ID A0A2K5NFR2_CERAT Unreviewed; 987 AA.
AC A0A2K5NFR2;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Pre-mRNA-processing ATP-dependent RNA helicase PRP5 {ECO:0000256|ARBA:ARBA00041162};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
DE AltName: Full=Pre-mRNA-processing ATP-dependent RNA helicase prp5 {ECO:0000256|ARBA:ARBA00040918};
GN Name=DDX46 {ECO:0000313|Ensembl:ENSCATP00000036261.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000036261.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000036261.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: ATP-dependent RNA helicase involved spliceosome assembly and
CC in nuclear splicing. Catalyzes an ATP-dependent conformational change
CC of U2 snRNP. Bridges U1 and U2 snRNPs and enables stable U2 snRNP
CC association with intron RNA. {ECO:0000256|ARBA:ARBA00037330}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX46/PRP5
CC subfamily. {ECO:0000256|ARBA:ARBA00038511}.
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DR AlphaFoldDB; A0A2K5NFR2; -.
DR STRING; 9531.ENSCATP00000036261; -.
DR Ensembl; ENSCATT00000060550.1; ENSCATP00000036261.1; ENSCATG00000040891.1.
DR GeneTree; ENSGT00940000157753; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000040891; Expressed in skeletal muscle tissue and 12 other cell types or tissues.
DR GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR CDD; cd17953; DEADc_DDX46; 1.
DR CDD; cd22473; KH-I_DDX46; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR PANTHER; PTHR47958:SF35; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000233060}.
FT DOMAIN 328..356
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 359..537
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 548..709
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 328..356
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 22..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..73
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..107
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..184
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 987 AA; 112235 MW; 796D35F32EE36AA3 CRC64;
MGRESRHYRK RSASRGRSGS RSRSRSPSDK RSKRGDDRRS RSRDRDRRRE RSRSRDKRRS
RSRDRKRLRR SRSRERDRSR ERRRSRSRDR RRSRSRSRGR RSRSSSPGNK SKKIENRKRK
ERVEKWREEQ RKKAMENIGE LKKEIEEMKQ GKKWSLEDDD DDEDDPAEAE KEGNEMEGEE
LDPLDAYMEE VKEEVKKFNM RSVKGGGGNE KKSGPTVTKV VTVVTTKKAV VDSDKKKGEL
MENDQDAMEY SSEEEEVDLQ TALTGYQTKQ RKLLEPVDHG KIEYEPFRKN FYVEVPELAK
MSQEEVNVFR LEMEGITVKG KGCPKPIKSW VQCGISMKIL NSLKKHGYEK PTPIQTQAIP
AIMSGRDLIG IAKTGSGKTI AFLLPMFRHI MDQRSLEEGE GPIAVIMTPT RELALQITKE
CKKFSKTLGL RVVCVYGGTG ISEQIAELKR GAEIIVCTPG RMIDMLAANS GRVTNLRRVT
YVVLDEADRM FDMGFEPQVM RIVDNVRPDR QTVMFSATFP RAMEALARRI LSKPIEVQVG
GRSVVCSDVE QQVIVIEEEK KFLKLLELLG HYQESGSVII FVDKQEHADG LLKDLMRASY
PCMSLHGGID QYDRDSIIND FKNGTCKLLV ATSVAARGLD VKHLILVVNY SCPNHYEDYV
HRAGRTGRAG NKGYAYTFIT EDQARYAGDI IKALELSGTA VPSDLEKLWS DFKDQQKAEG
KIIKKSSGFS GKGFKFDETE QALANERKKL QKAALGLQDS DDEDAAVDID EQIESMFNSK
KRVKDMAAPG TSSVPAPTAG NAEKLEIAKR LALRINAQKN LGIESQDVMQ QATNAILRGG
TILAPTVSAK TIAEQLAEKI NAKLNYVPLE KQEEERQDGG QNESFKRYEE ELEINDFPQT
ARWKVTSKEA LQRISEYSEA AITIRGTYFP PGKEPKEGER KIYLAIESAN ELAVQKAKAE
ITRLIKEELI RLQNSYQPTN KGRYKVL
//
