ID A0A0B5HTB1_9ACTN Unreviewed; 743 AA.
AC A0A0B5HTB1;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=SVTN_13575 {ECO:0000313|EMBL:AJF65290.1};
OS Streptomyces vietnamensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=362257 {ECO:0000313|EMBL:AJF65290.1, ECO:0000313|Proteomes:UP000031774};
RN [1] {ECO:0000313|EMBL:AJF65290.1, ECO:0000313|Proteomes:UP000031774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GIMV4.0001 {ECO:0000313|Proteomes:UP000031774};
RA Deng M.R., Guo J., Ma L.Y., Feng G.D., Mo C.Y., Zhu H.H.;
RT "Complete genome sequence of Streptomyces vietnamensis strain GIMV4.0001, a
RT genetic manipulable producer of the benzoisochromanequinone antibiotic
RT granaticin.";
RL Submitted (DEC-2014) 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; CP010407; AJF65290.1; -; Genomic_DNA.
DR RefSeq; WP_041129325.1; NZ_CP010407.1.
DR AlphaFoldDB; A0A0B5HTB1; -.
DR STRING; 362257.SVTN_13575; -.
DR KEGG; svt:SVTN_13575; -.
DR HOGENOM; CLU_007524_0_1_11; -.
DR Proteomes; UP000031774; 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; 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:AJF65290.1};
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:UP000031774}.
FT DOMAIN 354..551
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 365..369
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 743 AA; 79990 MW; 4C7D2A06A2B4EB86 CRC64;
MSNEGQPYRP AVVEGVLERI TYANEESGYT VARVDTGRGA GDLLTVVGAL LGAQPGESLR
MEGRWGSHPQ YGKQFTVDNY TTVLPATIQG IRRYLGSGLV KGIGPVFADR ITQHFGLDTL
DILEEAPARL IEVPGLGPKR TKNITAAWEE QKAIKEVMVF LQGVGVSTSI AVRIYKKYGD
ASISVVRNQP YRLAADVWGI GFLTADKIAQ SVGIPHDSPD RVKAGLQYAL SQSSDQGHCF
LPEERLIADA VKLLQVDTGL VIECLGELAD DPEGVVREVV PGPEGAPVTA VYLIPFHRAE
LSLAGQLRRL LRTEEDRMPA FQDVAWDKAL AWLADRTGAS LAPEQEEAVR LALTRKVAVL
TGGPGCGKSF TVRSIVELAR AKKAKVVLAA PTGRAAKRLA ELTGAEASTV HRLLELKPGG
DAAYDRDRPL DADLIVVDEA SMLDLLLANK LVKAVAPGAH LLLVGDVDQL PSVGAGEVLG
DLLAPGSPVP SVRLTRIFRQ AQQSGVVTNA HRINAGTPPL TQGLPDFFLF VEEETEDAAR
VTVDVAARRI PAKFGLDPRR DVQVLAPMHR GPAGAGSLNG LLQQAITPAR PDLPEKRFGG
RVFRVGDKVT QIRNNYEKGA NGVFNGTVGV VTALDTVEQR LTVRTDEDEE VAYDFDELDE
LAHAYAVTIH RSQGSEYPAV VIPVTMSAWM MLQRNLLYTA VTRARKLVVL VGSRRAIAQA
VRTVSAGRRF TALAHRLAGS ALV
//
