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Database: UniProt
Entry: Q634F1_BACCZ
LinkDB: Q634F1_BACCZ
Original site: Q634F1_BACCZ 
ID   Q634F1_BACCZ            Unreviewed;       778 AA.
AC   Q634F1;
DT   25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 98.
DE   RecName: Full=ATP-dependent RecD-like DNA helicase {ECO:0000256|HAMAP-Rule:MF_01488};
DE            EC=3.6.4.12 {ECO:0000256|HAMAP-Rule:MF_01488};
GN   Name=recD {ECO:0000313|EMBL:AAU16134.1};
GN   Synonyms=recD2 {ECO:0000256|HAMAP-Rule:MF_01488};
GN   OrderedLocusNames=BCE33L4137 {ECO:0000313|EMBL:AAU16134.1};
OS   Bacillus cereus (strain ZK / E33L).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=288681 {ECO:0000313|EMBL:AAU16134.1, ECO:0000313|Proteomes:UP000002612};
RN   [1] {ECO:0000313|Proteomes:UP000002612}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZK / E33L {ECO:0000313|Proteomes:UP000002612};
RX   PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006;
RA   Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Brown N.,
RA   Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA   Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA   Green L.D., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA   Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K.,
RA   Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T.,
RA   Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E.,
RA   Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA   Ticknor L.O., Wills P.L., Brettin T.S., Gilna P.;
RT   "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT   thuringiensis isolates closely related to Bacillus anthracis.";
RL   J. Bacteriol. 188:3382-3390(2006).
CC   -!- FUNCTION: DNA-dependent ATPase and ATP-dependent 5'-3' DNA helicase.
CC       Has no activity on blunt DNA or DNA with 3'-overhangs, requires at
CC       least 10 bases of 5'-ssDNA for helicase activity. {ECO:0000256|HAMAP-
CC       Rule:MF_01488}.
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|HAMAP-Rule:MF_01488};
CC   -!- SIMILARITY: Belongs to the RecD family. RecD-like subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01488}.
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DR   EMBL; CP000001; AAU16134.1; -; Genomic_DNA.
DR   RefSeq; WP_000528067.1; NZ_CP009968.1.
DR   AlphaFoldDB; Q634F1; -.
DR   KEGG; bcz:BCE33L4137; -.
DR   PATRIC; fig|288681.22.peg.1246; -.
DR   Proteomes; UP000002612; Chromosome.
DR   GO; GO:0043139; F:5'-3' DNA helicase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   CDD; cd17933; DEXSc_RecD-like; 1.
DR   CDD; cd18809; SF1_C_RecD; 1.
DR   Gene3D; 1.10.10.2220; -; 1.
DR   Gene3D; 2.30.30.940; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   HAMAP; MF_01488; RecD_like; 1.
DR   InterPro; IPR006345; DNA_helicase_RecD-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR029493; RecD-like_HHH.
DR   InterPro; IPR041451; RecD-like_SH13.
DR   InterPro; IPR027785; UvrD-like_helicase_C.
DR   NCBIfam; TIGR01448; recD_rel; 1.
DR   PANTHER; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR43788:SF6; RECBCD ENZYME SUBUNIT RECD; 1.
DR   Pfam; PF13245; AAA_19; 1.
DR   Pfam; PF14490; HHH_4; 1.
DR   Pfam; PF18335; SH3_13; 1.
DR   Pfam; PF13538; UvrD_C_2; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01488}; DNA-binding {ECO:0000256|HAMAP-Rule:MF_01488};
KW   Helicase {ECO:0000256|HAMAP-Rule:MF_01488};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01488, ECO:0000313|EMBL:AAU16134.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01488}.
FT   DOMAIN          156..247
FT                   /note="RecD helicase-like helix-hairpin-helix"
FT                   /evidence="ECO:0000259|Pfam:PF14490"
FT   DOMAIN          589..659
FT                   /note="RecD-like DNA helicase SH3"
FT                   /evidence="ECO:0000259|Pfam:PF18335"
FT   DOMAIN          676..724
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13538"
FT   BINDING         365..369
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ   SEQUENCE   778 AA;  87444 MW;  49CC93AC5974F6CA CRC64;
     MGNQHAMDLF EEEKKFIKAQ VLHTIFHNEE NLYSVVSMKV IETNETYDEK KVMINGHFPR
     MHEDEVFTLT GHFKDHPKYG KQYLVETFKK ELPQTKAGMV QYLASDLFKG IGKRTAEKIV
     DHLGEHAISK IMDDPEALNG VVNKQKAQEI YETIVEHQGL EKVMSFLNGY GFGTKLSIKI
     YQQYKEMTLE VIRNNPYQLI EEVDGIGFGR ADDIGRALGI SGNHDDRVRA GCFYTLENVS
     LQLGHVYMRK DQLIRETMSL LNNQEGRVTE EDIISCIEMM QSEGKVIIEE ERVYLASLFY
     SEKGVVKSIR RLMNQEETPS FPEAEVLKTL GEIEEQLNVQ YAPLQQEAIQ TALHKPMMLL
     TGGPGTGKTT VIKGIVEMYA SLHGLSLNPN EYSDDNPFPI LLTAPTGRAA KRMSESTGLP
     ACTIHRLLGW TPEGSFQRNE TDPVQGKLLI IDEFSMVDIW LANQLFKSLP TNIQVIVVGD
     EDQLPSVGPG QVLKDLLNAG AVPTVKLTEI YRQAEGSSVI QLAHAIKNGT LPPDLAQNQK
     DRSFIGCTGA QIVEVVKKVC ENAKTKGFSA RDVQVLAPMY RGPAGINVLN EALQEVFNPK
     REKSKEIAYG DVVYRRGDKV LQLVNQPESQ VFNGDIGEIV SVFYAKENVE QQDMIIVSFD
     GIEVTYTKPD LNQITHAYCC SIHKSQGSEF PIVIMPIVKS YNRMLRRNLI YTGITRSKKF
     LIICGEEAAF QSGVNRLDDA MRQTTLASRL QESQGEVQMV TVNGEEMDVE NISPYDFM
//
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