PRP22_YEAST
ID PRP22_YEAST Reviewed; 1145 AA.
AC P24384; D3DLR0;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP22;
DE EC=3.6.4.13 {ECO:0000269|PubMed:23096351};
GN Name=PRP22; OrderedLocusNames=YER013W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=1992352; DOI=10.1038/349487a0;
RA Company M., Arenas J., Abelson J.;
RT "Requirement of the RNA helicase-like protein PRP22 for release of
RT messenger RNA from spliceosomes.";
RL Nature 349:487-493(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP IDENTIFICATION IN THE CWC COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11884590; DOI=10.1128/mcb.22.7.2011-2024.2002;
RA Ohi M.D., Link A.J., Ren L., Jennings J.L., McDonald W.H., Gould K.L.;
RT "Proteomics analysis reveals stable multiprotein complexes in both fission
RT and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA
RT splicing factors, and snRNAs.";
RL Mol. Cell. Biol. 22:2011-2024(2002).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [8]
RP CATALYTIC ACTIVITY.
RX PubMed=23096351; DOI=10.1515/hsz-2012-0158;
RA Kudlinzki D., Schmitt A., Christian H., Ficner R.;
RT "Structural analysis of the C-terminal domain of the spliceosomal helicase
RT Prp22.";
RL Biol. Chem. 393:1131-1140(2012).
CC -!- FUNCTION: Acts late in the splicing of pre-mRNA. Mediates the release
CC of the spliced mRNA from spliceosomes. {ECO:0000269|PubMed:1992352}.
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:0000269|PubMed:23096351};
CC -!- SUBUNIT: Belongs to the CWC complex (or CEF1-associated complex), a
CC spliceosome sub-complex reminiscent of a late-stage spliceosome
CC composed of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2,
CC CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24,
CC CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1, NTC20, PRP8, PRP9,
CC PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3,
CC SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2.
CC {ECO:0000269|PubMed:11884590}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 907 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC DDX8/PRP22 sub-subfamily. {ECO:0000305}.
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DR EMBL; X58681; CAA41530.1; -; Genomic_DNA.
DR EMBL; U18778; AAB64546.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07664.1; -; Genomic_DNA.
DR PIR; S13643; S13643.
DR RefSeq; NP_010929.3; NM_001178904.3.
DR PDB; 5MQ0; EM; 4.17 A; V=1-1145.
DR PDB; 5YLZ; EM; 3.60 A; W=1-1145.
DR PDB; 6BK8; EM; 3.30 A; P=1-1145.
DR PDB; 6EXN; EM; 3.70 A; V=1-1145.
DR PDBsum; 5MQ0; -.
DR PDBsum; 5YLZ; -.
DR PDBsum; 6BK8; -.
DR PDBsum; 6EXN; -.
DR AlphaFoldDB; P24384; -.
DR SMR; P24384; -.
DR BioGRID; 36745; 347.
DR ComplexPortal; CPX-1651; PRP19-associated complex.
DR DIP; DIP-655N; -.
DR IntAct; P24384; 4.
DR MINT; P24384; -.
DR STRING; 4932.YER013W; -.
DR iPTMnet; P24384; -.
DR MaxQB; P24384; -.
DR PaxDb; P24384; -.
DR PRIDE; P24384; -.
DR EnsemblFungi; YER013W_mRNA; YER013W; YER013W.
DR GeneID; 856732; -.
DR KEGG; sce:YER013W; -.
DR SGD; S000000815; PRP22.
DR VEuPathDB; FungiDB:YER013W; -.
DR eggNOG; KOG0922; Eukaryota.
DR GeneTree; ENSGT00940000155510; -.
DR HOGENOM; CLU_001832_2_3_1; -.
DR InParanoid; P24384; -.
DR OMA; DPMVAPE; -.
DR BioCyc; YEAST:G3O-30200-MON; -.
DR PRO; PR:P24384; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P24384; protein.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IMP:SGD.
DR GO; GO:0071021; C:U2-type post-spliceosomal complex; IMP:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IDA:SGD.
DR GO; GO:0000350; P:generation of catalytic spliceosome for second transesterification step; IDA:SGD.
DR GO; GO:0000390; P:spliceosomal complex disassembly; IMP:SGD.
DR CDD; cd17971; DEXHc_DHX8; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR044762; DHX8/Prp22_DEXHc.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR Pfam; PF04408; HA2; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50126; S1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Helicase; Hydrolase; mRNA processing;
KW mRNA splicing; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..1145
FT /note="Pre-mRNA-splicing factor ATP-dependent RNA helicase
FT PRP22"
FT /id="PRO_0000055135"
FT DOMAIN 178..250
FT /note="S1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 493..656
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 678..854
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 254..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 603..606
FT /note="DEAH box"
FT BINDING 506..513
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT HELIX 477..480
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 485..488
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 489..497
FT /evidence="ECO:0007829|PDB:6BK8"
FT STRAND 500..505
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 512..524
FT /evidence="ECO:0007829|PDB:6BK8"
FT STRAND 531..536
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 538..552
FT /evidence="ECO:0007829|PDB:6BK8"
FT STRAND 558..564
FT /evidence="ECO:0007829|PDB:6BK8"
FT STRAND 567..569
FT /evidence="ECO:0007829|PDB:6BK8"
FT STRAND 576..580
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 581..590
FT /evidence="ECO:0007829|PDB:6BK8"
FT STRAND 598..602
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 610..625
FT /evidence="ECO:0007829|PDB:6BK8"
FT STRAND 630..636
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 641..646
FT /evidence="ECO:0007829|PDB:6BK8"
FT STRAND 652..654
FT /evidence="ECO:0007829|PDB:6BK8"
FT STRAND 663..665
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 674..687
FT /evidence="ECO:0007829|PDB:6BK8"
FT STRAND 692..697
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 701..717
FT /evidence="ECO:0007829|PDB:6BK8"
FT STRAND 725..730
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 736..739
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 740..743
FT /evidence="ECO:0007829|PDB:6BK8"
FT STRAND 750..756
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 758..760
FT /evidence="ECO:0007829|PDB:6BK8"
FT STRAND 769..774
FT /evidence="ECO:0007829|PDB:6BK8"
FT STRAND 777..784
FT /evidence="ECO:0007829|PDB:6BK8"
FT TURN 785..788
FT /evidence="ECO:0007829|PDB:6BK8"
FT STRAND 789..796
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 799..807
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 808..810
FT /evidence="ECO:0007829|PDB:6BK8"
FT STRAND 811..814
FT /evidence="ECO:0007829|PDB:6BK8"
FT STRAND 816..821
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 823..828
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 837..840
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 846..853
FT /evidence="ECO:0007829|PDB:6BK8"
FT STRAND 856..858
FT /evidence="ECO:0007829|PDB:6BK8"
FT TURN 859..861
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 869..881
FT /evidence="ECO:0007829|PDB:6BK8"
FT STRAND 889..891
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 893..899
FT /evidence="ECO:0007829|PDB:6BK8"
FT STRAND 901..903
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 905..916
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 920..931
FT /evidence="ECO:0007829|PDB:6BK8"
FT STRAND 940..942
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 943..953
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 960..972
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 977..982
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 987..1005
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 1018..1029
FT /evidence="ECO:0007829|PDB:6BK8"
FT STRAND 1030..1037
FT /evidence="ECO:0007829|PDB:6BK8"
FT TURN 1038..1040
FT /evidence="ECO:0007829|PDB:6BK8"
FT STRAND 1041..1044
FT /evidence="ECO:0007829|PDB:6BK8"
FT TURN 1045..1047
FT /evidence="ECO:0007829|PDB:6BK8"
FT STRAND 1060..1062
FT /evidence="ECO:0007829|PDB:6BK8"
FT STRAND 1065..1077
FT /evidence="ECO:0007829|PDB:6BK8"
FT STRAND 1079..1086
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 1088..1094
FT /evidence="ECO:0007829|PDB:6BK8"
FT TURN 1096..1098
FT /evidence="ECO:0007829|PDB:6BK8"
FT TURN 1108..1110
FT /evidence="ECO:0007829|PDB:6BK8"
FT TURN 1125..1128
FT /evidence="ECO:0007829|PDB:6BK8"
FT HELIX 1130..1140
FT /evidence="ECO:0007829|PDB:6BK8"
SQ SEQUENCE 1145 AA; 130011 MW; D92DBD620531B9A7 CRC64;
MSDISKLIGA IVGSDDPVII EFVLNIINKS GNLQEFIRNI QKLDAGISYE DSIKMYNAFL
GKQEEEKVRN KVKSSPLSQK INQVLKDDVN LDDPVVTEFV LSILNKSKSI TEFQEQLNLM
QSGLDNETIF KIYQIASPPV MKEEVSVLPS TKIPAKIEAK IEEEVQKIES LDPSPVLHKV
YEGKVRNITT FGCFVQIFGT RMKNCDGLVH ISEMSDQRTL DPHDVVRQGQ HIFVEVIKIQ
NNGKISLSMK NIDQHSGEIR KRNTESVEDR GRSNDAHTSR NMKNKIKRRA LTSPERWEIR
QLIASGAASI DDYPELKDEI PINTSYLTAK RDDGSIVNGN TEKVDSKLEE QQRDETDEID
VELNTDDGPK FLKDQQVKGA KKYEMPKITK VPRGFMNRSA INGSNAIRDH REEKLRKKRE
IEQQIRKQQS FDDPTKNKKD SRNEIQMLKN QLIVTEWEKN RMNESISYGK RTSLPISAQR
QTLPVYAMRS ELIQAVRDNQ FLVIVGETGS GKTTQITQYL DEEGFSNYGM IGCTQPRRVA
AVSVAKRVAE EVGCKVGHDV GYTIRFEDVT GPDTRIKYMT DGMLQREALL DPEMSKYSVI
MLDEAHERTV ATDVLFALLK KAAIKRPELK VIVTSATLNS AKFSEYFLNC PIINIPGKTF
PVEVLYSQTP QMDYIEAALD CVIDIHINEG PGDILVFLTG QEEIDSCCEI LYDRVKTLGD
SIGELLILPV YSALPSEIQS KIFEPTPKGS RKVVFATNIA ETSITIDGIY YVVDPGFAKI
NIYNARAGIE QLIVSPISQA QANQRKGRAG RTGPGKCYRL YTESAFYNEM LENTVPEIQR
QNLSHTILML KAMGINDLLK FDFMDPPPKN LMLNALTELY HLQSLDDEGK LTNLGKEMSL
FPMDPTLSRS LLSSVDNQCS DEIVTIISML SVQNVFYRPK DRQLEADSKK AKFHHPYGDH
LTLLNVYTRW QQANYSEQYC KTNFLHFRHL KRARDVKSQI SMIFKKIGLK LISCHSDPDL
IRKTFVSGFF MNAAKRDSQV GYKTINGGTE VGIHPSSSLY GKEYEYVMYH SIVLTSREYM
SQVTSIEPQW LLEVAPHFYK AGDAESQSRK KAKIIPLHNK FAKDQNSWRL SSIRQSRERA
LGIKR
