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Database: UniProt
Entry: R7QSB0_CHOCR
LinkDB: R7QSB0_CHOCR
Original site: R7QSB0_CHOCR 
ID   R7QSB0_CHOCR            Unreviewed;       596 AA.
AC   R7QSB0;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=ATP-dependent RNA helicase {ECO:0000256|RuleBase:RU365068};
DE            EC=3.6.4.13 {ECO:0000256|RuleBase:RU365068};
GN   ORFNames=CHC_T00007274001 {ECO:0000313|EMBL:CDF40628.1};
OS   Chondrus crispus (Carrageen Irish moss) (Polymorpha crispa).
OC   Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gigartinales;
OC   Gigartinaceae; Chondrus.
OX   NCBI_TaxID=2769 {ECO:0000313|EMBL:CDF40628.1, ECO:0000313|Proteomes:UP000012073};
RN   [1] {ECO:0000313|Proteomes:UP000012073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Stackhouse {ECO:0000313|Proteomes:UP000012073};
RX   PubMed=23503846; DOI=10.1073/pnas.1221259110;
RA   Collen J., Porcel B., Carre W., Ball S.G., Chaparro C., Tonon T.,
RA   Barbeyron T., Michel G., Noel B., Valentin K., Elias M., Artiguenave F.,
RA   Arun A., Aury J.M., Barbosa-Neto J.F., Bothwell J.H., Bouget F.Y.,
RA   Brillet L., Cabello-Hurtado F., Capella-Gutierrez S., Charrier B.,
RA   Cladiere L., Cock J.M., Coelho S.M., Colleoni C., Czjzek M., Da Silva C.,
RA   Delage L., Denoeud F., Deschamps P., Dittami S.M., Gabaldon T.,
RA   Gachon C.M., Groisillier A., Herve C., Jabbari K., Katinka M., Kloareg B.,
RA   Kowalczyk N., Labadie K., Leblanc C., Lopez P.J., McLachlan D.H.,
RA   Meslet-Cladiere L., Moustafa A., Nehr Z., Nyvall Collen P., Panaud O.,
RA   Partensky F., Poulain J., Rensing S.A., Rousvoal S., Samson G.,
RA   Symeonidi A., Weissenbach J., Zambounis A., Wincker P., Boyen C.;
RT   "Genome structure and metabolic features in the red seaweed Chondrus
RT   crispus shed light on evolution of the Archaeplastida.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:5247-5252(2013).
CC   -!- FUNCTION: RNA helicase. {ECO:0000256|RuleBase:RU365068}.
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|RuleBase:RU365068};
CC   -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC       family of RNA helicases and controls ATP binding and hydrolysis.
CC       {ECO:0000256|RuleBase:RU365068}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX51/DBP6
CC       subfamily. {ECO:0000256|ARBA:ARBA00038200}.
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DR   EMBL; HG002219; CDF40628.1; -; Genomic_DNA.
DR   RefSeq; XP_005710922.1; XM_005710865.1.
DR   AlphaFoldDB; R7QSB0; -.
DR   STRING; 2769.R7QSB0; -.
DR   EnsemblPlants; CDF40628; CDF40628; CHC_T00007274001.
DR   GeneID; 17318656; -.
DR   Gramene; CDF40628; CDF40628; CHC_T00007274001.
DR   KEGG; ccp:CHC_T00007274001; -.
DR   OMA; YEVFSWF; -.
DR   OrthoDB; 5476171at2759; -.
DR   PhylomeDB; R7QSB0; -.
DR   Proteomes; UP000012073; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
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   PANTHER; PTHR24031:SF68; ATP-DEPENDENT RNA HELICASE DDX51; 1.
DR   PANTHER; PTHR24031; RNA HELICASE; 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; 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:RU365068};
KW   Helicase {ECO:0000256|RuleBase:RU365068};
KW   Hydrolase {ECO:0000256|RuleBase:RU365068};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU365068};
KW   Reference proteome {ECO:0000313|Proteomes:UP000012073};
KW   RNA-binding {ECO:0000256|RuleBase:RU365068}.
FT   DOMAIN          20..235
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          291..457
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          533..555
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   596 AA;  65940 MW;  AFCF1DD1497997F6 CRC64;
     MGITSLFPMQ EAVFSYLQDA SAKRIVGDVI LCAPTGSGKT LAYALPIVQG IIGRKLPRLR
     AIIVLPTRDL ATQVAGVFKE LTGNFGISVA LVSGATSIVV ERASLKTAEI LIATPGRLVD
     HIENGDALSL RSVRYLVLDE SDRLLQDEYQ GWIDYVLPLL GTDRNLNSKQ AEQSCRTRST
     AGIIALAIQP EVSARAFMRS GQTSQESVRK VLVSATQTKN PKRLVRLGLR HPKFFEPISE
     REDTSLGNNY NIPSSLSEKA WIIRDAEDKP IVLLKTLGWI TPASSDMHND PAAQAVLALS
     GTKLIFTKSI QAAHRLCRLL EIFALLLGVE GDVIEMSGDL SPARRKQVMK TVHERKVVHP
     NSTVSPHSSR FLVVVCSDVL ARGVDIFNMD AVINYDVPVH IRTYVHRAGR TARAGRAGTV
     VTLLLSKQAH HFREMVRQAD RGDRKIQAKN LGLRDEERAS FIEKLDNALR LLRRLISRET
     LGLLSADKPL PEYARLEVCN LFEEMKADGW AQNEDATLPD DIRKRRITES LEPAKRGRLD
     LPPGDSPTAI PTDGLDNIEA TAENETLGGE DEFHDFLFSQ IARNLLSEKT RSFRAM
//
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