ID W6MUQ4_9ASCO Unreviewed; 820 AA.
AC W6MUQ4;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=KUCA_T00001800001 {ECO:0000313|EMBL:CDK25830.1};
OS Kuraishia capsulata CBS 1993.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetales incertae sedis; Kuraishia.
OX NCBI_TaxID=1382522 {ECO:0000313|EMBL:CDK25830.1};
RN [1] {ECO:0000313|EMBL:CDK25830.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK25830.1};
RA Genoscope - CEA;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDK25830.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK25830.1};
RA Morales L., Noel B., Porcel B., Marcet-Houben M., Hullo M-F., Sacerdot C.,
RA Tekaia F., Leh-Louis V., Despons L., Khanna V., Aury J-M., Barbe V.,
RA Couloux A., Labadie K., Pelletier E., Souciet J-L., Boekhout T.,
RA Gabaldon T., Wincker P., Dujon B.;
RT "Complete DNA sequence of /Kuraishia capsulata/ illustrates novel genomic
RT features among budding yeasts (/Saccharomycotina/).";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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; HG793126; CDK25830.1; -; Genomic_DNA.
DR AlphaFoldDB; W6MUQ4; -.
DR STRING; 1382522.W6MUQ4; -.
DR HOGENOM; CLU_004585_4_0_1; -.
DR OrthoDB; 208346at2759; -.
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: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}.
FT DOMAIN 11..287
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 288..591
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 751..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 820 AA; 91693 MW; A14C610BCAA52E04 CRC64;
MKPNLLDLFI GLNEAQLTAV TADPSRPIQI VAGPGTGKTR VLTSRVAFLI LEKKIPPSKI
IVTTFTKKAA NEMVERLTAM LSPFEVPVSE LFIGTFHSIC IRLLRRYHGK CGLRPDFGVA
DETDTKSVMK HTCPDLGEKE RAKARGYISK LKAQGITPDA YRAIPRHSAE IASVYTMYDS
YLESHGLLDF DDILLYGLRL ARDNGKCLDF VRHVLVDEFQ DTNKVQLDLL FALGDRSTKF
QHNVTVVGDP DQSIYGFRSA DPASFRSMAK RYENLHQVNL NTNYRSTASI LNVSEAIMGH
QTAKRTSKSL RSICSVKIPV VHSKHRTNND EARWISDQIS MLKAMPHLFE YSDVAILLRS
RFLSRVVEQE LMKKKIPYHL VQGQAFWDLK VVRSMLDYLR VVSSDLDVLA FSRTINFPAR
KVGAVSLEKL LSQFQSSVGF NNVGVSDMLI GVIEGTGIKL GSGVVSGLKE YLSLIQQCRE
DISVAENPLD GVLAAFDRIA RTTDLANCVR EEKSKRSKRE LRDDELPEND LEELRNQIRE
FEPAEEILED LKTETEQSFL DSFLESIHFY SAEKEEAQTK VTISTIHAAK GLEWPIVFVP
GLTMGVFPNY NAFKADEDEE FTVPKGDENA IDEEVRCFYV AATRSQRLLM LSSFERRAID
SETSLEVSPL LKGLGKMEPK LDTLDLGIRK LLYEAMTKKF QSVSDEERQL LEAIGGAAIV
GSGITTALYA PMNAPREVSG LSGRFKRKFE GQEGQRNLNR LPHINMERRG ANSEVSISSA
TGHSNSPLQP LVNSPKFAPP RGVTSGTGKK RLGMGRPRMM
//
