ID A5DV61_LODEL Unreviewed; 362 AA.
AC A5DV61;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Activator 1 40 kDa subunit {ECO:0000313|EMBL:EDK43069.1};
GN ORFNames=LELG_01247 {ECO:0000313|EMBL:EDK43069.1};
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508 {ECO:0000313|EMBL:EDK43069.1, ECO:0000313|Proteomes:UP000001996};
RN [1] {ECO:0000313|EMBL:EDK43069.1, ECO:0000313|Proteomes:UP000001996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 /
RC NRRL YB-4239 {ECO:0000313|Proteomes:UP000001996};
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).
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DR EMBL; CH981524; EDK43069.1; -; Genomic_DNA.
DR RefSeq; XP_001528727.1; XM_001528677.1.
DR AlphaFoldDB; A5DV61; -.
DR STRING; 379508.A5DV61; -.
DR GeneID; 5235788; -.
DR KEGG; lel:LELG_01247; -.
DR VEuPathDB; FungiDB:LELG_01247; -.
DR eggNOG; KOG2035; Eukaryota.
DR HOGENOM; CLU_042324_5_0_1; -.
DR InParanoid; A5DV61; -.
DR OMA; LMCEACK; -.
DR OrthoDB; 868at2759; -.
DR Proteomes; UP000001996; Unassembled WGS sequence.
DR GO; GO:0031391; C:Elg1 RFC-like complex; IEA:UniProt.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0090618; P:DNA clamp unloading; IEA:UniProt.
DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IEA:UniProt.
DR CDD; cd00009; AAA; 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; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11669; REPLICATION FACTOR C / DNA POLYMERASE III GAMMA-TAU SUBUNIT; 1.
DR PANTHER; PTHR11669:SF1; REPLICATION FACTOR C SUBUNIT 3; 1.
DR Pfam; PF13177; DNA_pol3_delta2; 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 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001996}.
FT DOMAIN 34..190
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 362 AA; 40615 MW; 53750D842290EFDA CRC64;
MSLWVDKYRP KTLAQLSYHK DITQNLQALS KSGDFPHLLV YGPSGAGKKT RIYATLHAIF
GVSVEKLKID VKTFTTPSNR KLEFNVLSSP HHLEITPSDM GNNDRVVIQD LLKDVASTEQ
VDFGNQSSKR HRFKVVIINE ADSLSRDAQA ALRRTMEKYS SNIRLILVCN SISNIIAPIK
SRTLLVRIPS PSVAEISLIL HDVAQEEKVK FSSTDQQALT GFYEQVATVS NRNLRRALLA
FETICMQNET INVKQMHSVI VLDWELIIRN MAKSISTTRN VANLAKLRTA TYELLSHCIP
ARTILKGLLF ELIKLEKGKT KLIAEIVKIA SIFDERLSLG TKSIFHIEGF IAKSMVAIDD
LS
//
