ID W7IRU7_9PSEU Unreviewed; 692 AA.
AC W7IRU7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=UO65_1622 {ECO:0000313|EMBL:EWC63058.1};
OS Actinokineospora spheciospongiae.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinokineospora.
OX NCBI_TaxID=909613 {ECO:0000313|EMBL:EWC63058.1, ECO:0000313|Proteomes:UP000019277};
RN [1] {ECO:0000313|EMBL:EWC63058.1, ECO:0000313|Proteomes:UP000019277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EG49 {ECO:0000313|EMBL:EWC63058.1,
RC ECO:0000313|Proteomes:UP000019277};
RX PubMed=24604655;
RA Harjes J., Ryu T., Abdelmohsen U.R., Moitinho-Silva L., Horn H., Ravasi T.,
RA Hentschel U.;
RT "Draft Genome Sequence of the Antitrypanosomally Active Sponge-Associated
RT Bacterium Actinokineospora sp. Strain EG49.";
RL Genome Announc. 2:e00160-14(2014).
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:EWC63058.1}.
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DR EMBL; AYXG01000057; EWC63058.1; -; Genomic_DNA.
DR RefSeq; WP_035280098.1; NZ_AYXG01000057.1.
DR AlphaFoldDB; W7IRU7; -.
DR STRING; 909613.UO65_1622; -.
DR PATRIC; fig|909613.9.peg.1635; -.
DR eggNOG; COG0210; Bacteria.
DR OrthoDB; 9806690at2; -.
DR Proteomes; UP000019277; 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:InterPro.
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|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:UP000019277}.
FT DOMAIN 12..292
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 293..541
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT DOMAIN 618..692
FT /note="HRDC"
FT /evidence="ECO:0000259|PROSITE:PS50967"
FT BINDING 33..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 692 AA; 75734 MW; 65337C261FD124FC CRC64;
MAGEHRPTDL LAGLDPDQLA AVRAPRGPVC VLAGAGTGKT RTIVSRIAAL VRAGHVTAGQ
VLAVTFTTRA AGEMRTRLRA MDVHGAQART FHAAAWKQLR YFWPRVVGDA PWDLLDGKLR
LVGQAAHRAG TGTEREALRD LAGEIEWAKA SLIGPEDYPA AAARARRDPP AAPELVAKVY
AGYEALKNDA RVLDFDDLLL HTAAALEEHS AVAEEFRDRY RCFVVDEYQD VTPLQQRVLD
AWLGERDDLT VVGDANQTIY SFAGASPRPL LDFTRRFPEA TVVRLERDYR STPEVVSLAN
RVIGAARDRP AGSRLRLIGQ RPPGPNPRFA EYDDEPAEAA AVAARIRELV DGGVALSEVA
VLFRVNAQSE VYEQALTELD IPYLVRGGER FFARQEVRQA MAALRTAAGS DPGGELPALV
RALLVPLGLT EEPPPGGRQR ERWESLLALV ELAEELVATE PGADLRRYAA ELEQRAQSQH
PPTVEGVTLA SLHAAKGLEW DAVFLVGLVE GTMPIQHADG DDAAIEEERR LLYVGVTRAR
VHLSLTWALA RAEGGKRYRR RSRFLYGVIP DNDPASRPAA SRQREQRVVE RPRFCRVCGD
QLHGVMPTKL GRCSDCPADL DEGLLDRLRE WRMERSKALR VPAYVIFTDA TLLAIAEQRP
ADRAALVAIS GIGASKLDKF GSEVLSLVTG AN
//
