ID A0A0G2HLS0_9SYNE Unreviewed; 472 AA.
AC A0A0G2HLS0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Replicative DNA helicase {ECO:0000256|ARBA:ARBA00021957, ECO:0000256|RuleBase:RU362085};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551, ECO:0000256|RuleBase:RU362085};
GN ORFNames=TE42_03340 {ECO:0000313|EMBL:KKZ12713.1};
OS Candidatus Synechococcus spongiarum SP3.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=1604020 {ECO:0000313|EMBL:KKZ12713.1, ECO:0000313|Proteomes:UP000035067};
RN [1] {ECO:0000313|EMBL:KKZ12713.1, ECO:0000313|Proteomes:UP000035067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP3 {ECO:0000313|EMBL:KKZ12713.1};
RA Burgsdorf I., Slaby B.M., Handley K.M., Haber M., Blom J., Marshall C.W.,
RA Gilbert J.A., Hentschel U., Steindler L.;
RT "Lifestyle Evolution in Cyanobacterial Symbionts of Sponges.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Participates in initiation and elongation during chromosome
CC replication; it exhibits DNA-dependent ATPase activity.
CC {ECO:0000256|RuleBase:RU362085}.
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=3.6.4.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001665,
CC ECO:0000256|RuleBase:RU362085};
CC -!- SIMILARITY: Belongs to the helicase family. DnaB subfamily.
CC {ECO:0000256|ARBA:ARBA00008428, ECO:0000256|RuleBase:RU362085}.
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:KKZ12713.1}.
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DR EMBL; JXQG01000013; KKZ12713.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2HLS0; -.
DR PATRIC; fig|1604020.3.peg.2418; -.
DR Proteomes; UP000035067; Unassembled WGS sequence.
DR GO; GO:1990077; C:primosome complex; IEA:UniProtKB-UniRule.
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-UniRule.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-UniRule.
DR CDD; cd00984; DnaB_C; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR036185; DNA_heli_DnaB-like_N_sf.
DR InterPro; IPR007692; DNA_helicase_DnaB.
DR InterPro; IPR007694; DNA_helicase_DnaB-like_C.
DR InterPro; IPR007693; DNA_helicase_DnaB-like_N.
DR InterPro; IPR016136; DNA_helicase_N/primase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00665; DnaB; 1.
DR PANTHER; PTHR30153:SF2; REPLICATIVE DNA HELICASE; 1.
DR PANTHER; PTHR30153; REPLICATIVE DNA HELICASE DNAB; 1.
DR Pfam; PF00772; DnaB; 1.
DR Pfam; PF03796; DnaB_C; 1.
DR SUPFAM; SSF48024; N-terminal domain of DnaB helicase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51199; SF4_HELICASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362085};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|RuleBase:RU362085};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU362085};
KW Helicase {ECO:0000256|RuleBase:RU362085, ECO:0000313|EMBL:KKZ12713.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362085};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362085}; Primosome {ECO:0000256|RuleBase:RU362085}.
FT DOMAIN 208..472
FT /note="SF4 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51199"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 472 AA; 51941 MW; 46F03B309CEB3D64 CRC64;
MVTAAPSNPQ QPRDLSLPRP SGDGAPTGGN PFNALPNQVP PQNLEAEEAV LGGILLDPDA
MGRVADILHP DAFYVAAHRE IFRTALALYS QNKPTDLTSM TAWLADAGHL DKVGGGMRLA
QLLERIIGTA AIDQYAQLVM DKYLRRQLIK AGNDVMELGF DQRRPLGGLL DEAEQKIFSV
SKERPQGGLV ATAEILTSTF NEIESRSMGD SVAGIPVNFY DLDAVTQGLQ RSDLIIVAGR
PAMGKTSIVL SMAKNVAALH QLPVCMFSLE MSKEQLTYRL LSMETGIEGG RLRTGRLNHQ
EWPLLGQGIS SLSQLPIFID DKPNSGVMEM RSLCRQLMAQ QRRDLGMVVV DYLQLMEGSN
SDNRAQDLSV ITRGLKQLAR ELEVPVIALS QLNRGVESRT NKRPMLSDLR ESGSIEQDAD
LVLMIYRDEY YNPETSDKGL AEVIVTKHRN GPVGTVKLLF ESQYTRFRNL AT
//
