PCNA_METBF
ID PCNA_METBF Reviewed; 245 AA.
AC Q46E39;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=DNA polymerase sliding clamp {ECO:0000255|HAMAP-Rule:MF_00317};
DE AltName: Full=Proliferating cell nuclear antigen homolog {ECO:0000255|HAMAP-Rule:MF_00317};
DE Short=PCNA {ECO:0000255|HAMAP-Rule:MF_00317};
GN Name=pcn {ECO:0000255|HAMAP-Rule:MF_00317}; OrderedLocusNames=Mbar_A0879;
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fusaro / DSM 804;
RX PubMed=16980466; DOI=10.1128/jb.00810-06;
RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT "The Methanosarcina barkeri genome: comparative analysis with
RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT rearrangement within methanosarcinal genomes.";
RL J. Bacteriol. 188:7922-7931(2006).
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.
CC {ECO:0000255|HAMAP-Rule:MF_00317}.
CC -!- SUBUNIT: Homotrimer. The subunits circularize to form a toroid; DNA
CC passes through its center. Replication factor C (RFC) is required to
CC load the toroid on the DNA. {ECO:0000255|HAMAP-Rule:MF_00317}.
CC -!- SIMILARITY: Belongs to the PCNA family. {ECO:0000255|HAMAP-
CC Rule:MF_00317}.
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DR EMBL; CP000099; AAZ69853.1; -; Genomic_DNA.
DR RefSeq; WP_011305902.1; NC_007355.1.
DR AlphaFoldDB; Q46E39; -.
DR SMR; Q46E39; -.
DR STRING; 269797.Mbar_A0879; -.
DR EnsemblBacteria; AAZ69853; AAZ69853; Mbar_A0879.
DR GeneID; 3626187; -.
DR KEGG; mba:Mbar_A0879; -.
DR eggNOG; arCOG00488; Archaea.
DR HOGENOM; CLU_043978_1_1_2; -.
DR OMA; TIRKDPN; -.
DR OrthoDB; 70433at2157; -.
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 3: Inferred from homology;
KW DNA replication; DNA-binding.
FT CHAIN 1..245
FT /note="DNA polymerase sliding clamp"
FT /id="PRO_1000019170"
SQ SEQUENCE 245 AA; 26759 MW; 482A51F006E1688F CRC64;
MFKAAINAEL LKDAVAALAV IVDEVRFKIN PEGISVKAVD PANVAMGIFE LGSSAFDEYN
ADECEIGVDL NKITDLLGIA DKNDTVRMEL EEENHKLLID VGGLSYTLSL LDPSTIRAEP
RVPQLELPAK VVLNGADLRR AVKAAEKISD HMLMGVSDDT FYMEAKGDTD QVRLEMGRDQ
LIDLKAGEAC SLFSLDYLTD IVKPTNKVNE VTLSLGKDFP ILIDFEIANG SGRISYLLAP
RIESD