ID A0A1Y4SYJ9_9FIRM Unreviewed; 730 AA.
AC A0A1Y4SYJ9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=B5E75_05055 {ECO:0000313|EMBL:OUQ35016.1};
OS Massilimicrobiota timonensis.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Massilimicrobiota.
OX NCBI_TaxID=1776392 {ECO:0000313|EMBL:OUQ35016.1, ECO:0000313|Proteomes:UP000195305};
RN [1] {ECO:0000313|Proteomes:UP000195305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An13 {ECO:0000313|Proteomes:UP000195305};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-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 -!- 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:OUQ35016.1}.
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; NFLJ01000011; OUQ35016.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4SYJ9; -.
DR OrthoDB; 9803432at2; -.
DR Proteomes; UP000195305; 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; 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; 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; 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.
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}.
FT DOMAIN 333..466
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 344..348
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 730 AA; 84315 MW; 611DDAFE767EF9BC CRC64;
MLTYTGIIKR IKFYSEDTKF IVCLIDSEQE DKPILATGYM SYVNLQDKYH FQGEYIIHPK
YGKQFQIQSY EIVLANEESE IIRYLSSPLF KGIGEKQATA IVEVLGKDAL TKIKEDKHVL
DHVRGMNETK RETIASVLSS QDFDQEVLMF FMGHGISTRH LALIQAVYQE KTLDILQNNP
YQLIDDIDGI GFKTADDLAL KIGVDQYDHH RIQAAIVYAL KEACFQDGST YHNYETIVKR
FHRYIPQIDD ESFEAAFTDV LEQNKIIQEE DRYYPYELYQ SEINISQIFK RWLHTPLYDI
NSKDIDKILE DLEKELFIEY DDFQKDAIKL FMEHSAMIIT GGPGTGKTTI VNAMIKIYQR
LNPDQRLAIV APTGRAAKRL SEVTGVEACT IHRLLKWDLH TNTFAVNEKN PLDVDLLIID
EFSMVDSLLF SHLLLACQKV SQILLIGDDQ QLPSVAPGHV LKDLIESECI PTIALHYIYR
QSKESGIVQL AHSIRNDQYD ENLFFQYSDI HFQTCTPYDV VKYVRVLVSK ALEDGYDGQD
IQVLAPMYNG VAGIDALNDC LQELLNPSDG FKNELRVGKR VFREGDKILQ LKNRVEDNVF
NGDIGTLVEI CYKDNFEYLT DKMIVDFDGT IVEYTPQEFY TLTHAYCMSV HKSQGNEFKI
VIMPVLKDYY IMLKKNLIYT GLTRAKQSLW FLGSHQAFVY GVTHKQDERR KTTLIERMKK
TPEISLYDFE
//