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Database: UniProt
Entry: A0A069K4B7_9ACTN
LinkDB: A0A069K4B7_9ACTN
Original site: A0A069K4B7_9ACTN 
ID   A0A069K4B7_9ACTN        Unreviewed;       551 AA.
AC   A0A069K4B7;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN   ORFNames=DT87_16545 {ECO:0000313|EMBL:KDQ68737.1};
OS   Streptomyces sp. NTK 937.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1487711 {ECO:0000313|EMBL:KDQ68737.1, ECO:0000313|Proteomes:UP000027475};
RN   [1] {ECO:0000313|EMBL:KDQ68737.1, ECO:0000313|Proteomes:UP000027475}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NTK 937 {ECO:0000313|EMBL:KDQ68737.1,
RC   ECO:0000313|Proteomes:UP000027475};
RA   Olano C., Cano-Prieto C., Losada A., Mendez C., Salas J.A.;
RT   "Draft genome sequence of marine actinomycete Streptomyces sp. NTK 937,
RT   producer of the benzoxazol antibiotic caboxamycin.";
RL   Submitted (APR-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=3.6.4.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00001665};
CC   -!- SIMILARITY: Belongs to the helicase family. RAD25/XPB subfamily.
CC       {ECO:0000256|ARBA:ARBA00006637}.
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:KDQ68737.1}.
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DR   EMBL; JJOB01000001; KDQ68737.1; -; Genomic_DNA.
DR   RefSeq; WP_030624828.1; NZ_JJOB01000001.1.
DR   AlphaFoldDB; A0A069K4B7; -.
DR   OrthoDB; 3713880at2; -.
DR   Proteomes; UP000027475; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   CDD; cd18029; DEXHc_XPB; 1.
DR   CDD; cd18789; SF2_C_XPB; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR032438; ERCC3_RAD25_C.
DR   InterPro; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR032830; XPB/Ssl2_N.
DR   PANTHER; PTHR11274:SF0; GENERAL TRANSCRIPTION AND DNA REPAIR FACTOR IIH HELICASE SUBUNIT XPB; 1.
DR   PANTHER; PTHR11274; RAD25/XP-B DNA REPAIR HELICASE; 1.
DR   Pfam; PF16203; ERCC3_RAD25_C; 1.
DR   Pfam; PF13625; Helicase_C_3; 1.
DR   Pfam; PF04851; ResIII; 1.
DR   PRINTS; PR00851; XRODRMPGMNTB.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000313|EMBL:KDQ68737.1};
KW   Helicase {ECO:0000313|EMBL:KDQ68737.1};
KW   Hydrolase {ECO:0000313|EMBL:KDQ68737.1};
KW   Nucleotide-binding {ECO:0000313|EMBL:KDQ68737.1}.
FT   DOMAIN          189..343
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          397..545
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   551 AA;  61369 MW;  235F8D4EF5CC0DA0 CRC64;
     MTGPLIVQSD KTLLLEVDHD QAEACRRAIA PFAELERAPE HIHTYRVTPL GLWNARAAGH
     DAEQVVDALV EYSRYPVPHA LLVDIAETMA RYGRLTLSKH PVHGLVLTTN DRPVLEEILR
     SKKVQPLVGA RLDPDTVAVH PSERGQIKQT LLKLGWPAED LAGYVDGEAH PIELAQDGWS
     LRPYQRQAVD GFWHGGSGVV VLPCGAGKTL VGAGAMAEAK ATTLILVTNT VSARQWKHEL
     VKRTSLTEDE IGEYSGTRKE IRPVTIATYQ VLTTRRKGVY PHLELFDSRD WGLVIYDEVH
     LLPAPVFKFT ADLQARRRLG LTATLVREDG RESDVFSLIG PKRFDAPWKE IEAQGYIAPA
     DCVEVRVNLT DSERLAYATA ETEEKYRFCA TTATKRKVTE ALVRKHRGEQ TLVIGQYIDQ
     LDELGEHLDA PVIKGETSNA QREKLFEAFR QGEISVLVVS KVANFSIDLP EATVAIQVSG
     TFGSRQEEAQ RLGRVLRPKA DGHEARFYSV VARDTVDQDF AAHRQRFLAE QGYAYRIVDA
     DELLAEPDPE S
//
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