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Database: UniProt
Entry: K9UUQ4_9CYAN
LinkDB: K9UUQ4_9CYAN
Original site: K9UUQ4_9CYAN 
ID   K9UUQ4_9CYAN            Unreviewed;       489 AA.
AC   K9UUQ4;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   ORFNames=Cal6303_0193 {ECO:0000313|EMBL:AFY99300.1};
OS   Calothrix sp. PCC 6303.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC   Calothrix.
OX   NCBI_TaxID=1170562 {ECO:0000313|EMBL:AFY99300.1, ECO:0000313|Proteomes:UP000010477};
RN   [1] {ECO:0000313|EMBL:AFY99300.1, ECO:0000313|Proteomes:UP000010477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6303 {ECO:0000313|EMBL:AFY99300.1,
RC   ECO:0000313|Proteomes:UP000010477};
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., Chen A., Kyrpides N.,
RA   Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA   Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT   "Finished chromosome of genome of Calothrix sp. PCC 6303.";
RL   Submitted (MAY-2012) 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=3.6.4.13;
CC         Evidence={ECO:0000256|ARBA:ARBA00001556};
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family.
CC       {ECO:0000256|RuleBase:RU000492}.
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DR   EMBL; CP003610; AFY99300.1; -; Genomic_DNA.
DR   RefSeq; WP_015195959.1; NC_019751.1.
DR   AlphaFoldDB; K9UUQ4; -.
DR   STRING; 1170562.Cal6303_0193; -.
DR   KEGG; calt:Cal6303_0193; -.
DR   PATRIC; fig|1170562.3.peg.207; -.
DR   eggNOG; COG0513; Bacteria.
DR   HOGENOM; CLU_003041_28_3_3; -.
DR   OrthoDB; 9805696at2; -.
DR   Proteomes; UP000010477; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR   CDD; cd00268; DEADc; 1.
DR   CDD; cd18787; SF2_C_DEAD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   PANTHER; PTHR47959:SF13; ATP-DEPENDENT RNA HELICASE RHLE; 1.
DR   PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000492};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU000492};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000492};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000492};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010477}.
FT   DOMAIN          1..29
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          32..242
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          268..415
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          65..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          408..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1..29
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT   COMPBIAS        408..435
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        440..457
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        473..489
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   489 AA;  53650 MW;  545ECCDA25970276 CRC64;
     MSFSTLGLSN EIVRAVTERG YTKPTPIQMQ AIPAVLLGGD ILAGAQTGTG KTASFTLPLL
     HRLSSSDNSQ DNSVQDASVE TSRGVGSRDN FPIVNRLKPN LKTTGGYPRI RALILTPTRE
     LAAQVQESVH DYGKYLNLRS MAMFGGVSIN PQKQRLRNGV DILVATPGRL LDHVQQGTVN
     LSGIEVLVLD EADRMLDMGF IRDIRRILSL LPKERQNLLF FATFSDSIKE LAAGLLNRPT
     MIEVARRNVT ADTVSQKIYQ VDHDKKRLLL AHLIKKDNWY QVLVFTRTKH GADRLVKQLG
     EDRIQALAIH GNKSQSARTA ALAKFKNGTL QVLVATDIAA RGLDISDLPH VVNFDLPNVP
     EDYVHRIGRT GRAGAKGEAV SLVCTDEQPL LAEIEKLIAK RLPREEITGF FSHPHPHKSS
     ESIPEGRKQR PKGGYDQRTS ARGAKSSPQT SPKKSAARTV AGGSKSGTKK PGTRRSGKRD
     APPERRSDR
//
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