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Database: UniProt
Entry: G8BDG1_CANPC
LinkDB: G8BDG1_CANPC
Original site: G8BDG1_CANPC 
ID   G8BDG1_CANPC            Unreviewed;       850 AA.
AC   G8BDG1;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Replication factor C subunit 1 {ECO:0000256|ARBA:ARBA00020401, ECO:0000256|PIRNR:PIRNR036578};
GN   OrderedLocusNames=CPAR2_209530 {ECO:0000313|CGD:CAL0000155065,
GN   ECO:0000313|EMBL:CCE43308.1};
OS   Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia
OS   parapsilosis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=578454 {ECO:0000313|EMBL:CCE43308.1, ECO:0000313|Proteomes:UP000005221};
RN   [1] {ECO:0000313|Proteomes:UP000005221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
RN   [2] {ECO:0000313|Proteomes:UP000005221}
RP   GENOME REANNOTATION.
RC   STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
RX   PubMed=22192698; DOI=10.1186/1471-2164-12-628;
RA   Guida A., Lindstaedt C., Maguire S.L., Ding C., Higgins D.G., Corton N.J.,
RA   Berriman M., Butler G.;
RT   "Using RNA-seq to determine the transcriptional landscape and the hypoxic
RT   response of the pathogenic yeast Candida parapsilosis.";
RL   BMC Genomics 12:628-628(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; HE605206; CCE43308.1; -; Genomic_DNA.
DR   AlphaFoldDB; G8BDG1; -.
DR   STRING; 578454.G8BDG1; -.
DR   EnsemblFungi; CPAR2_209530-T; CPAR2_209530-T-p1; CPAR2_209530.
DR   CGD; CAL0000155065; CPAR2_209530.
DR   VEuPathDB; FungiDB:CPAR2_209530; -.
DR   eggNOG; KOG1968; Eukaryota.
DR   Proteomes; UP000005221; Chromosome 2.
DR   GO; GO:0005663; C:DNA replication factor C complex; IEA:EnsemblFungi.
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:0003682; F:chromatin binding; IEA:EnsemblFungi.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003689; F:DNA clamp loader activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006272; P:leading strand elongation; IEA:EnsemblFungi.
DR   GO; GO:0006298; P:mismatch repair; IEA:EnsemblFungi.
DR   GO; GO:0000278; P:mitotic cell cycle; IEA:EnsemblFungi.
DR   GO; GO:0070914; P:UV-damage excision repair; IEA:EnsemblFungi.
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|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:UP000005221}.
FT   DOMAIN          148..225
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   REGION          1..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          240..294
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          801..850
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..45
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..97
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        240..276
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        279..294
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        815..829
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   850 AA;  94750 MW;  FCAF811719912B3D CRC64;
     MVNIQDFFKN SQEKPAAKRK VEETESPSAK RSKSATAKPK PEMIELDDDF EFDDDDIMEI
     EPPKKTTPRK KKPLASPRKT PAKASSPTKN ETKQKPTEPV VGESIDQVLA KIPDAELPEV
     NEGEKPNFFA LKAQQNATTS TSVDLPAAQP NCLTGLTIVF TGQMPSLDRN TAESTAQQYG
     AKVTKSISKK TSLVVIGSDA GPSKVKKIRE FKIKAIDEDG FIQLLSSMPA DGGSGEVALK
     AKEKREQEEK KIIEDAERDE REERKEEQKR AKKAQEIANR NVSGGTSQSP PVTQEVPAKD
     KLWTDKHAPK DFNQLCGNKG QVQKLRSWLE HWFENKAKNF PGGSDNPSSY RAALISGPPG
     IGKTTAAHLV ANSLGFDVLE KNASDVRSKS LLNANIKSVL NNTSVIGFFK HRDDEQQSSN
     SRKICLIMDE VDGMSSGDHG GAGALSQFCR ITNMPMILIC NDKSLPKMRT FDRVTYDLPF
     RRPTENEVKS RLMTIALREG IKLDPNIIGQ LVQATSNDIR QMINLLSTVS KTQKLIGTNN
     VKEIQASWKK QIILKPFDIA GRLLSSGIWT GPRQNLTEKL DLYFNDIDFA PLMIQENYLN
     TRPRLPGPHI QHVAQAADDI SISDSINSLI RSSEQQWSLL PFHGLMSTVK PSYEVAGQVT
     GRLNFSAWLG QNSKQMKFQR MLQELQYHTR VKTSTTKQEL RLDYLNPLWV KLNIPIKQQG
     EAGINQTIET MDAYYLTKED YDNISDMLNK PVDLDKKDKA AFTRKYNNVI HPTVIYKTGN
     SFGVGGKRAA STKVDYEEVV DDDMEDIDDD NDGDNSDKID TKKDKLIKQV PVGKSGAAKR
     TTKGPARKKQ
//
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