ID R7QMW7_CHOCR Unreviewed; 984 AA.
AC R7QMW7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=CHC_T00006834001 {ECO:0000313|EMBL:CDF39852.1};
OS Chondrus crispus (Carrageen Irish moss) (Polymorpha crispa).
OC Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gigartinales;
OC Gigartinaceae; Chondrus.
OX NCBI_TaxID=2769 {ECO:0000313|EMBL:CDF39852.1, 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 -!- 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. DEAH subfamily.
CC {ECO:0000256|ARBA:ARBA00008792}.
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DR EMBL; HG002086; CDF39852.1; -; Genomic_DNA.
DR RefSeq; XP_005710146.1; XM_005710089.1.
DR AlphaFoldDB; R7QMW7; -.
DR STRING; 2769.R7QMW7; -.
DR EnsemblPlants; CDF39852; CDF39852; CHC_T00006834001.
DR GeneID; 17317859; -.
DR Gramene; CDF39852; CDF39852; CHC_T00006834001.
DR KEGG; ccp:CHC_T00006834001; -.
DR OrthoDB; 5490433at2759; -.
DR PhylomeDB; R7QMW7; -.
DR Proteomes; UP000012073; Unassembled WGS sequence.
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 CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.10.10.2130; DEAH helicase family, winged-helix domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR042035; DEAH_win-hel_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF99; ATP-DEPENDENT RNA HELICASE DHX37-RELATED; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 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};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000012073}.
FT DOMAIN 46..222
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 244..433
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 725..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 953..984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..753
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..972
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 984 AA; 107954 MW; BC3C5662F84B051F CRC64;
MKTTNDIGSP LPRKRERRHF VVFERDPAAA KARLELPVCM HEQEIMEVVH ANDVVLISGA
TGTGKTTQVP QFLLEDGFGD PRAPVHKGIV AVTQPRRVAA VTCANRVAFE LKSQVGDIVG
YQIRHAAKLG AEVRAKFVTD GILLREAEND ILLKRYSAVV VDEVHERSLN TDLLLSFLSR
TVTLRRENPG TLGPLKVIVM SATLDVEGVF RGDEALFPNP PVVKVPSRQY SVTMHFAKRT
SEDYVEEAYK KVDKIHRRLP RGGILVFLTG RQEVADLCSR LDKHFANRKV KIQGDTGSEI
GIKVLPFYAL LSDRRQRGVF DDCGQDVRKV VVATNIAETS VTVPGISYVV DSGRAKEKVY
KGEGAHALSA YEIRWVSKAS ADQRAGRAGR TGPGHCYRLY SSAVFDRQFD AFREPEVLRT
PTDSVVLRLR AMGIKNVSKF PFPTRPCEKD LAASEKLLAD LGALHEPGRI PSLDIGSGFS
KGIEPNGTDL LGVTKLGKSL AKLPISPRFG KMLLSALSSK LPLNEGERQA TARYTCRIAG
VLTVGTVFDR TSESWREKHL VFQHRRSEIL TELSAVCAVE HAGIQGSRRA RYSVKSLDTQ
AMREVCKSYS LHFKSVTEAL EIGYQLEKHL WGSERPAAAS LLPPSKIVEE CILRAVLTGL
PDRIARRMTR DEGIAMGVIP RRRRKAFTVL GDGGAVYLEE SSSIFLNGGV EFVSFSSLNE
IELRRKRRRA EDDDEQRDDY ESSSDDERAP GDDEPQPEEG NPATEQGVNG AEAVPTKVIL
RGASVISPAW LTTDATSMCH FDSPSGGASA PSYDSGTDTV VEESSVRYGH WPLGVAKVPV
GLLALCRKGS DTRSSTGSAA QYRALAAAVV TGRVRPGLRV DFEKEGTDRS GRVCVQRVAD
EMRRRACALS AQGLAKAVVD VDWLTPAVEA CVGARFRAAV RKRYEEAVRR MVQEFSDGEG
DGARKHEGEH SGGEDDGEED GEEE
//
