ID POLG_HRV2 STANDARD; PRT; 2150 AA. AC P04936; DT 13-AUG-1987 (Rel. 05, Created) DT 13-AUG-1987 (Rel. 05, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE GENOME POLYPROTEIN [CONTAINS: COAT PROTEINS VP1 TO VP4; CORE PROTEINS DE P2A TO P2C, P3A; GENOME-LINKED PROTEIN VPG; PICORNAIN 3C DE (EC 3.4.22.28) (PROTEASE 3C) (P3C); RNA-DIRECTED RNA POLYMERASE P3D DE (EC 2.7.7.48)]. OS Human rhinovirus 2 (HRV-2). OC Viruses; ssRNA positive-strand viruses, no DNA stage; Picornaviridae; OC Rhinovirus. OX NCBI_TaxID=12130; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=85215603; PubMed=2987843; RA Skern T., Sommergruber W., Blaas D., Gruendler P., Fraundorfer F., RA Pieler C., Fogy I., Kuechler E.; RT "Human rhinovirus 2: complete nucleotide sequence and proteolytic RT processing signals in the capsid protein region."; RL Nucleic Acids Res. 13:2111-2126(1985). RN [2] RP REVISIONS. RA Kuechler E.; RL Submitted (FEB-1986) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: P3C POLYPEPTIDE IS A PROTEASE THAT CLEAVES AT CERTAIN CC Q/G SITES IN THE POLYPROTEIN. IT MAY BE A CYSTEINE PROTEASE. CC -!- SUBUNIT: THE VIRUS CAPSID IS COMPOSED OF 60 ICOSAHEDRAL UNITS, CC EACH OF WHICH IS COMPOSED OF ONE COPY EACH OF PROTEINS VP1, VP2, CC VP3, AND VP4. CC -!- PTM: SPECIFIC ENZYMATIC CLEAVAGES IN VIVO YIELD MATURE PROTEINS. CC -!- SIMILARITY: THE PROTEASE BELONGS TO PEPTIDASE FAMILY C3. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X02316; CAA26181.1; -. DR PIR; A03902; GNNYH2. DR HSSP; Q82122; 1AYN. DR MEROPS; C03.007; -. DR MEROPS; C03.021; -. DR INTERPRO; IPR000081; -. DR INTERPRO; IPR000199; -. DR INTERPRO; IPR000605; -. DR INTERPRO; IPR001205; -. DR INTERPRO; IPR001676; -. DR INTERPRO; IPR002527; -. DR PFAM; PF00548; Cys-protease-3C; 2. DR PFAM; PF00947; Pico_P2A; 1. DR PFAM; PF01552; Pico_P2B; 1. DR PFAM; PF00680; RNA_dep_RNA_pol; 1. DR PFAM; PF00910; RNA_helicase; 1. DR PFAM; PF00073; rhv; 3. KW Polyprotein; Coat protein; Core protein; Transferase; KW RNA-directed RNA polymerase; Hydrolase; Thiol protease; Myristate. FT CHAIN 2 69 COAT PROTEIN VP4 (P1A). FT CHAIN 70 330 COAT PROTEIN VP2 (P1B). FT CHAIN 331 567 COAT PROTEIN VP3 (P1C). FT CHAIN 568 856 COAT PROTEIN VP1 (P1D). FT CHAIN 857 992 CORE PROTEIN P2A. FT CHAIN 993 1087 CORE PROTEIN P2B. FT CHAIN 1088 1409 CORE PROTEIN P2C. FT CHAIN 1410 1486 CORE PROTEIN P3A. FT CHAIN 1487 1507 GENOME-LINKED PROTEIN VPG (P3B). FT CHAIN 1508 1690 PICORNAIN 3C. FT CHAIN 1691 2150 RNA-DIRECTED RNA POLYMERASE P3D. FT LIPID 2 2 MYRISTATE (BY SIMILARITY). FT ACT_SITE 1654 1654 PROTEASE (POTENTIAL). FT ACT_SITE 1668 1668 PROTEASE (POTENTIAL). SQ SEQUENCE 2150 AA; 241975 MW; 6E0DF9F4945D9D0C CRC64; MGAQVSRQNV GTHSTQNSVS NGSSLNYFNI NYFKDAASNG ASKLEFTQDP SKFTDPVKDV LEKGIPTLQS PTVEACGYSD RIIQITRGDS TITSQDVANA IVAYGVWPHY LSSKDASAID KPSQPDTSSN RFYTLRSVTW SSSSKGWWWK LPDALKDMGI FGENMFYHYL GRSGYTIHVQ CNASKFHQGT LIVALIPEHQ IASALHGNVN VGYNYTHPGE TGREVKAETR LNPDLQPTEE YWLNFDGTLL GNITIFPHQF INLRSNNSAT IIAPYVNAVP MDSMRSHNNW SLVIIPICPL ETSSAINTIP ITISISPMCA EFSGARAKRQ GLPVFITPGS GQFLTTDDFQ SPCALPWYHP TKEISIPGEV KNLVEICQVD SLVPINNTDT YINSENMYSV VLQSSINAPD KIFSIRTDVA SQPLATTLIG EISSYFTHWT GSLRFSFMFC GTANTTVKLL LAYTPPGIAE PTTRKDAMLG THVIWDVGLQ STISMVVPWI SASHYRNTSP GRSTSGYITC WYQTRLVIPP QTPPTARLLC FVSGCKDFCL RMARDTNLHL QSGAIAQNPV ENYIDEVLNE VLVVPNINSS NPTTSNSAPA LDAAETGHTS SVQPEDVIET RYVQTSQTRD EMSLESFLGR SGCIHESKLE VTLANYNKEN FTVWAINLQE MAQIRRKFEL FTYTRFDSEI TLVPCISALS QDIGHITMQY MYVPPGAPVP NSRDDYAWQS GTNASVFWQH GQAYPRFSLP FLSVASAYYM FYDGYDEQDQ NYGTANTNNM GSLCSRIVTE KHIHKVHIMT RIYHKAKHVK AWCPRPPRAL EYTRAHRTNF KIEDRSIQTA IVTRPIITTA GPSDMYVHVG NLIYRNLHLF NSEMHESILV SYSSDLIIYR TNTVGDDYIP SCDCTQATYY CKHKNRYFPI TVTSHDWYEI QESEYYPKHI QYNLLIGEGP CEPGDCGGKL LCKHGVIGIV TAGGDNHVAF IDLRHFHCAE EQGVTDYIHM LGEAFGNGFV DSVKEHIHAI NPVGNISKKI IKWMLRIISA MVIIIRNSSD PQTILATLTL IGCSGSPWRF LKEKFCKWTQ LNYIHKESDS WLKKFTEACN AARGLEWIGN KISKFIEWMK SMLPQAQLKV KYLNELKKLN LYEKQVESLR VADMKTQEKI KMEIDTLHDL SRKFLPLYAS EAKRIKTLYI KCDNIIKQKK RCEPVAIVIH GPPGAGKSIT TNFLAKMITN DSDIYSLPPD PKYFDGYDQQ SVVIMDDIMQ NPAGDDMTLF CQMVSSVTFI PPMADLPDKG KAFDSRFVLC STNHSLLTPP TITSLPAMNR RFFLDLDIIV HDNFKDPQGK LNVAAAFRPC DVDNRIGNAR CCPFVCGKAV SFKDRNSCNK YSLAQVYNIM IEEDRRRRQV VDVMTAIFQG PIDMKNPPPP AITDLLQSVR TPEVIKYCEG NRWIIPAECK IEKELNLANT IITIIANVIG MARIIYVIYK LFCTLQGPYS GEPKPKTKIP ERRVVTQGPE EEFGMSLIKH NSCVITTENG KFTGLGVYDR FVVVPTHADP GKEIQVDGIT TKVIDSYDLY NKNGIKLEIT VLKLDRNEKF RDIRRYIPNN EDDYPNCNLA LLANQPEPTI INVGDVVSYG NILLSGNQTA RMLKYSYPTK SGYCGGVLYK IGQVLGIHVG GNGRDGFSAM LLRSYFTDVQ GQITLSKKTS ECNLPSIHTP CKTKLQPSVF YDVFPGSKEP AVLSEKDARL QVDFNEALFS KYKGNTDCSI NDHIRIASSH YAAQLITLDI DPKPITLEDS VFGTDGLEAL DLNTSAGFPY IAMGVKKRDL INNKTKDISK LKEAIDKYGV DLPMVTFLKD ELRKHEKVIK GKTRVIEASS VNDTLLFRTT FGNLFSKFHL NPGIVTGSAV GCDPEVFWSK IPAMLDDKCI MAFDYTNYDG SIHPIWFEAL KQVLVDLSFN PTLIDRLCKS KHIFKNTYYE VEGGVPSGCS GTSIFNTMIN NIIIRTLVLD AYKNIDLDKL KIIAYGDDVI FSYIHELDME AIAIEGVKYG LTITPADKSN TFVKLDYSNV TFLKRGFKQD EKYNFLIHPT FPEDEIFESI RWTKKPSQMH EHVLSLCHLM WHNGRDAYKK FVEKIRSVSA GRALYIPPYD LLLHEWYEKF //