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Database: UniProt
Entry: A0A0Q5L2Y2_9MICO
LinkDB: A0A0Q5L2Y2_9MICO
Original site: A0A0Q5L2Y2_9MICO 
ID   A0A0Q5L2Y2_9MICO        Unreviewed;       563 AA.
AC   A0A0Q5L2Y2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   ORFNames=ASF82_09540 {ECO:0000313|EMBL:KQR44733.1};
OS   Frigoribacterium sp. Leaf164.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Frigoribacterium.
OX   NCBI_TaxID=1736282 {ECO:0000313|EMBL:KQR44733.1, ECO:0000313|Proteomes:UP000051005};
RN   [1] {ECO:0000313|EMBL:KQR44733.1, ECO:0000313|Proteomes:UP000051005}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf164 {ECO:0000313|EMBL:KQR44733.1,
RC   ECO:0000313|Proteomes:UP000051005};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQR44733.1, ECO:0000313|Proteomes:UP000051005}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf164 {ECO:0000313|EMBL:KQR44733.1,
RC   ECO:0000313|Proteomes:UP000051005};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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   -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC       {ECO:0000256|ARBA:ARBA00009922}.
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:KQR44733.1}.
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DR   EMBL; LMOX01000003; KQR44733.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q5L2Y2; -.
DR   STRING; 1736282.ASF82_09540; -.
DR   Proteomes; UP000051005; Unassembled WGS sequence.
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   CDD; cd17932; DEXQc_UvrD; 1.
DR   Gene3D; 1.10.10.160; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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   PANTHER; PTHR11070:SF45; ATP-DEPENDENT DNA HELICASE UVRD2; 1.
DR   PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 2.
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};
KW   Helicase {ECO:0000256|PROSITE-ProRule:PRU00560,
KW   ECO:0000313|EMBL:KQR44733.1};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00560};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000051005}.
FT   DOMAIN          2..282
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          283..524
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   REGION          532..563
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        541..555
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         23..30
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   563 AA;  61940 MW;  4FE3A8F3CCD128E2 CRC64;
     MAGLDEQQRE AARRLLGPVC LLAGAGTGKT RAITHRIAYG VATGVYAPNR VMALTFTSRA
     AAELRGRLRH LGAGGVSART FHASALSQLS YFWPQTMGGQ MPRLLDGKGK LLAHAAERLR
     LKLDTASLRD MAGEIEWRKV SRLTMDEYAL KVPSRSLPQS VSVEAALDLH AAYEDIKDER
     RQLDFEDVLL ATVGMLELEP RVAQQVREQY RFFVVDEYQD VSPLQQHLLE LWLGDRNDLC
     VVGDASQTIY SFAGASADYL LGFGSRYDDA TVVRLEQNYR SSRQIVDTAN QLMRGRPGAL
     HLHPAVETTG PVPPVTQYPT DMAEARGVAQ TIADEIASGV APEEIAVLYR VNVQAAALER
     ALSDVGVSTR VQGATRFFEL REVKEALMML KGAAVSIVGE PLFKTVSDVL RSLGWTQEAP
     EQRGAVRDRW ESLNALMGLA EASPPDTTLR QFVDELFARQ QGQHEPTMAA VTLATLHSAK
     GLEWRSVYLV GLSEGLVPIS YAQGLEAIDE ERRLLYVGVT RARERLRLSW GAAGQGRGGE
     RRPSRFLEEL RTRSRDAASS TSA
//
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