CGH2_SHV21
ID CGH2_SHV21 Reviewed; 254 AA.
AC Q01043;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 23-FEB-2022, entry version 109.
DE RecName: Full=Cyclin homolog;
DE AltName: Full=V-cyclin;
GN Name=72; Synonyms=ECLF2;
OS Saimiriine herpesvirus 2 (strain 11) (SaHV-2) (Herpesvirus saimiri).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX NCBI_TaxID=10383;
OH NCBI_TaxID=9521; Saimiri sciureus (Common squirrel monkey).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=1321287; DOI=10.1128/jvi.66.8.5047-5058.1992;
RA Albrecht J.-C., Nicholas J., Biller D., Cameron K.R., Biesinger B.,
RA Newman C., Wittmann S., Craxton M.A., Coleman H., Fleckenstein B.,
RA Honess R.W.;
RT "Primary structure of the herpesvirus saimiri genome.";
RL J. Virol. 66:5047-5058(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1314457; DOI=10.1016/0042-6822(92)90759-i;
RA Nicholas J., Cameron K.R., Coleman H., Newman C., Honess R.W.;
RT "Analysis of nucleotide sequence of the rightmost 43 kbp of herpesvirus
RT saimiri (HVS) L-DNA: general conservation of genetic organization between
RT HVS and Epstein-Barr virus.";
RL Virology 188:296-310(1992).
RN [3]
RP SIMILARITY TO G-PROTEIN COUPLED RECEPTORS.
RX PubMed=1309943; DOI=10.1038/355362a0;
RA Nicholas J., Cameron K.R., Honess R.W.;
RT "Herpesvirus saimiri encodes homologues of G protein-coupled receptors and
RT cyclins.";
RL Nature 355:362-365(1992).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 22-250.
RX PubMed=10368294; DOI=10.1016/s0969-2126(99)80035-5;
RA Schulze-Gahmen U., Jung J.U., Kim S.-H.;
RT "Crystal structure of a viral cyclin, a positive regulator of cyclin-
RT dependent kinase 6.";
RL Structure 7:245-254(1999).
CC -!- FUNCTION: May be highly relevant to the process of cellular
CC transformation and rapid T-cell proliferation effected by HVS during
CC latent infections of T-cells in susceptible hosts.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin D subfamily.
CC {ECO:0000305}.
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DR EMBL; S76368; AAB21115.1; -; Genomic_DNA.
DR EMBL; X64346; CAA45695.1; -; Genomic_DNA.
DR EMBL; M86409; AAA46148.1; -; Genomic_DNA.
DR RefSeq; NP_040274.1; NC_001350.1.
DR PDB; 1BU2; X-ray; 3.00 A; A=22-250.
DR PDB; 1JOW; X-ray; 3.10 A; A=1-254.
DR PDB; 1XO2; X-ray; 2.90 A; A=1-254.
DR PDB; 2EUF; X-ray; 3.00 A; A=1-254.
DR PDB; 2F2C; X-ray; 2.80 A; A=1-254.
DR PDB; 4TTH; X-ray; 2.90 A; A=1-254.
DR PDBsum; 1BU2; -.
DR PDBsum; 1JOW; -.
DR PDBsum; 1XO2; -.
DR PDBsum; 2EUF; -.
DR PDBsum; 2F2C; -.
DR PDBsum; 4TTH; -.
DR SMR; Q01043; -.
DR MINT; Q01043; -.
DR BindingDB; Q01043; -.
DR DrugBank; DB07379; (2S)-2-({6-[(3-Amino-5-chlorophenyl)amino]-9-isopropyl-9H-purin-2-yl}amino)-3-methyl-1-butanol.
DR DrugBank; DB07795; Fisetin.
DR GeneID; 1682479; -.
DR KEGG; vg:1682479; -.
DR EvolutionaryTrace; Q01043; -.
DR Proteomes; UP000000587; Genome.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0060153; P:modulation by virus of host cell cycle; IEA:UniProtKB-KW.
DR CDD; cd00043; CYCLIN; 1.
DR InterPro; IPR039361; Cyclin.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR015451; Cyclin_D.
DR InterPro; IPR015322; Cyclin_dom_herpesvir.
DR InterPro; IPR017285; Cyclin_herpesvir.
DR InterPro; IPR006671; Cyclin_N.
DR PANTHER; PTHR10177; PTHR10177; 1.
DR PANTHER; PTHR10177:SF65; PTHR10177:SF65; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR Pfam; PF09241; Herp-Cyclin; 1.
DR PIRSF; PIRSF037816; Viral_cyclin; 1.
DR SMART; SM00385; CYCLIN; 1.
DR SUPFAM; SSF47954; SSF47954; 2.
DR PROSITE; PS00292; CYCLINS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cyclin; Host-virus interaction;
KW Modulation of host cell cycle by viral cyclin-like protein;
KW Modulation of host cell cycle by virus; Reference proteome.
FT CHAIN 1..254
FT /note="Cyclin homolog"
FT /id="PRO_0000080509"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:2F2C"
FT HELIX 21..31
FT /evidence="ECO:0007829|PDB:2F2C"
FT TURN 40..43
FT /evidence="ECO:0007829|PDB:2F2C"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:1BU2"
FT HELIX 49..65
FT /evidence="ECO:0007829|PDB:2F2C"
FT HELIX 72..83
FT /evidence="ECO:0007829|PDB:2F2C"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:2F2C"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:2F2C"
FT HELIX 94..109
FT /evidence="ECO:0007829|PDB:2F2C"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:2F2C"
FT TURN 122..125
FT /evidence="ECO:0007829|PDB:1BU2"
FT HELIX 129..142
FT /evidence="ECO:0007829|PDB:2F2C"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:2F2C"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:2F2C"
FT HELIX 156..162
FT /evidence="ECO:0007829|PDB:2F2C"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:2F2C"
FT HELIX 170..184
FT /evidence="ECO:0007829|PDB:2F2C"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:2F2C"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:1XO2"
FT HELIX 195..208
FT /evidence="ECO:0007829|PDB:2F2C"
FT HELIX 218..228
FT /evidence="ECO:0007829|PDB:2F2C"
FT HELIX 232..247
FT /evidence="ECO:0007829|PDB:2F2C"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:2F2C"
SQ SEQUENCE 254 AA; 28637 MW; B682EB10111207F4 CRC64;
MADSPNRLNR AKIDSTTMKD PRVLNNLKLR ELLLPKFTSL WEIQTEVTVD NRTILLTWMH
LLCESFELDK SVFPLSVSIL DRYLCKKQGT KKTLQKIGAA CVLIGSKIRT VKPMTVSKLT
YLSCDCFTNL ELINQEKDIL EALKWDTEAV LATDFLIPLC NALKIPEDLW PQLYEAASTT
ICKALIQPNI ALLSPGLICA GGLLTTIETD NTNCRPWTCY LEDLSSILNF STNTVRTVKD
QVSEAFSLYD LEIL
