ID A5DTY3_LODEL Unreviewed; 741 AA.
AC A5DTY3;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=LELG_00819 {ECO:0000313|EMBL:EDK42641.1};
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:EDK42641.1, ECO:0000313|Proteomes:UP000001996};
RN [1] {ECO:0000313|EMBL:EDK42641.1, 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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000256|ARBA:ARBA00000600};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000256|ARBA:ARBA00000600};
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family.
CC {ECO:0000256|ARBA:ARBA00007913}.
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DR EMBL; CH981524; EDK42641.1; -; Genomic_DNA.
DR RefSeq; XP_001528299.1; XM_001528249.1.
DR AlphaFoldDB; A5DTY3; -.
DR STRING; 379508.A5DTY3; -.
DR GeneID; 5235978; -.
DR KEGG; lel:LELG_00819; -.
DR VEuPathDB; FungiDB:LELG_00819; -.
DR eggNOG; KOG1803; Eukaryota.
DR HOGENOM; CLU_001666_8_2_1; -.
DR InParanoid; A5DTY3; -.
DR OMA; TIIHGPP; -.
DR OrthoDB; 170190at2759; -.
DR Proteomes; UP000001996; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR Gene3D; 2.40.30.270; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR047187; SF1_C_Upf1.
DR InterPro; IPR048761; SMUBP-2_HCS1_1B.
DR PANTHER; PTHR43788:SF19; DNA-BINDING PROTEIN SMUBP-2; 1.
DR PANTHER; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 1.
DR Pfam; PF13086; AAA_11; 1.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF21138; SMUBP-2_HCS1_1B; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022806};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000001996}.
FT DOMAIN 244..504
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|SMART:SM00487"
FT DOMAIN 262..512
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 94..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 741 AA; 82838 MW; 8245BAA8CE6D7757 CRC64;
MNDLFDKFRD AIIKEQEEDV ATTSSYINAY SPKKLAQLGL AIINLNIVNI RTGIGGKTIL
ELQLDNAVSD GELSTSTMKT GDIVRISRMA KSEKSIKKGA TRSKGDKFKK GGDGGDSKSN
NDSKKRKSNN DCVNNEDSDD SNNAGESLEA VVAKVSTLTI TVSVDESTSD DKVLNYYNNT
NDPLARLWIV KLANSVTYKR MISTVNKVKE LKDNEKNDIH RLLLGETKYI AKDNGTLGAK
MEFHNPGLND SQKRAIDFAI NKSNISIIFG PPGTGKTMTI IELIRQLTDC GEKVLVCGPS
NISVDTILER LGDKYKAGDL IRIGHPARLL PVNLQHSLDV ISKSYGRDVI SDVENDIQTT
LGKIKKTKRY AERKVLYQEL KLLKKELIQR ERKVVQELLQ NAKVILATLH GAGSYELKRS
NIKFDTIIID EVSQSLEPQC WIPLLINDNF KRLVIAGDNM QLPPTIMLSG SNSSRSKNKN
QDKSNDCSNK TSILETTLFD RLVKKLDGEK FKTLLDVQYR MNDSIMKFPS MQLYKDKLKS
ADLVKDISLL DLSGVQKNDD TVLQCIWYDT QGGEFPEQIL ESVKGGDSKY NEMELLIVKA
HIKKLLKSGV QPTDIGVIAP YAAQVLLLKK QFGPDSQIEI STVDGFQGRE KEVIILTLVR
SNDDNEVGFL SEERRLNVAI TRPKRQLCVI GDLLLMSQSG HKFLKDWSKY VEDGYEDGQF
VKPYEIVYPN LNEYLEASEG A
//
