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Database: UniProt
Entry: K9VZS8_9CYAN
LinkDB: K9VZS8_9CYAN
Original site: K9VZS8_9CYAN 
ID   K9VZS8_9CYAN            Unreviewed;       835 AA.
AC   K9VZS8;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=ATP-dependent DNA helicase RecG {ECO:0000256|ARBA:ARBA00017846, ECO:0000256|RuleBase:RU363016};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551, ECO:0000256|RuleBase:RU363016};
GN   Name=recG {ECO:0000256|RuleBase:RU363016};
GN   ORFNames=Cri9333_2130 {ECO:0000313|EMBL:AFZ13007.1};
OS   Crinalium epipsammum PCC 9333.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Gomontiellales; Gomontiellaceae;
OC   Crinalium.
OX   NCBI_TaxID=1173022 {ECO:0000313|EMBL:AFZ13007.1, ECO:0000313|Proteomes:UP000010472};
RN   [1] {ECO:0000313|EMBL:AFZ13007.1, ECO:0000313|Proteomes:UP000010472}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 9333 {ECO:0000313|EMBL:AFZ13007.1,
RC   ECO:0000313|Proteomes:UP000010472};
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 chromosome of genome of Crinalium epipsammum PCC 9333.";
RL   Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Critical role in recombination and DNA repair. Helps process
CC       Holliday junction intermediates to mature products by catalyzing branch
CC       migration. Has a DNA unwinding activity characteristic of a DNA
CC       helicase with a 3'- to 5'- polarity. Unwinds branched duplex DNA (Y-
CC       DNA). {ECO:0000256|RuleBase:RU363016}.
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|RuleBase:RU363016};
CC   -!- SIMILARITY: Belongs to the helicase family. RecG subfamily.
CC       {ECO:0000256|ARBA:ARBA00007504, ECO:0000256|RuleBase:RU363016}.
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DR   EMBL; CP003620; AFZ13007.1; -; Genomic_DNA.
DR   RefSeq; WP_015203123.1; NC_019753.1.
DR   AlphaFoldDB; K9VZS8; -.
DR   STRING; 1173022.Cri9333_2130; -.
DR   KEGG; cep:Cri9333_2130; -.
DR   PATRIC; fig|1173022.3.peg.2299; -.
DR   eggNOG; COG1200; Bacteria.
DR   HOGENOM; CLU_005122_7_1_3; -.
DR   OrthoDB; 9804325at2; -.
DR   Proteomes; UP000010472; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   CDD; cd17992; DEXHc_RecG; 1.
DR   CDD; cd04488; RecG_wedge_OBF; 1.
DR   CDD; cd18811; SF2_C_RecG; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR004609; ATP-dep_DNA_helicase_RecG.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR047112; RecG/Mfd.
DR   InterPro; IPR045562; RecG_dom3_C.
DR   InterPro; IPR033454; RecG_wedge.
DR   NCBIfam; TIGR00643; recG; 1.
DR   PANTHER; PTHR47964; ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR47964:SF1; ATP-DEPENDENT DNA HELICASE HOMOLOG RECG, CHLOROPLASTIC; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF19833; RecG_dom3_C; 1.
DR   Pfam; PF17191; RecG_wedge; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363016};
KW   DNA damage {ECO:0000256|RuleBase:RU363016};
KW   DNA recombination {ECO:0000256|RuleBase:RU363016};
KW   DNA repair {ECO:0000256|RuleBase:RU363016};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU363016};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363016};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU363016};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010472}.
FT   DOMAIN          424..585
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          604..769
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          95..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..120
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   835 AA;  93212 MW;  56211A4A684C7822 CRC64;
     MTQSPDWVRL QKALSVEAEY GFTDLVGKQY RFSEFLCLSF GQTPTVITAL ERRRWQEMAS
     QFARYPQLTL LERQHLVAEA SQFIQQIEQG SAGAQGRRGA GEKMYNQQSK TQVKQPPTTP
     IVKTNSEANS GYSSNLSLDQ PLANVAEIGV RKGGYLTKLN LYTVRDLLFY YPRDHIDYAR
     QVNISELEAG ETVTLVGKIK SCNCFTTQKN NKLTILELVI TDQSGRIKLS RFFAGNRYSN
     RGWQEALKRR YESGSIVAAS GLVKKNKYGL TLDNPEIEVL AHPEDTIDSL NIGRVVPVYP
     LTEGVPADMV RQAVTAVLPA AAQLKDPLPS VIRNQYGLVG LKDAIANIHF PSDSAAKEAA
     RRRLVFDEFF YLQLGFLQRR QALRQVQNSA ILLPAGKLIE EFEQILPFKL TNAQQRVIND
     ILNDLQKPTP MNRLVQGDVG SGKTVVAVIA ILAAVQSGYQ GALMAPTEVL AEQHYRKLVS
     WFNLLHLPVE LLTGSTKTAK RRQIHAQLET GELSLLVGTH ALIQDPVNFH KLGLVVIDEQ
     HRFGVHQRAR LLSKGEQPHV LTMTATPIPR TLALTLHGDL DVSQIDELPP GRQAIYTTAL
     TGKERNNAYD LIRREIAEGR QVYVVLPLIE ESEKLDLRSA VDEHQHLSES IFPEFQVGLL
     HGRMSSAEKD EVINAFRDNK TQIIVSTTVI EVGVDVPNAT VMMIENAERF GLSQLHQLRG
     RVGRGSHRSY CLLMSSSTTP DARQRLNVLE QSQDGFFIAE MDMRLRGPGE VLGTRQSGLA
     DFALASLVED QEVLQIARDA AEKIILRDGN LEKLPLLQAE LDYRYQKLMG GAILT
//
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