PRP5_GIBZE
ID PRP5_GIBZE Reviewed; 1207 AA.
AC Q4IP34; A0A0E0RPB1; I1RBT4; V6QVE8;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Pre-mRNA-processing ATP-dependent RNA helicase PRP5;
DE EC=3.6.4.13;
GN Name=PRP5; ORFNames=FGRRES_01024, FGSG_01024;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
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 (By similarity). {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: The Q motif is unique to and characteristic of the DEAD box
CC family of RNA helicases and controls ATP binding and hydrolysis.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX46/PRP5
CC subfamily. {ECO:0000305}.
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DR EMBL; DS231663; ESU06293.1; -; Genomic_DNA.
DR EMBL; HG970332; CEF73086.1; -; Genomic_DNA.
DR RefSeq; XP_011316778.1; XM_011318476.1.
DR AlphaFoldDB; Q4IP34; -.
DR SMR; Q4IP34; -.
DR STRING; 5518.FGSG_01024P0; -.
DR PRIDE; Q4IP34; -.
DR EnsemblFungi; ESU06293; ESU06293; FGSG_01024.
DR GeneID; 23548481; -.
DR KEGG; fgr:FGSG_01024; -.
DR eggNOG; KOG0334; Eukaryota.
DR HOGENOM; CLU_003041_0_3_1; -.
DR InParanoid; Q4IP34; -.
DR Proteomes; UP000070720; Chromosome 1.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 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 Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 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; Coiled coil; Helicase; Hydrolase; mRNA processing;
KW mRNA splicing; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..1207
FT /note="Pre-mRNA-processing ATP-dependent RNA helicase PRP5"
FT /id="PRO_0000232364"
FT DOMAIN 608..786
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 817..961
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 962..1024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1041..1067
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 985..1034
FT /evidence="ECO:0000255"
FT MOTIF 577..605
FT /note="Q motif"
FT MOTIF 734..737
FT /note="DEAD box"
FT COMPBIAS 19..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..396
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..430
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..1010
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 621..628
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1207 AA; 133942 MW; FF64F4717FE30EB1 CRC64;
MARPRDSRSP SPAGSTHSSR RFRNDDRRDR DRRNDGRDHR RRTRSRSPDP RNRDRDRDRD
RDRARDRDNY RRRDRSLDRR DDNHYRGGRR DNRERDRRRS RDRFDDRIRS PMTDRRRNRS
RENDRDVRRR DDSRSRISGR REGTTDSPAR SNRDDGRNQK TPLDDSGNGG ASQVRHTLLD
FECIADGLQA QTPKAEGGQA DVDKKAERLA KLEAWKKKKE SASQKQKEVN PSQTRNLLAE
MDKKASGASS KTVSPSVSAI ASPAATPTVE SPAASYSGKF DPKAIAKKSA ASRAHDASKP
ALGSLEGQPE KISVPVKQAT TASALPANRT KASGFGFVKT NAETEKLTAK RKLDLDEEDT
TKRKLTKLPA LPIEADDTPY ADQDDDESDG DNFAENEEEA AAAARAAHER RLQAENQMDT
AEEETKPTDV ETNGDVAMNN NASQPEPATQ MEVDEEDDVD PLDAFMADLK QTDVRQPTKT
STTQKIQEPE AYFSDDEYDF NKKDEGDASA LLAITAKRKK KDIPTIDYSK IEIEPIRKNF
WHEPAELSLL TEAEVADLRL ELDGIKVNGK DVPKPVQKWA QCGLTRQTLD VVDNLGYEKP
TPIQMQALPA LMSGRDVIGV AKTGSGKTVA FLLPMFRHIK DQPPLKDTDG PIGLIMTPTR
ELAVQIHKDC KPFLKMMGLR AVCAYGGAPI REQIAELKRG AEIIVCTPGR MIDLLAANQG
RVTNLKRVTY VVLDEADRMF DMGFEPQVMK IFANMRPDRQ TILFSATMPR IIDSLTKKVL
KNPIEVTVGG RSVVAKEIEQ IVEVRDEPSK FHRVLELLGE LYDRDEDART LIFVERQEKA
DDLLKELMMK GYPCMSIHGG KDQIDRDSTI SDFKKGVVPI LIATSVAARG LDVKQLKLVI
NYDAPNHLED YVHRAGRTGR AGNTGVAVTF VTPEQENCAP GIAKALEQSG QPIPDRLNEM
RKAHREKVKS GKAKDTSGFG GKGLDRLDQE REAARLRERK VHKAEGEEEE VTEDKKEDED
EKAEKALDAI RAAASGVLAR ESAKADDADA KSMPPVKTSG VVKDKAKDPL DKVSSAVSAI
NSRLGKAGQL RAGQPIDNKG PDAGAFHATL EINDFPQKAR WAVTNRTNVA KILEATGTSI
TTKGNFYPAG KEVPAGAEPK LYILIEGDTE VVVSSALTEL TRLLREGTIA AVDADSRAPA
SGRYTIT
