PRP11_SCHPO
ID PRP11_SCHPO Reviewed; 1014 AA.
AC Q9P7C7; Q9UTW0;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Pre-mRNA-processing ATP-dependent RNA helicase prp11;
DE EC=3.6.4.13 {ECO:0000305|PubMed:14713954};
GN Name=prp11; ORFNames=SPCC10H11.01;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-82, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP LYS-468; THR-469; ASP-575; GLU-576 AND THR-608.
RX PubMed=14713954; DOI=10.1038/sj.emboj.7600050;
RA Xu Y.-Z., Newnham C.M., Kameoka S., Huang T., Konarska M.M., Query C.C.;
RT "Prp5 bridges U1 and U2 snRNPs and enables stable U2 snRNP association with
RT intron RNA.";
RL EMBO J. 23:376-385(2004).
CC -!- FUNCTION: ATP-dependent RNA helicase involved in pre-
CC spliceosome/complex A assembly and mRNA splicing (PubMed:14713954).
CC Bridges U1 and U2 snRNPs during pre-spliceosome assembly and enables
CC stable U2 snRNP association with intron RNA (PubMed:14713954). Through
CC its helicase activity probably catalyzes an ATP-dependent
CC conformational change of U2 snRNP (PubMed:14713954).
CC {ECO:0000269|PubMed:14713954}.
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:0000305|PubMed:14713954};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000305|PubMed:14713954};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:14713954}.
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; CU329672; CAB85446.1; -; Genomic_DNA.
DR EMBL; AB027964; BAA87268.1; -; Genomic_DNA.
DR RefSeq; NP_587856.1; NM_001022849.2.
DR AlphaFoldDB; Q9P7C7; -.
DR SMR; Q9P7C7; -.
DR BioGRID; 275512; 16.
DR DIP; DIP-59804N; -.
DR IntAct; Q9P7C7; 4.
DR STRING; 4896.SPCC10H11.01.1; -.
DR iPTMnet; Q9P7C7; -.
DR MaxQB; Q9P7C7; -.
DR PaxDb; Q9P7C7; -.
DR PRIDE; Q9P7C7; -.
DR EnsemblFungi; SPCC10H11.01.1; SPCC10H11.01.1:pep; SPCC10H11.01.
DR GeneID; 2538936; -.
DR KEGG; spo:SPCC10H11.01; -.
DR PomBase; SPCC10H11.01; prp11.
DR VEuPathDB; FungiDB:SPCC10H11.01; -.
DR eggNOG; KOG0334; Eukaryota.
DR HOGENOM; CLU_003041_0_1_1; -.
DR InParanoid; Q9P7C7; -.
DR OMA; ANCLDVI; -.
DR PhylomeDB; Q9P7C7; -.
DR PRO; PR:Q9P7C7; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0071004; C:U2-type prespliceosome; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:PomBase.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; ISO:PomBase.
DR GO; GO:1990446; F:U1 snRNP binding; IDA:PomBase.
DR GO; GO:1990447; F:U2 snRNP binding; IDA:PomBase.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; ISO:PomBase.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:1903241; P:U2-type prespliceosome assembly; IMP:PomBase.
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 1: Evidence at protein level;
KW ATP-binding; Helicase; Hydrolase; mRNA processing; mRNA splicing;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..1014
FT /note="Pre-mRNA-processing ATP-dependent RNA helicase
FT prp11"
FT /id="PRO_0000055146"
FT DOMAIN 449..627
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 638..802
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 815..875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 418..446
FT /note="Q motif"
FT MOTIF 575..578
FT /note="DEAD box"
FT COMPBIAS 11..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..848
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..874
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 462..469
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MUTAGEN 468
FT /note="K->A: Decreased ATP binding. Decreased ATP
FT hydrolysis activity. Loss of function in pre-
FT spliceosome/complex A assembly."
FT /evidence="ECO:0000269|PubMed:14713954"
FT MUTAGEN 469
FT /note="T->A: Decreased ATP binding. Decreased ATP
FT hydrolysis activity. Loss of function in pre-
FT spliceosome/complex A assembly."
FT /evidence="ECO:0000269|PubMed:14713954"
FT MUTAGEN 575
FT /note="D->A: No effect on ATP binding. Loss of ATP
FT hydrolysis activity. Loss of function in pre-
FT spliceosome/complex A assembly."
FT /evidence="ECO:0000269|PubMed:14713954"
FT MUTAGEN 576
FT /note="E->A: No effect on ATP binding. Loss of ATP
FT hydrolysis activity. Loss of function in pre-
FT spliceosome/complex A assembly."
FT /evidence="ECO:0000269|PubMed:14713954"
FT MUTAGEN 608
FT /note="T->A: No effect on ATP binding. Decreased ATP
FT hydrolysis activity. Loss of function in pre-
FT spliceosome/complex A assembly."
FT /evidence="ECO:0000269|PubMed:14713954"
SQ SEQUENCE 1014 AA; 114213 MW; 7700C6A90B79192B CRC64;
MSRRTRSRSP PRRSYNRERR DYRKYDDSED QKGARYNRYV DDVSSRRDRH DSFRSHESNK
IRRDNSWKHD KYSYEKRYQE RDREYARSKN IPDQYIGRSP RPTSHRHAEE KEVDNKTKSD
ETNPVLQGSA TEIKPQPRRS RFDRTERVGA SLSVSEIQSE NPRVDVIPKD KAVENNHQRN
AEKPVASDKI TDAKLLARLE RVRAWKESKA KQEASKKEEH KLNTKPQVTA KDQNAMPSTG
ISGFEINRQK DTSDMKRNNR VHMDDEDGPR RMNLEDYQEL WDQEDRGMLG NEQAASMEED
EVDPLDAYMA SLVGTTDTIR PGLLNTEVID PNANDDERMV ISETLEEEEN LLALAAKRSK
KKDVITVDHS KINYEDFKKD FYVEPEELKN LSPAEVDELR ASLDGIKIRG IDCPKPVTSW
SQCGLSAQTI SVINSLGYEK PTSIQAQAIP AITSGRDVIG VAKTGSGKTI AFLLPMFRHI
KDQRPLKTGE GPIAIIMTPT RELAVQIFRE CKPFLKLLNI RACCAYGGAP IKDQIADLKR
GAEIVVCTPG RMIDVLSANA GRVTNLHRCT YLVLDEADRM FDLGFEPQVM RIINNIRPDR
QTVLFSATFP RAMEALARKV LKKPVEITVG GRSVVASEVE QIVEVRPEES KFSRLLELLG
ELYNNQLDVR TLVFVDRQES ADALLSDLMK RGYTSNSIHG GKDQHDRDST ISDYKAGVFD
VLIATSVVAR GLDVKSLQLV VNYDCPNHME DYVHRVGRTG RAGHTGVAVT FITPEQEKYA
VDIAKALKMS KQPVPKELQT LASQFLEKVK AGKEKAAGGG FGGKGLSRLD ETRNAERKMQ
RKAYGEDEED VETEAEAKSP LEKITPEKST GDPTLDRVRA AVGGIAARAF ANQTAQSNKL
TQPISIIKTD GDEYKAKMEI NDYPQQARWA VTNNTNIVHV TELTGTSITT KGNFYLPGKN
PEPGEEKLYL WIEGPSELVV NRAITELRRL LLEGINHSLE GGNKPSASGR YTVV
