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Database: UniProt
Entry: A5E7K0_LODEL
LinkDB: A5E7K0_LODEL
Original site: A5E7K0_LODEL 
ID   A5E7K0_LODEL            Unreviewed;       402 AA.
AC   A5E7K0;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   SubName: Full=Activator 1 41 kDa subunit {ECO:0000313|EMBL:EDK47408.1};
GN   ORFNames=LELG_05589 {ECO:0000313|EMBL:EDK47408.1};
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:EDK47408.1, ECO:0000313|Proteomes:UP000001996};
RN   [1] {ECO:0000313|EMBL:EDK47408.1, 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).
CC   -!- SIMILARITY: Belongs to the activator 1 small subunits family.
CC       {ECO:0000256|ARBA:ARBA00005378}.
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DR   EMBL; CH981533; EDK47408.1; -; Genomic_DNA.
DR   RefSeq; XP_001523363.1; XM_001523313.1.
DR   AlphaFoldDB; A5E7K0; -.
DR   STRING; 379508.A5E7K0; -.
DR   GeneID; 5230311; -.
DR   KEGG; lel:LELG_05589; -.
DR   VEuPathDB; FungiDB:LELG_05589; -.
DR   eggNOG; KOG0989; Eukaryota.
DR   HOGENOM; CLU_042324_1_0_1; -.
DR   InParanoid; A5E7K0; -.
DR   OMA; AHSTRFC; -.
DR   OrthoDB; 275853at2759; -.
DR   Proteomes; UP000001996; Unassembled WGS sequence.
DR   GO; GO:0031391; C:Elg1 RFC-like complex; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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   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:UP000001996}.
FT   DOMAIN          67..205
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          266..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        267..298
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   402 AA;  44920 MW;  1497B4E7B531A925 CRC64;
     MATTAAAATA AATATATAAT TTDRSKYDED KLHHTPWVEK YRPKNLDDVA SQDHAVKVLK
     KQISTGNLPH MLFYGPPGTG KTSTILALAK QLYGPNLYKS RVLELNASDE RGISIVRQKI
     KNFAKLTVSN PTEDDLRNYP CPPYKIIILD EADSMTNDAQ SALRRTMETY ANITRFALVC
     NYITRIIDPL ASRCSKFRFK LLNNENSLNR LKYIAKEENL HLDEKGAPDE VLNEVLRISN
     GDMRKAITYL QSASKLSSSL QLENCKNDMN EDNKGESTPS SRKGDEKDDE EEEKDKGLIT
     KASIRETAGI LPDTLILQMV ESIKQKNEGI LINLVNDIIS SGWSVQQLID QLHDQLVWDD
     TIDSLKKNQI ALTLFDTDKK LNLGTDEHIQ LLNLVLQVSG IV
//
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