ID A0A1Z4J9S2_LEPBY Unreviewed; 754 AA.
AC A0A1Z4J9S2;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=NIES2135_03200 {ECO:0000313|EMBL:BAY53514.1};
OS Leptolyngbya boryana NIES-2135.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Leptolyngbya group; Leptolyngbya.
OX NCBI_TaxID=1973484 {ECO:0000313|EMBL:BAY53514.1, ECO:0000313|Proteomes:UP000217895};
RN [1] {ECO:0000313|EMBL:BAY53514.1, ECO:0000313|Proteomes:UP000217895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2135 {ECO:0000313|EMBL:BAY53514.1,
RC ECO:0000313|Proteomes:UP000217895};
RA Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT "Genome sequencing of cyanobaciteial culture collection at National
RT Institute for Environmental Studies (NIES).";
RL Submitted (JUN-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}.
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DR EMBL; AP018203; BAY53514.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z4J9S2; -.
DR Proteomes; UP000217895; Chromosome.
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};
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:UP000217895}.
FT DOMAIN 349..535
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 360..364
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 754 AA; 84696 MW; 0605E65B38BFBC50 CRC64;
MQPKANMMNI EELEGSIESI VFTSAKTGFT VARLQTVAEV VTIVGNFASL NLGQSLILSG
TWRTHSRYGL QFQVENYREA LPNTIASLEA YLSSGAIRGI GSAMAKRIVD RFGLETLTIL
ESDIDRLIEV KGIAQSKIAI IQSSWLEQKQ THSIMMFLQT YGIGRSQAVK VFKRYGEDAI
EIVSQNPYQL AADIRGIGFH SADGIATQLG IKPDSEARYR SAILHTLREA GRDGHCFLPQ
STLVERTARL LARPDYAAQT EQIEDQIVYL VATQELVVEE SRRYPGRLGY YLPAFYYAEM
SIATRLKLLL LEPLEIDHHF VETWMQQYCE SSDLLLSQEQ RQAVILAATQ RVVILTGGPG
VGKSHTTRAI VELWEAMGKQ VALASPTGRA ARRLSELTQR DASTLHRLLE YDRGSGYFQR
DHTRPLKADC IVVDEFSMTD VFLANALIKA VSLQSQLLIV GDVDQLPSVG AGAVLRDLIE
SEQVPVIRLT QVWRQAQSSA IICHAHALNR GEVPEIERFS TTPRSDCLWM PSHSPQHGIQ
CIQQLITETI PRLGFNAFND VQILCPMIKG DIGTKAINAV VQALLNPPQA DGFEVQAEER
KFRIGDRVIQ LENDYDREVM NGELGIIETY DAQRQILGVQ FEEHWVEYQR TEWDQMTLAY
SITGHKAQGS EFPVTIVPLF MQNTVMLSRP WLYTTLTRAK QLAILVGQPQ ALRQAISQCR
DKRRYTLLSQ RLQEEQIVPS FSSNPQNSHQ NSHN
//
