ID J7SB42_NAUDC Unreviewed; 1191 AA.
AC J7SB42;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN Name=NDAI0G05500 {ECO:0000313|EMBL:CCK73533.1};
GN OrderedLocusNames=NDAI_0G05500 {ECO:0000313|EMBL:CCK73533.1};
OS Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 / NBRC
OS 0211 / NRRL Y-12639) (Saccharomyces dairenensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCK73533.1, ECO:0000313|Proteomes:UP000000689};
RN [1] {ECO:0000313|EMBL:CCK73533.1, ECO:0000313|Proteomes:UP000000689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639
RC {ECO:0000313|Proteomes:UP000000689};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC translocating in the 3'-5' direction.; EC=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034617};
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000256|ARBA:ARBA00009922}.
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DR EMBL; HE580273; CCK73533.1; -; Genomic_DNA.
DR RefSeq; XP_003980209.1; XM_003980160.1.
DR AlphaFoldDB; J7SB42; -.
DR STRING; 1071378.J7SB42; -.
DR GeneID; 13927003; -.
DR KEGG; ndi:NDAI_0G05500; -.
DR eggNOG; KOG2108; Eukaryota.
DR HOGENOM; CLU_004585_4_0_1; -.
DR OMA; FFVAQTR; -.
DR OrthoDB; 208346at2759; -.
DR Proteomes; UP000000689; Chromosome 7.
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 CDD; cd18807; SF1_C_UvrD; 1.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 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}; Reference proteome {ECO:0000313|Proteomes:UP000000689}.
FT DOMAIN 36..341
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 342..685
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 651..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 882..924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 938..1040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1060..1098
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..726
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..924
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..972
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..1016
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1073..1088
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 57..64
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1191 AA; 135532 MW; 945FF72C5837BF8D CRC64;
MADNELIDTV QASHNNNTKD KINKNDSVTL KKILSGLNKQ QKLAVTFDYH NALQVIAGPG
TGKTKVLTSR VAYLLLKERI NPEDIIITTF TNKASMEMID RLSIMLRDTN ISTSNLLIGT
FHSVCIKILH RFGSKIDLSP TWRIADQNEI DNILSNIVDR MPDQIRDYAN SMTRKVNLCM
PKRGRGESDE WTVSPKLVKK QISKLKSSAI LPEEYINDSM HDTALAYFYE NFQSELAKIN
ALDFDDILMY TFRLLTKERC LPNIQHVLVD EFQDTNEIQM DLVFLFAKGN HHLSRGISVV
GDPDQSIYAF RNALAYNFQT MVQKSPIECS RIVLVENYRS SQKILDTSEM LISQQTRGRQ
NRLPLRAQFD YDFPPVYINF PASFLEASSI IKELLYLKAL PDLFSFNDFA ILVRKRIQIK
PLERALIEHR VPYKILRGHA FWDSKEIIAM LNLLKCIFSP NEKNAIIASL LYPSRGLGQT
SADKIKFIFE QETNSNFNST SSMQILRDIV ANKIQIDIPT KARNVIIDFL QMINTCTSLF
NVEPINVALS DIFEKLYELS GLRYEYLCLD GKKKKSIDMS KLEENFDNVR HKNVTILKTY
FLGPTNGPST SSTDTNTMTN IGSISSASVL EHIRNFFNSL TLYTSDLPEI SSSDEQQENM
NWQKVEERKK TQEGVTISTI HGAKGLEWPV VFIPGCNEGT IPSIFNDEAK DGSSDDEGDD
DDDRNEIDTD SKTSKKRRNL SMEELIDEER RMFFVAQTRA KYLLYLSSFI TERQFENEPS
RFLTSDLVKT MVDEQKVLEK VENVMRLYHA MKREPLVASN KKFSLKTLIK DYSNFIENRR
ERMIWGGEVV HDISNLNLIE NVSVQPQPSL VFTTAATQLR VQQQGTKTNQ HPPPPSISHH
PFNQRNNSQK TGPSKNYAPN GSLESDLLVS PTKVLAPLQT MSPSNSPSNV TKSFAPSYVP
KRNKSRSTSP IRKPFPSPER KKILSPTKSL KEEDKELALK STSKKSSSRN SEKSKRTLSS
SKYWANGNKI KQENDDDDDR MIFKKAPVNN PFQNTKVKFE SNGRISKSND SNGIIRLKRE
DDDKTADYDS SNNSNTTAAE LLHNPDDMII DNRPILTNAK TLADAIRKPR NRAENIKKEK
KSEEQVDSEN KGKKMIGLKK GVTASQMDIF SQLSRAKKKT KGNTGEIIII D
//
