entry stringlengths 6 10 | entry_name stringlengths 5 11 | protein_name stringlengths 3 2.44k | sequence stringlengths 2 35.2k | function stringlengths 7 11k |
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Q9PS09 | 3SOBB_DENAN | Dendrotoxin B (DTX-B) | MICYSHKTPQPSATIGCEEKTCYKKSVRKL | Blocks voltage-gated potassium channels (Kv). This is the slowly inactivating phase of potassium efflux which is blocked by this toxin. |
Q9PS27 | PRT_DICLA | Protamine | PRRRRQASRPVRRRRRTRRSTAERRRRRVVRRRR | Protamines substitute for histones in the chromatin of sperm during the haploid phase of spermatogenesis. They compact sperm DNA into a highly condensed, stable and inactive complex. |
Q9PS34 | 3SA5_NAJOX | Cytotoxin Vc-5 | LKCKKLVPLFSKTCPAGKNLCYKMFMVAAPHVPVKRGCIDVCPKSSLLVKYVCCNTDRCN | Shows cytolytic activity on many different cells by forming pore in lipid membranes. In vivo, increases heart rate or kills the animal by cardiac arrest. In addition, it binds to heparin with high affinity, interacts with Kv channel-interacting protein 1 (KCNIP1) in a calcium-independent manner, and binds to integrin a... |
Q9PSJ0 | MYCN_DANRE | N-myc protein (zN-Myc) | EDIWKKFELLPTPPLSPSRAALPGDPGELGAVAGDCSLMGFGLTDPLDWASELLLLPGDDIWGASDGDLFGSVLDTTDNSIIIQDCMWSGFSA | May function as a transcription factor. |
Q9PST3 | 3SA2B_NAJSP | Cytotoxin 2b (Cardiotoxin-2b) (CTX-2b) (Ctx2b) | MKTLLLTLVVVTTVCLDLGYTLKCNKLVPLFYKTCPAGKNLCYKMYMVATPKVPVKRGCIDVCPKSSLLVKYVCCNTDRCN | Shows cytolytic activity on many different cells by forming pore in lipid membranes. In vivo, increases heart rate or kills the animal by cardiac arrest. In addition, it binds to heparin with high affinity, interacts with Kv channel-interacting protein 1 (KCNIP1) in a calcium-independent manner, and binds to integrin a... |
Q9PT99 | PYY_DICLA | Peptide YY-like (PYY) | MIHSGAVMSMSILAFCLLACIHSGINAYPAKPASPRDGAPPEELAKYYSALRHYINLITRQRYGKRDTPDTVFSDVLMRESTESIPGSNYVRYDGLPLW | Gastrointestinal hormone and neuropeptide. |
Q9PTA2 | IVBL_BUNMU | Beta-bungarotoxin B chain-like (BL1) | MSSGGLLLLLGLLTLCAELTPVSSKDRH | Beta-1-bungarotoxin is a presynaptic neurotoxin of the venom. The B chain is homologous to venom basic protease inhibitors but has no protease inhibitor activity and blocks voltage-gated potassium channels (Kv) (By similarity). |
Q9PTG9 | MTB_DICLA | Metallothionein B (MT-B) | MDPCDCSKSGTCNCGGSCTCTNCSCTTCKKSCCPCCPSGCTKCASGCVCKGKTCDTSCCQ | Metallothioneins have a high content of cysteine residues that bind various heavy metals. |
Q9PTQ4 | UTS1_CARAU | UI [Cleaved into: Urophysin; Urotensin-1 (Urotensin I)] | MKPVPLVLLITSVLLTTHIPLSTCRPRDLSLVNSQLDDVLSNGAGDDAMSYLVGEKLLQYLQRNLGAQKASGVLHLPHFPAAQLRSPHEDSSLEELTEFSKRNDDPPISIDLTFHLLRNMIEMARNENQREQAGLNRKYLDEVGK | Urotensin is found in the teleost caudal neurosecretory system. It has a suggested role in osmoregulation and as a corticotropin-releasing factor. The non-hormonal portion of this precursor may be a urotensin binding protein, urophysin. |
Q9PTW9 | PSA7_CARAU | Proteasome subunit alpha type-7 (Proteasome subunit alpha 4) | MAARYDRAITVFSPDGHLFQVEYAQEAVKKGSTAVGIRGKDIVVLGVEKKSVAKLQEERTVRKICALDEHVCMAFAGLTADARIVINRARVECQSHRLTVEDPVTVEYITRYIATLKQRYTQSNGRRPFGISALIVGFDFDGTPRLYQTDPSGTYHAWKANAIGRSAKTVREFLEKNYTDEAIASDNDAIKLAIKALLEVVQSGGKNIELAVIRRNQPLKILESKEIETLVAEIEKEKEEEAEKKKQKKSS | The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. |
Q9PTY5 | RANB9_XENLA | Ran-binding protein 9 (RanBP9) (Ran-binding protein M) (RanBPM) | MSSPPLHGLSSVGHLSRDPPPRSWSPRDKCSYLGLSHGNLRVHYKGHGKTSKDAASVRSTHPIPAACGIFYFEVKIISKGRDGYMGIGLSTQGVNLNRLPGWDKHSYGYHGDDGHSFCSSGTGQPYGPTFTTGDVIGCCVNLIDNTCFYTKNGHSLGIAFTDLPPNLYPTVGLQTPGEVVDANFGQSPFVFDIEDYIREWRSKIQAQIERFPVAGEWQSMIQRMVSSYLVHHGYCSTAEAFAKSTDQTVQEELASIKNRQRIQKLVLSGRMGEAIETTQQLYPSLLERNPNLLFTLKVRQFIEMVNGTDSEVRCLGNRSL... | May act as scaffolding protein, and as adapter protein to couple membrane receptors to intracellular signaling pathways. Acts as a mediator of cell spreading and actin cytoskeleton rearrangement. Core component of the CTLH E3 ubiquitin-protein ligase complex that mediates ubiquitination and subsequent proteasomal degra... |
Q9PUR0 | GLUC2_PETMA | Glucagon-2 [Cleaved into: Glucagon-2 (Glucagon II) (Glu II); Glucagon-like peptide 2-II (GLP-2II)] | MSNASGTLLSYMFMMLLGLTLASLVPHETDDGDLNAEISLANRHSQGSFTSDYSKHLDVKQAKDFVTWLLNTKRRGVDAQAGANLEKRHSDGSFTNDMNVMLDRMSAKNFLEWLKQQGRG | Promotes hydrolysis of glycogen and lipids, and raises the blood sugar level. |
Q9PUR1 | GLUC1_PETMA | Glucagon-1 [Cleaved into: Glucagon-1 (Glucagon I); Glucagon-like peptide 1-I (GLP-1I); Glucagon-like peptide 2-I (GLP-2I)] | MSDPGFLAAPVLLLLLVSLASASLEQAASRDDDSAERPLSKRHSEGTFTSDYSKYLENKQAKDFVRWLMNAKRGGSELQRRHADGTFTNDMTSYLDAKAARDFVSWLARSDKSRRDGGDHLAENSEDKRHAEDVNALLDRTMAKTFIEWLEKQNSNDQTD | Promotes hydrolysis of glycogen and lipids, and raises the blood sugar level. |
Q9PVY0 | RX1_CHICK | Retinal homeobox protein Rx1 (cRax1) | MFLNKCEGDLGELRKPGDSEGTPPAAAEEEQPKKKHRRNRTTFTTYQLHELERAFEKSHYPDVYSREELAMKVNLPEVRVQVWFQNRRAKWRRQEKMEASSMKLHDTPMLSFNRPPMTANVGPMSNSLPLDPWLTSPISSATPVHSIPGFMGAPQALQPPYGGHSFLNTPPGMAQGMQPMAPAPYQCGTPFVDKYPLEDVDQRSSSIASLRMKAKEHIQTIDKTWQPI | Plays a critical role in eye formation by regulating the initial specification of retinal cells and/or their subsequent proliferation. |
Q9PWA3 | GRIN2_CHICK | GRIN2-like protein (G protein-regulated inducer of neurite outgrowth 2-like protein) (G(o)-alpha-interacting protein 6) | MGLESVVQTMNNQSPDNNSQSRTKTTNHFLIIEQSPASWEVGDTKMCVKSSTVENVSSACFKHQQSMGKMDEPRAVLQRSHSDLTCSCKQQSYVTHVETSATDSSLSSSSSRHGPSVVRMSFQTERYGSGIRNKENTSHYQNLVTHLPALPIDQKVPTNTFDSGGIPHNTTVYTDPGRFHSAVLGPHMPGNGFSNRTMLSQATGIIHGGLTYSNIPNSAFSPMAMTVHNSSAVPCNIRQDSCMKVDATIPAYCHSLPIPSIQLVPRLVCSVSESGKEQAAPDYFHSFSTSDILTYPKLVSSVSESGLDAKRVLKCCSIPG... | May be involved in neurite outgrowth. |
Q9PWD2 | HXA4_MORSA | Homeobox protein Hox-A4 | MTMSSYLINSNYIEPSFPPCDEYQQSGYIPNPGDYYERPKDTGFPHHDEPSYPRSNYTESGYDYGNVPATGLDDFGDGHHAQPQPVPQSHGPRLTAAPDGGAGANASKDCSLASEVYPGVAKGKEPVVYPWMKKVHVSTVNASYTGGVPKRSRTAYTRQQALELEKEFHFNRYLTRRRRVEIAHTMCLSERQVKIWFQNRRMKWKKEHKLPNTKIRSSSSASSSASGAQQQQIKTGQQLVPTPCTAGL | Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. |
Q9PWD3 | HXA5_MORSA | Homeobox protein Hox-A5 | MSSYFVNSFCGRYPNGADFQLHNYGDHSTANDQYRDSTAMHSSRYGYGYNGMDLTVGRAGTGHFVGNERTQGYSPSHSAATTPSVEPVRYTQSANSTGTSSLSPPPDPLPCSSVASSSPVTETQSQHRAVKNSITTPCSTPCSSSNGGTLLLNRDCVSKASPLEEEKPAGSAPTTPQNVSDSTQPQIYPWMRKLHINHDLAGPEGKRARTAYTRYQTLELEKEFHFNRYLTRRRRIEIAHALCLSERQIKIWFQNRRMKWKKDNKLKSMNMAAAGGGGYRP | Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. |
Q9PWD4 | HXA7_MORSA | Homeobox protein Hox-A7 | MSSYYVDGLLSKYTAGSSLFPNVERASCSIGPSGEDYGSARTTAAIAFAPSLSGVYSVSDAVYQSRPVFTSGYGQGQDAHTLHCSLFDQSRLFTDSCCHPEPGPLTSPPDKQYRMYPWMRASDPTRKRGRQTYSRYQTLELEKEFHFNRYLTRRRRIEIAHALCLSERQIKIWFQNRRMKWKKDHKEEPVSTPSGEKDCDIQPVSEAEEPKAVNNPERRFGVRNG | Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. |
Q9PWD5 | HXA9_MORSA | Homeobox protein Hox-A9 | MSTSGTLTSYYVDSLILPESEELSVPRYPSGPGLQHARQSASISDHSELGTCTFPSKPPVFGPSWSHVPAQFPGTVSSVYHHHYGHPQGPVGADTDGRYQSWLLEPMSGSLPMAGLPTTHHYGIKPEGLGTRADGALPGSHTALLLSDYANGTVATASPVEKDTLSGQAGDVSGEAEEKPGLDPSKSLQNNPVSNWLHASATRKKRCPYTKHQILELEKEFLFNTYLTRDRRYEVARLLNLTERQVKIWFQNRRMKMKKFNKDGAPKDE | Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. |
Q9PWD6 | HXA10_MORSA | Homeobox protein Hox-A10 | MSSMEMWMDAQRSCRMDQEHPVGPQVAPCSFPQNIKEESTYCLYEQPKCPKASTAEDLTYSRLTTTGLGSSTCTVTDGGGGGGGGSVPVPGYFRLSQTHAHSHKLYNTNGPQPNPSHSHFGLHPTAPARFHTPPTSTSTPATAQEGRNTEEPVSSGNADLQPHAAPGTEEARESSDAEVSSADETEEHDKERQAKSTKGDTKSENTANWLTAKSGRKKRCPYTKHQTLELEKEFLFNMYLTRERRLEISKSVHLTDRQVKIWFQNRRMKLKKMTRENRIRELTSNYGFS | Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. |
Q9PWL7 | HXBAA_DANRE | Homeobox protein Hox-B10a (Hox-B10) | MALHRHPFVHGAASWDGEQPSPVQLPHISACPFTSSGRKEDPFYFTLDPTGQARQPLDISAFSRIMTDMGSLNSADDHRPETSFYSGHKLLSLNTDTDPESPSLSSHSDSQHLHSLSLSAPCSETDNKHDMQYLAMESTKYPSQWSESRTNRSIITTLSISQRSKDDIEPNNLQTDFTRGDKTPREKTQDVTLENAANGWLSAKAGRKKRCPYSKHQILELEKEFLFNMYLTRERRLEISRSINLTDRQVKIWFQNRRMKLKKMTREHRTRDPGTSFTV | Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. |
Q9PY82 | MUNS_REOVJ | Protein mu-NS (MuNS) | MASFKGFSANTVPVSKTRKDTSSLTATPGLRAPSMSSPVDMAQSREFLTKAIEHGSMSIPYQHVNVPKVDRKVVSLVVRPFSAGAFSISGVISPAHAYLLECLPQLEQAMAFVASPEAFQASDVAKRFTIKPGMSLQDAITAFINFVSAMLKMTVTRQNFDVIIAEIERLASSGVVNRTEEAKVADEELMLFGLDHRAPQQIDVSEPVGISRAVEIQTTNNVHLAPGLGNIDPEIYNEGRFMFMQHKPLAADQSYFTTETADYFKIYPTYDEHDGRMVDQKQSGLILCTKDEVLAEQTIFKLDVPDDKTVHLLDRDDDHV... | Non-structural protein with ssRNA-binding activity. Is probably involved in the formation of viral inclusions, where the assembly of cores and the replication of viral RNA are thought to occur. Together with mu-2, recruits the other core proteins to these inclusions (By similarity). |
Q9PY94 | NSP1_ROTHC | Non-structural protein 1 (NSP1) (NCVP2) (Non-structural RNA-binding protein 53) (NS53) | MANSFREMLYWYRKIIDRKLPCVNVNIWRREIAYKANGICLNCLNECKVCPCDYCGIRHKCENCLNSDCFMNTNNEFNSHRWITFDEEPSQMVLFEYWIMYKDYFLSKFNYNYKAQLKILNMNKNRRFHINESKKKALSVPITSQYLKFKFNNKIYIMFGTFLTSKIQPWIQLKSLKVGYIQSLNVDRCAKLIATKGMFATNSFKSSCITEINARRPISECDYLIEACLCNENNEWKFSAVMGRDKIPVTKSLAMKYFCKNINTELFYYGHSKCHVVSECPRWNQQLRVLNASTLNIIFRRQFMNEVVEWFENFTQLTGM... | 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... |
Q9PY95 | NSP3_ROTHC | Non-structural protein 3 (NSP3) (NCVP4) (Non-structural RNA-binding protein 34) (NS34) [Cleaved into: p38; p8] | MATQASVEWIFNVAGSAASSSLDKAIKDAGGSENFSKYVITKFYDNYKDCIDDSGVYNACIGRAKTIDKALNDPKVAERNEEWYTNVATISRLDLELAELKLMLSNLGIKREERVLNSMFSVVREKGRSSNVIMMKQNAVKMIEEGKLKIKVERNETYTESLKNKIEELECIIDAFEKGKDITIDLDAMNGEVKLDGNSCSYNSTAALVSTILGTPIKMYNESGQPLFDVGNYMNPKNIIEKMIELEIPIFKSDYRNNESPDFDSWNERSNLKIVSVNDCHAICIFKFENNWWCFDDGRLKKHNGAGYPLIVANSKFQID... | May play a role in stimulating the translation of viral mRNAs. {ECO:0000255|HAMAP-Rule:MF_04090}. |
Q9Q0L7 | NEP_I96A0 | Nuclear export protein (NEP) (Non-structural protein 2) (NS2) | MDSNTITSFQDILQRMSKMQLESSSVDLNGMITQFERLKIYRDSLGESMMRMGDLHSLQNRNATWRNELSQKFEEIRWLIAECRNILTKTENSFEQITFLQALQLLLEVESEIRTFSFQLI | Mediates the nuclear export of encapsidated genomic RNAs (ribonucleoproteins, RNPs). Acts as an adapter between viral RNPs complexes and the nuclear export machinery of the cell. Possesses no intrinsic RNA-binding activity, but includes a C-terminal M1-binding domain. This domain is believed to allow recognition of RNP... |
Q9Q1T6 | CAPSD_TOMK1 | Capsid protein (Coat protein) | MSYPITSPSQFVFLSSVWADPIELLNVCTNSLGNQFQTQQARTTVQQQFSEVWEPFPQSTVRFPGDVYKVYRYNAVLDPLITALLGTFDTRNRIIEVENRQSPTTAETLDATRRVDDATVAIRSAINNLVNELVRGTGLYNQNTFESMSGLVWTSAPAS | Capsid protein self-assembles to form rod-shaped virions about 18 nm in diameter with a central canal enclosing the viral genomic RNA. |
Q9Q3G5 | CAPSD_TASV2 | Capsid polyprotein VP90 | MAAMADKVVVKKTTTRRRGRSNSRSRSRSRSRSRTKKTVKIIEKKPEKSILKKIDQAERRDAKQLRRIRKKVQGPPVNSRMTTVVTLGQITGNKDNTLERKHKCFLNPLLMKSQETGQTATPLSVRASQYNLWKLSRLHVRLIPLAGKANILGSVVFLDLEQEANTAGPESVDTIKARPHVEVPIGSKTVWKVHPRSALGPRQGWWNVDPGDSPTDSLGPALNMWTYLQTVNALQSAGGTQTPYTSALFLVEVLVTYEFSNYGPKPALSQMVSDSFPPASGSTATLKNTSDGAVAIQLSGAIARKMEEVEPKGRRSNAQT... | Capsid polyprotein VP90: self-assembles to form an icosahedral T=3 capsid. |
Q9Q6X7 | CAPSD_CARMS | Capsid protein (Coat protein) (p38) | MENKGEKIAMNPTVQTLAQKGDKLAVKLVTRGWASLSTNQKRRAEMLAGYTPAILAFTPRRPRMTNSPPRTSRNSPGQAGKSMTMSKTELLCTVKGTTGVIPSFEDWVVSPRNVAVFPQLSLLATNFNKYRITALTVKYSPACSFETNGRVALGFNDDASDTPPTTKVGFYDLGKHVETAAQTAKDLVIPVDGKTRFIRDSASDDAKLVDFGRLVLSTYGFDKADTVVGELFIQYTIVLSDPTKTAKISQASNDKVSDGPTYVVPSVNGNELQLRVVAAGKWCIIVRGTVEGGFTKPTLIGPGISGDVDYESARPIAICE... | Capsid protein self-assembles to form an icosahedral capsid with a T=3 symmetry, about 32-35 nm in diameter, and consisting of 180 capsid proteins. Also 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 accum... |
Q9Q8J2 | A18_MYXVL | Transcript termination protein A18 (EC 3.6.4.-) | MSVCSEIDYALYTELKKFLNSQPLFLFNADKNFVEVVPSSSFKFYIPIGVFSNSDVALIRPVHTTCTNHIESADATFPNLYPLQKRVVAEVTTSMRQKLSTHRPMYMTLHLSCGFGKTITACYLMVVHRRKTVICVPNKMLIHQWKAAVELTKLSYIISTDGVSVLLKQLRTKTADVLIIVSRHLSNDYFCKKIHDEYDTFILDESHMYNLMNNSALTKFLTFYPPRICYFLTATPRLANRIYCNDVVNVLKVSTLMKRLKIVEYFFEPYSTECIRQMAKHLNTENNKYHIYTEKILAEDLPRNNLIVDTVSREFKHGLV... | DNA helicase which seems to act as a postreplicative transcription termination factor. Involved in ATP-dependent release of nascent RNA. Forms a stable complex with single-stranded DNA, and to a lesser extent RNA (By similarity). |
Q9Q8K4 | ETF2_MYXVL | Early transcription factor 82 kDa subunit (ETF large subunit) | MRYVVNPQLVLYVEKGQKIKRALYLTPYGTLDDKSPIYYFLSTHLKITDPEVHKRHILLTLKISQLKGYLCDLLRIRNDVIIYSHKNNLEYSYVDNTIFNPFAHTQKKTLIKSDGFLYNIYPDACDFLVIWVADAEDTSIAEFGSYEDVDVNILKFETRLLEVFDDLDLDMTIESKFNNIFRTNLKFTGLRKLIKKINEFNGSRYKSLLYKSDEYFINLTGNKFILTDERLNLTVWDSDGVVTFSSDGDTIMINNVKLFTSLLTDIDLQMERIKGDVTYKIFLSTPITSRIKLNIETSFIFVETATNNILLSADKRISII... | 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). |
Q9Q8P6 | RP07_MYXVL | DNA-directed RNA polymerase 7 kDa subunit (EC 2.7.7.6) | MVFQLVCSTCGRDISEERYALLIKKIDLKTVLRGVKNNCCRLKLSTQIEPQRNLTVEPLLDIN | Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF) thereby a... |
Q9Q8Q1 | MP44_MYXVL | Probable metalloendopeptidase G1-type (EC 3.4.24.-) | MIVFDNGTRVFINSSTNKDIYVGFSGFGFEKDIGGILGIAHLLEHILISFDASRFVANASTARSYMSFWCTPIRGRATSVDAVRTLISWFFDKDGLKDDFPVSKIKYHIKELENEYYFRNEVFHCMDALTFLANGDLYNGGRLSMLDRLEDIPLILRDRMRTIIGPNVVIFVRELNDVVLSLLANTFGRLPACPLTIPCTVRTIIGGKTIMMPSPFYTVMVRVEPSLHNILSILCLYEIYHLVDYETVDNKLYVTFSFIHEHDYERFLQGSGRLNLTIYKKIRLCYGDDFLMNVYLSFPCIRHDIFDYLTIVNTDTSSMI... | Seems to be involved in viral proteins maturation by cleavage at Ala-Gly-|-Xaa motifs. |
Q9Q8W2 | A28_RFVKA | Envelope protein A28 homolog (Protein Gp116) | MNPVTVFFVVVVTVAACMILFQVYSIYLNYDNIKEFNAMHSPLEYSKMVNVTAIDRRIQDANDDIYDAKQKWRCVKLDDSYVSLSMFGYKSDGIGIRRFRTLNSCIDYTFSTSTHSSILNPCISPNDPKSRECTFLKSVL | Envelope protein required for virus entry into host cell and for cell-cell fusion (syncytium formation). |
Q9Q8X0 | A18_RFVKA | Transcript termination protein A18 (EC 3.6.4.-) | MSVCLEVDYTLYTELKKFLNGQPLFLFNADKNYVEVVPSSTLKFYIPIGLFSNSNVALIRPVHTTCTNHIESVDVTFPNLYPLQKHVVAEVTTSMRQKLSTHRPMYMTLHLSCGFGKTVTACYLMVVHRRKTVICVPNKMLIHQWKVAVELTKLSYIISTDGVSMLLKQLRTKTADVLIIVSRHLSNDYFCKKIHDEYDTFILDESHMYNLMNNSALTKFLTFYPPRICYFLTATPRLMNRIYCNDVVNVLKVSALTKRLKIVEYFFEPYSTDCIRQMAKHLNTENNKYHIYTEKILTEDLPRNNLIVETVSREFRNETI... | DNA helicase which seems to act as a postreplicative transcription termination factor. Involved in ATP-dependent release of nascent RNA. Forms a stable complex with single-stranded DNA, and to a lesser extent RNA (By similarity). |
Q9Q8Y2 | ETF2_RFVKA | Early transcription factor 82 kDa subunit (ETF large subunit) | MRYVVSPQLVLYVEKGQKIKRVLYLTPYGVLDDKSPIYYFLSTHLKITDPEIHRRHILLTLKISQLKGYLCNLLDIRNDIIIYSHKNNLEYSYVDNTIFNPFVHTQKKTLIKSDGFLYNIYPGACDFLVIWVANADDTSIAEFGSYEDVDVNILKFETRLLEVFDNLDLDMNIESKFNNIFRTNLKFTGLRKLIKKINELNGLYYKSLLYKSDEYFINLTGNKFILTDERLNLTVWDPDGVVTFSSDGDTITINNVKLFTSLLTDIDLQMERIKGDVTYKIFLSTPITSRIKLNIETSFIFVETATNNILLSADKRISII... | 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). |
Q9Q921 | RP07_RFVKA | DNA-directed RNA polymerase 7 kDa subunit (EC 2.7.7.6) | MVFQLICSTCGRDISEERFALLIKKIALKTVLKGVKNSCCRLKLSTQIEPQRNLTVEPLLDIN | Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF) thereby a... |
Q9Q926 | MP44_RFVKA | Probable metalloendopeptidase G1-type (EC 3.4.24.-) | MIVFDNGVRVFINTSTNKDIYVGISGFGFEKDIGGILGTAHLLEHILISFDVSRFIANASTARSYMSFWCTSIRGRSTPVDAIRTLISWFFDRDGLKHYFPVSKIKYHIKELENEYYFRNEVFHCMDALTFLANGDLYNGGRLSMLDRLDDMPLILQDRMCAITGPNIVIFVRELNDVVLSLLVSTFGTLPSCPLTIPCTLPTPIGGKIIMMPSPFYTVMVRVQPSLYNILSILCLYEIYHLVDYETVNNKLYVTISFIHEHEYESFLHGSARLNFTIYKKIRLHYGDDFLMNMYLSFPCIRHDIFDYLTIINTNVSTMI... | Seems to be involved in viral proteins maturation by cleavage at Ala-Gly-|-Xaa motifs. |
Q9QAQ4 | IORF_CVBOK | Protein I (Accessory protein N2) (N internal ORF protein) (IORF) (Protein in nucleocapsid ORF) | MASLSGPISPTNLEMFKPGVEELNPSKLLLLSNHQEGMLYPTILGSLELLSFKRERSLNLQRDKVCLLHQESQLLKLRGTGTDTTDVPLKQPMATSVNCCHDGIFTILEQDRMPKTSMAPTLTESSGSLVTRLMSIPRLTFSIGTQVAMRLFRLGFRLARYSLRVTILKAQEGLLLIPDLLHAHPVEPLVQDRAVEPILAIEPLPLV | Structural protein that is not essential for the viral replication either in tissue culture or in its natural host. |
Q9QAR0 | IORF_CVBLS | Protein I (Accessory protein N2) (N internal ORF protein) (IORF) (Protein in nucleocapsid ORF) | MASLSGPISPTNLEMFKPGVEELNPSKLLLLSNHQQGMLYPTILGSLELLSFKRERSLNLQRDKVCLLHQESQLLKLRGTGTDTTDVPLKQPMATSVNCCHDGIFTILEQDRMPKTSMAPTLTESSGSLVTRLMSIPRLTFSIGTQVAMRLFRLGFRLARYSLRVTILKAQEGLHLIPDLLHAHPVEPLVQDRAVEPILAIEPLPLV | Structural protein that is not essential for the viral replication either in tissue culture or in its natural host. |
Q9QAR7 | IORF_CVBLY | Protein I (Accessory protein N2) (N internal ORF protein) (IORF) (Protein in nucleocapsid ORF) | MASLSGPISPTNLEMFKPGVEELNPSKLLLLSNHQEGMLYPTILGSLELLSFKRERSLNLQRDKVCLLHQESQLLKLRGTGTDTTDVLLKQPMATSVNCCHDGIFTIWEQDRMPKTSMAPTLTESSGSLVTRLMSIPRLTFSIGTQVAMRLFRLGFRLARYSLRVTILKAQEGLLLIPDLLHAHPVEPLVQDRVVEPILATEPLPLV | Structural protein that is not essential for the viral replication either in tissue culture or in its natural host. |
Q9QAZ8 | RDRP_SJNNV | RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (RNA replicase) (Protein A) | MRRFEFELARMSGAAFCVVTGYRLLTSKWLADRVEDYRQRVIADRKQILRDAAVIRTSIQKQMELVRISVRKGHSHQEAATERNSATDTMIGVVEKCGYEPYIISPSPREKEYHGSRQFYSLADFRQDYRRDEITDRHVIVMTDVDYYVDMHELVGLGVPILLYTFQPSTVSGEVKDGYFTITDDHVHYRVAGGKDVRHRIWNYNQDTMFVRSKPRGFWASLKQILRDITGITALCGYLYLKLGIAPFGDQVTLFTVDQFKMGEHRNIVSIVPFATCRSNLLKISEYGAELDYMRYQQRNNNANFNAVTYISQEGPLISL... | RNA-dependent RNA polymerase which replicates the viral genome composed of 2 RNA segments, RNA1 and RNA2. |
Q9QB84 | ETF2_YMTV5 | Early transcription factor 82 kDa subunit (ETF large subunit) | MKYTISPQLVIYVGKGQEIKRALYLTPYGILDDKSSIYYFLKTHLNIHNPEIHKRHILLTLKIRQVKGYLSNLLNINDDIIIYSHKNNLEFSYVDNTIFNPFTNTQRKTLIRSDGFLYNIYPGACDFLVIWVTNSKDTPMLEFGSYEEVDSNILKFENHLLDVFNSLDLEMNIESKFNNIFRTNLKSTGLMTIIKKINESDTSYKSLLYKSDEYFINMTGNHFILTDEKLNLSVWDSDSCLAFSSDGDTIVINNVKLFTELVSDINAQMERIKGDVTYKVFLSTPITSRIKLDIETSFVFVETATNNILLSADKKISIIL... | 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). |
Q9QB92 | MCES_YMTV5 | mRNA-capping enzyme small subunit (mRNA (guanine-N(7))-methyltransferase) (EC 2.1.1.56) (mRNA cap methyltransferase) | MDQIAKCIKEGTHTLFPFYDNLPDVNLFLGNSPLPSLEYGANYFLQLSRVNDLNRLPTDLLSLFTHEIMVQENDLEKVYDILNIHSVKSYGKTIKADAVVIDLSAKNKLFKKDRELIKSNNYLTENNLYISDYKMLTFEVFRPLFEMSSEKYCIIKLPTLFGRCVIDTTRVYCSLFKSVRLFKCANDSWLKDSAIIVASNACKKNIDYFMSHIRSVTKSLNWKESNNVQFSILKDSVDKEFIDKFLNFSTKVYESLYYVHSLLYSSMTSESKSIENEYQKKLTKLLL | Catalyzes the last reaction in the mRNA cap formation pathway. |
Q9QBG0 | PG077_VACCP | Telomere-binding protein OPG077 (Telomere-binding protein I1) | MAEFEDQLVFNSISARALKAYFTAKINEMVDELVTRKCPQKKKSQAKKPEVRIPVDLVKSSFVKKFGLCNYGGILISLINSLVENNFFTKDGKLDDTGKKELVLTDVEKRILNAIDKSSPLYIDISDVKVLAARLKRSATQFNFNGHTYHLENDKIEDLINQLVKDESIQLDEKSSIKDSMYVIPDELIDVLKTRLFRSPQVKDNIISRTRLYDYFTRVTKRDESSIYVILKDPRIASILSLETVKMGAFMYTKHSMLTNAISSRVDRYSKKFQESFYEDITEFVKENERVNVSRVVEYLTVPNITISSNAE | DNA-binding protein which binds to the hairpin form of the viral telomeric sequence. Required for the production of mature virions (MV). |
Q9QBU2 | MVP_POLVP | Movement protein (p27) | MEIQSLDGVLGEELAIQNEVKKILLSHKTTKAILPLAPISQFSKWKIPKQGFYAPIDVKFVLTPHISERAQVRGVVKLVDSRDLSPSRELYRSKEFNIGHGLVIEGSQLPFCLPVGDYPLQFEVTVLQSQFRETANLYSTSVEWRMMSSTTPLSRVRSVMGAAQQPAMKLQPNFKMSLESSKGGGMKPHQKKSSKPNGHSRRGNLSGEVGGSSSSLPSGAQTGEWIDNDYGDGSSEYSGVST | 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 (By similarity). |
Q9QBU3 | CAPSD_POLVP | Capsid protein (p40) | MALVKRNNNMALIATEAGKLAAVKAGQVMLSPAGRELIWNGVNWVRRKLGRSKKSDVILHPGVLPGAIAAPVANTRIIRASKPKFTRSKGSVTIAHRELLGQFNNSSGLVVNGGVSGNLYRINPSNPVVFPWLQGIAASFDQYKFDRVQLQYVPMCATTETGRVAIYFDKDQQDVEPADRVELANMGHWTESAPWCESTLNVPVDNVKRFMNDNTTTDRKLVDLGQIGLATYGGGSTNPVGDLFIHYTITLFEPQPLASLVETEQSGAGAAPFGTNLVTVSSNATTTIITFRGPGVYLLALSQRAASFTTLVTAGGAVVN... | Capsid protein self-assembles to form an icosahedral capsid with a T=3 symmetry, about 32-35 nm in diameter, and consisting of 180 capsid proteins. |
Q9QDI8 | MVP_RMV | Movement protein (30 kDa protein) (Cell-to-cell transport protein) | MSYEPKVSDFLALTKKEEILPKALTRLKTVSISTKDVISVKESESLCDIDLLVNVPLDKYRYVGVLGVAFTGEWLVPDFVKGGVTVSVIDKRLENSRESMIGTYRAAAKDRRFQFKLVPNYFVSTADAKRKPWQVHVRIQNLKIEAGWQPLALEVVSVAMVTNNVVVKGLREKVIAVNDPNVEGFEGVVDDFVDSVAAFKAIDSFRKKKKKIGGRDVNNNKYRYRPERYAGPDSLQYKEENGLQHHELESVPVFRSDVGRAHSDA | 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 ... |
Q9QDJ8 | AC4_TYLCC | Protein C4 (10.9 kDa protein) (Protein L4) | MGLLTCMFSSNSKESSSVRIKDSSISHPHTGQHISIRTFRELKAQQMSNPTWKKTETCLIMEFSRSMEDRLEEVANLPTTHMPRQSIQGPKLRPSIY | 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. |
Q9QEE3 | CAPSD_RMV | Capsid protein (Coat protein) | MSYNITSSNQYQYFAAMWAEPTAMLNQCVSALSQSYQTQAARDTVRQQFSNLLSAIVTPNQRFPETGYRMYINSAVLKPLYESLMKSFDTRNRIIETEEESRPSASEVANATQRVDDATVAIRSQIQLLLNELSNGHGLMNRAEFEVLLPWATAPAT | Capsid protein self-assembles to form rod-shaped virions about 18 nm in diameter with a central canal enclosing the viral genomic RNA. |
Q9QEE7 | CAPSD_ICRSV | Capsid protein (CP) (Coat protein) | MSFDYTDPTFRNYPFPHYCDFDRHQHCDHDLRTNPPPTEPPSRKSKLMSTSENKGKQPLHPPPTEGFPKPPPPPSSTPTTPTPPDQTKAPEPIEKRIIHAFHAEPKTHTNGEAPPAFNPNNMNAVPLNLLNINLKYSPVTNSIANPKQTEAIGKAWVRILQIDPANVFLYAIDLARACADAGSSPEADIIGANEDLNPVVERNALAGVVRDFCPLRAFCAYYSRVVWNLMIKADQPPANWMKSGIDEGAKFAAFDFFHGVLSPASLYVPLERHPTAAERIANQAMFAVKIANAPGNGSELTMDHVAFTKGRITADSKPRP... | Required for genome encapsidation. Forms ribonucleoprotein complexes along with TGB1 helicase and viral RNA (By similarity). |
Q9QEJ4 | VP2_PESV | Protein VP2 (Minor capsid protein) | MSWIAGAMQGAGLLGDLAGTIGQIVLHNKQLNIMNSFNQAQIQLAKDQLKQNQQLANQYYEFNANLPVNQYNSAVSAGFDSVSARQLAGSREVRYLGGQQTPLVHQGQIHQMMFSPKHLMQAQHVVGTFSRGMPGVTPSKGLPRPQGVTAKVPVAGATTTHSKV | May be a minor structural protein present in one or two copies per virion. May play a role in RNA genome packaging (By similarity). |
Q9QJ16 | IE2_HHV6Z | Immediate-early protein 2 (IE2) | MKLSGLYHDADVTHRQPLSENTHQDPISSQDSRKNSRTPQDPRRAAQIHRQCTSSASNLPSNGNNSIHMRFASELPDQVLQPMYASQNQTTNSQCNFTSLPYQPNYDAYRSIESSYRESRNTDRGYDSNFRHHSHRPRGGKGRYDSRNYFNPNSKYQQPYGRFFPRSYNRRGRGHRLHDFSNRPADLSYQQYMHPNYEQYNPDLRMNNYKDVTQLTTNFNFQAQDYSMAFSQTSITTDPTYVQSDNHNYPTKTQTTPETTKTKEHENAKDNKEHKKQQVSTSPDAISLSYRPSSQKMDLIKKIYDTEVIPLPKEALIDNG... | Transcriptional transactivator. |
Q9QJ19 | CEP2_HHV6Z | Cytoplasmic envelopment protein 2 | MAISTFSIGDLGYLRNFLQNECNWFRICKKTFYREYRSVATSSPIFSLKNKPKKYCMHCEMVVLKRSHEFMFSLAVNGIHFGQFLTGIMKFKKKQVAEGLCYYVLELGSISPVDLSFIPKYNSDCVTSMHCVTPELIYENCSIVCPEEASRLTVKGLGDNKLIPLGGCGVWCLKNGGDLYIYAFVLAYDLYVACYDKTIFPSLAKIVFDMIACDSEDCVFCKDHNKHVSQAGHIVGCVSNQETCFCYTPCQKKMTDINNPELISLLCDQEINKIDIMYPEKKASLSLDINSYVHGYLGDEPCALKCVNWMPIRISSALSR... | Plays a critical role in cytoplasmic virus egress. Participates in the final step of tegumentation and envelope acquisition within the host cytoplasm by directly interacting with the capsid. Upon virion binding to target cell, a signaling cascade is triggered to disrupt the interaction with the capsid, thereby preparin... |
Q9QJ20 | CVC1_HHV6Z | Capsid vertex component 1 | METHLYYDTLYQYQGGVYPAHICLPTDAYLPMRVDCIESLYFRCVFFKNGMHYTEWSKLKFTVISREIKFKDVLKNADFDELFTGLVVMTIPIPIVDFHFDIDSVILKLVYPQLVHREIVLRLYDLICIRPSSDRPSEVSAKNIGIDFYQLTSQGNKQTPDEEKRCLFFQQGPLEPPSTVRGLKAAGNAKPMQFPAHVNEKMTESFLSDSWFEQKVRCKKILDFTQTYRVVVCWYELSFSREMQIENNLLSASQLKRVNAADFWDRTDRYLRDIGSRVLTHIVKTLQIHNRQFKQKFNCNFPVNFSFEHLLSFMQLGKDF... | Capsid vertex-specific component that plays a role during viral DNA encapsidation, assuring correct genome cleavage and presumably stabilizing capsids that contain full-length viral genomes. {ECO:0000255|HAMAP-Rule:MF_04017}. |
Q9QJ23 | TRM3_HHV6Z | Tripartite terminase subunit 3 (EC 3.1.-.-) (Terminase large subunit) | MLRTCDITHIKNNYEAIIWKGERNCSTISTKYPNSAIFYKKRFIMLTPELGFAHSYNQQVKPLYTFCEKQRHLKNRKPLTILPSLTRKLQEMKFLPASDKSFESQYTEFLESFKILYREPLFLQIDGFIKDFRKWIKGEFNDFGDTRKIQLEPFQKNILIHVIFFIAVTKLPALANRVINYLTHVFDIEFVNESTLNTLKQKTNVFLVPRRHGKTWFIVPIISFLLKNIEGISIGYVAHQKHVSHFVMKEVEFKCRRMFPEKTITCLDNVITIDHQNIKSTALFASCYNTHSIRGQSFNLLIVDESHFIKKDAFSTILGF... | Component of the molecular motor that translocates viral genomic DNA in empty capsid during DNA packaging. Forms a tripartite terminase complex together with TRM1 and TRM2 in the host cytoplasm. Once the complex reaches the host nucleus, it interacts with the capsid portal vertex. This portal forms a ring in which geno... |
Q9QJ26 | MCP_HHV6Z | Major capsid protein (MCP) | MENWQATEILPKIEAPLNIFNDIKTYTAEQLFDNLRIYFGDDPSRYNISFEALLGIYCNKIEWINFFTTPIAVAANVIRFNDVSRMTLGKVLFFIQLPRVATGNDVTAPKETTIMVAKHSEKHPINISFDLSAACLEHLENTFKNTVIDQILNINALHTVLRSLKNSADSLERGLIHAFMQTLLRKSPPQFIVLTMNENKVHNKQALSRVQRSNMFQSLKNRLLTSLFFLNRNNNSSYIYRILNDMMESVTESILNDTNNYTSKENIPLDGVLLGPIGSIQKLTNILSQYISTQVVSAPISYGHFIMGKENAVTAIAYRA... | Self-assembles to form an icosahedral capsid with a T=16 symmetry, about 200 nm in diameter, and consisting of 150 hexons and 12 pentons (total of 162 capsomers). Hexons form the edges and faces of the capsid and are each composed of six MCP molecules. In contrast, one penton is found at each of the 12 vertices. Eleven... |
Q9QJ27 | TRX2_HHV6Z | Triplex capsid protein 2 | METVYCTFDHKLSLSDISTLCKLMNIVIPIPAHHHLIGSGNLGLYPIVSSNKDYVHIRNVLRTMVVTILQKVEGNQLVLRKPMTGQQYAIKNTGPFPWEKGDTLTLIPPLSTHSEEKLLKLGDWELTVPLVVPTAIAAEINIRLLCIGLIAVHREYNEMQTIIDELCSIQYRDVLIKLPDIVNDKQSMYSMKTACISLSMITAMAPDIVRTYIDRLTLEDHSMLLIKCQELLSKRTTLSTQRCGQLHATDIKDELKKIKSVLTMIDQINSLTNEKTYFVVCDVSADNRMATCIYKN | Structural component of the T=16 icosahedral capsid. The capsid is composed of pentamers and hexamers of major capsid protein/MCP, which are linked together by heterotrimers called triplexes. These triplexes are formed by a single molecule of triplex protein 1/TRX1 and two copies of triplex protein 2/TRX2. Additionally... |
Q9QJ32 | DPOL_HHV6Z | DNA polymerase catalytic subunit (EC 2.7.7.7) | MDSVSFFNPYLEANRLKKKSRSSYIRILPRGIMHDGAAGLIKDVCDSEPRMFYRDRQYLLSKEMTWPSLDRVRSKDYDHTRMKFHIYDAVETLMFTDSIENLPFQYRHFVIPSGTVIRMFGRSEDGEKICVNVFGQEQYFYCECVDGKSLKATINNLMLTGEVKMSCSFVIEPADKLSLYGYNANTVVNLFKVSFGNFYVSQRIGKILQNEGFVVYEIDVDVLTRFFVDNGFLSFGWYNVKKYIPQDMGKGSNLEVEINCHVSDLVSLENVNWPLYGCWSFDIECLGQNGNFPDAENLGDIVIQISVVSFDTEGDRDERH... | Replicates viral genomic DNA. |
Q9QJ33 | UL32_HHV6Z | Packaging protein UL32 homolog | MYKGWDSEALSIQSEIVNEILLYCYLTPQPPIPSETTTATSPTNIENEISNLESSENLEELKRLSVALNIDRRCNICSIVNLCLKQNKSWIYDYSLLCYKCNYAPKTPLSLLIVSAEFIMLIRERFPNINFDGLFQNNIVSIFDFHVHFFIHRCFANTVNDHIQSENITLNHMAIIRSTLLKEDSIPHIKIKKFLTKKMNPKKTQSPELNKKLTVPMKTRFTTLLFYMWSGTNVFDRVPFTDLTIRKHRFIKNLYSNKTDIELTAGPILLAQIPFSITKNKTTSVCLLCELMAASKQDYLFLKYLHQSIMDYCQNNLKMI... | Plays a role in efficient localization of neo-synthesized capsids to nuclear replication compartments, thereby controlling cleavage and packaging of virus genomic DNA. |
Q9QJ34 | TRM2_HHV6Z | Tripartite terminase subunit 2 | MMDSSPEKTNLELLYEQVCEQGREFEVVFYPMLPRLYEMMLPSLEARLNFLSVGYRHVAFSRYVHGDVDCVHREVMAQKMVLLTSILSKLLNVNGILEHQEYLNTE | Component of the molecular motor that translocates viral genomic DNA in empty capsid during DNA packaging. Forms a tripartite terminase complex together with TRM1 and TRM3 in the host cytoplasm. Once the complex reaches the host nucleus, it interacts with the capsid portal vertex. This portal forms a ring in which geno... |
Q9QJ35 | NEC2_HHV6Z | Nuclear egress protein 2 | MANVLKEKMYDELLSATCRILKLGSHDYRMTERNLLSKNPKFPLCDIILKLDYAYNLEYLLSLWEHVTKQEPRFVFKNTGGAVSMSCYLHAPVKAEGHHAVRECNILRVNECLTVRMSDIVAMKPSTFAVFTKCIIRRNRDETYVVEFVAFGPENESEYISLLKAIFLKKCSMGKQHLESNRFCQGLRRRSSHVLEKGQLGSSGEIANKASAVVTSQESINQFYEKEKSFLSGVKFSRLSERHCRVAIVSICFLLALYFCYVLLKKTPTPASGPVV | Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear m... |
Q9QJ38 | ITP_HHV6Z | Inner tegument protein | MTHDNRQLLPQETKLVTPNKDTLSSRYLHVLIIDNTLSTIEFVYMVVKAVLTQADTLKAFEQRKNRPTNRILGLSTSVSKRYINIPKFSSSGANNSQGVKTLAAIRKFSLPDKNCFRNFLSFSTTLFKVPASIDIYFLFFTASTVSTMAARALDLEFILSSLKNSTSPESLLAATAKIEILSLAADSVTHNRVIAFINRLPPKKYHFDLIREYTVFYFLNSTTLTSENKLLSAELLHEELSQIRSSSSPGTELENLNNAEVLYVFDRILNSIKMLKNELSSPIGKLRVQPAANDPGTDKTIKYSKIQSIIQKVHSFTREN... | Plays an essential role in cytoplasmic secondary envelopment during viral egress. Interacts with the capsid via the large tegument protein/LTP and participates in its transport to the host trans-Golgi network (TGN) where secondary envelopment occurs. Modulates tegumentation and capsid accumulation at the viral assembly... |
Q9QJ39 | RIR1_HHV6Z | Ribonucleoside-diphosphate reductase large subunit-like protein | MKRKERRINKDFGYNRKCVCHYEASQKRFCYSQYSCASVLYERVRDIAKIMDRLDSGLDAWCLRDAIISVLRATHCVPRVDRMLGRWYLKTSIFYDFCPDDLILSCPNVIMPNVLNFVKKYRDFIRSVLYKVSVSWKNQYMPGVLGASRFLEEISNSLNGVEESIPCIYLRMCATLTEIVLRNGYLREIYQENPYVIFEELAFSLFTQKWVLPFSCMTNLGLVEKANSTVFDVAIYNTCLYSLADFITVNGEHLFPALLNGSNISMNVTRYQQEAKNIFEILLSQIQVVERDTDKTVQLTVYVEVWHVSALTWLDLYQVL... | Does not possess a ribonucleotide reductase activity. Betaherpesviruses probably use another strategy to expand the dNTP pool in a quiescent host cell. {ECO:0000255|HAMAP-Rule:MF_04027}. |
Q9QJ40 | VPAP_HHV6Z | DNA polymerase processivity factor (Phosphoprotein P41) (PP41) (Polymerase accessory protein) (PAP) | MERGSRDHHRDHRDHREHRELREPPTLAFHMKSWKTINKPLKAFTKLLKENTTVTFTPQPSIIIQSAKNHLVQKLTIQAECLFLSDTEHFLTKTINNHIPLFESFMNIISNPEVTKLYIQHDSDLYTRVLVTASDTCTQASVPCVHGQEVVRDSGKSPLRIDLDHSTVSEVLKWLSPVTKTKRSGKSDAFMAHIIVQVNPPTIKFVTEMNELEFSNSNKVIFYDVNNMRFNLSAKNLQQALSMCAVIKTSCSLRTVAAKDCKLILTSKSTLLTVEAFLTQEQLKEESRFERMGKQDDGKGDRNHKNEDGSALASKQETQY... | Accessory subunit of the DNA polymerase that acts to increase the processivity of polymerization. |
Q9QJ42 | U24_HHV6Z | U24 protein | MDRPRTPPPSYSEVLMMDVMYGQVSPHASNDTSFVECLPPPQSSRSAWNLWNKRRKTFAFLVLTGLAIAMILFIAFVIYVFNVNRRKK | Down-regulates the TCR/CD3E complex and the transferrin receptor TFRC in host T-cells by blocking them from recycling back to the cell surface. |
Q9QJ45 | U21_HHV6Z | U21 glycoprotein | MMICFVFLCVLTFVRGEIYPSTCPALGAGNGEAVRSGEMLLEISAYRNWRSGKMELWGSAAVNNQVFYGGMEDSQIEYDFGKFLVFRCFQVFHNVHKLLFNTVSSATMHLARKRVQKCGHGKMTFISIQVQCSVNKKSIRLSRMNETNLKKQVLRVAFFLDGSNNSWIADKNFQGEDRTMLRLWTELSTYRQYLISSCNNDVKVLSELYGEFRRMALSYDEELKLNFMPVIRSSSERLFRADDLKCSFSRWLGAEGEFAVCEYSGWGVSKLGKIEIFAEEPLTFDMVWKTVKMRSSGAYTSLFRDDVTWGLISLDKWVGD... | Binds to MHC class I molecules in the endoplasmic reticulum and targets them from the Golgi directly to the lysosomes. Once in the lysosomes both proteins are degraded. In consequence, surface class I molecules are down-regulated and infected cells are masked for immune recognition by cytotoxic T lymphocytes (By simila... |
Q9QJT5 | NV_SHRV | Non-virion protein | MPGNNHNDRPVALIMSRLSRDPRDCIHHTVDTRGMTPGKIIHQVIPPHPTQMRHTNRPSPPVILNLQILSEGGHVCARDVDTADPVPRAGPERTIQWGTDRDATEELASPAPEEIYEDNDSW | Plays an essential role for the viral pathogenicity. |
Q9QJT7 | MATRX_SHRV | Matrix protein | MPFIRRPKRAILIPPLHLTLKDDDKVLVVETVGTLIISGMTPSNLTEKLGLAMKLASAILGGDSHPAFNPLVEIFSGAMEFGASVEKLDFMTRENKVITTYKVARGKAVALSNFPMEKRVGEKSYTTQIRNGSITYTGSFLFSAEHVGLKDNRSLFAAGEGLRESPDMAQAREAFAGSLPKGKNESSRK | Plays a major role in assembly and budding of virion. Completely covers the ribonucleoprotein coil and keep it in condensed bullet-shaped form. Inhibits viral transcription and stimulates replication (By similarity). |
Q9QJT8 | PHOSP_SHRV | Phosphoprotein (Protein P) (Protein M1) | MAESIEMGEELVSSPSTLLALKGKLENPSPDDATILGILGKKTPTVKMEKGKGKGDPIEAFLLEFVDERRQVEANKRLRQYIRQLKMSHQEELTAHLERASAENRANLKSMMESQAESNKTTKTILATLITLRDHVIEEGSKKPRGLDKDQIKLERALGFERGYSSAIAIVNQLKVTEPSQVCKPSVRAAALSAMEKGEFESSGEVFKAVVKRAKAELTK | Non catalytic polymerase cofactor and regulatory protein that plays a role in viral transcription and replication. Stabilizes the RNA polymerase L to the N-RNA template and binds the soluble protein N, preventing it from encapsidating non-genomic RNA (By similarity). |
Q9QJT9 | NCAP_SHRV | Nucleoprotein (NP) (Nucleocapsid protein) (Protein N) | MAFQKEFFGLRDVKVDLSAGEGLDFDPSEVELTVYRTGADTDGNTIIKALAAVGGPKTNEALSVLLAFVTLGTDQDEYETRIKILKEIGFSVKEVPMAKDASSGIEAPLENVAALVKPETVYQVIRGVLYTCALFVKYNVEKMQKYIKNKLPALATSYGVPELEEFPTESSALKKLASCIRPGQRITNALYAFLLVEMARPETQQGARALAAMRINGTGMTMVGLFTQAAKNLGATPSDLLEDLCMRSLVDSARRIVRLMVQVSQAETIQARYAVMMSRMLNENYFKAYGLNDNSRISAILVAVNGHFSEDTIEALEGIK... | Encapsidates the genome, protecting it from nucleases. If expressed without protein P it binds non-specifically RNA and therefore can bind it's own mRNA. Interaction with protein P abolishes any non-specific RNA binding, and prevents phosphorylation. The soluble N-P complex encapsidates specifically the genomic RNA, wi... |
Q9QL89 | NCAP_HIRRV | Nucleoprotein (NP) (Nucleocapsid protein) (Protein N) | MANLKEEFAGLRGVKGGALEDSGTEYDPTKINLTLYGTDKLYTLAIIKRAVSQVGGSQTNKALGILCAFVTSENNPDMTDAAVKLLVDMRFKVDVVPVDDRLGDNLDDPNSKLAEVLTEENMVDLVKGLLFTCALMVKYDVDKMATYCQQKLERLANSQGLNELTLISTSRAVLARIGAAVRPGQKLTKAIYGIILINLMDPATAARAKALCAMRLSGTGMTMVGLFNQASKNLGAPPADLLEDLCMKSIIDSARRIVKLMRIVADVEDMTAKYAIMMSRMLGDGYFKSYGINENSRITCILMNINEQYDEGTTGGLAGV... | Encapsidates the genome, protecting it from nucleases. If expressed without protein P it binds non-specifically RNA and therefore can bind it's own mRNA. Interaction with protein P abolishes any non-specific RNA binding, and prevents phosphorylation. The soluble N-P complex encapsidates specifically the genomic RNA, wi... |
Q9QM81 | V_TPMV | Non-structural protein V | MNNTEIIENASKVLEAIDAAKEEELRNLNSLVQPRAPLNAGSTPGEIINEIKHLSTRDQEGGTSSKDEEESGAGRTVAEGAATRDHKYSKSRPKKQPRSGLQSGAAGKNPTPDGEGGDTCNRELDQHSDGDGHSNTEGASSDLASIQPCQTDDAPCSSTSYLDEEDEPAVRPKTQCKQSGLIESKEDEDGMLSELHEQHKGRSKRLSALGRVNSSPIPSPRPDELLKKGHRREYSMVWSNDGVFIESWCNPMCARIRPLPIREICVCGRCPLKCSKCLLDPE | Blocks host interferon signaling. |
Q9QNB0 | VP6_ROTHK | Intermediate capsid protein VP6 | MEVLYSLSKTLKDARDKIVEGTLYSNVSDLIQQFNQMIVTMNGNDFQTGGIGNLPIRNWTFDFGLLGTTLLNLDANYVENARTTIEYFIDFIDNVCMDEMAREAQRNGVAPQSEALGKLAGIKFKRINFDNSSEYIENWNLQNRRQRTGFVFHKPNIFPYSASFTLNRSQPMHDNLMGTMWLNAGSEIQVAGFDYSCAINAPANIQQFEHIVQLRRALTTATITLLPDAERFSFPRVINSADGATTWFFNPVILRPNNVEVEFLLNGQIINTYQARFGTIIARNFDTIRSLFQLMRPPNMTPAVNALFPQAQPFQHHATV... | Intermediate capsid protein that self assembles to form an icosahedral capsid with a T=13 symmetry, which consists of 230 trimers of VP6, with channels at each of its five-fold vertices. This capsid constitutes the middle concentric layer of the viral mature particle. The innermost VP2 capsid and the intermediate VP6 c... |
Q9QNB2 | VP2_ROTHK | Inner capsid protein VP2 | MAYRKRGAKREDLSQQHERLQEKEIENNTDVTMENKNNNNNRKQRLSDKVLSQKEEIITDVQDDIKIADEVKKSSKEESKQLLEILKTKEEHQKEVQYEILQKTIPTFEPKESILKKLEDIRPEQAKKQMKLFRIFEPRQLPIYRTNGEKELRNRWYWKLKKDTLPDGDYDVREYFLNLYDQILIEMPDYLLLKDMAVENKNSRDAGKVVDSETANICDAIFQDEETEGVIRRFIADMRQQVQSDRNIVNYPSILHPIDHAFNEYFLNHQLVEPLNNEIIFNYIPERIRNDVNYILNMDMNLPSTARYIRPNLLQDRLNL... | Inner capsid protein that self-assembles to form an icosahedral capsid with a T=2 symmetry, which consists of 120 copies of VP2, with channels at each of its five-fold vertices. This capsid constitutes the innermost concentric layer of the viral mature particle. It encapsidates the polymerase VP1, the capping enzyme VP... |
Q9QPN4 | MVP_TRVPP | Movement protein (29 kDa protein) (Cell-to-cell transport protein) (P1a) | MEDKSLVTLKKKTFEVSKFSNLGAIELFVDGRRKRPKYFHRRRETVLNHVGGKKSEHKLDVFDQRDYKMIKSYAFLKIVGVQLVVTSHLPADTPGFIQIDLLDSRLTEKRKRGKTIQRFKARACDNCSVAQYKVEYSISTQENVLDVWKVGCISEGVPVCDGTYPFSIEVSLIWVATDSTRRLNVEELNSSDYIEGDFTDQEVFGEFMSLKQVEMKTIEAKYDGPYRPATTRPKSLLSSEDVKRASNKKNSS | 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. Displays RNA-binding activity. |
Q9QUB8 | CAPSD_TTVV2 | Capsid protein | MAYGWWRRRRRRWRRWRRRPWRRRWRTRRRRPARRRGRRRNVRRRRRGGRWRRRYRRWKRKGRRRKKAKIIIRQWQPNYRRRCNIVGYIPVLICGENTVSRNYATHSDDTNYPGPFGGGMTTDKFTLRILYDEYKRFMNYWTASNEDLDLCRYLGVNLYFFRHPDVDFIIKINTMPPFLDTELTAPSIHPGMLALDKRARWIPSLKSRPGKKHYIKIRVEAPKMFTDKWYPQTDLCDMVLLTVYATTADMQYPFGSPLTDSVVVNFQVLQSMYDQNISILPTEKSKRTQLHDNITRYTPFYNTTQTIAQLKPFVDAGNVT... | Self assemble to form an icosahedral capsid. |
Q9QXI3 | GPR26_RAT | G-protein coupled receptor 26 | MNSWDAGLAGLLVGTIGVSLLSNGLVLLCLLHSADIRRQAPALFTLNLTCGNLLCTVVNMPLTLAGVVAQRQPAGDRLCRLAAFLDTFLAANSMLSMAALSIDRWVAVVFPLSYRAKMRLRDAAFMVAYTWLHALTFPATALALSWLGFHQLYASCTLCSRRPDERLRFAVFTSAFHALSFLLSFIVLCFTYLKVLKVARFHCKRIDVITMQTLVLLVDIHPSVRERCLEEQKRRRQRATKKISTFIGTFLVCFAPYVITRLVELFSTAPIDSHWGVLSKCLAYSKAASDPFVYSLLRHQYRRSCKELLNRIFNRRSIHS... | Orphan receptor. Displays a significant level of constitutive activity. Its effect is mediated by G(s)-alpha protein that stimulate adenylate cyclase, resulting in an elevation of intracellular cAMP (By similarity). |
Q9QXU2 | SURF1_RAT | Surfeit locus protein 1 | MAAVMALTVLRSRITRWPQWACAGPAPFCAVRRSVFGFSVRSGMVCRPHRCCSSTAETAAAKAEDDSFLQWFLLFIPATAFGLGTWQVQRRKWKLKLIAELESRVMAEPIPLPADPMELKNLEYRPVKVRGHFDHSKELYIMPRTMVDPVREARDAGRLSSTESGAYVVTPFHCSDLGVTILVNRGFVPRKKVNPETRQQGQVLGEVDLVGIVRLTENRKPFVPENNPERSLWYYRDLDAMAKRTGTDPIFIDADFNSTTPGGPIGGQTRVTLRNEHMQYIITWYGLCAATSYLWFRKFVRRTPGV | Component of the MITRAC (mitochondrial translation regulation assembly intermediate of cytochrome c oxidase complex) complex, that regulates cytochrome c oxidase assembly. |
Q9QXX2 | IFNG_SIGHI | Interferon gamma (IFN-gamma) | MNSRLCIMALLLCFSQALLGHFTVIEEIEKLKKYFNSSSSDVGDQKDIVSDILRNWQNDRDVKVIESQIVSFYLKLFEALKEHKTIQESINTIRADLIVNFFNNSREKMDDFIKLTTIPVNDLQVQRKAVNELVGVMHRLSSNIRRKKKGSRCCFGGGDRLNQNYPARSI | Type II interferon produced by immune cells such as T-cells and NK cells that plays crucial roles in antimicrobial, antiviral, and antitumor responses by activating effector immune cells and enhancing antigen presentation. Primarily signals through the JAK-STAT pathway after interaction with its receptor IFNGR1 to affe... |
Q9QYR2 | RHOX5_MUSMI | Homeobox protein Rhox5 (Homeobox protein Pem) (Placenta and embryonic expression protein) (Reproductive homeobox on chromosome X 5) | MEAQSSSRQVTGPLYLGVKEDWEEQHDVKAEAFLQAGEGRKEKGAQGQPGVGAVGKEGEGEELSGGEGQFGPGAPGPMGDEDKDGGTRAGGVEEEQNEPAAEGTESQKNGKPEDRQMPLQGSRFAQQRLSELQSILQRTNSFDVPREDLYRLMDTCVARVQNWFKIRRAAARRNRRRTTPVPEHFRGTFECPACRGVRWGERCPFATPRF | Transcription factor required for differentiation of embryonic stem cells (ESCs) into primordial germ cells. |
Q9QYU2 | EFTS_RAT | Elongation factor Ts, mitochondrial (EF-Ts) (EF-TsMt) (2A3-2) | MSLLRSLRFFPVACTGRSARAVLLQPSQPWHTLHAGPSLSSSASSKELLMKLRRTTGYSFVNCKKALETCGGDLKQAEAWLHKQAQKEGWSKAAKLHGRKTKEGLIGLLQEENTAVLVEVNCETDFVSRNVKFQQLVQQVALGTMAHCQNLTDQLSTYSKGFLNSSELSELAAGPDGEGSLKDQLALAIGTLGENMSLKRAAWVKVPSGFYVGSYVHGEMQSPSLQNLVLGKYGALVICQTPEQITNLEEVGRRLGQHVVGMAPLSVGSLDDEPGGETETRMLPQPYLLDPSITLGQYVQPQGVTVVDFVRFECGEGEQV... | Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome. {ECO:0000255|HAMAP-Rule:MF_03135}. |
Q9QYW5 | EMP3_RAT | Epithelial membrane protein 3 (EMP-3) | MSLLLLVVSALHILILVLLFVATLDKSWWTLPEKESLNLWYDCTWNTTAKTWACSNVSENGWLKAVQALMVLSLILCCLSFILFMIQLYTMRRGGLFYATGLCQLCTSAAVFSGALIYAIHAKEILAKHPSGGSFGYCFALAWVAFPLALVSGIIYIHLRKRE | Probably involved in cell proliferation and cell-cell interactions. |
Q9QZ57 | HSPB3_MOUSE | Heat shock protein beta-3 (HspB3) | MAKIILRHLIETPVRYQEEFEARGLEDCRLDHTLYALPGPTIEDLSKARGAGTPQALAEDSASTEKPPGEGKSRFQILLDVVQFLPEDIIIQTFEGWLLIKAQHGTRMDEHGFISRSFTRQYKLPDGVETKDLSAILCHDGILVVEVKDSLGTK | Inhibitor of actin polymerization. |
Q9QZ58 | HSPB3_RAT | Heat shock protein beta-3 (HspB3) | MAKIILRHLIETPVRYQEEFEARGLEDCRLDHALYALPGPTIEDLRKARGTPKALAEDSDSAETPPGEGKSRFQILLDVVQFLPEDIIIQTFEGWLLIKAQHGTRMDEHGFISRSFTRQYKLPDGVETKDLSAILCHDGILVVEVKDPLETK | Inhibitor of actin polymerization. |
Q9QZM9 | FBX16_MOUSE | F-box only protein 16 | MMAFAPPKSIDGPKMQTKMSTWTPLNHQLLNDQVFEERRALLGKWFDKWTDSQRRRILTGLLERCSLSQQKFCCRKLQEKIPAEALDFTTKLPRVLSVYIFSFLDPRSLCRCAQVSWYWKSLAELDQLWMLKCLRFNWYISFSPTPFEQGVWKKHYIQMVRELHVTKPKTPPKDEFTTADVQPIPGNSPDEKQSPSLAFRSSSSLRKKNNPGEKELPPWRSSDKHPTDIIRFNYLDNCDPELFRLGRRKRSEVTPDFKRQLRDKKNKLQDRARLRKAQSLISLSSPPKVPVRLAWPLHLPVAPSDREAATEALLEHLQKH... | Probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. |
Q9QZN0 | FBX15_MOUSE | F-box only protein 15 | MPSEILVKILSYLDAVTLVCIGCVSRRFYHLADDNLIWVRKYAAAFRSKRSRWKATSVEETATSLSLLSVWDKEDGYWKKEYITKQISSVRAALTNSLSPVKRRTSLPSKTKESLRISGLGWTIILREASGKEHIMQHSNLSVNDNSVTVFWHDKNWPHVDTLSTLDLYGATPIFMEQYKGPNTSCPRWLSLIEKYDLSNLRKSAMIGCDRHVRVFCVNPGLLVGLWQENGGLAFVMANIHSHGLFERSIMGSDTIPYTLPPDTTFVDNYPDSMTFYGDKGFQLHIDIHGSKTYFLCSTFHNLFCRRAGINNGYVKFLMI... | Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. |
Q9QZN3 | FBX8_MOUSE | F-box only protein 8 | MGQGLWRVARNHHLQQEAYSETGYLSREQSRRVASSNISHTSHRKQAQGGIDIYHLLKARKSKEQEGFINLEMLPPELSFTILSYLNATDLCLASCVWQDLANDELLWQGLCKSTWGHCSIYNKNPPLGFSFRKLYMQLDEGSLTFNANPEEGVSYFMSKGILDDSPKEIAKFIFCTRTLNWKKLRIYLDERRDVLDDLVTLHNFRNQFLPNALREFFRHIHAPEERGEYLETLITKFSHRFCACNPDLMRELGLSPDAVYVLCYSLILLSIDLTSPHVKNKMSKREFIRNTRRAAQNISEDFVGHLYDNIYLIGHVAA | May promote guanine-nucleotide exchange on an ARF. Promotes the activation of ARF through replacement of GDP with GTP (Potential). |
Q9QZU5 | KR151_MOUSE | Keratin-associated protein 15-1 (Keratin-associated protein 15) (Pubertal mammary gland-specific protein 2) | MSYTCNSGNYSSQSFGGFLRQPVSTYNSFYPTSNVVYSPKNFQLGSSFYNGQQETFSEPLEGHLPCVGSASFHTSCFRPKQYFSSPCQGGFTGSFGYGNTGFGAFGFGSSGIRSQGCGSNFYRPGYFSSKSIQSSYYQPGYSSGFCGSNF | 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... |
Q9R0Q9 | MPU1_MOUSE | Mannose-P-dolichol utilization defect 1 protein (Suppressor of Lec15 and Lec35 glycosylation mutation homolog) (SL15) | MAGEADGRFKGLLVPILLPEKCYDQLFVQWDLLHVPCLKILLSKGLGLGIVAGSLLVKLPQVFKLLGAKSAEGLSLQSVMLELVALTGTVVYSITNNFPFSSWGEALFLTLQTVAICFLVMHYRGETVKGVAFLACYAMVLLALLSPLTPLAVVTLLQASNVPAVVVGKLLQAATNYRNGHTGQLSAITVFMLFGGSLARIFTSVQETGDPLMAGVFVVSSLCNGLIAAQVLFYWNAKAPHKQKKEQ | Required for normal utilization of mannose-dolichol phosphate (Dol-P-Man) in the synthesis of N-linked and O-linked oligosaccharides and GPI anchors. |
Q9R0Z7 | AAGAB_RAT | Alpha- and gamma-adaptin-binding protein p34 | MAAGVPCALVTSCSATFTGDRLVQHILGTEDAVVEATSSDAVRFYPWTIDNKYYSAEVNLCVVPSKCRVTAEIAEAVQAFVVYFDSTQKSGLDSVSSWLPLAETWLPEVMILVCDRVCEDGINRQQAQEWCIKHGFELVELCPEELPEEDDDFPESTGVKRIVQALNANVWSNVVMKNDRSQGFSLLNSLAGASRSVGSAESCQCEQEPSPTAERTESLPGHRSGACGPAGAQVDSIVDPMLDLDIQELASLTTGGGDLENFERLFSKLKEMKDKAATLPHEQRKLHAEKVAKAFWMAIGGDRDEIEGLSSDDEH | May be involved in endocytic recycling of growth factor receptors such as EGFR. |
Q9R1Q7 | PLP2_MOUSE | Proteolipid protein 2 | MADSERLSAPGCWLACTSFSRTKKGILLFAEIILCLVILICFSASTTSAYSSLSVIEMICAAVLLVFYTCDLHSKISFINWPWTDFFRSLIATILYLITSIVVLVEGRGSSRVVAGILGLLATLLFGYDAYITFPLKQQRHTAAPTDPTDGP | May play a role in cell differentiation in the intestinal epithelium. |
Q9R4J4 | ASPN_PSEFR | Peptidyl-Asp metalloendopeptidase (EC 3.4.24.33) (Endopeptidase Asp-N) | ESNQGYVNSNVGIELARYETTNYTESGSFDTDLARFRGTSDSIHTSRNTYTAADCATGYYSFAHEIGHLQSARDIATDSSTSPYAYGHGYRYEPATGWRTIMAYNCTRSCPRLNYWSNPNISYDIGPDNQRVLVNTKATIAAFR | Metalloprotease, specifically cleaves on the N-terminal side of aspartyl, glutamyl and cysteic acid residues. |
Q9R4P2 | RS20_BREVE | Small ribosomal subunit protein bS20 (30S ribosomal protein S20) | ANNPGARKAIRKIEARTEVN | Binds directly to 16S ribosomal RNA. |
Q9R4P5 | RL24_BREDI | Large ribosomal subunit protein uL24 (50S ribosomal protein L24) | AAKIKKGDNVVVLTG | 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. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. |
Q9R4P7 | RS20_BREDI | Small ribosomal subunit protein bS20 (30S ribosomal protein S20) | ANNAGARKAIRKIEARTEVN | Binds directly to 16S ribosomal RNA. |
Q9R5C6 | LC3_BACIU | Antibacterial protein LC3 (Antibacterial protein LCIII) | ASGGTVGXYGAWMRSXSLVSXSTITTFS | Antibacterial activity against X.campestris, especially strain G, and P.solacearum PO1. |
Q9R5H8 | GVPA_DACSA | Gas vesicle protein A (GvpA) (Gas vesicle structural protein) (GVP) | AVEKTNSSSSLGEVVDRILDKGVVVDLWVRVSLVGIELLALEARVVI | Gas vesicles are hollow, gas filled proteinaceous nanostructures found in some microorganisms. During planktonic growth they allow positioning of the organism at a favorable depth for light or nutrient acquisition. GvpA forms the protein shell. {ECO:0000255|HAMAP-Rule:MF_00576, ECO:0000269|PubMed:1527496}. |
Q9R5K5 | CH60_DELAC | Chaperonin GroEL (EC 5.6.1.7) (60 kDa chaperonin) (Chaperonin-60) (Cpn60) | HAKDVVFGGEARARMVEGVNILANA | Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. {ECO:0000255|HAMAP-Rule:MF_00600}. |
Q9R5V7 | RL31_PSEME | Large ribosomal subunit protein bL31 (50S ribosomal protein L31) | MKADIHPNYVEIDATXSXGN | Binds the 23S rRNA. |
Q9R6P8 | IF1_MYCGA | Translation initiation factor IF-1 | MKETNLSIKGVVKEIIKGDKFKVLLENNLLIEAHVSGKIRMHKIRILPGDSVEVEFSPYDLTKGRIIYRH | One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-... |
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