ID A0A1I4YSC1_9CLOT Unreviewed; 737 AA.
AC A0A1I4YSC1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=SAMN04488695_101765 {ECO:0000313|EMBL:SFN40867.1};
OS Proteiniclasticum ruminis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Proteiniclasticum.
OX NCBI_TaxID=398199 {ECO:0000313|EMBL:SFN40867.1, ECO:0000313|Proteomes:UP000181899};
RN [1] {ECO:0000313|EMBL:SFN40867.1, ECO:0000313|Proteomes:UP000181899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ML2 {ECO:0000313|EMBL:SFN40867.1,
RC ECO:0000313|Proteomes:UP000181899};
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; FOVK01000001; SFN40867.1; -; Genomic_DNA.
DR RefSeq; WP_074910494.1; NZ_FOVK01000001.1.
DR AlphaFoldDB; A0A1I4YSC1; -.
DR STRING; 398199.SAMN05421804_101355; -.
DR eggNOG; COG0507; Bacteria.
DR OrthoDB; 9803432at2; -.
DR Proteomes; UP000181899; 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:UP000181899}.
FT DOMAIN 332..482
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 343..347
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 737 AA; 82850 MW; BC71A48D2B664F9F CRC64;
MERLEGVVRD IVFQNEESAF CIIKIEDEQE VHTALGTFPY ISVGQTLVLH GESVLHATFG
KQFKCESYEE IVPSTMAGIE KYLSSGAVAG IGPITAKKLV EKFGAEIFSI IENEPEKLKE
LDGIGDKKVR LIYESYIKGR EVKNIMVFLQ SYGVTPKQAL KIYRVFGNDS VAKVKENPYI
LSDEVPSIGF KTADKIARNL GITLDSPFRI QSGIKYIINE YCAQGSTFIP KEMLLEKGQS
ILEVGREELE ENILHEVMKS KLMLERIDEV EGVFTMPYLY AEISVTKHML GLLLEGVEAL
DIPVKDYIHD FEKTNGISFH DKQIEAITGA AENGIEIITG GPGTGKTTII KCILNIFERA
GKKVLMGAPT GRAAKRMSEA TGRESKTIHR LIDLSVSTEE DEVLFDEDET LNCDVVIIDE
ASMIDVMLMN NLLKSIKPKT RLILVGDVDQ LPSVGSGKVL EDIIDSGAFP VVKLQFIYRQ
GKESFITTNA HRINTGVMPV LNAKESDFFF IQGNDSEDSL QKVIELVTTR LPKFNEKWDR
VKDFQILTPM RKGELGVYNL NLVLQKALNP RRKKYSFTDL QIGDKVMQTK NNYMIKWRKV
KRTFGEPPEG QGIFNGDIGY VTDINEEDNT VSVLFDEDKI VEFESQDLDE LELAYAVTIH
KSQGSEFKVV LVPLFMGPPL LMSRNLIYTA VTRARELIVL VGSQKALSYM IKNTKTYDRH
TSLKYRIMSV MDNVGVE
//
