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Database: UniProt
Entry: A0A1E5P9U4_9ACTN
LinkDB: A0A1E5P9U4_9ACTN
Original site: A0A1E5P9U4_9ACTN 
ID   A0A1E5P9U4_9ACTN        Unreviewed;       551 AA.
AC   A0A1E5P9U4;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN   ORFNames=AS594_19320 {ECO:0000313|EMBL:OEJ26321.1};
OS   Streptomyces agglomeratus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=285458 {ECO:0000313|EMBL:OEJ26321.1, ECO:0000313|Proteomes:UP000095759};
RN   [1] {ECO:0000313|EMBL:OEJ26321.1, ECO:0000313|Proteomes:UP000095759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=6-3-2 {ECO:0000313|EMBL:OEJ26321.1,
RC   ECO:0000313|Proteomes:UP000095759};
RA   Chen X.;
RT   "Complete genome sequence of Streptomyces agglomeratus strain 6-3-2, a
RT   novel anti-MRSA actinomycete isolated from Wuli of Tebit, China.";
RL   Submitted (AUG-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. 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:OEJ26321.1}.
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DR   EMBL; MEHJ01000001; OEJ26321.1; -; Genomic_DNA.
DR   RefSeq; WP_069928224.1; NZ_MEHN01000001.1.
DR   AlphaFoldDB; A0A1E5P9U4; -.
DR   STRING; 285458.BGM19_17635; -.
DR   OrthoDB; 3713880at2; -.
DR   Proteomes; UP000095759; 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:OEJ26321.1};
KW   Helicase {ECO:0000313|EMBL:OEJ26321.1};
KW   Hydrolase {ECO:0000313|EMBL:OEJ26321.1};
KW   Nucleotide-binding {ECO:0000313|EMBL:OEJ26321.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095759}.
FT   DOMAIN          189..343
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          397..549
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   551 AA;  61121 MW;  38E159F1EB4040F4 CRC64;
     MNGPLIVQSD KTLLLEVDHE LADACRRAIA PFAELERAPE HIHTYRVTPL GLWNARAAGH
     DAEQVVDALV EFSRYPVPHA LLVDVAETMA RYGRLTLSKH PVHGLVLTST DRPVLEEILR
     SKKVQPLVGA RIDADTVAVH PSERGQIKQT LLKLGWPAED LAGYVDGEAH AIDLAEDGWA
     LRPYQKQAVE GFWHGGSGVV VLPCGAGKTL VGAGAMAQAK ATTLILVTNT VSARQWKHEL
     VKRTSLTEDE IGEYSGTRKE IRPVTIATYQ VLTTKRKGIY PHLELFDSRD WGLIVYDEVH
     LLPAPVFKFT ADLQARRRLG LTATLVREDG RESDVFSLIG PKRFDAPWKE IEAQGYIAPA
     DCVEVRVNLT ETERLAYATA ETEEKYRFCA TTATKRKVTE ALVRKFAGQQ ILVIGQYIDQ
     LDELGEHLDA PVIKGETSNA QREKLFEAFR QGEISVLVVS KVANFSIDLP EATVAIQVSG
     TFGSRQEEAQ RLGRVLRPKA DGHQAHFYSV VARDTIDQDF AAHRQRFLAE QGYAYRIVDA
     DELMAEDGTT P
//
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