ID C9DZL9_9VIRU Unreviewed; 1254 AA.
AC C9DZL9;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 22-FEB-2023, entry version 64.
DE RecName: Full=Structural polyprotein {ECO:0000256|ARBA:ARBA00014555};
DE AltName: Full=p130 {ECO:0000256|ARBA:ARBA00033029};
OS Ross River virus.
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Martellivirales; Togaviridae; Alphavirus.
OX NCBI_TaxID=11029 {ECO:0000313|EMBL:ACV67000.1, ECO:0000313|Proteomes:UP000152871};
RN [1] {ECO:0000313|EMBL:ACV67000.1, ECO:0000313|Proteomes:UP000152871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9057 {ECO:0000313|EMBL:ACV67000.1};
RX PubMed=19759236; DOI=10.1099/vir.0.014209-0;
RA Jones A., Lowry K., Aaskov J., Holmes E.C., Kitchen A.;
RT "Molecular evolutionary dynamics of Ross River virus and implications for
RT vaccine efficacy.";
RL J. Gen. Virol. 91:182-188(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Autocatalytic release of the core protein from the N-terminus
CC of the togavirus structural polyprotein by hydrolysis of a -Trp-|-
CC Ser- bond.; EC=3.4.21.90; Evidence={ECO:0000256|ARBA:ARBA00000840};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Cell
CC membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004251}. Cytoplasm
CC {ECO:0000256|ARBA:ARBA00004496}. Host cell membrane
CC {ECO:0000256|ARBA:ARBA00004598}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004598}. Host cell membrane
CC {ECO:0000256|ARBA:ARBA00004402}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004402}. Host cytoplasm
CC {ECO:0000256|ARBA:ARBA00004192}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}. Virion membrane
CC {ECO:0000256|ARBA:ARBA00004385}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004385}. Virion membrane
CC {ECO:0000256|ARBA:ARBA00004563}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004563}.
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DR EMBL; GQ433358; ACV67000.1; -; Genomic_RNA.
DR MEROPS; S03.001; -.
DR Proteomes; UP000152871; Genome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0039619; C:T=4 icosahedral viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; 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:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR Gene3D; 1.10.287.2230; -; 1.
DR Gene3D; 2.60.40.350; -; 1.
DR Gene3D; 2.60.40.3200; Alphavirus E2 glycoprotein, A domain; 1.
DR Gene3D; 2.60.40.4310; Alphavirus E2 glycoprotein, domain B; 1.
DR Gene3D; 2.60.40.2400; Alphavirus E2 glycoprotein, domain C; 1.
DR Gene3D; 2.60.98.10; Tick-borne Encephalitis virus Glycoprotein, domain 1; 3.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR002548; Alpha_E1_glycop.
DR InterPro; IPR000936; Alpha_E2_glycop.
DR InterPro; IPR002533; Alpha_E3_glycop.
DR InterPro; IPR042304; Alphavir_E2_A.
DR InterPro; IPR042305; Alphavir_E2_B.
DR InterPro; IPR042306; Alphavir_E2_C.
DR InterPro; IPR000336; Flavivir/Alphavir_Ig-like_sf.
DR InterPro; IPR036253; Glycoprot_cen/dimer_sf.
DR InterPro; IPR038055; Glycoprot_E_dimer_dom.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR000930; Peptidase_S3.
DR Pfam; PF01589; Alpha_E1_glycop; 1.
DR Pfam; PF00943; Alpha_E2_glycop; 1.
DR Pfam; PF01563; Alpha_E3_glycop; 1.
DR Pfam; PF00944; Peptidase_S3; 1.
DR PRINTS; PR00798; TOGAVIRIN.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR SUPFAM; SSF56983; Viral glycoprotein, central and dimerisation domains; 1.
DR PROSITE; PS51690; ALPHAVIRUS_CP; 1.
PE 4: Predicted;
KW Capsid protein {ECO:0000256|ARBA:ARBA00022561};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Fusion of virus membrane with host endosomal membrane
KW {ECO:0000256|ARBA:ARBA00022510};
KW Fusion of virus membrane with host membrane
KW {ECO:0000256|ARBA:ARBA00022506};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Host cell membrane {ECO:0000256|ARBA:ARBA00022511};
KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200};
KW Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW T=4 icosahedral capsid protein {ECO:0000256|ARBA:ARBA00022973};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804};
KW Viral penetration into host cytoplasm {ECO:0000256|ARBA:ARBA00022595};
KW Virion {ECO:0000256|ARBA:ARBA00022844};
KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296}.
FT TRANSMEM 1229..1250
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 122..270
FT /note="Peptidase S3"
FT /evidence="ECO:0000259|PROSITE:PS51690"
FT REGION 63..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..111
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 148
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR600936-1"
FT ACT_SITE 170
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR600936-1"
FT ACT_SITE 222
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR600936-1"
SQ SEQUENCE 1254 AA; 138432 MW; 84DFC79F4D749E1C CRC64;
MNYIPTQTFY GRRWRPRPAF RPWQVPMQPT PTMVTPMLQA PDLQAQQMQQ LISAVFALTT
KQNVKAPKGQ RKKKQQKPKE KKENQKKKPT QKKKQQQKPK PQAKKKKPGR RERMCMKIEN
DCIFEVKLDG KVTGYACLVG DKVMKPAHVK GTIDNPDLAK LTYKKSSKYD LECAQIPVHM
KSDASKYTHE KPEGHYNWHH GAVQYSGGRF TIPTGAGKPG DSGRPIFDNK GRVVAIVLGG
ANEGARTALS VVTWTKDMVT RVTPEGTEEW SAALMMCILA NTSFPCSSPP CYPCCYEKQP
EQTLRMLEDN VNRPGYYELL EASMTCRNRS RHRRSVTEHF NVYKATRPYL AHCADCGDGY
FCYSPVAIEK IRDEASDGML KIQVSAQIGL DKAGTHAHTK LRYMAGHDVQ ESKRDSLRVY
TSAACSIHGT MGHFIVAHCP PGDYLKVSFE DADSHVKACK VQYKHDPLPV GREKFVVRPH
FGVELPCTSY QLTTAPTDEE IDMHTPPDIP DRTLLSQTAG NVKITAGGRT IRYNCTCGRD
NVGTTSTDKT INTCKIDQCH AAVTSHDKWQ FTSPFVPRAD QTARRGKVHV PFPLTNVTCR
VPLARAPDVT YGKKEVTLRL HPDHPTLFSY RSLGAEPHPY EEWVDKFSER IIPVTEEGIE
YQWGNNPPVR LWAQLTTEGK PHGWPHEIIQ YYYGLYPAAT IAAVSGASLM ALLTLAATCC
MLATARRKCL TPYALTPGAV VPLTLGLLCC APRANAASFA ETMAYLWDEN KTLFWMEFAA
PAAALALLAC CIKSLICCCK PFSFLVLLSL GASAKAYEHT ATIPNVVGFP YKAHIERNGF
SPMTLQLEVV ETSLEPTLNL EYITCEYKTV VPSPFIKCCG TSECSSKEQP DYQCKVYTGV
YPFMWGGAYC FCDSENTQLS EAYVDRSDVC KHDHASAYKA HTASLKATIR ISYGTINQTT
EAFVNGEHAV NVGGSKFIFG PISTAWSPFD NKIVVYKDDV YNQDFPPYGS GQPGRFGDIQ
SRTVESKDLY ANTALKLSRP SPGVVHVPYT QTPSGFKYWL KEKGSSLNTK APFGCKIKTN
PVRAMDCAVG SIPVSMDIPD SAFTRVVDAP AVTDLSCQVA VCTHSSDFGG VATLSYKTDK
PGKCAVHSHS NVATLQEATV DVKEDGKVTV HFSTASASPA FKVSVCDAKT TCTAACEPPK
DHIVPYGASH NNQVFPDMSG TAMTWVQRLA SGLGGLALIA VVVLVLVTCI TMRR
//