PRP16_BOVIN
ID PRP16_BOVIN Reviewed; 1227 AA.
AC Q17R09;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP16;
DE EC=3.6.4.13;
DE AltName: Full=ATP-dependent RNA helicase DHX38;
DE AltName: Full=DEAH box protein 38;
GN Name=DHX38; Synonyms=PRP16;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable ATP-binding RNA helicase. Involved in pre-mRNA
CC splicing as component of the spliceosome.
CC {ECO:0000250|UniProtKB:Q92620}.
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: Identified in the spliceosome C complex.
CC {ECO:0000250|UniProtKB:Q92620}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92620}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC PRP16 sub-subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC118085; AAI18086.1; -; mRNA.
DR RefSeq; NP_001069266.1; NM_001075798.1.
DR AlphaFoldDB; Q17R09; -.
DR BMRB; Q17R09; -.
DR SMR; Q17R09; -.
DR STRING; 9913.ENSBTAP00000042866; -.
DR PaxDb; Q17R09; -.
DR PRIDE; Q17R09; -.
DR Ensembl; ENSBTAT00000045480; ENSBTAP00000042866; ENSBTAG00000013265.
DR GeneID; 520046; -.
DR KEGG; bta:520046; -.
DR CTD; 9785; -.
DR VEuPathDB; HostDB:ENSBTAG00000013265; -.
DR VGNC; VGNC:57044; DHX38.
DR eggNOG; KOG0924; Eukaryota.
DR GeneTree; ENSGT00940000156898; -.
DR InParanoid; Q17R09; -.
DR OMA; VMFHRSP; -.
DR OrthoDB; 354219at2759; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000013265; Expressed in trachea and 107 other tissues.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IEA:Ensembl.
DR GO; GO:0005681; C:spliceosomal complex; 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; 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; 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 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..1227
FT /note="Pre-mRNA-splicing factor ATP-dependent RNA helicase
FT PRP16"
FT /id="PRO_0000282329"
FT DOMAIN 542..705
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 727..902
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 59..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1155..1227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 652..655
FT /note="DEAH box"
FT COMPBIAS 59..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1156..1196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 555..562
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92620"
FT MOD_RES 117
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q92620"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92620"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92620"
FT MOD_RES 1194
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92620"
FT CROSSLNK 482
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92620"
FT CROSSLNK 483
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92620"
FT CROSSLNK 504
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92620"
FT CROSSLNK 1166
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92620"
SQ SEQUENCE 1227 AA; 140405 MW; 4ACC6320AD6FE18C CRC64;
MEDSGEDASL HRLEGTDVDS QVGGLIFKTK SAASEQHVFK APAPRPSLLG LDLLASLKRK
EREEKDDGED KKKSRISSYK DWEESKDDQR DAEAEDSDQA GRSGRKDRHY RSARVETPSH
PGGVSEEFWE RSRQRERERR EHGVYASSKD EKDRKKERSR DRDCDRKRDR DERDRSRHSG
RSERDGGSDR SSRRNEPESP RHRPKDAATP SRSTWEEEDS GYGSSRRSQW ESPSPTPSYR
DSERSHRPSS RDRDRSVRSR YSDDTPLPTP SYKYNEWADD RRHLGSTPRL SRGRGRREDG
EEGISFDTEE ERQQWEDDQR QADRDWYMMD EGYDEFHNPL AYSSDDYVRR REQHLHKQKQ
KRISAQRRQI NEDNERWETN RMLTSGVVHR LEVDEDFEED SAAKVHLMVH NLVPPFLDGR
IVFTKQPEPV IPVKDATSDL AIIARKGSQT VRKHREQKER KKAQHKHWEL AGTKLGDIMG
VKKEEEPDKS LTEDGKVDYR TEQKFADHMK KKSEASSEFA KKKSILEQRQ YLPIFAVQQE
LLTIIRDNSI VIVVGETGSG KTTQLTQYLH EDGYTDYGMI GCTQPRRVAA MSVAKRVSEE
MGGNLGEEVG YAIRFEDCTS ESTLIKYMTD GILLRESLRE ADLDHYSAII MDEAHERSLN
TDVLFGLLRE VVARRSDLKL IVTSATMDAE KFASFFGNVP IFHIPGRTFP VDILFSKTPQ
EDYVEAAVKQ SLQVHLSGAP GDILIFMPGQ EDIEVTSDQI VEHLEELENA PALAVLPIYS
QLPSDLQAKI FQKAPDGVRK CIVATNIAET SLTVDGIMFV IDSGYCKLKV FNPRIGMDAL
QIYPISQANA NQRSGRAGRT GPGQCFRLYT QSAYKNELLT TTVPEIQRTN LANVVLLLKS
LGVQDLLQFH FMDPPPEDNM LNSMYQLWIL GALDNTGGLT STGRLMVEFP LDPALSKMLI
VSCDMGCSSE ILLIVSMLSV PAIFYRPKGR EEESDQIREK FAVPESDHLS YLNVYLQWKN
NNYSTIWCND HFIHAKAMRK VREVRAQLKD IMVQQRMSLA SCGTDWDIVR KCICAAYFHQ
AAKLKGIGEY VNIRTGMPCH LHPTSSLFGM GYTPDYIVYH ELVMTTKEYM QCVTAVDGEW
LAELGPMFYS VKQAGKSRQE NRRRAKEEAS AMEEEMALAE EQLRARRQEQ EKRSPLGSVR
STKIYTPGRK EQGEPMTPRR TPARFGL
