ID E6ZTM4_SPORE Unreviewed; 1155 AA.
AC E6ZTM4;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
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 ORFNames=sr10250 {ECO:0000313|EMBL:CBQ70581.1};
OS Sporisorium reilianum (strain SRZ2) (Maize head smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX NCBI_TaxID=999809 {ECO:0000313|EMBL:CBQ70581.1, ECO:0000313|Proteomes:UP000008867};
RN [1] {ECO:0000313|EMBL:CBQ70581.1, ECO:0000313|Proteomes:UP000008867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRZ2 {ECO:0000313|Proteomes:UP000008867};
RX PubMed=21148393; DOI=10.1126/science.1195330;
RA Schirawski J., Mannhaupt G., Muench K., Brefort T., Schipper K.,
RA Doehlemann G., Di Stasio M., Roessel N., Mendoza-Mendoza A., Pester D.,
RA Mueller O., Winterberg B., Meyer E., Ghareeb H., Wollenberg T.,
RA Muensterkoetter M., Wong P., Walter M., Stukenbrock E., Gueldener U.,
RA Kahmann R.;
RT "Pathogenicity determinants in smut fungi revealed by genome comparison.";
RL Science 330:1546-1548(2010).
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 EMBL; FQ311441; CBQ70581.1; -; Genomic_DNA.
DR AlphaFoldDB; E6ZTM4; -.
DR EnsemblFungi; CBQ70581; CBQ70581; sr10250.
DR VEuPathDB; FungiDB:sr10250; -.
DR eggNOG; KOG0334; Eukaryota.
DR HOGENOM; CLU_003041_0_2_1; -.
DR OrthoDB; 5483490at2759; -.
DR Proteomes; UP000008867; Chromosome 2.
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 CDD; cd17953; DEADc_DDX46; 1.
DR CDD; cd22474; KH-I_PRP5_like; 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, ECO:0000313|EMBL:CBQ70581.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 479..507
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 510..688
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 716..864
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 899..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 961..987
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1025..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 479..507
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 1..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..165
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..917
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1155 AA; 125838 MW; E9E5412D02A59F2C CRC64;
MAGYDDRDDY RRSSSSSHHR SRTSKHDPSS SSSYRSPGHA PTRRRSRSSS SYTHTHSSRS
HRDRSDEPYL NGAGYDRRYD QDRQREWDRR DCDSRAGAQP PRDDRYSHAE APRHDKRRRW
DEGTTTQQGA PAVAPSGAYG ALPSRPPVAP PGAAPGPPPT LPPAVTMSAP STVATSSSAV
PVSAEEQAKL AKKARLEAWR KEQAAKKALE EARQRAQSIA SAVAPAPQRT AAPATSSNPQ
SLSTPINATG LRTLSLRTDP TRTSAQNRSR TMMEDASEPS TRMQLNRLGD LPPLDPSVDT
ARKGTFADDD DEEDRNAKTG AATQTRASNA DMDVDEEEEE DPLDAFMSTV KTQVAQVNAE
DRRKAGASGE GALAQAKSRA VVLGQDDSDA EAEDQDEELD ELDRVGVATE DLLALAAKKV
KKKELATVDH ANVDYEPFRK EFYNPPAEIQ DMSEELANQI RLEMDAITVR GKDCPKPLTK
WSHCGLPASC LDVIKRLGYA APTPIQSQAI PAIMSGRDII GVAKTGSGKT MAFLLPMFRH
IKDQRPVEVG EGPVGIVMTP TRELAVQIYR EMRPFIKALG LRAACVYGGA PISEQIAEMK
KTADIVVATP GRLIDLLTAN SGRVTNLRRV TYLVLDEADR MFDMGFEPQV MKIVNNIRPD
RQTVLFSATF PKQMESLARK VLKNKPLEIT VGGRSVVAAE IEQIVEVRPE NTKFHRLLEI
LGELYNREKD ARTLIFVDRQ EAADDLLKDL IRKGYVTMSL HGGKDQVDRD ETISDFKAGN
VPIVTATSVA ARGLDVKQLK LVINYDVPNH MEDYVHRAGR TGRAGQKGTC ITFVTPEQDR
YARDIIAALK ASAAHVPAEL ETMAAAFKEK LAAGKAKAAG SGFGGKGLDR LETDREKALK
AQKSAYGEAD EEGKAVNAGD ASEANAKPGT ATGAASSSED QLSKIQGMKI EIMHGAAPES
VRDNKIVSAS DEASAAAAKT KTDQEQDTKE AAQLKAQEAA LEAAKAHGAD TTKLAAVLEN
IRRQANARKD AARHTDADKQ KERKARDPDA TDYHAIVPIN DFPQRARWRV TNKETMSHLI
ESTGASITNK GVFYKEGTEP QPGEPPKLQL LIESNTKSMV EDAVREIQRL LVEATQAALE
AEARNPGTTG RYTVV
//
