ID A0A1H9XRQ0_9ACTN Unreviewed; 753 AA.
AC A0A1H9XRQ0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=SAMN04487983_107215 {ECO:0000313|EMBL:SES48818.1};
OS Streptomyces sp. yr375.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1761906 {ECO:0000313|EMBL:SES48818.1, ECO:0000313|Proteomes:UP000198568};
RN [1] {ECO:0000313|EMBL:SES48818.1, ECO:0000313|Proteomes:UP000198568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YR375 {ECO:0000313|EMBL:SES48818.1,
RC ECO:0000313|Proteomes:UP000198568};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOFF01000072; SES48818.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9XRQ0; -.
DR STRING; 1761906.SAMN04487983_107215; -.
DR OrthoDB; 9763659at2; -.
DR Proteomes; UP000198568; 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; PF14520; HHH_5; 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:SES48818.1};
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:UP000198568}.
FT DOMAIN 367..548
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 378..382
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 753 AA; 81391 MW; 55E4C4169356E4D8 CRC64;
MSQQTGAAPG AGERQLATLE GVLERITYAN EDNGYTVARV DTGRGAGDLL TVVGALLGAQ
VGESLRMEGR WGSHPQYGKQ FTVENYTTVL PATVQGIRRY LGSGLVKGIG PVFADRITQH
FGMDTLTVIE EEPKRLIEVP GLGPKRTKKI ADAWEEQKAI KEVMLFLQTV EVSTSIAVRI
YKKYGDASIS VVKNQPYRLA ADVWGIGFLT ADKIAQSVGI PHDSPERVKA GLQYALSQAT
DQGHCYLPEE RLIADAVKLL QVDTGLVIEC LADLATPPEE GEDDPGVVRE KVPAADGGDP
VTAVYLVPFH RAELSLAAQL TRLLRTGEDR MPAFRDVAWD KALTWLKSRT KAELAPEQEA
AVKLALTEKV AVLTGGPGCG KSFTVRSIVE LARARKAKVV LAAPTGRAAK RLAELTGAEA
STVHRLLELK PGGDAAYDRD RPLDADLVVV DEASMLDLLL ANKLVKAVPP GAHLLFVGDV
DQLPSVGAGE VLRDLLAADS PVPAVRLTRV FRQAQQSGVV TNAHRINAGQ HPLTDGMKDF
FLFVEDDTEE AGRLTVDVAA RRIPARFGLD PRRDVQVLAP MHRGPAGAGA LNGLLQQAVT
PGRPDLPEKR FGGRVFRVGD KVTQIRNNYD KGKNGVFNGT VGVVTSLDPV DQRLTVLTDE
DEEVPYDFDE LDELAHAYAV TIHRSQGSEY PAVVIPVTTG AWMMLQRNLL YTAVTRAKKL
VVLVGSRKAI GQAVRTVSAG RRCTALDFRL ARQ
//
