POLG_PVCV1
ID POLG_PVCV1 Reviewed; 2179 AA.
AC Q91DM0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Genome polyprotein;
DE Includes:
DE RecName: Full=Aspartic protease;
DE Short=PR;
DE EC=3.4.23.-;
DE Includes:
DE RecName: Full=Reverse transcriptase;
DE Short=RT;
DE EC=2.7.7.49 {ECO:0000255|PROSITE-ProRule:PRU00405};
DE EC=2.7.7.7 {ECO:0000255|PROSITE-ProRule:PRU00405};
OS Petunia vein clearing virus (isolate Shepherd) (PVCV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Caulimoviridae; Petuvirus.
OX NCBI_TaxID=492094;
OH NCBI_TaxID=4101; Petunia.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=9299626; DOI=10.1006/viro.1997.8712;
RA Richert-Poggeler K.R., Shepherd R.J.;
RT "Petunia vein-clearing virus: a plant pararetrovirus with the core
RT sequences for an integrase function.";
RL Virology 236:137-146(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Richert-Poeggeler K.R., Hohn T.;
RT "Isolation of an infectious full-length clone of petunia vein clearing
RT virus (PVCV) from infected Nicotiana glutinosa.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Encodes presumably for at least four polypeptides: Movement
CC protein (MP), capsid protein (CP), Protease (PR), and reverse
CC transcriptase (RT). {ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00405};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00405};
CC -!- SIMILARITY: Belongs to the Petuviruses genome polyprotein family.
CC {ECO:0000305}.
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DR EMBL; U95208; AAK68664.1; -; Genomic_DNA.
DR RefSeq; NP_127504.1; NC_001839.2.
DR SMR; Q91DM0; -.
DR GeneID; 921337; -.
DR KEGG; vg:921337; -.
DR Proteomes; UP000002245; Genome.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0046740; P:transport of virus in host, cell to cell; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.270; -; 2.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR000477; RT_dom.
DR InterPro; IPR041577; RT_RNaseH_2.
DR InterPro; IPR028919; Viral_movement.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF01107; MP; 1.
DR Pfam; PF17919; RT_RNaseH_2; 1.
DR Pfam; PF00078; RVT_1; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS50878; RT_POL; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 3: Inferred from homology;
KW Aspartyl protease; Coiled coil; DNA-binding; Endonuclease; Hydrolase;
KW Magnesium; Metal-binding; Nuclease; Nucleotidyltransferase; Protease;
KW Reference proteome; RNA-directed DNA polymerase; Transferase; Transport;
KW Viral movement protein; Zinc; Zinc-finger.
FT CHAIN 1..2179
FT /note="Genome polyprotein"
FT /id="PRO_0000318062"
FT DOMAIN 1409..1591
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT ZN_FING 1112..1125
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 503..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1822..1848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2114..2144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2160..2179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..678
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..721
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..737
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..812
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2121..2144
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2161..2179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1226
FT /note="For protease activity; shared with dimeric partner"
FT /evidence="ECO:0000250"
FT BINDING 1479
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic; for reverse transcriptase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT BINDING 1542
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic; for reverse transcriptase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT BINDING 1543
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic; for reverse transcriptase
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
SQ SEQUENCE 2179 AA; 252214 MW; D45A30A28AD0CF38 CRC64;
MTSPSDYQSN SSLATTYSNA PKLSKALSNK YDYLYEVDIL KENQKISDTY LPLLNPYSAF
AKRSVTPWSQ IRSLVQSKPR HVKEYVAASK LDQHPVFATG EEQFVTLHIP EEFASHWKSH
QFTHIHFGAV KIALTYHGRK GQPVVARLAL LDTRYLEYQH ANLGTAEITL NAGTVFITLF
PNFTMSLSDA NLSTALKIQV QIQGAPLTKD SIQATLHYQI AWRVQNHAMD LTLPGGEEAL
FLKIDAGSGA TQCTQVPRQL SKEDLIKILP DSWVTNYEKL REPEEPLRST EVSMSKRHDK
SVAISFDHSH YKKLRNTHHF MGMISDDVIV LDDPETFSKT LPSLMQTHDW IHHFQLDGRA
VSWYKDPFDG HCPWDIDCQC YSCLYSEDEE DFEDGFPTKY KGIPRPGSIA ERKMQEEANL
KKLYEEKDPF VGSLSRPGKY EYLVRYDAPS WAKDPHLTVE PTGWDSDEPI PPKQPFTTRN
TLPKIYMFNP LNYENNFPPL SSFSKDGADH TPKIPKRNVV LPSGAKDPTG DLEATVNWQT
ENALAQNRML TTIDRTLKET VTKVDRVTDQ SSKNQGLIKV LEQQLQDLNK RICPPGTSLF
HFFDQQKSEM ASLKEQIRLL KEQPQKNETD TPSYQSSYQP FHSFSSPYMP SNPPNSPFTT
FANTPQPQPS LFSQYPIQPK SPNTFDLAKL VWEKKDAIAA EKRAKKKLQK DEVKQKTSLP
PESKRPDPQS SSHLGDQFMI SDPALPKVYA LNEPSVPSED TSSQSYISTE ESVEDTDSFS
VVSEESTQLS QLSSSSNDSP ENNENTLPQT FMVRPTEPEI SEVEDEVDGM TEEPIPERRP
EITPPKMVGT GFHTFSLDDI SITKWPERIQ DFHTWMLTKQ LVEREPFLIL SEFTARLSGT
LREWWNSVGP DDKNRFLTSQ DFTWNIRILY SYFCGDQSQN KEELRRQIFE MKCLSYDRKK
IDRHFQRMIK LFYHIGGDIS LKQAFISSLP PILSERISAL IKERGTSVTQ MHVGDIRQTA
FYVLDDLCSK RKFFNQMKKM SRDLEKACTK SDLIIKGDKG CSGYCNPSRR RKYKRFKLPS
FKERDGRQYR KRRRFFRRSK TSKAMRQKPR SCFTCGKIGH FSRNCPQNKK SIKLISEIQK
YTGIDIEDDL ESVFSIEDEP SEDTLFSLEF YEEYAGEQYQ ITSYEAPKTE NPPLPKIHTI
VEIPQTEVKI YTSKWDKPIS VIAFYDTGAA YSIMDPAILP SEYWIPHFRH FGTADDGILT
TTVKTKHPIT IEFFPGFKYT TKLLGSDIPG KDLLIGFDIY RQLNNKLRIG ADGIRWKNQF
KRYTEIPRLF QLTTSNELQQ LEDVIKNQLC ADSHVDFLSK CSHPLWLNQD FFIQLPFKKN
ENINPTKASH SGMNPEHLQL AIKECDELQQ FDLIEPSDSQ WACEAFYVNK RSEQVRGKLR
LVINYQPLNH FLQDDKFPIP NKLTLFSHLS KAKLFSKFDL KSGFWQLGIH PNERPKTGFC
IPDRHFQWKV MPFGLKTAPS LFQKAMIKIF QPILFSALVY IDDILLFSET LEDHIKLLNQ
FISLVKKFGV MLSAKKMILA QNKIQFLGMD FADGTFSPAG HISLELQKFP DTNLSVKQIQ
QFLGIVNYIR DFIPEVTEHI SPLSDMLKKK PPAWGKCQDN AVKQLKQLAQ QVKSLHIPSE
GKKILQTDAS DQYWSAVLLE EHNGKRKICG FASGKFKVSE QHYHSTFKEI LAVKNGIKKF
NFFLIHTNFL VEMDMRAFPK MIRLNPKIVP NSQLLRWAQW FSPYQFEVKH LKGKDNILAD
FLSRPHEFSQ RLKNSPKVLM FQRRTRSSST KSKADSSQST GSSYKLSHNL PENPPEVFNL
DYPWDTSVFL ERRTFYELQV FKKYGGSILR PFGVDPEYPF AHIFIPNPTD FSEDLLWMFW
YLLNHFHILM KFRCSKFSKI DQVNPWMLKF LLWFNNHNYW ASLFKCMKGI KKYVVIWFYR
PVNYYQGKLC ALPHSSIVKW NHVSVLNDED EYSELQRFIF QENKCIPKEI WPGSSGSWNY
GNSDHPHGQW IRDALREYRE MNDYFQDAQD PYPAYSKVDL TQEELNTLRI TRSYGSSSED
ADMVKRSIYT VQSNIVKDSP RKRKGKAKSR SSTRSEKRRA KNKCKYRSLH GEDWWIELGY
STKPSTPSWT QDSSSEPCV
