PRP5_USTMA
ID PRP5_USTMA Reviewed; 1156 AA.
AC Q4PFD9; A0A0D1E5J5;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Pre-mRNA-processing ATP-dependent RNA helicase PRP5;
DE EC=3.6.4.13;
GN Name=PRP5; ORFNames=UMAG_01174;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; CM003141; KIS71274.1; -; Genomic_DNA.
DR RefSeq; XP_011387116.1; XM_011388814.1.
DR AlphaFoldDB; Q4PFD9; -.
DR SMR; Q4PFD9; -.
DR STRING; 5270.UM01174P0; -.
DR PRIDE; Q4PFD9; -.
DR EnsemblFungi; KIS71274; KIS71274; UMAG_01174.
DR GeneID; 23562272; -.
DR KEGG; uma:UMAG_01174; -.
DR VEuPathDB; FungiDB:UMAG_01174; -.
DR eggNOG; KOG0334; Eukaryota.
DR HOGENOM; CLU_003041_0_2_1; -.
DR InParanoid; Q4PFD9; -.
DR OMA; CGLGVQT; -.
DR OrthoDB; 245118at2759; -.
DR Proteomes; UP000000561; Chromosome 2.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0071004; C:U2-type prespliceosome; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:EnsemblFungi.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:1990446; F:U1 snRNP binding; IEA:EnsemblFungi.
DR GO; GO:1990447; F:U2 snRNP binding; IEA:EnsemblFungi.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:1903241; P:U2-type prespliceosome assembly; IEA:EnsemblFungi.
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; 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; Helicase; Hydrolase; mRNA processing; mRNA splicing;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..1156
FT /note="Pre-mRNA-processing ATP-dependent RNA helicase PRP5"
FT /id="PRO_0000232367"
FT DOMAIN 507..685
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 697..861
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 900..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1028..1049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 476..504
FT /note="Q motif"
FT MOTIF 633..636
FT /note="DEAD box"
FT COMPBIAS 1..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..169
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..918
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 520..527
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1156 AA; 126208 MW; 357BC85CDAA9444A CRC64;
MSGYDNRDDY RHSSSSSHHR SRNSKHDSSS SSYRSHGYAP TRRRSRSPSS YHSSSRSHRD
HTTDPYPNGS GHDRRHDRDR NRERDRRDHD SPIEAAPSPD GRRFHVEGAP RQGGRRRWDE
GAPTPPTAAA PVHVSDPTRS SLNTQLPSRP IVAPPGMAPG PPPSLPSSTP IVPSTGISIS
PEEQAKLAKK ARLEAWRKEQ AAKKALEEAR QRARSIASAV APSSQRTESF SSSSTPQTAP
TSINAAGLRT LSLRTDPSRT TAQNRSRTMM DDASESSKRI HLSRLGDLPP LDPSIDTAHI
ATTSVDAEDD DHQLGVAPPT QGSSAAAMDV DDDDEEEDPL DAFMLTVKSQ VAQVNDDDRR
KASASGGHER TQAKSKAVVL GRDDSDGEAE DQYEELDELD RVGMATEDLL ALAAKKVKKK
DLVTVDHSAI DYEPFNKAFY HPPAEIQDMS EELANQIRLE MDAITVRGRD CPKPLTKWSH
CGLPASCLDV IKRLGYSAPT PIQSQAMPAI MSGRDIIGVA KTGSGKTMAF LLPMFRHIKD
QRPVEPSEGP VGIIMTPTRE LAVQIYREMR PFIKALGLRA ACVYGGAPIS EQIAEMKKTA
DIVVATPGRL IDLLTANSGR VTNLYRVTYL VLDEADRMFD MGFEPQVMKI LNNIRPDRQT
VLFSATFPKQ MESLARKVLK NKPLEITVGG RSVVAAEIEQ IVEVRSEDTK FHRLLEILGE
LYNREKDART LIFVDRQEAA DDLLKDLIRK GYVTMSLHGG KDQVDRDETI SDFKAGNVPI
VTATSVAARG LDVKQLKLVI NYDVPNHMED YVHRAGRTGR AGQKGTCITF ITPEQDRYAR
DIIAALKASA AHVPPELEAM AASFKEKLAA GKAKAAGSGF GGKGLDRFEL DREKTLKAQK
SAYGEADDDA KAAAAGDSSE DKAKTGAPPG ASSSEDQLSK IQGMKIEIMQ GAAPESVRDN
KTLSASQEAS AAAAAAAAAR SKAEPEQELK EAAQLKAQEA ALEAAKAHGA DTTKLAAVLE
NIRRQANARK EAAKNSELDK HKDRKARDPD ATDYHAIVPI NDFPQRARWR VTNKETMRHL
IESTGASITN KGVFYKEGTE PQPGEPPKLQ LLIESNTKSM VEDAVREIQR LLVEATQAVL
EAEARNPGTT GRYTVV
