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Database: UniProt
Entry: R6BY29_9CLOT
LinkDB: R6BY29_9CLOT
Original site: R6BY29_9CLOT 
ID   R6BY29_9CLOT            Unreviewed;       746 AA.
AC   R6BY29;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
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=BN687_02453 {ECO:0000313|EMBL:CDA68120.1};
OS   Clostridium sp. CAG:510.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1262816 {ECO:0000313|EMBL:CDA68120.1, ECO:0000313|Proteomes:UP000018120};
RN   [1] {ECO:0000313|EMBL:CDA68120.1, ECO:0000313|Proteomes:UP000018120}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:510 {ECO:0000313|Proteomes:UP000018120};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CDA68120.1}.
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DR   EMBL; CBCI010000034; CDA68120.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6BY29; -.
DR   STRING; 1262816.BN687_02453; -.
DR   Proteomes; UP000018120; 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; 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:CDA68120.1};
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:UP000018120}.
FT   DOMAIN          340..490
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   BINDING         351..355
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ   SEQUENCE   746 AA;  83783 MW;  CF1C5E905FF182AA CRC64;
     MEKITGFVEH IVFQNTDNGY TVLELSGEEG EIILVGMMKG ITQGESIDAE GDYIEHPVYG
     RQFKVSSYRT VTPKDAAGME RYLASGAIKG VGAALAARIV KAFGTDTFRI IEEEPIRLVE
     VKGISDRIAR EIAAQMEEKR DLREAFLFLQ QYGISNTLAV KIYNTYGDNL YRVLQENPYK
     MTEDIEGVGF KIADEIASRI GIHTDSDYRI RSGILYVLSQ AMAEGHMYLP EELLIKRTQE
     LLLVDEDNIR PHLQNLGMDK KLVLKKMPDE EELQVFAASA YYAELSCAGM LHDLNLSLYG
     EEGMLPAVET KIKGQIESIT REEHLELDSL QEEAVFQCVK NGVFILSGGP GTGKTTTINT
     IIKYFEQEKL DIFLAAPTGR AAKRMTEATG YEARTIHRML ELSGALSGGD RKAGFERNED
     NPLEADVVII DEMSMVDIYL FQALLRAIVP GTRLILVGDV DQLPSVGPGQ VLRDLMASKA
     FPCVVLSKIF RQAESSDIVV NAHKINKGEQ ISLNNKSRDF FFLERNDVNV IYKHMVQLIT
     DKLPRYVNGE PYDIQVLTPM RKGSLGVETL NPTLQKYMNP PAPNKREHTF GSVTFREGDK
     VMQIKNNYDL EWEIVSRYGI PIDKGLGIFN GDMGRITEIN EYASTLTVEY DEHRRVTYAF
     VQAEELELAY AITIHKSQGS EYAAVVMPLL SGPKMLFNRN LLYTGVTRAK NCVTILGSSE
     TVRQMINNAE VNRRYTALTE RIKELS
//
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