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PCNA3_SULTO
ID   PCNA3_SULTO             Reviewed;         246 AA.
AC   Q973F5; F9VNC0;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=DNA polymerase sliding clamp 3 {ECO:0000255|HAMAP-Rule:MF_00317};
DE   AltName: Full=Proliferating cell nuclear antigen homolog 3 {ECO:0000255|HAMAP-Rule:MF_00317};
DE            Short=PCNA3 {ECO:0000255|HAMAP-Rule:MF_00317};
GN   Name=pcn3 {ECO:0000255|HAMAP-Rule:MF_00317}; Synonyms=pcnC;
GN   OrderedLocusNames=STK_09440;
OS   Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS   (Sulfolobus tokodaii).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfurisphaera.
OX   NCBI_TaxID=273063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX   PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA   Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA   Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA   Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA   Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT   "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT   Sulfolobus tokodaii strain7.";
RL   DNA Res. 8:123-140(2001).
RN   [2]
RP   FUNCTION, INTERACTION WITH PCNA1 AND PCNA2, AND SUBUNIT.
RC   STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX   PubMed=18782564; DOI=10.1016/j.bbrc.2008.08.150;
RA   Lu S., Li Z., Wang Z., Ma X., Sheng D., Ni J., Shen Y.;
RT   "Spatial subunit distribution and in vitro functions of the novel trimeric
RT   PCNA complex from Sulfolobus tokodaii.";
RL   Biochem. Biophys. Res. Commun. 376:369-374(2008).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND SUBUNIT.
RX   PubMed=21352919; DOI=10.1016/j.jsb.2011.02.006;
RA   Kawai A., Hashimoto H., Higuchi S., Tsunoda M., Sato M., Nakamura K.T.,
RA   Miyamoto S.;
RT   "A novel heterotetrameric structure of the crenarchaeal PCNA2-PCNA3
RT   complex.";
RL   J. Struct. Biol. 174:443-450(2011).
CC   -!- FUNCTION: Sliding clamp subunit that acts as a moving platform for DNA
CC       processing. Responsible for tethering the catalytic subunit of DNA
CC       polymerase and other proteins to DNA during high-speed replication (By
CC       similarity). Both trimeric complexes inhibit DNA ligase and both 3'-5'
CC       and 5'-3' activity of Hel308 (Hjm) helicase, but stimulate Hjc, the
CC       Holliday junction cleavage enzyme. {ECO:0000255|HAMAP-Rule:MF_00317,
CC       ECO:0000269|PubMed:18782564}.
CC   -!- SUBUNIT: The subunits circularize to form a toroid; DNA passes through
CC       its center. Replication factor C (RFC) is required to load the toroid
CC       on the DNA (By similarity). Forms dimeric complexes with PCNA1 and
CC       PCNA2, and trimeric complexes with PCNA123 and PCNA323; does not form
CC       homotrimers (PubMed:18782564). Crystal structures show a heterotetramer
CC       of 2 PCNA2 and 2 PCNA3, which would be large enough to clamp a Holliday
CC       junction (PubMed:21352919). {ECO:0000250, ECO:0000269|PubMed:18782564,
CC       ECO:0000269|PubMed:21352919}.
CC   -!- SIMILARITY: Belongs to the PCNA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00317}.
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DR   EMBL; BA000023; BAK54417.1; -; Genomic_DNA.
DR   RefSeq; WP_010978940.1; NC_003106.2.
DR   PDB; 3AIX; X-ray; 2.90 A; A=1-246.
DR   PDB; 3AIZ; X-ray; 2.80 A; C/D=1-246.
DR   PDBsum; 3AIX; -.
DR   PDBsum; 3AIZ; -.
DR   AlphaFoldDB; Q973F5; -.
DR   SMR; Q973F5; -.
DR   STRING; 273063.STK_09440; -.
DR   EnsemblBacteria; BAK54417; BAK54417; STK_09440.
DR   GeneID; 1458909; -.
DR   KEGG; sto:STK_09440; -.
DR   PATRIC; fig|273063.9.peg.1056; -.
DR   eggNOG; arCOG00488; Archaea.
DR   OMA; EMKLINM; -.
DR   OrthoDB; 70433at2157; -.
DR   EvolutionaryTrace; Q973F5; -.
DR   Proteomes; UP000001015; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030337; F:DNA polymerase processivity factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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..246
FT                   /note="DNA polymerase sliding clamp 3"
FT                   /id="PRO_0000149219"
FT   STRAND          2..6
FT                   /evidence="ECO:0007829|PDB:3AIZ"
FT   HELIX           8..18
FT                   /evidence="ECO:0007829|PDB:3AIZ"
FT   TURN            19..21
FT                   /evidence="ECO:0007829|PDB:3AIZ"
FT   STRAND          23..29
FT                   /evidence="ECO:0007829|PDB:3AIZ"
FT   STRAND          31..39
FT                   /evidence="ECO:0007829|PDB:3AIZ"
FT   STRAND          45..52
FT                   /evidence="ECO:0007829|PDB:3AIZ"
FT   HELIX           53..55
FT                   /evidence="ECO:0007829|PDB:3AIZ"
FT   STRAND          56..60
FT                   /evidence="ECO:0007829|PDB:3AIZ"
FT   STRAND          65..70
FT                   /evidence="ECO:0007829|PDB:3AIZ"
FT   HELIX           71..78
FT                   /evidence="ECO:0007829|PDB:3AIZ"
FT   STRAND          86..91
FT                   /evidence="ECO:0007829|PDB:3AIZ"
FT   STRAND          93..95
FT                   /evidence="ECO:0007829|PDB:3AIZ"
FT   STRAND          97..111
FT                   /evidence="ECO:0007829|PDB:3AIZ"
FT   STRAND          129..135
FT                   /evidence="ECO:0007829|PDB:3AIZ"
FT   HELIX           136..149
FT                   /evidence="ECO:0007829|PDB:3AIZ"
FT   STRAND          152..159
FT                   /evidence="ECO:0007829|PDB:3AIZ"
FT   STRAND          162..168
FT                   /evidence="ECO:0007829|PDB:3AIZ"
FT   STRAND          173..178
FT                   /evidence="ECO:0007829|PDB:3AIZ"
FT   TURN            180..183
FT                   /evidence="ECO:0007829|PDB:3AIZ"
FT   STRAND          186..190
FT                   /evidence="ECO:0007829|PDB:3AIZ"
FT   STRAND          193..198
FT                   /evidence="ECO:0007829|PDB:3AIZ"
FT   HELIX           199..203
FT                   /evidence="ECO:0007829|PDB:3AIZ"
FT   HELIX           204..208
FT                   /evidence="ECO:0007829|PDB:3AIZ"
FT   TURN            209..211
FT                   /evidence="ECO:0007829|PDB:3AIZ"
FT   STRAND          213..220
FT                   /evidence="ECO:0007829|PDB:3AIZ"
FT   STRAND          223..231
FT                   /evidence="ECO:0007829|PDB:3AIZ"
FT   TURN            232..234
FT                   /evidence="ECO:0007829|PDB:3AIZ"
FT   STRAND          235..241
FT                   /evidence="ECO:0007829|PDB:3AIZ"
SQ   SEQUENCE   246 AA;  27437 MW;  BA370A5D227B4E7F CRC64;
     MRVKVIDADA FSYIFRTLEE FIDEITLDFT SDGLKIRGID PSRVTFIDIL IPAGYFEEYN
     VEKEEKVGVK LEDFTDVLKT VTKNDSLYLE TDENQNIKVT LDGVYERTFT FPSIVASEIE
     TPNLNLEFPF KAKALTVTFT DIIDEIEDIG GDSITFKAEG GKLYLSANSD MGSSTIELST
     ENGGLLESEG GDAESVYGLE YVVNTSKMRK PSDTVEIAFG SQIPLKLRYN LPQGGYADFY
     IAPRAE
 
 
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