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Database: UniProt
Entry: K9X7Q1_9NOST
LinkDB: K9X7Q1_9NOST
Original site: K9X7Q1_9NOST 
ID   K9X7Q1_9NOST            Unreviewed;       451 AA.
AC   K9X7Q1;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 51.
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=Cylst_6281 {ECO:0000313|EMBL:AFZ28518.1};
OS   Cylindrospermum stagnale PCC 7417.
OG   Plasmid pCYLST.02 {ECO:0000313|EMBL:AFZ28518.1,
OG   ECO:0000313|Proteomes:UP000010475}.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae;
OC   Cylindrospermum.
OX   NCBI_TaxID=56107 {ECO:0000313|EMBL:AFZ28518.1, ECO:0000313|Proteomes:UP000010475};
RN   [1] {ECO:0000313|EMBL:AFZ28518.1, ECO:0000313|Proteomes:UP000010475}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7417 {ECO:0000313|EMBL:AFZ28518.1,
RC   ECO:0000313|Proteomes:UP000010475};
RC   PLASMID=Plasmid pCYLST.02 {ECO:0000313|Proteomes:UP000010475};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA   Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA   Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA   Pitluck S., Woyke T., Kerfeld C.;
RT   "Finished plasmid 2 of genome of Cylindrospermum stagnale PCC 7417.";
RL   Submitted (JUN-2012) 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}.
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DR   EMBL; CP003644; AFZ28518.1; -; Genomic_DNA.
DR   RefSeq; WP_015186415.1; NC_019744.1.
DR   AlphaFoldDB; K9X7Q1; -.
DR   KEGG; csg:Cylst_6281; -.
DR   PATRIC; fig|56107.3.peg.7295; -.
DR   eggNOG; COG0305; Bacteria.
DR   HOGENOM; CLU_005373_0_0_3; -.
DR   OrthoDB; 9773982at2; -.
DR   Proteomes; UP000010475; Plasmid pCYLST.02.
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:AFZ28518.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362085};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU362085}; Plasmid {ECO:0000313|EMBL:AFZ28518.1};
KW   Primosome {ECO:0000256|RuleBase:RU362085};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010475}.
FT   DOMAIN          169..450
FT                   /note="SF4 helicase"
FT                   /evidence="ECO:0000259|PROSITE:PS51199"
SQ   SEQUENCE   451 AA;  49966 MW;  7040EED2B00C7114 CRC64;
     MIDKLPPQNI EAEEAILGGI MLDPEAIGRV SDRLVPEAFY ISTHKDIYQA ALRLHCSGKP
     TDLLTVTAWL TDHDLLVRIG GRNKLATLVD RTVSAINIDA LAELVMDKFA RRQLIKAGNE
     IVHLGYETET ELPKILDQSE QKVFQLSNQT LSSNTEHNST INVAAYEDLN SGNPIYPTGL
     HELDNLMVGF ESGTLTIVAG RPSMGKSQIA LFLALQMILL HNLSVVVFSL EMTKKQLEYR
     LWSLISITNA YKHLELTPLK SDRIRRHRSG NKPLANWEFT SIAKIVGIAS KLPLYMNDSR
     GITVSGIASE CRQIKAKEGK LGLVIVDYLQ MMAEDSGANR SYELGDVARG LYKMAGELDV
     PVLALSQISR GVEGRQNKRP MISDLSQSGI LEMVADNIIL AYRDEYYNPD TTDQGILELI
     MAKARHGETG TATVFFDKSY GIIQNLHSGN I
//
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