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DDX23_DICDI
ID   DDX23_DICDI             Reviewed;         834 AA.
AC   Q54Y81; Q23910;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=ATP-dependent RNA helicase ddx23;
DE            EC=3.6.4.13;
DE   AltName: Full=ATP-dependent RNA helicase helB2;
DE   AltName: Full=DEAD box protein 23;
GN   Name=helB2; Synonyms=ddx23, hel2B; ORFNames=DDB_G0277857;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 272-834.
RC   STRAIN=AX2;
RX   PubMed=7695838; DOI=10.1515/bchm3.1994.375.11.759;
RA   Mahal B., Nellen W.;
RT   "Developmental regulation of DEAD box proteins and cloning of putative RNA
RT   helicase genes from Dictyostelium discoideum.";
RL   Biol. Chem. Hoppe-Seyler 375:759-763(1994).
CC   -!- FUNCTION: Probable ATP-dependent RNA helicase which may be involved in
CC       mRNA splicing. {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   -!- 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. DDX23/PRP28
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AAFI02000023; EAL68101.1; -; Genomic_DNA.
DR   EMBL; X81824; CAA57418.1; -; mRNA.
DR   RefSeq; XP_642321.1; XM_637229.1.
DR   AlphaFoldDB; Q54Y81; -.
DR   SMR; Q54Y81; -.
DR   STRING; 44689.DDB0219950; -.
DR   PaxDb; Q54Y81; -.
DR   PRIDE; Q54Y81; -.
DR   EnsemblProtists; EAL68101; EAL68101; DDB_G0277857.
DR   GeneID; 8621527; -.
DR   KEGG; ddi:DDB_G0277857; -.
DR   dictyBase; DDB_G0277857; helB2.
DR   eggNOG; KOG0333; Eukaryota.
DR   HOGENOM; CLU_003041_11_2_1; -.
DR   InParanoid; Q54Y81; -.
DR   OMA; YLVSTEM; -.
DR   PhylomeDB; Q54Y81; -.
DR   Reactome; R-DDI-72163; mRNA Splicing - Major Pathway.
DR   Reactome; R-DDI-72165; mRNA Splicing - Minor Pathway.
DR   PRO; PR:Q54Y81; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; 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; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
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; 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; 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; Cytoplasm; Helicase; Hydrolase; mRNA processing;
KW   mRNA splicing; Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN           1..834
FT                   /note="ATP-dependent RNA helicase ddx23"
FT                   /id="PRO_0000327433"
FT   DOMAIN          444..643
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          654..815
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   REGION          1..245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          322..371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          813..834
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           413..441
FT                   /note="Q motif"
FT   MOTIF           570..573
FT                   /note="DEAD box"
FT   COMPBIAS        1..26
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..57
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..202
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        215..245
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        323..368
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         457..464
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   834 AA;  95823 MW;  D333AD48BE893C48 CRC64;
     MDPPKLTFIS KRDTKKKDEV NKEQPTKNLK ILDLFSNDEE FSNPTQEEPT NTLQEKLMNV
     DPLEFFSKGG LKEEQKKERD DHRDDYRDSR DRDRDYRDNG GRDRDRDYRD GGGGGGGRDR
     DRNRDRDRDR DRDYRDGGGG RDRYRDNDRY RDTDRYRDND RRDGSGSGSS RRRDERRENS
     GRRDYRDNDR RDDRRDNGRY GRDNDNSGGG GSGKNSSDKK EEINPVSNNN DIHKDRIKRD
     TTQFSHKVFE QINNKRDRED PELRDIKVDY MGIKRDENRK KIKGEKGKFV FEWDSSEDTS
     SDYNTLYTKK LEIQPQFGHG NFGGYEKNNN NNGNHYNGNI YNNNNNNNNN NNNNNNINNN
     NNGSMIGGKQ ISELPDTHWS KKPLKSMTKR DWHIFKEDFN ISTKGGIAPN PIRTWQESNL
     PREILEAIRQ LGYEKPSPIQ MQSIPISLTG RDILGIAETG SGKTCAFVIP MLIYISKQPR
     LTKDTEADGP YALVMAPTRE LVQQIEKETR NFAQHFGFRV VSLVGGQSIE DQAYQVSKGC
     EIIIATPGRL NDCLEKRYLV LNQCNYIVLD EADMMIDLGF EPQVTSVLDA MPSSFLKSED
     DEMAEKQESD RSHIYRTTIL FSATMPPLVE KLSKKYLRRP CTITIGEAGK VVDRIRQTVI
     FVKSENDKKE HLTQLIKDGP PPPIIIFVNK KKHCDIIAPV LEECRVSYTI LHSGRSQEQR
     EAALEGFKKR KYEVLIATGV ASRGIHVDGV THVINFDIPK NIEDYTHRIG RTGRAGSAGL
     ASSFITDKDV EIMYDLKQIL TSTNNIVPIE LLKHPSSQQK HGSSKDHNKS VIFK
 
 
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