ID A0A2P8QD95_9ACTN Unreviewed; 854 AA.
AC A0A2P8QD95;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364053};
DE EC=5.6.2.4 {ECO:0000256|RuleBase:RU364053};
GN Name=pcrA {ECO:0000313|EMBL:PSM44206.1};
GN ORFNames=C6Y14_07625 {ECO:0000313|EMBL:PSM44206.1};
OS Streptomyces dioscori.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX NCBI_TaxID=2109333 {ECO:0000313|EMBL:PSM44206.1, ECO:0000313|Proteomes:UP000240429};
RN [1] {ECO:0000313|EMBL:PSM44206.1, ECO:0000313|Proteomes:UP000240429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A217 {ECO:0000313|EMBL:PSM44206.1,
RC ECO:0000313|Proteomes:UP000240429};
RA Zhikuan W.;
RT "Streptomyces dioscori sp. nov., a novel endophytic actinobacterium
RT isolated from bulbil of Dioscorea bulbifera L.";
RL Submitted (MAR-2018) 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}.
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:PSM44206.1}.
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DR EMBL; PYBJ01000003; PSM44206.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8QD95; -.
DR OrthoDB; 4812256at2; -.
DR Proteomes; UP000240429; 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}; Reference proteome {ECO:0000313|Proteomes:UP000240429}.
FT DOMAIN 73..371
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 372..675
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 94..101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 854 AA; 93459 MW; 055DC9107ED12327 CRC64;
MSSLFDDSFL ADLKPSRAHE EEPPPPPEDE APDHGPDDLF GGRFDVPPPS RPRDGYYRDG
APRPLVDPAA LLDGLNENQR AAVVHHGSPL LIVAGAGSGK TRVLTHRIAH LLGERKVHPG
EILAITFTNK AAGEMKERVE QLVGPRANAM WVMTFHSACV RILRRESKKL GFTSSFSIYD
AADSKRLMAL VCRDLDLDPK RFPPKSFSAK ISNLKNELID EEDFAAQASD GFEKTAAQAY
AMYQSRLREA NALDFDDLIM TTVNLLRAFP DVAEHYRRRF RHVLVDEYQD TNHAQYSLVR
ELVGSATDPV AHPEDVPPRE DDLPPAELCV VGDADQSIYA FRGATIRNIL QFEEDYPNAT
TILLEQNYRS TQTILTAANA VIERNESRRP KNLWTNAGAG ARITGYVADT EHDEAQFVAE
EIDRLTDAGD AKAGDVAVFY RTNAQSRVFE EIFIRVGLPY KVVGGVRFYE RKEVRDVLAY
LRVLANPEDS VPLRRILNVP KRGIGDRAEA MIDALSQREK ISFPQALRRV DEAYGMAARS
TNAVKRFNTL MEDLRTIVES GAGPATVVEA ILERTGYLAE LQASTDPQDE TRIENLQELA
SVALEFEQEA AAGGGAAGTA ANEGEAEGEA EAGTPTGLAA FLERVALVAD SDQIPDEDED
GSGVITLMTL HTAKGLEFPV VFLTGMEDGV FPHMRALGQT KELEEERRLA YVGITRARER
LYLTRASMRS AWGQPSYNPP SRFLEEIPEA HLDWKRTGSM GAVASGPVGG VAASLSSSRS
RSAASGASGF ATRRGSSEKP VVSLAVGDRV THDQFGLGTV VGVKGMGANS EATVDFGGEK
PKRLLLRYAP VEKL
//
