DHX16_PANTR
ID DHX16_PANTR Reviewed; 1044 AA.
AC Q7YR39; Q1XI06;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Pre-mRNA-splicing factor ATP-dependent RNA helicase DHX16;
DE EC=3.6.4.13;
DE AltName: Full=ATP-dependent RNA helicase #3;
DE AltName: Full=DEAH-box protein 16;
GN Name=DHX16; Synonyms=DBP2, DDX16;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12799463; DOI=10.1073/pnas.1230533100;
RA Anzai T., Shiina T., Kimura N., Yanagiya K., Kohara S., Shigenari A.,
RA Yamagata T., Kulski J.K., Naruse T.K., Fujimori Y., Fukuzumi Y.,
RA Yamazaki M., Tashiro H., Iwamoto C., Umehara Y., Imanishi T., Meyer A.,
RA Ikeo K., Gojobori T., Bahram S., Inoko H.;
RT "Comparative sequencing of human and chimpanzee MHC class I regions unveils
RT insertions/deletions as the major path to genomic divergence.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7708-7713(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16702430; DOI=10.1534/genetics.106.057034;
RA Shiina T., Ota M., Shimizu S., Katsuyama Y., Hashimoto N., Takasu M.,
RA Anzai T., Kulski J.K., Kikkawa E., Naruse T., Kimura N., Yanagiya K.,
RA Watanabe A., Hosomichi K., Kohara S., Iwamoto C., Umehara Y., Meyer A.,
RA Wanner V., Sano K., Macquin C., Ikeo K., Tokunaga K., Gojobori T.,
RA Inoko H., Bahram S.;
RT "Rapid evolution of major histocompatibility complex class I genes in
RT primates generates new disease alleles in humans via hitchhiking
RT diversity.";
RL Genetics 173:1555-1570(2006).
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. Interacts
CC with GPKOW. {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; BA000041; BAC78177.1; -; Genomic_DNA.
DR EMBL; AB210151; BAE92763.1; -; Genomic_DNA.
DR EMBL; AB210152; BAE92764.1; -; Genomic_DNA.
DR RefSeq; NP_001035839.1; NM_001042380.1.
DR AlphaFoldDB; Q7YR39; -.
DR SMR; Q7YR39; -.
DR STRING; 9598.ENSPTRP00000030599; -.
DR PaxDb; Q7YR39; -.
DR Ensembl; ENSPTRT00000033119; ENSPTRP00000030599; ENSPTRG00000017935.
DR GeneID; 462546; -.
DR KEGG; ptr:462546; -.
DR CTD; 8449; -.
DR VGNC; VGNC:11059; DHX16.
DR eggNOG; KOG0923; Eukaryota.
DR GeneTree; ENSGT00940000158480; -.
DR HOGENOM; CLU_001832_7_1_1; -.
DR InParanoid; Q7YR39; -.
DR OrthoDB; 354219at2759; -.
DR TreeFam; TF313473; -.
DR Proteomes; UP000002277; Chromosome 6.
DR Bgee; ENSPTRG00000017935; Expressed in cortex of kidney and 21 other tissues.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; ISS:UniProtKB.
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; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
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; PF00270; DEAD; 1.
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; Phosphoprotein; Reference proteome;
KW Spliceosome.
FT CHAIN 1..1044
FT /note="Pre-mRNA-splicing factor ATP-dependent RNA helicase
FT DHX16"
FT /id="PRO_0000055152"
FT DOMAIN 412..576
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 601..774
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 101..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 523..526
FT /note="DEAH box"
FT COMPBIAS 143..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 425..432
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60231"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60231"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60231"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60231"
FT MOD_RES 715
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O60231"
SQ SEQUENCE 1044 AA; 119650 MW; 2BD5B595177A37AA CRC64;
MATPAGLERW VQDELHSVLG LSERHVAQFL IGTAQRCTSA EEFVQRLRDT DTLDLSGPAR
DFALRLWNKV PRKAVVEKPA RAAEREARAL LEKNRSYRLL EDSEESSEET VSRAGSSLQK
KRKKRKHLRK KREEEEEEEE EEASEKGKKK TGGSKQQTEK PESEDEWERT ERERLQDLEE
RDAFAERVRQ RDKDRTRNVL ERSDKKAYEE AQKRLKMAEE DRKAMVPELR KKSRREYLAK
REREKLEDLE AELADEEFLF GDVELSRHER QELKYKRRVR DLAREYRAAG EQEKLEATNR
YHMPKETRGQ PARAVDLVEE ESGAPGEEQR RWEEARLGAA SLKFGARDAA SQEPKYQLVL
EEEETIEFVR ATQLQGNEEP SAPPTSTQAQ QKESIQAVRR SLPVFPFREE LLAAIANHQV
LIIEGETGSG KTTQIPQYLF EEGYTNKGMK IACTQPRRVA AMSVAARVAR EMGVKLGNEV
GYSIRFEDCT SERTVLRYMT DGMLLREFLS EPDLASYSVV MVDEAHERTL HTDILFGLIK
DVARFRPELK VLVASATMDT ARFSTFFDDA PVFRIPGRRF PVDIFYTKAP EADYLEACVV
SVLQIHVTQP PGDILVFLTG QEEIEAACEM LQDRCRRLGS KIRELLVLPI YANLPSDMQA
RIFQPTPPGA RKVVVATNIA ETSLTIEGII YVLDPGFCKQ KSYNPRTGME SLTVTPCSKA
SANQRAGRAG RVAAGKCFRL YTAWAYQHEL EETTVPEIQR TSLGNVVLLL KSLGIHDLMH
FDFLDPPPYE TLLLALEQLY ALGALNHLGE LTTSGRKMAE LPVDPMLSKM ILASEKYSCS
EEILTVAAML SVNNSIFYRP KDKVVHADNA RVNFFLPGGD HLVLLNVYTQ WAESGYSSQW
CYENFVQFRS MRRARDVREQ LEGLLERVEV GLSSCQGDYI RVRKAITAGY FYHTARLTRS
GYRTVKQQQT VFIHPNSSLF EQQPRWLLYH ELVLTTKEFM RQVLEIESSW LLEVAPHYYK
AKELEDPHAK KMPKKIGKTR EELG
