POLB_CHPVE
ID POLB_CHPVE Reviewed; 3165 AA.
AC Q04350;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 97.
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 EP713) (CHV-1/EP713) (Chestnut blight
OS fungus hypovirulence-associated virus).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Duplopiviricetes;
OC Durnavirales; Hypoviridae; Hypovirus.
OX NCBI_TaxID=12478;
OH NCBI_TaxID=5116; Cryphonectria parasitica (Chestnut blight fungus) (Endothia parasitica).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2009854; DOI=10.1002/j.1460-2075.1991.tb08004.x;
RA Shapira R., Choi G.H., Nuss D.L.;
RT "Virus-like genetic organization and expression strategy for a double-
RT stranded RNA genetic element associated with biological control of chestnut
RT blight.";
RL EMBO J. 10:731-739(1991).
RN [2]
RP PROTEOLYTIC PROCESSING OF POLYPROTEIN, PROTEIN SEQUENCE OF 419-428, AND
RP MUTAGENESIS OF ASP-321; HIS-323; ASP-330; CYS-341; ASP-356; ASP-363;
RP CYS-373; ASP-376; SER-377; SER-381; HIS-382; SER-383; ASP-384; CYS-386;
RP HIS-388; ASP-399; PRO-413; ASP-414; ILE-415; LEU-416; VAL-417; GLY-418;
RP ALA-419; GLU-420; GLU-421 AND GLY-422.
RX PubMed=1918054; DOI=10.1016/s0021-9258(18)55013-4;
RA Shapira R., Nuss D.L.;
RT "Gene expression by a hypovirulence-associated virus of the chestnut blight
RT fungus involves two papain-like protease activities. Essential residues and
RT cleavage site requirements for p48 autoproteolysis.";
RL J. Biol. Chem. 266:19419-19425(1991).
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 may be further processed.
CC {ECO:0000269|PubMed:1918054}.
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 EP713 is a highly hypovirulent strain.
CC -!- SIMILARITY: In the C-terminal section; belongs to the DEAD box helicase
CC family. {ECO:0000305}.
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; M57938; AAA67458.1; -; Genomic_RNA.
DR PIR; S15010; S15010.
DR RefSeq; NP_041091.1; NC_001492.1.
DR MEROPS; C08.001; -.
DR GeneID; 1403614; -.
DR KEGG; vg:1403614; -.
DR Proteomes; UP000007251; 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 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 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; Helicase; Host membrane; Hydrolase;
KW Membrane; Nucleotide-binding; Nucleotidyltransferase; Protease;
KW Reference proteome; RNA-directed RNA polymerase; Thiol protease;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..418
FT /note="Papain-like protease p48"
FT /id="PRO_0000038881"
FT CHAIN 419..3165
FT /note="Putative RNA-directed RNA polymerase/helicase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000038882"
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 1193..1213
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 2495..2515
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2517..2537
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2590..2610
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 271..418
FT /note="Peptidase C8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01223"
FT DOMAIN 2651..2796
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT REGION 453..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1793..2208
FT /note="RNA-directed RNA polymerase"
FT /evidence="ECO:0000255"
FT MOTIF 2751..2754
FT /note="DEFH box"
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 2664..2671
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"
FT MUTAGEN 321
FT /note="D->E: No effect on cleavage."
FT /evidence="ECO:0000269|PubMed:1918054"
FT MUTAGEN 323
FT /note="H->S: No effect on cleavage."
FT /evidence="ECO:0000269|PubMed:1918054"
FT MUTAGEN 330
FT /note="D->E: No effect on cleavage."
FT /evidence="ECO:0000269|PubMed:1918054"
FT MUTAGEN 341
FT /note="C->S: Complete loss of cleavage."
FT /evidence="ECO:0000269|PubMed:1918054"
FT MUTAGEN 356
FT /note="D->E: No effect on cleavage."
FT /evidence="ECO:0000269|PubMed:1918054"
FT MUTAGEN 363
FT /note="D->E: No effect on cleavage."
FT /evidence="ECO:0000269|PubMed:1918054"
FT MUTAGEN 373
FT /note="C->S: Partial loss of cleavage."
FT /evidence="ECO:0000269|PubMed:1918054"
FT MUTAGEN 376
FT /note="D->E: No effect on cleavage."
FT /evidence="ECO:0000269|PubMed:1918054"
FT MUTAGEN 377
FT /note="S->T: No effect on cleavage."
FT /evidence="ECO:0000269|PubMed:1918054"
FT MUTAGEN 381
FT /note="S->T: No effect on cleavage."
FT /evidence="ECO:0000269|PubMed:1918054"
FT MUTAGEN 382
FT /note="H->S: No effect on cleavage."
FT /evidence="ECO:0000269|PubMed:1918054"
FT MUTAGEN 383
FT /note="S->T: No effect on cleavage."
FT /evidence="ECO:0000269|PubMed:1918054"
FT MUTAGEN 384
FT /note="D->E: No effect on cleavage."
FT /evidence="ECO:0000269|PubMed:1918054"
FT MUTAGEN 386
FT /note="C->S: Partial loss of cleavage."
FT /evidence="ECO:0000269|PubMed:1918054"
FT MUTAGEN 388
FT /note="H->S: Complete loss of cleavage."
FT /evidence="ECO:0000269|PubMed:1918054"
FT MUTAGEN 399
FT /note="D->E: No effect on cleavage."
FT /evidence="ECO:0000269|PubMed:1918054"
FT MUTAGEN 413
FT /note="P->A,R,S: No effect on cleavage."
FT /evidence="ECO:0000269|PubMed:1918054"
FT MUTAGEN 414
FT /note="D->A,R,S: No effect on cleavage."
FT /evidence="ECO:0000269|PubMed:1918054"
FT MUTAGEN 415
FT /note="I->L,R,V: Complete loss of cleavage."
FT /evidence="ECO:0000269|PubMed:1918054"
FT MUTAGEN 416
FT /note="L->A,E,R,S: No effect on cleavage."
FT /evidence="ECO:0000269|PubMed:1918054"
FT MUTAGEN 416
FT /note="L->G: Complete loss of cleavage."
FT /evidence="ECO:0000269|PubMed:1918054"
FT MUTAGEN 417
FT /note="V->A,G,L,M,R,S: Complete loss of cleavage."
FT /evidence="ECO:0000269|PubMed:1918054"
FT MUTAGEN 417
FT /note="V->I: No effect on cleavage."
FT /evidence="ECO:0000269|PubMed:1918054"
FT MUTAGEN 418
FT /note="G->A,E,R,S,T,V: Complete loss of cleavage."
FT /evidence="ECO:0000269|PubMed:1918054"
FT MUTAGEN 419
FT /note="A->G,L,S,V: No effect on cleavage."
FT /evidence="ECO:0000269|PubMed:1918054"
FT MUTAGEN 419
FT /note="A->R: Complete loss of cleavage."
FT /evidence="ECO:0000269|PubMed:1918054"
FT MUTAGEN 420
FT /note="E->A,R,S: No effect on cleavage."
FT /evidence="ECO:0000269|PubMed:1918054"
FT MUTAGEN 420
FT /note="E->P: Complete loss of cleavage."
FT /evidence="ECO:0000269|PubMed:1918054"
FT MUTAGEN 421
FT /note="E->A: No effect on cleavage."
FT /evidence="ECO:0000269|PubMed:1918054"
FT MUTAGEN 421
FT /note="E->P: Partial loss of cleavage."
FT /evidence="ECO:0000269|PubMed:1918054"
FT MUTAGEN 422
FT /note="G->P: No effect on cleavage."
FT /evidence="ECO:0000269|PubMed:1918054"
SQ SEQUENCE 3165 AA; 361718 MW; 732862977C2CD344 CRC64;
MYKEAERPIE VWRTQVMDGP TWTALSESCR DRLFFASGEG GEHMTLDIIQ PDSYTKIRLF
RSGRFEVSVD GKSFGQGGNR YRFVFRYDSL LSTPFGYPAE DKEIALQDYN HKQLLGEMFL
KLPDSYVDGR PIAEAFFRYV DDLKWDVGVF RDRRSLTELH LPASSGLTTA QVSVAKLEWP
PLPIIQAQPT ILAGIIDNFK ICFPVNGKWI YGQGLSWTRY DGDASVPTSL LSNRQHARFW
NEKDIPTGLK LSKEGFIKLW AQKSRKWQDH MARSIGLSHE AAVELVRATR VNEAKPHLVP
MEEAKEAPRQ QLVPRRSTFV DNHEEEVEID TLRVPVEEGR CFELLFNNQV TPAIFDKKPL
LKDVLGVFEE NVCTMDSLEI SHSDQCVHIV AGETFRNYDE IKAVLEVILE NEPDILVGAE
EGSVADYVKA GKHFLFENHQ WVRNGLKLAK GLAEPGQRAK DNTNPSTPRP IEDADYIHPF
DNGQPLPGRS DQWVSGFEVT RLRHHDEMPH IRSVRNTGIH GLPGDFLSNY PRLPTPVFHR
LRDLWDDVIG ILMKLEFGDN CSPVLNVTAN ADWVRSETTI NFISDQPGKA QSRPREDGGF
DILVPCRGIA TRSIRLLPLF IRLPNRFRAV ALLNGRQSDY DNYGWPVFNP VIPLPQMDSF
YVEAVAAGRS MYPPGFLLGR YDALEYLVHT ATVYGAEEAF LLPFTHHVRV YPPPRPGREI
PFGSWCKNYK FEAERFWYDA DWKLRVHETN HDFDRLIEIT KTCRRNPPEE NLQAKLEDTA
RKVCSVWQYN IMIASSVAFL VPLYFTLYVP YLQFYLHVDP GDYILLPPVL WLVWTNLCYG
YACDAWCRLF FFVEEAGKKE LVHSSEEFSS DPSSTLLIPT MGTRGDHVPP RFFANMAVLA
GVKTHLLKLQ TATYGDLENL KKGKLGSLLP GYLQNHYSVL RGYKAAFTPH VELDMPNATS
YNLAPPRSYI NKIRYLTDEN RSGASMIDRA VTWFAEELAD TFWPDWQIGC LRGCNLPRSA
DGVSLITKQP NLKTGKIGWL HGSADPAVVP KDIRDKYPLV PNGDHNEIFR HYDKIYMPGG
AGAVQTAIAC GCEVVVTDVN LDRDYHTMPT QKDFHQPSIL PYFAWLWRQG FDVKLPRVLL
VIGWLKFHYS IRYKHLEFAA DFVIRAGLFW WYGCLHLLPF MAAAIMAPRF VKKYLVGMAW
LTEPGLLMLK ALWRFPIFMV TPRWMLPFIV TVSVYNWWWP LSQDGLNYAS KRFELIFEPV
TRGKHTFSYP FGHWCLRDTN SMIVYEGKFV NPSETSIGSP FKLSKSVRPV RPGAVFHLVP
FHVQKLLDSM DEAPLPYSAN HNCTTVILKG IMYRSALGFV FAYMVSWAVY LVLRPPQAAA
TVYHWVYPER SWDTSRLYHL LLGFAAGGTV PMEVIDEEHV EEKPSVAGQS EPAAEIDNDK
ISDYDQEWWG SQDSIDTVVN DLCYLLSFLK DTAIPEEVKL DVVELAYTQL VQDEKERIPE
PKGTKILDMP NWKPGNWAKL IDETHRVLSQ FTQYTPRVLN ELVVWLKGLG ENLYRVAEPI
LMLLVRAMRA AKSVSDRATR SVYHCLCHWL DVMYGGSAPT RVKTVWGLTG LVASGMTSQK
AILAQNIAMM EYQGRGNFLD DYDNFVSNIK EPGKGLPGIN TIGGPQRRPI RYKNPVMSHQ
AAEICGLKPG EYEVDDRYQE RINDYLAEGI PQAVDGVLFG DRNPDRIARS ISRYEPEYSG
CSPEDKALVE DTARAMFEQW PEVFADRDIM LPKGVELYIK EKYSAGTPFI SSFYKSRKAL
KQAGVMDVIR KNALECISTG KYPTQFYHAF AKSQAVPGQP LLAPRMKDLR TVVSEDLSAY
MVDQIFQIEA NKRITWETYG AGSGMPLSQS MARIWDELHD LRKREGGQFI IADATAYDSN
CKPALFHGAG KLVELGFQNH PSGKGRQFAQ VVQCKFEAMQ NAWVMGITEP SYTALTFHVP
DVAVRHELES KYPAHFATFS ELLAHNNVNV TEWKRLSWEE RKACARDMQA VPGKVFLTND
PALRLQGSSW QGSFTTEPKR DEFRKYQTYF YDSKAAMRED IKRIVFANRE VISNVHHKNR
GGGTGQSATS WDNTATFKLG VISAWARATG KPPKDFFCSN RLYNTSDDTV WWSKDLLSSA
EVDRFKQAAA DFGILLEIGS TKKITEVEYL SKLPRRPTAE DSADYRAWRQ GRIENMRSSG
RFSEEQLLSI EREQLPQFLM VQNPTAILMR RTAFRYYQSS PSKFLYTSCE RGAGHALVTA
FQPALYKRFA IEYAEDLNRL CKEHHINQRY ELVSQQDRMK MQVINVNPNW KRNFKLSPRQ
EAFLRWIRQA KFPSYRQVLD IHLRIRDPDP SAHDRFIAKL DRAWRNPDEG IRDIVDGVYR
YTDMIPEEFK RFMPSTDMLY AENPWHTHNQ YVEKFIYLKL LETTTVDELT FAQFDAVAKE
SPYGICMNTI KFWEDLRDPD YLKDLLASEA MIDKVRIYQG MTVIISAMYF AMHWVELFIQ
SLFLIGPLYN LFMWSFWGLS KVYGLANTFY WHGKARSSRE ISSILPRDPY MWSKRFVSTM
ADFIPERFAL GIVPVTLVLD GLAEIIEVLF GRMWRLFANL KSVGTDFSDA RSGKSLNVPS
NPWAAYAHTY ATKAIEHGHV TVAAKTASGK STFFPAAVWA ERRNIGIKKL WIVMPRKILR
DNWEIPFDIR SQIVKRGKTL DPSADIYVTT YGHFRTRIGG LVPRDNLVFF DEFHEMDGFM
LQDVEDWKGP TIFMSATPVA LHGMAGIPFL EPTLPKRFNL TVYKVDSDDV LEMWNRARNQ
FADQPELLAR PMIIVPTYNE LKKTIAGLEN LDRSITWHEV SSNSPLVPKT GGLVCTPYVQ
TGIDIKPAPS ILIDSGRDVI VHKGRLVTPH PYTDEKTNEQ RVNRVGRTMD GVVIQPQLAG
TGNPPVKYPS GIFFSSELVA GQYKVPRLTK VNGCVHPELP YMSIKYTSEL SDPAKAREEE
QSVTKSLLFI HLMALAGVRQ SEWALRYNRY FELHLPFGED EDHLERILTS GKLRYANHIP
VDMAMQLLGN GHVTWGIGGV PTITRPRYPC DGMWVEDPSS RKSYAHKVLL HQREHAEIGM
WQAQVNELRA QNLALQSQLR SACTRRSTAG RILRHTRPPD IPVCG
