ID A0A5C5FWG8_9BASI Unreviewed; 888 AA.
AC A0A5C5FWG8;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE RecName: Full=Replication factor C subunit 1 {ECO:0000256|ARBA:ARBA00020401, ECO:0000256|PIRNR:PIRNR036578};
GN ORFNames=DMC30DRAFT_446392 {ECO:0000313|EMBL:TNY21158.1};
OS Rhodotorula diobovata.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=5288 {ECO:0000313|EMBL:TNY21158.1, ECO:0000313|Proteomes:UP000311382};
RN [1] {ECO:0000313|EMBL:TNY21158.1, ECO:0000313|Proteomes:UP000311382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCD-FST 08-225 {ECO:0000313|EMBL:TNY21158.1,
RC ECO:0000313|Proteomes:UP000311382};
RA Fakankun I.U., Fristensky B., Levin D.B.;
RT "Rhodosporidium diobovatum UCD-FST 08-225 genome sequencing, assembly, and
RT annotation.";
RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TNY21158.1}.
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DR EMBL; SOZI01000049; TNY21158.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5C5FWG8; -.
DR STRING; 5288.A0A5C5FWG8; -.
DR Proteomes; UP000311382; Unassembled WGS sequence.
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:InterPro.
DR GO; GO:0003689; F:DNA clamp loader activity; IEA:UniProtKB-UniRule.
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; 2.
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 Nucleotide-binding {ECO:0000256|PIRNR:PIRNR036578};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR036578};
KW Reference proteome {ECO:0000313|Proteomes:UP000311382}.
FT DOMAIN 191..281
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 801..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..850
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..867
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..888
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 888 AA; 96240 MW; FE3FF8811EEFC9B8 CRC64;
MAPRIKLASS DSDDTAPARK LAPAKKRKAP STDVVTLSDS SSSEDDVKPQ KKKAKVAKKH
DTSSDDDVKP AAKGKAGKKA TTKPSTSSSN AKGKGKKRDD DYEGGTSSSD DDVHMKDDDE
EEDVKPKKKS ASSSKALSST ATSKAKAPAA MAKKPTAVKD EDADDVKPKP KWTFKPKTGP
VAPGSKEIPD GDPDCLAGLT IVFTGELASL SREEGQELVK RYGGRVTTAP SSKTSYVVLG
SEAGPKKLEQ IAKHKIKTLD EDGFLALIGS RRSDPNDPKV REAKQKEEAK VKEAVKGLKG
LGKDAPEHLT QLWTTKYAPQ RLADICGNKS HVEKLQRWLE NWPKYLAANF KKPGPDAMGT
HRCVLISGPP GIGKTTSAHL VAKLLGYDVL ELNASDTRSK KLLEEAFRSK TSDTTLAGFV
KKEGEDHASG LSVNRKSLII MDEVDGMSAG DRGGVGALNA VIKKSKVPII AIANDAKSQK
MKPLLNTTFQ MLFKRPTAQE IRSRIMSIAF KEGLKLDGKV VDQLVQGSQS DIRQIINMLA
TYKLGAQAIS FDQGKALVRM NEKNTLQTPR TLFSKLFGPQ AFSPVSGMTL NDKLDVYFHD
FGLMPLFVQD NYLKGKFSRA AGTSGVEEKV RNLELVCKAA EAISDGDLVD AMIHGQQQQW
SLMPVHGMLS CVRPASLCYG GGGGYPTFPA WLGKNSTQNK LQRALSEIQV RMRLRVSGDK
RDLRQSYLPT LFPRLVEPLQ ERGTDGVDEV IELMDEYYLG RDEWDTIVEL GVGDGRTMEE
VLKKIPSQTK SAFTRKYNAQ DHPIPYHKPE AGRAQAKKLA PQGDAPDLEE AFVEDDLPDD
DGDGADDAAG DSDSSDVTKD KLVKAKKPKG AAGKKAPAKK ASAVKGKK
//