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Database: UniProt
Entry: H3NH49_9LACT
LinkDB: H3NH49_9LACT
Original site: H3NH49_9LACT 
ID   H3NH49_9LACT            Unreviewed;       816 AA.
AC   H3NH49;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 49.
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=recD2 {ECO:0000256|HAMAP-Rule:MF_01488};
GN   ORFNames=HMPREF9708_00188 {ECO:0000313|EMBL:EHR38104.1};
OS   Facklamia languida CCUG 37842.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Facklamia.
OX   NCBI_TaxID=883113 {ECO:0000313|EMBL:EHR38104.1, ECO:0000313|Proteomes:UP000006190};
RN   [1] {ECO:0000313|EMBL:EHR38104.1, ECO:0000313|Proteomes:UP000006190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 37842 {ECO:0000313|EMBL:EHR38104.1,
RC   ECO:0000313|Proteomes:UP000006190};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Heiman D., Howarth C., Larimer J., Lui A.,
RA   MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Facklamia languida CCUG 37842.";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
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}.
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:EHR38104.1}.
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DR   EMBL; AGEG01000002; EHR38104.1; -; Genomic_DNA.
DR   AlphaFoldDB; H3NH49; -.
DR   STRING; 883113.HMPREF9708_00188; -.
DR   PATRIC; fig|883113.3.peg.186; -.
DR   eggNOG; COG0507; Bacteria.
DR   HOGENOM; CLU_007524_0_1_9; -.
DR   OrthoDB; 9803432at2; -.
DR   Proteomes; UP000006190; Unassembled WGS sequence.
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; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 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; IPR010994; RuvA_2-like.
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; PF13604; AAA_30; 1.
DR   Pfam; PF14490; HHH_4; 1.
DR   Pfam; PF14520; HHH_5; 1.
DR   Pfam; PF18335; SH3_13; 1.
DR   Pfam; PF13538; UvrD_C_2; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF47781; RuvA domain 2-like; 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, ECO:0000313|EMBL:EHR38104.1};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01488};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01488}; Reference proteome {ECO:0000313|Proteomes:UP000006190}.
FT   DOMAIN          149..239
FT                   /note="RecD helicase-like helix-hairpin-helix"
FT                   /evidence="ECO:0000259|Pfam:PF14490"
FT   DOMAIN          581..651
FT                   /note="RecD-like DNA helicase SH3"
FT                   /evidence="ECO:0000259|Pfam:PF18335"
FT   DOMAIN          668..715
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13538"
FT   REGION          752..781
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        752..778
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         358..362
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ   SEQUENCE   816 AA;  92151 MW;  76CB2D0BB2AEB16C CRC64;
     MEEVVIYGKA VAIYFENNRN FYKVIRIEVD QERTDVMVED ELVITGQFVS IHLDTTYQFF
     GQWTHHPKYG QQFSVTHYQN IQPTSRKGMI DYLSSHRFKG IGVKTATAIM DTLGDQALDI
     ILEDPQALDR VPGLTRKKAQ NLRQQLMRHQ GAERIFMQLS QWGFSPNLAD KIFHVFKEET
     LDKIKDDPFC LIEGVEGIGF SKADQIAAQL GGDPDDPRRI CAALVSVVGQ IASERGDTYV
     TKSDALQEAR NLLEKSRPHL ISDGLLFQGL DMALMEDLLL IVGEDLVLPS IFYAEYGSSK
     KIKEFIELEE IERYQDEDLE LAIDQLQADI DIIYDEDQRR ALKLAMSSPM SIITGGPGTG
     KTTLVRGLIH LHARLKGYDL ASLRIDNFDS PIRLAAPTGR AAKRMQEASQ LPATTIHRLI
     GFTRDSEIGY FQPETIEGSL LIVDEMSMVD VWLMNWLLEA IPYDMQVVFV GDKDQLPSVG
     PGKVFADMIE SQVLSTISLH RIYRQAKDSS IIRLAHDVRQ GRLPEDLLTK QADRSFIPCP
     THQIPQAIHQ IVNKAIEKGY TSQTLQVLAP MYKGPAGIDQ INQLMQAMLN PPKARKRELT
     YFDRVYRVGD KVLQLVNNTE EGVYNGDVGQ ITAILTSKET ESKSEEVVVS FDEVEIHYQR
     SDLNQLTLAY CTSIHKAQGS EYDLVILPLV NQFSRMLRRD ILYTAITRAS QSLILLGDPQ
     AFYQAATHQQ IDRKTNLLDF LGLVFEQKVS TDQEAPGSRS ERSAVDLSSE QENLHVSQDP
     PLPSLDLDNF LSLTNYRQID PMIGMEGLTP FDFMPN
//
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