CAPSD_PHUV
ID CAPSD_PHUV Reviewed; 251 AA.
AC Q06912;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Capsid protein;
DE AltName: Full=Coat protein;
DE Short=CP;
GN ORFNames=AR1, AV1;
OS Pepper huasteco yellow vein virus (PHYVV) (Pepper huasteco virus).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Begomovirus.
OX NCBI_TaxID=223303;
OH NCBI_TaxID=4072; Capsicum annuum (Capsicum pepper).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8409944; DOI=10.1099/0022-1317-74-10-2225;
RA Torres-Pacheco I., Garzon-Tiznado J.A., Herrera-Estrella L.,
RA Rivera-Bustamante R.F.;
RT "Complete nucleotide sequence of pepper huasteco virus: analysis and
RT comparison with bipartite geminiviruses.";
RL J. Gen. Virol. 74:2225-2231(1993).
CC -!- FUNCTION: Encapsidates the viral DNA into characteristic twinned
CC ('geminate') particles. Binds the genomic viral ssDNA and shuttles it
CC into and out of the cell nucleus. The CP of bipartite geminiviruses is
CC not required for cell-to-cell or systemic movement.
CC -!- SUBUNIT: Homomultimer. Binds to single-stranded and double-stranded
CC viral DNA. Interacts (via nuclear localization signals) with host
CC importin alpha-1a (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host nucleus {ECO:0000250}.
CC Note=It is actively transported into the host cell nucleus. It may be
CC exported out of the nucleus through a nuclear export signal for cell-
CC to-cell movement and spread (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the geminiviridae capsid protein family.
CC {ECO:0000305}.
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DR EMBL; X70418; CAA49855.1; -; Genomic_DNA.
DR PIR; JQ2299; JQ2299.
DR PIR; S31874; S31874.
DR RefSeq; NP_040320.1; NC_001359.1.
DR SMR; Q06912; -.
DR GeneID; 988143; -.
DR KEGG; vg:988143; -.
DR Proteomes; UP000002321; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0039615; C:T=1 icosahedral viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.20; -; 1.
DR InterPro; IPR000650; Gem_coat_AR1.
DR InterPro; IPR000263; GV_A/BR1_coat.
DR InterPro; IPR029053; Viral_coat.
DR Pfam; PF00844; Gemini_coat; 1.
DR PRINTS; PR00224; GEMCOATAR1.
DR PRINTS; PR00223; GEMCOATARBR1.
PE 3: Inferred from homology;
KW Capsid protein; DNA-binding; Host nucleus; Host-virus interaction;
KW Metal-binding; T=1 icosahedral capsid protein;
KW Viral penetration into host nucleus; Virion; Virus entry into host cell;
KW Zinc; Zinc-finger.
FT CHAIN 1..251
FT /note="Capsid protein"
FT /id="PRO_0000222189"
FT ZN_FING 63..80
FT /evidence="ECO:0000255"
FT MOTIF 3..20
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 35..49
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 96..117
FT /note="Nuclear export signal"
FT /evidence="ECO:0000255"
FT MOTIF 195..242
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
SQ SEQUENCE 251 AA; 29153 MW; 737A26E679DCE0E4 CRC64;
MPKRDAPWRL TAGTAKISRT GNNSRALIMG PSTSRASAWV NRPMYRKPRI YRMYRTPDVP
KGCEGPCKVQ SFEQRHDVSH VGKVICISDV TRGNGITHRV GKRFCVKSVY ILGKIWMDEN
IKLKNHTNSV MFWLVRDRRP YGTPMDFGQV FNMYDNEPST ATVKNDLRDR YQVMHRFYAK
VTGGQYASNE QALVRRFWKV NNHVVYNHQE AGKYENHTEN ALLLYMACTH ASNPVYATLK
IRVYFYDSIM N