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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//