ID A0A3N1A4Z5_9ACTN Unreviewed; 783 AA.
AC A0A3N1A4Z5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364053};
DE EC=5.6.2.4 {ECO:0000256|RuleBase:RU364053};
GN ORFNames=EDC02_6640 {ECO:0000313|EMBL:ROO51754.1};
OS Micromonospora sp. Llam0.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=2485143 {ECO:0000313|EMBL:ROO51754.1, ECO:0000313|Proteomes:UP000275308};
RN [1] {ECO:0000313|EMBL:ROO51754.1, ECO:0000313|Proteomes:UP000275308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Llam0 {ECO:0000313|EMBL:ROO51754.1,
RC ECO:0000313|Proteomes:UP000275308};
RA D'Agostino P.;
RT "Genome mining of underrepresented organisms for secondary metabolites.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034618,
CC ECO:0000256|RuleBase:RU364053};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC translocating in the 3'-5' direction.; EC=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034617};
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000256|ARBA:ARBA00009922, ECO:0000256|RuleBase:RU364053}.
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:ROO51754.1}.
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DR EMBL; RJJY01000002; ROO51754.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N1A4Z5; -.
DR Proteomes; UP000275308; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:InterPro.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR CDD; cd18807; SF1_C_UvrD; 1.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR005751; ATP-dep_DNA_helicase_PcrA.
DR InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR NCBIfam; TIGR01073; pcrA; 1.
DR PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF21196; PcrA_UvrD_tudor; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; DNA-binding {ECO:0000256|RuleBase:RU364053};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000275308}.
FT DOMAIN 18..303
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 304..587
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 39..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 783 AA; 85449 MW; 22D22FADDB915305 CRC64;
MAGRGPAEPN LAGAALLTGL NGPQREAVTH AGGPLLIVAG AGSGKTKVLT HRIAYLLAAR
QTHPGEVLAI TFTNKAAGEL KERVGNLVGP RARMMWVSTF HSACVRILRA EHEHAGLKST
FSIYDADDSR RLMQLVAREL DLDPKRYPAR GLATQVSNLK NELVDPETFT DRAAGPNERA
LAEAYTLYQR RLREAHALDF DDLIMTTVHL LQAHPHVAGS YRRRFRHVLV DEYQDTNHAQ
YQLVKELVGD GSDDVPPGEL CVVGDADQSI YAFRGATIRN ILEFERDFAQ AKTILLEQNY
RSTQTILTAA NAVITNNAGR KPKRLWSDQG DGEPIVGYVA DTEHAEADWA ARQIDRLCDD
GAARPGDMAV FYRTNAQSRV FEEVFIRVGL PYKVVGGVRF YERKEVRDAL AYLRAVVNAD
DTVSIRRVLN TPRRGIGDRA EACVEALAAR ERISFGAALG RAAEAPGIST RAVNAIADFV
ALLDGVREQL ATTTPEEALE SVLLRSGYLT ELEESLDPQD AGRVENLQEL VSVAREYTER
VEASDEPATV AGFLEQVALV ADADQVPDDD PDHQGVVTLM TLHTAKGLEF PVVFLTGLED
GVFPHLRALG DTGELEEERR LAYVGITRAR QRLFLSRSVT RAAWGQPAYN PPSRFLSELP
AELVRWERTE AAYTSWSGTG GGVGGRSAAA DRSPVARGGG FAGGTPKAAR LAQRLGVDPS
RLSTASELPT APKLTVGERV NHQRYGLGRV LAVEGHGPGA RAQVDFGDQR MWLVLRHAPI
EKI
//
