ID G8B903_CANPC Unreviewed; 357 AA.
AC G8B903;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN OrderedLocusNames=CPAR2_300910 {ECO:0000313|CGD:CAL0000144665,
GN ECO:0000313|EMBL:CCE41102.1};
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:CCE41102.1, 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 -!- SIMILARITY: Belongs to the activator 1 small subunits family.
CC {ECO:0000256|ARBA:ARBA00005378}.
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DR EMBL; HE605204; CCE41102.1; -; Genomic_DNA.
DR AlphaFoldDB; G8B903; -.
DR STRING; 578454.G8B903; -.
DR EnsemblFungi; CPAR2_300910-T; CPAR2_300910-T-p1; CPAR2_300910.
DR CGD; CAL0000144665; CPAR2_300910.
DR VEuPathDB; FungiDB:CPAR2_300910; -.
DR eggNOG; KOG0989; Eukaryota.
DR Proteomes; UP000005221; Chromosome 3.
DR GO; GO:0031390; C:Ctf18 RFC-like complex; IEA:EnsemblFungi.
DR GO; GO:0005663; C:DNA replication factor C complex; IEA:EnsemblFungi.
DR GO; GO:0031391; C:Elg1 RFC-like complex; IEA:EnsemblFungi.
DR GO; GO:0031389; C:Rad17 RFC-like complex; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:EnsemblFungi.
DR GO; GO:0090618; P:DNA clamp unloading; IEA:EnsemblFungi.
DR GO; GO:0006272; P:leading strand elongation; IEA:EnsemblFungi.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; IEA:EnsemblFungi.
DR GO; GO:0007062; P:sister chromatid cohesion; 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; 3.40.50.300; 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:SF20; REPLICATION FACTOR C SUBUNIT 4; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000005221}.
FT DOMAIN 46..184
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 357 AA; 40152 MW; C2974D596E74A486 CRC64;
MTTSSYEEEK LHHTPWVEKY RPKNLNDIAS QEHAVKVLEK QVSTGNLPHM LFYGPPGTGK
TSTILALAKQ LYGPNLYKSR VLELNASDER GISIVRQKIK NFARLTVSNP TPEDLKNYPC
PPYKIIILDE ADSMTNDAQS ALRRTMETYA NITRFALVCN YITRIIDPLA SRCSKFRFKL
LNSENSLNRL KYIANEEHLN LDKSQGEDAV LNEVLRISNG DLRKAITYLQ SASKLSTSLQ
LEDDEDGDGK AGLITKQSIR ETAGVLPDDL IDNLVKTIRS KNEEKLVAVV NDVISSGWSA
QQLIDQLHEV LVMDDSINSL VKNQIALILF DTDKKLNFGT DEHIQLLNLV LQVSKII
//
