entry stringlengths 6 10 | entry_name stringlengths 5 11 | protein_name stringlengths 3 2.44k | sequence stringlengths 2 35.2k | function stringlengths 7 11k |
|---|---|---|---|---|
Q9YEA0 | VATI_AERPE | V-type ATP synthase subunit I (V-ATPase subunit I) | MLLPRMLEEVVLAVPARDYDRVVAGLAVEGIFHVDSPPQGVKGEVDRSYRALLTQASERSSRIRQYFDLAGVEPYRVSGVEIEVGGWGESWKRYLEKYSGVEKFYSGLLEEYSEAEARLKELLDIEARIAPVAHLDVDIARLYRSGAFDFAVYYGSYSEGLESRVGEIVSRVGGLAAVEASGGSVVVAVAVPKGALSKISPEILRLNLSIYTPPEGVPGSPREAMEYIRGEKARLGRRLVSIQEMASERLGELAEFYTVVTAFENIFKFLVSTLRRGETRIVRGFVDVRDSGRLRSIVDRMTRGSYVLLSLGVRRGGEAP... | Produces ATP from ADP in the presence of a proton gradient across the membrane. |
Q9YEC1 | SECG_AERPE | Preprotein translocase subunit SecG (Protein transport protein Sec61 subunit beta homolog) | MSVRRRRERRATPVTAAGLLSFYEEYEGKIKISPTIVVGAAILVSAVVAAAHIFLPAVP | Involved in protein export. The function of the beta subunit is unknown, but it may be involved in stabilization of the trimeric complex (By similarity). |
Q9YEF2 | SAHH_AERPE | Adenosylhomocysteinase (EC 3.13.2.1) (S-adenosyl-L-homocysteine hydrolase) (AdoHcyase) | MAQGFKVRDLSLAGEGRMQIEWAERHMPVLMRLRSSMGGDKPLSGVRVAACLHVTKETAVLVETLRKWGAEVYLAPSNPLSTQDEVAAALAEAGIGVFAWRGMTPEEYKWALSTVAGREPDIVIDDGADLHVLLHEEMRSVGEKVWGGTEETTTGVIRLRALEREGRLLYPVIAVNDALTKFMFDNRYGTGQSTVDGVLRATNILIAGKTVVVAGYGWVGRGIAARFRGMGAKVVVTEVDPVRALEAAMDGFTVTTMDEAASLGDVFITATGNINVIDARHMEKMKDGAILANAGHFNVEINVAALEEMSVSKRRVRRYL... | May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine. {ECO:0000255|HAMAP-Rule:MF_00563}. |
Q9YEL4 | AROC_AERPE | Chorismate synthase (CS) (EC 4.2.3.5) (5-enolpyruvylshikimate-3-phosphate phospholyase) | MASRDSLGEVFRVSIFGESHGPGVGALVTGVPPGLEVDEAYINRELERRRPGGPYASPRREADRVEILSGVFRGRTTGAPILLFIRNVDVKPGFYEEFRYKPRPGHADYVAYERYLGHQDYRGGGIFSGRRTAALVAAGAIAKLVLARYGVRVYAYVKSIGGVEARVEPRDSEEFRRAIDRDPLKCPDPEASERMRRLVEEARREGDSLGSVVEAVAFNVPPGLGDPPLGGVDALLARAVMAIPAAKAVEFGEGFALAFMRGSEAHDSPRAVGGRIVHETNRSGGIVGGLTNGMPIVFRVAFKPPSSIPKPRRTVDLRSL... | Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a s... |
Q9YEM5 | RSMA_AERPE | Probable ribosomal RNA small subunit methyltransferase A (EC 2.1.1.-) (16S rRNA dimethyladenosine transferase) (16S rRNA dimethylase) (S-adenosylmethionine-6-N',N'-adenosyl(rRNA) dimethyltransferase) | MPPGSGRGGRRRAESLVREVLGLAGLRPSDRLGQHFLIDDRAVGEFLKPLEKAAAEGIREALEIGPGAGSITLPAAEVLDRIVAVELDNRLASALSRLAPARVAVITGDGVSHAAASQAPLVFSNTPFNLSPAIVEALAVNNRVAAAVLGVQYEVARRMTARPGSRDYSRLSVLVSLVFHAELAGVVRPQAYYPRPQVLTAVVTLRRRRRWRSLYARALELAGCAFTQRNKKASKVLRRCLEAAGCAPPPWLDSLGDARVWMLRPEDFVGLAEACRG | Specifically dimethylates two adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits (By similarity). |
Q9YEQ4 | RL37_AERPE | Large ribosomal subunit protein eL37 (50S ribosomal protein L37e) | MGKGTPSMGKHGRSKTHIVCRRCGRRSYNVAKGYCAACGFGRSRRMRRYSWQNKKWNRVRVV | Binds to the 23S rRNA. |
Q9YES0 | RTCA_AERPE | RNA 3'-terminal phosphate cyclase (RNA cyclase) (RNA-3'-phosphate cyclase) (EC 6.5.1.4) | MGSGEWVVVDGSMGEGGGQILRTAVALAAVLGRPLRIVNIRAKRRPPGLRPQHLTAVRAVAAISGGRLRGAEVGSTSLEFTPGRVRGGRYRFDVGTAGSVALIIQALAPLLAYSDSPVEVELTGGTDVPMAPTIDYMREVFASILAMLGYEIEIRVLRRGHYPRGGGRVVVRVPDPPGGFRARSFVERGPLKGVYVRSHAVKLPGSIAERQARSAASLVRERLGVDPIVEIEAYKPHRDPHLGPGTGVLVWAVFGETVMGGDSIGKKGKPAEVVGREAAESLLEDMATGAALDRHMSDMAPVYLALAGGVSTVFGARLTG... | Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in t... |
Q9YES9 | NEP1_AERPE | Ribosomal RNA small subunit methyltransferase Nep1 (EC 2.1.1.-) (16S rRNA (pseudouridine-N1-)-methyltransferase Nep1) | MKIVFLECSVELVPRSLWSHPQVLKSARRYGIEPGDLLLDKSLHYNAMAELPAKWKRGRPDILHVALLTTTDSPLYNEGLLRIYFQVYDGRLFEVGTGVRVPKNYERFRGLVAQLLKTERVPPGEGEALIRLHSRSLAEFVEREGRFILMWEKGSPTTTTYVAARALSTGLPIGVGCFPRGEFKRSTLRKASEAYSIMGGAPLKTWGVASRIVYALERLKSPFT | Methyltransferase involved in ribosomal biogenesis. Specifically catalyzes the N1-methylation of the pseudouridine corresponding to position 914 in M.jannaschii 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_00554}. |
Q9YEY2 | CREN7_AERPE | Chromatin protein Cren7 | MSQKQLPPVKVRDPTTGKEVELTPIKVWKLSPRGRRGVKIGLFKSPETGKYFRAKVPDDYPETG | A probable chromatin protein, binds double-strand DNA without sequence specificity. Constrains negative DNA supercoils. {ECO:0000255|HAMAP-Rule:MF_01387}. |
Q9YEZ5 | PCNA3_AERPE | DNA polymerase sliding clamp 3 (DNA polymerase sliding clamp B2) (Proliferating cell nuclear antigen homolog 3) (PCNA 3) | MADARFYFSDARTWRYMVASIEKIIEEGVFVATGEGLSLRALDTSHVAMVDLYYPNTAFIEYDIGGESVEFGVSFDLLSKVLRRARKEDELVLEVEGSRLAVKLKSRGERTFRIPQVVMTYEKLPEPKVSFTVRARMLGSTFREAVRDLEPHSETLTLRALEDALLLVGSSEMATVEIELSQSRGSLLDYEAESQDRASYSIEYFSEMLSAAQAADAVVVSFSEDAPVRVDMEYLGGGRLTFYVSPKIE | Sliding clamp subunit that acts as a moving platform for DNA processing. Responsible for tethering the catalytic subunit of DNA polymerase and other proteins to DNA during high-speed replication. {ECO:0000255|HAMAP-Rule:MF_00317}. |
Q9YEZ8 | PRIS_AERPE | DNA primase small subunit PriS (EC 2.7.7.-) | MVEARGGLDPRRLFKAYYSLSPPVEEPRDIAYREFAFQLFDGDVYVRHIGFDSMEELLSYMAREAPKNAYYSVARYSLPTARSMEEKGWLGSELMFDIDVDSLEGCGEVLGDSCLSRGYKQAVRLVEALYRDFGVPSTLYFTGNRGFHVLADCGWCRRLGREERREIARYFTLEGLRLELIIPRPGRRGVRPAPPSPDDPGLRGWIARAALERGVDLSAVHEAIEDLLDDVRVAIDVKVTQDISRLARIVGSLNGKAGLLVARLGLEGFHPGDWLSPFRGEVEFRASARLEESRILGRTVSLEPGRVYSMPAHIAVLLQL... | Catalytic subunit of DNA primase, an RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. The small subunit contains the primase catalytic core and has DNA synthesis activity on its own. Binding to the large subunit stabilizes and modulates the ac... |
Q9YF00 | RL44E_AERPE | Large ribosomal subunit protein eL42 (50S ribosomal protein L44e) | MKFPKRIRTYCPRCNTHTEHRVAQYRAGKRRAMALGERRYRRKQEGYGSQRRPEQKRFAKVTKKQVLVITCTVCGRKRPFLGIRLKRLELVDVVR | Binds to the 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_01476}. |
Q9YF02 | IF2A_AERPE | Translation initiation factor 2 subunit alpha (aIF2-alpha) (eIF-2-alpha) | MSEEGGVEVKLLKPRKPLPDVGEIVVGTVQEVHDYGAYLILDEYGGVRAFLPWSEIASRAVRNIHAVLKPRQKVVVKVIRVYKKRGQVDVSLKRVMDSEKKRKMMFYKRYLKAATLVELIAEKLGKSVDEAYREVLWKLEDAYGDPMKGLEAAVLQGREALEKAGVPEEWIEPLLETAKTHVRVKTVKITFYLTLRSMAGDGVERVRKVLEAAKSQIESFKDSKVVARIYTVGAPKYRVELQGYNYKTLEKALEKMVEAARKTASKLGVEFSFERED | eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. |
Q9YF05 | CDPAS_AERPE | CDP-archaeol synthase (EC 2.7.7.67) (CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase) | MALELAVDWRIDNILEAIILMLPAMIANATPVVAGGRRPVDMGVVLPDGRRLLGDGKTIEGLLAGFAAGSAAGVLAALASGNMLLAVHSPAIALGALAGDMAGSFVKRRLGIERGRPAPLLDQLDFYLGALAVSIALGYTWTPRVAVEAAAAVLLLHLAANITAYLLGLKKVPW | Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids. {ECO:0000255|HAMAP-Rule:MF_01117}. |
Q9YF31 | VATE_AERPE | V-type ATP synthase subunit E (V-ATPase subunit E) | MAKVQGDPRRFADTVLEKPFKEALARVEEAREAGLKLVEEAYKSALSAARKRLESRVEEARERLQGLKSKADLEVRTEAERVKDELVSRLIEEALAEFRRRKAGMESYRQYLERVLGSAAGESGGSVAKVLCAPEDEEIVREVLGKLGLDGVSVEAVEGIYGGVVVELAEGARLDYTVNNIIAAEEPRLRRAVKRALFEA | Produces ATP from ADP in the presence of a proton gradient across the membrane. {ECO:0000255|HAMAP-Rule:MF_00311}. |
Q9YF35 | VATA_AERPE | V-type ATP synthase alpha chain (EC 7.1.2.2) (V-ATPase subunit A) | MAVKGSIVRISGPLVVAEGMSGAQMYEMVYVGEDRLIGEITRIRGDRAFIQVYESTSGLKPGEPVVGTGAPLSVELGPGLLGTIYDGVQRPLPIIAEKVAEVDPRRRMFVERGIQAPPLPRDRKFHFKPEPLKEGDKVEGGDALGRVPETSLIEHVVMVPPGIRGRLKWLASEGDYSVEDTIAVVERDGRDVEIRMHQRWPVRIPRPFKEKLEPQLPLITGVRIIDTFFPMAKGGTGAVPGGFGTGKTVTLHSLAQWSEARVVIYIGCGERGNEMTEVLERFPQYKDPWTGKPLMDRTVLIANTSNMPVAAREASIYVGI... | Produces ATP from ADP in the presence of a proton gradient across the membrane. The archaeal alpha chain is a catalytic subunit (By similarity). |
Q9YF36 | VATB_AERPE | V-type ATP synthase beta chain (V-ATPase subunit B) | MALGVREYRNISEIKGPLLVVEGVSRVAYDEIVEVETAAGEKRRGRVLEVGMGYAVVQVFEGTTGISPTGTVVRFMGRPLEIPVTEDMLGRIMNGLGEPIDGGPKIDADERRDVNGAPLNPAERAYPEDFIQTGVSAIDGMNTLVRGQKLPIFSGAGLPHNRLAAQIARQATVRGEEEEFAVVFSAIGIKYDDFLFFKKFFEETGALGRVAMFVNLADEPAMIRLITPRAALTLAEYLAYERDMHVLVIITDMTNYAEALREISAAREEVPGRQGYPGYLYSDLASIYERAGRVKGKKGSITQMPILTMPNDDITHPIPD... | Produces ATP from ADP in the presence of a proton gradient across the membrane. The archaeal beta chain is a regulatory subunit (By similarity). |
Q9YF38 | VATD_AERPE | V-type ATP synthase subunit D (V-ATPase subunit D) | MAVDPRKVLPTKINLIRLRRELAMLRRIRRVMEEKREVILHYITSMAAEYVRYQREVYSELERIYQNYYLGVAAEGIERARAFTAPAEGSLEVDVSTRTLFAVKTPVFSLREETVPPLPLPAGSDPKLVQSILDMRSILDKLLKLAEYEETLQRLISELKDTQRLINALDYVILPSYQNAIKFIKLVLEDRMREDFVRLKIIKRKMEAKTQ | Produces ATP from ADP in the presence of a proton gradient across the membrane. |
Q9YF74 | RS19_AERPE | Small ribosomal subunit protein uS19 (30S ribosomal protein S19) | MAFEMRPEWKKFRYRGRTLEELLKMDIEELARLFPARQRRSLLRGLTPAQQKLLLKVRKIRRRLEEGRLKRPPVIRTHVRDMVILPEMVGLTIAVYNGKEFIPVKIVPEMIGHYLGEFSPTTRIVQHGEPGLKATRSSLHVASK | Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA. |
Q9YF76 | RL22_AERPE | Large ribosomal subunit protein uL22 (50S ribosomal protein L22) | MPRWGYSVKLRDESEVAKAVLRNVPVHPKIMAEVARAISGMRVDEARRYLRAVIEKREAVPFRRAHGKQAHRRGLADKWGWPVGRYPVKAARYMLKLLDNVEANAANKNLDVERLKIIHVAAHKGITLKRWMPRAWGRATPRNRVHSHIEIMVREV | This protein binds specifically to 23S rRNA. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome. {ECO:0000255|HAMAP-Rule:MF_01331}. The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended bet... |
Q9YF78 | RS3_AERPE | Small ribosomal subunit protein uS3 (30S ribosomal protein S3) | MPTKVVKHFLNQGLLRTKIDEWLAQNFYEAGYSRVKVVQTSLGTNITIWAERPALIIGRRGATIRRLQEVFQTVFGLPNPRIRVEQPENPMLDARVQAFRIARSIERGIHFRRVAFAAINRIMSNGALGVEITISGKLTSERARFEKFKAGKVYKSGHKVDELVDRASAYARLPKGVIGVDVIIVKPGKPGDHVRIKSEEEVKDVVDAIRSEIESLGLQEETASTLREHMEAARPGEEHEEDREES | Binds the lower part of the 30S subunit head. {ECO:0000255|HAMAP-Rule:MF_01309}. |
Q9YF79 | RNP1_AERPE | Ribonuclease P protein component 1 (RNase P component 1) (EC 3.1.26.5) (Rpp29) | MKGRRPSHRRQLIPPLLTGLRVKVLAHSDPSLEGLEGWVVVEEARSLRILTLEGRVSTVLKDLAVIEVEAPGGEYIRISGRVLIGNPLDRVKEYRWRVSRRCRSSSRLKT | Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. {ECO:0000255|HAMAP-Rule:MF_00754}. |
Q9YF81 | RS17_AERPE | Small ribosomal subunit protein uS17 (30S ribosomal protein S17) | MPKFKQVKNLKIPGVEPPEKVCSDPNCPWHGTLRVRGVLLEGVVAKARARRMVVVQHVYLYYDKKYNRYERRSKKIHAHLPDCISVKEGDVVVIGETMPISKTVKFTVLGVKRR | One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA. {ECO:0000255|HAMAP-Rule:MF_01345}. |
Q9YF82 | RL14_AERPE | Large ribosomal subunit protein uL14 (50S ribosomal protein L14) | MAKKKKYGVVVSRYGVNTGLQVGSYVPVADNSGAKEVMIISVPQVKTRLRRLPSAGVGDLVVVSVKKGTPQMRRQVVYAVVVRQRRPFRRPDGTWVSFEDNAVVIVNPDGTPRGSEVRGPIAREAAERWPRVAKIATMIV | Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome. {ECO:0000255|HAMAP-Rule:MF_01367}. |
Q9YF83 | RL24_AERPE | Large ribosomal subunit protein uL24 (50S ribosomal protein L24) | MPVLTRSRQPRKQRRALYRAPLHARQKLVSATLSPELREKYGVRSLPVRKGDKVRVMRGDFKGHEGKVVKVDLRRLRIYIDGVTVTKADGTPVFRPIHPSNVMIVELDLSDEYRKKMIERRAAGRRGGGNSE | One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. {ECO:0000255|HAMAP-Rule:MF_01326}. Located at the polypeptide exit tunnel on the outside of the subunit. {ECO:0000255|HAMAP-Rule:MF_01326}. |
Q9YF87 | RL5_AERPE | Large ribosomal subunit protein uL5 (50S ribosomal protein L5) | MSAKAQSLPIPPERVSEILDEWKRSPMRRPRIVKVTVNISIGQSGERLQRAAEVLEELTGQKPVFRKAKRTIRAFGVRKGENIAVMVTLRGEKALNFLKRALDAVGHRIKTSSIDEHGNVSFGIEEHILIPGVKYDPRVGILGMDVAITIQRPGHRIVERRRQRRGHIPRRHRVTREETMVLLNQLFGVTFV | This is one of the proteins that bind and probably mediate the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits this bridge is implicated in subunit movement.... |
Q9YF89 | RS8_AERPE | Small ribosomal subunit protein uS8 (30S ribosomal protein S8) | MVMLDTLANAMAAIKNAEMRGKGEAIIMPSSKLIANVLRILEKEGYIGGFEYIDDGRWGKFRVKLLGRINDIGVVKPRTPVSYRELAKMPEHLRKYLASRDVGLLILSTPQGVMTHREALKRKIGGIVIAYVY | One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit. {ECO:0000255|HAMAP-Rule:MF_01302}. |
Q9YF91 | RL6_AERPE | Large ribosomal subunit protein uL6 (50S ribosomal protein L6) | MAKDVHVVERVEVPEGVTVSIDGMRVKVSGPKGEVERDFSHARGVLIRLEDNSVVVESFFAKARQRALVGAIAGHIRNMIKGVQGGFRYKLKIMYSHFPINVKVEGDKFIISNFLGEKGLRIARIMPGVKVQVKGSDVIVEGIDVEKVAQTAANIELATKVKDKDRRKFMDGIYIYEREVIA | This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center. {ECO:0000255|HAMAP-Rule:MF_01365}. |
Q9YF93 | RL19E_AERPE | Large ribosomal subunit protein eL19 (50S ribosomal protein L19e) | MDYRFQRRLAAEILGVGESRIWISPDPELREEIEGAVTKADVRALIKRGVIKVLPEKGNAGHASKVRHLQRRKGRRRGMGRRKGVATARLDPKERWMHRIRKIRRYLRYLRDKQVIDRKTYRRLYMLAKGGTFRDLASLKRYMADRGLVPEEKIR | Binds to the 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_01475}. |
Q9YF94 | RL18_AERPE | Large ribosomal subunit protein uL18 (50S ribosomal protein L18) | MGRGPRYRVPLRRRREGKTNYYRRFRLVKSGKPRMAVRISNEYLWVQFLEARIEGDRVIAAAHSRELIKKFGWKGDGNNTCAAYLTGYLAGLRALEKGVREAVLDVGLHKPVKGSRVFAALKGALDAGVEIPHSEEILPGDERVRCEHIAQWAEALKEENAELYQRQFSRYLDRGLNPEELPGHVEEVKKAIEEAYKHVAEETAAEGEEVEVKA | This is one of the proteins that bind and probably mediate the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. {ECO:0000255|HAMAP-Rule:MF_01337}. |
Q9YF95 | RS5_AERPE | Small ribosomal subunit protein uS5 (30S ribosomal protein S5) | MSQREAGQVDLEAWQPRTRVGRLVKEGKIKSIDEIFRRNLPILETEIVDYLLPGLDHEVIDVSIVQKMTDAGRITRFRAVVVVGNKDGYVGLGKGKARQFRFAIEKAIRNAKLNIIPVRRGCGSWECTCGEAHSVPFTVRGKSGSVEVILKPAPKGTGLVAGDVAKVVLRLAGISDVWTFTKGETRTSYNFARATYLALRNTYRFVTPADWAEARLRL | With S4 and S12 plays an important role in translational accuracy. {ECO:0000255|HAMAP-Rule:MF_01307}. |
Q9YF98 | RL15_AERPE | Large ribosomal subunit protein uL15 (50S ribosomal protein L15) | MVVRRRKKSRKLRGRTRTMSWGRIGQHRKSGSKGGYGAAGLGKHEWTWTIKYAPTWYGKKGFNPPRIRAGLEVTTINVGQLDEIAALLEAQGKAEKEDGKIVVNLEKLGIHKLLGEGRVARPLKVITPLASELAIKKIEEAGGEVIVTRATREEAEES | Binds to the 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_01341}. |
Q9YFJ2 | DPCKG_AERPE | GTP-dependent dephospho-CoA kinase (EC 2.7.1.237) (Dephospho-coenzyme A kinase) (DPCK) | MSVALSIPLLSLPEDMREALAAAAGPVYSGDRFRRQLLQTPCSGVACIGDYVSQACIATLSTAWTGPLILVVDGKTRRESWRDMVVPQGFRVHRVRSPPGSLSLEAYTTICKLMEEYGRHVVFVEGEEDLIALAALDCGIDWTVVYGLPGVGGVVVHRCLRKPGLENSSVLAFKPGTGVHHQSSP | Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA). {ECO:0000255|HAMAP-Rule:MF_00590}. |
Q9YFM0 | RL23_AERPE | Large ribosomal subunit protein uL23 (50S ribosomal protein L23) | MKPEEVIIRVYVTEKTTRMLEEENTLTFIVRREATKNDVKRAVEQLFGVKVEKVRTLITPRGYKKAYVKLAPEYKALDVATKLGAV | Binds to 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. {ECO:0000255|HAMAP-Rule:MF_01369}. |
Q9YFM1 | RL4_AERPE | Large ribosomal subunit protein uL4 (50S ribosomal protein L4) | MAYTYMTLYMEQEKIVPVYDERGGEKDSVVLPQIFRFPVRKDLIRRAFLSEFTARLQPKGRDPMAGKRTSAVSLGVGRGVARVPRIKGSLRAALVNMARGGRAAHPPRVEKVLKEYINKKEKRLATISAISATSREDLVRQRGHRFSAETLPIVLDSSVLAKISTAREARSLLESVGVYEDVLRAKEGKRYNAGKGKMRGRRYKVPKSVLFVLEDPRSPLALAVKGMPGVDVVTPTLLSVLHLAPGGHPGRLTIYTTEALKLLSRRFEVTLP | One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome. {ECO:0000255|HAMAP-Rule:MF_01328}. Forms part of t... |
Q9YFM2 | RL3_AERPE | Large ribosomal subunit protein uL3 (50S ribosomal protein L3) | MGARKKRAPRRGSLGFSPRKRASRLVPRVKRWPEVDIGKPVPLAFLGYRAGMTHVFMVDDRPGRPTSGKEIFVPVTIVETPPMFVAAVRLYGYDPNRGRYSLGEAWAQPPPELELQRRISTLGSFDTDKMLKSLEERLDKAEDVRLIAASQPKLAGGLSKKKPDLLEIKVGGVSDVTKLFDYAKDVLGNLIAVNDVFEEGQLVDVIAVTKGKGFQGVIKRWGVKELPRWHKHRKGSRRIGARSHGRSTFWETPQAGQTGFHRRTEYNKRILMIDDDGYKVTPAGGFLRYGVVRSTFVMLSGSIPGTPKRPIVMRWAIRPP... | One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. {ECO:0000255|HAMAP-Rule:MF_01325}. |
Q9YFN1 | RL2_AERPE | Large ribosomal subunit protein uL2 (50S ribosomal protein L2) | MGKRLRQQRAGRGTPTYRSRAHIHPGPAKYPPLSGDTLRGKVVELIHDPGRYVPLARVVREDGVEFLMPAAEGMYVGQIIEIGPAAKPEAGNILPLGKIPEGTEVFNVELRPGDGGKLARQAGSYALVVGRAGAKTILRLPSGKDKEVPNDSRATIGIPAGAGRIEKPIMKAGFAYHKWKVKARKWPRVRGVAMNAVDHPFGGGRHQHKGRPSTVARTAPPGRKVGHIAARRTGRRKR | One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome. {... |
Q9YFP5 | KPTA_AERPE | Probable RNA 2'-phosphotransferase (EC 2.7.1.-) | MAEELPELALCCDGTVVEGRSNCRCKARAVLPGGMRVRLSKTLAGILRHHPGRYGVRLTREGWARVSEVVEGLRKAGWSWVEEWHIVGVALHDPKGRYELRNGEIRARYGHSIPVNVEPLPGEPPPILYHGTTEEALPLIMERGIMRGRRLKVHLTSSLEDAVSTGRRHGNLVAVLLVDVECLRRRGLKVERMSKTVYTVDWVPPECIAEVRRESLGRSL | Removes the 2'-phosphate from RNA via an intermediate in which the phosphate is ADP-ribosylated by NAD followed by a presumed transesterification to release the RNA and generate ADP-ribose 1''-2''-cyclic phosphate (APPR>P). May function as an ADP-ribosylase (By similarity). |
Q9YFQ1 | NAC_AERPE | Nascent polypeptide-associated complex protein | MLPVNPRDLEKMMRRLGIKVEQLSADEARIVLGSGETMVFRSPTVIVMRAKGQPPMVYLVGDYTVEKPREETAAEITEEDVALVAEQAGVSMEEARKALEESGGDIAEAILRLKGEE | Contacts the emerging nascent chain on the ribosome. {ECO:0000255|HAMAP-Rule:MF_00814}. |
Q9YFT8 | PCNA1_AERPE | DNA polymerase sliding clamp 1 (Proliferating cell nuclear antigen homolog 1) (PCNA 1) | MFRYEAKVFKELVDSVSKILDEGLFIITGEGLRLRGMDPARVALVDIEIPSSSFFDFYMAGDVERVELGVNMETLKGVVARAKKGDQLEVRVREDKVLFIVESVVLRRYLLPNLEVIVDVPEDISLEFDATATVIADVVKKTLRDVELVGDIVEFDAGEDYLSIRSVGPERRRVETRLTRESPALIDLEVKEPATSRYDVGYLKRMLGVAKIAESIELSFSTDKPLKMVFKSPDGSRVTYLLAPSTG | Sliding clamp subunit that acts as a moving platform for DNA processing. Responsible for tethering the catalytic subunit of DNA polymerase and other proteins to DNA during high-speed replication. {ECO:0000255|HAMAP-Rule:MF_00317}. |
Q9YFV2 | ARCH_AERPE | Protein archease | MQCGGWMHEEHTADVLVIAYGRTLEEAFENAARGVYEVVTDTSRVEPRRRVDASIEGIDLENLLYRFIENLIAYTDSEGLVFGLFRVCKIECNGESCSIVASAWGEEFDPSRHEHRTIVKAMTYADMEIKEENGCWRVQFVVDI | Activates the tRNA-splicing ligase complex by facilitating the enzymatic turnover of catalytic subunit RtcB. Acts by promoting the guanylylation of RtcB, a key intermediate step in tRNA ligation. Can also alter the NTP specificity of RtcB such that ATP, dGTP or ITP is used efficiently (By similarity). |
Q9YFV3 | AMZA_AERPE | Archaemetzincin (EC 3.4.-.-) | MESSLTFLLLPVGFPGEVLVTLARRAREAMPVPSLWLASTDPLEPPIEAYSWERMQFDAEKVNEHIHSVLYDYVREGIRIIGVVDADGYIPGFNFVFGLASTALGVATVYTRRLKTGGNGLYTERLLKEVLHEAGHLLGLDHCSNRECVMSFSRSVEEVDRKAPLFCSSCKAKLVLKYGSRGQ | Probable zinc metalloprotease whose natural substrate is unknown. {ECO:0000255|HAMAP-Rule:MF_01842}. |
Q9YFZ1 | RAD50_AERPE | DNA double-strand break repair Rad50 ATPase | MYVLKRLELRNIMSHFNTSIDFREGFTAIVGRNGAGKSTILEAILFSITPHQAPRRSSMISENSSRGEIYLALQSSEGRLLELRNKLIRRGGGTNTEAAIITLEGRRIASKPTGYKEEIHKILGLRGLPNPASYIEKAIIISQGGLQTLAEILSEPKELRDLLDAALGYALLKQAISNIGDVVLGVSPDGSPVKLGSKSITRLQSGYMTLRNEVLGVDREIREASKRLEELEREREELERRARDLESEAKALQSEIGKLETMEEMLVNVTSMIRSERSKLDTINTRLRYAESKISSIDDLEKRRAELRAKASLAHEVAEL... | Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA. Rad50 controls the balance between DNA end bridging and DNA resection via ATP-dependent structural rearr... |
Q9YG32 | DUT_AERPE | Probable deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) (EC 3.6.1.23) (dUTP pyrophosphatase) | MFLSGRDLVLLGVVKGHSNGAIQPAGVDLSVGEIESLADAGFLGEEDKIMPKGDRIQCEYGVCELEPGAYRLRFNEVVSIPPGHVGFCFPRSSLLRMGCYLGCAVWDPGYTGRGQAMLLVANPHGLRLEMGSRIAQLVVARVEGPLTSLYKGDYQGEGL | This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. {ECO:0000255|HAMAP-Rule:MF_00635}. |
Q9YG68 | PCKA_AERPE | Phosphoenolpyruvate carboxykinase (ATP) (PCK) (PEP carboxykinase) (PEPCK) (EC 4.1.1.49) | MEDVVKALAKEVLSSADIEWNPPPGLLRRESSRYAGFTKTGSLAVVSSKARARRPDRTRVKYLRDEGFDRLVVDAWDYVVKASFYAVERCVGSGDRRFRILALVEKSYPHLALMSHLNFFPCGSTGSYDMVTIDVPSYSDVWMLVERRSNSTLVLGSDYYGELKMSFLRLAMNEARDRHLGVGLHAASKLYRVRVEGSMREVGVLVFGLSGTGKTTLTVEDHGLREPEYVRVMQDDIVILDWRGVAHGTEMNLYPKTDSVPELKKLEPAVLHPDAVLENVVVKSDGTPDFTDLSLTRNARALAIREAIPIASGSVDLMGT... | Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA. {ECO:0000255|HAMAP-Rule:MF_00453}. |
Q9YGA3 | MTBC_METTE | Dimethylamine corrinoid protein | TLQGQKDVIELLKEEGLRDKIKVMVGGAPATQAWADKIGADCYAENASEAVAKAKELLA | Acts as a methyl group carrier between MtbB and MtbA. |
Q9YGA9 | TRPA_THEKO | Tryptophan synthase alpha chain (EC 4.2.1.20) | MFEKGSLIPYLTAGDPSVEKTLEFLLAVEEFAGLIELGIPFSDPMADGKTIQESHYRALRNGFKLDDTFRILREFRRHSSTPVILMTYYNPVFRTGVKKFLGEAKASGADGILVVDLPVSHAGEFLDAAKEEGLKTVFLAAPNTPDERLREIDKASTGFVYLISLYGTTGARDRLPETAFEFVRRARKICNNKLAVGFGVSRREQVEELLKAGADGVVVGSALIELISRSENPVEELRRKVAELSGYSRAL | The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. {ECO:0000255|HAMAP-Rule:MF_00131}. |
Q9YGC2 | 3S11_LATLA | Short neurotoxin OKI-17/NCA-06 | MKTLLLTLVVVTIVCLDLGYTRRCFNHPSSQPQTNKSCPPGENSCYNKQWRDHRGTIIERGCGCPTVKPGIKLTCCQSEDCNN | Binds to muscle nicotinic acetylcholine receptor (nAChR) and inhibit acetylcholine from binding to the receptor, thereby impairing neuromuscular transmission. |
Q9YGC4 | 3S13_LATLA | Short neurotoxin OKI-01/OKI-19 | MKTLLLTLVVVTIVCLDLGYTRRCFNHPSSQPQTNKSCPPGENSCYNKQWRDHRGTITERGCGCPTVKPGIKLTCCQSEDCNN | Binds to muscle nicotinic acetylcholine receptor (nAChR) and inhibit acetylcholine from binding to the receptor, thereby impairing neuromuscular transmission. |
Q9YGC7 | 3S15_LATCO | Short neurotoxin NCA-02/NCA-05/UER-05 | MKTLLLTLVVVTMVCLDLGYTRRCFNQQSSQPKTTKSCPLGENSCYNKQWRDHRGSITERGCGCPKVKPGIKLRCCESEDCNN | Binds to muscle nicotinic acetylcholine receptor (nAChR) and inhibit acetylcholine from binding to the receptor, thereby impairing neuromuscular transmission. |
Q9YGH3 | SMS1B_CARAU | Somatostatin-1B [Cleaved into: [Pro12]-somatostatin-24; [Pro2]-somatostatin-14] | MQLLSSLVSLLLVLYSVRAAAVLPVEERNPAQSRELSKERKELILKLISGLLDGVDNSVLDGEIAPVPFDAEEPLESRLEERAVYNRLSQLPQRDRKAPCKNFFWKTFTSC | Somatostatin inhibits the release of somatotropin. |
Q9YGH5 | SMS1A_CARAU | Somatostatin-1A [Cleaved into: Somatostatin-26; Somatostatin-14] | MLSTRIQCALALLSLALAVCSVSAAPTDAKLRQLLQRSLLNPAGKQELARYTLADLLSELVQAENEALEPEDLSRAVEKDEVRLELERAAGPMLAPRERKAGCKNFFWKTFTSC | Somatostatin inhibits the release of somatotropin. |
Q9YGH9 | 3NO52_BUNMU | Long neurotoxin homolog NTL2 | MKTLLLSLVVVIIVCLDLGYTMQCKTCSFYTCPNSETCPDGKNICVKRSWTAVRGDGPKREIRRECAATCPPSKLGLTVFCCTTDNCYH | Exhibits M2 muscarinic acetylcholine receptor (CHRM2)-blocking activity, but has a weak binding activity toward nicotinic AChR. Moreover, it inhibits collagen-induced platelet aggregation. |
Q9YGI1 | 3NO23_NAJAT | Probable weak neurotoxin NNAM3 | MKTLLLTLVVVTIVCLDLGYTLTCLICPEKYCNKVHTCLNGEKICFKKYDQRKLLGKGYIRGCADTCPKLQNRDVIFCCSTDKCNL | Binds with low affinity to muscular (alpha-1-beta-1-delta-epsilon/CHRNA1-CHRNB1-CHRND-CHRNE) and very low affinity to neuronal (alpha-7/CHRNA7) nicotinic acetylcholine receptor (nAChR). |
Q9YGI2 | 3NO21_NAJAT | Probable weak neurotoxin NNAM1 | MKTLLLSLVVVTIVCLDLGYTLTCLICPEKYCNKVHTCLNGEKICFKKYDQRKLLGKRYIRGCADTCPVRKPREIVECCSTDKCNH | Binds with low affinity to muscular (alpha-1-beta-1-delta-epsilon/CHRNA1-CHRNB1-CHRND-CHRNE) and very low affinity to neuronal (alpha-7/CHRNA7) nicotinic acetylcholine receptor (nAChR). |
Q9YGJ5 | 3S1A2_NAJSP | Alpha-neurotoxin NTX-2 (NTX2) | MKTLLLTLLVVTIVCLDLGYTLECHNQQSSQAPTTTGCSGGETNCYKKSWRDHRGYRIERGCGCPSVKKGIEINCCTTDRCNN | Binds to muscle nicotinic acetylcholine receptor (nAChR) and inhibit acetylcholine from binding to the receptor, thereby impairing neuromuscular transmission. |
Q9YGJ6 | 3S1A1_NAJSP | Alpha-neurotoxin NTX-1 (NTX1) | MKTLLLTLLVVTIVCLDLGYTLECHNQQSSETPTTTGCSGGETNCYKKSWRDHRGYRIERGCGCPSVKKGIEINCCTTDRCNN | Binds to muscle nicotinic acetylcholine receptor (nAChR) and inhibit acetylcholine from binding to the receptor, thereby impairing neuromuscular transmission. |
Q9YGM9 | CAV2_TAKRU | Caveolin-2 | MGLEKEKLECSIIMDEDEFNRSIEPILSKKARLYSSAPDRDPHDINAQLKVGFEDVIAEPASAHSFDRVWIGSSATFELVKFIFYRLLTTLLAVPAAFILGVVFGVLSCIHIWLVMPVTRSFLMLLPSIQVVWKSVTDMFITPLFHSMGRSLSSIQVRTSDT | May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity (By similarity). |
Q9YGP6 | SLBP2_XENLA | Oocyte-specific histone RNA stem-loop-binding protein 2 | MPQTLLPEPWMVINGNTAMEDLFGVPSRSRFLSAPGLLSKEECPLNLSGNELRSEFAESISCTEQTYGANTVSVGVDTELDLLEFGRSDFRMATSPDAVGYETDEATLHRRQKQIDYGKNTVGYQCYLQQVPKTERKSGVHPRTPNKSKKYSRRSWDMQIKLWRRDLHAWDPPSQNSFQEDHSFKQTQRLLESWLQESNSLQNPDMDWLGLQLSSLQNLGYSEDQIQNSFDWLQFRGHTNDYTYPHWIGL | Binds the stem-loop structure of replication-dependent histone mRNAs. Is associated with translationally inactive histone mRNA stored in oocytes. Could be a specific translational repressor. Not involved in histone pre-mRNA processing. |
Q9YGT0 | HXCCB_DANRE | Homeobox protein Hox-C12b | MGEHNLFNPGFVGQLVNINARDAFYLSNFRASGGQLAGLQTLRLSRRDNVCSLPWNPSEACSGYPQSHISGPVTLNHTYNQSCDITRQEDNKCFYSDSACATSGGGDNNSTNLISKEGALDNSSVSITAENGQNNLNGMDNGGSYSKYDCLTPAEQPIPNPRLCRSLESVSGCSFINEGAKTSSGITHSLTSPDIQTSVAALNGGALWYPMHRQTRKKRKPYSKLQLNELEGEFILNEFITRQRRRELSDRLNLTDQQVKIWFQNRRMKKKRLLMREQALSYF | Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. |
Q9YGT4 | HXB6B_DANRE | Homeobox protein Hox-B6b (Homeobox protein Hox-A7) | MSSYFVNSTFPVSLPGGQESFLGQIPLYSSGYTDSLRHYPSATFGATNVQDKVYTSSYYQQAGGVFGRSGSTSACDYSTPNIYRTADRSCAIGSLEDSLVLTQDQCKTDCTEQGTERYFSTEDKPCTPVYPWMQRMNSCNGMPGSTGRRGRQTYTRFQTLELEKEFHFNRYLTRRRRIEISHALCLTERQIKIWFQNRRMKWKKENKAVNSAKVSDEEDGGKAG | Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. |
Q9YGT6 | HXA5A_DANRE | Homeobox protein Hox-A5a | MSSYFVNSFCGRYPNGVDYPLHNYGDHNSSGQCRDSTGMHSGRYACGYNGMDLSTGHSSPGHFLSSGERTQSYKDSPTATPVRYNQPVTASSAEPSSDHLPCSSLANSPVSEQSHRALKISLSSTAGSASKSFGTVLSREGVSKVSSSMEEEKPPGSGQTASQNVSEAPQIYPWMRKLHISHDNLAGPEGKRPRTAYTRYQTLELEKEFHFNRYLTRRRRIEIAHTLCLSERQIKIWFQNRRMKWKKDNKLKSMNMAAAGSGYRP | Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. |
Q9YGW8 | 3S14_LATLA | Short neurotoxin VAN-29 | MKTLLLTLVVVTIVCLDLGYTRRCFNQQSSEPQTNKSCPPGENSCYNKQWRDHRGTIIERGCGCPQVKSGIKLTCCQSDDCNN | Binds to muscle nicotinic acetylcholine receptor (nAChR) and inhibit acetylcholine from binding to the receptor, thereby impairing neuromuscular transmission. |
Q9YGW9 | 3S12_LATLA | Short neurotoxin VAN-10 | MKTLLLTLVVVTIVCLDLGYTRRCFNQQSSEPQTNKSCPPGENSCYNKQWRDHRGTITERGCGCPQVKSGIKLTCCQSDDCNN | Binds to muscle nicotinic acetylcholine receptor (nAChR) and inhibit acetylcholine from binding to the receptor, thereby impairing neuromuscular transmission. |
Q9YGX0 | 3S14_LATCO | Short neurotoxin NCA-04 | MKTLLLTLVVVTTVCLDLGYTRRCFNQQSSQPKTTKSCPLGENSCYNKQWRDHRGSITERGCGCPKVKPGIKLRCCESEDCNN | Binds to muscle nicotinic acetylcholine receptor (nAChR) and inhibit acetylcholine from binding to the receptor, thereby impairing neuromuscular transmission. |
Q9YGX1 | 3S1ED_LATSE | Short neurotoxin OKI-Ed | MKTLLLTLVVVTIVCLDLGYTRRCFNQQSSEPQTNKSCPPGENSCYRKQWRDHRGTIIERGCGCPTVKPGIKLRCCESEDCNN | Binds to muscle nicotinic acetylcholine receptor (nAChR) and inhibit acetylcholine from binding to the receptor, thereby impairing neuromuscular transmission. |
Q9YH95 | PAX5_XENLA | Paired box protein Pax-5 (XPax-5) | MEIHCKHDPFAAMHRHGGVNQLGGVFVNGRPLPDVVRQRIVELAHQGVRPCDISRQLRVSHGCVSKILGRYYETGSIKPGVIGGSKPKVATPKVVDKIADYKRQNPTMFAWEIRDRLLAERVCDNDTVPSVSSINRIIRTKVQQPTNQQIPPSNHSIASTGSVTQVSSVSTDSAGSSYSISGILGITSSNAETNKRKRDEGIQESPIPNGHSLPGRDFLRKQMRGDLFTQQQLDVLDRVFERQHYTDIFTSTEPIKPEQTEYSAMASLTGGLDEMKSSLTSPSSADIGGTVPGPQSYPLVTGRDLASTTLPGYPPHVPPA... | Probable transcription factor. |
Q9YH98 | EYA4_CHICK | Eyes absent homolog 4 (EC 3.1.3.48) | RKLAFRYRRVKELYNTYKNNIGGLLGPAKRDAWLQLRAEIEALTDSWLTNALKSLSIISTRSNCVNVLVTTTQLIPALAKVLLYSLGGAFPIENIYSATKIGKESCFERIVSRFGTNIT | Tyrosine phosphatase that specifically dephosphorylates 'Tyr-142' of histone H2AX (H2AXY142ph). 'Tyr-142' phosphorylation of histone H2AX plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. Promotes efficient DNA repair by dephosphorylatin... |
Q9YHA1 | EYA4_TAKRU | Eyes absent homolog 4 (EC 3.1.3.48) | RKLAFRYRRVKELYTTYKNNVGGLLGPAKRDAWLQLRAEVEALTDSWLTHALKSLSIISSRSNCVNVLVTTTQLIPALAKVLLYSLGAVFPIENIYSATKIGKESCFERIVSRFGTNIT | Tyrosine phosphatase that specifically dephosphorylates 'Tyr-142' of histone H2AX (H2AXY142ph). 'Tyr-142' phosphorylation of histone H2AX plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. Promotes efficient DNA repair by dephosphorylatin... |
Q9YI98 | OAZ1_DANRE | Ornithine decarboxylase antizyme 1 (ODC antizyme, short form) (ODC-Az-S) | MVKSNLQTILNSHCFVREKESNIPKMPVIELTRNKPESESSHRCSNPCPGPLWCSDVPLPPLKIPGGRGNDQRDHSLSAKLFYSDAQLLVLEEAPQSNSRVRFLLFERRCSVSKHLVWRGALKGTNLYIEIPTGVLPEGSKDSFSLLLEFAEEKLQVDHVFICFHKSRDDRASLLRTFSFMGFEIVRPGHPLVPTRPDAFFMAYRIERDSDGDE | Ornithine decarboxylase (ODC) antizyme protein that negatively regulates ODC activity and intracellular polyamine biosynthesis and uptake in response to increased intracellular polyamine levels. Binds to ODC monomers, inhibiting the assembly of the functional ODC homodimer, and targets the monomers for ubiquitin-indepe... |
Q9YJJ8 | VP8_BAVJK | Intermediate capsid protein VP8 (Virion protein 8) (VP8) | MANRATSAFLDNPHPVGVNYVDEGSRQFVAVAELLASKLIASSRESDESNSDVPFVQAYSKFADDNPRHLRVKTGGKMANALTNVIRSYYSINAPAIVPQVEIDRLASKATVSGDMYNSYAVFNSVPIVEVLSPAQTTVSIVGSDRADVTMLNTGAGAANITFNFGQIAETVILKGSVPFQLARANQPMPAARFTYKLRPLDGPFIVVLPVGNPLVISATAATRIQVPLAFNKALVESGFQTAMNDGLFDAQNVNYYSSFDEFIIAQYHALDGINRVSTCVVLGLALQAYDQMRRALPVRRV | Self assembles to form an icosahedral capsid with a T=13 symmetry, which consists of 230 trimers, with channels at each of its five-fold vertices. |
Q9YJQ9 | MVP_TOMS1 | Movement protein (30 kDa protein) (Cell-to-cell transport protein) | MALVVKGKVNINEFIDLSKSEKLLPSMFTPVKSVMVSKVDKIMVHENESLSEVNLLKGVKLIEGGYVCLVGLVVSGEWNLPDNCRGGVSVCLVDKRMERADEATLGSYYTAAAKKRFQFKVVPNYGITTKDAEKNIWQVLVNIKNVKMSAGYCPLSLEFVSVCIVYKNNTKLGLREKVTSVNDGGPMELSEEVVDEFMENVPMSVRLAKFRTKSSKRGPKNNNNLGKGRSGGRPKPKSFDEVEKEFDNLIEDEAETSVADSDSY | Transports viral genome to neighboring plant cells directly through plasmosdesmata, without any budding. The movement protein allows efficient cell to cell propagation, by bypassing the host cell wall barrier. Forms a ribonucleoprotein complex with viral RNA. Binds microtubules and modulates microtubule stability. Can ... |
Q9YK98 | POL2_BRAV | RNA2 polyprotein (P2) [Cleaved into: Protein 2A; Movement protein (MP); Coat protein (CP)] | MSESGNTTSMPGCGRMCALRSTWSKRAFLVACKDGALTSDGRCPQYGCGALVSITKGVQQPKKTASAKVVKCLCWVQPARWCEKHSKGPASPNGSVTTKRSNSARAAPAPLPYKKQTCDVVVTVGPLELVYPALVSEELPTPVAATPTKVEEVPIPELPLWLAPAWMVEQPYAATPEVLCLTQREEFALLKKRLTRKGKLLQRRATHARFEARAALARVRAATQRKVEEVTALVIKGRRILAAHQLLRELEEVAPLSQAQEQLVASSCAAAAARQEECASFLRRAKAWRKSISATPPVAFATAVASKVVSATMPWAHLGL... | [Protein 2A]: Implicated in RNA2 replication. Could also be required for nematode transmission of the virus (By similarity). [Movement protein]: Transports viral genome to neighboring plant cells directly through plasmosdesmata, without any budding. The movement protein allows efficient cell to cell propagation, by by... |
Q9YKK9 | LEF10_NPVAC | Late expression factor 10 | MTNVWFATDVNLINCVLKDNLFLIDNNYIILNVFDQETDQVRPLCLGEINALQTDAAAQADAMLDTSSTSELQSNAST | Plays an essential role in viral DNA replication. |
Q9YKL8 | NSP1_ROTD9 | Non-structural protein 1 (NSP1) (NCVP2) (Non-structural RNA-binding protein 53) (NS53) | MATFKDACFHYRKITKLNRELLRIGANSVWIPVSSNKIKGWCIECCQLTELTFCHGCSLAHVCQWCIQNKRCFLDNEPHLLKLRTFESPITKEKLQCIIDLYNLLFPINPGIINRFKKIVNQRKCRNEFEQSWYNQLLFPITLNAAVFKFHSREVYVFGLYEGSSSCINLPYRIVNCIDLYDRLLLDQINFERMSSLPASLQSVYANKYFKLSRLPSMKLKQIYYSDFSKQNLINKCKIKSRIVLRNLTEFTWDSQISLHYDVINNREKILTALSTSSLKRFETHDLNLGRIKADIFELGHHCKPNFISSNHWQPASNVS... | Plays a role in the inhibition of host innate immunity by inducing the degradation of key host factors required to activate interferon production such as IRF3, IRF5 or IRF7. Associates with components of cullin RING ligases (CRLs) including CUL1 or CUL3, which are essential multisubunit ubiquitination complexes, to mod... |
Q9YMS9 | LEF11_NPVLD | Late expression factor 11 | MAPAVVGASQLRGGDSPGPARNRDHCLNRSEVYALTREAINKRKHLGDVKGVCAHLFDDSFSAQSDYIRENLATAFIVVGDNCRERKHLGQHAARFDRVFSLKRRTLYDEYHASAGRYGDTKPCRKRRFSRAAQVRDQPAQQERLGDQSVQDSPLRKEKDLVPHQGVGGVRPGQENGQARQEEQSQQ | Involved in late/very late gene activation. |
Q9YNA4 | PB2_THOGV | Polymerase basic protein 2 (PB2) (RNA-directed RNA polymerase subunit P3) | MDREEPAESECTLRALVEEYNGACKEAPKEMSKQFTDYNTFKRYTTSKKDHAPQMRLVYSVRKPWPISMTPSKEIPLVFNGTKLKDTILDLGESKRTRANIVVPDYWSKYGSQTSLEVVNAILYAEDLKVQRFFSTEWGEIRYGRMLPFRKPVQACPTIEEVNPASIPHTLLQVFCPQYTTLDSKRKAHMGAVEKLKRVMEPICKVQTQESAVHIARSLIDSNKKWLPTVVDHTPRTAEMAHFLCSKYHYVHTNTQDLSDTRSIDNLCGELVKRSLKCRCPKETLVANLDKITIQGRPMREVLADHDGELPYLGICRVAM... | subunit of the RNA-dependent RNA polymerase which is responsible for replication and transcription of virus RNA segments. The transcription of viral mRNAs occurs by a unique mechanism called cap-snatching. 5' methylated caps of cellular mRNAs are cleaved after 10-13 nucleotides by PA. In turn, these short capped RNAs a... |
Q9YNE2 | CAPSD_OLV2I | Capsid protein (CP) (Coat protein) | MSSAAQPMSRRARRRAARRALGSQPGTSGGMVIPVSFVVSGATSADFVTYHSLYSRLAAYNGDLWIRRVAVRVTGSVAKRMGKYAFFEGLAVDKSQILSAAHARPYVYGLPSTLSLPGGRRQVKDFQSINLFFLLDGTAHAGEFAAGTFYFEFEGSPNVDFPRDSEGSNQAVEKFYLEHINA | Capsid protein self-assembles to form a quasi-spherical capsid, about 26 nm, or bacilliform. |
Q9YPD5 | RDRP_MBVLF | RNA-directed RNA polymerase (EC 2.7.7.48) | MDSGLYPKTGAPTWFYGWSKQREGGFSDFGSEIFRLRALPPLKAEIFRGIREVVEYNITGDSHPGYPWCKLGSDNKAVLTGFGDLIWDEVAKRFNNMLGYGDAIFSMTPSELVQNGICDAVKVFIKQEPHSLEKVNAGRLRIIAAVGLVDQIVTRLLCMKQNNAEIDCWESCPSAPGMGLNDEGLRTLYSTAQVMAEHGTICETDISGWDWSVQQWELDSDARLRTQLAGEEIGGYLNFFLRVHAYVVGHSVFVMPDGEMLEQTVPGGQLSGDYNTSSSNSRMRVIATMFARYLAGQVSGFPLLGIKAMGDDSFEIWFKG... | RNA-dependent RNA polymerase which replicates the viral genome. |
Q9YPS1 | AC4_MYMVV | Protein AC4 (Protein AL4) | MKMENLISMFCFSSKGSSKRRTKGSSTWFPQPDQHITIRTFRRLKAHQMLSHTWTKTETSLTMEVSKSMADQLEEVNSLPTTLMPRHSIVDPSYRPSIY | Pathogenicity determinant (By similarity). May act as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. |
Q9YPS4 | REN_MYMVV | Replication enhancer protein (REn) (Protein AC3) (Protein AL3) | MDFRTGDNITAAQLKNGVFIWEVRNPLSFKIMQHRQIRPGSQMYVTQIRIMFNHGLKKALLMHKCFLDLTLYHYLTATSGMILSTFSDQLFRYLNNLGVISIGNVLKGASHILYEKLHHVEDVSLTHNVQYKLY | Increases viral DNA accumulation. Enhances infectivity and symptom expression (By similarity). |
Q9YPS6 | AV2_MYMVV | Protein AV2 | MWDPLVNDFPKSLHGFRCMLAIKYLQYIQENYPSNSLGFVYLTELIQVLRIRKHAKAELRYRLLYPDVECAEEADLRHPAFLTCHCGKCPCQREKEEVDQPTHVEETEILSVIPLS | Through its interaction with host SGS3, acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. |
Q9YPS7 | MVP_MYMVV | Movement protein BC1 (Movement protein BL1) | MENYSGAVVNNKYVETKSCEYRLTNNEMPIKLQFPSYLEQKTVQIMGKCMKVDHAVIEYRNQVPFNAKGTVIVTIRDTRLSYEQAAQAAFTFPIACNVDLHYFSSSFFSLKDETPWEIVYKVEDSNVIDGTTFAQIKAKLKLSSAKHSTDIRFKPPTINILSKDYTEECVDFWSVEKPKPIRRMLNPGPNQGPYPISGHRPIMLQPGETWATRSSIGRSSSMRYTNNDRPSILDNTSASDADYPLRHLHKLPEASLDPGDSVSQSHSNAMSKREIEDIIETTISKCLISQRSNVNKAL | Transports viral genome to neighboring plant cells directly through plasmosdesmata, without any budding. The movement protein allows efficient cell to cell propagation, by bypassing the host cell wall barrier. Begomovirus genome is shuttled out of nucleus by Nuclear shuttle protein (NSP) and the movement protein transp... |
Q9YRB2 | CAPSD_NCBVS | Capsid protein (CP) (Coat protein) [Cleaved into: Large capsid protein; Small capsid protein] | MDANVQIRPARNNPSQGNQGRNNNNKRRRRRRGLKLPPVVAPITSPGQMAEPANHANTRVNRGRTRVRGLRQAMMESPMAATSEAWIHDYLDPDGEYKTSLDDGKIPDGAIPQSTCGQFRGTVGARYPGLNSTTLPLDGGTWPLLVMHLPFFRHPLLFITTTSNTEVEVTNADLDAFANDWNNRTDWTEATYPSWAQVGNVFYMVVPTEALTDVPPPTQLGVSGLLESYRLTSSGVTAYFNAPTLVNQGVAVIAQFQPDKEHQKENPDIVAGTTQTGGTLQLGGSGPNYTLTMTIGDQVEFGGAAIPLPTVSMGPMPESG... | Self-assembles to form an icosahedral capsid with a T=4 symmetry, about 35 nm in diameter, and consisting of 240 copies of the two structural proteins. |
Q9YTU3 | POLA_CHPVU | Polyprotein p69 (ORFA polyprotein) [Cleaved into: Papain-like protease p29 (EC 3.4.22.-); p40 protein] | MSCLRKPSQSLVLSESVDPTTVDPFVDVRAEEVVPTGCMTLWEYRDSCGDVPGPLSHGDLRRLRTPDGVCKCQIHFEFPTVLKSGSTGTVPEHPAVVAAFMGRPRRCSLEQRTKELDFRFLQLVHEGLPVRPSYMIARPPRPVRGLCSSRDGSLAQFGQGYCYLSAIVDSARWRVARTTGWCVRVADYLRLLQWVGRRSFGSFQIEESTVEHVYHVIVDTEHQSEQDGALFYQAVSDLAARDPLARIGNQLNPLAAEFCPRSARRVEPVTPQVTRRKGLARMPGRSPTVVSVGNVGMAITSIQDALVATELRNVNFGRRD... | P40 protein is involved in reduction of conidiation of the host. Not necessary for replication. Also involved in reduction of orange pigmentation of the host (By similarity). [Papain-like protease p29]: Cysteine protease of the peptidase family C7 that contributes to hypovirulence-associated traits like the reduction ... |
Q9YW20 | NMT_MSEPV | Putative glycylpeptide N-tetradecanoyltransferase (EC 2.3.1.97) (Myristoyl-CoA:protein N-myristoyltransferase) (NMT) (Peptide N-myristoyltransferase) | MNYWESKSICTVFTKYNDTEIINKIDPVKSNIDHSLYKQYTIGYMSNFNIVNICKFVNKHSNYIFDIDTFSWLVLNPFSDPSFNIVLYDNDKIVATIVGILRSIKIKNEIHKIIHTTFLTVDENYRKQGIHFYIIDKLMENAFNKGVLLGIFSTMKKIKKIKCVNVQDTYIIKSDSKKYKENNNVFDYKKLNQKNDDLYFIYNDMEIEYWFNKKYCHIISIYNNLFCFLKIKYKNNENLNILIEQYIHNKNINKYSIPNNSIMFSQYIQLPQIKLQNQIYTYIYNLNFNNLKCNICMF | Adds a myristoyl group to the N-terminal glycine residue of certain proteins. |
Q9YW29 | ETF2_MSEPV | Early transcription factor 82 kDa subunit (ETF large subunit) | MDYIETFINPQVIFLYNENKKIIKTIFLSKDSMIEDSHVMTVYNYLLSSHSDIFENKPQFINDHVILTFTLEQARGYIKNILGLSDDIILFSIWNNFDYYLKNGIFDPYNIQNMLLVEPNDDKSILYNIYQNIVEGAVFCVTTNKNIGSQLARSNVYSSVYRDYISEIINNIYKNRYAMKSSIIDAMEYSINIDFQDLLRISNIPDYNKTLCISAYNNFYIKGNKITILDNFDSMYESKYLKIYDKNININIYDDVLYVKKLSDFTDILNKYNIKSINIKSLKPKTTIYVYFNTFLNPNLTIEFDFDFFINDTKKTKNIF... | Acts with RNA polymerase to initiate transcription from early gene promoters. Is recruited by the RPO-associated protein of 94 kDa (RAP94) to form the early transcription complex, which also contains the core RNA polymerase. ETF heterodimer binds to early gene promoters (By similarity). |
Q9YWQ2 | VP10_BAVJK | Structural protein VP10 | MDVLSKSSLKELLAHLERTPLEEAISYKIGTIPYQNVLISRNEYYNQPYPDVTSLIDGVAREGQRNVNGLIMSIISYVVSGSGHYIPNIGYTLLRRSILDILTKHDTGLNTNNINYDMIARNLTVSKMNCEQRKRMLICFKLLAYKDGNLNDYETYLNQNISLKQIAPNFIPGDMRTVMSNSDKLSIVGIPAYRLTQSTELSIRDDNAKSYKIGYVDWYNSSSFLREGNDFNLISLKDRDNKYVRLNGW | Forms the virion spike 'foot' and helps anchor the VP9 spike 'head' protein in the virion. |
Q9YYS0 | DUT_ADEG8 | Deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTPase) (EC 3.6.1.23) (dUTP pyrophosphatase) | MSFDSGCPPTPPVKLLFKKHSPFAVTPQRATSGAAGYDLCSSADVVVPPKSRSLIPTDLSFQFPRGVYGRIAPRSGLAVKFFIDVGAGVIDSDYRGIVSVLLFNFSDHNFNVRRGDRIAQLILERHLTPDLEERSGLDETARGAAGFGSTGGFDTGVCPSSFS | This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. |
Q9Z0C8 | MVP_MDV1 | Putative movement protein (MP) | MADPVYYQGYQDDGDIDAQKRHQALYLIGIIILIMVCIIILWVCIMLACYIPGFLKKTMEAWLSSSSMMKRRVAATITRTPFEATGPERERNWDARRQTNAASSQPSNGGVF | May transport viral genome to neighboring plant cells directly through plasmosdesmata, without any budding. The movement protein allows efficient cell to cell propagation, by bypassing the host cell wall barrier (By similarity). |
Q9Z0D0 | NSP_MDV1 | Putative nuclear shuttle protein | MADWFASPLKTCTHVCDFPTLAGDPSQEITCCDSMKNKLNDSRKVLLVSCSVSFNGSFYGGNRNVRGQLQISMLEDDGVCRPIGYVPIGGYLYHNDYGYYEGEKTFNLDIESQYLKKDEDYNRKFIVSVLNENGLDSLCDLKVFIVHALRIKV | Putative nuclear shuttle protein. |
Q9Z0D2 | CLINK_MDV1 | Cell cycle link protein (Clink) | MGLKYFAHLPLELREKIVRDHLQEERKKEFLEKAIEDSCRRHEALLIEDPSPAELNSLSKFLTALSDYVGNQFNTRCLIRWKKDVPSKVKFGFMDEQHHKLYGSMDMDDLSCGELFIPDEEDDLTYEDGVIVRCSQLDQLFKSLGIEIVYIVVSKHCIWAPLSKEIVIK | Interacts with and disrupts the function of host retinoblastoma-related proteins RBR, which are key regulators of the cell cycle. Induces transcriptional activation of E2F-regulated S-phase and G2/M-phase-specific genes. Inactivation of the ability of RBR to arrest the cell cycle leads to the stimulation of viral DNA r... |
Q9Z0K9 | AMEL_CAVPO | Amelogenin | MGTWILFACLLGTAFAMPLPPHPGHPGYINFSYEKSHSNAINIDRTALVLTPLKWYQSMIRQPYPSYGYESMGGWVHHQVIPVLSQQHPPSHTTLPPHHHIPVGPAQQPVVPQQPLMPVPGHHSMTPNQHHQPNLPPTSQQPFQQPFPTQPVQPQHHQPIQPIQPIQPIQPIQPIQPQSPLHPIQPLPPQQALPPMFSMQPIAPLLPDLPLEAWPATDKTKREEVD | Plays a role in the biomineralization of teeth. Seems to regulate the formation of crystallites during the secretory stage of tooth enamel development. Thought to play a major role in the structural organization and mineralization of developing enamel (By similarity). |
Q9Z1J8 | S14L3_RAT | SEC14-like protein 3 (45 kDa secretory protein) (rsec45) | MSGRVGDLSPKQAETLAKFRENVQDVLPALPNPDDYFLLRWLRARNFDLQKSEAMLRKYMEFRKTMDIDHILDWQPPEVIQKYMPGGLCGYDRDGCPVWYDIIGPLDPKGLLFSVTKQDLLKTKMRDCERILHECDLQTERLGRKIETIVMIFDCEGLGLKHFWKPLVEVYQEFFGLLEENYPETLKFMLIVKATKLFPVGYNLMKPFLSEDTRRKIVVLGNSWKEGLLKLISPEELPAHFGGTLTDPDGNPKCLTKINYGGEIPKSMYVRDQVKTQYEHSVQISRGSSHQVEYEILFPGCVLRWQFSSDGADIGFGVFL... | Probable hydrophobic ligand-binding protein may play a role in the transport of hydrophobic ligands like tocopherol, squalene and phospholipids. |
Q9Z287 | KR121_MOUSE | Keratin-associated protein 12-1 | MCHTSCSSGCQPSCCVSSSCQPSCCVSSPCQASCFVSSPCQPSCCVSSSCQSACCRPAICIPVRYQVACCVPVSCGPTVCMAPSCQSSVCVPVSCRPVCVTSSCQSSGCCQPSCPTLVCKPVTCSNPSCC | In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of ha... |
Q9Z2Y8 | PLPHP_MOUSE | Pyridoxal phosphate homeostasis protein (PLP homeostasis protein) (Proline synthase co-transcribed bacterial homolog protein) (Pyridoxal phosphate-binding protein) | MLRGGSMTAELGVGFALRAVNERVQQSVARRPRDLPAIQPRLVAVSKTKPADMVIEAYGHGQRTFGENYVQELLEKASNPKILSSCPEIKWHFIGHLQKQNVNKLMAVPNLSMLETVDSVKLADKVNSSWQKKGPTEPLKVMVQINTSGEDSKHGLLPSETIAVVEHIKASCPSLEFVGLMTIGSFGHDLSQGPNPDFQRLLTLRRELCEKLGIPVEQVELSMGMSMDFQHAIEVGSTNVRIGSTIFGERDYSKKPALDKTADAKASVPLVQGH | Pyridoxal 5'-phosphate (PLP)-binding protein, which may be involved in intracellular homeostatic regulation of pyridoxal 5'-phosphate (PLP), the active form of vitamin B6. {ECO:0000255|HAMAP-Rule:MF_03225}. |
Q9Z302 | OXDA_CRIGR | D-amino-acid oxidase (DAAO) (DAMOX) (DAO) (EC 1.4.3.3) | MRVVVIGAGVIGLSTALCIHERFSPVQPLHMKIYADRFTPFTTSDVAAGFWQPYLSDPRNPQEVEWNQQTFDYLLSHIHSPNAEKMGLSLISGYNLFKEEVPDPFWRNTVLGFRKLTPREMDIFPDYGYGWFNTSLTLEGKSYLPWLTERLTERGVKLFHRKVESFEEVARGGADVIINCTGVWAGALQADTSLQPGRGQIIQVEAPWMKHFILTHDPRLGIYNSPYIIPGSKTVTLGGVFQLGNWNELNSVHDHNTIWKSCCKLEPTLKNAKIVGELTGFRPVRHQVRLKKKQLHFGSSSVEVIHNYGHGGYGLTIHWG... | Regulates the level of the neuromodulator D-serine in the brain. Has high activity towards D-DOPA and contributes to dopamine synthesis. Could act as a detoxifying agent which removes D-amino acids accumulated during aging. Acts on a variety of D-amino acids with a preference for those having small hydrophobic side cha... |
Q9Z313 | RL13_CRIGR | Large ribosomal subunit protein eL13 (60S ribosomal protein L13) | MAPSRNGMILKPHFHKDWQRRVDTWFNQPARKIRRRKARQAKARRIAPRPASGPIRPIVRCPTVRYHTKVRAGRGFSLEELRVAGIHKKVARTIGISVDPRRRNKSTESLQANVQRLKEYRSKLILFPRKPSAPKKGDSSAEELKLATQLTGPVMRIRNVYKKEKARVITEEEKNFKAFASLRMARANARLFGIRAKRAKEAAEQDVEKKK | Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosom... |
Q9Z364 | URED_ACTNA | Urease accessory protein UreD | MSTTGELYLRIAQDGDRSIAVDQYHRGALRVFRPLYLDGTGQVAYYVVNPGGGYLDGDSYLTEVEVLQGASAVLTTQAATKIYRTPTRPVRQDTRASLAPGAVLELVPDQVIAYRGASYRQTTLVEMDPTATFMSLEVLTPGWAPDGSAFGYDCVRMRTEIRVGGRCAVVDNLRLVPGEAGMAGLGALEGHSHLASFTALDARIDAALVTEIGELLEVDGVRGAVTRVPGPGLIARALGDDTTRLTALMLDISELLRDRWFGAPRLDLRKY | Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. {ECO:0000255|HAMAP-Rule:MF_01384}. |
Q9Z3B7 | UREE_ACTNA | Urease accessory protein UreE | MIIESISGNIHDLPGEDLEDVHVESVVLPLADLTKRIQRVRSDHGTELGIRLAPGAPDLREGDILLRNERGIVVVRLEPTDVLVIAPVTVREMGVVAHNLGNRHLPAQFFGPAEPFPGLEGHDGVMVIQYDHTAEHYLEHLGVRHARMERSMPVPFRHAEHTH | Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly. {ECO:0000255|HAMAP-Rule:MF_00822}. |
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