DBP2_COCIM
ID DBP2_COCIM Reviewed; 545 AA.
AC Q1DP69; J0HG23;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=ATP-dependent RNA helicase DBP2;
DE EC=3.6.4.13;
GN Name=DBP2; ORFNames=CIMG_07894;
OS Coccidioides immitis (strain RS) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=246410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=RS;
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
CC -!- FUNCTION: ATP-dependent RNA helicase involved nonsense-mediated mRNA
CC decay and ribosome biogenesis through rRNA processing. {ECO:0000250}.
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 -!- SUBUNIT: Associates with polysomes. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX5/DBP2
CC subfamily. {ECO:0000305}.
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DR EMBL; GG704913; EAS29148.3; -; Genomic_DNA.
DR RefSeq; XP_001240731.2; XM_001240730.2.
DR AlphaFoldDB; Q1DP69; -.
DR SMR; Q1DP69; -.
DR STRING; 246410.Q1DP69; -.
DR EnsemblFungi; EAS29148; EAS29148; CIMG_07894.
DR GeneID; 4559783; -.
DR KEGG; cim:CIMG_07894; -.
DR VEuPathDB; FungiDB:CIMG_07894; -.
DR InParanoid; Q1DP69; -.
DR OMA; STMPKFE; -.
DR OrthoDB; 245118at2759; -.
DR Proteomes; UP000001261; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 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 Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 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; Cytoplasm; Helicase; Hydrolase; Nonsense-mediated mRNA decay;
KW Nucleotide-binding; Nucleus; Reference proteome; Ribosome biogenesis;
KW RNA-binding; rRNA processing.
FT CHAIN 1..545
FT /note="ATP-dependent RNA helicase DBP2"
FT /id="PRO_0000255991"
FT DOMAIN 159..334
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 362..509
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 50..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 128..156
FT /note="Q motif"
FT MOTIF 282..285
FT /note="DEAD box"
FT BINDING 172..179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 545 AA; 59913 MW; 461DBB91E3355B5D CRC64;
MSYGGGYSSS RDHYGGGHHS GGSGYRSGGY GGSNGYSHGN SNGYGSYGGN SHGSGVGSHG
GGHHGDRMSN LGSGLKQQEW DLNALPKFEK HFYKEHPNVT NRSAQDVEAF RKEHEMTVYG
KNVPRPVETF DEAGFPQYVI SEVKAQGFAK PTPIQSQGWP MALSGRDVVG IAETGSGKTL
TYCLPAIVHI NAQPLLGPGD GPIVLVLAPT RELAVQIQAE ITKFGKSSRI RNTCVYGGVP
RGPQIRDLSR GVEVCIATPG RLIDMLEAGK TNLRRVTYLV LDEADRMLDM GFEPQIRKII
GQIRPDRQTC MWSATWPKEV RQLAHDFLHD YIQVYIGSQD LSANHRITQI VEIVSDFEKR
DRMINHLERI MDDKKSKILI FTGTKRVADD ITRFLRQDGW PALSIHGDKQ QNERDWVLNE
FKTGKSPIMV ATDVASRGID VRDITHVLNY DYPNNSEDYV HRIGRTGRAG AKGTAITLFT
TDNAKQARDL VNILTESKQQ IDPRLAEMAR FGGGGGGGGR WGGRGRGRGG FTASNAAPLG
HNRRW
