ID B8HS23_CYAP4 Unreviewed; 1272 AA.
AC B8HS23;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 88.
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 OrderedLocusNames=Cyan7425_0288 {ECO:0000313|EMBL:ACL42682.1};
OS Cyanothece sp. (strain PCC 7425 / ATCC 29141).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Gomontiellales; Cyanothecaceae;
OC Cyanothece.
OX NCBI_TaxID=395961 {ECO:0000313|EMBL:ACL42682.1};
RN [1] {ECO:0000313|EMBL:ACL42682.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PCC 7425 {ECO:0000313|EMBL:ACL42682.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Meineke L., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ovchinnikova G., Liberton M., Stoeckel J., Banerjee A., Singh A., Page L.,
RA Sato H., Zhao L., Sherman L., Pakrasi H., Richardson P.;
RT "Complete sequence of chromosome Cyanothece sp. PCC 7425.";
RL Submitted (JAN-2009) 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|ARBA:ARBA00002835, 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}.
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DR EMBL; CP001344; ACL42682.1; -; Genomic_DNA.
DR AlphaFoldDB; B8HS23; -.
DR STRING; 395961.Cyan7425_0288; -.
DR KEGG; cyn:Cyan7425_0288; -.
DR eggNOG; COG0305; Bacteria.
DR eggNOG; COG1372; Bacteria.
DR HOGENOM; CLU_005373_2_1_3; -.
DR OrthoDB; 9773982at2; -.
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:0004519; F:endonuclease activity; IEA:InterPro.
DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-UniRule.
DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR CDD; cd00081; Hint; 4.
DR Gene3D; 2.170.16.10; Hedgehog/Intein (Hint) domain; 4.
DR Gene3D; 3.10.28.10; Homing endonucleases; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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; IPR003586; Hint_dom_C.
DR InterPro; IPR003587; Hint_dom_N.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR027434; Homing_endonucl.
DR InterPro; IPR006142; INTEIN.
DR InterPro; IPR030934; Intein_C.
DR InterPro; IPR004042; Intein_endonuc.
DR InterPro; IPR006141; Intein_N.
DR InterPro; IPR004860; LAGLIDADG_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00665; DnaB; 1.
DR NCBIfam; TIGR01443; intein_Cterm; 2.
DR NCBIfam; TIGR01445; intein_Nterm; 2.
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; 3.
DR Pfam; PF14890; Intein_splicing; 2.
DR Pfam; PF14528; LAGLIDADG_3; 2.
DR PRINTS; PR00379; INTEIN.
DR SMART; SM00305; HintC; 2.
DR SMART; SM00306; HintN; 2.
DR SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 2.
DR SUPFAM; SSF55608; Homing endonucleases; 2.
DR SUPFAM; SSF48024; N-terminal domain of DnaB helicase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50818; INTEIN_C_TER; 2.
DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 2.
DR PROSITE; PS50817; INTEIN_N_TER; 2.
DR PROSITE; PS51199; SF4_HELICASE; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362085};
KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
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:ACL42682.1};
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};
KW Protein splicing {ECO:0000256|ARBA:ARBA00023000};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 331..448
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000259|PROSITE:PS50819"
FT DOMAIN 590..612
FT /note="Intein C-terminal splicing"
FT /evidence="ECO:0000259|PROSITE:PS50818"
FT DOMAIN 612..780
FT /note="SF4 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51199"
FT DOMAIN 894..1043
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000259|PROSITE:PS50819"
FT DOMAIN 1188..1210
FT /note="Intein C-terminal splicing"
FT /evidence="ECO:0000259|PROSITE:PS50818"
FT DOMAIN 1210..1270
FT /note="SF4 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51199"
SQ SEQUENCE 1272 AA; 142107 MW; FC89F75F9EB238A3 CRC64;
MHDLNFQVAA DRLPPQNVEA EEAILGGILL DPEAIGRVAD ILRPEAFYLS AHQEIYRAAL
ALNAQGSPTD LMCIAAWLQD QDLLAKVGGQ SKLAQLVDRT VSAVNIDQYA QLIKDKYLRR
QLIKVATDVS QMAYETTKPL DSILDQAEQK VFSVTQDRVQ QGLVSTEDIL AQTFNELEQR
SLGNVLPGLS CNFYDLDAMT QGFQRSDLVI VAGRPSMGKC LVADSEILLA DGRLVTIAQI
YQQKQAQLLT LQQNWKFGLT WASDFVDDGI KPVFRVTTRL GRTVTTTLSH PFLTIKGWRP
LGELQTGTKI AVPRKLAVFG NETLRECELK ILGYLLGDGC LTKTCPEFTN SNPLLQQDFQ
TAVTEFGQDG LTFWLKKLEL WGKGAHTKFI PAVIFQLQRS QIALFLNRLF ATDGWATVLA
SGQSQLGFAT VSEKLARQVQ HLLLRFGIIA TLKHRQVKYQ DHRRQAWQLD ITDHLSIKSF
IDEIGIFGKE AALARVKEAL AGRKYQTNTD LIPIEAWERV KTAKGDQTWV SIAEKAGING
TNLHVDRGSF SRERLWKLAT ALENLSLQQL ADSEVYWDEI VAIEPVGEQQ VYDLTIPDTH
NFVANDICVH NTALSLQIAR RIAEIHKLGV AVFSLEMSKE QLVQRLLASE SRIDSNYLRA
GRISQNQWEP ISRAIGSLSQ LPIYIDDTPN PTLGEIRSNA RRLMAERPEG LGLILLDYLQ
LMGGGDATDG RVQELSKITR SLKGLARELN VPVIALSQLS RGVESRTNKR PLMSDLRESG
CLTGDSLITL ADTGKQVPLR QLIGQSGFAV WALNQSTLKL ERAIVSHAFA TGTKPVFRLQ
TALGRAIRAT GNHKFLTITG WKRLDELQPG ERIALPRKIP SPDLQLMDDH ELALLGHLIG
DGCTLPRHSI QYTTRELDLA EMVSSLATKV FGKSLNPRIN PEKKWYQVYL TSNQSLAPGL
KNPVTKWLEH LGIFGLRSYE KFIPDQVFEQ PPAAIALFLR HLWSTDGCIR PSKKGIVYPA
IYYATSSERL ARDVQSLLLR LSINGRLLVS SQAGKGRDQY HVWVSGKSDI EKFVQQVGAV
GQYKTASLEE VKTRLEASVA NTNRDIIPYT VWRSCAVPAM QRLGITGREM QKALGNAYCG
TSLYKQNLSR ERASRLAAIV NCETIAQLAD SDVYWDEVIS ITQDGSEDVF DLTVPEHHNF
VVNNIIVHNS IEQDADLIIL LYRDEYYNPD TPDRGICELI IAKHRNGPVG TVKLLFDPQY
TRFENLAQGR DR
//
