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CTF8_YEAST
ID   CTF8_YEAST              Reviewed;         133 AA.
AC   P38877; D3DLD9;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 157.
DE   RecName: Full=Chromosome transmission fidelity protein 8;
GN   Name=CTF8; OrderedLocusNames=YHR191C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, IDENTIFICATION IN THE
RP   CTF18-RFC COMPLEX, AND SUBCELLULAR LOCATION.
RX   PubMed=11389843; DOI=10.1016/s1097-2765(01)00254-4;
RA   Mayer M.L., Gygi S.P., Aebersold R., Hieter P.;
RT   "Identification of RFC(Ctf18p, Ctf8p, Dcc1p): an alternative RFC complex
RT   required for sister chromatid cohesion in S. cerevisiae.";
RL   Mol. Cell 7:959-970(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091229; DOI=10.1126/science.8091229;
RA   Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA   Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA   Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA   Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA   St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA   Waterston R., Wilson R., Vaudin M.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   VIII.";
RL   Science 265:2077-2082(1994).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   IDENTIFICATION IN THE CTF18-RFC COMPLEX, AND FUNCTION OF THE CTF18-RFC
RP   COMPLEX.
RX   PubMed=15964801; DOI=10.1128/mcb.25.13.5445-5455.2005;
RA   Bylund G.O., Burgers P.M.;
RT   "Replication protein A-directed unloading of PCNA by the Ctf18 cohesion
RT   establishment complex.";
RL   Mol. Cell. Biol. 25:5445-5455(2005).
CC   -!- FUNCTION: Essential for the fidelity of chromosome transmission.
CC       Required for the DNA replication block checkpoint. Component of the
CC       RFC-like complex CTF18-RFC which is required for efficient
CC       establishment of chromosome cohesion during S-phase and may load or
CC       unload POL30/PCNA. During a clamp loading circle, the RFC:clamp complex
CC       binds to DNA and the recognition of the double-stranded/single-stranded
CC       junction stimulates ATP hydrolysis by RFC. The complex presumably
CC       provides bipartite ATP sites in which one subunit supplies a catalytic
CC       site for hydrolysis of ATP bound to the neighboring subunit.
CC       Dissociation of RFC from the clamp leaves the clamp encircling DNA.
CC       {ECO:0000269|PubMed:11389843, ECO:0000269|PubMed:15964801}.
CC   -!- SUBUNIT: Component of the CTF18-RFC complex, which consists of CTF18,
CC       CTF8, DSCC1, RFC2, RFC3, RFC4 and RFC5. {ECO:0000269|PubMed:11389843,
CC       ECO:0000269|PubMed:15964801}.
CC   -!- INTERACTION:
CC       P38877; P49956: CTF18; NbExp=4; IntAct=EBI-5216, EBI-4560;
CC       P38877; P25559: DCC1; NbExp=2; IntAct=EBI-5216, EBI-5661;
CC       P38877; P40348: RFC2; NbExp=2; IntAct=EBI-5216, EBI-14992;
CC       P38877; P38629: RFC3; NbExp=2; IntAct=EBI-5216, EBI-15000;
CC       P38877; P40339: RFC4; NbExp=2; IntAct=EBI-5216, EBI-15009;
CC       P38877; P38251: RFC5; NbExp=2; IntAct=EBI-5216, EBI-15016;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11389843}.
CC       Note=Associates with chromatin.
CC   -!- SIMILARITY: Belongs to the CTF8 family. {ECO:0000305}.
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DR   EMBL; U53671; AAA98983.1; -; Genomic_DNA.
DR   EMBL; U00030; AAB68366.1; -; Genomic_DNA.
DR   EMBL; AY558287; AAS56613.1; -; Genomic_DNA.
DR   EMBL; BK006934; DAA06883.1; -; Genomic_DNA.
DR   PIR; S46688; S46688.
DR   RefSeq; NP_012061.3; NM_001179322.3.
DR   PDB; 5MSM; X-ray; 2.29 A; B/E=1-133.
DR   PDB; 5OKC; X-ray; 2.30 A; F/H=1-133.
DR   PDB; 5OKI; X-ray; 4.50 A; D/H=1-133.
DR   PDB; 6S1C; X-ray; 6.10 A; C/G=1-133.
DR   PDB; 6S2E; EM; 4.20 A; D=1-133.
DR   PDB; 6S2F; EM; 5.80 A; D=1-133.
DR   PDBsum; 5MSM; -.
DR   PDBsum; 5OKC; -.
DR   PDBsum; 5OKI; -.
DR   PDBsum; 6S1C; -.
DR   PDBsum; 6S2E; -.
DR   PDBsum; 6S2F; -.
DR   AlphaFoldDB; P38877; -.
DR   SMR; P38877; -.
DR   BioGRID; 36625; 650.
DR   ComplexPortal; CPX-1731; CTF18-RFC complex.
DR   DIP; DIP-2727N; -.
DR   IntAct; P38877; 8.
DR   MINT; P38877; -.
DR   STRING; 4932.YHR191C; -.
DR   MaxQB; P38877; -.
DR   PaxDb; P38877; -.
DR   PRIDE; P38877; -.
DR   EnsemblFungi; YHR191C_mRNA; YHR191C; YHR191C.
DR   GeneID; 856598; -.
DR   KEGG; sce:YHR191C; -.
DR   SGD; S000001234; CTF8.
DR   VEuPathDB; FungiDB:YHR191C; -.
DR   eggNOG; KOG4487; Eukaryota.
DR   HOGENOM; CLU_090690_1_0_1; -.
DR   InParanoid; P38877; -.
DR   OMA; QRPLPIM; -.
DR   BioCyc; YEAST:G3O-31219-MON; -.
DR   PRO; PR:P38877; -.
DR   Proteomes; UP000002311; Chromosome VIII.
DR   RNAct; P38877; protein.
DR   GO; GO:0031390; C:Ctf18 RFC-like complex; IPI:SGD.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0035753; P:maintenance of DNA trinucleotide repeats; IMP:SGD.
DR   GO; GO:0007064; P:mitotic sister chromatid cohesion; IMP:SGD.
DR   InterPro; IPR018607; Ctf8.
DR   Pfam; PF09696; Ctf8; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; DNA replication; DNA-binding; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..133
FT                   /note="Chromosome transmission fidelity protein 8"
FT                   /id="PRO_0000079494"
FT   STRAND          3..7
FT                   /evidence="ECO:0007829|PDB:5MSM"
FT   HELIX           9..14
FT                   /evidence="ECO:0007829|PDB:5MSM"
FT   STRAND          22..25
FT                   /evidence="ECO:0007829|PDB:5MSM"
FT   STRAND          29..40
FT                   /evidence="ECO:0007829|PDB:5MSM"
FT   HELIX           45..50
FT                   /evidence="ECO:0007829|PDB:5MSM"
FT   TURN            54..56
FT                   /evidence="ECO:0007829|PDB:5MSM"
FT   STRAND          59..62
FT                   /evidence="ECO:0007829|PDB:5MSM"
FT   STRAND          65..84
FT                   /evidence="ECO:0007829|PDB:5MSM"
FT   TURN            85..87
FT                   /evidence="ECO:0007829|PDB:5MSM"
FT   STRAND          88..107
FT                   /evidence="ECO:0007829|PDB:5MSM"
FT   TURN            108..111
FT                   /evidence="ECO:0007829|PDB:5MSM"
FT   STRAND          112..125
FT                   /evidence="ECO:0007829|PDB:5MSM"
SQ   SEQUENCE   133 AA;  15169 MW;  D1E4A255B974D51F CRC64;
     MPSVDIDASQ WQKLTQSREK QTTVITPLGM MMLEIQGELE LPKDFASLAR RDSPNEGRFS
     EQDGETLIRF GSLQIDGERA TLFVGKKQRL LGKVTKLDVP MGIMHFNSKD NKVELVDVMK
     YKVIFKDRPL PIM
 
 
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