ID D4YS02_9LACO Unreviewed; 784 AA.
AC D4YS02;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
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:EFG56096.1};
GN Synonyms=recD2 {ECO:0000256|HAMAP-Rule:MF_01488};
GN ORFNames=HMPREF0493_0280 {ECO:0000313|EMBL:EFG56096.1};
OS Lactobacillus amylolyticus DSM 11664.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=585524 {ECO:0000313|EMBL:EFG56096.1, ECO:0000313|Proteomes:UP000004069};
RN [1] {ECO:0000313|EMBL:EFG56096.1, ECO:0000313|Proteomes:UP000004069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11664 {ECO:0000313|EMBL:EFG56096.1,
RC ECO:0000313|Proteomes:UP000004069};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (APR-2010) 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:EFG56096.1}.
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DR EMBL; ADNY01000011; EFG56096.1; -; Genomic_DNA.
DR RefSeq; WP_006351434.1; NZ_AZEP01000005.1.
DR AlphaFoldDB; D4YS02; -.
DR STRING; 83683.B1745_03995; -.
DR PATRIC; fig|585524.9.peg.1336; -.
DR eggNOG; COG0507; Bacteria.
DR OrthoDB; 9803432at2; -.
DR Proteomes; UP000004069; 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; PF13604; AAA_30; 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:EFG56096.1};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01488, ECO:0000313|EMBL:EFG56096.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01488}; Reference proteome {ECO:0000313|Proteomes:UP000004069}.
FT DOMAIN 341..494
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 784 AA; 86810 MW; 6CD247A623271FB5 CRC64;
MVKFTGKVNG IVFENDQDMF KILDVEILGK LEGYPRDEIK VTGSFGEIQI AGRYQFDGRL
IMHDKFGLQF RSDSYQQVMP HEEGSLTKYL SSNKFPGIGL KAAGKIIDEL GINALDVLKN
NPAKIDTLAL TQKQKDSLLS GINSMDSFSE IILKLAQYGV KKKVATRLYQ FYHGEALKKL
QQNPYAAIAE VQGYGFKTAD IIGRELNIKA DDPKRIQGAV YQVLIDALTS SGDTYVGLAE
LLTESSKMLD ISAFDPIAKE VNTLQKNGKV VVDGENVAIS NIYETEVNIA RTLKNLVQRR
QDQHDETYSD SEMEDAIEEA EKKLKIKYDD TQKAAIKNAL NNPVSILTGG PGTGKTTIIN
GILLSLRQLA DIPASALYSE DPPFLLAAPT GRAAKRMGEI TGIAAKTIHR LLGLGIGETD
EAELNELNGE ILIIDEMSMV DMFLFKQLVS SINQTRHIVF VGDKDQLPSV GAGNVFSDLI
KSHAFPTTIL KQIHRQGDDS TIITLAHDVN DGKNQDELFK KTKNYSFIPC QPQLVGEAVG
QIVELALKRG FSKDDIQVLG AMYHGNGGII NLNDILQEIM NPPKAKSKQV EAHNENFRIG
DRVLQLQNNP EKDIYNGQIG KVVGIDDHSS DKCLIANFDE REVEFNKKDL SDLTRAYAIT
IHKSQGSEFP LVVLNLTMQN YVMLKRNLLY TAITRAEKNL VLVGEPRAYI TALNTPGNDR
KTGLTAKLQK ELKVDQSNDD AAKTAKKLPP KSAEQEDYIL TKEKIYSGEI DPMIGMQDIS
LKAR
//
