ID A5Y0T0_9PICO Unreviewed; 2249 AA.
AC A5Y0T0;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
OS Duck hepatitis virus 2 strain 04G.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Picornaviridae; Paavivirinae; Avihepatovirus;
OC Avihepatovirus A.
OX NCBI_TaxID=427748 {ECO:0000313|EMBL:ABO09965.1, ECO:0000313|Proteomes:UP000127277};
RN [1] {ECO:0000313|EMBL:ABO09965.1, ECO:0000313|Proteomes:UP000127277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=04G {ECO:0000313|EMBL:ABO09965.1};
RX PubMed=17292992; DOI=10.1016/j.virusres.2007.01.012;
RA Tseng C.H., Tsai H.J.;
RT "Molecular characterization of a new serotype of duck hepatitis virus.";
RL Virus Res. 126:19-31(2007).
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000256|ARBA:ARBA00004180}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004180}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004180}. Host cytoplasmic vesicle membrane
CC {ECO:0000256|ARBA:ARBA00004295}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004295}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004295}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
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DR EMBL; EF067923; ABO09965.1; -; Genomic_RNA.
DR MEROPS; C03.011; -.
DR Proteomes; UP000127277; Genome.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0039618; C:T=pseudo3 icosahedral viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0005216; F:monoatomic ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; 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:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR GO; GO:0039707; P:virus-mediated pore formation in host cell membrane; IEA:UniProtKB-KW.
DR CDD; cd23193; ps-ssRNA_Picornaviridae; 1.
DR CDD; cd00205; rhv_like; 2.
DR Gene3D; 1.20.960.20; -; 1.
DR Gene3D; 2.60.120.20; -; 2.
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; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR006703; G_AIG1.
DR InterPro; IPR045058; GIMA/IAN/Toc.
DR InterPro; IPR004004; Helic/Pol/Pept_Calicivir-typ.
DR InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR044067; PCV_3C_PRO.
DR InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001676; Picornavirus_capsid.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR033703; Rhv-like.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR029053; Viral_coat.
DR PANTHER; PTHR10903:SF135; GTP-BINDING PROTEIN A; 1.
DR PANTHER; PTHR10903; GTPASE, IMAP FAMILY MEMBER-RELATED; 1.
DR Pfam; PF04548; AIG1; 2.
DR Pfam; PF00548; Peptidase_C3; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF00073; Rhv; 1.
DR Pfam; PF00910; RNA_helicase; 1.
DR PRINTS; PR00918; CALICVIRUSNS.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF88633; Positive stranded ssRNA viruses; 3.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS51874; PCV_3C_PRO; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR PROSITE; PS51218; SF3_HELICASE_2; 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 Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200};
KW Host cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00022488};
KW Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, 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:ARBA00022670};
KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484};
KW T=pseudo3 icosahedral capsid protein {ECO:0000256|ARBA:ARBA00022706};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448};
KW Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804};
KW Viral ion channel {ECO:0000256|ARBA:ARBA00023039};
KW Viral RNA replication {ECO:0000256|ARBA:ARBA00022953};
KW Virion {ECO:0000256|ARBA:ARBA00022706};
KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296}.
FT TRANSMEM 135..154
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1270..1432
FT /note="SF3 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51218"
FT DOMAIN 1610..1795
FT /note="Peptidase C3"
FT /evidence="ECO:0000259|PROSITE:PS51874"
FT DOMAIN 2014..2129
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT REGION 253..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2249 AA; 252470 MW; 379DD5271D3B8EC4 CRC64;
MDTLTKNIED STVQLIGACA EKVQKTISGL GAVESVASTN AVIATANATT TQTIPDPTEG
STDDFYSCSY EVGAQGDNIS RLVHLFTGQW TNNSQLLSCL RWLPTPQCFY DVDTKPAYGQ
TRYFRFIRCG YHFRLLVNAP SGAAGGLMLV WFPYPFNRVL TGTNTLSNAV EPRSLMNLPY
AILDLRTNSE VDLVVPYVNY TNYVNLMATE AIGGSIAVFV LGRYAVGNGT SATVDFSLFG
ELLETDLQCP RAFNDQGKRK PRRRPIHKPV NPPQESRIII QPGPGAANLS NSSVITLAES
AALANEGTSV DYSTVGCASS IDDVLVVLRR WQIIGNFNWA NTSTPGDRIT RYQIIFNNMP
TFALFFDKFQ FWRGSLEVKL LTFGSQFNTG RYQMSWYPLG SGNHTLAQCQ NSVFVTGDVC
ATPVTLILPF TNTTWRKSTD ESYGYLEWHV VNRLTVNATA PNTIPCVILM RVGKDFQLTA
PLYGTLQMAA NNQGDTNQLG DDEPVCFLNF ETANVPIQGE SHTLVKHLFG RQWLVRTVQH
DAQDGVQELD LEVPDRGHGS LLRFFAYFSG ELVITVVNNG TTPLMVAHNY HLDNLTSEYA
VTSMGGILVP ANTAKNILIP FYSGTPLRPT RPTTDRRTPF GRLYIWTQTG SASIFLGLHK
PALFFPLPSP TYTALHVNHI ETLALHNQSD TVDCHICDLC RKMKKWARNR RPFRFCLRLK
TLAFELHLEI ESDQIRNVRD LTTEGVEPNP GPVMVVGKSG SGKSVLCNVI ADVNLFESKL
TPYTLTTKHQ VETVTVCGRQ ITLIDTPEIP KYDGPIRCFL YMIEVGRFTQ EDVTFMKTMR
QYFPGFEKST ILVLNRADEF SNNDQLKDWI KTNGELESLV RACDGRIAKF YRGKIATAKL
LDKIAEIPEY RGHLPCLVYK DRKMYRHYGV QCGNVVFHMD SEDIMKSALN GEVTIKQEKW
NGNWKPASEH MESTASIYLK SDTMPKFKFS VDENCESWAR QLLGDYGPTQ GTVLKERLMW
AAALGFFMTM KITTDQSFPG KDAIHTVLTK ISNFIFGGLE NEVVRIVIRT VIRIVCYLIL
YIHSPNIVTT GTLVALLALD ATSMSMDQGL KTLCMSLVDG DFGKFCSVLL QKIQTVDEAD
LKGTIPSFTD MMDNQSGKPI GPKSFNDWTT CAKNVQWWLE SFVKVVNWLR EKVFPSKTDP
ALQWLEDHEE HISIMLALCD EHLCMLRTDK DYICEHTTKP KHQKLVEMVS GTLNQLNGIP
SAKDLCLRLQ HVLNKLHQVN FEPELEWTHR PEPLGIWISG GPGIGKSFLS NFIVKQIAKR
KHWKSYANPT GSKHMDGYVS QEIHVFDDFG QSREEEDYSL ICNLISSVPF ITPKASVEAK
GTQYRGRLVV VTTNRRDFTS CKLTDPDALE RRFPIRLNIR PLQKYNHKGR LDVATAMRDG
SLQNGTCWER DIGGLGLEHW NPINGDTLVD EILSELQVRQ EVASFMNQGK VRRLSDLDSM
FEELDELKLD FDFDRLEEQA RLFVRPKEGK ISKFRTWVKE CINKIKGFLE RNKAWILGIG
TLGTIVSLIT MCIPLARKFT QSFYSAQPMA KTLPKDFKVA VQKHVEKLES VLQDQSGRVN
FRHICNRLVN VSSEDEVATG LAIGGKNVLT FGHSKFTQLD SIRDMTFNSP AKGTPITYDG
LPTDLQILEC DIPHQFKDVT KLIATDDYRG NGWLVWKDDD QYMIQEVTKI RPFGQTTTAS
GTTSCQTYIY NCKTGPGSCG GVLVALVGGN LKILGIHTSG NGTMGASNRV FPVFNQGAVV
SKRYSGKILY HQPRKTAYQK SPVFEDSPYE PAVLSINDQR LAVPIEDMAK KASDKYIGNV
FDPPPPAFQL AKTHVAEKLA KVLGSHDCVS FEQAISSDII PMNWDTSPGI KYKGETKRQL
VLKSTFKQDV MEQLQSPSTV FVCYLKDELR KKEKIKEGKT RGIEACNFDY TVAFRMVMGE
IYSNIYDDSF ILSGCAVGIN PFSEWDNLLA NLQPYNLCLD FSGFDGSLSA RILEEAVDVL
SFFHNDPALV KKIHAPTIYS THYVTDEIWE VEGGMCSGSP CTTVLNSVVN QLACYTVLAT
LGYDISQCYV VSYGDDCVLS VPEKRDISKL SHYFKLFFGM TATASDKASD IAWRGPMEIE
FLKRTPAFLP DTRKIVGVLD KEVLEGKIQW CKGPEAFKQQ LDSFFLEAAL HGPEYYDYVC
RKLKARCPVL EIQPWGVARM RAFTACMMI
//