ID A0A109FK91_9BASI Unreviewed; 932 AA.
AC A0A109FK91;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Replication factor C subunit 1 {ECO:0000256|ARBA:ARBA00020401, ECO:0000256|PIRNR:PIRNR036578};
GN ORFNames=RHOSPDRAFT_15825 {ECO:0000313|EMBL:KWU46046.1};
OS Rhodotorula sp. JG-1b.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1305733 {ECO:0000313|EMBL:KWU46046.1, ECO:0000313|Proteomes:UP000062823};
RN [1] {ECO:0000313|EMBL:KWU46046.1, ECO:0000313|Proteomes:UP000062823}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JG-1b {ECO:0000313|EMBL:KWU46046.1,
RC ECO:0000313|Proteomes:UP000062823};
RG DOE Joint Genome Institute;
RA Goordial J., Raymond-Bouchard I., Riley R., Ronholm J., Shapiro N.,
RA Woyke T., Grigoriev I.V., Labutti K.M., Greer C., Whyte L., Bakermans C.;
RT "Draft genome of eurypsychrophile Rhodotorula sp. JG1b isolated from
RT permafrost in the hyper-arid Upper Elevation McMurdo Dry Valleys,
RT Antarctica.";
RL Submitted (DEC-2015) 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}.
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DR EMBL; KQ954469; KWU46046.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A109FK91; -.
DR STRING; 1305733.A0A109FK91; -.
DR OrthoDB; 6297at2759; -.
DR Proteomes; UP000062823; 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; cd17752; BRCT_RFC1; 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:SF37; 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|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR036578};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|PIRNR:PIRNR036578};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR036578}; Nucleus {ECO:0000256|PIRNR:PIRNR036578};
KW Reference proteome {ECO:0000313|Proteomes:UP000062823}.
FT DOMAIN 212..302
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 879..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..122
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 879..893
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..909
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 932 AA; 100693 MW; 00EB0EADD7D5F6C3 CRC64;
MEILSEAGKK STTASPRKRK VAASNEIILS SSSSDEDAGA DKPAKKKKKV TAVEDDGKKG
KKPIKKEAVA SKATKASTSK AAPAKKKKKK VEASSSSDEY DKDASASSEE DEYDDDEEEE
EEDVKPLKGK KKATAATVTK KAITTAASKP KASTSKGAPA ASKSKATKSV KKEVVDDDND
DDEEEEARPK PKWQYKPRAG PAAPGSKEIP VGDEGCLAGL TFVFTGELES LSREAGQDLV
KRYGGRVTTA PSSKTSYVVL GSDAGPKKLE LIKKHKLKTL DEDGFLGLIG NRKADPNDPK
LVEAKKKEEA KVKEAAKALT LAKDAPTLTN RLNPPSTHPL DREHLTQLWT TKYAPQRLAD
ICGNKSQVEK LKKWLENWPK SLACGFKKPG PDAMNTFRCV LISGPPGIGK TTAAHLVAKM
LGFDVLELNA SDTRSKRLLE EAFRSKVTDT TLSGFFKTEG GGGGDDDGGE GEGLGVNNKS
LIIMDEVDGM SAGDRGGIGA LNSFLKKTKI PIIAIANDSK SQKMKPLINT TFQMLFKRPS
AQEVRSRVMS IAFKEGLKLE QGVVDQLVAG SQSDIRQIIN MLATYKLGAK AMNFDASKKL
AKMNEKNTIQ TPWTLYSKLF GPQAFSPVSG LTLNDKLDVY FQDHSIMPLF VQENYLRGRF
QRAGGEVGPG LQLKNLELAS KAAESISDGD LVDAMIHGTQ QQWSLMPLHG MLSCVRPASF
CYGQGGGYPN FPAWLGKNST QGKLGRALGE IQIRMRLRVS GDKREIRQSY LPTLVPRLVS
PLVEHGTEGV QEVIELMDQY YLGKEEWDAI VEMGIGEGMG VEQVLKSIPT TTKSAFTRKY
NSSDHPIPYY KPEAGRAKAK KIAPQGEAPD LEEAFDLAEA DLVDDDDEGD SASDGPESFA
KDKMIKAKKP KGGAAAASKK KATATKGKAA KK
//
