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Database: UniProt
Entry: Q5RC67
LinkDB: Q5RC67
Original site: Q5RC67 
ID   DDX23_PONAB             Reviewed;         820 AA.
AC   Q5RC67;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   11-DEC-2019, entry version 79.
DE   RecName: Full=Probable ATP-dependent RNA helicase DDX23;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAD box protein 23;
GN   Name=DDX23;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in pre-mRNA splicing and its phosphorylated form (by
CC       SRPK2) is required for spliceosomal B complex formation.
CC       {ECO:0000250|UniProtKB:Q9BUQ8}.
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: The phosphorylated form (by SRPK2) is a component of the
CC       U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at
CC       least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, WDR57,
CC       SNRNP40, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39 (By
CC       similarity). Identified in the spliceosome C complex (By similarity).
CC       Interacts with ERBB4 (By similarity). Interacts with ERCC6 (By
CC       similarity). {ECO:0000250|UniProtKB:Q9BUQ8}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BUQ8}.
CC   -!- PTM: Phosphorylated by SRPK2 and this phosphorylation is required for
CC       its association with the tri-snRNP (U4/U6-U5 tri-small nuclear
CC       ribonucleoproteins) and subsequent spliceosomal B complex formation.
CC       {ECO:0000250|UniProtKB:Q9BUQ8}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX23/PRP28
CC       subfamily. {ECO:0000305}.
DR   EMBL; CR858413; CAH90640.1; -; mRNA.
DR   RefSeq; NP_001125347.1; NM_001131875.1.
DR   SMR; Q5RC67; -.
DR   STRING; 9601.ENSPPYP00000005101; -.
DR   PRIDE; Q5RC67; -.
DR   GeneID; 100172249; -.
DR   KEGG; pon:100172249; -.
DR   CTD; 9416; -.
DR   eggNOG; KOG0333; Eukaryota.
DR   eggNOG; ENOG410XNVG; LUCA.
DR   InParanoid; Q5RC67; -.
DR   KO; K12858; -.
DR   OrthoDB; 820037at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   ATP-binding; Helicase; Hydrolase; Isopeptide bond; mRNA processing;
KW   mRNA splicing; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Spliceosome; Ubl conjugation.
FT   CHAIN           1..820
FT                   /note="Probable ATP-dependent RNA helicase DDX23"
FT                   /id="PRO_0000055129"
FT   DOMAIN          422..627
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          651..799
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   NP_BIND         435..442
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOTIF           391..419
FT                   /note="Q motif"
FT   MOTIF           549..552
FT                   /note="DEAD box"
FT   COMPBIAS        20..122
FT                   /note="Arg-rich"
FT   COMPBIAS        128..240
FT                   /note="Glu-rich"
FT   MOD_RES         14
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BUQ8"
FT   MOD_RES         16
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BUQ8"
FT   MOD_RES         107
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BUQ8"
FT   MOD_RES         109
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BUQ8"
FT   CROSSLNK        686
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BUQ8"
FT   CROSSLNK        811
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BUQ8"
SQ   SEQUENCE   820 AA;  95600 MW;  CBB9738A19E68305 CRC64;
     MAGELADKKD RDASPSKEER KRSRTPDRER DRDRDRKSSP SKDRKRHRSR DRRRGGSRSR
     SRSRSKSAER ERRHKERERD KERDRNKKDR DRDKDGHRRD KDRKRSSLSP GRGKDFKSRK
     DRDSKKDEED EHGDKKPKAQ PLSLEELLAK KKAEEEAEAK PKFLSKAERE AEALKRRQQE
     VEERQRMLEE ERKKRKQFQD LGRKMLEDPQ ERERRERRER MERETNGNED EEGRQKIREE
     KDKSKELHAI KERYLGGIKK RRRTRHLNDR KFVFEWDASE DTSIDYNPLY KERHQVQLLG
     RGFIAGIDLK QQKREQSRFY GDLMEKRRTL EEKEQEEARF RKLRKKEAKQ RWDDRHWSQK
     KLDEMTDRDW RIFREDYSIT TKGGKIPNPI RSWKDSSLPP HILEVIDKCG YKEPTPIQRQ
     AIPIGLQNRD IIGVAETGSG KTAAFLIPLL VWITTLPKID RIEESDQGPY AIILAPTREL
     AQQIEEETIK FGKPLGIRTV AVIGGISRED QGFRLRMGCE IVIATPGRLI DVLENRYLVP
     SRCTYVVLDE ADRMIDMGFE PDVQKILEHM PVSNQKPDTD EAEDPEKMLA NFESGKHKYR
     QTVMFTATMP PAVERLARSY LRRPAVVYIG SAGKPHERVE QKVFLMSESE KRKKLLAILE
     QGFDPPIIIF VNQKKGCDVL AKSLEKMGYN ACTLHGGKGQ EQREFALSNL KAGAKDILVA
     TDVAGRGIDI QDVSMVVNYD MAKNIEDYIH RIGRTGRAGK SGVAITFLTK EDSAVFYELK
     QAILESPVSS CPPELANHPD AQHKPGTILT KKRREETIFA
//
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