ID B9WN68_CANDC Unreviewed; 637 AA.
AC B9WN68;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN OrderedLocusNames=Cd36_35510 {ECO:0000313|CGD:CAL0000171913};
GN ORFNames=CD36_35510 {ECO:0000313|EMBL:CAX40535.1};
OS Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS NRRL Y-17841) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=573826 {ECO:0000313|EMBL:CAX40535.1, ECO:0000313|Proteomes:UP000002605};
RN [1] {ECO:0000313|EMBL:CAX40535.1, ECO:0000313|Proteomes:UP000002605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841
RC {ECO:0000313|Proteomes:UP000002605};
RX PubMed=19745113; DOI=10.1101/gr.097501.109;
RA Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT Candida albicans.";
RL Genome Res. 19:2231-2244(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=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034618};
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000256|ARBA:ARBA00009922}.
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DR EMBL; FM992695; CAX40535.1; -; Genomic_DNA.
DR RefSeq; XP_002422527.1; XM_002422482.1.
DR AlphaFoldDB; B9WN68; -.
DR GeneID; 8049652; -.
DR KEGG; cdu:CD36_35510; -.
DR CGD; CAL0000171913; Cd36_35510.
DR VEuPathDB; FungiDB:CD36_35510; -.
DR eggNOG; KOG2108; Eukaryota.
DR HOGENOM; CLU_004585_7_0_1; -.
DR OrthoDB; 1981871at2759; -.
DR Proteomes; UP000002605; Chromosome R.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF46; ATP-DEPENDENT DNA HELICASE HMI1, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}.
FT DOMAIN 4..271
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 266..548
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 25..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 637 AA; 72034 MW; F582B25010EDFAA6 CRC64;
MELTPTQLKI VNHHYNPKSV LSIQAGPGTG KTFALVKRIQ KLIADGVSPQ SIVVLSLTNR
TVNSLRSALA EYIGSQPGDV VIKTFHSFAH DLIESNLQEY FPEKGRQMLL DDISFQNYRA
LFMSGKGVKQ LHLEKAMSEV RDGKDIADVA EKYEIVQSDL CDTIKFFNDN GMIRYSDFIR
NAIGLLDISK GEIVKDIQVL MVDEFQDMQP QLVTFIEKLV EFGDKHITLA GDSNQCIYEF
LGSSPDITEN FISKLGWETE EICLNESFRL SPQNLDISNV VIDQNKLVSM KEPSAGPTVY
SLVSKYDEYN YIGSEIARLI CQSGGLLKFS DFMILASQNR EVDSISKFMT DHFGYNVNKY
SSNSDWVNSN VHILIDILSV LNKGTGSDLA LLCTLMKLGN SKSLVRDLYL SYRSTQSPGL
EDYLKSESAT CKFNTKPRFK FKERIDLFLN VIQQERKNLD DPVSIMASLA RIIKETGIIA
QLNKPARGHK DQENETKLLN NLSSFYESLS LSYKKTPSLD YFLNNYLEDE PVLEEHSINV
STVHKAKGLE FPVVFVTNFP GYYRSVNARL LYVALTRAKN LLYTGYQGNT FQAYSSSRGF
EMNRAWISST ARDLQRNNPS KHLLNAGMRI LKTSRLI
//
