ID G3U5Q8_LOXAF Unreviewed; 1031 AA.
AC G3U5Q8;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
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:ENSLAFP00000023166.1};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000023166.1, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000023166.1, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000023166.1,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000023166.1}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000023166.1};
RG Ensembl;
RL Submitted (NOV-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; G3U5Q8; -.
DR Ensembl; ENSLAFT00000032090.1; ENSLAFP00000023166.1; ENSLAFG00000010465.4.
DR GeneTree; ENSGT00940000157753; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
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:UP000007646}.
FT DOMAIN 372..400
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 403..581
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 592..753
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 372..400
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..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..228
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1031 AA; 117946 MW; 3E79E67A8B76C988 CRC64;
MGRESRHYRK RSASRGRSGS RSRSRSPSDK RSKRGDDRRS RSRDRDRRRE RSRSRDKRRS
RSRDRKRLRR SRSRERDRSR ERRRSRSRDR RRSRSRSRGR RSRSSSPGNK SKKAENRSRS
KEKTDGGESS KEKKKDKDDK EDEKEKDAGN FDQNKLEEEM RKRKERVEKW REEQRKKAME
NIGELKKEIE EMKQGKKWSL EDDDDDEDDP AEAEKEGNEM EGEELDPLDA YMEEVKEEVK
KFNMRSVKGG GGNEKKSGPT VTKVVTVVTT KKAVVDSDKK KGELMENDQD AMEYSSEEEE
VDLQTALTGY QTKQRKLLEP VDHGKIEYEP FRKNFYVEVP ELAKMSQEEV NVFRLEMEGI
TVKGKGCPKP IKSWVQCGIS MKILNSLKKH GYEKPTPIQT QAIPAIMSGR DLIGIAKTGS
GKTIAFLLPM FRHIMDQRSL EEGEGPIAVI MTPTRELALQ ITKECKKFSK TLGLRVVCVY
GGTGISEQIA ELKRGAEIIV CTPGRMIDML AANSGRVTNL RRVTYVVLDE ADRMFDMGFE
PQVMRIVDNV RPDRQTVMFS ATFPRAMEAL ARRILSKPIE VQVGGRSVVC SDVEQQVIVI
EEEKKFLKLL ELLGHYQESG SVIIFVDKQE HADGLLKDLM RASYPCMSLH GGIDQYDRDS
IINDFKNGTC KLLVATSVAA RGLDVKHLIL VVNYSCPNHY EDYVHRAGRT GRAGNKGYAY
TFITEDQARY AGDIIKALEL SGTAVPPDLE KLWSDFKDQQ KAEGKIIKKS SGFSGKGFKF
DETEQALANE RKKLQKAALG LQDSDDEDAA VDIDEQIESM FRTAKPMNDF GNITLYLIPS
VRYAAKLHIW VGLCIRVMHC QREFLKKIIE DVMQQATNAI LRGGTILAPT VSAKTIAEQL
AEKINAKLNY VPLEKQEEER QDGGQNESFK RYEEELEIND FPQTARWKVT SKEALQRISE
YSEAAITIRG TYFPPGKEPK EGERKIYLAI ESANELAVQK AKAEITRLIK EELIRLQNSY
QPTNKGRYKV L
//
