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Database: UniProt
Entry: Q01043
LinkDB: Q01043
Original site: Q01043 
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   05-JUN-2019, entry version 101.
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; Herpesvirales; Herpesviridae; Gammaherpesvirinae;
OC   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;
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
RT   herpesvirus saimiri (HVS) L-DNA: general conservation of genetic
RT   organization between 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
RT   and 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
CC       during latent infections of T-cells in susceptible hosts.
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin D subfamily.
CC       {ECO:0000305}.
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-methylbutan-1-ol.
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; Complete proteome; Cyclin;
KW   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       Cyclin homolog.
FT                                /FTId=PRO_0000080509.
FT   HELIX        15     18       {ECO:0000244|PDB:2F2C}.
FT   HELIX        21     31       {ECO:0000244|PDB:2F2C}.
FT   TURN         40     43       {ECO:0000244|PDB:2F2C}.
FT   STRAND       45     47       {ECO:0000244|PDB:1BU2}.
FT   HELIX        49     65       {ECO:0000244|PDB:2F2C}.
FT   HELIX        72     83       {ECO:0000244|PDB:2F2C}.
FT   TURN         84     86       {ECO:0000244|PDB:2F2C}.
FT   TURN         91     93       {ECO:0000244|PDB:2F2C}.
FT   HELIX        94    109       {ECO:0000244|PDB:2F2C}.
FT   HELIX       116    119       {ECO:0000244|PDB:2F2C}.
FT   TURN        122    125       {ECO:0000244|PDB:1BU2}.
FT   HELIX       129    142       {ECO:0000244|PDB:2F2C}.
FT   TURN        143    145       {ECO:0000244|PDB:2F2C}.
FT   HELIX       152    154       {ECO:0000244|PDB:2F2C}.
FT   HELIX       156    162       {ECO:0000244|PDB:2F2C}.
FT   HELIX       167    169       {ECO:0000244|PDB:2F2C}.
FT   HELIX       170    184       {ECO:0000244|PDB:2F2C}.
FT   HELIX       188    190       {ECO:0000244|PDB:2F2C}.
FT   STRAND      191    193       {ECO:0000244|PDB:1XO2}.
FT   HELIX       195    208       {ECO:0000244|PDB:2F2C}.
FT   HELIX       218    228       {ECO:0000244|PDB:2F2C}.
FT   HELIX       232    247       {ECO:0000244|PDB:2F2C}.
FT   HELIX       251    253       {ECO:0000244|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
//
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