ID G0WB40_NAUDC Unreviewed; 892 AA.
AC G0WB40;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=Replication factor C subunit 1 {ECO:0000256|ARBA:ARBA00020401, ECO:0000256|PIRNR:PIRNR036578};
GN Name=NDAI0E01440 {ECO:0000313|EMBL:CCD24960.1};
GN OrderedLocusNames=NDAI_0E01440 {ECO:0000313|EMBL:CCD24960.1};
OS Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 / NBRC
OS 0211 / NRRL Y-12639) (Saccharomyces dairenensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCD24960.1, ECO:0000313|Proteomes:UP000000689};
RN [1] {ECO:0000313|EMBL:CCD24960.1, ECO:0000313|Proteomes:UP000000689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639
RC {ECO:0000313|Proteomes:UP000000689};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR036578}.
CC -!- SIMILARITY: Belongs to the activator 1 large subunit family.
CC {ECO:0000256|ARBA:ARBA00006116, ECO:0000256|PIRNR:PIRNR036578}.
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DR EMBL; HE580271; CCD24960.1; -; Genomic_DNA.
DR RefSeq; XP_003670203.1; XM_003670155.1.
DR AlphaFoldDB; G0WB40; -.
DR STRING; 1071378.G0WB40; -.
DR GeneID; 11498850; -.
DR KEGG; ndi:NDAI_0E01440; -.
DR eggNOG; KOG1968; Eukaryota.
DR HOGENOM; CLU_003574_1_0_1; -.
DR OMA; LICNERN; -.
DR OrthoDB; 6297at2759; -.
DR Proteomes; UP000000689; Chromosome 5.
DR GO; GO:0005663; C:DNA replication factor C complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003689; F:DNA clamp loader activity; IEA:UniProtKB-UniRule.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IEA:UniProt.
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; 3.40.50.10190; BRCT domain; 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; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR InterPro; IPR013725; DNA_replication_fac_RFC1_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR012178; RFC1.
DR InterPro; IPR047854; RFC_lid.
DR PANTHER; PTHR23389; CHROMOSOME TRANSMISSION FIDELITY FACTOR 18; 1.
DR PANTHER; PTHR23389:SF6; REPLICATION FACTOR C SUBUNIT 1; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF08519; RFC1; 1.
DR PIRSF; PIRSF036578; RFC1; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00292; BRCT; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1.
DR PROSITE; PS50172; BRCT; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRNR:PIRNR036578};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|PIRNR:PIRNR036578};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR036578};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR036578};
KW Reference proteome {ECO:0000313|Proteomes:UP000000689}.
FT DOMAIN 179..256
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 824..892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..852
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 892 AA; 97818 MW; 38D52EB9086671E5 CRC64;
MVNITDFFNK SAKRKIPSKT ATKSSSSSSS GAPNSIPQEV INLDDSDEDD IIIKKPARKK
TKTTAEPPTI EKKKEADSDI INLSSSPIAS KKEAKSATER ITESKSKPAA PKKTTKPSSI
SSATSHGSIT AQDILDKLPS VDLSQVHAKE NVGFDFSKAG GATTGEEVDA EAPPDFPEGQ
PNCLLGLTIV FTGVLPNLER EVAESIAKRY GARVTKSISG RTSVVVLGDE AGPKKLEKIK
QLKIKAIDED GFRQLVSGMP AEGGDGEAAE KARQKREQEE AKAVQEAEEL LKTENAKKER
IKMAKGSGEF INKEDSVREE DKLWTVKYAP TSSVGICGNK TSVTKLKNWL TNWETNKKND
FKTAGRDGTG IFRSAMLYGP PGIGKTTAAH LVAKELGYDV LEQNASDVRS KSLLNAGVKN
ALGNMSVIGY FKNQPGMNVD INGNGKKFVI IMDEVDGMSG GDRGGVGQLA QFCRKTTTPM
ILICNERNLP KMRPFDRICL DLQFRRPDAN SIKSRLMTIA IREKFKLDPN IIDKLVQTTR
GDIRQIINLL STISKTTKNI GHENIQEISK AWEKNIALKP FDIAHKLLDG YIYTDVGSNT
FTLNDKIALY FDDFDFAPLM IQENYLNCKP SNLPSGVSHL QAVADAAESI SAADLVEKKI
RSSEQLWGLL PLHAVLSSVR PSSMIAGRMT GRINFSAWLG QNSKTNKYYR LLQELQYHTR
LSTSTDKLGL RLAYLPTFKR RLLEPLLHKG AEGVSDVIEL MDDYYLTRED WDTIMDFMIG
PDITTLQLKK IPTSVKTAFT RKYNSMTHPV AIYKTGSSIG TGVGSAARST PDFEDVVDAD
DAVPGAEDED EGKEDTDIKK DKLIKQKVRP TKRKKAVGAA GAAATKKRKT KA
//