ID F3Z797_9ACTN Unreviewed; 777 AA.
AC F3Z797;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
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=STTU_4463 {ECO:0000313|EMBL:EGJ77252.1};
OS Streptomyces sp. Tu6071.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=355249 {ECO:0000313|EMBL:EGJ77252.1};
RN [1] {ECO:0000313|EMBL:EGJ77252.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tu6071 {ECO:0000313|EMBL:EGJ77252.1};
RA Erxleben A., Wunsch-Palasis J., Gruening B.A., Luzhetska M., Bechthold A.,
RA Gunther S.;
RT "Genome sequence of Streptomyces sp. Tu6071.";
RL Submitted (APR-2011) 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; CM001165; EGJ77252.1; -; Genomic_DNA.
DR RefSeq; WP_007826794.1; NZ_CM001165.1.
DR AlphaFoldDB; F3Z797; -.
DR HOGENOM; CLU_007524_0_3_11; -.
DR Proteomes; UP000003955; 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; PF13604; AAA_30; 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};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01488};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01488}.
FT DOMAIN 361..558
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 739..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 372..376
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01488"
SQ SEQUENCE 777 AA; 83389 MW; 011EADDD6A29BAD9 CRC64;
MAPSTPGDQA RATASPLAVL EATLERITFA SEENGFTVAR VDTGRGGGDL LTVVGALLGA
QPGEALRMRG RWGSHPRHGK QFVVENYTTV LPATIQGIRR YLGSGLVKGI GPVFADRVTR
HFGTDTLDVI EHEPKRLIEV KGLGPKRVAK IIAAWEEQKA IKEVMVFLQS VEVSTSIAVR
IYKKYGDDSI EVVKAEPYRL AADVWGIGFL TADRIARAVG IPEDSPERVK AGLQYALSQA
TDQGHCYLPE ERLISDAVKL LGVDTGLVIE CLGELAEDPE GVVRERLTDP DGQPVTGVYL
VPFHRAELSL AGQVRRLLTA PEDRLAGFQD VDWGPALGWL ARKTGTTLAP EQEAAVRLAL
TRKVAVLTGG PGCGKSFTVR SVVELARARR AKVVLAAPTG RAAKRLAELT GAEASTVHRL
LELKPGGDAA YDRDRPLDAD LVVVDEASML DLLLANKLVK AVAPGAHLLL VGDVDQLPSV
GAGEVLRDLL SEGGPVPAVR LTRIFRQARE SGVVTNAHRI NEGQHPVTQG LKDFFLFVEE
DTEAAGRLTV DVVARRIPAR FGLDPRTDVQ VLAPMHRGPA GAGTLNALLQ QALTPPGPRT
EEKRFGGRVF RVGDKVTQIR NNYEKGENGV FNGTVGVVTG LDTVEQRLTV RTDEDEDVVY
EFDELDELAH AYAMTIHRSQ GSEYPAVVVP VTTSAWTMLQ RNLLYTAVTR AKRLVVLVGS
RRALGQAIRT VSAGRRHTGL AGRLRAPEVP GQRAAGPGQR GAGGGAGAES PASHSSR
//
