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PCNA2_SACS2
ID   PCNA2_SACS2             Reviewed;         245 AA.
AC   Q97Z84;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   05-MAR-2002, sequence version 2.
DT   25-MAY-2022, entry version 127.
DE   RecName: Full=DNA polymerase sliding clamp 2 {ECO:0000255|HAMAP-Rule:MF_00317};
DE   AltName: Full=Proliferating cell nuclear antigen homolog 2 {ECO:0000255|HAMAP-Rule:MF_00317};
DE            Short=PCNA2 {ECO:0000255|HAMAP-Rule:MF_00317};
GN   Name=pcn2 {ECO:0000255|HAMAP-Rule:MF_00317}; Synonyms=pcnA-2;
GN   OrderedLocusNames=SSO1047;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN   [2]
RP   INTERACTION WITH DPO1 AND PCNA1, AND SUBUNIT.
RX   PubMed=12535540; DOI=10.1016/s1097-2765(02)00824-9;
RA   Dionne I., Nookala R.K., Jackson S.P., Doherty A.J., Bell S.D.;
RT   "A heterotrimeric PCNA in the hyperthermophilic archaeon Sulfolobus
RT   solfataricus.";
RL   Mol. Cell 11:275-282(2003).
RN   [3]
RP   SUBUNIT.
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=12675797; DOI=10.1046/j.1365-2958.2003.03444.x;
RA   Roberts J.A., Bell S.D., White M.F.;
RT   "An archaeal XPF repair endonuclease dependent on a heterotrimeric PCNA.";
RL   Mol. Microbiol. 48:361-371(2003).
RN   [4]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=17011573; DOI=10.1016/j.jmb.2006.09.011;
RA   Dorazi R., Parker J.L., White M.F.;
RT   "PCNA activates the Holliday junction endonuclease Hjc.";
RL   J. Mol. Biol. 364:243-247(2006).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS), AND SUBUNIT.
RX   PubMed=17012780; DOI=10.1107/s1744309106034075;
RA   Williams G.J., Johnson K., Rudolf J., McMahon S.A., Carter L., Oke M.,
RA   Liu H., Taylor G.L., White M.F., Naismith J.H.;
RT   "Structure of the heterotrimeric PCNA from Sulfolobus solfataricus.";
RL   Acta Crystallogr. F 62:944-948(2006).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS), AND SUBUNIT.
RX   PubMed=17052461; DOI=10.1016/j.molcel.2006.08.015;
RA   Pascal J.M., Tsodikov O.V., Hura G.L., Song W., Cotner E.A., Classen S.,
RA   Tomkinson A.E., Tainer J.A., Ellenberger T.;
RT   "A flexible interface between DNA ligase and PCNA supports conformational
RT   switching and efficient ligation of DNA.";
RL   Mol. Cell 24:279-291(2006).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH PCNA1 AND FEN,
RP   SUBUNIT, AND MUTAGENESIS OF 146-GLU--ASP-149.
RX   PubMed=16945955; DOI=10.1093/nar/gkl623;
RA   Dore A.S., Kilkenny M.L., Jones S.A., Oliver A.W., Roe S.M., Bell S.D.,
RA   Pearl L.H.;
RT   "Structure of an archaeal PCNA1-PCNA2-FEN1 complex: elucidating PCNA
RT   subunit and client enzyme specificity.";
RL   Nucleic Acids Res. 34:4515-4526(2006).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND SUBUNIT.
RX   PubMed=18703842; DOI=10.1107/s0907444908021665;
RA   Hlinkova V., Xing G., Bauer J., Shin Y.J., Dionne I., Rajashankar K.R.,
RA   Bell S.D., Ling H.;
RT   "Structures of monomeric, dimeric and trimeric PCNA: PCNA-ring assembly and
RT   opening.";
RL   Acta Crystallogr. D 64:941-949(2008).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 1-244 IN COMPLEX WITH DPO4, AND
RP   SUBUNIT.
RX   PubMed=19054331; DOI=10.1111/j.1365-2958.2008.06553.x;
RA   Xing G., Kirouac K., Shin Y.J., Bell S.D., Ling H.;
RT   "Structural insight into recruitment of translesion DNA polymerase Dpo4 to
RT   sliding clamp PCNA.";
RL   Mol. Microbiol. 71:678-691(2009).
CC   -!- FUNCTION: One of the sliding clamp subunits that acts as a moving
CC       platform for DNA processing. Responsible for tethering the catalytic
CC       subunit of DNA polymerase to DNA during high-speed replication.
CC       Heterotrimer stimulates the Holliday junction resolvase Hjc. DNA
CC       polymerase I, DNA ligase and the flap endonuclease may be
CC       constitutively associated with the PCNA heterotrimer forming a scanning
CC       complex able to couple DNA synthesis and Okazaki fragment maturation.
CC       {ECO:0000269|PubMed:17011573}.
CC   -!- SUBUNIT: Forms homodimers with PCNA1, which then recruit PCNA3; does
CC       not form homotrimers (PubMed:12535540, PubMed:18703842). The
CC       heterodimers interact with RfcS homotetramers (PubMed:12535540).
CC       Heterotrimer which circularizes head-to-tail (head is at N-terminus,
CC       tail is at C-terminus) to form a toroid; DNA passes through its center.
CC       Replication factor C (RFC) is required to load the toroid on the DNA.
CC       This subunit interacts with DNA polymerase I (dpo1) (PubMed:12535540).
CC       The heterotrimer also interacts with flap endonuclease 1, DNA ligase
CC       and XPF via the other subunits. {ECO:0000269|PubMed:12535540,
CC       ECO:0000269|PubMed:12675797, ECO:0000269|PubMed:16945955,
CC       ECO:0000269|PubMed:17011573, ECO:0000269|PubMed:17012780,
CC       ECO:0000269|PubMed:17052461, ECO:0000269|PubMed:18703842,
CC       ECO:0000269|PubMed:19054331}.
CC   -!- SIMILARITY: Belongs to the PCNA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00317}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK41309.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE006641; AAK41309.1; ALT_INIT; Genomic_DNA.
DR   PIR; F90256; F90256.
DR   RefSeq; WP_009989181.1; NC_002754.1.
DR   PDB; 2HII; X-ray; 2.79 A; B/Y=1-245.
DR   PDB; 2HIK; X-ray; 3.30 A; B/M/Y=1-245.
DR   PDB; 2IO4; X-ray; 2.60 A; B/D=1-245.
DR   PDB; 2IX2; X-ray; 2.20 A; B=1-245.
DR   PDB; 2IZO; X-ray; 2.90 A; B=1-245.
DR   PDB; 2NTI; X-ray; 2.50 A; B/E/H=1-245.
DR   PDB; 3FDS; X-ray; 2.05 A; D=1-244.
DR   PDB; 7RPO; EM; 4.16 A; B=1-245.
DR   PDB; 7RPW; EM; 4.38 A; B=1-245.
DR   PDB; 7RPX; EM; 4.20 A; B=1-245.
DR   PDBsum; 2HII; -.
DR   PDBsum; 2HIK; -.
DR   PDBsum; 2IO4; -.
DR   PDBsum; 2IX2; -.
DR   PDBsum; 2IZO; -.
DR   PDBsum; 2NTI; -.
DR   PDBsum; 3FDS; -.
DR   PDBsum; 7RPO; -.
DR   PDBsum; 7RPW; -.
DR   PDBsum; 7RPX; -.
DR   AlphaFoldDB; Q97Z84; -.
DR   SMR; Q97Z84; -.
DR   STRING; 273057.SSO1047; -.
DR   EnsemblBacteria; AAK41309; AAK41309; SSO1047.
DR   GeneID; 44129976; -.
DR   KEGG; sso:SSO1047; -.
DR   PATRIC; fig|273057.12.peg.1041; -.
DR   eggNOG; arCOG00488; Archaea.
DR   HOGENOM; CLU_043978_1_1_2; -.
DR   InParanoid; Q97Z84; -.
DR   OMA; KERTADY; -.
DR   PhylomeDB; Q97Z84; -.
DR   EvolutionaryTrace; Q97Z84; -.
DR   Proteomes; UP000001974; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030337; F:DNA polymerase processivity factor activity; IBA:GO_Central.
DR   GO; GO:0006272; P:leading strand elongation; IBA:GO_Central.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00317; DNApol_clamp_arch; 1.
DR   InterPro; IPR000730; Pr_cel_nuc_antig.
DR   InterPro; IPR022649; Pr_cel_nuc_antig_C.
DR   InterPro; IPR022659; Pr_cel_nuc_antig_CS.
DR   InterPro; IPR022648; Pr_cel_nuc_antig_N.
DR   PANTHER; PTHR11352:SF0; PTHR11352:SF0; 1.
DR   Pfam; PF02747; PCNA_C; 1.
DR   Pfam; PF00705; PCNA_N; 1.
DR   PRINTS; PR00339; PCNACYCLIN.
DR   PROSITE; PS01251; PCNA_1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA replication; DNA-binding; Reference proteome.
FT   CHAIN           1..245
FT                   /note="DNA polymerase sliding clamp 2"
FT                   /id="PRO_0000149216"
FT   MUTAGEN         146..149
FT                   /note="LSDL->KLSK: Loss of interaction with PCNA3, no
FT                   change with PCNA1."
FT                   /evidence="ECO:0000269|PubMed:16945955"
FT   STRAND          1..6
FT                   /evidence="ECO:0007829|PDB:3FDS"
FT   HELIX           8..19
FT                   /evidence="ECO:0007829|PDB:3FDS"
FT   STRAND          23..30
FT                   /evidence="ECO:0007829|PDB:3FDS"
FT   STRAND          33..39
FT                   /evidence="ECO:0007829|PDB:3FDS"
FT   STRAND          43..52
FT                   /evidence="ECO:0007829|PDB:3FDS"
FT   HELIX           53..55
FT                   /evidence="ECO:0007829|PDB:3FDS"
FT   STRAND          56..64
FT                   /evidence="ECO:0007829|PDB:3FDS"
FT   STRAND          66..71
FT                   /evidence="ECO:0007829|PDB:3FDS"
FT   HELIX           72..79
FT                   /evidence="ECO:0007829|PDB:3FDS"
FT   STRAND          87..92
FT                   /evidence="ECO:0007829|PDB:3FDS"
FT   STRAND          94..112
FT                   /evidence="ECO:0007829|PDB:3FDS"
FT   STRAND          129..135
FT                   /evidence="ECO:0007829|PDB:3FDS"
FT   HELIX           136..146
FT                   /evidence="ECO:0007829|PDB:3FDS"
FT   TURN            147..149
FT                   /evidence="ECO:0007829|PDB:3FDS"
FT   STRAND          151..158
FT                   /evidence="ECO:0007829|PDB:3FDS"
FT   STRAND          161..167
FT                   /evidence="ECO:0007829|PDB:3FDS"
FT   STRAND          172..177
FT                   /evidence="ECO:0007829|PDB:3FDS"
FT   STRAND          181..183
FT                   /evidence="ECO:0007829|PDB:3FDS"
FT   STRAND          185..189
FT                   /evidence="ECO:0007829|PDB:3FDS"
FT   STRAND          193..197
FT                   /evidence="ECO:0007829|PDB:3FDS"
FT   HELIX           198..203
FT                   /evidence="ECO:0007829|PDB:3FDS"
FT   HELIX           204..209
FT                   /evidence="ECO:0007829|PDB:3FDS"
FT   STRAND          212..218
FT                   /evidence="ECO:0007829|PDB:3FDS"
FT   STRAND          224..229
FT                   /evidence="ECO:0007829|PDB:3FDS"
FT   HELIX           231..233
FT                   /evidence="ECO:0007829|PDB:2IX2"
FT   STRAND          235..240
FT                   /evidence="ECO:0007829|PDB:3FDS"
SQ   SEQUENCE   245 AA;  27436 MW;  7A1B0506463DFE5E CRC64;
     MKAKVIDAVS FSYILRTVGD FLSEANFIVT KEGIRVSGID PSRVVFLDIF LPSSYFEGFE
     VSQEKEIIGF KLEDVNDILK RVLKDDTLIL SSNESKLTLT FDGEFTRSFE LPLIQVESTQ
     PPSVNLEFPF KAQLLTITFA DIIDELSDLG EVLNIHSKEN KLYFEVIGDL STAKVELSTD
     NGTLLEASGA DVSSSYGMEY VANTTKMRRA SDSMELYFGS QIPLKLRFKL PQEGYGDFYI
     APRAD
 
 
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