ID A0A1T4WE16_9CLOT Unreviewed; 739 AA.
AC A0A1T4WE16;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=SAMN05443428_10139 {ECO:0000313|EMBL:SKA75530.1};
OS Caloramator quimbayensis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Caloramator.
OX NCBI_TaxID=1147123 {ECO:0000313|EMBL:SKA75530.1, ECO:0000313|Proteomes:UP000190105};
RN [1] {ECO:0000313|EMBL:SKA75530.1, ECO:0000313|Proteomes:UP000190105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USBA 833 {ECO:0000313|EMBL:SKA75530.1,
RC ECO:0000313|Proteomes:UP000190105};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FUYH01000001; SKA75530.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4WE16; -.
DR STRING; 1147123.SAMN05443428_10139; -.
DR OrthoDB; 9803432at2; -.
DR Proteomes; UP000190105; 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 GO; GO:0006281; P:DNA repair; IEA:InterPro.
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; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
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; 2.
DR Pfam; PF18335; SH3_13; 1.
DR Pfam; PF13538; UvrD_C_2; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00278; HhH1; 3.
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, ECO:0000313|EMBL:SKA75530.1};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01488};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01488}.
FT DOMAIN 81..102
FT /note="Helix-hairpin-helix DNA-binding motif class 1"
FT /evidence="ECO:0000259|SMART:SM00278"
FT DOMAIN 116..135
FT /note="Helix-hairpin-helix DNA-binding motif class 1"
FT /evidence="ECO:0000259|SMART:SM00278"
FT DOMAIN 180..199
FT /note="Helix-hairpin-helix DNA-binding motif class 1"
FT /evidence="ECO:0000259|SMART:SM00278"
FT DOMAIN 332..484
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 739 AA; 82832 MW; 2F6E014E78C47305 CRC64;
MIEIEGTVVS IVYRNDENGY TVAKVKHGRD TDSVVGYMPF LSEGQKAKFC GEWTIHKTFG
QQLKVESFEE IMPATLEGVE KYLSSGLIKG IGPATAKRIV EKFGMDSLDI IEMNPGRLTE
IEGIGEKRAQ SIAEAFKEQR ELREVLVSLQ SYGISVTYGL KIYKRYGKET FNIIKENPYK
LCDDISGIGF KTADRIARNL GVDLNSTYRI MAGIKYILSG CIANGHVYLP KLTLYDECVK
LLNVPIEIIE EALISLMTSK QVICDDIEGE TAVYLSSLFY SELGVARRLV EFSLQKIGED
FKDIEDDIKE YEKLNNIEFA TEQKEAVIES VKNGVCIITG GPGTGKTTII KCIIEIFKKR
GMEVVLAAPT GRASKRITEA TGYEAKTIHR LLEMEYTSED SFPVFTKDEA DPLECDAVII
DEASMVDILL MNSLLKAMPQ GCRLIMVGDV DQLPSVGPGN VLRDIIDSHA ISVVRLNRIY
RQADESLIAV NAHRINSGDM PILNDREKDF FFIQKGNSQD MVEEIVRLVD SRIPSFKEGF
DPMRDIQVLS PTRKGEVGIY NLNIKLQEVL NPKSSKKGEK QFRDFTFRVG DKVMQIKNNY
SLKWQSISNE SESGMGIFNG DIGFVESVDS ENQNLTVIFD DDKRVVYDFS NLDELEMAYA
VTIHKSQGCE FPVVIIPVFF GPPMLLTRNL IYTGVTRAKK LVVLVGVRAA LSNMINNNTI
AQRYTGLKKR ILAMVNAIR
//
