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RFCL_NANEQ
ID   RFCL_NANEQ              Reviewed;         430 AA.
AC   P60373;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-FEB-2004, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Replication factor C large subunit {ECO:0000255|HAMAP-Rule:MF_01508};
DE            Short=RFC large subunit {ECO:0000255|HAMAP-Rule:MF_01508};
DE   AltName: Full=Clamp loader large subunit {ECO:0000255|HAMAP-Rule:MF_01508};
GN   Name=rfcL {ECO:0000255|HAMAP-Rule:MF_01508}; OrderedLocusNames=NEQ430;
OS   Nanoarchaeum equitans (strain Kin4-M).
OC   Archaea; Nanoarchaeota; Candidatus Nanoarchaeia; Nanoarchaeales;
OC   Nanoarchaeaceae; Nanoarchaeum.
OX   NCBI_TaxID=228908;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kin4-M;
RX   PubMed=14566062; DOI=10.1073/pnas.1735403100;
RA   Waters E., Hohn M.J., Ahel I., Graham D.E., Adams M.D., Barnstead M.,
RA   Beeson K.Y., Bibbs L., Bolanos R., Keller M., Kretz K., Lin X., Mathur E.,
RA   Ni J., Podar M., Richardson T., Sutton G.G., Simon M., Soell D.,
RA   Stetter K.O., Short J.M., Noorderwier M.;
RT   "The genome of Nanoarchaeum equitans: insights into early archaeal
RT   evolution and derived parasitism.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:12984-12988(2003).
CC   -!- FUNCTION: Part of the RFC clamp loader complex which loads the PCNA
CC       sliding clamp onto DNA. {ECO:0000255|HAMAP-Rule:MF_01508}.
CC   -!- SUBUNIT: Heteromultimer composed of small subunits (RfcS) and large
CC       subunits (RfcL). {ECO:0000255|HAMAP-Rule:MF_01508}.
CC   -!- SIMILARITY: Belongs to the activator 1 small subunits family. RfcL
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01508}.
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DR   EMBL; AE017199; AAR39275.1; -; Genomic_DNA.
DR   AlphaFoldDB; P60373; -.
DR   SMR; P60373; -.
DR   STRING; 228908.NEQ430; -.
DR   PRIDE; P60373; -.
DR   EnsemblBacteria; AAR39275; AAR39275; NEQ430.
DR   KEGG; neq:NEQ430; -.
DR   PATRIC; fig|228908.8.peg.441; -.
DR   HOGENOM; CLU_027255_1_1_2; -.
DR   OMA; GGWTRYG; -.
DR   Proteomes; UP000000578; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003689; F:DNA clamp loader activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_01508; RfcL; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR023935; Rep_factor-C_lsu.
DR   Pfam; PF00004; AAA; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA replication; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..430
FT                   /note="Replication factor C large subunit"
FT                   /id="PRO_0000135957"
FT   BINDING         75..82
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01508"
SQ   SEQUENCE   430 AA;  49797 MW;  46923FE3844436F4 CRC64;
     MPSLWDYLNK DKKPVIKKVE PPKKKEIKRD IPLFIKYRPK TLDEVENQEQ AKQILRDYVI
     NYKKKYKGKA LLLYGPPGTG KTSSVYALAN ELGYEVLEVN ASDERDAIHI HHIVGEASKG
     KPLFHKGRII LVDEVDGLSG KEDRGGVGAL VNIIKQSSWP IICTANDPWD QKLKKLREIS
     IMVEFKRLSP KHVYNVLKKI VTNEKIKISD KILWDIAYKS GGDLRAAIND LETIIKSGII
     DENFVKALGN REQEIDIFKA LGIMFKTENL ATAVSAFNNV DLEFDEIFPW LEENIPVEYK
     RLDDIYRAYY WLGKADIFRK RIIKTQHWRL LVYAQIDAYG GIALAKNKKY PGFTRYQPPK
     RLKLLAQMKE KLEKLREHVS KLREKLHMSK RDIIKYYVSF ALKLKNLNKT VADKFLKAIG
     LSLKEIEEIR
 
 
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