ID A0A1R1YBU7_9FUNG Unreviewed; 1010 AA.
AC A0A1R1YBU7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=ATP-dependent DNA helicase hus2/rqh1 {ECO:0000313|EMBL:OMJ24350.1};
GN ORFNames=AYI70_g1649 {ECO:0000313|EMBL:OMJ24350.1};
OS Smittium culicis.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX NCBI_TaxID=133412 {ECO:0000313|EMBL:OMJ24350.1, ECO:0000313|Proteomes:UP000187283};
RN [1] {ECO:0000313|EMBL:OMJ24350.1, ECO:0000313|Proteomes:UP000187283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GSMNP {ECO:0000313|EMBL:OMJ24350.1,
RC ECO:0000313|Proteomes:UP000187283};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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=3.6.4.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001665};
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000256|ARBA:ARBA00005446}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OMJ24350.1}.
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DR EMBL; LSSN01000360; OMJ24350.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R1YBU7; -.
DR STRING; 133412.A0A1R1YBU7; -.
DR Proteomes; UP000187283; Unassembled WGS sequence.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd17920; DEXHc_RecQ; 1.
DR CDD; cd18794; SF2_C_RecQ; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032284; RecQ_Zn-bd.
DR InterPro; IPR018982; RQC_domain.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR NCBIfam; TIGR00614; recQ_fam; 1.
DR PANTHER; PTHR13710:SF105; BLOOM SYNDROME PROTEIN; 1.
DR PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF16124; RecQ_Zn_bind; 1.
DR Pfam; PF09382; RQC; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00956; RQC; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:OMJ24350.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000187283}.
FT DOMAIN 424..603
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 621..774
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 106..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 937..1010
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 269..325
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 106..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..148
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 937..951
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..1010
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1010 AA; 114981 MW; 1144290C33E97D71 CRC64;
MATSEIVILD EIESSNPKIE NVKSEYILGF KTPRLTKKQL IDSIESDDDF MSFKTLSSSK
KTDLSTKKSK NYFEKVYDNI NDEIEEIDYF SDSLIEEVIS NSELKIKNSI PSPPSSKGVK
SMVKSSEPPK FNNERKAKKE TPQSSKVKKE FIDLEEDSEY LSPIDLIDDM NCTDLSKTLH
NSSDKLEYTI DKIENDMAFI EQVPDRDVEI IVKEDNLNVD EVNTFDVSEF DDLEFLENNF
NFDDIDLDEE ATITNSETTE NVYLESYREK DLELKLESLL MRKARISDEI CDIELSNSSS
ANLKIEKLKE ERIKVLGQIE SLKKLQKTRK NQPQSSKRSS MELIHIDDDI LSTVESSFST
RSYQSAFSES KDDLPLSSRT INQPPKPAPP KRIEFKHKWS REVAKALHQI FKMSEFRPKQ
LDAIDATLSG KNVFVLMPTG GGKSLCYQLP AVIQTGNTRG VTVVISPLLA LMQDQVNHLV
AWGIPSIALT GDLNAAQRNF AFDEISKRDP RLRLLYVTPE MLSKSDKMRE AIDSLYNRKL
LARFVVDEAH CVSQWGHDFR PDYVLIGNYK RQYPGIPFMA LTATANMRVQ SDIISNLNIK
GCLTLSSSFN RPNLFYEIRK KSNDVISEIS SFVLSRYHGK SGIIYCRSKA NCEKVTEMLQ
TKSGISAGYY HAGLAKEDRQ RIQLDWQENR ISIIVATVAF GMGIDKPDVR FVIHHTFPDS
IESYYQETGR AGRDGKPSTC VLFYSYRDKR TIEKFIEEGE GNKFHKERQT ENLNRVIQFC
ENRTECRRKL VLSYFGENFD SNLCVKSCDN CLAKENRVVN LVDYTELSSN MIKLAKRILS
TGRKVTLLYI VDVSRGSRAK KILEIGDNNL DLFGFCKNYK KDDLVELLRL LVTKKAFTEI
TETNFRGNLV TYLSLGPNST KFENMLERIT IEVASSMPSV EASQNESSGR DPALNRNDKN
EILHGSTISK LQGFGFSDNS SFSEPSISEK ATNKKSAYFS NDSDKGNPDF
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