DDX10_CHICK
ID DDX10_CHICK Reviewed; 875 AA.
AC Q5ZJF6;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Probable ATP-dependent RNA helicase DDX10;
DE EC=3.6.4.13;
DE AltName: Full=DEAD box protein 10;
GN Name=DDX10; ORFNames=RCJMB04_18j24;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Putative ATP-dependent RNA helicase. {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 -!- 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. DDX10/DBP4
CC subfamily. {ECO:0000305}.
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DR EMBL; AJ720478; CAG32137.1; -; mRNA.
DR RefSeq; NP_001073193.1; NM_001079725.1.
DR AlphaFoldDB; Q5ZJF6; -.
DR SMR; Q5ZJF6; -.
DR STRING; 9031.ENSGALP00000027656; -.
DR PaxDb; Q5ZJF6; -.
DR GeneID; 418965; -.
DR KEGG; gga:418965; -.
DR CTD; 1662; -.
DR VEuPathDB; HostDB:geneid_418965; -.
DR eggNOG; KOG0343; Eukaryota.
DR InParanoid; Q5ZJF6; -.
DR OrthoDB; 973872at2759; -.
DR PhylomeDB; Q5ZJF6; -.
DR PRO; PR:Q5ZJF6; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0006364; P:rRNA processing; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR025313; DUF4217.
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; PF13959; DUF4217; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01178; DUF4217; 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 2: Evidence at transcript level;
KW ATP-binding; Coiled coil; Helicase; Hydrolase; Nucleotide-binding;
KW Reference proteome; RNA-binding.
FT CHAIN 1..875
FT /note="Probable ATP-dependent RNA helicase DDX10"
FT /id="PRO_0000252208"
FT DOMAIN 104..278
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 291..453
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 528..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 736..773
FT /evidence="ECO:0000255"
FT MOTIF 73..101
FT /note="Q motif"
FT MOTIF 226..229
FT /note="DEAD box"
FT COMPBIAS 567..584
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..828
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 93..95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 117..124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 875 AA; 100157 MW; 1CF610BF99761ACA CRC64;
MGRAGGGSGD GGEEPAALEA VRSFERWKKK YSRRTRRLRL QRKERERPEW QVEREGIGRL
VQRYPQINAN EIQRFSDFPL SKKTLKGLQE AQYRMVTEIQ RQTIGLALQG KDVLGAAKTG
SGKTLAFIVP ALELLYRLQW TSADGLGVLI ISPTRELAFQ TFKVLRKVGK NHDFSAGLII
GGKDLKEESE RIHHINMLIC TPGRLLQHMD ETSYFYASDL QMLILDEADR ILDMGFADTM
NAIIENLPKK RQTLLFSATQ TKSVKDLARL SLKDPEYVWV HEKAKFSTPA TLDQNYIVCE
LQHKINVLYS FLRSHLKKKS IVFFASCKEV QYLFRVFCKL QPGLPVLALH GKQQQMKRME
VYTCFVRKKA AVLFATDIAA RGLDFPAVNW VIQFDCPEDA NTYIHRVGRT ARYKEGGEAL
LVLLPSEEKG MVEQLAQRKV PVNEIKINPE KITDIQKRMQ AFLAQDQELK EKAQRCFVSY
LRSVYLMKNK EVFDVFKLPL AEYALSLGLA MAPRVRFLQK VQKQLSVKET SERNPLKDTE
QNKNTISSLN KEGMEECRIN PSGKLSVNRS KEEENRKETE QYPPSSEGTE ESGSECESKE
ASEEEEKEGA LSSRVPYTNS MQFFEDDDDD DDTKDLDLLT VKRRDVFDLE SKDSPALNAS
NSKMKKKTTK TQEAKKILKK KFKVNTRIVF TEDGELVQQW PPVQKSGLAK ADEEDDASGI
NLDKVREILR EEDKFDKEEY RKKIKEKHRE KRLKEKAARR EARNKNARAE GETVAVLAHS
GSEDEFDPST LPDPDKYKDS DEEQDTESED SYRELEEKSG RKRRSHGGSI AAGEMPQKRK
KAKFSQEEDP FLPLDTGLSL AEDEELVLHL LKSHS
