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Database: UniProt
Entry: A0A1G4V936_9FIRM
LinkDB: A0A1G4V936_9FIRM
Original site: A0A1G4V936_9FIRM 
ID   A0A1G4V936_9FIRM        Unreviewed;       739 AA.
AC   A0A1G4V936;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
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=SAMN02910339_00512 {ECO:0000313|EMBL:SCX03152.1};
OS   Lachnospiraceae bacterium YSD2013.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=1520828 {ECO:0000313|EMBL:SCX03152.1, ECO:0000313|Proteomes:UP000199278};
RN   [1] {ECO:0000313|EMBL:SCX03152.1, ECO:0000313|Proteomes:UP000199278}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YSD2013 {ECO:0000313|EMBL:SCX03152.1,
RC   ECO:0000313|Proteomes:UP000199278};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FMTX01000007; SCX03152.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G4V936; -.
DR   STRING; 1520828.SAMN02910339_00512; -.
DR   OrthoDB; 9803432at2; -.
DR   Proteomes; UP000199278; 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:InterPro.
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; IPR003593; AAA+_ATPase.
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; PF13245; AAA_19; 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   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
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};
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:UP000199278}.
FT   DOMAIN          331..518
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   BINDING         342..346
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ   SEQUENCE   739 AA;  82185 MW;  A03907266805A8AA CRC64;
     METIQGFISS IRYRNPDNGY SVLSFVVDDN EETLVGNFLS VSEGEMLKVT GEWVVHPIYD
     KQFKATSYES IQPEDELAVL RYLSSGIIKG IGPTLAKRIV DEFGKDTFMV MEEQPELLER
     VKGITLKKAQ EIGVLMQEKR GYREAMMFLT KYGIGNALAI KVYSYYGDRI YSILKENPYK
     LAEDIPGIGF KTADEIAARL GVKGDSNYRI QSGILYTLVL ATGQGHMYLP KDILEEEASK
     ILDVTADLVQ PEIDNLTVER KLIIKGTDVY APSNFYVEQS VAGLLRSVVS DVFCDEYEDD
     LSIAKEVENI ATQAGYALDP LQTKAVVQAI TNGVSIITGG PGTGKTTTIK TLIGYFDAEG
     MDIALAAPTG RAAKRMTEAT GYEAKTIHRL LELNGTIDED GKDAGFERNE DNPLDVDAVI
     VDEMSMVDIF LFRALLKAIP PGARLVMVGD AHQLPSVGPG QVLRDLLESE CFPVTRLETI
     FRQEGSGDIV VNAHRINNGE DIETPKGSRD FFFIERSDPS KIMLNMVELI TKNLPGYVGA
     EPFDIQVLTP TRKGNLGVIT LNRYLQNALN PPSKDKAEHY YGEEIFREGD KVMQIRNNYQ
     ANWEVLGKHN IPIDSGIGIF NGDMGRIVEI DESDSSLTVE FDDNKRVTYD FTNLDELELA
     YAITVHKSQG SEYGAVIMPV APGPRQLMNR NLLYTGVTRA KKCLVMIGNP GIVHEMIENN
     HENLRYSGLK CRIIEMFTE
//
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