYLEGTCVEWLRRYLKNGNATLLRTDSPKAHVTHHSRPEDKVTLRCWALGFYPADITLTWQLNGEELIQDMELVETRPAGDGTFQKWASVVVPLGKEQYYTCHVYHQGLPEPLTLRWEPPPSTVSNMATVAVLVVLGAAIVT... | Function: Involved in the presentation of foreign antigens to the immune system.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 41302
Sequence Length: 369
Subcellular Location: Membrane
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O14346 | MSKILKIQYLKLYNVISCFLWMSVLLRTGLIWGITKDTAVVFHETNTLVRWVQTLAIAEVFHSIFGLVSSSPLTTIIQVASRLYLVWGVCYPFSYVIEGSPIYLSMIIAWSITEIIRYAFYAFNLNGDIPAFLTWLRYNTFLILYPIGAGSEFLLVLKSRIAAQYVWSLNKLLWPILMSIYPPGLYIMYTHMLAQRRKISKRAAARRT | Function: Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-Co... |
P40857 | MSKKLASPLSFLPLYNLLSAVGWSYLLYLVISLYPKVGQPAFFYQTKNVATLVQCGAIIEIINSFLGVVRSPLLTTVAQVSSRLLVVLGIFQLLPNTSGVQSVVYISLLLAWSITEIVRYLYYFFMLVFKNGAPKILILLRYNLFWILYPTGVASELRIIYCALNAAESQYSLLYKRILIAAMLAYIPGFPMLFLHMVAQRKKVMKSLRSSFGKKLI | Function: Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-Co... |
Q8IYU2 | MERAMEQLNRLTRSLRRARTVELPEDNETAVYTLMPMVMADQHRSVSELLSNSKFDVNYAFGRVKRSLLHIAANCGSVECLVLLLKKGANPNYQDISGCTPLHLAARNGQKKCMSKLLEYSADVNICNNEGLTAIHWLAVNGRTELLHDLVQHVSDVDVEDAMGQTALHVACQNGHKTTVQCLLDSGADINRPNVSGATPLYFACSHGQRDTAQILLLRGAKYLPDKNGVTPLDLCVQGGYGETCEVLIQYHPRLFQTIIQMTQNEDLRENMLRQVLEHLSQQSESQYLKILTSLAEVATTNGHKLLSLSSNYDAQMKSL... | Function: E3 ubiquitin-protein ligase involved in Golgi membrane fusion and regulation of small GTPases. Acts as a regulator of Golgi membrane dynamics during the cell cycle: recruited to Golgi membrane by Rab proteins and regulates postmitotic Golgi membrane fusion. Acts by mediating ubiquitination during mitotic Golg... |
Q54DA9 | MDGVEIIAKSIKNSAIEKVFGIVGVPITPIAYELQAQGVGFFGFRNEQSCSYAASIVGYLTGLPGLCMTVSGPGVVHALAGVLNAQSNGWPMILLSSSIDQSLVGKGGFQECKQFESAELYCKKCYYLTEIDHFPEILKDAIETSLSNRPGPVYIQIPADLIKSKCKESPNIREAAGYGTIAIKSVVPDMKLIKDAVQLLSEAKRPLVIGGKGAAYCRSENELLEFIEATKIPFLPSPMGKGLLRDDHPLVVGAARSYALKNADVVLVLGARLNWMFNFGKAPTFSTDVKFIIVDVDENQASKTKNPNVVPEIAIVGDAR... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Peroxisomal 2-OH acyl-CoA lyase involved in the cleavage (C1 removal) reaction in the fatty acid alpha-oxydation in a thiamine pyrophosphate (TPP)-dependent manner. Involved in the degradation of 3-methyl-branched fatty acids and the shortening of 2-hydroxy long-chain... |
Q9UJ83 | MPDSNFAERSEEQVSGAKVIAQALKTQDVEYIFGIVGIPVTEIAIAAQQLGIKYIGMRNEQAACYAASAIGYLTSRPGVCLVVSGPGLIHALGGMANANMNCWPLLVIGGSSERNQETMGAFQEFPQVEACRLYTKFSARPSSIEAIPFVIEKAVRSSIYGRPGACYVDIPADFVNLQVNVNSIKYMERCMSPPISMAETSAVCTAASVIRNAKQPLLIIGKGAAYAHAEESIKKLVEQYKLPFLPTPMGKGVVPDNHPYCVGAARSRALQFADVIVLFGARLNWILHFGLPPRYQPDVKFIQVDICAEELGNNVKPAVT... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Peroxisomal 2-OH acyl-CoA lyase involved in the cleavage (C1 removal) reaction in the fatty acid alpha-oxydation in a thiamine pyrophosphate (TPP)-dependent manner . Involved in the degradation of 3-methyl-branched fatty acids like phytanic acid and the shortening of ... |
O61856 | MVLFLIIAAIIIGLLLWKWLDVRSTDELTSMVKLLGSGNGQHVLSNAFQVDEKSKRHGGELVASVLKAHDVEEIFVLCGGHISPILVAAEKLGIKIVDTRHEVTAVFAADAVARLRQSIGVAAVTAGPGLTNTITAVKNAQMAESPLLLIGGAAPTLLKGRGALQDIDQMVLFRPLCKYVARVERLRDIVPTVREAIKAAKSGCPGPVFVEFPVDVLYPYELVVKEIGFNPNAKGFIQRALNFYLRCHVSRQFGNAWAPQTITPLPTNIPMPKSEKIQEIVQLVKSAKRPVLLIGSQATLPPVKPADLVKAVEALGCPVF... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Endoplasmic reticulum 2-OH acyl-CoA lyase involved in the cleavage (C1 removal) reaction in the fatty acid alpha-oxydation in a thiamine pyrophosphate (TPP)-dependent manner.
Catalytic Activity: 2-hydroxyoctadecanoyl-CoA = formyl-CoA + heptadecanal
Location Topology: ... |
Q6NV04 | MDISMYLGCSLGAALGGVIFASYKLGLLYQLFHKTERQSPRHGGESVAEVLRSHGVKFVFTLVGGHISPILVACEKLGIRIVDTRHEATAVFAADAVARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAESPLLLIGGAAATLLQGRGALQDIDQMSLFKPLCKFCASVRTVREIVPTVRKALAIAQSGTPGPVFIEFPIDTLYPYHVVEKEFAPKNTPKGLMGKIIAWYLKNHLSNLFAGAWESRDLSPLPVHIPHATDDQVQRCVELVSRAKKPVILLGSQATLPPTPADDIRKALESLGIPCFLGGMSRGLLGKNSPL... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Endoplasmic reticulum 2-OH acyl-CoA lyase involved in the cleavage (C1 removal) reaction in the fatty acid alpha-oxydation in a thiamine pyrophosphate (TPP)-dependent manner.
Catalytic Activity: 2-hydroxyoctadecanoyl-CoA = formyl-CoA + heptadecanal
Location Topology: ... |
A1L0T0 | METPAAAAPAGSLFPSFLLLACGTLVAALLGAAHRLGLFYQLLHKVDKASVRHGGENVAAVLRAHGVRFIFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAMARLSGTVGVAAVTAGPGLTNTVTAVKNAQMAQSPILLLGGAASTLLQNRGALQAVDQLSLFRPLCKFCVSVRRVRDIVPTLRAAMAAAQSGTPGPVFVELPVDVLYPYFMVQKEMVPAKPPKGLVGRVVSWYLENYLANLFAGAWEPQPEGPLPLDIPQASPQQVQRCVEILSRAKRPLMVLGSQALLTPTSADKLRAAVETLGVPCFLGGM... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Endoplasmic reticulum 2-OH acyl-CoA lyase involved in the cleavage (C1 removal) reaction in the fatty acid alpha-oxydation in a thiamine pyrophosphate (TPP)-dependent manner. Involved in the phytosphingosine degradation pathway.
Catalytic Activity: 2-hydroxyoctadecano... |
Q8BU33 | METSAAAASAGGFFPSFLLLAFGTLVAAVLGVAHRLGLFYQLMHKVDKTSIRHGGESVAAVLRAHGVRFVFTLVGGHISPLLVACEKLGIRVVDTRHEVTAVFAADAVARLTGTVGVAAVTAGPGLTNTVTAVKNAQVAQSPVLLLGGAASTLLQKRGALQAIDQMSLFRPLCKFCASVRRVRDIVPTLRTAIAAAQSGTPGPVFVELPLDVLYPYFMVEKEMIPTKLPNSLMGRVVVWYLQNCLANLFVGAWEPRPEGPLPLDIPQASPQQVQRCVEILSRAKRPLLVLGSQALLPPTPANKLRAAVETLGVPCFLGGM... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Endoplasmic reticulum 2-OH acyl-CoA lyase involved in the cleavage (C1 removal) reaction in the fatty acid alpha-oxydation in a thiamine pyrophosphate (TPP)-dependent manner. Involved in the phytosphingosine degradation pathway.
Catalytic Activity: 2-hydroxyoctadecano... |
Q84YJ9 | MEYHHRPHSPPPSDDDVVVIQMNAAAIAAVDEWSSTNEVDDAAAGKGGGLTRRTFSQAYKMKHRTPLEFTWRQVALLSFQSLGVVYGDLGTSPLYVFSSISLDDPGEADFVGILSIILWTFTMICLVKYVFIVLKADDHGEGGTFALYSLLRQHVNFKGNMPVPVTHLASDINLKFHSKKRILTSKLLKFLEQSTKWQAVITYIVLAGTCMVLGDGALTPAISVLSAVQGIQSRSSSITQAHVVLLSVIILFILFFFQKHGTSKVSFTFSPIMILWFTFVAFIGLYNIIKHYPPILKAVSPHYIIIYFIRNKRAAWETLG... | Function: High-affinity potassium transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 82596
Sequence Length: 739
Subcellular Location: Membrane
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Q5ZC87 | MPVADCESGLSPADVTGAGAANGNPGHWRSYYRHVLLLAYQSCGVVYGDLSTSPLYVYKSTFIIGSLRRFQDEEIVFGVFSLVFWTLTLIPLLKYVFIVLAADDNGEGGTFALYSLLVRHAKFSLMPNQEAADEELTSYYRPGYAPQETPILTALRRFLENHRKSRTFLLVTVLFGASLVIGDGVLTPPMSVLSSFSGLQVHSTALTSGEVEILSCTVLVCLFMVQHWGTHRVAFLFAPVVIVWLLLLGALGVYNIVVWNPRVLRALSPYYLVRFFQHTGKDGWISLGGILLSMTGTEAMYADLGHFTAASIRVAFVGLI... | Function: High-affinity potassium transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 89321
Sequence Length: 808
Subcellular Location: Membrane
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Q5JK32 | MTEPLHTSSNGGAERGPNAAFESEKTLQTTTRLQRFDSLHMEAGKIPGGQSHTAKVGWATTLHLAFQSIGVVYGDMGTSPLYVFSSTFTNGIKDTNDILGVMSLIIYTVVLLPLIKYCFIVLRANDNGDGGTFALYSLISRYARISLIPNQQAEDAMVSHYKLESPSNRVKRAHWIKEKMENSPNFKIILFLVTILATSMVIGDGVLTPCISVLSAVGGIKESAKSLTQGQIAGIAIAILIVLFLVQRFGTDKVGYSFGPIILTWFIFIAGTGVYNLFKHDTGVLKAFNPKYIVDYFERNGKQGWISLGGVILCITGTEA... | Function: High-affinity potassium transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 87075
Sequence Length: 781
Subcellular Location: Membrane
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Q5JMH0 | MVPPGNGNGAAAAAGNDVILELSTPGDDWSHELQGDDVEANGGGNGDAPPRRTFSFGQAYKTRHRQPQVFTVWQTLMLGYQSLGIVYGDLGTSPLYVFPSVVLPDADATDFLGILSLIIWTLTLMSLVKYALIVLKADDHGEGGTFALYSLLRQHVNFKGNIPVPLTRLESDVHLKFHSKRRSRPSRLQLFLENSPKAQLAITIIVLIGTCMLIGDGALTPAISVLSAVQGIQSRSSHIKQKHVVVLSAVILVLLFLVQRFGTSRVSFTFSPIMLLWFASIAGIGVYNIVMHYPPVLKAVSPHYIYYYFAKNKRVGWEQL... | Function: High-affinity potassium transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 81886
Sequence Length: 748
Subcellular Location: Membrane
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Q8H3P9 | MPSYQYLLSLLFYILDCTDRFSVIVTIHNHRVGVLMIVLLQDQWKSYCRTISLLAFQSFGVVYGDLSTSPLYVYKSAFSGRLNNYRDETTIFGLFSLIFWTLTLLPLLKYVIIVLNADDNGEGGTFALYSLLCRHAKFSLLPNQQSADEELSTYYQPGVGGIISSPLKRFLEKHRKLRTCLLLFVLFGACMVIGDGVFTPAISVLSAISGLKDPGPGGIPDGWVVFIACIVLVGLFALQHRGTHRVAFMFAPIVVVWLLSIGVIGLYNIIHWNHRIFLALSPHYVIKFFKMTGKDGWLSLGGVLLAITGTEAMFADLGHF... | Function: High-affinity potassium transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 90850
Sequence Length: 811
Subcellular Location: Membrane
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Q9LFC0 | MLQIRLRRDSPTETGNGARPSPTETVTVACPDHLVLADLPVAKGIGSVTPTTVIKPVGRRSRRQLGERVHFCVRCDFPIAIYGRLIPCDHAFCLECARSDSICYLCDERIQKIQTIKMMEGIFICAAPHCLRSFLKKLDFEAHVHDLHGSLLQADAEKEDGNQSDVQSTMQQSSASESTLRAPLRSQLQQSRELNRSASFAKSQSGFSQVQNYPPDSDNSRPPGFETASPKPGIRFPDYPQPMNLMQPPSLPVPMNQNPGLPQQFGFPSYPTTESGSSQQFFNGAQYEMTRTESGGSEQSSLLGYPPPSPMTNLNFQGSY... | Function: Probable E3 ubiquitin-protein ligase which is a subunit of the N6-methyltransferase complex, a multiprotein complex that mediates N6-methyladenosine (m6A) methylation at the 5'-[AG]GAC-3' consensus sites of some mRNAs . Associates with MTA, MTB, FIP37 and VIR to form the m6A writer complex which is essential ... |
M9PBE2 | MDTEEVKRGRGRGRGTRARGRGRGRGRGRGKKIDDSSIADAAALAASSCAALEDSPGRLDASEDSVMQELDKDGELETPGALEEPLPHGALGAVAASGNMTPATQQPQVLQQVPPPVMSQTTISLSLARAVDMEADISQLEAPTFTTLSRGPPEPMLRLKWNHKVSLIGEKVLNPMIHCCDQCDKPILVYGRMIPCKHVFCLKCARAEPIKSCPRCTDKVLRVEQSGLGTVFMCTHGGSRYGSSGCRRTYLSQRDLQAHINHRHVAPQPPPLQPQPQLSAMAEQPKMTDLGGVGLGLELHKQRKLSESSVPISVSASIAS... | Function: E3 ubiquitin-protein ligase required during early development . E3 ubiquitin-protein ligases mediate ubiquitination of target proteins . Required for epithelial integrity and midgut morphogenesis . Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a... |
Q9JIY2 | MDHTDNELQGTNSSGSLGGLDVRRRIPIKLISKQASKVKPAPRTQRTVSRMPAKAPQGDEEGFDYNEEQRYDCKGGELFGNQRRFPGHLFWDFKINILGEKDDTPVHFCDKCGLPIKVYGRMIPCKHVFCYDCAILHEKKGDKMCPGCSDPVQRIEQCTRGSLFMCSIVQGCKRTYLSQRDLQAHINHRHMRAGKPVTRASLENVHPPIAPPPTDIPDRFIMPPDKHHMSHIPPKQHIMMPPPPLQHVPHEHYNQPHEDIRAPPAELSMAPPPPRSVSQETFRISTRKHSNLITVPIQDDSSSGAREPPPPAPAPAHHHP... | Function: E3 ubiquitin-protein ligase that mediates ubiquitination of several tyrosine-phosphorylated Src substrates, including CDH1, CTTN and DOK1 . Targets CDH1 for endocytosis and degradation . Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modificati... |
Q4V7X9 | MDHNDNDLQGTNSMGSLSGLDVRRRIPIKLISKHPNKIKPAPRPQRNMNRIPTKPQPGFDYNEEERYENKGDVFNNQRRFSAHLFWDFKLNLIGEKEDTPVHFCDKCGLPIKIYGRMIPCKHVFCYDCALMHEKKADKLCPGTLVEDSTDTFKRMSCNDPVQRIEQCARGSLFMCSIVQGCKRTYLSQRDLQAHINHRHMRASKPTARPQPEPIHPPLAPPPAEIPDRFIMPPDKHHLSHMPPKQHILMPPPPMQHVPHEHFSQQHDDIRPSPADISLAPPPPRSVNQDAFRISTRQHSNLITVPIQDDSNSGARETPQA... | Function: E3 ubiquitin-protein ligase that mediates ubiquitination of several tyrosine-phosphorylated Src substrates. Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing.
Cat... |
Q5W6B9 | MPRRRGTPLPTILLLLAFVGGACGTEILSKSRLESCSHDSDAGGRLKCDRKLVVDLAVPSGASGGEASLVARVAGVEEENDTPSATKSIRDPPVITVSKSATYALYALTYLDRDVAYRPDEKYVKTHKCEPYAGAKVVGECERLWDEKGNVIKQTEPICCPCGPHRVQSKCGDIWSKLTKGKANTAHCVRFPGDWFHVFGIGAWSLRFSIRVQVKKGSSVWDVVVGPENKTVVSGDNFLRVKVVGDYTGYTSIPSFEDNYLVTPRKGTGSSQPQDLGNEHSKWMILDRVRFTLDGLECDKIGVGYEAYRNQPNFCSAPYG... | Function: Required for male fertility. Plays a role in pollen tube guidance and successful gamete attachment. Essential for the fusion of gametes during double fertilization, where one male gamete fuses with the egg to produce a zygote, and another male gamete fuses with the central cell to produce the endosperm . Medi... |
B9G4M9 | MAPRRRRRAARSSRPLLLALLAAAVNNFAPAGGVEVLAKSRLESCARGGSDDGRDRLTCDSKIVVDLAVPSGSASLVARVAEVEENGTEAGEMPIRDPLIITINKSEVYALYDLTYLRDVAYKPEEKFVKTRKCEPEAGANVVKSCERLRDEKGSIIEHTEPVCCPCGPHRRVPSSCGNILDKVAKGKANTAHCLRFPDDWFHVFDIGRRSLWFSIRVQVKKGSSESEVIVGPENRTVVSEDSSLRVNLVGDFAGYTSLPSLENFYLVTPRKGVGGGQLEVLGDDFSRWMLLERVLFTLDGLECNKIGVGYEAFRSQPNF... | Function: Required for male fertility. Plays a role in pollen tube guidance and successful gamete attachment. Essential for the fusion of gametes during double fertilization, where one male gamete fuses with the egg to produce a zygote, and another male gamete fuses with the central cell to produce the endosperm. Media... |
F4JP36 | MVNAILMACILAGIFVGMFNEVDGIQILSKSKLEKCEKTSDSGNLNCSTKIVLNLAVPSGSSGGEASIVAEIVEVEDNSSSNMQTVRIPPVITVNKSAAYALYDLTYIRDVPYKPQEYHVTTRKCEHDAGPDIVQICERLRDEKGNVLEQTQPICCPCGPQRRMPSSCGDIFDKMIKGKANTAHCLRFPGDWFHVFGIGQRSLGFSVRVELKTGTRVSEVIIGPENRTATANDNFLKVNLIGDFGGYTSIPSFEDFYLVIPREAAEAGQPGSLGANYSMWMLLERVRFTLDGLECNKIGVGYEAFNTQPNFCSSPYWSCL... | Function: Required for male fertility . Plays a role in pollen tube guidance and successful gamete attachment . Essential for the fusion of gametes during double fertilization, where one male gamete fuses with the egg to produce a zygote, and another male gamete fuses with the central cell to produce the endosperm . Me... |
A7SIM4 | MGRGQIIMILVGLLCLANESYSDVIAKSSLQMCENTGNSDDPYNVVDQKACEKKLIVTLSVRSGQNGTEFLKAVTNVSKVYDQTEKEMARLYNPFIITLAKTPVKLTYPYYYLAMVNNKPTERVVISDSKWHASGSYHACSDAWDDEDALCGFYTDAEGKPIWDSQGFCCRCTEQEKWRGSFNDKNPYSRAGINCKLFGTQAAAHCMTFDDLWYTVNEVGLWQMDFSIHVKAYDLVVEKVGNKTQSKWVDGGEIVIGPTIRSGVGVHGRLHATFIGEFQSHKQFPVLTTKYLLIPYVSEKVDPKTHPQFRNGPHDYMLID... | Function: During fertilization, required on male gametes for their fusion with female gametes . Probably initiates the fusion of gamete cell membranes by inserting part of its extracellular domain into the cell membrane of a female gamete .
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 9646... |
Q4YCF6 | MKNKLINLRSKHIYKLIIIIFFCIILKYYKWCDFKNKVFFIQLVYSFAKKSVCTSSLDDSTCHTVTFGELDVSNNSVVRLKVMRKGGKGYFLTIRRDYVTVSYYLKYVKDIPLEFREIIDIFNNHKFEQYTQEQINKYTYTCNVRKIEDIDKYDEKNPTKFHEYTRGEACRCQTYNYFKDDEFIKRAKLKCIYYNMLFTESATVYSRHCPIIDLMHFAVYDIEYPPIFNTIVNITIEEYYYNDVSSVLNNKSDLVTKEKKYQLNDTITEIRDDYFDLWLFLKGETHGKRTLVNLSNDYIVIPSSPINNRDVIASDITRNC... | Function: During fertilization, required on male gametes for their fusion with female gametes, and for subsequent ookinete formation in the host . Thereby, required for mosquito-mediated transmission to other animals . Probably initiates the fusion of gamete cell membranes by inserting part of its extracellular domain ... |
A0A060A682 | MKFLAFGLIYFHFCILNRCEYITSSTIQKCYNSSNEPNNCSQKAVIVLSLENGQIANTEQVVATLNQLSDSGVNKQLQNSFIFEVTKSPVTALFPLIYLQDFNSQPLEQVIATTLFSCKDGFYDSSPTCKFQYDSKGQKILDSQGYCCYCSLSDILGMGNDLSRGKVCYALNLGAGSATAHCLKFSPLWYSAFKIQQYQLYFEVNINIYTVDSQNQKNLKQTLKLSTSNPTMKSSDNSTISKIIGTFTPTQPPADLSSYYLVKPSFPATDPRVLQGISSWMFVDKTMFTLDGTQCNKIGVSYSGFRQQSSSCSQPVGSCL... | Function: During fertilization, required for the formation of intercellular membrane pores and subsequent exchange of gametic pronuclei between cells. Probably initiates the formation of intercellular membrane pores by inserting part of its extracellular domain into the cell membrane of the adjoining cell in the mating... |
Q48259 | NSGLVYRDMSGGINEAFSDIAGEAAEYFMRGNVDWIVGADIFKSSGGLRYFDQPSRDGRSIDHASQYYSGIDVHSSGVFNRAFYLLANKSGWNVRKGFEVFAVANQLYWTPNSTFDQGGCGVVKAAQDLNYNTADVVAAFNTVGVNASCGTTPPPVGKVLEKGKPITGLSGSRGGEDFYTFTVTNSGSVVVSISGGTGDADLYVKAGSKPTTSSWDCRPYRSGNAEQCSISAVVGTTYHVMLRGYSNYSGVTLRLD | Cofactor: Binds 1 zinc ion.
Function: May play a role in ulcer formation. Proteolytic digestion of gastric mucus has been suggested as an important mechanism by which its pathogenicity is at least partly exerted.
Sequence Mass (Da): 27276
Sequence Length: 256
Subcellular Location: Secreted
EC: 3.4.24.-
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Q17QR8 | MAIPITVLDCDLLLYGRGHRTLDRFKLDDVTDEYLMSMYGFPRQFIYYLVELLGASLSRPTQRSRAISPETQILAALGFYTSGSFQTRMGDAIGISQASMSRCVANVTEALVERASQFIHFPADEASVQALKDEFYGLAGIPGVIGVVDCMHVAIKAPNAEDLSYVNRKGLHSLNCLMVCDIRGALMTVETSWPGSLQDCVVLQQSSLSSQFEAGMHKESWLLGDSSFFLRTWLMTPLHIPETPAEYRYNMAHSATHSVIEKTFRTLCSRFRCLDGSKGALQYSPEKSSHIILACCVLHNISLEHGMDVWSSPVTGPVEQ... | Function: Transposase-derived protein that may have nuclease activity (Potential). Does not have transposase activity (By similarity).
Sequence Mass (Da): 39003
Sequence Length: 349
Subcellular Location: Nucleus
EC: 3.1.-.-
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Q6AZB8 | MALSIAILDCDLLLHGRGHKTLDRFDIETVSDDFLLNTFGFPREFIYYLVELLKDSLLRRTQRSRAISPDVQILAALGFYTSGSFQSKMGDAIGISQASMSRCVSNVTKALIEKAPEFIGFTRDEATKQQFKDEFYRIAGIPNVTGVVDCAHIAIKAPNADDSSYVNKKGFHSINCQLVCDARGLLLSAETHWPGSLTDRAVFKQSNVAKLFEEQENDDEGWLLGDNRYPLKKWLMTPVQSPESPADYRYNLAHTTTHEIVDRTFRAIQTRFRCLDGAKGYLQYSPEKCSHIIQACCVLHNISLQSGLDAWTFERTEATD... | Function: Transposase-derived protein that may have nuclease activity (Potential). Does not have transposase activity (By similarity).
Sequence Mass (Da): 39329
Sequence Length: 349
Subcellular Location: Nucleus
EC: 3.1.-.-
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Q96MB7 | MAIPITVLDCDLLLYGRGHRTLDRFKLDDVTDEYLMSMYGFPRQFIYYLVELLGANLSRPTQRSRAISPETQVLAALGFYTSGSFQTRMGDAIGISQASMSRCVANVTEALVERASQFIRFPADEASIQALKDEFYGLAGMPGVMGVVDCIHVAIKAPNAEDLSYVNRKGLHSLNCLMVCDIRGTLMTVETNWPGSLQDCAVLQQSSLSSQFEAGMHKDSWLLGDSSFFLRTWLMTPLHIPETPAEYRYNMAHSATHSVIEKTFRTLCSRFRCLDGSKGALQYSPEKSSHIILACCVLHNISLEHGMDVWSSPMTGPMEQ... | Function: Transposase-derived protein that may have nuclease activity (Potential). Does not have transposase activity.
Sequence Mass (Da): 39146
Sequence Length: 349
Subcellular Location: Nucleus
EC: 3.1.-.-
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Q5U538 | MAVPITVLDCDLLLYGRGHRTLDRFRLDDVTDDYLVTTYGFPRPFIDYLVDLLGASLSRPTHRSRAISPETQIMAALGFYTSGSFQTRMGDTIGISQASMSRCVTNVTEALVERASQFISFPRDERSVQGLKDEFYNLAGVPGVLGVVDCTQVNIKAPNSEDLSYVNSRGLHSLNCLLVCDARGSLLWAETSRLGSMQDNAVLHQSELSGLFETKMHKQGWLLADNAFILRPWLMTPVQIPESPSDYRYNMAHTATHSVMERTQRSLRLRFRCLDGSRATLQYSPEKSAQIVLACCILHNIALQHDLDIVSESGATSLEP... | Function: Transposase-derived protein that may have nuclease activity (Potential). Does not have transposase activity (By similarity).
Sequence Mass (Da): 38928
Sequence Length: 347
Subcellular Location: Nucleus
EC: 3.1.-.-
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P14483 | MALQIPSLLLSAAVVVLMVLSSPGTEGGDSERHFVYQFMGECYFTNGTQRIRYVTRYIYNREEYVRYDSDVGEHRAVTELGRPDAEYWNSQPEILERTRAELDTVCRHNYEGPETHTSLRRLEQPNVVISLSRTEALNHHNTLVCSVTDFYPAKIKVRWFRNGQEETVGVSSTQLIRNGDWTFQVLVMLEMTPRRGEVYTCHVEHPSLKSPITVEWRAQSESAWSKMLSGIGGCVLGVIFLGLGLFIRHRSQKGPRGPPPAGLLQ | PTM: Ubiquitinated in immature dendritic cells leading to down-regulation of MHC class II.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 30128
Sequence Length: 265
Subcellular Location: Membrane
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P29826 | MALQTPSFLLPAAVVVLMVLSSPGTEGRDSPRDFVYQFKGLCYYTNGTQRIRDVIRYIYNQEEYLRYDSDVGEYRALTELGRPSAEYFNKQYLEQTRAELDTVCRHNYEGSEVRTSLRRLEQPNVAISLSRTEALNHHNLLVCSVTDFYPAQIKVRWFRNGQEETAGVVSTQLIRNGDWTFQILVMLEMTPQRGEVYICHVDHPSLESPVTVEWRAQSESAQSKMLSGIGGFVLGVIFLGLGLFIRHKRQKGPRGPPPAGLLQ | Function: Involved in the presentation of foreign antigens to the immune system.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 29935
Sequence Length: 263
Subcellular Location: Membrane
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P18211 | MVWLARDSCVAAVILLLTVLSPPVALVRDPTPRFLEQVKGECHFYNGTQRVRFLARYIYNREEYTRFDSDVGEFRAVTELGRPSAEYYNKQKEYMEQLRATVDTACKHDYEISESFLVPRTVEPKVTVYPSKTQPLEHHNLLVCSVSDFYPGSVEVRWFRNGEEEKDGLVSTGLIRNGDWTFQLLVMLETVPQGGEVYTCQVEHPSLPSPVRVEWKAQSTSAQNKKMSGVGGIVLGLLFLGAGLFVYFRNQKGQSGLQPTGLLN | Function: Involved in the presentation of foreign antigens to the immune system.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 29876
Sequence Length: 264
Subcellular Location: Membrane
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Q7N4V9 | MKELIVNQEKRVSPELHYEISQFLYYEIALLDEWRFRDWLELLSEDLSYTMRTIVNAQTRDRRKSIQPPTTWLFNDNKFQLERRIARLETGMAWAEEPPSRTRHLLTNLVITETDLPDQFHVQSNYLLYRSQKERDEVFYVGKRLDCVRRNPKTDSWLICKREITLDQAVLTFHNLSVLF | Function: Part of the multicomponent 3-phenylpropionate dioxygenase. Converts 3-phenylpropionic acid (PP) and cinnamic acid (CI) into 3-phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid-dihydrodiol (CI-dihydrodiol), respectively.
Catalytic Activity: 3-phenylpropanoate + H(+) + NADH + O2 = 3-(cis-5,6-dihyd... |
Q9BXC0 | MYNGSCCRIEGDTISQVMPPLLIVAFVLGALGNGVALCGFCFHMKTWKPSTVYLFNLAVADFLLMICLPFRTDYYLRRRHWAFGDIPCRVGLFTLAMNRAGSIVFLTVVAADRYFKVVHPHHAVNTISTRVAAGIVCTLWALVILGTVYLLLENHLCVQETAVSCESFIMESANGWHDIMFQLEFFMPLGIILFCSFKIVWSLRRRQQLARQARMKKATRFIMVVAIVFITCYLPSVSARLYFLWTVPSSACDPSVHGALHITLSFTYMNSMLDPLVYYFSSPSFPKFYNKLKICSLKPKQPGHSKTQRPEEMPISNLGR... | Function: Acts as a receptor for L-lactate and mediates its anti-lipolytic effect through a G(i)-protein-mediated pathway.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39295
Sequence Length: 346
Subcellular Location: Cell membrane
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Q9P1Z3 | MEAEQRPAAGASEGATPGLEAVPPVAPPPATAASGPIPKSGPEPKRRHLGTLLQPTVNKFSLRVFGSHKAVEIEQERVKSAGAWIIHPYSDFRFYWDLIMLLLMVGNLIVLPVGITFFKEENSPPWIVFNVLSDTFFLLDLVLNFRTGIVVEEGAEILLAPRAIRTRYLRTWFLVDLISSIPVDYIFLVVELEPRLDAEVYKTARALRIVRFTKILSLLRLLRLSRLIRYIHQWEEIFHMTYDLASAVVRIFNLIGMMLLLCHWDGCLQFLVPMLQDFPPDCWVSINHMVNHSWGRQYSHALFKAMSHMLCIGYGQQAPV... | Function: Hyperpolarization-activated potassium channel. May also facilitate the permeation of sodium ions.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 86032
Sequence Length: 774
Domain: The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino aci... |
G3XD67 | MHLLERQHDIQPLSRADMTIHLNGQPVAAAAGETVLNVLNAVGLRRLARNDHGQASGAFCGMGVCHCCLVAIDGRPKRRACQTVVRPGMRVETESNRFDQEERP | Function: A three-component membrane-bound flavoenzyme that catalyzes the formation of hydrogen cyanide, a secondary metabolite, by transfer of electrons to a cyanide-resistant branch of the aerobic respiratory chain.
Catalytic Activity: 2 A + glycine = 2 AH2 + CO2 + hydrogen cyanide
Sequence Mass (Da): 11427
Sequence ... |
O85226 | MRQIDRNFDIQPLQHADMTISLNGQPVTAALGETVLSVIQATGLRQVARNDHGQLVGAYCGMGVCHCCLVQIDGRHKRRACQTLVKPGMQVQTLSNRITETEPTL | Function: A three-component membrane-bound flavoenzyme that catalyzes the formation of hydrogen cyanide, a secondary metabolite, by transfer of electrons to a cyanide-resistant branch of the aerobic respiratory chain. Contributes to suppression of black root rot of tobacco .
Catalytic Activity: 2 A + glycine = 2 AH2 + ... |
Q9I1S2 | MNLRPVIVGGGSAGMAAAIELARRGVPCVLFDEASRPGGVVYRGPLRAGVDPAYLGARYTRMLEKLRRDFSACAGHIDLRLNSRVVGGDGQRLMVLDEAERLHEVEYSHLLLATGCHERSVPFPGWTLPGVMLLGGLQLQIKSGVVKPLGDTLIAGSGPLLPLVACQLHAAGVRVAGVYEACAFGRMARESLALLNKPQLFLDGLSMLGYLKLNGIPLHYGWGVVEASGDGELTEVTVAPYDEEWRPDLENARPVKASTLAVGYGFIPRTQLSQQLGLEHGFSDDGYLRAECNVWQQSSQPHIHLAGDMAGIRGGEAAMI... | Function: A three-component membrane-bound flavoenzyme that catalyzes the formation of hydrogen cyanide, a secondary metabolite, by transfer of electrons to a cyanide-resistant branch of the aerobic respiratory chain.
Catalytic Activity: 2 A + glycine = 2 AH2 + CO2 + hydrogen cyanide
Sequence Mass (Da): 50389
Sequence ... |
G3XD12 | MNRTYDIVIAGGGVIGASCAYQLSRRGNLRIAVVDDKRPGNATRASAGGLWAIGESVGLGCGVIFFRMMSSRNRREAQGAAVAVDASTPHILPPAFFDLALQSNALYPELHRELIERHGMDFKFERTGLKYVIQDDEDRQYAEHIVAQIPHLAEQVRWLDREELRRAEPAVSHAAHGALEFLCDHQVSPFRLADAYLEAARQNGVELLPGTNVTGVLRQGRRISGVRTDNAGVLHCRTLINAAGAWAAELSEMATGRRIPVKPVKGQIVLTERMPRLLNGCLTTSDCYMAQKDNGEILIGSTTEDKGFDVSNTFPEIAGL... | Function: A three-component membrane-bound flavoenzyme that catalyzes the formation of hydrogen cyanide, a secondary metabolite, by transfer of electrons to a cyanide-resistant branch of the aerobic respiratory chain.
Catalytic Activity: 2 A + glycine = 2 AH2 + CO2 + hydrogen cyanide
Location Topology: Single-pass memb... |
F4I4W2 | MDIDASCSLVLYGKSSVETDTATRLKNNNVLKLPDNSKVSIFLQSEIKNLVRDDDSSFNLSLFMNSISTHRFGRFLIWSPYLSSTHDVVSHNFSEIPVGSVCVSDIQLKGRGRTKNVWESPKGCLMYSFTLEMEDGRVVPLIQYVVSLAVTEAVKDVCDKKGLSYNDVKIKWPNDLYLNGLKIGGILCTSTYRSRKFLVSVGVGLNVDNEQPTTCLNAVLKDVCPPSNLLKREEILGAFFKKFENFFDLFMEQGFKSLEELYYRTWLHSGQRVIAEEKNEDQVVQNVVTIQGLTSSGYLLAIGDDNVMYELHPDGNSFDF... | Function: Seems to have no or limited implication in biotin-dependent carboxylase biotinylation in planta.
Sequence Mass (Da): 37152
Sequence Length: 329
Subcellular Location: Cytoplasm
EC: 6.3.4.-
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Q1XF11 | MVPPGNILFLLLLPVATAQMTPGSCSGCGPLSLPLLAGLVAADAVVSLLIVVVVFVCARLRSRPTQEDDKIYINMPGRG | Function: Transmembrane adapter protein which associates with KLRK1 to form an activation receptor KLRK1-HCST in lymphoid and myeloid cells; this receptor plays a major role in triggering cytotoxicity against target cells expressing cell surface ligands such as MHC class I chain-related MICA and MICB, and UL16-binding ... |
Q9UBK5 | MIHLGHILFLLLLPVAAAQTTPGERSSLPAFYPGTSGSCSGCGSLSLPLLAGLVAADAVASLLIVGAVFLCARPRRSPAQEDGKVYINMPGRG | Function: Transmembrane adapter protein which associates with KLRK1 to form an activation receptor KLRK1-HCST in lymphoid and myeloid cells; this receptor plays a major role in triggering cytotoxicity against target cells expressing cell surface ligands such as MHC class I chain-related MICA and MICB, and UL16-binding ... |
Q9QUJ0 | MDPPGYLLFLLLLPVAASQTSAGSCSGCGTLSLPLLAGLVAADAVMSLLIVGVVFVCMRPHGRPAQEDGRVYINMPGRG | Function: Transmembrane adapter protein which associates with KLRK1 to form an activation receptor KLRK1-HCST in lymphoid and myeloid cells; this receptor plays a major role in triggering cytotoxicity against target cells expressing cell surface ligands such as MHC class I chain-related MICA and MICB, and UL16-binding ... |
Q9GJR5 | MAPPGGILFLLLLPVAAAQVTSGSCSGCGPLSLPLLAGLVAADAVVSLLIVVGVFVCGRPRSRPTQEDGKIYINMPGRG | Function: Transmembrane adapter protein which associates with KLRK1 to form an activation receptor KLRK1-HCST in lymphoid and myeloid cells; this receptor plays a major role in triggering cytotoxicity against target cells expressing cell surface ligands such as MHC class I chain-related MICA and MICB, and UL16-binding ... |
E4MYY0 | MAEFEIPDFYVPFPLECNPHLEEASRAMWEWIDANGLAPTERARDRMRRTGADLSGAYVWPRADLDTLTIGLKWIALTFRIDDQIDEDDTAERLPARMTAIDELRGTLHGLPVSGRSPTARALGALWQETALGRPATWCDAFIGHFEAFLQTYTTEAGLNAHGAGLRLDDYLDRRMYSVGMPWLWDLDELRLPIFLPGSVRTCGPMNKLRRAGALHIALVNDVFSVERETLVGYQHNAVTIIREAQGCSLQEAVDQVAVLVEAQLHTVLQARQELLEELDRQALPSRAREAAVDYAANVAANLSGQLVWHSSVERYAVDD... | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Catalyzes the conversion of (2E,6E)-farnesyl diphosphate (FPP) into (2Z,6E)-hedycaryol via a 1,11-cyclization.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + H2O = (2Z,6E)-hedycaryol + diphosphate
Sequence Mass (Da): 37591
Sequence Length: 338
Domain: The Asp-Asp... |
D4NUX0 | MVCIKSSCVVKPSEPTPNVKLFLPESDQVKPWTHAPVFFVYQPEVDNSVSTSLENLKFSLSRALVPYYPLAGRLNGIGGGRFELHCNTMGAVIIEAESDARLEDFGDFRPTSETTKLAPYVDYAKDVSELPLLLVQLTRFKCGGIGIGIAMSHIVSDGKGAFGFITTWAKINRGEKGIIEPFHDRTAFYKGDPTAKPRCDHVELKGYPVLLGNKSAKEERAKETTTRMLNLSKNQVDKLKEKSNLGKPKDYVGREYSRFEAMSGHIWRCASKARRHENEQLTSLRITIDCRNRLRPPLPPRYSGNATMVTTSIAESGELL... | Function: Catalyzes the formation of cimicifugic acids. Uses hydroxycinnamoyl-CoA thioesters as hydroxycinnamoyl donor substrates. Has a strict specificity for piscidic acid as an acceptor substrate as none of the various other acceptors tested including 4-hydroxyphenyllactic acid, malate, spermidine or tetrahydroxyhex... |
P70288 | MAYSQGGGKKKVCYYYDGDIGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSDEYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVAGAVKLNRQQTDMAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNFPMRDGIDDESYGQIFKPIISKVMEMYQPSAVVLQCGADSLSGDRLGCFNLTVKGHAKCVEVAKTFNLPLLMLGGGGYTIRNVARCWTYETAVA... | Function: Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) . Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events . H... |
Q6YV04 | MDPSSAGAGGNSLASASCGDAQKRRVCYFYDPEVGNYYYGQGHPMKPHRVRMTHALLAHYGLLAPAKMQVLRPLPARDRDLCRFHSDDYVAFLRAVTPETQFDQIRSLRRFNVGEDCPVFDGLYAYCQTYAGASVGAAVKLNHGTHDIAINWSGGLHHAKKSEASGFCYVNDIVLAILELLKLHERVLYIDIDIHHGDGVEEAFYTTNRVMTVSFHKFGDYFPGTGDIRDIGYSEGKYYCLNVPLDDGIDDDSYQSIFKPIISKVMEMYRPGAVVLQCGADSLSGDRLGCFNLSGKGHAECVKFMRSFNVPLLLLGGGGY... | Cofactor: Binds 1 zinc ion per subunit.
Function: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and deve... |
Q803C3 | MTNRTAYFYDPDVGNFHYGAGHPMKPHRLSLTHSLVLHYGLYKKMMVFKPYKASQHDMCRFHSEDYIDFLQKVSPNNMQGFTKSLNTFNVGGDCPVFPGLFEFCSRYTGASLQGATQLNHKICDIAINWAGGLHHAKKFEASGFCYVNDIVISILELLKYHPRVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYCLNVPLRDGIDDQSYRQLFQPVIKQVVDFYQPTCIVLQCGADSLGCDRLGCFNLSIRGHGECVEFVKGFKIPLLVLGGGGYTVRNVARCWTFETSLLVEESIS... | Function: Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4), and some other non-histone substrates. Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle pr... |
O15379 | MAKTVAYFYDPDVGNFHYGAGHPMKPHRLALTHSLVLHYGLYKKMIVFKPYQASQHDMCRFHSEDYIDFLQRVSPTNMQGFTKSLNAFNVGDDCPVFPGLFEFCSRYTGASLQGATQLNNKICDIAINWAGGLHHAKKFEASGFCYVNDIVIGILELLKYHPRVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYCLNVPLRDGIDDQSYKHLFQPVINQVVDFYQPTCIVLQCGADSLGCDRLGCFNLSIRGHGECVEYVKSFNIPLLVLGGGGYTVRNVARCWTYETSLLVEEAIS... | Function: Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4), and some other non-histone substrates . Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle p... |
Q7Y0Y6 | MDPSSAGAGGNSLASASCGDAQKRRVCYFYDPEVGNYYYGQGHPMKPHRVRMTHALLAHYGLLAPAKMEVLRPLPARGIDLCRFHSDDYVAFLRAVTPETQLGQVRALRRFNIGPDCPVFDGLYAYCQTYAGASVGAAVKLNHGTHDIAINWSGGLHHAKKSEASGFCYVNDIVLAILELLKLHERVLYIDIDIHHGDGVEEAFYTTNRVMTVSFHKFGDYFPGTGDIRDIGYSEGKYYCLNVPLDDGIDDDSYQSIFKPIISKVMEMYRPGAVVLQCGADSLSGDRLGCFNLSGKGHAECVKFMRSFNVPLLLLGGGGY... | Cofactor: Binds 1 zinc ion per subunit.
Function: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and deve... |
Q974S1 | METISIDDLPLDIKIIDILKRRGIRTLNPPQSEAIRKGLLDGKRLLVTSPTASGKTLIAELGMINYLLSKGGKAIYITPLRALTNEKYNTFKDWETLGIKTGMTSGDYDTDDAWLENYDIIVTTYEKLDSLWRHKAKWLNEVSYFVLDEFHYLNDPERGPTVESVAIRAKKRGIVLGLSATISNGKEIANWLNAELVATNWRPVPLKEGIIYPEKKGFVVVYKDNTSRKVYGDDAIIAYTLDIVSKGGQVLVFRSSRKLAENTARKIVQYMNFVKLEDKKLLEIARKIKEVEDAGSNEKEDLYNLVLRGVAYHHAGLSKG... | Function: An ATP, Mg(2+)-dependent DNA 3'-5' and 5'-3' helicase that may be involved in repair of stalled replication forks. Stimulated by both ss and dsDNA. Unwinds both leading and lagging strands in replication fork structures, unlike orthologs in P. furiosus and M. thermautotrophicus which only unwind the lagging s... |
Q9HJX7 | MKISELGYDRAFLQLFDGNDFQLYDHQRMAIEQIRKGRNVVVSVPTAAGKTLIAYSAIYETFQRNLKSIYIVPLRSLAMEKFSELSRLRDLGLKVKMSIGDYDDSPDFIKRYDAVILTSEKADSLLHHDPYILNDVGLLVLDEIHTIGDESRGPTLETVASIARYVNPDVRILALSATVSNAMELASWLDASLIKSDFRPVPLKTGILYRDQLYLDGKRRSGVSINQIIRETVEDNGQVLMFVSSRKKAEDTARDLAQIFGSDANIKISSDETNVYDDMLNEILPRGVAFHHAGLSNDQRAFIEREFRARRIKVIVATPT... | Function: DNA-dependent ATPase and 3'-5' DNA helicase that may be involved in repair of stalled replication forks.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 75754
Sequence Length: 674
EC: 3.6.4.12
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Q97AI2 | MKISDLGYDESFLDLFEGNDFELYDHQRMAIEQFRKGKNIMVSVPTAAGKTLIAYSAIYETFKKKLKSIYIVPLRSLAMEKYEELSRLRELGMRVKLSIGNYDDTPDFIKRYDVVILTSEKADSLMHHDPYMMEEVGLMVIDEIHMIGDEYRGPTLETVITTARYVNPETRIIALSATVSNASEIAEWLNASLIKSSFRPVPLKVGILYRNRLFLDGDARSDVDINLLVKETVDDGGQVLIFVSSRKRAEDMAKNLSQLFDPINDLKVSSEDANVYDDLLNEMLPHGVSFHHAGLSNEQRSFIEKAFRHRKLKVIVATPT... | Function: DNA-dependent ATPase and 3'-5' DNA helicase that may be involved in repair of stalled replication forks.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 76594
Sequence Length: 674
EC: 3.6.4.12
|
P28462 | MNIISVGVNHKTAPIEIRERIALSEVQNKEFVTDLVSSGLASEAMVVSTCNRTELYVVPGMPEVNCDYLKDYIISYKDARNAVRPEHFFNRFYCGTARHLFEVSSAIDSLVLGEGQILGQVKDAYRIAAEVGTAGILLTRLCHTAFSVAKKVKTRTKLMEGAVSVSYAAVELAQKIFSNLSMKKVLLIGAGETGELAAKHMYAKNARNIVITNRTQSKAEALAEELGTNRVLPYESYKEHLHEFDIIITAVSTKEYILNAAEMQQSMAKRRLKPVIILDLGLPRNVDPEVGALQNMFLKDIDALKHIIDKNLERRRAELP... | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 48142
Sequence Length: 426
Domain: Possesses an unusual extended V-shaped dimeric str... |
Q9Z7J1 | MVLGVVGISYREAALKERERAIQYLQSFEKNLFLAQRFLGKGGAFIPLLTCHRAELYYYSESPEIAQAALLSELTSQGIRPYRHRGLSCFTHLFQVTSGIDSLIFGETEIQGQVKRAYLKGSKERELPFDLHFLFQKALKEGKEYRSRIGFPDHQVTIESVVQEILLSYDKSIYTNFLFVGYSDINRKVAAYLYQHGYHRITFCSRQQVTAPYRTLSRETLSFRQPYDVIFFGSSESASQFSDLSCESLASIPKRIVFDFNVPRTFLWKETPTGFVYLDIDFISECVQKRLQCTKEGVNKAKLLLTCAAKKQWEIYEKKS... | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 39104
Sequence Length: 339
Domain: Possesses an unusual extended V-shaped dimeric str... |
O84669 | MVREGEERIGNRVSLGVIGVSYRETTLQQREQVLHILQQAQGSFRPEVFQEERDYVLLATCHRVELYSVAPAELFDSLAQEIELLGVSPYFYRNQDCFAHLFCVAGGLDSLVLGETEIQGQVKRAYLQAAREQKLSFALHFLFQKALKEGKVFRAKGGAPYAEITIPILVDQELRRRQIDKKASLLFIGYSEINRSVAYHLQRQGFSCITFCSRQQLPTLSMRQVVREELCFQDPYRVVFLGSSELQYALPHSLWESIWDIPDRIVFDFAVPRALPSHTVFPHRYVDMDQISDWLREHRKEVNSAHLHSLREVAYRYWNS... | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 38855
Sequence Length: 335
Domain: Possesses an unusual extended V-shaped dimeric str... |
Q1QXC7 | MTLLALGINHKTATIEVREQVAFTPAELAGALAELKSLPGVNEAAVLSTCNRTELYCVTDSQGEREVLDWLGRFHALPPETLMQSAYHYLDGEAARHLMRVAAGLDSMVLGEPQILGQLKEAYQLARDNAGLGGELERLFQHTFSVAKQVRSETGIGENPVSVAYAAVSLASHIFDDFGRARALLIGAGETIELVARHLREAGIRGLTVANRTRERAELLAHEVDAEAISLGEIPQALAHADIIISSTASPLPILGKGMVESALKKRRHRPMFMVDIAVPRDIESQVGELDDVFLYSVDDLQEVIEENRKQRAVAAAQAE... | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 46560
Sequence Length: 424
Domain: Possesses an unusual extended V-shaped dimeric str... |
C0QS44 | MEIFAVGLNYKTAPVDVREKLAISEDQLSGLLKKISEINSIYEVSILSTCNRVEIYGVTDDPDDAFNRIVQILSSYSGLQKNELEKYLFKLTGREAIKHIFKVSASLDSMVIGEPQIVCQFKDAFTKAREEKTVRHILTRLFDKALNVSKKIRTSTGISKRAVSISYAAVELAKKIFGDLSDKNVLLLGAGEMAELAARHLSSSGVKHIFVSNRTFEKAVQLAEEFGGSAIRFDKLFEFLPESDIVIVSTGAKEPILRKEHFEEINRIRKGDPVFIIDISVPRNVAEDVNDVDNVYLYNIDDLKVVVDKNLEERKLAALS... | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 50257
Sequence Length: 438
Domain: Possesses an unusual extended V-shaped dimeric str... |
Q6L0J9 | MIIMIPIYAITWNFRDTPEGFDKIVNNDYNYFESLCKKSSIDEFVILITCNRVEIYAYTRNEIDKDLFKDSLIYNYPESTMHLLRVASGLESMSIGENDIMRQVKEAYELSIKRKTSGKILSYIFKKALNVGKEVRTQTSISRGKTSIPAISLDICDNEYGINNKSILIIGNGKMATDFSRYLKEYRPGNVTIAGRSIDHARNLAVLYGYSYDSIKNLNNLIKNSDIIIAATSAGNYIVKDLGDLARNKYFIDISKPENIDPEISKYARLLSINEIGKILKRNEDEKKGEVEIAEVIINQEQKTIDEKLKEMMLDDVIAM... | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 46302
Sequence Length: 401
Domain: Possesses an unusual extended V-shaped dimeric str... |
Q9PA72 | MTLWVLGLNHQTAPMELRERASFVGDALPRALDSLRNLPNVNEAALLSTCNRTELYAETTNAQILLNWLEQHRPGLQNHLYQYRDAAAVRHLFRVATGLDSMVLGESQILGQVKDSWSMARTHGTLGNTLDRLFQHGFSVAKHARTNTRIGANPVSIASTAVRLAQDAFSPLNESTVLLIGTGETIQLAAKHLSEGRVQRLLIANRTHAKAQMLASQHGGYALPLTELNLHLAEADIIFSATAAPTPIVTQSNVESALHIRKRKPMLLFDLAIPRDIETEVGTLTDAYLYTIDDLERAVEENRRSRREAAETAEAIIELQ... | Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Mass (Da): 47936
Sequence Length: 432
Domain: Possesses an unusual extended V-shaped dimeric str... |
Q6CCW0 | MESLVRQSKKLCPYIGRTSASSLKQLGNGRLTQKAGQCPIMGKAMGVRGFKSDAGSNAESATVDVHAAVDTSKGTCPHAAQYSPVYPSSRLDNYPFGMTQRGLGKVPTQDAHNATTFNYESFYENKINAKHQDKSYRYFNNINRLAAEFPRAHRGSIEEDKVTVWCANDYLGMGRNPVVVDAMHETLDKYGAGAGGTRNIAGHNRHAVELEAAIADLHKKEAALVFSSCYVANDSTLSLLGQALPNCVYFSDASNHASMIHGIRHGGSEKVVWKHNDLADLEAKLARYPKSTPKVIAFESVYSMCGSIGPIEEICDLADK... | Function: Catalyzes the synthesis of 5-aminolevulinate (ALA) from succinyl-CoA and glycine, the first and rate-limiting step in heme biosynthesis.
Catalytic Activity: glycine + H(+) + succinyl-CoA = 5-aminolevulinate + CO2 + CoA
Sequence Mass (Da): 61237
Sequence Length: 563
Pathway: Porphyrin-containing compound metab... |
P09950 | MQRSIFARFGNSSAAVSTLNRLSTTAAPHAKNGYATATGAGAAAATATASSTHAAAAAAAAANHSTQESGFDYEGLIDSELQKKRLDKSYRYFNNINRLAKEFPLAHRQREADKVTVWCSNDYLALSKHPEVLDAMHKTIDKYGCGAGGTRNIAGHNIPTLNLEAELATLHKKEGALVFSSCYVANDAVLSLLGQKMKDLVIFSDELNHASMIVGIKHANVKKHIFKHNDLNELEQLLQSYPKSVPKLIAFESVYSMAGSVADIEKICDLADKYGALTFLDEVHAVGLYGPHGAGVAEHCDFESHRASGIATPKTNDKGG... | Function: Catalyzes the synthesis of 5-aminolevulinate (ALA) from succinyl-CoA and glycine, the first and rate-limiting step in heme biosynthesis.
Catalytic Activity: glycine + H(+) + succinyl-CoA = 5-aminolevulinate + CO2 + CoA
Sequence Mass (Da): 59362
Sequence Length: 548
Pathway: Porphyrin-containing compound metab... |
Q180R9 | MNIVVGTRGSNLALIQTEWVINELKKKYPEISFEIKIIKTKGDLIQNVSLDKIGDKGLFVKEIEQQLLDGKIDIAVHSMKDMPSYLANGLKFAHTPKREDPRDVLILREGYKNLDDLPHGAVIGTGSKRRKFQLLKQRPDLNIVQVRGNVETRIRKIKDENMHGIVLAASGIIRANLQDKISSYLPVDVVIPAPAQGALAIEIRSNDSAIEGIVNSLKDENTEIQILAERGFLDGVNGSCHIPMAAYCEIIQDKIHLTGLYGDSEGKKVVIKSIDGDISSPRELGLKLAKLVLKEYENYEG | Cofactor: Binds 1 dipyrromethane group covalently.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Mass (Da): 33399
Sequence Length: 301
Pathway: Porphy... |
Q8XKG4 | MELIIATRKSKLAQVQTEKVMELLKGKENVDSKKLLVMTEGDRRLDVSLNKIGGKGLFVKEIELALLNKEAHGAVHSMKDVPFELPSEFELVAMPEREDIRDAFVSLNGSTLSNLRKGARIGTSSIRRAEQLKLFRDDLEIVPIRGNVQTRIKKITEENLDGIILAAAGLKRLGMEDVISDYFDPKVFLPAIGQGALGIECLKGGEFNDYFKALDSKEVRTTVEAERSFMKVLNGGCHSLIGAYSEVKDNDLYMIGTFTVNNRIVKKDILGNKEDNILLGKKLAEKILEEV | Cofactor: Binds 1 dipyrromethane group covalently.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Mass (Da): 32393
Sequence Length: 291
Pathway: Porphy... |
Q8FSF7 | MTLRIGTRGSKLATTQAGHMRDRLKHFGRDAELTIVTTPGDVNMSPVERIGVGVFTQALRDALVADEIDVAVHSFKDLPTAPDPRFHLVVPTRADARDALIARDGLTLEELPEGAKVGTSAPRRISQLKALRPDLEILPLRGNIDTRMGKVTSGELDAVVLAFAGLSRVGMQDRATQVFDPDMLMPAPAQGALAIECRVEDEDIITGLNMLMHADTYVTAVAERTVLNRLEAGCTAPVAAHATLDGYAGDTMTLTAGVFALDGSEQLVFSAQGAGERPEELAEQVAAQLIEQGAATLLG | Cofactor: Binds 1 dipyrromethane group covalently.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Mass (Da): 31784
Sequence Length: 299
Pathway: Porphy... |
Q8NT90 | MTLKIGTRGSKLATTQAGTIRDQLKHYGRDAELHIVTTPGDVNMSPVERIGVGVFTQALRDVLHSGECDVAVHSMKDLPTATDPRFHLVVPTRADSREALIARDGLTLAELPEGAKVGTSAPRRISQLKAIRPDLEILPLRGNIDTRMGKVTSGELDAVMLAYAGLTRVGMQDRATEVFDADIIMPAPAQGALAIECRADDTETVRALNMLMHADTFVSAVAERTVLNRLEAGCTAPVAAHATLDGYSGDTMTLTAGVYALDGSDQLVFSAEGDGARPEELGELVAQQLIDAGAANLLGDRS | Cofactor: Binds 1 dipyrromethane group covalently.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Mass (Da): 32009
Sequence Length: 302
Pathway: Porphy... |
B6J3T6 | MIKKRSILIVTRKSPLALWQAEFVKQQIENSHPHLACQILGCTTQGDRLTTEKLVDSGGKDLFVKDLQKALLNRDADIAVHSIKDMSACDGPELMVGAFIRREDPRDVLIVKGELSTLPPHAVIGTSSPRRQCQLKKFQPGCKIKEIRGNVGTRLAKLDAGHYEAIVLAAAGLKRLGLENRIHYYFDPHEFIPAIGQGAIGVECRSDDHEMQTLLKSLDHRETRLCVTAERAVNEKLGGDCFTPIAAHAIIKNDQLSLFAMLGKIDGRVIIRATEIGNSEEAKRIGFKVASQLLEQGGDSLLRELKQ | Cofactor: Binds 1 dipyrromethane group covalently.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Mass (Da): 33927
Sequence Length: 307
Pathway: Porphy... |
Q4K3X3 | MSSREIRIATRKSALALWQAEYVKARLQEAHPGLVVTLVPMVSRGDKLLDSPLSKIGGKGLFVKELETALLENQADIAVHSMKDVPMDFPEGLGLFCICEREDPRDAFVSNTYASLDELPEGSVVGTSSLRRQAQLLTRRPDLQIRFLRGNVNTRLAKLDAGEYDAIILAAAGLIRLGFEDRISSSISVDDSLPAGGQGAVGIECRSADIEIHALLAPLHHADTASRVTAERALNKHLNGGCQVPIACYAVLEGEQIWLRGLVGEPSGGLLLSAEARGPRASAAELGVQVADALLAQGADDILRAVYGEAGEE | Cofactor: Binds 1 dipyrromethane group covalently.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Mass (Da): 33422
Sequence Length: 313
Pathway: Porphy... |
Q8ZYW7 | MRLKVATRGSRLSLLQTEEFLAQIKAVEPRVDFEIKIVKTTGDLVQDKPLFQIGVKGIFEKEVNLAVLKGEADIAIHSLKDLPSEISPGLVLAGFSKRTLPYDAVVSAVGYDLESLPKGALVGTSSVRRAEFIKSLRPDVRIEPLRGNVDTRVQKILQGKYDAAVMAAAGILRLYGESPPVKLSLLRPELLPPPPGQGIVAAVVREGEGWLIDLLKKASDPRATVEALAEREFLKNVGAGCHVAVGGTAFSRNGYIEFIAGYAASGKRFVVKLFGEDPVEVGRRAAEEIKRVAASVR | Cofactor: Binds 1 dipyrromethane group covalently.
Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Mass (Da): 32075
Sequence Length: 297
Pathway: Porphy... |
Q9AAT8 | MSTDQDLDTKKAAARAWFESLRDQICAAFEQLEDEAPADLYPGAPGRFAKKAWDRPAGGGGVMGMMHGRLFEKVGVHVSTVFGTFTPEMAKTMPGAAEDPRFFATGISLIAHMTNPRVPAVHMNTRFIATTKSWFGGGGDLTPLLGYQRQQDFPDAIDFHAAYKRACDKYDPEWHPKYKAWCDEYFFLPHRNEPRGIGGIFYDHHDSGDWARDFAFTQDVGRAFLEIYPTLVRRRMGEAWTADEREQQLIQRGRYVEFNLLYDRGTMFGLKTGGNVESILSSMPPAVKWP | Function: Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX.
Catalytic Activity: coproporphyrinogen III + 2 H(+) + O2 = 2 CO2 + 2 H2O + protoporphyrinogen IX
Sequence Mass ... |
Q9PHC7 | MSDFDRVRDYLTALQDRICNVVETIDGQSHFHEDHWQRTEGGGGRTRLLRDGAVFEQAGIGFSDVCGTHLPPSASVRRPELAGANWRACGVSLVFHPKNPFVPTTHLNVRYFRAERDGKQVAAWFGGGFDLTPFYPFDEDVVHWHTVARDLCAPFGDERYAAHKRWCDEYFVLRHRNETRGVGGLFFDDLDKDFERDFAYQRAVGDGFLDAYFPIVTRRHDTPYGDRERAFQLYRRGRYVEFNLLFDRGTLFGLQSGGRAESILISLPPLVRWEYGYHPLPGSAEARLADYLLPRDWLNESRICE | Function: Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX.
Catalytic Activity: coproporphyrinogen III + 2 H(+) + O2 = 2 CO2 + 2 H2O + protoporphyrinogen IX
Sequence Mass ... |
P11353 | MPAPQDPRNLPIRQQMEALIRRKQAEITQGLESIDTVKFHADTWTRGNDGGGGTSMVIQDGTTFEKGGVNVSVVYGQLSPAAVSAMKADHKNLRLPEDPKTGLPVTDGVKFFACGLSMVIHPVNPHAPTTHLNYRYFETWNQDGTPQTWWFGGGADLTPSYLYEEDGQLFHQLHKDALDKHDTALYPRFKKWCDEYFYITHRKETRGIGGIFFDDYDERDPQEILKMVEDCFDAFLPSYLTIVKRRKDMPYTKEEQQWQAIRRGRYVEFNLIYDRGTQFGLRTPGSRVESILMSLPEHASWLYNHHPAPGSREAKLLEVT... | Function: Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX.
Catalytic Activity: coproporphyrinogen III + 2 H(+) + O2 = 2 CO2 + 2 H2O + protoporphyrinogen IX
Sequence Mass ... |
P31964 | MNFTVPVQAIQSIWSVGKESDDAIAEACKPPFCIYFSKKTPYTVTNGSNADHGDDEVRQMMRGLLYNSSCISAQGHTPLALYSTAMLYPPMYGSCPQYVKLFDGSGSESVDVISSSYFVATWVLLVVVIILVFIIISFCISN | PTM: N-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 15571
Sequence Length: 142
Subcellular Location: Virion membrane
|
P0C0V9 | MLSLILFFPSFAFAATPVTPYYGPGHITFDWCGFGDSRSDCTNPQSPMSLDIPQQLCPKFSSKSSSSMFLSLHWNNHSSFVSYDYFNCGVEKVFYEGVNFSPRKQYSCWDEGVDGWIELKTRFYTKLYQMATTSRCIKLIQLQAPSSLPTLQAGVCRTNKQLPDNPRLALLSDTVPTSVQFVLPGSSGTTICTKHLVPFCYLNHGCFTTGGSCLPFGVSYVSDSFYYGYYDATPQIGSTESHDYVCDYLFMEPGTYNASTVGKFLVYPTKSYCMDTMNITVPVQAVQSIWSEQYASDDAIGQACKAPYCIFYNKTTPYTV... | Function: Structural protein that makes short spikes at the surface of the virus. Contains receptor binding and receptor-destroying activities. Mediates de-O-acetylation of N-acetyl-9-di-O-acetylneuraminic acid, which is probably the receptor determinant recognized by the virus on the surface of erythrocytes and suscep... |
Q9Z7V1 | MTTPAYLLANFGGPRHAKDLQEFLISLLTDRDVTGTFLPRVLHRHLFTFIAKKRVPKVLPQYQSLQNWSPIYFDTETLAKTLSEILRAPVIPFHRYLPSTHEKTLLALRTLHTRHVIGIPLFPHFTYSVTGSIVRFFMKHVPEIPISWIPQFGSDSKFVSLITCHIRDFLQKLGILEKECCFLFSVHGLPVRYISQGDPYSKQCYESFSAITTNFKQSENFLCFQSKFGPGKWLSPSTAQLCQNIDTDKPNVIVVPFGFISDHLETLYEIERDYLPLLRSRGYRALRIPAIYSSPLWVSTLVDIVKENSTVVAEELIKSG... | Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
Sequence Mass (Da): 37503
Sequence Length: 327
Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
Subcellular Location: C... |
Q83FA4 | MAKQAIKRAKILAVKNNNKIGVLLINLGTPDEPSVPAVRRYLRQFLSDPKVIDVPSLVRWIIVHLCILPFRPKRSAKLYQKIWMPEGSPLLVYSEMLRERVGETLGDDFCVALGMRYGKPSIETALKKLQEAQCRQLIVLPLFPQYSTSTTASALEEVRAKNSFKEMTVIDRFFEEPHYIDSMTTLIHENLNEFQPDYFLFSYHGLPERHLVKSGCQLAICNRKNNCSPISSSNENCYRAQCFETSRLIAKKLNLTDQQYGVAFQSRLGRAKWIEPYTDKYLIELSKKGIKKLMVVCPSFPVDCLETLEEIGIRAQSQWQ... | Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
Sequence Mass (Da): 40554
Sequence Length: 354
Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
Subcellular Location: C... |
A7MNM8 | MQSVKSGVLLVNLGTPQAPTPAAVKRYLKQFLSDRRVVDVPRFIWWPLLRGVILPLRSPRVAKLYKSIWMEEGSPLMVYSRRQEKALSAALGDVPVALGMSYGQPSLDSAVQKLLDQHVDHIIVLALYPQYSCSTVAAVWDELARITARYRKLPSMTLIRDYACEPAYISALAQSVQRSFEKHGEPDLLLLSYHGIPQRYADEGDDYPQRCRDTTRELVSALGIAPEKVMMTFQSRFGREPWLTPYTDETMKMLGEKGVKHIQVMCPGFSSDCLETLEEIAEQNREIFIEAGGEKYEYIPALNDEPAHIAMMKELVDRYR | Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
Sequence Mass (Da): 36343
Sequence Length: 320
Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
Subcellular Location: C... |
Q9RV98 | MTTLTNQKPLGVLFMAYGGPENLGEMPGYLADIRAGRVTSQAILDEITNNYRLIGGKSPLPEFTRAQVEATMEQLASTGRPLKAYIGMRHWSPWIEDAVREMLDDGIEQAIAIVLAPQYSSLSVAKYQKKIKAALEMNHGHIDFAYIDNYHTEPGYITALADRVRIGIQEFPEDERDDVHVILSAHSLPVRIIKEGDPYADQLHETARLVAAQAGLTDEQWSWSYQSAGRSPEPWLGPQLDEHLRDLNEQGIKKVVSIAIGFVSDHVEILFDIDIAAQEVAHELGMTLVRPPALNTDPLFIGTLASVIERKAAEVA | Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
Sequence Mass (Da): 35019
Sequence Length: 316
Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
Subcellular Location: C... |
Q888A2 | MTDHALLLVNLGSPASTQVADVRSYLNQFLMDPYVIDIPWPLRRLLVSLILIKRPEQSAHAYASIWWDEGSPLVVLSKRLQQAMKKEWSHGPVELAMRYGEPSIETVLTRLSEQGFKKVTLAPLYPQFADSTVTTVIEEAKRVVRAKSLKMQFSVLQPFYDQPEYVSALVESVRPHLEQPYDHLLLSFHGLPERHLHKRDPTGKHCLKDDCCMTAPAQVVATCYRAQCLQSAAAFAKRMGIPDGKWSVSFQSRLGRAKWIEPYTEARLDELAAQGVKKLLVMCPAFVADCIETLEEIGDRGAEQFKEAGGEELILVPCLN... | Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
Sequence Mass (Da): 38398
Sequence Length: 340
Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
Subcellular Location: C... |
Q7UFZ7 | MSELPPYDSFLLVSFGGPEGQDDVMPFLENVLRGKNVPRERMLEVAEHYKHFGGVSPINEQNRQLIAALQKRFDANGIDLPIYWGNRNWDPYFADTLRQMKADGKKRSLAFFTSMFSCYSGCRQYRENIIQAREEVGEGAPLVEKVRMGFNHPGFIAAMADNVSKAAQTIGASPARTKVLFTAHSIPMGMADNCDYEKQLRESCRLVADACGAVDWDLVYQSRSGPPSQPWLEPDVLDAIAEMDDAKKLESLVILPIGFVSDHMEVLFDLDEEAAQLCRERGIKMARASAAGTHPDFVEMICGLVQERLGKLNEKPALGE... | Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
Sequence Mass (Da): 39081
Sequence Length: 351
Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
Subcellular Location: C... |
Q59735 | MTIANRILPHAPADHPPVPVPRVGVLLANLGTPDATDYWSMRRYLNEFLSDRRVIDYPIWKWQPLLQLIILSKRPFTSGNNYRSIWNEERDESPLMTITRDQVRKLRAAVETRYGAGNVVVDFCMRYGNPSTRDVLDDMLAQGCERILFLPLYPQYAGATSATANDQFFRALMQVKRQPAARTVPEYFARPSYIEALASSVERVYATLDTRPDVLVASYHGMPKRYHREGDPYHCQCQKTSRLLRERLGWGPDSIDTTFQSVFGTEEWLRPYTVEHVVQLAEAGKKNIAVISPAFSADCIETLEEINGEIREAFEHAGGE... | Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
Sequence Mass (Da): 39955
Sequence Length: 351
Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
Subcellular Location: C... |
P0ACB9 | MLKVLLLFVLLIAGIVVGPMIAGHQGYVLIQTDNYNIETSVTGLAIILILAMVVLFAIEWLLRRIFRTGAHTRGWFVGRKRRRARKQTEQALLKLAEGDYQQVEKLMAKNADHAEQPVVNYLLAAEAAQQRGDEARANQHLERAAELAGNDTIPVEITRVRLQLARNENHAARHGVDKLLEVTPRHPEVLRLAEQAYIRTGAWSSLLDIIPSMAKAHVGDEEHRAMLEQQAWIGLMDQARADNGSEGLRNWWKNQSRKTRHQVALQVAMAEHLIECDDHDTAQQIIIDGLKRQYDDRLLLPIPRLKTNNPEQLEKVLRQQ... | Function: Involved in a late step of protoheme IX synthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45245
Sequence Length: 398
Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis.
Subcellular Location: Cell inner membrane
|
P44772 | MFRVLFLMLTLLVGLVAGPYISGQQGYVRIETANRIIEMSITTLVIFFIISLAIIYAFEWGVTRFFRLSRSSYQWFSNRKRVKAQKQTLEGLVKMDEGDYAKAEKLIGKNAKHSAEPVLNLIKAAEAAQQRGDEFSANRYLIEATELAGSDNLLVEIARTRILLQQNKLPAARSSVDSLLEMARRNKEVLKLAVEIYLRSKAYQALDKILDNVANSGLFNDEEFKDLRSKTENGLLDEKMNEEGIDGLLTWWNQQPRHRRNNIELKISLIQRLIDCNDHESATELTFEILKKLGDNTAISLPLCTQITRLQPEDNSKLLK... | Function: Involved in a late step of protoheme IX synthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48776
Sequence Length: 428
Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis.
Subcellular Location: Cell inner membrane
|
Q796V8 | MQIKIEGIHDDRLHRPLQNIANLFYEECELAYGGEEPADFVISLALSQTDEHVTVSGEVKGTGIKEQHTKFFSPDMTEKEAFKQVKNTISYVYLNLLQAHTGITQKWGILTGIRPTKLLHKKLQSGMSKEQAHAELKKDYLIHDEKIMLMQEIVDRQLAAVPDLYRVKDEVSIYIGIPFCPTKCAYCTFPAYAIQGQAGRVGSFLWGLHYEMQKIGEWLKEHDVKVTTIYFGGGTPTSITAEEMDLLYEEMVRSFPDVKNIREITVEAGRPDTITEEKLAVLNKYDIDRISINPQSYENETLKAIGRHHTVEETIEKYHL... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Involved in the biosynthesis of porphyrin-containing compound.
Sequence Mass (Da): 57527
Sequence Length: 501
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosyn... |
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