ID A0A1N6SUK3_9ACTN Unreviewed; 788 AA.
AC A0A1N6SUK3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364053};
DE EC=5.6.2.4 {ECO:0000256|RuleBase:RU364053};
GN ORFNames=SAMN05421833_102119 {ECO:0000313|EMBL:SIQ44788.1};
OS Microbispora rosea.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Microbispora.
OX NCBI_TaxID=58117 {ECO:0000313|EMBL:SIQ44788.1, ECO:0000313|Proteomes:UP000186096};
RN [1] {ECO:0000313|EMBL:SIQ44788.1, ECO:0000313|Proteomes:UP000186096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12950 {ECO:0000313|EMBL:SIQ44788.1,
RC ECO:0000313|Proteomes:UP000186096};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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}.
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DR EMBL; FTNI01000002; SIQ44788.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1N6SUK3; -.
DR STRING; 58117.SAMN05421833_102119; -.
DR Proteomes; UP000186096; 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}.
FT DOMAIN 39..334
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 335..625
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 711..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..735
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 60..67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 788 AA; 87611 MW; 8B2725CF4D893164 CRC64;
MVRHITLNVT CRASGLRMSV RGHNLRRVST RAATHPLLDG LNPQQRDAVT HQGSPLLIVA
GAGSGKTRVL THRIAYLLAE RGVQPGEILA ITFTNKAARE MKERVDKLIG PRSRAMWVMT
FHSACVRILR REAKRLGFSS SFSIYDQADS QRLMAMVCRE LDLDPKRYPP RSFSAQVSNF
KNELIDYETA ADRASTHLER TLAEAYRTYQ RRLTEAGAMD FDDLIMLTVT LLQLFPDVAE
HYRRRFRHVM VDEYQDTNHA QYTLIRELVG RPEVRTADGD VVREGVEPSE LVVVGDADQS
IYAFRGATIR NILEFERDYP DARTILLEQN YRSTQTILNA ANSVISRNEG RKPKNLWSDQ
GAGPKIIGYA ADNEHDEAMF VAQEVDRLSD DHGVTPGDVA IFYRTNAASR VFEEIFIRTG
LPYKVVGGVR FYERKEVKDL LAYLRVLANP NDTVSLRRIL NVPKRGIGDR AEAMVEAFAN
RERIAFWDAL RRADEAPGVA TRSLNAIRDF VAMLDELRAK ELPLPDLAEE VLSVTGYRTE
LETSGDPQDE SRLENLNELI AVAAEFEEAN PEGTLVDFLE QVSLVADADQ IPGGSGGVVP
PGERAPDGGD HGGVVTLMTL HTAKGLEFPV VFLTGMEDGV FPHMRSLSDP KELEEERRLA
YVGITRAMER LYLSRSAVRS AWGAPSFNPA SRFLSEVPGD LIEWRGDPGK TAWSAATSRP
AARTAPAQKT GGRQIPNLSP GDRVTHDTFG LGTVVAVDGQ AEKTRVKIDF GSEGEKTLLL
AYAPIDKL
//
