ID B5XGM4_SALSA Unreviewed; 335 AA.
AC B5XGM4;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Replication factor C subunit 5 {ECO:0000313|EMBL:ACI69994.1, ECO:0000313|RefSeq:NP_001135046.1};
GN Name=RFC5 {ECO:0000313|EMBL:ACI69994.1};
GN Synonyms=rfc5 {ECO:0000313|RefSeq:NP_001135046.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|EMBL:ACI69994.1};
RN [1] {ECO:0000313|EMBL:ACI69994.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Thyroid {ECO:0000313|EMBL:ACI69994.1};
RG cGRASP (B.F. Koop & W.S. Davidson);
RA Leong J., von Schalburg K., Cooper G., Moore R., Holt R., Davidson W.S.,
RA Koop B.F.;
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACI69994.1, ECO:0000313|RefSeq:NP_001135046.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Thyroid {ECO:0000313|EMBL:ACI69994.1};
RX PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA Koop B.F.;
RT "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT evolutionary pressures on a post-tetraploidization genome.";
RL BMC Genomics 11:279-279(2010).
RN [3] {ECO:0000313|EMBL:ACI69994.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Thyroid {ECO:0000313|EMBL:ACI69994.1};
RG cGRASP (B.F. Koop & W.S. Davidson);
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|RefSeq:NP_001135046.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the activator 1 small subunits family.
CC {ECO:0000256|ARBA:ARBA00005378}.
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DR EMBL; BT050193; ACI69994.1; -; mRNA.
DR RefSeq; NP_001135046.1; NM_001141574.1.
DR STRING; 8030.ENSSSAP00000082997; -.
DR PaxDb; 8030-ENSSSAP00000082997; -.
DR GeneID; 100196545; -.
DR KEGG; sasa:100196545; -.
DR OrthoDB; 275853at2759; -.
DR Proteomes; UP000087266; Chromosome ssa20.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
DR CDD; cd18140; HLD_clamp_RFC; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.272.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 InterPro; IPR047854; RFC_lid.
DR PANTHER; PTHR11669; REPLICATION FACTOR C / DNA POLYMERASE III GAMMA-TAU SUBUNIT; 1.
DR PANTHER; PTHR11669:SF9; REPLICATION FACTOR C SUBUNIT 5; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF08542; Rep_fac_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266}.
FT DOMAIN 46..174
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 335 AA; 37693 MW; 98419DCA75B1FE28 CRC64;
MASIGKIPLQ SRNLPWVEKY RPQTLDDLIS HKDILSTIQK FISEDRLPHL LFYGPPGTGK
TSTVLASAKQ LYKEKEFNAM VLELNASDDR GIDVVRGPIL SFASTRTIFK KGFKLVILDE
ADAMTRDAQN ALRRVIEKYT ENTRFCLICN YLSKIIPALQ SRCTRFRFGP LSQDQMIPRL
EFVIQQESID VTPDGMKAIV TLSSGDMRRS LNILQSTSMA YGKVTEDNVY TCTGHPLRSD
IANILDWSLN KDFTSAYNQI LQLKTLKGLA LHDILTEVHL LIHRVDFPPA IRMGLLIKLA
DIEYRLASGT SEKIQLSSMV AAFQAVRDIV VNEAA
//
