ID A0A0T1SR38_9ACTN Unreviewed; 742 AA.
AC A0A0T1SR38;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=ASD33_00065 {ECO:0000313|EMBL:KQX58750.1};
OS Streptomyces sp. Root1304.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1736450 {ECO:0000313|EMBL:KQX58750.1, ECO:0000313|Proteomes:UP000051136};
RN [1] {ECO:0000313|Proteomes:UP000051136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1304 {ECO:0000313|Proteomes:UP000051136};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQX58750.1, ECO:0000313|Proteomes:UP000051136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1304 {ECO:0000313|EMBL:KQX58750.1,
RC ECO:0000313|Proteomes:UP000051136};
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:KQX58750.1}.
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DR EMBL; LMEP01000001; KQX58750.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T1SR38; -.
DR STRING; 1736450.ASD33_00065; -.
DR Proteomes; UP000051136; 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 CDD; cd18807; SF1_C_UvrD; 1.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 1.10.150.80; HRDC domain; 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; IPR010997; HRDC-like_sf.
DR InterPro; IPR002121; HRDC_dom.
DR InterPro; IPR044876; HRDC_dom_sf.
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; PF00570; HRDC; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 2.
DR SMART; SM00341; HRDC; 1.
DR SUPFAM; SSF47819; HRDC-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50967; HRDC; 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:KQX58750.1};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00560};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}.
FT DOMAIN 38..318
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 319..574
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT DOMAIN 660..740
FT /note="HRDC"
FT /evidence="ECO:0000259|PROSITE:PS50967"
FT REGION 611..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 59..66
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 742 AA; 80853 MW; 0EF2EF6087E4A5EA CRC64;
MDKPPRRVRP TWQHWGVTAA THSTLFPQVP ETADAVLDGL DPEQREVALA LTGPVCVLAG
AGTGKTRAIT HRIAYGVRSG RLQPASVLAV TFTNRAAGEM RGRLRQLGAG GVQARTFHAA
ALRQLQFFWP KAVGGDLPRL LERKIQLVAD AAARCRVRLD RNELRDVTGE IEWAKVTQTV
PADYPAVVAK SLRDAPRDPA EISQIYAMYE QLKRDRSVID FEDVLLLTVG ILQDRHDIAD
QIRSQYQHFV VDEYQDVSPL QQRLLDLWLG DRDNLCVVGD ASQTIYSFTG ATPDHLLNFR
TRHPGATMVK LVRDYRSTPQ VVHLANGLLS QARGRAADHR LELISQRDPG PEPVYTEYAD
EPTEAEGTAR RIRDLIAAGV PAGEIAVLYR INAQSEVYEQ ALADAGVPYQ LRGAERFFER
QEVREAGIAL RGAARAGGND SLLDDAEDLP AQVRAVLSTK GWSTRPPAGS GAVRDRWESL
AALVRLAEDF ARAKRGATLS DLVAELDERA AAQHAPTVQG VTLASLHAAK GLEWDAVFLV
GLTEGMLPIT YAKTDEQVEE ERRLLYVGVT RARLHLTLSW ALARSPGGRA SRRPSRFLKG
LRPGSGSLGT VASGGAGSFG RGSGTAGRRK PRGPALCRVC GTTLTEAGAM KLMRCEDCPS
DMDEGLYERL REWRTEQARE LGQPGYCVFT DKTLMAIAER IPTTGGELSM ISGVGARKLD
RFGADVLAIC AGEDSGAGDD ED
//