CAPSD_CLVK
ID CAPSD_CLVK Reviewed; 258 AA.
AC P03561;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Capsid protein;
DE AltName: Full=Coat protein;
DE Short=CP;
GN ORFNames=AR1, AV1;
OS African cassava mosaic virus (isolate West Kenyan 844) (ACMV) (Cassava
OS latent virus (isolate West Kenyan 844)).
OC Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC Geplafuvirales; Geminiviridae; Begomovirus.
OX NCBI_TaxID=10818;
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].
RA Stanley J., Gay M.R.;
RT "Nucleotide sequence of cassava latent virus DNA.";
RL Nature 301:260-262(1983).
RN [2]
RP SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNALS, AND NUCLEAR EXPORT
RP SIGNAL.
RX PubMed=11485405; DOI=10.1006/viro.2001.1003;
RA Unseld S., Hoehnle M., Ringel M., Frischmuth T.;
RT "Subcellular targeting of the coat protein of African cassava mosaic
RT geminivirus.";
RL Virology 286:373-383(2001).
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
CC {ECO:0000269|PubMed:11485405}. Note=It is actively transported into the
CC host cell nucleus. It may be exported out of the nucleus through a
CC nuclear export signal for cell-to-cell movement and spread (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the geminiviridae capsid protein family.
CC {ECO:0000305}.
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DR EMBL; J02057; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A04164; QQOMC1.
DR PDB; 6EK5; EM; 4.20 A; 1/2/3/A/B/B1/B2/B3/BA/BB/BC/BD/BE/BF/BG/BH/BI/BJ/BK/BL/BM/BN/BO/BP/BQ/BR/BS/BT/BU/BV=48-252.
DR PDBsum; 6EK5; -.
DR SMR; P03561; -.
DR Proteomes; UP000008452; 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 1: Evidence at protein level;
KW 3D-structure; Capsid protein; DNA-binding; Host nucleus;
KW Host-virus interaction; 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_0000222180"
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; 30130 MW; F22A7F54DB56C9DD CRC64;
MSKRPGDIII STPGSKVRRR LNFDSPYRNR ATAPTVHVTN RKRAWVNRPM YRKPTMYRMY
RSPDIPRGCE GPCKVQSFEQ RDDVKHLGIC KVISDVTRGP GLTHRVGKRF CIKSIYILGK
IWLDETIKKQ NHTNNVIFYL LRDRRPYGNA PQDFGQIFNM FDNEPSTATI KNDLRDRFQV
LRKFHATVVG GPYGMKEQAL VKRFYRLNHH VTYNHQEAGK YENHTENALL LYMACTHASN
PVYATLKIRI YFYDSIGN