ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q27490 | MARTKHTARKSFGGKAPRKSLATKAARKVFPVDGQVKKRYRPSSNALKEIRKYQKSTELLVRKLPFQRLVREVAQEIMPNVRFQSAAIQALHEAAEAYLIGLFEDTNLCAIHAKRVTIMPKDMQLARRIRGERG | Function: Putative variant histone H3 which may replace conventional H3 in a subset of nucleosomes. 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 r... |
Q27532 | MARTKQTARKSTGGKAPRKALATKAARKSAIVTGSVKKVHRFRPGTVALREIRRYQKSTELLLRKLPFQRLVREIAQDFKTDLRFQSAAIGALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDMQLARRIRGERS | Function: Putative variant histone H3 which may replace conventional H3 in a subset of nucleosomes. 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 r... |
Q27489 | MCPGGKAPRKQLATKAARKNAIVVGAVKKPHRFRPGTVALREIRRYQKSTDLLLRKLPFQRLVREIAQDVKQDLRFQSAAIQALQEASEYFLVGLFEDTNLCAIHAKRVTIMPKDMQLARRIRGERN | Function: Putative variant histone H3 which may replace conventional H3 in a subset of nucleosomes. 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 r... |
P59169 | MARTKQTARKSTGGKAPRKQLATKAARKSAPTTGGVKKPHRYRPGTVALREIRKYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSHAVLALQEAAEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA | Function: Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes. Constitutes the predominant form of histone H3 in non-dividing cells and is incorporated into chromatin independently of DNA synthesis. Deposited at sites of nucleosomal displacement throughout transcribed genes,... |
Q8J1L3 | MSGRGKGGKGLGKGGAKRHRKILRDNIQGITKPAIRRLARRGGVKRISALIYEETRSVLKTFLESVIRDAVTYTEHAKRKTVTSLDVVYALKRQGRTLYGFGG | 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... |
P84040 | MTGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG | 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... |
Q89443 | MGKPTLLEPGHLYNVPAEHKNDVPIHYIITWIKQRLPEFGGAIPTSLADRVLIIKSRTGSGKSTALPVHVFRILRNENTHSFQKYLGRSVICTQPRVLTAVTLAKDIGASTHYPDMILGQTVGYHTKPLTEKPNRGLIYATAGVLLAQLHTMTDDEIASRYAFMIIDEAHERALGIDLMLMYIKSMLQRMLQRGSIGALRIPFVILTSATIDTHKYSTYFGIGKENIILVEGRQYGVETHWPLYNTNNYIKTACETALTIHKENIHDRPTEADILIFMPGMAEIRFLSMLLNNANMDLAKEKLPLMLILPIDSEAIAQEN... | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 109630
Sequence Length: 962
Subcellular Location: Host membrane
EC: 3.6.4.13
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P83716 | MKEDNNTSEESGRINRRNVLKTVGAAGLFAAGSTGMAAAADSLSQAEEPKLLTGTEKRTLARELAKTPAFRELAQRARADGAQIRSDADSIVAGYARGEDFAREVVQYDLENLTDAAEASIVIGRNPETGEIEVANLDYYYETDDGVLDEVHRFEPTNASETDGVQSAATSDGATVIAVDTDAIREAQNSEIDVDESSPSNAAPTPADIDITGCSACKYAAGQVCTIGCSAAGGFICGLLGITIPVAGLSCLGFVEIVCTVADEYSGCGDAVAKEACNRAGLC | Function: Has antibacterial activity against a wide variety of haloarchaeons. Causes cell lysis and death, possibly by disrupting the cell wall .
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Sequence Mass (Da): 29379
Sequence Length: 28... |
Q8TLF1 | MLFDYRKGGLFLGTISEKIFSRAAGTEAKANDFVLADVDYAMAHDGTSVLAVNAFKEMEMEKVWDPSRIVVPFDHIAPANNETSATLQREIREWVKEQGIPNFYEVGEGICHQVLPENGFALPGKLVVGADSHSCTYGAFGAFATGVGATDMAEIFATGKLWFKVPESFRMTVEGSLRKGVYAKDLTLYLIGKTGIAGATYKAVEFYGQAIRELTVAGRMTLCNMAIEMGAKTGIVPPDEKTFEFLKNRAAATYEPVYADPDAVYLEEFTYDADDIEPQVACPHQVDNVKPVGEVEGTHVDQVFIGTCTNGRLEDLEVAA... | Function: Component of a hydro-lyase with broad substrate specificity for cis-unsaturated tricarboxylic acids. Catalyzes both the reversible dehydration of (R)-homocitrate ((R)-2-hydroxybutane-1,2,4-tricarboxylate) to produce cis-homoaconitate ((Z)-but-1-ene-1,2,4-tricarboxylate), and its hydration to homoisocitrate ((... |
Q58409 | MTLVEKILSKKVGYEVCAGDSIEVEVDLAMTHDGTTPLAYKALKEMSDSVWNPDKIVVAFDHNVPPNTVKAAEMQKLALEFVKRFGIKNFHKGGEGICHQILAENYVLPNMFVAGGDSHTCTHGAFGAFATGFGATDMAYIYATGETWIKVPKTIRVDIVGKNENVSAKDIVLRVCKEIGRRGATYMAIEYGGEVVKNMDMDGRLTLCNMAIEMGGKTGVIEADEITYDYLKKERGLSDEDIAKLKKERITVNRDEANYYKEIEIDITDMEEQVAVPHHPDNVKPISDVEGTEINQVFIGSCTNGRLSDLREAAKYLKGR... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Component of a hydro-lyase with broad substrate specificity for cis-unsaturated tricarboxylic acids. Catalyzes both the reversible dehydration of (R)-homocitrate ((R)-2-hydroxybutane-1,2,4-tricarboxylate) to produce cis-homoaconitate ((Z)-but-1-ene-1,2,4-tricarb... |
Q9ZNE0 | MGQTLAEKILSHKVGRPVRAGELVVVEVDQVMVVDSIAGSFFKRLEYLEATPRYPERVSIVIDHVAPAANLEVAKAQKEIREWGKRHGIRVFDVGRGVCHQVLIEEGLAQPGWVVVGSDSHSTTYGAVGAFGTGMGATDIALAAASGRTWLRVPESVKVVFRGRLPKGVTAKDAALEMVRLLTAEGATYMAVEIHLLDGAEALTRGERMTLANLTVEAGAKAGLVVPSGEILEMYRVPDWLYPDPDARYAKEVEIDLSALTPRVSVPFYVDNVHEVAQVKGKRVDQVFIGTCTNGRIEDLRAAAEVLRGRKVAPWVRLLV... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the reversible hydration of cis-homoaconitate ((Z)-but-1-ene-1,2,4-tricarboxylate) to homoisocitrate ((1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate). Can catalyze neither the dehydration of (R)-homocitrate ((2R)-2-hydroxybutane-1,2,4-tricarboxylate) int... |
Q8TRF7 | MANPIVGRVWKFGDDINTDAIIPGKYLRTRDMQIFGTHAMEGIDPEFTKKAKPGDIIVAGTNFGCGSSREQAPLALKHSGIACIVAKSFARIFFRNAINIGLPLMEADVECQEGDEIKVDLFKGEVLVPEKGIFKGNKLPDFLLDILNDGGLVAHRKKVKGEHK | Function: Component of a hydro-lyase with broad substrate specificity for cis-unsaturated tricarboxylic acids. Catalyzes both the reversible dehydration of (R)-homocitrate ((R)-2-hydroxybutane-1,2,4-tricarboxylate) to produce cis-homoaconitate ((Z)-but-1-ene-1,2,4-tricarboxylate), and its hydration to homoisocitrate ((... |
Q58667 | MIIKGRAHKFGDDVDTDAIIPGPYLRTTDPYELASHCMAGIDENFPKKVKEGDVIVAGENFGCGSSREQAVIAIKYCGIKAVIAKSFARIFYRNAINVGLIPIIANTDEIKDGDIVEIDLDKEEIVITNKNKTIKCETPKGLEREILAAGGLVNYLKKRKLIQSKKGVKT | Function: Component of a hydro-lyase with broad substrate specificity for cis-unsaturated tricarboxylic acids. Catalyzes both the reversible dehydration of (R)-homocitrate ((R)-2-hydroxybutane-1,2,4-tricarboxylate) to produce cis-homoaconitate ((Z)-but-1-ene-1,2,4-tricarboxylate), and its hydration to homoisocitrate ((... |
O26917 | MEGIIRGRVWRFGDNVDTDMIIPGRYLRTFSLDELASHVMEGARPEFASQVRKGDIIVAGRNFGCGSSREQAPVALKHAGVVAIIAESFARIFYRNAINIGLPVIMAKVDADDGDEVSIDLRSGQIRNLTAGSEYRMKPFNDYMLSILEDGGLVNHYLKTIDTGISGDEG | Function: Component of a hydro-lyase with broad substrate specificity for cis-unsaturated tricarboxylic acids. Catalyzes both the reversible dehydration of (R)-homocitrate ((R)-2-hydroxybutane-1,2,4-tricarboxylate) to produce cis-homoaconitate ((Z)-but-1-ene-1,2,4-tricarboxylate), and its hydration to homoisocitrate ((... |
Q9ZND9 | MPRVWKFGDQINTDDILPGKYAPFMVGEDRFHLYAFAHLRPEFAKEVRPGDILVFGRNAGLGSSREYAPEALKRLGVRAIIAKSYARIFFRNLVNLGIVPFESEEVVDALEDGDEVELDLESGVLTRGEERFALRPPPPFLLEALKEGSLLDYYKKHGRFPGE | Function: Catalyzes the reversible hydration of cis-homoaconitate ((Z)-but-1-ene-1,2,4-tricarboxylate) to homoisocitrate ((1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate). Can catalyze neither the dehydration of (R)-homocitrate ((2R)-2-hydroxybutane-1,2,4-tricarboxylate) into cis-homoaconitate in vitro, nor the reverse re... |
Q4W1W1 | MASSEEDGTNGGASEAGEEKEAPGRRRRLGLLATVWLTFYNIAMTAGWLVLAIAMVRFYMEKGTHKGLYKSIQKTLKFFQTFALLEIVHCLIGIVPTSVIVAGVQVSSRIFMVWLITHSIKPIQNEESVVLFLVAWTVTEITRYSFYTFSLLDHLPYFIKWARYNFFIILYPVGVVGELLTIYAALPYVKKTGMFSIRLPNKYNVSFDYYYFLLITMASYIPLFPQLYFHMLRQRRKVLHGEVIVEKDD | 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... |
B0YJ81 | MGRLTEAAAAGSGSRAAGWAGSPPTLLPLSPTSPRCAATMASSDEDGTNGGASEAGEDREAPGERRRLGVLATAWLTFYDIAMTAGWLVLAIAMVRFYMEKGTHRGLYKSIQKTLKFFQTFALLEIVHCLIGIVPTSVIVTGVQVSSRIFMVWLITHSIKPIQNEESVVLFLVAWTVTEITRYSFYTFSLLDHLPYFIKWARYNFFIILYPVGVAGELLTIYAALPHVKKTGMFSIRLPNKYNVSFDYYYFLLITMASYIPLFPQLYFHMLRQRRKVLHGEVIVEKDD | 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... |
Q8TF76 | MAASLPGPGSRLFRTYGAADGRRQRRPGREAAQWFPPQDRRRFFNSSGSSDASIGDPSQSDDPDDPDDPDFPGSPVRRRRRRPGGRVPKDRPSLTVTPKRWKLRARPSLTVTPRRLGLRARPPQKCSTPCGPLRLPPFPSRDSGRLSPDLSVCGQPRDGDELGISASLFSSLASPCPGSPTPRDSVISIGTSACLVAASAVPSGLHLPEVSLDRASLPCSQEEATGGAKDTRMVHQTRASLRSVLFGLMNSGTPEDSEFRADGKNMRESCCKRKLVVGNGPEGPGLSSTGKRRATGQDSCQERGLQEAVRREHQEASVPK... | Function: Serine/threonine-protein kinase that phosphorylates histone H3 at 'Thr-3' (H3T3ph) during mitosis. May act through H3T3ph to both position and modulate activation of AURKB and other components of the chromosomal passenger complex (CPC) at centromeres to ensure proper chromatid cohesion, metaphase alignment an... |
O13924 | MESRSKVKTYGKNRRYINKDIEIWASLDERPCALKPRNIENFNNQERSDLEHIHSKPKKDSLLSWNILLKKGSYKENELLAKRNQNLVPTVIIPASPRDNASKSVVSKKEVVNLSSSVALSGKPANNSKLDPLHRLLQIVAQEDALPFSQFVKSQTFEIQKIGEASYSEVYQASNADDVPVVWKVIPFGEDGQAQYADVLNEVQISQWIKVDGFANLHQVVVVKGTYPSLLLEEWDRYLMQNGSENDRPDSYSSTQLYCVLCLDHSGTDLEHFELRSWRECWSVFYETLKILSLVETRYEFEHRDLHWGNILIRKADRSE... | Function: Serine/threonine haspin-like protein kinase involved in cell cycle regulation. Acts in chromosomal passenger complex (CPC) targeting to centromeres by phosphorylating histone H3 at 'Thr3' (H3T3ph).
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 56521... |
Q9Z4Z7 | MKTESDVQTGAPTAADGALIALAREVCPGFAPGEVVYRSRTSLVVGGELDGVEALAKVRTPDWRRQCLREIDTYDLFDAVPPPVPVPRRFASDRERAVLVMERLTGEVLAPDRFPVTPVSREDLAGVLEAVERLRHWRPAAAGAWAVDYRGMLEGVHAQGVFDDGHWADLLRLLELSGAPREFGHGDLVLANVVRSRGRQVLIDWASSALYLPGLDLAQLWMLLGDVPGARARIEVEVADRADDRDGMMPFLVNLTLLLYRERRAHRRFTDDASRARAVGLDAAWELTRHRVRQCLATAG | Function: Phosphotransferase that is responsible for the production of the 3-phosphohydroxyasparaginyl residues found at position 9 in the non-ribosomally synthesized calcium-dependent antibiotic (CDA) derivatives CDA1b and CDA2a/b. It is not known whether the phosphorylation reaction takes place before, during or afte... |
Q7BLV3 | MNTLSQAIKAYNSNDYQLALKLFEKSAEIYGRKIVEFQITKCKEKLSAHPSVNSAHLSVNKEEKVNVCDSPLDIATQLLLSNVKKLVLSDSEKNTLKNKWKLLTEKKSENAEVRAVALVPKDFPKDLVLAPLPDHVNDFTWYKKRKKRLGIKPEHQHVGLSIIVTTFNRPAILSITLACLVNQKTHYPFEVIVTDDGSQEDLSPIIRQYENKLDIRYVRQKDNGFQASAARNMGLRLAKYDFIGLLDCDMAPNPLWVHSYVAELLEDDDLTIIGPRKYIDTQHIDPKDFLNNASLLESLPEVKTNNSVAAKGEGTVSLDW... | Function: Catalyzes the polymerization of hyaluronan, a polysaccharide composed of a repeating disaccharide of N-acetylglucosamine (GlcNAc) and glucuronic acid (GlcUA) units. Each unit has the composition in beta-(1->4)-GlcUA-beta-(1->3)-GlcNAc.
Catalytic Activity: [hyaluronan](n) + UDP-N-acetyl-alpha-D-glucosamine = H... |
Q4X0W8 | MALILERLYLLSSPRNAIIRNTRSEAGRELIFSFGLPSLSLPSCIASQYGKRRRLYFTTQLHVNSFLHWTCDANDAVNITLVQPDEQKLKTVSSFHPQFTYPIFGDDERIFGYKGLIIRLRFAAHDLRPQLHISYDEKFKPVEDIAAVDIPKTLKPWIPEDAFVTLPDYEKAVLEDKAAKDFKPPGKLVHCYVSRNRNFEIWAGSLADPEVRRLLDRAQIFVSLFIEAGTPLATDDPEWTLQRWTVYFVYEIVKPPTPTASKYSIVGYATTYRWWHYRRDRTQVPVVKNDPFPSGPEIHPSQLPSRLRIAQFLILPPHQN... | Function: Catalytic component of the histone acetylase B (HAT-B) complex. Acetylates 'Lys-12' of histone H4 which is required for telomeric silencing. Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. Involved in DNA double-strand break repair.
Catalytic Activity: acetyl-CoA + L-l... |
Q2UEX1 | MASEGDWTCDANDAVQITLVQPGEQKPKTLSSFHPQFTYPIFGDDETIFGYKGLIIRLRFAAHDLRPHIHISYDEKFKTVGDTSAVDLIKTLSPFIPEEAFSTLPDYENAVQEDKDAKDFVPPGKLVHNYVTRGRTYEIWAASLADPQVRRLLDRAQVFVSLFIEAGTPLETEDPEWTLERWTVYFVYEKVKPPTPTASQYSIVGYATTYRWWFYQRDSPEKGTVTNDPFPGPEIRPAQLPARLRIAQFLILPPHQGSGHGTHLYTTIHTACFNDSTIVELTVEDPNEAFDALRDTADFHILRPEFLKHNVNINPDPYAE... | Function: Catalytic component of the histone acetylase B (HAT-B) complex. Acetylates 'Lys-12' of histone H4 which is required for telomeric silencing. Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. Involved in DNA double-strand break repair.
Catalytic Activity: acetyl-CoA + L-l... |
Q59VF4 | MSSAKEQSSVTAALQPEQWTTSSNEALKLFVTNPEAALNFQPTFTYPIFGDAETIYGYKDLDIFLCFDHYTFKPFLNIKYSAKLTDDPEIIDIKKTIDEFLPKSTIFKDEVKWVDSIKEEKDNGYKIPGKLIDSFSENDKEYDIYKIDLKSDNGYELHQRLQILVLLFIEAGSFIDAKDELWNLYVLYEKDNKSTSNNEPSIVGFTTAYNYWKYPGAKKFDSTEQESRIKISQFIILPIYQGQGLGQLFYSHLFDKWLAQDDIIEVVVEDPNESFDDLRDRADLKRLNTSEQFDFKAVTPKVDKEWVEKTRRALKLEKRQ... | Function: Catalytic component of the histone acetylase B (HAT-B) complex. Acetylates 'Lys-14' of histone H4 which is required for telomeric silencing. Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. Involved in DNA double-strand break repair.
Catalytic Activity: acetyl-CoA + L-l... |
Q6FKS5 | MSIDDFKPEKWTISSNEALKLSLVSEDNAIQFSPTFTYPIFGTEEQIFGYKDLVIHLAFDAITFKPFLNVKFSSKFEGSEEELVNIKEKLLEYLPIDDTIYKDEEKWIDSFKKEQESIEAYKNDQNIDEYKIDNADFEIYKVNLQDPKMKRFHRRIQIFSLLFIEAASYIDEDDPKWEIFIVQTKKDKKFVGYATAYNYWYYPGANNFDSESKYRYRGKISQFLILPPYQGRGHGSHLYNSIVKNWRNDSSILEIVVEDPNESFDDLRDVNDLEMLYKDGFFNKLPQERPIPNAWIESTRLKYKIEKRQFSRLLEMILLS... | Function: Catalytic component of the histone acetylase B (HAT-B) complex. Acetylates 'Lys-12' of histone H4 which is required for telomeric silencing. Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. Involved in DNA double-strand break repair.
Catalytic Activity: acetyl-CoA + L-l... |
P0CO07 | MAETLEEWISDSNQVLNLQMVRTPEDASLLQYEEQQNIDVFNPAFTYPIFGDNEKIFGYKGLDIKLHFASGSLRQYLDISYDAKLASSTTPPDEIEGALYKFIPPDYTKSEVEFQKRVAGDAETFKPLGEKIGSYAHPSAGRKGKGQGDSGMAAGKAIEDNEDVVEYEMYKATWSTPGFREYHRRMQIFVLLFIEGGSYVHEDEDAWEFIVLYERRTRPDSGIFTYHFVGYVSVYPFWCYPDRVRLRLSQFVILPPYQHQGHGSKLYNMLFRHMLDRSEVAELTIEDPAEAFEDLRDRNDLRFLVKEGIVKDPMLYVDVG... | Function: Catalytic component of the histone acetylase B (HAT-B) complex. Acetylates 'Lys-12' of histone H4 which is required for telomeric silencing. Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. Involved in DNA double-strand break repair.
Catalytic Activity: acetyl-CoA + L-l... |
Q81105 | MQLFHLCLIISCTCPTFQASKLCLGWLWGMDIDPYKEFGATVELLSFLPSDFFPSVRDLXDTASALYREALESPEHCSPHHTALRQAILCWGKLMTLATWVGNNLEDPASRDLVVNYVNTNMGLKIRQLLWFHISCLTFGRETVLEYLVSFGVWIRTPPAYRPPNAPILSTLPETTVVRRRDRGRSPRRRTPSPRRRRSQSPRRRRSQSRESQC | Function: May regulate immune response to the intracellular capsid in acting as a T-cell tolerogen, by having an immunoregulatory effect which prevents destruction of infected cells by cytotoxic T-cells. This immune regulation may predispose to chronicity during perinatal infections and prevent severe liver injury duri... |
P0C6G7 | MQLFHLCLIISCSCPTVQASKLCLGWLWGMDIDPYKEFGASVELLSFLPSDFFPSIRDLLDTASALYREALESPEHCSPHHTALRQAILCWGELMNLATWVGSNLEDPASRELVVSYVNVNMGLKIRQLLWFHISCLTFGRETVLEYLVSFGVWIRTPPAYRPPNAPILSTLPETTVVRRRGRSPRRRTPSPRRRRSQSPRRRRSQSRESQC | Function: May regulate immune response to the intracellular capsid in acting as a T-cell tolerogen, by having an immunoregulatory effect which prevents destruction of infected cells by cytotoxic T-cells. This immune regulation may predispose to chronicity during perinatal infections and prevent severe liver injury duri... |
Q62I60 | MTAIRGGSRRAPGLALALLGGVLLGACHGDENAQVNALPGFVSGSVRKTAYDGASDDLLTAGLGKTGLGSDTRPGFANPAQPSAAELRRLAIYSNYRALVDITPNGGYGRFWGPNVDLAGNDTLGEGKIAGTEYLAYSDDGSGRKNVTLLVQVPASFDPANPCIVTATASGSRGVYGAIAAAGEWGLKRGCAVAYNDKGGGNGAHEIGTGVVTLIDGTLATASSAGSSSLFTASESSSTLAAFNSAFPNRYAYKHAHSQQNPEQDWGRVTLQAVEFAYWALNEQFGPVVDGTRHGIRYRPGDITTIAASVSNGGGSALAA... | Function: Participates in the degradation of poly-3-hydroxybutyrate (PHB). It works downstream of poly(3-hydroxybutyrate) depolymerase, hydrolyzing D(-)-3-hydroxybutyrate oligomers of various length (3HB-oligomers) into 3HB-monomers.
Catalytic Activity: (3R)-hydroxybutanoate dimer + H2O = 2 (R)-3-hydroxybutanoate + H(+... |
Q0K9H3 | MHSTQIPPQQKQKRRLRLTVLAAAASMLAAACVSGDDNNNGNGSNPNTKPANIGTVTINSYNGTTDDLLTAGLGKDGLASATAPLPANPTAPTAAELRRYAIHTNYRAIVDTTASGGYGSLYGPNVDAQGNVTGSDGKVAGVEYLAFSDDGSGQQNVTMLVQIPASFNTSKPCMITATSSGSRGVYGAIATGEWGLKRGCAVAYTDKGTGAAPHDLDTDTVPLIDGTRATRAAAGKNAQFAAPAGATSLADFTAANPHRLAFKHAHSQRNPEKDWGKFTLQAVEFAIWAINDRFGAVSANGTRQRTLDKDRIVVIASSVS... | Function: Participates in the degradation of poly-3-hydroxybutyrate (PHB). It works downstream of poly(3-hydroxybutyrate) depolymerase, hydrolyzing D(-)-3-hydroxybutyrate oligomers of various length (3HB-oligomers) into 3HB-monomers. Seems to have also poly(3-hydroxybutyrate) depolymerase activity since it is able to r... |
A1TWS1 | MKRMMLCTLIGAATVTLTACKKDEVFNSLPDFLVSDVRQFDYDGNTDDLLTAGLGPEGLASATPPAFVDALNPTPAELRRLAIYNNYRALVDTAPGGGYGSLFGPAVGNASGRIPGQEFIAMMQVPGATVPVTVMAQVPDSFDPDFPCMVTAPSSGSRGIYGAIGTAGEWGLKKGCAVVYTDKGTGTGAHNLATNTAQSVNGTLTMEPEEALFRADLDAQSRDDFNSQWPDRFAWKHAHSKQNPEADWGRHVLQSIEFGFYMLNTLHGRELGNGETLRTINPRNTLVIASSVSNGGGASVRAAEQDEKGLIDGVAVSEPN... | Function: Participates in the degradation of poly-3-hydroxybutyrate (PHB). It works downstream of poly(3-hydroxybutyrate) depolymerase, hydrolyzing D(-)-3-hydroxybutyrate oligomers of various length (3HB-oligomers) into 3HB-monomers.
Catalytic Activity: (3R)-hydroxybutanoate dimer + H2O = 2 (R)-3-hydroxybutanoate + H(+... |
A1VUF3 | MTIIIAGKNTLTLTSLAAAVLALGACGGNSDPFESKNTKPAYLGAVAIASYDGASDDLLTAGLGKTGLGGTAPAVADPLKPTPAELRRLAIFNNYRAILDISTNGGYGTLYGPNVDAKGVITTGEGKIAGTEYIAYSDDGTGRQNITMMVQVPASFNPANACIVTGTSSGSRGVYGAIGSAGEWGLKNGCAVAYTDKGTGTGIHDLQNNTVNVQNGVRTDAAAAGKNSIFTAELSASERAAFNAATPNRFAVKHAHSQQNPEKDWGKWTLQSVEFAYFVLNEKYGDLARDGATHLKKLTPSNTIVIASSVSNGAGAALAA... | Function: Participates in the degradation of poly-3-hydroxybutyrate (PHB). It works downstream of poly(3-hydroxybutyrate) depolymerase, hydrolyzing D(-)-3-hydroxybutyrate oligomers of various length (3HB-oligomers) into 3HB-monomers.
Catalytic Activity: (3R)-hydroxybutanoate dimer + H2O = 2 (R)-3-hydroxybutanoate + H(+... |
Q7N4V5 | MRNQTFIIVGAGQAGAMAAATLRQQQFDGDIILIGKEYHAPYERPILSKDYLINPEEAPKYLFSEDFYLEKQIDLRIGQLVSQIMPSKHCVVLENGGKLRYDKLLLTMGARARRFPLLDQLGENIYTLRTLDDAQRLRQAVKKDKRILIVGGGVIGLELAATSCELGANVTVIEQADNIMGRCAPPLLQDYLLNRHQEKGVQFFLDTNIVSAQKQGSELVLILNTGEKVIGDIIIYGIGAEFRDQLAADAGLVTDGGIVIDSRCQTSEPDIFAAGDVCLQREPLTGDLQRRETWENANRQATIAAHAMMGLAPPQPGAPW... | Function: Part of the multicomponent 3-phenylpropionate dioxygenase, that converts 3-phenylpropionic acid (PP) and cinnamic acid (CI) into 3-phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid-dihydrodiol (CI-dihydrodiol), respectively.
Catalytic Activity: H(+) + NAD(+) + 2 reduced [2Fe-2S]-[ferredoxin] = N... |
P0ABR6 | MTTPSDLNIYQLIDTQNGRVTPRIYTDPDIYQLELERIFGRCWLFLAHESQIPKPGDFFNTYMGEDAVVVVRQKDGSIKAFLNQCRHRAMRVSYADCGNTRAFTCPYHGWSYGINGELIDVPLEPRAYPQGLCKSHWGLNEVPCVESYKGLIFGNWDTSAPGLRDYLGDIAWYLDGMLDRREGGTEIVGGVQKWVINCNWKFPAEQFASDQYHALFSHASAVQVLGAKDDGSDKRLGDGQTARPVWETAKDALQFGQDGHGSGFFFTEKPDANVWVDGAVSSYYRETYAEAEQRLGEVRALRLAGHNNIFPTLSWLNGTA... | Cofactor: Binds 1 Fe cation.
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 (By similarity).
Catalytic Activity: 3-phenylpro... |
Q01770 | MSNAMFCYQCQETVGNKGCTQVGVCGKKPETAALQDALIYVTKGLGQIATRLRAEGKAVDHRIDRLVTGNLFATITNANFDDDILAERVRMTCAAKKELAASLTDKSGLSDAALWEASEKSAMLAKAGTVGVMATTDDDVRSLRWLITFGLKGMAAYAKHADVLGKHENSLDAFMQEALAKTLDDSLSVADLVALTLETGKFGVSAMALLDAANTGTYGHPEITKVNIGVGSNPGILISGHDLRDLEMLLKQTEGTGVDVYTHSEMLPAHYYPAFKKYAHFKGNYGNAWWKQKEEFESFNGPVLLTTNCLVPPKDSYKDR... | Cofactor: Binds 1 spin-admixed [4Fe-4S] cluster.
Function: Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O.
Catalytic Activity: A + H2O + NH4(+) = AH2 + H(+) + hydroxylamine
Sequence Mass (Da): 58659
Sequence Length: 545
Subcellular Location: Cytoplasm
EC: 1.7.99.1
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P31101 | MFCFQCQETAKNTGCTVKGMCGKPEETANLQDLLIFVLRGIAIYGEKLKELGQPDRSNDDFVLQGLFATITNANWDDARFEAMISEGLARRDKLRNAFLAVYKAKNGKDFSEPLPEAATWTGDSTAFAEKAKSVGILATENEDVRSLRELLIIGLKGVAAYAEHAAVLGFRKTEIDEFMLEALASTTKDLSVDEMVALVMKAGGMAVTTMALLDEANTTTYGNPEITQVNIGVGKNPGILISGHDLKDMAELLKQTEGTGVDVYTHGEMLPANYYPAFKKYPHFVGNYGGSWWQQNPEFESFNGPILLTTNCLVPLKKEN... | Cofactor: Binds 1 spin-admixed [4Fe-4S] cluster.
Function: Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O.
Catalytic Activity: A + H2O + NH4(+) = AH2 + H(+) + hydroxylamine
Sequence Mass (Da): 59979
Sequence Length: 553
Subcellular Location: Cytoplasm
EC: 1.7.99.1
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A0A2H5AIZ1 | MIINIKETTMVRPSQPTPSQRLWNSNLDLVVPRFHTPSVYFYRRPGNASDFFDARVLKEALGRALVPFYPMAGRLARDEDGRVEIDCNGEGVRFVVAETDSAIDEFGDFAPTMELKKLIPKVEYGDDISAFPLLVLQITHFKCGGTSLGVGMQHHVADGASGLHFINSWSDIARGLDIAVPPFIDRSLLRARDPPSPSFPHIEYQPAPSMNTSPAPIQDPTVKSDPTATAVSIFKLTKQQLDLLKSRVSAKYSSYALVAGHVWRCTSIARGLPDDQRTKLYCATDGRARLQPPLPSGYFGNVIFTATPVADAGEITGEDS... | Function: Hydroxycinnamoyl transferase that catalyzes the transfer of an acyl from p-coumaryol-CoA to various acyl acceptors. Can use feruloyl-CoA and caffeoyl-CoA as acyl donors.
Sequence Mass (Da): 47985
Sequence Length: 436
Pathway: Phenylpropanoid metabolism.
EC: 2.3.1.-
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P45579 | MPHNPIRVVVGPANYFSHPGSFNHLHDFFTDEQLSRAVWIYGKRAIAAAQTKLPPAFGLPGAKHILFRGHCSESDVQQLAAESGDDRSVVIGVGGGALLDTAKALARRLGLPFVAVPTIAATCAAWTPLSVWYNDAGQALHYEIFDDANFMVLVEPEIILNAPQQYLLAGIGDTLAKWYEAVVLAPQPETLPLTVRLGINNAQAIRDVLLNSSEQALSDQQNQQLTQSFCDVVDAIIAGGGMVGGLGDRFTRVAAAHAVHNGLTVLPQTEKFLHGTKVAYGILVQSALLGQDDVLAQLTGAYQRFHLPTTLAELEVDINN... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the NADPH-dependent reduction of 2-oxoglutarate and 2-oxobutanoate, leading to the respective 2-hydroxycarboxylate. Cannot use NADH instead of NADPH as a redox partner. Do not catalyze the reverse reactions.
Catalytic Activity: 2-hydroxybutanoate + NADP(+) = 2... |
P30178 | MESGHRFDAQTLHSFIQAVFRQMGSEEQEAKLVADHLIAANLAGHDSHGIGMIPSYVRSWSQGHLQINHHAKTVKEAGAAVTLDGDRAFGQVAAHEAMALGIEKAHQHGIAAVALHNSHHIGRIGYWAEQCAAAGFVSIHFVSVVGIPMVAPFHGRDSRFGTNPFCVVFPRKDNFPLLLDYATSAIAFGKTRVAWHKGVPVPPGCLIDVNGVPTTNPAVMQESPLGSLLTFAEHKGYALAAMCEILGGALSGGKTTHQETLQTSPDAILNCMTTIIINPELFGAPDCNAQTEAFAEWVKASPHDDDKPILLPGEWEVNTR... | Function: Catalyzes the NAD(P)H-dependent reduction of 2-oxoglutarate, phenylpyruvate and (4-hydroxyphenyl)pyruvate, leading to the respective 2-hydroxycarboxylate in vitro. Shows a preference for NADPH over NADH as a redox partner. Do not catalyze the reverse reactions.
Catalytic Activity: 2-hydroxyglutarate + NADP(+)... |
P80960 | SLLRKNVDSLTEEEILTLQSVMRELQNDSSEHGFQSIASFHGSPPLCPSPEANKKVACCVHGMASFPQWHRIFTKQMEAALMGHGAKVGMPYWDWTTSFTKLPRFIPYDDEQLNPFVRITDLEDHFTTRDPQPELFKDPEGGDESFFFRQVLIALEQRDYCDFEVQFEVIHNSIHYWIGGHQKYGMSTLEYTAYDPLFFIHHSNVDRLWAIWQELQKYRGLPYDESDCGVELMREPLQPFAQTSATNPNNVTRAHSTPKSLFNYRQLAGYTYDTLTLNGMTISQLESSLLRLQKEEDRVFAGFLLRGIGSSADVTFDLCD... | Cofactor: Binds 2 copper ions per heterodimer.
Function: Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many mollusks and arthropods.
Sequence Mass (Da): 46756
Sequence Length: 407
Subcellular Location: Secreted
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P83040 | DDQGHTHRNLVRKSVRNLSPAERRSLVHALKSLQEDSSADGFQSLASFHAQPPLCPYPEANKRFACCVHGMATFPEWHRLYTVQFEDALRRHGSVVGIPYWDTVVPQEDLPAFFNDEIWDDPLFHANFTNPFNGADIDFNHQKIARDINVDKLFKEGPKGYDTWSFKQYIYALEQEDYCDFEVQFEIAHNAIHAWVGGTEEYSMGHLHYASYDPVFILHHSNTDRLFALWQELQKFRGHDPNEVNCALEMMREPLKPFSFGAPYNLNPTTKEHSKPEDTFDYKGHFHYEYDHLELQGMNVQRLHDYINQQKERDRVFAGF... | Cofactor: Binds 2 copper ions per heterodimer.
Function: Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many mollusks and arthropods.
Sequence Mass (Da): 47963
Sequence Length: 413
Subcellular Location: Secreted
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Q9HXM1 | MTRRTAFFFDELCLWHAAGPHALTLPVGGWVQPPAAAGHAESPETKRRLKSLLDVSGLTARLQLRSAPPASDEDLLRVHPAHYLERFKALSDAGGGSLGQDAPIGPGSYEIARLSAGLAIAALDAVLAGEADNAYSLSRPPGHHCLPDQAMGFCFFANIAVAIEAAKARHGVERVAVLDWDVHHGNGTQAIYYRRDDVLSISLHQDGCFPPGYSGAEDIGEDRGRGFNLNVPLLPGGGHDAYMQAMQRIVLPALERFRPQLIVVASGFDANAVDPLARMQLHSDSFRAMTAMVRDAAERHAGGRLVVVHEGGYSEAYVPF... | Cofactor: Binds 1 zinc ion per subunit.
Function: Probable protein deacetylase that catalyzes deacetylation of acetylated lysine residues. In vitro, exhibits high activity against artificial HDAC (histone deacetylase) substrates containing acetylated and trifluoroacetylated lysine residues. Is not able to deacetylate a... |
Q9XSK7 | MSRSNRQKEYKCGDLVFAKMKGYPHWPARIDEMPEAAVKSTANKYQVFFFGTHETAFLGPKDLFPYEESKEKFGKPNKRKGFSEGLWEIENNPTVKASGYQSSQKKSCVEEPEPEPEATEGDGDKKGNAEGSSDEEGKLVIDEPTKEKNEKGALKRRAGDLLEDSPKRPKEAEDLEGEEKEGATLEGERPLPVEAEKNSTPSEPGSGRGPPQEEEEEEEEEEAAKEDAEAPGLRDHESL | Function: Acts as a transcriptional repressor (By similarity). Has mitogenic activity for fibroblasts (By similarity). Heparin-binding protein (By similarity).
PTM: Sumoylated with SUMO1. Sumoylation prevents binding to chromatin.
Sequence Mass (Da): 26604
Sequence Length: 239
Domain: The PWWP domain harbors the hepari... |
P51858 | MSRSNRQKEYKCGDLVFAKMKGYPHWPARIDEMPEAAVKSTANKYQVFFFGTHETAFLGPKDLFPYEESKEKFGKPNKRKGFSEGLWEIENNPTVKASGYQSSQKKSCVEEPEPEPEAAEGDGDKKGNAEGSSDEEGKLVIDEPAKEKNEKGALKRRAGDLLEDSPKRPKEAENPEGEEKEAATLEVERPLPMEVEKNSTPSEPGSGRGPPQEEEEEEDEEEEATKEDAEAPGIRDHESL | Function: Acts as a transcriptional repressor . Has mitogenic activity for fibroblasts . Heparin-binding protein .
PTM: Sumoylated with SUMO1. Sumoylation prevents binding to chromatin.
Sequence Mass (Da): 26788
Sequence Length: 240
Domain: The PWWP domain harbors the heparin-binding sites and is responsible for DNA-bi... |
P52357 | MSLSSLFNGKYDTKFLLNMSSAAKVELIVEKVAALADACLETPLPTDWFRNILDPELEFNSNFEEIHSIGDEEFAQPLPFLPFRVLLITGTAGAGKTSSIQTLAANSDCLITATTSIAAQNLSGLLNRTKSAQVKTIFKTFGFNSSHVSMNERISCSVTTLDSIADQQKHDLSTYWNVIADIAERALNAANGKTKVIPDLCESSVIVIDEAGVILRHILHTVVFFYWFYNGLHKTQLYKNRVIPCIVCVGSPTQSGALISSFNPLTQNKDVKKGFDILSALICDDILSNYCKISENWVIFVNNKRCTDVEFGEFLKHIEF... | Function: Component of the helicase/primase complex. Unwinds the DNA at the replication forks and generates single-stranded DNA for both leading and lagging strand synthesis. The primase synthesizes short RNA primers on the lagging strand that the polymerase elongates using dNTPs. Possesses helicase-like motifs and the... |
Q6UDG9 | MAEDRGTRLWQFPDHVYLNFTAMHGIQHVVDRISSLAEESVTPAERPPLSWFEAVARADSPDEVPPRELPFRVYLITGNAGSGKSTCIQALTEMLNCVTTGSTRVAALNVFTKLSSAYTSPAIQTIFHDFGFKGSHVQAVLGKFKYPKQPDPKSLVDAQMSDLYYYWDVLKDIANKVVEGGLPETMRVLLSLELKSGKPFTDAAPFLSAATPALIRSNVVLIDEAGVLGKHILTAVVFSWWLHNALWQTRRYAEGKVPVIVCIGSPTQTDAMESVFEHSTLRHLVSNKTNILSHLIRSSEMAERMNLNRNWTIFINNKRC... | Function: Component of the helicase/primase complex. Unwinds the DNA at the replication forks and generates single-stranded DNA for both leading and lagging strand synthesis. The primase synthesizes short RNA primers on the lagging strand that the polymerase elongates using dNTPs. Possesses helicase-like motifs and the... |
Q01014 | MAELSPEFILNMTSDAKVRIIVEKIRKLSNITTRPPEMTLYNDQFDPEQCPGTLLPFTCYVITGTAGAGKSTSISALYQNLNCLITGATTVASQNLSRCLKTYCPTIFNAFGFKSKHINILPRSVPRRTLDTIEQIQNFELCKYWPILTSIIQEFSKKKNLGQYSSISLAAFNMLAKMTTTLWTTNVIVIDEAGTLSSHILTAVVFCYWFYNSWLNTPLYRSGAVPCIVCVGSPTQTDAFNSTYNHIQQKYNIMECDNILSFIIGNKVVSEYISLTNNWALFINNKRCTDPEFGHLLKTLEYSLKISPKTMEYIDRFVVP... | Function: This protein may be a helicase and is required for replication of viral DNA.
Sequence Mass (Da): 88254
Sequence Length: 781
Subcellular Location: Host nucleus
EC: 3.6.4.-
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Q9NRZ9 | MPAERPAGSGGSEAPAMVEQLDTAVITPAMLEEEEQLEAAGLERERKMLEKARMSWDRESTEIRYRRLQHLLEKSNIYSKFLLTKMEQQQLEEQKKKEKLERKKESLKVKKGKNSIDASEEKPVMRKKRGREDESYNISEVMSKEEILSVAKKNKKENEDENSSSTNLCVEDLQKNKDSNSIIKDRLSETVRQNTKFFFDPVRKCNGQPVPFQQPKHFTGGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPDIPTMLYHGTQEERQKLVRNIYKRK... | Function: Plays an essential role in normal development and survival. Involved in regulation of the expansion or survival of lymphoid cells. Required for de novo or maintenance DNA methylation. May control silencing of the imprinted CDKN1C gene through DNA methylation. May play a role in formation and organization of h... |
Q60848 | MAEQTEPAVITPAMLEEEEQLEAAGLEKERKMLEEAQKSWDRESTEIRYRRLQHLLEKSNIYSKFLLTKMEQQQLEEQKKKEKLEKKKRSLKLTEGKSLVDGNGEKPVMKKKRGREDESYNISEVMSKEEILSVAKKHKDNEDESSSTTSLCVEDIQKNKDSNSMIKDRLSQTVRQNSKFFFDPVRKCNGQPVPFQQPKHFTGGVMRWYQVEGMEWLRMLWENGINGILADEMGLGKTVQCIATIALMIQRGVPGPFLVCGPLSTLPNWMAEFKRFTPEIPTLLYHGTREDRRKLVKNIHKRQGTLQIHPVVVTSFEIAM... | Function: Plays an essential role in normal development and survival. Involved in regulation of the expansion or survival of lymphoid cells. Required for de novo or maintenance DNA methylation. May control silencing of the imprinted CDKN1C gene through DNA methylation. May play a role in formation and organization of h... |
H2KY86 | MNRTPIRRCKSAEIEEDPFSPIPKFSRLRTPRTSREYVCPLKSTSPQSPSSSTENEPPPVSVTSPPARKRALEESTVTPIQQKIGPPVLKRSSLSKLADGFRTAAYLNNESENDDDPFGLSFRNEQVLMSKCAPAPEKRPETLTLDPSKCLPERDMEMYRKIKKLDKFYDWQQECLSDKRLLDGENCILSLPTGAGKTLIAEVLMLREAIVRKRNAILVLPYVAIVQEKISALAPFEDAFGINIEEYASNKGRFPPIKRRKRVSVYVATIEKANMLINSLITQGQLDRVGMVVVDELHMIGDGGRGAILEQLLAKFLYKG... | Function: Single-stranded 3'-5' DNA helicase that plays a key role in homology-driven double-strand break (DSB) repair . Involved in different DSB repair mechanisms that are guided by annealing of extensive stretches of complementary bases at break ends, such as microhomology-mediated end-joining (MMEJ), single-strand ... |
Q9YFQ8 | MSKGLYDIPSWATTETRTLAKLAGVERLFEPQYMALQAGVEKGENLVVAAPTGSGKTFIALVAIVNSLARAGGRAFYLVPLKSVAYEKYTSFSILSRMGLKLKISVGDFREGPPEAPVVIATYEKFDSLLRVSPSLARNVSVLIVDEIHSVSDPKRGPILESIVSRMLASAGEAQLVGLSATVPNAGEIAEWIGGKIVESSWRPVPLREYVFKEYKLYSPTGGLREVPRVYGLYDLDLAAEAIEDGGQALVFTYSRRRAVTLAKRAAKRLGRRLSSREARVYSAEASRAEGAPRSVAEELASLIAAGIAYHHAGLPPSLR... | 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): 80474
Sequence Length: 735
EC: 3.6.4.12
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P0DMI1 | MKVEELAESISSYAVGILKEEGIEELFPPQAEAVEKVFSGKNLLLAMPTAAGKTLLAEMAMVREAIKGGKSLYVVPLRALAGEKYESFKKWEKIGLRIGISTGDYESRDEHLGDCDIIVTTSEKADSLIRNRASWIKAVSCLVVDEIHLLDSEKRGATLEILVTKMRRMNKALRVIGLSATAPNVTEIAEWLDADYYVSDWRPVPLVEGVLCEGTLELFDGAFSTSRRVKFEELVEECVAENGGVLVFESTRRGAEKTAVKLSAITAKYVENEGLEKAILEENEGEMSRKLAECVRKGAAFHHAGLLNGQRRVVEDAFRR... | 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): 77835
Sequence Length: 691
Domain: The N-terminal region (1-400) has DNA-dependent ATPase activity but no helicase activity.
EC: 3... |
A8MB76 | MNIEELPLPSLLRDFLISKRGIRTLYPPQEEAIRAGLLNGENILMVSATASGKTLLAEVAAVNNVLVNDKKSLVAVPLKALAFEKLNDFNTYSELGIRVAASTGDYNSEDKWLGSYDVIITTYEKLDSLLRLKPSWIWNVGQLIIDEIHFINDDERGPIIESIVAKLRMLNLNPQIIGLSATIGNPEELANWLNAKLVKSDWRPVSLREGVYHKGVVTYVNDGEKRISGQGDSLINLTVDTLNDGGQVLVFSSSRQGAVRIARKLAEYICSSPVRYIDPGEAGKLAEEVRETSSSRILAEELTGLIKCGVSFHHAGLELE... | 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): 84006
Sequence Length: 756
EC: 3.6.4.12
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Q5UYM9 | MDVADLPGVPEWLPDHLRDDGIEELYPPQAEAVEAGVTEGENLVASIPTASGKTLIAELAMLSSVARGGKALYIVPLRALASEKQADFEEFEQYGLDIGVSTGNYESEGGWLADKDIVVATSEKVDSLVRNDAPWIEDLTCVVTDEVHLVDDGERGPTLEVTLAKLRRLNPDLQTVALSATIGNAEALATWLDAGLVDSDWRPIDLQKGVHYGQALHLEDGSQQRLSVQNNEKQTAAIVRDTLEDDGSTLVFVNSRRNAEAAAGRLANTVRPHLSTEERDQLADIAEEIRDVSDTETSDDLADAVADGAAFHHAGLSRGH... | 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): 86768
Sequence Length: 799
EC: 3.6.4.12
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B9MRJ1 | MLWVIGINHKVEVDIRQKFSLIKTKLQEKLISLKKLANEVIILSTCNRTEIYFFSEEYVDIEKIFTELDWDKRYMHLFYIYKDKDCIKHLFEVVCGFDSLLIGEDQIVAQVKEAKEISKLVGGKNPVLERLFEVALKCSKEFRTKARLNEHPITIASVVGKVLKESNIRKIAIIGLGNIGILFCNYFKNSDVDKVFLIGRKNEKIDQFVKLNPEKFRYYDKKKTILEAQCLICSTSAPHSVVHKDDIPEGKNLLIFDLAVPRDVDVEVYELPNVKVIDIDQVHKIDTINREFRISKMQENYHIIDKYVDEFIDWLEFRQY... | 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): 46380
Sequence Length: 394
Domain: Possesses an unusual extended V-shaped dimeric str... |
A8MAH6 | MGIDDYLSKIRALTLNHKRVSTITLSETYFNRDEVYGKLMNYYDEVFLLQTCNRVEVYVYGDDDSVAEDMYKVKGTINHVDKLVGMNAVRHIFRVAAGLESAAVGESEILGQVEDAFNDARKRGALGGLLGFTIERAIRTGKEIRSRFPEISIGLASIGSLVAEYVHRVRGLNSRIAVIGAGSIGSDIVRRLAEKGFRNVIIVNRTLDKAKAAALRYGFNYAPIDSLRSVIRDSDVVIFATSATNPLLRRRDAEELSGKPIIIDVGVPRNVDPEIPGVVSIDELKNIENEIREGKRKALDEASRLIELRLIEYRRLFARR... | 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): 45009
Sequence Length: 406
Domain: Possesses an unusual extended V-shaped dimeric str... |
A5VM68 | MYLMCVSLNYHQLPLDLREKFSFTKEEVPKADKLLNDEKSILENLLISTCNRTEVYAVVDQIHTGRYYIRRFLAEWFHYTIDDFTKFVTVTTKDAVAEHLFKVITGLDSLIKGEPQILGQMKDAFQIATKEGTTGAILNHLFRQAITFSKRMHTKYRVSELAQSSGQAGLHQIKMQFGSLEGKTLAVVGLGQIGKHTAYNASNMGFSKVLLLNRTDSKAEQIATELQGVVEARPFNQLATVVHNVDAAIFAATVKQPLFKADEQISTMIVDLGVPRNVAVNSTKLKYYDVDHVHMILNSNDEKRRLMIQKIANEIPQEVN... | 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): 47865
Sequence Length: 421
Domain: Possesses an unusual extended V-shaped dimeric str... |
Q8Y6X4 | MFILTMGLNHHTAPIDIREKLVFKETEEEMALVTLQQEKSILENVIISTCNRTEIVAVVDQIHTGRYYLKRFMANWFQMDMEKIEPYLFFHEETEAVNHLYKVTAGLDSLVLGETQILGQVKHAFEIAKQTETTGTLLNKLFREVVTFAKKVHHHTKINENAVSVSYAAVEVAKKLYGSLDNKKIVLVGAGEMSELALQNLAGSGIADITIINRTKSNAELLANQFQAKVGAYENMNEHLMLADIVLVSTSATEPIIKQAAMQDLMEQKASSMLVIDIGLPRNVEHDCSYIPNFHLYDIDDLAGVVSANSLERQRIVLEL... | 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): 49250
Sequence Length: 435
Domain: Possesses an unusual extended V-shaped dimeric str... |
A0LDT6 | MKLVVVGLNHKSAPVSLREKVAYSSDTLPRSLQALTRLDAVHEGTILSTCNRVEIYMASRDPDAAAAQTSQWIARDHALDPADVTPHLYTKAESEAVRHGFCVASSLDSMVLGEAQILGQMKQAYQDALSAGSTGVVLNRFFQHAFLTAKRVRTETSIAENSVSVASAAVDLAKRIFGDLSGHSCLLIGAGEMCELAARHLVTHGVKEVLVTNRTFSRAVDLAQQFDGHAFPIEALAENLHRADIVISSTGSTVYMVGPDMVKQALKSRRQRPIFLIDIAVPRDLDPEIGQVDSAFLYDMDDLNKIVNDNRQDRAEAAQA... | 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): 46617
Sequence Length: 421
Domain: Possesses an unusual extended V-shaped dimeric str... |
Q0W5T5 | MAQVCSISVNHRHAGIEGIERARFRDPDVAMLRLLSLPGVSEAVVLQTCNRVEIYAVAESVEDIVGFARAEGMPLEIAEVRAGDDCLKGLLRLACGLESMIVGEDQILGQLKTALLQARRLGTIGPVLSTAIQKSIHVGARARIETEINKGSVSIGSAAVELAESLLGDLRGRTILVVGAGEMGTLVANAMAEKSLRAIYVANRTFEQAEKLASSLQGVAIRLERLCDYMGSADVVICATGAPHLIITKKMVEQCKGEKPLIFIDITNPRNIEETVGEVPGVTLHNIDSLRQINEASMRRRQGEARKVEAIIEEELVLLQ... | 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): 46694
Sequence Length: 427
Domain: Possesses an unusual extended V-shaped dimeric str... |
A9FDP5 | MIFVGLSHKTAPIEVRERLAIGRDRLPEVLARLTAHPAIGEALVLSTCNRVEIYASPRQQAPAPPRPGSAPPPSDEELSRNNEALRAAVATLVGLGGDAVRGHLAGRVGSDAVLHLFRVAASLDSMVVGEPQILGQMKEAIEVARGAKTLGVRLGRAAHRAIKVGKRVRTETAIGAGQVSVSSVAIDLARQIFADLAGHTALLIGAGDMAEAASKLLVRAGARLIVVNRSPDRAAALAREVGGEPRPWADLERSVIDADIVISSTSSPNYVVTPDLVRRARKARKGRSLFLIDIAVPRDIDPAVNKLDSVYLYDVDDLSQ... | 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): 55293
Sequence Length: 529
Domain: Possesses an unusual extended V-shaped dimeric str... |
A6TJD5 | MRTIKIGSRASQLALVQAEIIINMLKEKFPQYTYEIIKITTLGDRILDKTLDKIGGKGLFVKEIQKALAEEKIDLAIHSMKDMPGETPEELVLGAITKREDPRDVLITRENKSLEELPKGAVIGSSSLRRQAQVMALRGDIKVVPIRGNVGTRLGKIETESLDGVILAAAGLNRLGLKEKISSYLEIEDFTPAVGQGALGCEARRKDIEMLEMLLAINHEETYRCVMAERAFLKLLEGGCHVPIGAYGQQQGQELHMTGMVASSDGRRVIKEQVMGDIADFQALGIQLGETLIEKGAKEILETVNTDNRIVNTEGS | 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): 34706
Sequence Length: 316
Pathway: Porphy... |
A8MGE4 | MKIRVGSRESKLAVKQSEIVIEAIRKYDPNIEIELVTMKTTGDIKLDQTLDKIGGKGLFIKELDQALYDDRVDITVHSFKDMPMAIDEYLPIVAVSKREDPRDVLVLPKTVKEPDFSKPIGCSSFRRKIQLQEIYPHCSVEPIRGNVLTRLEKLDRGEFSAITLALAGLKRLGLEERISRIFEVTEILPAACQGVIVVQARKGFDVSFLSDFHDKEAWDISMAERSFVRTLNGGCSSPVAAYGEIKDNYLTLTGLYVDSSNSVHKKTITGARKQGEEMGFNLALQMKGEDEVHGKD | 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): 33149
Sequence Length: 296
Pathway: Porphy... |
O66621 | MKIRIGTRKSKLALWQANYVKDFLEKHWGVEVELVKITTTGDKITDVPLAKIGGKGLFVKEIEKALLEGSIDLAVHSLKDVPMVIPKGLKLGAITKRENPYDVLISRSGKKLYELPSGSVIGTSSLRRQVQIKKRRRDLKVEVLRGNVDTRMRKLKEGLYDAVILAYAGVKRMGYESEITEVLEDFIPAVGQGSLAIEIREGDKRIEELIKPLNNEESFLCAIAERTFLRRLEGGCQVPVGAFAKIENGTLKMKAFISDIEAERYIEGYREGNPEEAEKLGLSLAEELLKKGGEEILKEIYSSQ | 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): 34031
Sequence Length: 304
Pathway: Porphy... |
Q43316 | MDIASSSLSQAHKVVLTRQPSSRVNTCSLGSVSAIGFSLPQISSPALGKCRRKQSSSGFVKACVAVEQKTRTAIIRIGTRGSPLALAQAYETREKLKKKHPELVEDGAIHIEIIKTTGDKILSQPLADIGGKGLFTKEIDEALINGHIDIAVHSMKDVPTYLPEKTILPCNLPREDVRDAFICLTAATLAELPAGSVVGTASLRRKSQILHKYPALHVEENFRGNVQTRLSKLQGGKVQATLLALAGLKRLSMTENVASILSLDEMLPAVAQGAIGIACRTDDDKMATYLASLNHEETRLAISCERAFLETLDGSCRTPI... | 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): 41043
Sequence Length: 382
Pathway: Porphy... |
O29026 | MKLIVGTRGSKLALAQTNKVAERLKERYEVEIRIVKTAGDIMKDKPLYEFKGMGAFVRALDTALAEGKVDVAVHSFKDVPSQRVEGTVVAAVIERDSPCDVLISRDGSTLEELDEGAVVGTSSLRRRAQLSRLRGDLRFENLRGNLDTRLRKLREGNYDAIVVAEAGLKRLGLDREVEYQPFPPEVIVPPANQGIIAIATRKGEEDLVAFLNDEKTWLEAMVERAVIKELGVGCAVPVGVYAEAQSRVRLICEILDKKYLRVEEKLSKDTAVEEAAEIGKDLRKEIYGG | 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): 32006
Sequence Length: 289
Pathway: Porphy... |
Q75DY0 | MGEETLRIAGRRSKLAVIQSESVKEIVQREFPNYTCTVLAKQTLGDQVQSKPLYAFGGKALWTKELEDLLYEEDLDQRIDMIVHSLKDMPTQLPEGFELGAITKRVDPSDCLVMAAGSPYKTLGDLPNGSVVGTSSIRRSAQLRRRYPHLVFASVRGNIQTRLKKLDDPENECKCIILATAGLVRLGLESRITQRFDSTIMLHAVGQGALGIETRTGDERLQAILAKVADRNSTICCLAERSLMRTLEGGCSVPIGVYSTFDEETSMLTLDGLVVSVDGADAAEATVSYKIKSDKEDAIACGQLLAAKLLEAGAKKILDA... | 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): 35526
Sequence Length: 326
Pathway: Porphy... |
Q6CT60 | MESKETVRIGGRRSKLAVVQSEQVKVMIESKFSHIECPLLSVHTLGDQVQSKPLYSFGGKAVWTKELEDLLYKDDESRIDLIVHSLKDMPTLLPDGFELGGITKRVDPTDALVMPIGSPYSSLSELPDGSVVGTSSVRRSAQLKRKFPNLKFESIRGNIQTRLAKLDDPETPYKCIVLASAGLMRSGLDSRITQRFNADTMCYAVGQGALGIEIRKDDEKMKKILKEICDPSTTICCLAERSLLRTLEGGCSVPIGVVSNYDESTKVLTLKGIVINVEGTEWVEIEHKVTISNEREDSINCGKELAAKLTQNGAKEILDS... | 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): 36045
Sequence Length: 327
Pathway: Porphy... |
Q1INI6 | MATLRIGSRGSQLALWQANHISALLRERGHEVELEIIKTTGDKILDVALAKVGTKGMFTKEIEEALAAGKVDVAVHSLKDLPTELPQGFELAAVTKRENPRDVFLSVKYDSISGLPQGAKVGTSSLRRQAQIKAIRPDLEIFPLRGNVDTRVRKLEQGEYDAIILAFAGLNRLGKTQLVKEIISEDVMCPAAGQGALGIEIRLGDTRMREILSFLNDYDARATTTAERALLNQLGGGCQVPIGAFAEVKDGQVHLTAICARPDGSEILRESKSGADPAHLGEEVGKTLLARGATKILEDVYSQNIAAPAQP | 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): 33492
Sequence Length: 311
Pathway: Porphy... |
C4Z552 | MHYRIGTRGSKLALVQSEYVKRRMEEAYPEDTFELVIIKTTGDKVTDKPLAAIGTKGFFVKEIEEALLSGSIDMAVHSMKDMPAECAAGLTFAKAWKREDCRDVLILKTAGSFSELPSGAVIGTGSLRRACQLAMLRPDIQFTAIRGNVDTRINKLMDDSYGLDGIVLAAAGLNRLGRSSEITEYLDPEVVIPAPAQGVLAIETAEVNTELLDKINALSDDNSDREAVAERTFLRLTGGGCHAPVGAHCVTKDNGDLRMVVLFGNDDCSRILRIEVTGTDSEAVGHEAARMLGLE | 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): 31916
Sequence Length: 295
Pathway: Porphy... |
Q1MPL2 | MKKITIATRGSKLAFWQANYIKDQLQKMYSYLEVDLMVIKTKGDHILDVPLAKVGGKGLFVKEIEEALLSGEADCAVHSMKDVPMELPFELCLAAITEREDPTDMFLSIKYSGVKSLPENALVGTSSLRRQAQLLALRPDLQIIPLRGNIDTRLRKLMAEEFDAIIMATAGIKRLGLIAPYMSSLPCSVMLPAVGQGALGIEVQKERQDVLELFSFLNHKETYHCIQAERDFLAGLDGGCQVPIAGYATICKQETICLEGLVAKSDGSVMIRNRLERSVSDAYDIGMTLSKILLAEGADDILASMHTIL | 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): 33993
Sequence Length: 309
Pathway: Porphy... |
Q5ZRY6 | MSAKIIRIATRQSPLALWQANHVREMLVKQWPNLSIELLPMITSGDRFLKDKLLSAGGKGLFVKELEEALLDKRADLAVHSTKDMPAQLPDGLLLTAICKRDNPFDALISPQFKSLAALPKNAIIGTSSLRRQSQLLAYNPNLQIKTLRGNIHTRLSKLESGEYQAIILAAAGLERMGLAHHITQLIPDDIMLPTCAQGALCIECRTDDLEIQELVHGLNDPISALCVHTERRVNAKLGGNCHIPFAVYCTITEEKLLLLRAKVLNMDGSQMIDDEQQGKIAEAEVIADRCTESLMTKGAMSLLSTIPS | 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): 33987
Sequence Length: 309
Pathway: Porphy... |
Q6AHF1 | MIVSDGPAERRQGALRVGTRGSPLAVAQTQAVSAAVARATGFDIELVTVTTHGDTSRESLSELGGTGVFATALRDALRNGECDLVVHSLKDLPTAPAPGLVLGAVPKRADARDTLCARDGLRFGELPEGASVGTGSPRRAAQLRAQRPGLDIVDIRGNVDTRLSRVSAGDLDAVVLAAAGLGRLGRLDAATDFFSLSTMPTAPGQGALALEVREGDERGRGPIARALAAVDHATTCAATTAERAVLAGLEAGCAAPVGATAMIDDGLLFLTATVYRPDGAAQLTASHAATPDSFGAAHLDEAARDVGERVVAELLASGAA... | 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): 33375
Sequence Length: 329
EC: 2.5.1.61
|
A5VM67 | MTNKVIVGSRKSKLAMAQTELVIASLEKIFPDIKFEIKNVITEGDRNRHVSLAKIGGKGVFVKEIEDELKDGTIDFAVHSLKDVMPILPEELVLGAFPKRVSPYDCLVSRKNLSSLNDLPKGARIGTNSLRRQGQLLSIRPDLKIIPIRGNIDTRLRKIDTEALDGIILAEAGLTRLNIDLSSYHVLDLQNYIMPAVGQGCLAIECRKNDTRIRKMLDQINDEESAYCVQVEREFMRELGGSCNFPIGGHAYAKNGQILFDGLIASPNGEHVIKETKIPANNSGVGKKVADQLLAKDKFGIIEGE | 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): 33658
Sequence Length: 305
Pathway: Porphy... |
Q8Y6X5 | MKRKIIVGSRRSKLALTQSNWVINKLKENYPEFDFEIKEIVTKGDRILDVTLSKVGGKGLFVSEVEQALSDEAIDFAVHSMKDVPSSLKEGLIIGAIPKRESPLDCFVFNQVNSLDELPQGSVIGTSSLRRAAQLLKHRPDFVIKPIRGNIDTRLQKLHAENFDAIILAKAGLARMGWLENTTLKLEDIPPEVCLPAVGQGALAIECRESDQQIRDMLTSIHHEETGICVEAERVFLKKLNGGCEIPIAGFATRANEFVQFKGLVGNADGSIILESEQVGANPSEIGNKVAEDLLSEGADTIIKELRNV | 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): 33937
Sequence Length: 309
Pathway: Porphy... |
Q4L709 | MRKLVVGSRRSKLALTQSQQFIDKLKAVDPTLEIEIKEIVTKGDRIVNKQLSKVGGKGLFVKEIQQELFDKEIDMAIHSLKDVPSIIPEGLTLGCIPDREVPFDAYISKNHIPLNELPDGSIIGTSSLRRGAQILSKYPNLEIKWIRGNIDTRLKKLEIEDYDAIILAAAGLRRMGWSDDIVTTYLDKDILLPAIGQGALGIECRSDDVELLELLSKVHNQAVANCVTAERTFLSAMDGSCQVPIGGYATNKENGEIEFTGLIMTPDGTKRYEHTEVGKNPVDLGEAVSRVLKEQGAYEIIKKLNEEQAH | 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): 34349
Sequence Length: 310
Pathway: Porphy... |
A3CL78 | MKVIKVGTRKSKLAMTQTQQLVDQLKALHPERDFVLVPYTTKGDRLTHVSLQEIGGKGVFVKEIERALLAGEINMAVHSLKDMPAKLAEGCALGAISQREDVRDCLIFRQAGQTLADLPKGSLIGTSSIRRQVQLQAQRPDLAFKPLRGNIDTRIKKLEEGEYDAIVLAMAGLKRLGWLDQSRLHIQPLETSLCLPAISQGALAVECREEDEELLSLLAAVQDEKTAAEVAVERAVLAQMNADCTFPIAAFAQKNGQGYQLEAMLAKEDGQCIFVSLQGQDGQQLAEQAVRQLADKGAVGMPWLKK | 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): 33494
Sequence Length: 306
Pathway: Porphy... |
Q30S90 | MKKLVIATRGSQLALWQSNHIKAILQEQNPGLEVELNVIVTTGDRIQDKALSKIGGKGLFLKELEEAMLQGEAQIAVHSLKDVPTVMPDGLILAAITEREDSRDALLSEKYANIDALPKNAVVGTSSLRRRMQIQKLRPDLIIKDLRGNVDTRIRKLKEGEFDAIILAAAGINRLSLLDAVKHVYPISLEEMVPSMGQGALGIEAVNDAEVLRIVAGLEDEYSRIETTIERSFVDELEGGCQVPIGVNASVLDDGTISIRAVLGLPNGEEMLSDSKITSKKDYENIGREIAAEFIEKGAKELLSRAEAMMENK | 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): 34233
Sequence Length: 313
Pathway: Porphy... |
Q4KKQ4 | MTTRTEAVKAYLLDLQDRICAALETEDGGARFIEDAWTRPAGGGGRTRVIGDGAVIEKGGVNFSHVFGSGLPPSASAHRPELAGRGFEALGVSLVIHPHNPHVPTSHANVRFFIAEKEGEEPVWWFGGGFDLTPYYGNIDDCVHWHRVAERACAPFGADVYPRYKAWCDSYFHIKHRNEPRGIGGLFFDDLNEWDFDTSFAFMRAIGDAYIEAYLPIVQRRKAAAYTAQQREFQEFRRGRYVEFNLVYDRGTLFGLQSGGRTESILMSLPPQVRWGYDWKAEPGSEEARLTEYFLQDRDWLAASN | 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 ... |
Q8XXC3 | MDTQAVRAYLLDLQDRITTAVGTLDGGTFVTDTWDKPPTERLRGSGRTCILENGAVLERGGVGFSHVMGDTLPPSATANRPELAGRGFEAMGVSLVFHPRNPYAPTVHMNVRCFVAQRPDAEPVWWFGGGMDLTPYYGFAEDAAHFHRTCKQALEPFGEELYPRFKQWCDDYFYLKHRKEARGVGGIFFDDFAELGFERSFEMMRAVGDALLPAWLPIAEQRHATPYGERERAFQAYRRGRYVEFNLVFDRGTLFGLQSGGRTESILMSMPPVANWRYDWQPEPGSPEAALYTDFLPARDWV | 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 ... |
Q3B7D0 | MALRLGQLGSGPWWRAVRGDYAQLRAPSPRSASACVCRLPGTAGTQPRRGLGHGSSAGGGSRLGTGLAAALAGMAGLAAAVLGHVQRAEMVPKSSGARSPSPGRLEEDGDELARRCSTFMSSPVTELRELGRRPDDMKTKMELMIMETQAQVCRALAQVDGVADFSVDRWERKEGGGGITCVLQDGRVFEKAGVNISVVHGNLSEEAANQMRSRGKALKKKDGKLPFTAMGISSVIHPKNPYAPTMHFNYRYFEVEEADGKMHWWFGGGCDLTPTYLNREDAVHFHRTLKEACDQHGPDIYPKFKKWCDDYFFIAHRGER... | 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 (By similarity).
Catalytic Activity: coproporphyrinogen III + 2 H(+) + O2 = 2 CO2 + 2 H2O + protoporphyrinogen I... |
P13103 | MALNVIATLTLISVCVHADRICVGYLSTNSSERVDTLLENGVPVTSSIDLIETNHTGTYCSLNGVSPVHLGDCSFEGWIVGNPACTSNFGIREWSYLIEDPAAPHGLCYPGELNNNGELRHLFSGIRSFSRTELIPPTSWGEVLDGTTSACRDNTGTNSFYRNLVWFIKKNNRYPVISKTYNNTTGRDVLVLWGIHHPVSVDETKTLYVNSDPYTLVSTKSWSEKYKLETGVRPGYNGQRSWMKIYWSLIHPGEMITFESNGGFLAPRYGYIIEEYGKGRIFQSRIRMSRCNTKCQTSVGGINTNRTFQNIDKNALGDCP... | Function: Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-i... |
A6X6W2 | MSEMDKVQEKPSQTTKTEVQAKLPKVGVLLVNLGTPDGTSYGPMRRYLAEFLSDRRVIEWPRLIWYPILYGIVLNTRPKRSGKLYDRIWNREKNESPLRTYTRAQGEKLATALADYPNVVVDWAMRYGQPSIESVTDRLLQQGCERIVMFPLYPQYSATTTATVNDKFFEALMKKRFQPAVRIVPSYETEPVYIEALARSIEKHLETLSFKPEVVLASYHGIPKSYSDKGDPYRQQCLETSRLLQARLGLDDSQFRSTFQSRFGPEEWLQPYTDETVEELAKHGVKSMAVLNPGFVADCLETVDEIGNEAAEEFLENGGE... | Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
Sequence Mass (Da): 40051
Sequence Length: 350
Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
Subcellular Location: C... |
Q92FV4 | MKKRIAIVLFNLGGPKNLKSVKPFLFNLFYDKAIINLPNPLRYIIAKIISITREKKSQKIYSLIGGKSSLLQETEEQKLALTEKLKQLIKEDFAIFINMRYSAPFAKEVIGQIKKYNPSEIILLPLYSQFSSTTTGSSVKNFLQNLDIDIPIKTICCYPLEKDFIKAHVSLIKEKLYDKNFRILFSAHGLPEKIIKAGDPYSFQIKETVQAIVKELNIKDLDYKITYQSRVGPIEWLKPNTEDEIELAGKLKKDIIIVPISFVSEHVETLVELDIEYKLIADKYEIQYIRIPTLGTNKIFINSLTNILLRFINKVDTNLV... | Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
Sequence Mass (Da): 39238
Sequence Length: 342
Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
Subcellular Location: C... |
Q9ZC84 | MNKRIAIVLFNLGGPEDIEYVKPFLFNLFYDKAIINLPNPLRYIIAKIISITREKKSQKIYSLIGSKSYLIQETEKQKLAITEKLKEFIKEDFIIFINMRYSTPFAKEVIGQIKEYNPSEIILLPLYPQFSSTTTGSSVKNFLQNIDIDIPIKTICCYPIEEDFIKAHVSIIKEKLYDKNFRILFSAHGLPKRIIKAGDPYSFQIKETVNKIVKELNIKDLDYKITYQSRVGPIEWLKPNTEDEIELAGKLKKDIIIVPISFVSEHVETLVELDIEYKLIADKYKIQYTRIPTLGTNKIFINSLTNILLRFINNTNTNLV... | Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
Sequence Mass (Da): 39611
Sequence Length: 342
Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
Subcellular Location: C... |
Q5T8I9 | MEENNLQCSSVVDGNFEEVPRETAIQFKPPLYRQRYQFVKNLVDQHEPKKVADLGCGDTSLLRLLKVNPCIELLVGVDINEDKLRWRGDSLAPFLGDFLKPRDLNLTITLYHGSVVERDSRLLGFDLITCIELIEHLDSGDLARFPEVVFGYLSPSMIVISTPNSEFNPLFPSVTLRDSDHKFEWTRMEFQTWALYVANRYDYSVEFTGVGEPPAGAENVGYCTQIGIFRKNGGKATESCLSEQHDQHVYKAVFTTSYPSLQQERFFKLVLVNEVSQQVESLRVSHLPRRKEQAGERGDKPKDIGGSKAPVPCFGPVFTE... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Methyltransferase that adds a 2'-O-methyl group at the 3'-end of piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a Dicer-independent mechanism and are primarily derived from transposons and other repeated sequence elements. This probably protects the... |
Q9UST9 | MGVSSFYPPLHVQRRRKLFKILQGGFPVRSLLDIGCGDARFLSYLVPCNDQVPIEFLAGIDINEQSIERATEALQVRTEDFLQLRWRPLHIELLLGNIKDFTHYKHVDAVVASEFIEHCQVAEILAFEKLVFGNLKPNVCVVSTPNFEFNTIFEKLSTLTSSISSRTSTNFRHPEHVFEWDRKEFAKWAYKICKRYPEYTVEFTGCGLLNDLIDGDDLLHFRPSSTYGFCTQIAVFHQSKNNAASHCFLKDQNSSILLYKKITYPFMEQLFPPTVQQFMNLLKKAFFDHLFGRHCLLLFQVIAGKCALSVKLPFLFIWES... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Methyltransferase that adds a 2'-O-methyl group at the 3'-end of small RNAs.
Catalytic Activity: S-adenosyl-L-methionine + small RNA 3'-end nucleotide = H(+) + S-adenosyl-L-homocysteine + small RNA 3'-end 2'-O-methylnucleotide
Sequence Mass (Da): 43827
Sequence Length... |
Q230X8 | MIEAYETDVFMDPIGMKVWEKRHQYVATKLSALNCKRVLDMGTNTCKLIQRLSRSLQFTQIDGLDIDGQLLETQGIQNAKPDLIQNQYASMRDHQLVVNLYQGSALNKIQHLKDQQYDAVILVELIEHLQVEDVFLIEQNLFGFLRPQFVIVTTPNSDFNVYFNFKEQGVLFRDKDHKFEWSQNQFQIWAQKVCQNYGYKVIELTGVGEHKTEGTKNGFCTQIVVFEKDTQQEKYLNFAFFNLQEGEIRQVCQILYPFESKEQHFQREVVDSIRYILHITDKQNQFEDGSYQNYTTLSRIMQNHSISSNWQIQGDYFKLK... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Methyltransferase that adds a 2'-O-methyl group at the 3'-end of piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a Dicer-independent mechanism and are primarily derived from transposons and other repeated sequence elements. This probably protects the... |
C0IN03 | MELEFFKPPLYQQRYQFVKSYVDTYKPKKVADLGCSTCSLLHTLRFWDCIKVLVGLDIDEDVLSRKKFTLTPLPAHYLEPRNTSLTINLYQGSVTQKDPALLGFDLITCIELIEHLEAEELENFREVLFGFMAPITVIISTPNAEFNILFPKCTGFRHPDHKFEWNRREFQSWATEVAKCFNYTVEITGVGEPPRDSKNVGFCSQIAVFTRNYTESEESLQRKMECKSVYKTVLHIVYPSLQEEKYLRRAVQKVALFHAYQIKANFLQQFIHREEEEEPHNTDTEHRPCMDLKLTSRWPTLPQTEQDESMEPFLQEDTLY... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Methyltransferase that adds a 2'-O-methyl group at the 3'-end of piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a Dicer-independent mechanism and are primarily derived from transposons and other repeated sequence elements. This probably protects the... |
Q05819 | MKKQILYLIVLQQLFLCSAYAQQKKSGNIPYRVNVQADSAKQKAIIDNKWVAVGINKPYALQYDDKLRFNGKPSYRFELKAEDNSLEGYAAGETKGRTELSYSYATTNDFKKFPPSVYQNAQKLKTVYHYGKGICEQGSSRSYTFSVYIPSSFPDNATTIFAQWHGAPSRTLVATPEGEIKTLSIEEFLALYDRMIFKKNIAHDKVEKKDKDGKITYVAGKPNGWKVEQGGYPTLAFGFSKGYFYIKANSDRQWLTDKADRNNANPENSEVMKPYSSEYKTSTIAYKMPFAQFPKDCWITFDVAIDWTKYGKEANTILKP... | Function: Degrades heparin and heparan sulfate. Also implicated in the release of heparin-bound growth factors from the extracellular matrix.
PTM: The N-terminus is blocked.
Catalytic Activity: Eliminative cleavage of polysaccharides containing (1->4)-linked D-glucuronate or L-iduronate residues and (1->4)-alpha-linked... |
P05546 | MKHSLNALLIFLIITSAWGGSKGPLDQLEKGGETAQSADPQWEQLNNKNLSMPLLPADFHKENTVTNDWIPEGEEDDDYLDLEKIFSEDDDYIDIVDSLSVSPTDSDVSAGNILQLFHGKSRIQRLNILNAKFAFNLYRVLKDQVNTFDNIFIAPVGISTAMGMISLGLKGETHEQVHSILHFKDFVNASSKYEITTIHNLFRKLTHRLFRRNFGYTLRSVNDLYIQKQFPILLDFKTKVREYYFAEAQIADFSDPAFISKTNNHIMKLTKGLIKDALENIDPATQMMILNCIYFKGSWVNKFPVEMTHNHNFRLNEREV... | Function: Thrombin inhibitor activated by the glycosaminoglycans, heparin or dermatan sulfate. In the presence of the latter, HC-II becomes the predominant thrombin inhibitor in place of antithrombin III (AT-III). Also inhibits chymotrypsin, but in a glycosaminoglycan-independent manner.
PTM: Phosphorylated by FAM20C i... |
P49182 | MKHPLCTLLSLITFMCIGSKGLAEQLTNENLTTSFLPANFHKENTVTNDWIPEGEEDEDYLDLEKLLGEDDDYIYIIDAVSPTDSESSAGNILQLFQGKSRIQRLNILNAKFAFNLYRVLKDQATTSDNLFIAPVGISTAMGMISLGLRGETHEEVHSVLHFRDFVNASSKYEVTTIHNLFRKLTHRLFRRNFGYTLRSVNGLYIQKQFPIREDFKAAMREFYFAEAQEANFPDPAFISKANNHILKLTKGLIKEALENIDPATQMLILNCIYFKGTWVNKFPVEMTHNHNFRLNEREVVKVSMMQTKGNFLAANDQELD... | Function: Thrombin inhibitor activated by the glycosaminoglycans, heparin or dermatan sulfate. In the presence of the latter, HC-II becomes the predominant thrombin inhibitor in place of antithrombin III (AT). Also inhibits chymotrypsin, but in a glycosaminoglycan-independent manner.
PTM: N-glycosylated; different glyc... |
Q2U0K2 | MWWPRATADRLQTCTFWFLWLFTWDDEIDQSTSDLFIHIHKANDFRKESLEYVKFCLGVGDDETAKWDFQNNPPNRPLIRSLDVIGAHLQKVYNHDQIMTFVNEIDYYMGCQQREQKRKLTGRLPIVAEYLETRMGTSAVTSMLALNEYGGALILGLKRR | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Sesquiterpene cyclase; part of the gene cluster that mediates the biosynthesis of heptelidic acid (HA), a sesquiterpene lactone that acts as an inhibitor of glyceraldehyde-3-phosphatedehydrogenase (GAPDH) and a growth inhibitor of the salt-tolerant lactic acid bacter... |
P49008 | MKRLTFGACICCLLSLMACSQKAKQVQIPEYDKGINIIPLPMQLTESDDSFEVDDKTTICVSAEELKPIAKLLADKLRASADLSLQIEIGEEPSGNAIYIGVDTALPLKEEGYMLRSDKRGVSIIGKSAHGAFYGMQTLLQLLPAEVESSNEVLLPMTVPGVEIKDEPAFGYRGFMLDVCRHFLSVEDIKKHIDIMAMFKINRFHWHLTEDQAWRIEIKKYPRLTEVGSTRTEGDGTQYSGFYTQEQVRDIVQYASDRFITVIPEIEMPGHAMAALAAYPQLACFPREFKPRIIWGVEQDVYCAGKDSVFRFISDVIDEV... | Catalytic Activity: Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
Location Topology: Lipid-anchor
Sequence Mass (Da): 87661
Sequence Length: 777
Subcellular Location: Cell outer membrane
EC: 3.2.1.52
|
P48823 | MSFITSAHATAAQVPLTTSQMLGQKLMLDFRYYCGESKKPSGDCRAAMTTLPPELSELISRYDIGGAILFAENVQNTAQIISLTNALQSAAQQSKSQLPLFIAIDQEGGRVARINREQATSFTGNMSIGATYPKQGDIYATKVASAIGKELNSLGINVNFAPTVDVNSNPNNPVINVRSFSENPTVVTKLGLAQVKAFEAAGVLSALKHFPGHGDTHVDSHTGLPRVDHDRDKINQQDLLPFAEIIKASPPGMIMTAHIQYPALDNSKVVNSQGESMIRPATMSYQIMTQLLRHELGYQGVTVTDALDMAGISDFFNPVD... | Function: Most active towards p-nitrophenyl-N-acetyl-beta-D-glucosaminide(PNP-beta-GlcNAc) and diacetylchitobiose.
Catalytic Activity: Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
Sequence Mass (Da): 64539
Sequence Length: 598
EC: 3.2.1.52
|
Q54K55 | MIILKRNIVFLLIIIIVLGIFIATSIEIKNYKLSLNQNKNEISKNPPIWPAPFYGQFGNNSILISKEFNFTIISDSTLLLNKTLSKYYNLIFTQDNLINSSSNTLNKLNINLKSKNEILKFGFDESYKLIIKNNENSKLEGNTVYGIMRGLETFYQLIKYNFSDNSYFIENCLPLIINDKPRFPHRGVMLDTSRHFYSVDTILKVIESLSYNKFNTLHWHIIDSQSFPLSSKSYPNLINGAWSKSEIYSYHDIKRIIKYGKENGIRIQLEIDMPGHAKSWSVGYPDLLPHGWNDSTTTIKCPDYDVPLDPSSPLSLPISF... | Function: Responsible for the degradation of GM2 gangliosides, and a variety of other molecules containing terminal N-acetyl hexosamines.
Catalytic Activity: Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
Sequence Mass (Da): 64555
Sequence Length: 560
Subcellular Lo... |
Q54K56 | MKLKFIFLILFFIIGNSIGIKISKEINKIKLNDISIDGEILLNKSSDSSSSQSSKIINIWPMPKKVLNGDITVYISPHFQFTTNLTKSTTLKKAMDRYYKLIFTEDSKSHSGISILNEIKILVKSEDETLQIGFDESYEIYIDDSGDDGGKIIAETVYGAIRGLETLYQMIGFDYQREYYQIKHCPWIIQDSPRYPHRGVMLDTSRHFYSVDVLKEFIEALAYNKFNVFHWHAVDSQSFPLTSTTFPKITKGSWSSQEIYSTRDIKEIIQHAKEYGIRVELEIDMPGHAYSWGIGYPSVLPANFSHSIQCQQPCPTECNI... | Function: Responsible for the degradation of GM2 gangliosides, and a variety of other molecules containing terminal N-acetyl hexosamines.
Catalytic Activity: Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
Sequence Mass (Da): 64566
Sequence Length: 564
Subcellular Lo... |
Q86M34 | MIVLLLLISYCFAGNGVNVKNQLLLMPYPTTVNAQFGSNDCVEATSNIKMVLSNNCQNDPNCLSFMTFNFNHTITYPLQRQRNLEDFRVSIFAPIDIEEMKGNVVYSANTVNIELTGNNIEEIYPPLKIGIDESYSLDVTKEGIKISATTVYGARLGLETLIQMLRPYQGKYIIKHIPIMIEDKPRLQWRGLMIDVARNSFSRSAFVKIINAMAAIKANVLHIHLSDAQTFMFESKEYPELSKKGAFFQNKVLTQSFIKQLVQYGAKRGVIVYPEIDTPAHTASWNAGYPGVVADIWDYIVSSSMRYGENVLALNPANEK... | Function: Hydrolyzes the non-reducing end N-acetyl-D-hexosamine and/or sulfated N-acetyl-D-hexosamine of glycoconjugates . May contribute to amoebic pathogenicity and may be involved in the destruction of extracellular matrix components (Probable).
PTM: Glycosylated.
Catalytic Activity: Hydrolysis of terminal non-reduc... |
P49614 | MRHRGLGLAALLALLAAVAPRSSAAAGAALWPMPLSVKTSPRLLHLSRDNFSIGYGPSSTAGPTCSLLQEAFRRYHEYIFGFDKRQRRPAKPNSAIELQQLLVTVVLDSECDLFPNITSDESYTLLVKEPVAFLKANRVWGVLRGLETFSQLIYQDSYGTFTVNESDIIDSPRFPHRGILIDTARHFLPVKSILKTLDAMAFNKFNVLHWHIVDDQSFPYQSVTFPELSNKGSYSLSHVYTPNDVHTVIEYARLRGIRVIPEFDSPGHTQSWGKGQKDLLTPCYNEHKQSGTFGPINPILNSTYNFLSQFFKEVSMVFPD... | Function: Hydrolyzes the non-reducing end N-acetyl-D-hexosamine and/or sulfated N-acetyl-D-hexosamine of glycoconjugates, such as the oligosaccharide moieties from proteins and neutral glycolipids, or from certain mucopolysaccharides. The isozyme B does not hydrolyze each of these substrates, however hydrolyzes efficie... |
P07686 | MELCGLGLPRPPMLLALLLATLLAAMLALLTQVALVVQVAEAARAPSVSAKPGPALWPLPLLVKMTPNLLHLAPENFYISHSPNSTAGPSCTLLEEAFRRYHGYIFGFYKWHHEPAEFQAKTQVQQLLVSITLQSECDAFPNISSDESYTLLVKEPVAVLKANRVWGALRGLETFSQLVYQDSYGTFTINESTIIDSPRFSHRGILIDTSRHYLPVKIILKTLDAMAFNKFNVLHWHIVDDQSFPYQSITFPELSNKGSYSLSHVYTPNDVRMVIEYARLRGIRVLPEFDTPGHTLSWGKGQKDLLTPCYSRQNKLDSFG... | Function: Hydrolyzes the non-reducing end N-acetyl-D-hexosamine and/or sulfated N-acetyl-D-hexosamine of glycoconjugates, such as the oligosaccharide moieties from proteins and neutral glycolipids, or from certain mucopolysaccharides . The isozyme B does not hydrolyze each of these substrates, however hydrolyzes effici... |
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