DHX16_DICDI
ID DHX16_DICDI Reviewed; 1106 AA.
AC Q54MH3;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Putative pre-mRNA-splicing factor ATP-dependent RNA helicase DHX16;
DE EC=3.6.4.13;
DE AltName: Full=DEAH-box protein 16;
GN Name=dhx16; ORFNames=DDB_G0285937;
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).
CC -!- FUNCTION: Required for pre-mRNA splicing as component of the
CC spliceosome. Contributes to pre-mRNA splicing after spliceosome
CC formation and prior to the first transesterification reaction.
CC {ECO:0000250|UniProtKB:O60231}.
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: Component of pre-catalytic spliceosome complexes.
CC {ECO:0000250|UniProtKB:O60231}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O60231}. Nucleus,
CC nucleoplasm {ECO:0000250|UniProtKB:O60231}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC DDX16/PRP8 sub-subfamily. {ECO:0000305}.
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DR EMBL; AAFI02000082; EAL64503.1; -; Genomic_DNA.
DR RefSeq; XP_638017.1; XM_632925.1.
DR AlphaFoldDB; Q54MH3; -.
DR SMR; Q54MH3; -.
DR STRING; 44689.DDB0233398; -.
DR PaxDb; Q54MH3; -.
DR PRIDE; Q54MH3; -.
DR EnsemblProtists; EAL64503; EAL64503; DDB_G0285937.
DR GeneID; 8625368; -.
DR KEGG; ddi:DDB_G0285937; -.
DR dictyBase; DDB_G0285937; dhx16.
DR eggNOG; KOG0923; Eukaryota.
DR HOGENOM; CLU_001832_7_1_1; -.
DR InParanoid; Q54MH3; -.
DR OMA; PHYHKKK; -.
DR PhylomeDB; Q54MH3; -.
DR Reactome; R-DDI-72163; mRNA Splicing - Major Pathway.
DR PRO; PR:Q54MH3; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:dictyBase.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
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:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
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 Pfam; PF04408; HA2; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 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; Helicase; Hydrolase; mRNA processing; mRNA splicing;
KW Nucleotide-binding; Nucleus; Reference proteome; Spliceosome.
FT CHAIN 1..1106
FT /note="Putative pre-mRNA-splicing factor ATP-dependent RNA
FT helicase DHX16"
FT /id="PRO_0000330890"
FT DOMAIN 477..640
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 665..838
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 73..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 587..590
FT /note="DEAH box"
FT COMPBIAS 73..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 490..497
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1106 AA; 126564 MW; 428EE89A2AAFA115 CRC64;
MSSNNESIKN WVSDKIFDIL GYRESTMVDY IIALSKKAKD VNSFISTLTE QDFPINSNTK
SFAQELLNKS QQKIQNITSS SSSSSSTSLS SSSSSKDKEK EKIEFLKKNK SYKLVIDHDD
DIVNSSGSSD SDSDSERKRK KKEKKKEKKD KKDKKDKKSS TRKKSDNNWD DEIEPEPIKP
NEKEDENNNN ENNDNNNDNN NLQKRQPYKS IIEEENNNDN NNNNGEEDEY EREQREVKEL
SDRIKKRDEK STKKKIVDDS ETKESIERKN RLEQNEQLET ERTKSRRKYL VGEEQKRLIL
LKREIEEEYE LFKDQKLTEQ EIKDFEKKKK LYELASQRIN ESQQSDDYYQ LPSEIKDKDS
LLKSSYINDN KNKKGNDSSS SSSYNPEQKE WEQNRMKSAI SENRGLSTAN IGGGNEEYEY
VFEDQIEFIK EEVLKQGQKG DGVMILKPGD DGSAQAKMTI QEVRKSLPVY PYREQLIDAV
REYQVLIIVG ETGSGKTTQI PQYLHEAGFS KTGKIGCTQP RRVAAMSVAA RVAEEVGCKL
GNEVGYSIRF EDCTSQKTVL QYMTDGMLVR EFLTAPDLAS YSVLIIDEAH ERTLHTDILF
GLLKDITRFR PDLKLLISSA TMDAERFSDY FDGAPTFNIP GRKYEVTTHY TQAPEADYLD
AAVVTVLQIH ITEPLGDILV FLTGQEEVDQ AAEMLQTRTR GLGTKIKELI ITRIYSTLPT
DLQAKIFEPT PPNARKVVLA TNIAETSLTI DGIIYVIDPG FCKQKMFNPR TGMESLVITP
VSRASANQRK GRAGRVAPGK CFRLFTAWAF DNELEENTIP EIQRTNLGNV VLLLKSMGIN
DLMNFDFMDP PPAQTLIAAL EQLYALGALN DRGQLTKLGR KMAEFPVDPQ LSKMIIASEK
YKCSEEILTI CAMLSVGNTI FYRPKDKAFA ADAARKLFFH PQGDHLTLMN VFNQWRESGY
AVQWCFENFI QHRSMKRAQD VRDQLELLLE RVEIPLVSNV DDTDSIRKCI ASGFFYNSAK
LEKSGLFRTT KHNQSVQIHP SSCLFQSPPK WVVYHELVLT TKEFMRQIVE IQSSWLHEIA
PHIYKEKDVN DNQKLPKNIG KKQINK
