ID A0A0L8KT19_9ACTN Unreviewed; 747 AA.
AC A0A0L8KT19;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=ADK37_37990 {ECO:0000313|EMBL:KOG29088.1}, AQJ84_37545
GN {ECO:0000313|EMBL:KUN90981.1};
OS Streptomyces resistomycificus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX NCBI_TaxID=67356 {ECO:0000313|EMBL:KOG29088.1, ECO:0000313|Proteomes:UP000037251};
RN [1] {ECO:0000313|EMBL:KOG29088.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRRL 2290 {ECO:0000313|EMBL:KOG29088.1};
RA Tran T., Druce J.;
RT "MeaNS - Measles Nucleotide Surveillance Program.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000037251}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 2290 {ECO:0000313|Proteomes:UP000037251};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KUN90981.1, ECO:0000313|Proteomes:UP000052992}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40133 {ECO:0000313|EMBL:KUN90981.1,
RC ECO:0000313|Proteomes:UP000052992};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces resistomycificus DSM 40133, type
RT strain for the species Streptomyces resistomycificus.";
RL Submitted (OCT-2015) 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:KOG29088.1}.
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DR EMBL; LGUS01000224; KOG29088.1; -; Genomic_DNA.
DR EMBL; LMWZ01000040; KUN90981.1; -; Genomic_DNA.
DR RefSeq; WP_030044220.1; NZ_LGUS01000224.1.
DR AlphaFoldDB; A0A0L8KT19; -.
DR STRING; 67356.AQJ84_37545; -.
DR PATRIC; fig|67356.5.peg.8127; -.
DR eggNOG; COG0507; Bacteria.
DR OrthoDB; 9763659at2; -.
DR Proteomes; UP000037251; Unassembled WGS sequence.
DR Proteomes; UP000052992; 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:KOG29088.1};
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:UP000037251}.
FT DOMAIN 361..542
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 372..376
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 747 AA; 81155 MW; AD185BF20D0F8D53 CRC64;
MAQETASEER RLAVLEGVLE RITYANEENG YTVARVDTGR GAGDLLTVVG ALLGAQVGES
LRMEGRWGSH PQYGKQFTVE NYTTVLPATV QGIRRYLGSG LVKGIGPVFA DRITQHFGLD
TLQVIEEEPK RLIEVPGLGP KRTKKIADAW EEQKAIKEVM LFLQTVEVST SIAVRIYKKY
GDASISVVKN QPYRLAADVW GIGFLTADKI AQSVGIPHDS PQRVMAGLQY ALSQSTDQGH
CYLPEEQLIA DAVKLLQVDT GLVIECLAQL AAPPEEGEDP GVVREKVPGP DGTPVTAVYL
VPFHRAELSL CAQLMRLLRT DQDRMPGFQD VAWDKALGWL KGRTGVELAP EQEAAVRLAL
SKKVAVLTGG PGCGKSFTVR SIVELARAKK AKVVLAAPTG RAAKRLSELT GAEASTVHRL
LELKPGGDAA YDKDRPLDAD LVVVDEASML DLLLANKLVK AVPPGAHLLF VGDVDQLPSV
GAGEVLRDLL AEGGPIPAVR LTRVFRQAQQ SGVVTNAHRI NSGQHPLTDG MKDFFLFVED
DTEEVGRLTV DVAARRIPAK FGLDPRRDVQ VLAPMHRGPA GAGNLNGLLQ QAITPGRPEL
PEKRFGGRVF RVGDKVTQIR NNYEKGTNGV FNGTVGVVTS LDPVDQRLTV RTDEDEEVPY
EFDELDELAH AYAVTIHRSQ GSEYPAVVIP VTTSAWMMLQ RNLLYTAVTR AKKLVVLVGS
RKAIGQAVRT VSAGRRCTTL DFRLSER
//
