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Database: UniProt
Entry: A5Z851_9FIRM
LinkDB: A5Z851_9FIRM
Original site: A5Z851_9FIRM 
ID   A5Z851_9FIRM            Unreviewed;       750 AA.
AC   A5Z851;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 71.
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=EUBVEN_01891 {ECO:0000313|EMBL:EDM50574.1};
OS   Eubacterium ventriosum ATCC 27560.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Eubacterium.
OX   NCBI_TaxID=411463 {ECO:0000313|EMBL:EDM50574.1, ECO:0000313|Proteomes:UP000006000};
RN   [1] {ECO:0000313|EMBL:EDM50574.1, ECO:0000313|Proteomes:UP000006000}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27560 {ECO:0000313|EMBL:EDM50574.1,
RC   ECO:0000313|Proteomes:UP000006000};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EDM50574.1, ECO:0000313|Proteomes:UP000006000}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27560 {ECO:0000313|EMBL:EDM50574.1,
RC   ECO:0000313|Proteomes:UP000006000};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Eubacterium ventriosum (ATCC 27560).";
RL   Submitted (APR-2007) 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:EDM50574.1}.
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DR   EMBL; AAVL02000036; EDM50574.1; -; Genomic_DNA.
DR   RefSeq; WP_005358657.1; NZ_DS264265.1.
DR   AlphaFoldDB; A5Z851; -.
DR   STRING; 411463.EUBVEN_01891; -.
DR   GeneID; 66467152; -.
DR   eggNOG; COG0507; Bacteria.
DR   HOGENOM; CLU_007524_0_2_9; -.
DR   OrthoDB; 9803432at2; -.
DR   Proteomes; UP000006000; 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; 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   SMART; SM00382; AAA; 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:EDM50574.1};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01488};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01488}.
FT   DOMAIN          342..494
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   BINDING         353..357
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ   SEQUENCE   750 AA;  83513 MW;  25B2FA605169A4B2 CRC64;
     MKTVSGYVEN ITFRNEDNGF TVLTLSSGKE DITCTGNFGY IGQGEYVEIE GEEVFHEIYG
     KQIKATNYKI VPATDELSLK KYLGSGAIKG LGAVLADRIV DKFGEDTFRI IEEEPERLAE
     IRGITTRKAM DISTQLEEKK DMRDVMIFLQ GYGISPTLST KIFNNYGTRV YDIIKTNPYQ
     LADDVTGIGF KTADEIARRA GVEVNASVRI KSGMCYALTE ASLSGHTYLP KEKMVETTIN
     LLGLRDQYLN ADGTYNMELL DNCFTELVLE KKLILKEIDD NQAVFLSTFY YTELNIARML
     LELNISTPED DYILGVKMDT VEDMSGIHLD DLQRQAVVAT QNNGVSIITG GPGTGKTTTI
     NAIIQLFESD GLEVSLAAPT GRAAKRMTEA TGHEAKTIHR MLEISGGQSD DPELDAKFGR
     NEQNPLETDV VIVDEMSMVD TFLMHAFLKA VTVGTRLVFV GDVNQLASVG PGNVLKDIIE
     SECFKVVRLT KVFRQAGESG IVTNAHKINE GKEVKLDNSF GDFLYIEREN AQMALNATIG
     LIKTKLPAYV GANEMDIQVL TPMRNGILGV NSLNPGLQMY MNPPDKNKNE KEIAGVVFRE
     GDKVMQIKNN YQLEWEQRTD KGFLVDSGSG IFNGDMGIIT KINNLTNYIE VKFDDDRYVT
     YDSKQAEELE LAYAVTIHKS QGSEYPAVVM PLVSGASMLM TRNLLYTGVT RAKKCVCIVG
     RKETFNAMVK NEDQHKRYSG LKWQLINYYQ
//
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