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Database: UniProt
Entry: A0A269WBF2_9BACL
LinkDB: A0A269WBF2_9BACL
Original site: A0A269WBF2_9BACL 
ID   A0A269WBF2_9BACL        Unreviewed;       637 AA.
AC   A0A269WBF2;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN   ORFNames=CHH75_04410 {ECO:0000313|EMBL:PAK55484.1};
OS   Paenibacillus sp. 7541.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=2026236 {ECO:0000313|EMBL:PAK55484.1, ECO:0000313|Proteomes:UP000215741};
RN   [1] {ECO:0000313|EMBL:PAK55484.1, ECO:0000313|Proteomes:UP000215741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7541 {ECO:0000313|EMBL:PAK55484.1,
RC   ECO:0000313|Proteomes:UP000215741};
RA   Kalinowski J., Ahrens B., Al-Dilaimi A., Winkler A., Wibberg D.,
RA   Schleenbecker U., Ruckert C., Wolfel R., Grass G.;
RT   "Isolation and whole genome analysis of endospore-forming bacteria from
RT   heroin.";
RL   Submitted (AUG-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. 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:PAK55484.1}.
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DR   EMBL; NQLZ01000005; PAK55484.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A269WBF2; -.
DR   Proteomes; UP000215741; 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; 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; 1.
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:PAK55484.1};
KW   Helicase {ECO:0000313|EMBL:PAK55484.1};
KW   Hydrolase {ECO:0000313|EMBL:PAK55484.1};
KW   Nucleotide-binding {ECO:0000313|EMBL:PAK55484.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215741}.
FT   DOMAIN          259..415
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          466..618
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          176..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..195
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        196..221
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   637 AA;  70754 MW;  14F141C764F3C040 CRC64;
     MEQKPCIVQR DRTVLLETAH PSFQKARAEL AQYADLVKSP AAYHTYRITP LSLWNAAAAG
     LTADHICISL RSLSRWELPA ALEEDIRRLV ARYGQLTLKM HPARDGRLLL QSRSASVLAE
     LKGYPSLASS GLVILSELEA EAPSRLRGLL KQELTRLGYP VLDHVGYQDG QFLPLDWRDG
     DRSASGQREP ERQEPLSEQT GTPRAISAAA SAQSSGQKGR SAEQEGAERV DGIPAGSVAA
     PKGSFRLRDY QRAAVDAFKE SGGEGGSGVL VLPCGAGKTI IGLAAMRELQ CETLILTSNA
     TSVTQWISEL LDKTTLLPEQ IGEYTAEHKA VRPVTVATYQ ILTHRHRKEE EQFHMKLFNE
     RRWGLIIYDE VHLLPAPVFR ATADIQATRR LGLTATLVRE DGREADVFSL IGPKRYEMPW
     KALEEQGWIA AVRCIEVKVP LPGPIKERCR YSGKREQYRL AAENPAKLEL IKALVRRHPG
     AQILIIGQYL NQLTAIAEQL QVPLISGQMP QQRRHELYAS FRRGETPVLV VSKVANFAVD
     LPDASVAIEV SGTFGSRQEE AQRLGRILRP KSGENRAYFY TLVSSDSREE MFAMRRQLFL
     VEQGYVYEAM SIPLAEEQGR KPGQIGAAAE REVSGQR
//
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