ID   RFC2_BOVIN              Reviewed;         352 AA.
AC   Q05B83;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Replication factor C subunit 2;
DE   AltName: Full=Activator 1 subunit 2;
GN   Name=RFC2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Brain cortex;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The elongation of primed DNA templates by DNA polymerase
CC       delta and epsilon requires the action of the accessory proteins
CC       proliferating cell nuclear antigen (PCNA) and activator 1. This subunit
CC       binds ATP (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterotetramer of subunits RFC2, RFC3, RFC4 and RFC5 that can
CC       form a complex either with RFC1 or with RAD17. The former interacts
CC       with PCNA in the presence of ATP, while the latter has ATPase activity
CC       but is not stimulated by PCNA. RFC2 also interacts with PRKAR1A; the
CC       complex may be involved in cell survival. Interacts with DDX11.
CC       {ECO:0000250|UniProtKB:P35250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the activator 1 small subunits family.
CC       {ECO:0000305}.
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DR   EMBL; BC122635; AAI22636.1; -; mRNA.
DR   RefSeq; NP_001074372.1; NM_001080903.1.
DR   AlphaFoldDB; Q05B83; -.
DR   SMR; Q05B83; -.
DR   BioGRID; 165290; 1.
DR   STRING; 9913.ENSBTAP00000024740; -.
DR   PaxDb; Q05B83; -.
DR   PRIDE; Q05B83; -.
DR   Ensembl; ENSBTAT00000024740; ENSBTAP00000024740; ENSBTAG00000018589.
DR   GeneID; 508652; -.
DR   KEGG; bta:508652; -.
DR   CTD; 5982; -.
DR   VEuPathDB; HostDB:ENSBTAG00000018589; -.
DR   VGNC; VGNC:33886; RFC2.
DR   eggNOG; KOG0991; Eukaryota.
DR   GeneTree; ENSGT00550000075050; -.
DR   HOGENOM; CLU_042324_0_1_1; -.
DR   InParanoid; Q05B83; -.
DR   OMA; SCNYSSQ; -.
DR   OrthoDB; 1071197at2759; -.
DR   TreeFam; TF300585; -.
DR   Proteomes; UP000009136; Chromosome 25.
DR   Bgee; ENSBTAG00000018589; Expressed in diaphragm and 105 other tissues.
DR   ExpressionAtlas; Q05B83; baseline and differential.
DR   GO; GO:0031390; C:Ctf18 RFC-like complex; ISS:UniProtKB.
DR   GO; GO:0005663; C:DNA replication factor C complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003689; F:DNA clamp loader activity; IEA:Ensembl.
DR   GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR   GO; GO:0017116; F:single-stranded DNA helicase activity; IEA:Ensembl.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IBA:GO_Central.
DR   GO; GO:1900264; P:positive regulation of DNA-directed DNA polymerase activity; ISS:UniProtKB.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR013748; Rep_factorC_C.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF08542; Rep_fac_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF48019; SSF48019; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; DNA replication; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..352
FT                   /note="Replication factor C subunit 2"
FT                   /id="PRO_0000330461"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         74..81
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P35250"
FT   MOD_RES         28
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35250"
FT   MOD_RES         161
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P35250"
FT   MOD_RES         302
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P35250"
SQ   SEQUENCE   352 AA;  38730 MW;  6841C45B36474076 CRC64;
     MEAQDSGGGT GECGAQDAAP GPSKAPGSAG HYELPWVEKY RPVKLNEIVG NEDTVSRLEV
     FAREGNVPNI IIAGPPGTGK TTSILCLARA LLGPALKDAV LELNASNDRG IDVVRNKIKM
     FAQQKVTLPK GRHKIIILDE ADSMTDGAQQ ALRRTMEIYS KTTRFALACN ASDKIIEPIQ
     SRCAVLRYTK LTDMQILARL LSVIEKEKVQ YTDDGLEAII FTAQGDMRQA LNNLQSTYSG
     FGFINSENVF KVCDEPHPLL VKEMIQHCVS ADIDEAYKIL AHLWHLGYSP EDIIGNIFRV
     CKTFQMAEYL KLEFIKEIGY THMKIAEGVN SLLQMAGLLA RLCQKTMAPV AS