ID A0A0M2RI86_9ACTN Unreviewed; 1065 AA.
AC A0A0M2RI86;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=LQ51_28580 {ECO:0000313|EMBL:KKJ94105.1};
OS Micromonospora sp. HK10.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1538294 {ECO:0000313|EMBL:KKJ94105.1, ECO:0000313|Proteomes:UP000034330};
RN [1] {ECO:0000313|EMBL:KKJ94105.1, ECO:0000313|Proteomes:UP000034330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HK10 {ECO:0000313|EMBL:KKJ94105.1,
RC ECO:0000313|Proteomes:UP000034330};
RA Talukdar M., Das D., Borah C., Deka Boruah H.P., Bora T.C., Singh A.K.;
RT "Draft genome sequence of Micromonospora HK10, isolated from Kaziranga
RT National park, Assam, India.";
RL Submitted (NOV-2014) 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 -!- 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}.
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:KKJ94105.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JTGL01000235; KKJ94105.1; -; Genomic_DNA.
DR RefSeq; WP_046563736.1; NZ_KQ058712.1.
DR AlphaFoldDB; A0A0M2RI86; -.
DR STRING; 1538294.LQ51_28580; -.
DR PATRIC; fig|1538294.3.peg.1333; -.
DR HOGENOM; CLU_005571_0_0_11; -.
DR OrthoDB; 4812256at2; -.
DR Proteomes; UP000034330; 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; cd19067; PfuEndoQ-like; 1.
DR CDD; cd18807; SF1_C_UvrD; 1.
DR Gene3D; 1.10.10.160; -; 2.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
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; IPR016195; Pol/histidinol_Pase-like.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF00580; UvrD-helicase; 2.
DR Pfam; PF13361; UvrD_C; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF89550; PHP domain-like; 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}.
FT DOMAIN 515..749
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 750..1013
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 455..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..476
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..498
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 536..543
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1065 AA; 115707 MW; 2B86C024702A1FE8 CRC64;
MPPFSAAPPG GLPPFVADLH IHSKYSRACS RDLTLPNLGW WARRKGVGVL GTGDFTHPAW
YDHLRETLHP AEPGLYRLSP EAERDIARRL PPRLAAGAEA DPVRFMLSVE ISTIYKRDDR
TRKVHHLIYL PDLAAVARFN AALGRIGNLG SDGRPILGLD SRDLLEITLE ASPDGYLVPA
HIWTPWFSAL GSKSGFDAIA DCYADLAGHV FAVETGLSSD PEMNWRVGSL DRYQLVSNSD
AHSPPALARE ATVFHSARDY FAIREALRTG DGLAGTIEFF PEEGKYHADG HRLCGVNWSP
ERTRQAGGRC PECGKPLTVG VLSRVEELAD RPAGHRPGHA RAVTHLVPLA ELLGEINKVG
ARSKKVEGRL NELVAALGPE LEILTSTPLD EIGRVGGELL AEGIGRLRRG EVRRIPGYDG
EYGVITLFDP AELGGAGGGA SGGQETLFDV PVPAQRKPAE PAARPKARRA AAVKAEPKRK
PAPPPAPPIA PAPSPHEPFE PMLAGMEEVG TGLLDRLDAM QRVAASAPGG PLLIVAGPGT
GKTRTLTHRI AYLCAELNVF PEQCLAITFT RRAAEELRHR LDGLLGPVAE DVTVGTFHSL
GLTILRENAA AAGLPADFRI ADDTDRAATR AEAGADDERY TALLRKHDLV DLDELLTVPV
ALLKADRKLV REYRDRWKWI FVDEYQDVDA VQYELLRLLS PADGNLCAIG DPDQAIYSFR
GADVGYFLRF SQDFTDARLV RLNRNYRSSA PILAAAVQAI APSSLVRGRR LDPARLDPEA
PLVGRYAAAS VADEADFVVR TIDELVGGLS HRSLDSGRID GRSTSLSFSD IAVLYRTDSQ
AAPVVDALAR ANIPVQKRSH DRLRDRPGVP AIARELRHAG LDGSLPARVR LAGQVLAERF
AVPTLDGSGA VRPEDVRTAV DLLTPLARRC GDDLGLFLSQ LATGAEVDAL DPRAEAVTLL
TLHAAKGLEF PVVFLVGAED GLLPLRWPGQ EPGEDAVAEE RRLFFVGLTR AQDRLYVSHA
ARRSRHGTER DCRPSPFLDV IDPGLFERFG EAETRRPRDR QLRLI
//
