ID A0A1W6I4N3_9POTY Unreviewed; 903 AA. AC A0A1W6I4N3; DT 05-JUL-2017, integrated into UniProtKB/TrEMBL. DT 05-JUL-2017, sequence version 1. DT 19-JAN-2022, entry version 18. DE RecName: Full=Genome polyprotein 2 {ECO:0000256|ARBA:ARBA00017447}; DE Flags: Precursor; OS Wheat yellow mosaic virus. OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes; OC Patatavirales; Potyviridae; Bymovirus. OX NCBI_TaxID=75746 {ECO:0000313|EMBL:ARM39029.1}; RN [1] {ECO:0000313|EMBL:ARM39029.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=LM4 {ECO:0000313|EMBL:ARM39029.1}; RA Geng G., Yu C., Yuan X.; RT "Sequence analysis of one new isolate of Wheat yellow mosaic virus from RT Shandong province, China."; RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolyzes a Gly-|-Gly bond at its own C-terminus, commonly in CC the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the processing of the CC potyviral polyprotein.; EC=3.4.22.45; CC Evidence={ECO:0000256|ARBA:ARBA00001848}; CC -!- SIMILARITY: Belongs to the bymoviruses polyprotein 2 family. CC {ECO:0000256|ARBA:ARBA00010000}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KX467329; ARM39029.1; -; Genomic_RNA. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR Gene3D; 1.20.120.70; -; 1. DR Gene3D; 3.90.70.150; -; 1. DR InterPro; IPR001456; HC-pro. DR InterPro; IPR031159; HC_PRO_CPD_dom. DR InterPro; IPR042308; HC_PRO_CPD_sf. DR InterPro; IPR036417; TMV-like_coat_sf. DR Pfam; PF00851; Peptidase_C6; 1. DR SUPFAM; SSF47195; SSF47195; 1. DR PROSITE; PS51744; HC_PRO_CPD; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Protease {ECO:0000256|ARBA:ARBA00022670}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 477..502 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 134..254 FT /note="Peptidase C6" FT /evidence="ECO:0000259|PROSITE:PS51744" FT REGION 521..544 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 806..826 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 522..536 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 142 FT /note="For helper component proteinase activity" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01080" FT ACT_SITE 214 FT /note="For helper component proteinase activity" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01080" SQ SEQUENCE 903 AA; 100959 MW; 2997D71ED563577D CRC64; MASTSSNIYY MDGDPRWPTR DPGAPITRDA LPQRISEAWN TVIIRHMLSD GDDQDSILGR DGLPATRFNA YSGLLPTFVQ SLGLPVNRLR LHAPVSAIEA PLCVDTSYAP WLYMSNGTHA YEATRLQPVR TFIAFNLANG YCYLNFFIPM SFQISGANVE AFSRFIEQLP DVLGAYPTLG NLLKTAIYLM RIFPEILDAP IPIIAKRPGV AQFHVTDNRG LPPTWFSMMC GSVSSFVMLL LHNLGNELLN GIVGSAEETG QYTNWNFEHD HWITSKFITL EDYYTTMSSA LSVDYRTKGG CAALYDLFSD LGYSNMVRRR KRFPESTQGL SSFYFHLSDK APFEAIQVFL SVLREIINSD DYDSPYRNIR TRLINLSSLP YDNPDACFTR NIFEDENKLV WNFEFYKVVT IASNATADRE TFYRSHVLPF RSFVKEASND RYNLPSPFEI TTPVKATPDE APLVESTTES ATTNLSVWWQ VAVGLITAIL TALLFFFWRC FLSAKKIKFR KKDTFPWFSY SHGGPPPSPP GGSPPGSPRD ASYQQVPRTV VRDLSFDEDD DLQSVDLEEA GIRFKSLITT IERGNLQELQ AVIPEHISDL NVLQSSAHGS GFYTMVSLYL STLGDAITAF EQRNDVSPAT IQSLRTLELQ LEARHLRFNE AGTPTHILQR SISASVGRAV IRLTQSALLA SGEGFRTRMA STLQRIADES SNNLTSFDAR ALDMTSELFQ SIAAALDSDS SDIVPLLANA EASLQVYNNF FGVNYVSTTL LALRRELILR SAEGRVGEQP TGISEESNEE LVQKSMQKLD KEIELFQAQI DSQRRVAEIT ESSNLRENIL QPINTVANIA MAGAFLRGGA RSRLPGVLPQ AQPHTQAFRP FTGQAHHLTT TGRVQRFLRR PGH //