ID C8PAU3_9LACO Unreviewed; 780 AA.
AC C8PAU3;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
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=recD {ECO:0000313|EMBL:EEW52582.1};
GN Synonyms=recD2 {ECO:0000256|HAMAP-Rule:MF_01488};
GN ORFNames=HMPREF0520_0213 {ECO:0000313|EMBL:EEW52582.1};
OS Lactobacillus iners DSM 13335.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=525328 {ECO:0000313|EMBL:EEW52582.1, ECO:0000313|Proteomes:UP000004115};
RN [1] {ECO:0000313|EMBL:EEW52582.1, ECO:0000313|Proteomes:UP000004115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13335 {ECO:0000313|EMBL:EEW52582.1,
RC ECO:0000313|Proteomes:UP000004115};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (SEP-2009) 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:EEW52582.1}.
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DR EMBL; ACLN01000003; EEW52582.1; -; Genomic_DNA.
DR RefSeq; WP_006730028.1; NZ_GG700811.1.
DR AlphaFoldDB; C8PAU3; -.
DR GeneID; 69785115; -.
DR PATRIC; fig|525328.13.peg.304; -.
DR HOGENOM; CLU_007524_0_1_9; -.
DR OrthoDB; 9803432at2; -.
DR Proteomes; UP000004115; 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; 2.
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:EEW52582.1};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01488, ECO:0000313|EMBL:EEW52582.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01488}; Reference proteome {ECO:0000313|Proteomes:UP000004115}.
FT DOMAIN 341..498
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 352..356
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 780 AA; 87629 MW; 5362E5290A81C3A1 CRC64;
MAELQLIGMV EGIIYENNEE LFKILDVHII RKIAGYDHDS IRVMGNFGEM DLSIRYKFVG
EIIEHSKFGM QFKAKSYQAI MPAEYNAIVD YLASDKFAGI GKKTAEKIVS QLGEDLFTKI
KDNNKVVEDL KLTDKQRQSL LNGILHMDQL GEILTQAVQY GINKSIITDL YNKYKGETLS
KIEEDPYALI AETRGYGFKI ADSIANKLGF KADDSRRLKG ALMQVLLDSA LKDGNTYLLM
DKWLENTSEL LYIDDFDLLA NEVNNLKKDN KVVIFDDKVS LTNMYTIEKD IANDLKRISD
SNKKDIPYLD DDLNSAIKHV EQKFDISYDD TQKKAIKTAL NNSISILTGG PGTGKTTIIR
GILATLQEIE KIPNDVLYTD DPPFLLAAPT GRAAKRMSEL TGIDAKTIHR LLGLGISDLN
QENMNELNGE ILIIDEMSMV DMFLFKNLVS SIFQLKHIVF VGDKDQLPSV GPGNIFSDLI
ASSAFPTTKL SMIHRQSDDS SIVDLAHKIN QNNAQANIFT KTPNYSFISC KPNSIADAIE
KIVDIALEKG FCADDIQVLT AMYNGVSGIN SLNDLLQNIM NPAKIDSKKV EVHNEFFRIG
DRVLQLQNNP EKEIYNGQIG KVVGIDDSQK SAKLIVRFDD REVMLTSNDL SDLTRAYAIT
IHKSQGSEFP LVILALTMQN YIMLKKNLLY TGITRAQQNL VMIGEEQAYQ MALKTEGNDR
QTDLCSKIQC IFNKNDIELQ ENEIDNADNH SENYILTPDL IYSNKIDPMI GMEDVRLSDI
//
