GenomeNet

Database: UniProt
Entry: G4WWA9_9POTY
LinkDB: G4WWA9_9POTY
Original site: G4WWA9_9POTY 
ID   G4WWA9_9POTY            Unreviewed;      3148 AA.
AC   G4WWA9;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=Gp1 {ECO:0000313|EMBL:AEP81236.1};
OS   Cucumber vein yellowing virus.
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Stelpaviricetes;
OC   Patatavirales; Potyviridae; Ipomovirus.
OX   NCBI_TaxID=137475 {ECO:0000313|EMBL:AEP81236.1};
RN   [1] {ECO:0000313|EMBL:AEP81236.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Jordanian {ECO:0000313|EMBL:AEP81236.1};
RX   PubMed=22383057; DOI=10.1007/s00705-012-1264-4;
RA   Galipienso L., Rubio L., Aramburu J., Velasco L., Janssen D.;
RT   "Complete nucleotide sequence of a severe isolate of cucumber vein
RT   yellowing virus from Jordan.";
RL   Arch. Virol. 157:1189-1192(2012).
CC   -!- FUNCTION: An RNA-dependent RNA polymerase that plays an essential role
CC       in the virus replication. {ECO:0000256|ARBA:ARBA00029404}.
CC   -!- FUNCTION: Has RNA-binding and proteolytic activities.
CC       {ECO:0000256|ARBA:ARBA00029399}.
CC   -!- FUNCTION: Indispensable for virus replication.
CC       {ECO:0000256|ARBA:ARBA00034080}.
CC   -!- FUNCTION: Mediates the cap-independent, EIF4E-dependent translation of
CC       viral genomic RNAs (By similarity). Binds to the cap-binding site of
CC       host EIF4E and thus interferes with the host EIF4E-dependent mRNA
CC       export and translation (By similarity). VPg-RNA directly binds EIF4E
CC       and is a template for transcription (By similarity). Also forms
CC       trimeric complexes with EIF4E-EIF4G, which are templates for
CC       translation. {ECO:0000256|ARBA:ARBA00037225}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes glutaminyl bonds, and activity is further
CC         restricted by preferences for the amino acids in P6 - P1' that vary
CC         with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln-|-(Ser or
CC         Gly) for the enzyme from tobacco etch virus. The natural substrate is
CC         the viral polyprotein, but other proteins and oligopeptides
CC         containing the appropriate consensus sequence are also cleaved.;
CC         EC=3.4.22.44; Evidence={ECO:0000256|ARBA:ARBA00000785};
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle
CC       {ECO:0000256|ARBA:ARBA00004541}. Host cytoplasmic vesicle
CC       {ECO:0000256|ARBA:ARBA00034108}. Vesicle
CC       {ECO:0000256|ARBA:ARBA00004373}. Virion
CC       {ECO:0000256|ARBA:ARBA00004328}.
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; JF460793; AEP81236.1; -; Genomic_RNA.
DR   GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0044161; C:host cell cytoplasmic vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031982; C:vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR   CDD; cd23175; ps-ssRNAv_Potyviridae_RdRp; 1.
DR   Gene3D; 3.30.70.270; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR022199; DUF3725.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR002540; Pept_S30_P1_potyvir.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001592; Poty_coat.
DR   InterPro; IPR001730; Potyv_NIa-pro_dom.
DR   InterPro; IPR013648; PP_Potyviridae.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR001205; RNA-dir_pol_C.
DR   InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR   PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR   PANTHER; PTHR18934:SF83; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE DHX16; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF12523; DUF3725; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00863; Peptidase_C4; 1.
DR   Pfam; PF01577; Peptidase_S30; 1.
DR   Pfam; PF00767; Poty_coat; 1.
DR   Pfam; PF08440; Poty_PP; 1.
DR   Pfam; PF00680; RdRP_1; 1.
DR   PRINTS; PR00966; NIAPOTYPTASE.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51436; POTYVIRUS_NIA_PRO; 1.
DR   PROSITE; PS51871; PV_P1_PRO; 2.
DR   PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Capsid protein {ECO:0000256|ARBA:ARBA00022561};
KW   Covalent protein-RNA linkage {ECO:0000256|ARBA:ARBA00022520};
KW   Helical capsid protein {ECO:0000256|ARBA:ARBA00022497};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Host cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00022488};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Protease {ECO:0000256|ARBA:ARBA00022825};
KW   RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Viral RNA replication {ECO:0000256|ARBA:ARBA00022953};
KW   Virion {ECO:0000256|ARBA:ARBA00022844}.
FT   TRANSMEM        1091..1114
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          393..525
FT                   /note="Peptidase S30"
FT                   /evidence="ECO:0000259|PROSITE:PS51871"
FT   DOMAIN          690..843
FT                   /note="Peptidase S30"
FT                   /evidence="ECO:0000259|PROSITE:PS51871"
FT   DOMAIN          1253..1404
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1423..1583
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          2049..2272
FT                   /note="Peptidase C4"
FT                   /evidence="ECO:0000259|PROSITE:PS51436"
FT   DOMAIN          2525..2648
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50507"
FT   REGION          2848..2895
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2854..2895
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3148 AA;  360612 MW;  7F7619AD9B8E30A4 CRC64;
     MTEVYSFVPK TDYEKRMVKR FGTDKFLQFR EQCPLNQVRK CWTHFKVCDG ACYAYLPVHF
     AEEEAREFLE LSEGRRKLVL DNVRRALCSA LYYNPNDEDF ECECGNSNTS WKRVCEDCGQ
     VYAYSEMNLL QELSRIAATL SCNINELKNF TIHDIADEVS YAERSRRMTT VESGFKTVDE
     ISLRTEVVGA VISEKPVEPV TVKAVVAEKP VEASNNSRVA MEEKQPQIKQ VWRMVTEKPK
     PTVVPECKLE APTKKEIQTC LDLVVQIGDF IINTCTREFK MVDGKSERIE KVEETEVKES
     VVENSNKDTV VLDNFFKNFQ FNEERRSKIY TDKHGNVRYG RRPVKRQKRS KKVELMSDKI
     ITKIEIPEEV QPVYSFEDLP SIKKAYSKEK PREIIETRTK YSVKSLVKEI GKTCSLTEIM
     IIDKKVRKIK RRGSRYFVDV RHLDGCNPEV DLDHSRFSDE ILDWLMASLA VKSTRLSEIV
     PGTSGLITAG RNEFGKFTII RGWLDRMVDA REKLTKSQLR RIRNYTIHGL HAFKKRYQTN
     VIDRERTTQI QIKDNVVYLK GEGALQNFIN SSTLGGLVRN VSGATKPALA CLRKATKYGV
     GFDMMMNHYV CCRCHVRCTD ISLMDPMCSE CGENMFESVG HESPFVTLPI NPFECDVHPA
     VAEIMKEAWW RDGVEDWPIE KKYHSNGKEI YVEKQGQRAW RSEFQLRETS SNREFDLGLA
     AANNGVCLCE ANFAWLDMFP CVTLNHIFGL DFDDDMDSEI RDIMTRENAQ RVFSTGRLVK
     YADICPGWSG VVITEDAVQP EEWNKFAWYN GICVVQGKNR ESGIIENAII MKTADEKDKI
     DFYSFDLSWA KSKTKFIEYF AEDETRIIKA CCTPSSLWLF AKKSSLYKYV DYLLLHESSI
     VDLCVKFEFV GKHLSLLENV EDACIEFSHF MDEMIQSRNV QDEPELARIR ALIRSQFDSV
     RESSKYEIID RIIEKKTKLQ ADEIIMRELI RRQYAELFSW RERALMNFCS KRTRLYDLWE
     KREEANSSSS SIISLLMSRP GLEIMTNWAS TVCKTQYARS IRAVDCTIRF VWHRIVSLSK
     QALFKWWESC VFHVFCVLLT ALVTYSLSQV VSFLKKMTDK EKKEALELEG DLVEIQGKKE
     EATIMKWCAM LTLVMSFINF DWALASVSAL GKMKTIFSAL GPNLIELQSG EEDAFKFTTF
     EVEVPGNGKS CDEQTFEDWI SHCIKYNLTT PEPTTSGPML VLEKGKAKEL AEKIRMHDSC
     DLRVYGGVGT GKSTSLPSEI MKFGPVLICV PTRVLANALH DSYMALFGYD VSVAYRGRVR
     TGTQPITVMT YGYALNHFHY NPQNLNSFEY VVMDEIHTFP TELNPLFSLI RETNPRKKII
     KTSATHVGHN VELSTNFKVN IETLSPMGVK KWVELQGTNV FGDATSSGEV ILVFVATYNE
     VDEAAEGLRN KGFPVLKVDG RNFRKNTEVQ KMVDDLPGTI KFIVATNIIE NGVTLDVDTL
     VDFGERVSPV LDSDGRSIIM ARRRISKAER QQRFGRVGRM KPGTIYKFGK EALPDSMKSV
     VGATESAMIC FAYGIKPVVD DVDIGSIARV TKKQALTASL YDLNRIFTVH HVDKHGFIPR
     TVHELFKTFM LRTEAVAICE SYLSSDSSSW KALHTYLRPS EEMAHVRNVK IPWYCSDMSN
     EFIIKLAECV NHAKPKFSCG YDVENVDFHV VAHKISVGEH NIEESKALVS EILNRVKQWR
     DNLVYKMSTP RNNSLMSLMV GWIPKKIEKT RSXLEMRIQR LEMLLSQLDN VSVNHDYESL
     VRFFAENPHS AEYLESQGKS EYLEKRILKT NIKEADWRVI AGVITITTCM AGFTYWYLRR
     RSAVDQVEIQ GKVGYRRDKR VGRFVFDGPD EDIIENFGVE YSHDVVTKKM SKAQKLKQAK
     ERGWKIGKVD RPKKIFKQLY GVNPLEFDEV YLTVGDFKGE IWETKDMDID EMYSDLYSDF
     NLGNRKGYSK DVYLVFSKKD SDIEAVVDLQ PHRSKMASSM SLNPMGFPEE EGRWRQSGDV
     KMRKRIEEEV EVQVAETAIA SKFAHIFQRL GRLGFSGRGL NCIFHGDKSI MPYHLASGGD
     PGDSLIVTTS RGQFDMGPME MIKCKKITDF DLVVGQLPKD MQPFKSTNIM RKPKMDEDVV
     IITLKRDKGK MLIRTSDTSK IYKAGDKYAH LWVHFIKSES GDCGSPIVAL SDNKIVGFHS
     GMIKDKLGVF LRSVFTPVND ELLRTLNEKS EMNDFWKFNQ DAISWNAVIK TSSLFPVMKD
     ILGVHLQVGA GDKYIGGNLM TVGEVNKHAY HNHVIKGKRK EFVEFCAQNP NNNFEKFRDF
     YGPSVMTVSA FYKDLLKYDE PIRVGVIDFP SLVHAYLNVE DKLLSLGFDE DCGPEWDPYE
     IYCDLNKKAA MGALYQGSKN EWLKEITPKE FIEQVQESYR LLGHGVVGIW SGSLKAELRT
     KAKIAEGKTR VFTGAPIDVL LAGKVLVDKF NKHFYTQHLK GPWSVGINKF NRGWDKLARY
     FNHDWKFIDC DGSRFDSSLS PILFQMVCHM RERFGHFDWA ETNALRNLYA QIVYTPILTI
     DGNIVKKHKG NNSGQPSTVV DNTLILMLVV EYCKSWHLKQ SGIEMEFKYM CNGDDLIINA
     PDKEISIIQS TFKNLFKECG LNYDFDDLHD SIEDVEYMSH HFVLREGFYI PKLSKERLVA
     ILEWERSDEL FRTRSALNAA YIESFGYDDI HWEIERFAAY WANLKGVKNV LMSEDHVRKL
     YLDENFELTD EIVQTLSPAS FEFGCVELQA DEIDKEAIEQ EIEKLRNEWK ANGPSRTVSN
     YEARKKQTPI AAKVDELLKQ LKEAGVETLK RPCGQPNADE DKKESSNSNW TGESEDEDEE
     KKKKMPLRGG GKILKRDDVD KIPTNAMEFK RDFKPARASR TSYIWIPRSQ RDNLTPDVIK
     NFLAYIPPSQ AIDNQMASGS QVENWAMRTA SAYGVTIQQF YETVLPAWIV NCIVNGTSDE
     RKTETVWRAV ELNAQGEDVD DMEYPIEPIY KHALPTMRKI MRNFSSQAIL MYQNSVAEGK
     AFTVKAARNA GYTEIEDQWL GIDFLAEAQL SRNQLNIKHQ TLAANVSRNR RNLFALAAPG
     DDGRVNAERH LTTDASASRH TYGGAMIE
//
DBGET integrated database retrieval system