PRP5_PHANO
ID PRP5_PHANO Reviewed; 1184 AA.
AC Q0UN57;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Pre-mRNA-processing ATP-dependent RNA helicase PRP5;
DE EC=3.6.4.13;
GN Name=PRP5; ORFNames=SNOG_06807;
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH445334; EAT85458.2; -; Genomic_DNA.
DR RefSeq; XP_001797169.1; XM_001797117.1.
DR AlphaFoldDB; Q0UN57; -.
DR SMR; Q0UN57; -.
DR STRING; 13684.SNOT_06807; -.
DR PRIDE; Q0UN57; -.
DR EnsemblFungi; SNOT_06807; SNOT_06807; SNOG_06807.
DR GeneID; 5974059; -.
DR KEGG; pno:SNOG_06807; -.
DR eggNOG; KOG0334; Eukaryota.
DR HOGENOM; CLU_003041_0_3_1; -.
DR InParanoid; Q0UN57; -.
DR OrthoDB; 245118at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
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; 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; Helicase; Hydrolase; mRNA processing; mRNA splicing;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..1184
FT /note="Pre-mRNA-processing ATP-dependent RNA helicase PRP5"
FT /id="PRO_0000256035"
FT DOMAIN 575..754
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 780..933
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 148..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 973..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 544..572
FT /note="Q motif"
FT MOTIF 702..705
FT /note="DEAD box"
FT COMPBIAS 160..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 973..993
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 588..595
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1184 AA; 127644 MW; 4037346BB0CB5C55 CRC64;
MHGHRASASA IHPDYPVTHR ESTWRRATLI VQGSTATVDD TLRPAVPARG LQAAEIAREI
ATEIATAVAE VVTTVTVLEI DVTTAETTAA MTVETTAETA AAHVHHPVAR GHRTAEMIVT
AETTAGTTAG TTVAMIGTGV EVPRHVGQAR DVLQPHRPRT SAATREERVN PEKQKEDKLA
ERAAKLLEWK KRKEAERLAQ EKAGTPGSGA SPAGSVPSTP AVAATPPPRE AKPTVAKSKV
PKPATEKVKQ KQPEKSSFKL DESAAARPLI AKPAGKPVAI AAASKYHHID YKCSNQLTQT
DGAAAAATTK ANGNIGSFGL KTKSTAEEDI SSKALLDDEI DTGKRKLQAL PVFATHDEPE
TTAGVEDDAA MSDIGTDDDE TNAQLQAKLQ SRRAELSHDQ AADKDTNMEE VPTADNTGDQ
MDVDDNAGAE EDDVDPLDAF MADLSVPQQP SRAAPQGETM FNDDLEPEQT AVEGEDLLAL
RAAKKKKKEV PTINHEKVEY EPFRKDFYTE PAEITQMSAE DVADLRHELD GIKVKPDDVP
RPVTKWAQMG LLQQTMDVFT RVGYARPTAI QAQAIPIAES GRDLIGVAKT GSGKTLAFGI
PMIRHVLDQR PLKPADGPIG LILAPTRELS LQIVNELKPF LNASGITIKC AYGGQPISDQ
IAMIKRGGIH ILCATAGRLI DLLQSNSGRV LSFRRITYVV LDEADRMFDM GFEPQVMKIL
ASIRPDRQTI LFSATFPKTM AALARKALDK PAEVIIGGRS KVAPEITQHI TIVPPSYEKK
IAKLLHHLGQ TFSDDENAQV LIFTERQETA EDLLSKLFKA KYFAVNTIHG AKDQTDRNEA
INEFKQGLLN ILIATSVAAR GLDVPGLALV YNFDCPTHLE DYVHRCGRTG RAGNKGLAVT
LIENPGQERF AVHIVKALKE SGAEVPDDLQ AMANAFHEKV KSGTEKYYNV GFKGKGLDEL
DASRALDKKR EKRALKLGDD DASDDEPDLP KLKKPEASGP GVAKSTNGDA AAEPVQDEPA
WKKLLLGKIV VNKTERAETG KPTTAKERAM AAARKIDGNL SRKGTVHAGQ PIDNKGPDAG
LYHSTLEIND FPQKARWAVT NRTNVAKILD ATGVSITTKG NFYGPGKEPG ETDLPKLYIL
VEGDTEGVVT QAMLELTRLL TDATVAAEEA ASTRGPTGRY SVMS
