CAPSD_CLVN
ID CAPSD_CLVN Reviewed; 258 AA.
AC P14966;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Capsid protein;
DE AltName: Full=Coat protein;
DE Short=CP;
GN ORFNames=AR1, AV1;
OS African cassava mosaic virus (isolate Nigerian) (ACMV) (Cassava latent
OS virus (isolate Nigerian)).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Begomovirus.
OX NCBI_TaxID=222073;
OH NCBI_TaxID=197394; Hewittia sublobata.
OH NCBI_TaxID=3996; Jatropha multifida (Coralbush).
OH NCBI_TaxID=194268; Laportea.
OH NCBI_TaxID=3983; Manihot esculenta (Cassava) (Jatropha manihot).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2308831; DOI=10.1093/nar/18.1.197;
RA Morris B., Coates L., Lowe S., Richardson K., Eddy P.;
RT "Nucleotide sequence of the infectious cloned DNA components of African
RT cassava mosaic virus (Nigerian strain).";
RL Nucleic Acids Res. 18:197-198(1990).
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}.
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; X17095; CAA34950.1; -; Genomic_DNA.
DR PIR; S07591; VCOMCN.
DR SMR; P14966; -.
DR PRIDE; P14966; -.
DR Proteomes; UP000008453; 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..258
FT /note="Capsid protein"
FT /id="PRO_0000222181"
FT ZN_FING 69..86
FT /evidence="ECO:0000255"
FT MOTIF 3..20
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 41..55
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 102..123
FT /note="Nuclear export signal"
FT /evidence="ECO:0000255"
FT MOTIF 202..249
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
SQ SEQUENCE 258 AA; 30210 MW; 2692A85DAC8CD253 CRC64;
MSKRPGDIII STPGSKVRRR LNFDSPYRNR ATAPTVHVTN RKRAWMNRPM YRKPMMYRMY
RSPDIPRGCE GPCKVQSFEQ RDDVKHLGIC KVISDVTRGP GLTHRVGKRF CIKSIYILGK
IWMDENIKKQ NHTNNVMFYL LRDRRPYGNT PQDFGQIFNM FDNEPSTATI ENDLRDRFQV
LRKFHATVIG GPSGMKEQAL VKRFYRLNHH VTYNHQEAGK YENHTENALL LYMACTHASN
PVYATLKIRI YFYDSIGN
