ID W1SIC1_9BACI Unreviewed; 1069 AA.
AC W1SIC1;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=BAVI_10306 {ECO:0000313|EMBL:ETI69141.1};
OS Neobacillus vireti LMG 21834.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX NCBI_TaxID=1131730 {ECO:0000313|EMBL:ETI69141.1, ECO:0000313|Proteomes:UP000018877};
RN [1] {ECO:0000313|EMBL:ETI69141.1, ECO:0000313|Proteomes:UP000018877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21834 {ECO:0000313|EMBL:ETI69141.1,
RC ECO:0000313|Proteomes:UP000018877};
RX PubMed=24708037; DOI=10.1111/1462-2920.12478;
RA Mania D., Heylen K., van Spanning R.J., Frostegard A.;
RT "The nitrate-ammonifying and nosZ-carrying bacterium Bacillus vireti is a
RT potent source and sink for nitric and nitrous oxide under high nitrate
RT conditions.";
RL Environ. Microbiol. 16:3196-3210(2014).
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=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034618};
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:ETI69141.1}.
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DR EMBL; ALAN01000059; ETI69141.1; -; Genomic_DNA.
DR RefSeq; WP_024028255.1; NZ_ALAN01000059.1.
DR AlphaFoldDB; W1SIC1; -.
DR STRING; 220686.AA980_20280; -.
DR PATRIC; fig|1131730.3.peg.2151; -.
DR eggNOG; COG1074; Bacteria.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000018877; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR038726; PDDEXK_AddAB-type.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF23; RECBCD ENZYME SUBUNIT RECB; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF52980; Restriction endonuclease-like; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000018877}.
FT DOMAIN 5..437
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 449..725
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 26..33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1069 AA; 122494 MW; C8BAA66EE1149B28 CRC64;
MTKVIQDQAA RDKITSRLGT NFLVEAGAGS GKTTSLVERM VNLIHTGTAE IQEIVAITFT
RKAADELKLR FQAKLEEAWK KETDLDANYR LGDALQNMER CFLGTVHSFC AKLLRERPIE
AHLDLTFKEL EEADDLDILA EAWQLYLQEL MDQDSHHFRE IAELGINVDD IFPWLKELKE
YSDVAWEADT VSKPELHKDY EYFMMLIQEA KKFVPDTEPL KGYDALQKAV VTACQKTRFI
DSLQDKDIIG IFSLFAKNLK PTYNRWPSKE DAQYYEEKIT AAFEENIKPL IQAWKEFCHP
KIVSFLIGAV QSYEELKKER SLLNFQDLMM HTSKLLKENR EVRSYFQGKY RFLLVDEFQD
TDPLQAEIMF YLTSEDSEEK NWTSCKPKPG SLFVVGDPKQ AIYRFRRADI DTYNRVKQLL
EEHGGEVLQL TTNFRTLDTV TKPLNTVFEQ QLPVVETVYQ AAYRPLISYH EDEGIGFSGV
KLLSVPADVK KKEEIILKDA ESIALTIHNL MKQGYRAKDF MVLTRYNDGV ATYAKLIEDI
GIPVSISGEV ILGETREFQD LWILLKSFLD PTDEVAFVAV LRGIFFGISD EELYQWKHAK
GRFSVYADIP DGLSSDVKAK FALTLSKLQH CQKQIRTLSP TVAIEKISEE IGFYPLLLKN
VRGKRMYKSL LQVIEALRKQ ETSGNTIYKQ VVETLTEMIF EKTVVANLEE EADAVRIMNV
HKAKGLEAPI VFLAHPAKAV SPESFLSKHI RREDLSSKGF FTFTVDTGYQ SKEMAIPLHW
AAHKAEELMY LSEEELRIIY VASTRAEKAL IISANGGNKK NPWNILFEMN TIEELEIPVG
DAFERKIPQG EITLNEFQSK TIGKHEWIDA SSEKSYDLWT PTKDKDYSEI TIERESGGGK
DWGTLIHDVF EKAVQGNDLT HYLKTALNKF NLPAAREAEV ETYLQNLKKS QLWDHLQTAD
EVLTEVPFTL KVEKGHKLYT LITKNPEDKH PFLVKGTIDL IYKRNGSWTI VDYKTDRAKH
EEDYIKLHAF YSSQLAFYKG AWEAVTGEKV SGGLLYFLLP DRLTAVAGS
//
