ID C2EMI1_9LACO Unreviewed; 787 AA.
AC C2EMI1;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
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=HMPREF0548_0877 {ECO:0000313|EMBL:EEJ72190.1};
OS Lactobacillus ultunensis DSM 16047.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=525365 {ECO:0000313|EMBL:EEJ72190.1, ECO:0000313|Proteomes:UP000005583};
RN [1] {ECO:0000313|EMBL:EEJ72190.1, ECO:0000313|Proteomes:UP000005583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16047 {ECO:0000313|EMBL:EEJ72190.1,
RC ECO:0000313|Proteomes:UP000005583};
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 (JAN-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:EEJ72190.1}.
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; ACGU01000043; EEJ72190.1; -; Genomic_DNA.
DR RefSeq; WP_007125405.1; NZ_GG693253.1.
DR AlphaFoldDB; C2EMI1; -.
DR STRING; 525365.HMPREF0548_0877; -.
DR PATRIC; fig|525365.8.peg.731; -.
DR eggNOG; COG0507; Bacteria.
DR HOGENOM; CLU_007524_0_1_9; -.
DR OrthoDB; 9803432at2; -.
DR Proteomes; UP000005583; 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:EEJ72190.1};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01488, ECO:0000313|EMBL:EEJ72190.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01488}.
FT DOMAIN 341..494
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 740..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 352..356
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 787 AA; 87676 MW; 8CDE66374A9949A8 CRC64;
MVEFTGKVNG IVFENDKDLY KILDVEIIGS LENYSRDEIK VTGNFGDIQI ESSYRFEGKL
VMHEKFGLQF RASSYKQVLP HEEGSLTKYL SSNKFPGIGK KAANTIIDEL GLNALDVLKE
NPAKIDTLSL SSKQKDSLLS GLNAMDSYSE IVLKLAQYGI NKRIAGKVYQ LYHGDSLKKL
EKDPYATVND VAGFGFKTAD IMGKQLDIKV DDPRRINGAI YQVLLDALNG DGNTYVKSPE
LLTEASKLLQ INQFDPIANC VINLCQQGKI VVDGDKVSLQ NIFKTEQDIA RSMKYLVETR
KQQEDEQYGD DDVAEAIRDA EKELEIKYDD TQKLAIKNAL NHPISILTGG PGTGKTTIIN
GILLALRKLA EIPASALYSE DPPFLLAAPT GRAAKRMSEV TGISAKTIHR MLGLGIGDTG
TEELNELNGE ILIIDEMSMV DMFLFKQLLS SINQVRHIVF VGDKDQLPSV GAGNVFSDLI
KSRAFPTTIL KQIHRQGDDS TIITLAHDIN EGKNEQALFK RTKNYSFISC RPELVGDAVG
QIVTLALKRG FAKDDIQVLG AMYHGNGGVN NLNDIIQEIM NPAKEHSKSL EAHNEIFRIG
DRILQLQNNP EKDIYNGQIG KIMSIDEDKS KECMVANFDG REVTFDRKDL NDLTRAYAIT
IHKSQGSEFP LVVLNLTMQN YVMLKRNLLY TAVTRAEKNL VLVGDPRAFV AAFKTPGNDR
KTDLADKICK QLGIELEENK SEQVKKQVKE EKTEKSTKKE TEDYILTPEK IYSGEIDPMI
GMENIKL
//
