POLG_PVCV2
ID POLG_PVCV2 Reviewed; 2180 AA.
AC Q6XKE6; Q6XKE5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 86.
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 Hohn) (PVCV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Caulimoviridae; Petuvirus.
OX NCBI_TaxID=492095;
OH NCBI_TaxID=4101; Petunia.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=12970195; DOI=10.1093/emboj/cdg443;
RA Richert-Poggeler K.R., Noreen F., Schwarzacher T., Harper G., Hohn T.;
RT "Induction of infectious petunia vein clearing (pararetro) virus from
RT endogenous provirus in petunia.";
RL EMBO J. 22:4836-4845(2003).
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; AY228106; AAO67368.1; -; Genomic_DNA.
DR EMBL; AY228106; AAO67369.1; ALT_SEQ; Genomic_DNA.
DR SMR; Q6XKE6; -.
DR Proteomes; UP000008483; 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..2180
FT /note="Genome polyprotein"
FT /id="PRO_0000318063"
FT ZN_FING 1113..1126
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 507..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1824..1848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2115..2145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2161..2180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 573..624
FT /evidence="ECO:0000255"
FT COMPBIAS 627..679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..722
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..739
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..809
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2120..2145
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2162..2180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1227
FT /note="For protease activity; shared with dimeric partner"
FT /evidence="ECO:0000250"
FT BINDING 1480
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT BINDING 1543
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT BINDING 1544
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
SQ SEQUENCE 2180 AA; 252579 MW; 064C7E35DEE22E13 CRC64;
MMTSPSDYQS NSSLATTYSN APKLSKALSN KYDYLYEVDI LKENQKISDT YLPLLNPYSA
FAKRSVTPWS QIRSLVQSKP RHVKEYVAAS KLDQHPVFAT GEEQFVTLHI PEEFASHWKS
HQFTHIHFGA VKIALTYHGR KGQPVVARLA LLDTRYLEYQ HANLGTAEIT LNAGTVFITL
FPNFTMSLSD ANLSTALKIQ VQIQGAPLTK DSIQATLHYQ IAWRVQNHAM DLTLPGGEEA
LFLKIDAGNG ATQCTQVPRQ LSKEDLIKIL PDSWVTNYEK LKEPEEPLRS TEVSMSKRHD
KSVAISFDHS HYKKLRNTHH FMGMISDDVI VLDDPETFSK TLPSLMQTHD WIHHFQLDGR
AVSWYKDPFD GHCPWDIDCQ CYSCLYSEDE EDFEDGFPTK YKGIPRPGSI AERKMQEEAN
LKKLYEDKDP FVGSLSRPGK YEYLVRYDAP SWAKDPHLTV EPTGWDSDEP ILPNQPFITR
NTLPKIYMFN PLNYENNFPP LSSFSKDGAD HTPKIPKRNV VLPSGAKDPT GDLEATVNWQ
TENALAQNRM LTTIDRTLKE TVTKVDRVSD QSSKNQGLIR VLEQQLQDLN KRICPPGTSL
FHFFDQQKSE MASLKEQIRL LKEQPQKNET DTPSYQSSYQ PFHNFSSPYM PSNPPNSPFT
NFANTPQPQP SLFSQYPIQP KSPNTFDLAK LVWEKKDAIA EEKRAKKKLQ KDEVKQKTSL
PPESKRPDPQ SSSHLGDQFM ISDPTLPKVY ELNEPSVPSE DTSSQSYIST EESVEDTDSF
SVVSEESTQL SQLSSSSNDS PENNENTLPQ TFMVRPTEPE ISEVEDEVDG MTEEPIPERR
PEITPPKMVG TGFHTFSLDD ISITKWPERI QDFHTWMLTK QLVEREPFLI LSEFTARLSG
TLREWWNSVG PDDKNRFLTS QDFTWNIRIL YSYFCGDQSQ NKEELRRQIF EMKCLSYDRK
KIDRHFQRMI KLFYHIGGDI SLKQAFISSL PPILSERISA LIKERGTSGT QMHVGDIRQT
GFYVLDDLCS KRKFFNQMKK MSRDLEKACT KSDLIIKGDK GCSGYCNPSR RRKYKRFKLP
SFKERDGRQY RKRRRFFRKS KTSKAMRQKP RSCFTCGKIG HFSRNCPQNK KSIKLISEIQ
KYTGIDIEDD LESVFSIEDE PSEDTLFSLE FYEEYAGEQY QITSYEAPKT ENPPLPKIHT
IVEIPQTEVK VYTSKWDKPI SVIAFYDTGA AYSIMDPAIL PSEYWIPHFR HFGTADDGIL
TTTVKTKHPI TIEFFPGFKY TTKLLGSDIP GKDLLIGFDI YRQLNNKLRI GADGIRWKNQ
FKRYTEIPRL FQLTTSNELQ QLEDVIKNQL CAESHVDFLS KCSHPLWLNQ DFFIQLPFKR
NENINPTKAS HSGMNPEHLQ LALKECDELQ QFDLIEPSDS QWACEAFYVN KRSEQVRGKL
RLVINYQPLN HFLQDDKFPI PNKLTLFSHL SKAKLFSKFD LKSGFWQLGI HPNERPKTGF
CIPDRHFQWK VMPFGLKTAP SLFQKAMIKI FQPILFSALV YIDDILLFSE TLEDHIKLLN
QFISLVKKFG VMLSAKKMIL AQNKIQFLGM DFADGTFSPA GHISLELQKF PDTNLSVKQI
QQFLGIVNYI RDFIPEVTEH ISPLSDMLKK KPPAWGKCQD NAVKQLKQLA QQVKSLHIPS
EGKKILQTDA SDQYWSAVLL EEHNGKRKIC GFASGKFKVS EQHYHSTFKE ILAVKNGIKK
FNFFLIHTNF LVEMDMRAFP KMIRLNPKIV PNSQLLRWAQ WFSPYQFEVK HLKGKDNILA
DFLSRPHEFS QRLKNSPKVL MFQRRTRSNS TKSKADSSQS TGSSYKLSHN LPENPPEAFD
LDYPWDTSVF LERRTFYELQ VFKKYGGSIL RPFGVDPEYP FAHIFIPNPT DFSEDLLWMF
WYLLNHFHIL MEFRCSKFSK FDQVNPWMMK FLLWFNNHNY WASLFKCMKG IKKYVVIWFY
RPVNYYQGKL CALPHSSIVK WNHVSVLNDE DEYSELQRFI FQENKCIPKE IWPGSLGSWN
YGNSDHPHGQ WIRDALREYR EMNDYFQDAQ DPYPAYSKVD LTQEELNTLR ITRSYGSSSE
DADMVKRSIY TVQSNIVKNS PRKRKGKAKS KSSTRNEKRR AKNKCKYRSL HGEDWWIELG
YSTKPSTPSW TQDSSSEPCI
