ID A0A1K2FXH9_9ACTN Unreviewed; 663 AA.
AC A0A1K2FXH9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN Name=recQ_2 {ECO:0000313|EMBL:SFY52260.1};
GN ORFNames=STEPF1_05532 {ECO:0000313|EMBL:SFY52260.1};
OS Streptomyces sp. F-1.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=463642 {ECO:0000313|EMBL:SFY52260.1, ECO:0000313|Proteomes:UP000095403};
RN [1] {ECO:0000313|EMBL:SFY52260.1, ECO:0000313|Proteomes:UP000095403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Streptomyces sp. F1 {ECO:0000313|EMBL:SFY52260.1};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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}.
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DR EMBL; FKJI03000021; SFY52260.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1K2FXH9; -.
DR OrthoDB; 9760034at2; -.
DR Proteomes; UP000095403; 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:0016887; F:ATP hydrolysis activity; IEA:RHEA.
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 GO; GO:0009432; P:SOS response; IEA:InterPro.
DR CDD; cd17920; DEXHc_RecQ; 1.
DR CDD; cd18794; SF2_C_RecQ; 1.
DR Gene3D; 1.10.150.80; HRDC domain; 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; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR InterPro; IPR006293; DNA_helicase_ATP-dep_RecQ_bac.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR010997; HRDC-like_sf.
DR InterPro; IPR002121; HRDC_dom.
DR InterPro; IPR044876; HRDC_dom_sf.
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; TIGR01389; recQ; 1.
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; PF00570; HRDC; 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; SM00341; HRDC; 1.
DR SMART; SM00956; RQC; 1.
DR SUPFAM; SSF47819; HRDC-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50967; HRDC; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:SFY52260.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:SFY52260.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000095403}.
FT DOMAIN 45..213
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 234..388
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 558..638
FT /note="HRDC"
FT /evidence="ECO:0000259|PROSITE:PS50967"
FT REGION 521..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..536
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..663
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 663 AA; 71961 MW; D6DF4184806AC50E CRC64;
MEATGGISEM PTVTEELGAA GSEVLATLNR VFGYEAFRGQ QEAIIEHVVA GGDALVLMPT
GGGKSLCYQI PALVRPGTGV VVSPLIALMQ DQVDALRALG VRAGFVNSTQ DFDERRTVEA
EFLAGELDLL YLAPERLRLD STLDLLSRGK ISVFAIDEAH CVSQWGHDFR PDYLSLSLLG
ERWPDVPRIA LTATATRATH EEITQRLNMP AARHFVASFD RPNIQYRIVP KADPRKQLLA
FLREEHQGDA GIVYCLSRNS VERTAEFLTA NGIEAVPYHA GLDAGTRAAH QSRFLREDGL
VVVATIAFGM GIDKPDVRFV AHLDLPKSIE GYYQETGRAG RDGLPSTAWM AYGLNDVVQQ
RKLIQSGDGD EAFRRRAAAH LDAMLALCET ARCRRGQLLA YFGQEPDATG CGNCDTCLTP
PETWDGTVAA QKVLSTVVRL QRERGQKFGA LQIVDILLGK RTAKVIQFDH DQLSVFGIGK
DLEEGEWRGA IRQLLAQGLL AVEGEYGTLV LTEASGSVLR GEREVPLRKE PKRPAASRSR
PAGGSGGGKA KAVAAELPEE LLPAFEALRA WRTGQAREQG VPPYIIFNDA TLRAIVSLMP
RSIRELATVS GVGEKKLVTY GEEVLSVLAS LDGPAAPAAA PVPEEAPADD DWPAPEDEPD
FWE
//
