ID A0A218QMM9_9CYAN Unreviewed; 774 AA.
AC A0A218QMM9;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364053};
DE EC=5.6.2.4 {ECO:0000256|RuleBase:RU364053};
GN ORFNames=NIES4075_40860 {ECO:0000313|EMBL:GAX43075.1};
OS Tolypothrix sp. NIES-4075.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=2005459 {ECO:0000313|EMBL:GAX43075.1, ECO:0000313|Proteomes:UP000198313};
RN [1] {ECO:0000313|EMBL:GAX43075.1, ECO:0000313|Proteomes:UP000198313}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-4075 {ECO:0000313|EMBL:GAX43075.1,
RC ECO:0000313|Proteomes:UP000198313};
RA Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT "Genome sequencing of cyanobaciteial culture collection at National
RT Institute for Environmental Studies (NIES).";
RL Submitted (JUN-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}.
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:GAX43075.1}.
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DR EMBL; BDUC01000004; GAX43075.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A218QMM9; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000198313; 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:UP000198313}.
FT DOMAIN 9..342
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 343..619
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 30..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 774 AA; 88690 MW; 30EFFE7FEEBB2D46 CRC64;
MTTTIDFLSH LNPSQRQAVE HFCGPLLVVA GAGSGKTRAL TYRIANLILK HRVDPENILA
VTFTNKAARE MKERIQKLFA EQLAMSEYGE RFDLLTEYQQ IELKSKVYRI YIKDLWCGTF
HSLFSRILRF DIEKYQDEKG RRWNRNFSIF DDSDSQSIVK EIVTKQLNLD EKKFEPRSVR
YAISNAKNQG LSPQEFEREN PKYWGRVVAE VYSCYQDKLA QNNALDFDDL ILIPVKLFQQ
NEQVLGYWHR KFRHILVDEY QDTNRTQYDL IRLLVTNGEN SKNNWDWGDR SVFVVGDADQ
SIYSFRMADF TILLEFQQDF GDSLPDEDTR TMVKLEENYR SCENILEAAN QLIENNTQRI
DKILKPTRGA GEQIYCHKAD DEIAEAAFVI NQIRTLERQN PEVNWGNFAI LYRTNAQSRP
FEEALVRAGI PYTIVGGLKF YDRKEIKDVL SYLKAIANPS DTLSLLRVIN TPRRGIGKAT
IDALVNAAQQ LGTTLWEILI DETSVNTLAG RSAKAVNNFA QMIRKLQEQI STVPVSEIVE
KLLEASGYVQ DLQNQGTEEA DNRLLNVKEL YNAVLQFEEE NEDVSLGAFL ESTSLSSDLD
NLKEGQKAVS LMTLHSSKGL EFPVVFLVGL EQGLFPNYRS LDNPTALEEE RRLCYVGITR
AQERLYLSHA RERRLYGNRE PAVRSQFLNE LPEELLTSAH QIKQSFTKTA SVSPGKQQNI
QNWQVGDRVL HKSFGIGEIT HVFGSGNKIS VAIKFTSLGQ KIIDPRVAQL QRVE
//
