ID A0A0F4GVT1_9PEZI Unreviewed; 792 AA.
AC A0A0F4GVT1;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Pre-mRNA-splicing ATP-dependent RNA helicase PRP28 {ECO:0000256|ARBA:ARBA00040398};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
DE AltName: Full=Pre-mRNA-splicing ATP-dependent RNA helicase prp28 {ECO:0000256|ARBA:ARBA00039685};
GN ORFNames=TI39_contig289g00047 {ECO:0000313|EMBL:KJY01492.1};
OS Zymoseptoria brevis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJY01492.1, ECO:0000313|Proteomes:UP000033647};
RN [1] {ECO:0000313|EMBL:KJY01492.1, ECO:0000313|Proteomes:UP000033647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zb18110 {ECO:0000313|EMBL:KJY01492.1,
RC ECO:0000313|Proteomes:UP000033647};
RA Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT "RNA-seq based gene annotation and comparative genomics of four
RT Zymoseptoria species reveal species-specific pathogenicity related genes
RT and transposable element activity.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00001556};
CC -!- SUBUNIT: Component of the U5 snRNP complex.
CC {ECO:0000256|ARBA:ARBA00038719}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX23/PRP28
CC subfamily. {ECO:0000256|ARBA:ARBA00037954}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJY01492.1}.
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DR EMBL; LAFY01000281; KJY01492.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4GVT1; -.
DR STRING; 1047168.A0A0F4GVT1; -.
DR OrthoDB; 5487240at2759; -.
DR Proteomes; UP000033647; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd17945; DEADc_DDX23; 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; ATP-DEPENDENT RNA HELICASE DBP3; 1.
DR PANTHER; PTHR47958:SF56; RNA HELICASE; 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; 1.
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, ECO:0000256|RuleBase:RU000492};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU000492};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000492};
KW mRNA processing {ECO:0000256|ARBA:ARBA00023187};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU000492};
KW Reference proteome {ECO:0000313|Proteomes:UP000033647}.
FT DOMAIN 359..387
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 390..588
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 599..762
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 757..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 359..387
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 1..25
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..47
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..778
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 792 AA; 87125 MW; 143DDB89D2C01FBD CRC64;
MDIPPPPPPL EDVPPPPPPP DLESTAPPRS LASYLPPRPP PPPPSDDLDA DGESAPVVTL
VSKKRKLAAP KPEPLSVEEL LAKKKARDAA AAKPKFLSKK EREKLAQEKA QKEAAALKKD
QPVPVATLAA NGHAVHNGQN GHNGVPSGPR SMRNGNAPAG PSVTRPSLSE KGFDTLPPPP
PPQRSDREPD NAKLKKKNHN QSESEVAAEL IKQRYMGAEQ NVSTFSAKNK RKRTTEKKFN
FEWNAEEDTS PDYNPLYNVR SENNFFGRGK LGGFADDAND TAAKQYARAI EERDPDAGRR
RAAEMLEMEK RRREEGGRNG IDKHWSEKRL EHMRERDWRI FKEDFNIATK GGAIPNPMRS
WEESGLPKRL LDIVYDAGYV EPSAVQRAAI PIALQSRDLI GVAVTGSGKT AAFLLPLLVY
ISNLPPLDEM TKNDGPYAII LAPTRELAQQ IELEAKKFAT PLGFTCVSLV GGHSIEEQSY
NMRDGAEIII ATPGRLVDCI ERRVLVLSQC CYIIMDEADR MIDLGFEEPV NKILDALPVS
NEKPDSDIAE DPNAMAKHTY RQTMMYTATM PPAVERIARK YLRRPATVTI GNVGEAVDTV
EQRVEFVPGE DKRKKRLAEI LHSREFAAPI IVFVNVKRAC DSLARDIQKM GFQTVTLHGS
KTQDQREAAL ASLRNGQTEV LVATDLAGRG IDVPDVSLVV NFMMSHNIEA YTHRIGRTGR
AGKEGVAITF LGNEDADVMY DLKQMIGKSK ISRLPNELAK HEAAQQRSKG KRDRGGGAIE
ESGGFGGKGG WG
//
