ID   POLB_CHPVU              Reviewed;        3164 AA.
AC   Q9YTU2;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=ORFB polyprotein;
DE   Contains:
DE     RecName: Full=Papain-like protease p48 {ECO:0000255|PROSITE-ProRule:PRU01223};
DE              EC=3.4.22.- {ECO:0000255|PROSITE-ProRule:PRU01223};
DE   Contains:
DE     RecName: Full=Putative RNA-directed RNA polymerase/helicase;
DE              EC=2.7.7.48;
DE              EC=3.6.4.13;
OS   Cryphonectria hypovirus 1 (strain Euro7) (CHV-1/Euro7) (Chestnut blight
OS   fungus hypovirulence-associated virus).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Duplopiviricetes;
OC   Durnavirales; Hypoviridae; Hypovirus.
OX   NCBI_TaxID=321609;
OH   NCBI_TaxID=5116; Cryphonectria parasitica (Chestnut blight fungus) (Endothia parasitica).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=9882299; DOI=10.1128/jvi.73.2.985-992.1999;
RA   Chen B., Nuss D.L.;
RT   "Infectious cDNA clone of hypovirus CHV1-Euro7: a comparative virology
RT   approach to investigate virus-mediated hypovirulence of the chestnut blight
RT   fungus Cryphonectria parasitica.";
RL   J. Virol. 73:985-992(1999).
CC   -!- FUNCTION: Papain-like protease p48 is a cysteine protease of the
CC       peptidase family C8. {ECO:0000255|PROSITE-ProRule:PRU01223}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC         COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC         EC=2.7.7.48;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC   -!- SUBCELLULAR LOCATION: [Putative RNA-directed RNA polymerase/helicase]:
CC       Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC   -!- PTM: Papain-like protease p48 is autocatalytically processed. The
CC       putative RNA-directed RNA polymerase/helicase is probably further
CC       processed (By similarity). {ECO:0000250}.
CC   -!- MISCELLANEOUS: Hypoviruses induce hypovirulence in their fungal host
CC       Cryphonectria parasitica. The consequence is attenuation of the related
CC       fungal disease, chestnut blight, that causes cankers that enlarge and
CC       kill branches and trunks. The virus-like genetic elements consist of
CC       cytoplasmically replicating double-stranded RNA.
CC   -!- MISCELLANEOUS: CHV-1 strain Euro7 is a mild hypovirulent strain.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the DEAD box helicase
CC       family. {ECO:0000305}.
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DR   EMBL; AF082191; AAD13750.1; -; Genomic_RNA.
DR   MEROPS; C08.001; -.
DR   PRIDE; Q9YTU2; -.
DR   Proteomes; UP000008451; Genome.
DR   GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR021912; DUF3525.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005315; Peptidase_C8.
DR   Pfam; PF12039; DUF3525; 2.
DR   Pfam; PF03569; Peptidase_C8; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS51875; HAV_P48_PRO; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Helicase; Host membrane; Hydrolase; Membrane;
KW   Nucleotide-binding; Nucleotidyltransferase; Protease;
KW   RNA-directed RNA polymerase; Thiol protease; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..418
FT                   /note="Papain-like protease p48"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000038883"
FT   CHAIN           419..3164
FT                   /note="Putative RNA-directed RNA polymerase/helicase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000038884"
FT   TRANSMEM        684..704
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        791..811
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        823..843
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1166..1186
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1215..1235
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1356..1376
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2494..2514
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2516..2536
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2589..2609
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          271..418
FT                   /note="Peptidase C8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01223"
FT   DOMAIN          2650..2795
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   REGION          1419..1445
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1792..2207
FT                   /note="RNA-directed RNA polymerase"
FT                   /evidence="ECO:0000255"
FT   MOTIF           2750..2753
FT                   /note="DEFH box"
FT   COMPBIAS        1419..1444
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        341
FT                   /note="For papain-like protease p48 activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01223"
FT   ACT_SITE        388
FT                   /note="For papain-like protease p48 activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01223"
FT   BINDING         2663..2670
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   SITE            418..419
FT                   /note="Cleavage; by papain-like protease p48"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01223"
SQ   SEQUENCE   3164 AA;  362598 MW;  11C6BCA397B557D4 CRC64;
     MYKEAERPIE VWRTQVMDGP TWTALSEPCR NRLFFASGKG GEHLTLDVIQ PDSYTKIRLF
     RSGRFEVSVD GKSFGQGGNR YRFVFRYDSL LSTPFGYPAE DKEMALQGYN HEQLLGEMFL
     KLPDSYVDGR PIAEAFFRYV DDLKWDVGVF RDRRSLTELH LPASSGLTTE QARVAKLEWP
     PLPIIQAQPT ILAGIIDNFK ICFPVNGKWV YGQGLSWTRY DGDASVPISL LTNRQHARFW
     NDKDVPTGLK LSKEGFIKLW AQKSRKWQDH MARAIGLSHA ATAELVRATK VNEAKPHLVP
     MEEAKEAPRQ QLVPRRSTFV DSHEKGVEVD PLRLPTEEGR CFELLFNNQV TPAIFDKKPL
     LRDVLAVFKE NVCTMDSLEI SHSDRCVHIV TGETFRNYKE IKAVLEVIIW NDPNILVGAE
     EGSIADYVKA GKHFLFENHQ WVRNGLKLAK GLAEPGQLAK DNTNPSTPKP IETTDYIHPF
     DNGQPLPGRS DQWVSGFEVT RLRHHEEMPH IRNVRNTGIH GLPGDFLSNY PRLPTPVFHR
     LRDLWYDVIG ILMKLEFGDN RSPVLNVTAN ADWVRSETTV NFISDQPGKA RSRPRKDGGF
     DILVPCRGIA TRSIRLLPLF IRLPPRFKAV ALLNGRQSDY DNYGWPVFNP VIPLPQIDSF
     YVEAVAAGRS MYPPGFLLDR YDALGFLIHT ATVYGAEEAF LLPFTHHARV YPPPRPGREI
     AFGSWCKNYK FTAERYWYDA DWKLRVHETN HDFDRLIEIT KTCRRNPPEE NLQARLKDTA
     REVCSIWQYN IMIASSVAFL IPLFYTLYVP YLQFYLHVDP GDYMLLPPVL WLVWTNLCYG
     YACDAWCRLF FFVEEAGKKE LVHSSEEFSS DPSSTLLIPT MGTRGDHVPP RFFANMAVLA
     GVKTHLLKLQ TATYGDLENL KKGKLGSLLP GYLQNHYSVL RGYKAVFTPH VELDMPNATS
     YNLAPPRSYI NKIRYLTDEN RSGASIVDRA VTWFAEELAD TFWPDWQIGC LRGCNLPRSA
     DGVSLITKRP NLKTGKIGWL HGSADPAVVP KDIRDRYPLV PNGDHNEIFR HYDKIYMPGG
     AGAVQTAIAC GCEVVVTDVN LDRDYHTMPT QKDFHQPSIL PYFAWLWRQG FDVKLPRVLL
     VVGWLKFHYS IRYKHLEFAA DFVIRAGLFW WYGCLHLLPF MAAAIMTPRF VKKYLVSMAW
     LTEPGLLMLK ALWRFPIFMV TPRWMLPFIV TVSAYNWWWP LSQDGLNYAS KRFELIFEPV
     ARGKYTFSYP FGHWCLRDTN SMIIYEGKFV DSSETSIGSP FKLSKSVRPV RPGAVFHLVP
     FHIQKLLDSM DEEPLPYSAN HNCTTVILKG IMYRSALGFV FAYAVSWAVY LVLRPPQAAA
     TVYHWMYPER SWDTSRLYHL LGFAAGGTVP MEVIDEEPIE EKPSDAGRSE PIPDNDKQEE
     SDYDQEWWGS QDSIDTVSND LCYLLSFLKD TAIPEEVKLD VIELAYTQFV RNEKGRIPEP
     KETRILVMPN WKPDNWARLI DETHRVLSQF THYTPRVLNE LVVWLKGLGE NLYRVAEPIL
     MLLVRAMRAA KSVSDRATRS IYHCLCHWLD VMYGGSAPTR VKTVWGLTGL IASGMTSQKA
     ILAQNIAMME YQGRGNFLDD YDNFVSNIKE PGKGLPGINT IGGPQRRPIR YKNPVMSHQA
     AEICGLKPGE YEVDEKYQER INDYLAEGIP QAVDGVLFGD RNPDRIARSI NRYEPEYSGC
     SPEDKALVED TARAMFEQWP EVFADRDIML PKGVELYIKE KYSAGTPFIS SFYKSRKALK
     QAGVMDVIRK NALECIKTGK YPTQFYHAFA KSQAVPGQPL LAPRMKDLRT VVSEDLSAYM
     VDQIFQIEAN KRITWETYGA GSGMPLSQSM ARIWDELHDL RKREGGQFII ADATAYDSNC
     KPVLFHGAGK LVELGFQNHP SGKGRQFAQV VQCKFEAMQN AWVMGITEPS YSALTFHVPD
     AEVRRDLESK FPRHFVTFSE LLEHNNMNVT EWKRLTWEEQ KACARDMQSV PGKVFLTNDP
     ALRLQGSSWQ GSFTTEPKRD EFRKYQTYFC NSKEAMKEDI KRIVFANREV ISNVHHKNRG
     GGTGQSATSW DNTATFKLGV ISAWARATGK LPKDFFCSNR LYNTSDDTVW WSKDLLSSAE
     VDRFKQAAAD FGILLEIGST KKITEVEYLS KLPRRPTAED SADYRTWRQG RIENMRSSGR
     FTEEQMLSIE REQLPQFLMV QNPTAILMRR TAFRYYQSSP SKFLYTSCER GAGHALVTAF
     QPALYKRFAI EYAEDLNRLC KEHHINQRYE LVSQQDRIKM QVINVNPNWK QGFRLSPRQE
     AFLRWIRQAK FPSYRQVLDI HLRTKDPDPS AHDRFIAKLD RAWRNPDEGI RDMVDGVYRY
     TDLIPEEFKR FMPSTDMLYA ENPWHTHNQY VEKFIYLKLL ETTTVDELTF AQFDAVAKES
     PYGICMNTIK FWEDLRDPDY LKDLLASEAM IDKVRIYQGM TVIISAMYFA MHWVELFVQS
     LFLIGPLYNL FMWSFWGLSK VYGLANTFYW HGKARSSREI SSIMPRDPYM WSKRFVSTMA
     DFIPERFALG LVPATLILDG LAEIIEVLFG RMWRMFANLK SVGTDFGDAR SGKSLNVPSN
     PWAAYAHTYA TKAIEHGHVT VAAKTASGKS TFFPAAVWAE RRNIGVKKLW IVMPRKILRD
     NWEIPFDIRS QIVKRGKTLD PTADIYITTY GHFRTRIGGL VPRDNLVFFD EFHEMDGFML
     QDVEEWKGPT IFMSATPVAL HGMADIPFLE PTLPKRFNLT VYKVDSDDVL EMWNRARNQF
     ADQPALLARP MIIVPTYNEL KKTIAGLENL DRSVTWHEVS SNSPFVPKTG GLVCTPYVQT
     GIDIKPAPSI LIDSGRDVVV HKGRLITPHP YTDEKTNEQR VNRVGRTMDG VVIQPQLAGT
     GDPPVKYPSG IFFSSRLVAG QYRVPRLTEV DGCVHPELPY ISIKYTSELS NPVEAKKEEQ
     NVRKSLLFIH LMALAGVRQS EWALRYNRYF ELHLPFGEDE DHLQRILEQG KLRYAHHIPV
     DMAMQLLGNG HVTWGIGGVP TITRPRYPCD GMWVEDPSSR KSYVHKVLLH QREHAEIGMW
     QAQVNELKAQ KLALQSQLRS VCTRRSTASR ILRHIRPPDI PVCG