ID A0A1C0V192_9CYAN Unreviewed; 1185 AA.
AC A0A1C0V192;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=BCR12_12040 {ECO:0000313|EMBL:OCQ91538.1};
OS Limnothrix sp. P13C2.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pseudanabaenales;
OC Pseudanabaenaceae; Limnothrix.
OX NCBI_TaxID=1880902 {ECO:0000313|EMBL:OCQ91538.1, ECO:0000313|Proteomes:UP000093334};
RN [1] {ECO:0000313|EMBL:OCQ91538.1, ECO:0000313|Proteomes:UP000093334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P13C2 {ECO:0000313|EMBL:OCQ91538.1};
RA Tan B., Te S.H., Gin K., Thompson J.;
RT "Draft genome of Limnothrix sp. P13C2.";
RL Submitted (JUL-2016) 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 -!- 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:OCQ91538.1}.
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DR EMBL; MBRF01000024; OCQ91538.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C0V192; -.
DR STRING; 1880902.BCR12_12040; -.
DR Proteomes; UP000093334; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR038726; PDDEXK_AddAB-type.
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; PF12705; PDDEXK_1; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 2.
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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000093334}.
FT DOMAIN 1..444
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 445..770
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 860..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..883
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..935
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 936..950
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 20..27
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1185 AA; 133080 MW; 9C420A55261DA5DC CRC64;
MLTPDQRRAA EAPQSVAVLA GAGTGKTHML AARYLYHVTA FGCSPIEIVA VTFTRKAAEE
LRSRIRQDLQ QLLATEAAAL ASGHPSALTQ LYDRWPGCDL LADLEAAAVN TFHAVAGQIC
REQAHHLELA PNFTIQEAWE TSLWQKEQLD LALDELPESH YAAVPYSTLR PILEGLLADR
YTAEQALQRD RADWETQVKI WRQAALDRLV NAPSWQSAQQ FLSQWAGRPG DGAEGNRQRI
LELMDAIAQD RDSDQWAAWT KAIDFNKGRG SKKNWDSAEL LESVRAAMKA VRGQINQALK
EGAILCKLGE VDDRFEEKLK TIRQVYVWVR SRLEVAKKQA RIMDFSDLEW YALKALEMPE
VQAYYRQRWQ AFLVDEFQDT NPVQSALLDR LQHDRAKVTI VGDSKQSIYR FRRAEVVLFQ
DWCDRLARAA EGDRVSLSQS FRTHQDLVVA GNALCEPLLN ELHQPLRGDR AEPPLDRPVT
LLAVAATSKA QKVAIRRVAE AQAIGQRLRD WVDRGLLIFD KALGTPRPLE FRDIAILGRT
HRQLSIIAQT LTAAGLPVNL CSGDLLDTRE AKDGTALLRF LADPQDSVAL VTILRSPWFA
VSDRALFAVS RQFPAPEPAT PDGSPAPRRS PNWWAALQEL LTDSATFNQL DEGDQQALKR
AVEQLRRWRG DRRRELPSQL LHRADRATGY SATIANLPDG ARRLRDWRDF ADWIAQLEEG
VGDTFGVVRR LRRIETVRRL NSGDLKTLFA RSPLEAGNAI DLMTIHASKG LEWPVVVLPD
LNPQRDFQQS TSWRMSADLG FVFQWRDQPQ ENPQIPALWH LLAAADREAE QAETRRLLYV
ALTRARDRLL LSANLPWHED KAEKGEKPDK PETSEDETGD RFRPWDWVQG VAQAQGWPID
CVMIPADSPD FPDRPNSTNQ PDPTNPANSQ NPQDPTAPGD RPPTAPRPLP GDGQPLWGWV
SSGLDELPVV ALSEYARCPR RFAWRIVDDH PPSGDGPARS RRIGTLVHRA IERRIQNVAT
LAAQDPGLDL EAVSEALTLA DRFWQDPALV PLSHDPQAQQ EVPIGFDLAL PHGQTLRLNG
VADWVGTAGV LDFKTDRDRV PSEHRLQLWA YAHALGADRA ALVYLRHPDR PIEWFTQPQL
QPLQAQAIEI AQRIRAGQFD PTPGPACQFC PYHDTCDAAP KERST
//
