PRP8_CAEEL
ID PRP8_CAEEL Reviewed; 2329 AA.
AC P34369;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Pre-mRNA-splicing factor 8 homolog;
GN Name=prp-8; ORFNames=C50C3.6;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2057-2329, AND ABSENCE OF BOUND
RP METAL.
RX PubMed=17473007; DOI=10.1110/ps.072872007;
RA Zhang L., Shen J., Guarnieri M.T., Heroux A., Yang K., Zhao R.;
RT "Crystal structure of the C-terminal domain of splicing factor Prp8
RT carrying retinitis pigmentosa mutants.";
RL Protein Sci. 16:1024-1031(2007).
CC -!- FUNCTION: Functions as a scaffold that mediates the ordered assembly of
CC spliceosomal proteins and snRNAs. Required for the assembly of the
CC U4/U6-U5 tri-snRNP complex. Functions as scaffold that positions
CC spliceosomal U2, U5 and U6 snRNAs at splice sites on pre-mRNA
CC substrates, so that splicing can occur. Interacts with both the 5' and
CC the 3' splice site. {ECO:0000250|UniProtKB:Q99PV0}.
CC -!- SUBUNIT: Part of the U5 snRNP complex and of the U4/U6-U5 tri-snRNP
CC complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: The MPN (JAB/Mov34) domain has structural similarity with
CC deubiquitinating enzymes, but lacks the residues that would bind the
CC catalytic metal ion.
CC -!- DOMAIN: Contains a region with structural similarity to reverse
CC transcripase, presenting the classical thumb, fingers and palm
CC architecture, but lacks enzyme activity, since the essential metal-
CC binding residues are not conserved. {ECO:0000250}.
CC -!- DOMAIN: Contains a region with structural similarity to type-2
CC restriction endonucleases, but the residues that would bind catalytic
CC metal ions in endonucleases are instead involved in hydrogen bonds that
CC stabilize the protein structure. {ECO:0000250}.
CC -!- DOMAIN: Contains a region with structural similarity to RNase H, but
CC lacks RNase H activity. {ECO:0000250}.
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DR EMBL; FO080718; CCD66122.1; -; Genomic_DNA.
DR PIR; S44625; S44625.
DR RefSeq; NP_498785.1; NM_066384.4.
DR PDB; 2P87; X-ray; 2.30 A; A=2057-2329.
DR PDB; 2P8R; X-ray; 2.10 A; A=2057-2329.
DR PDBsum; 2P87; -.
DR PDBsum; 2P8R; -.
DR AlphaFoldDB; P34369; -.
DR SMR; P34369; -.
DR BioGRID; 41358; 36.
DR DIP; DIP-27427N; -.
DR STRING; 6239.C50C3.6; -.
DR iPTMnet; P34369; -.
DR EPD; P34369; -.
DR PaxDb; P34369; -.
DR PeptideAtlas; P34369; -.
DR PRIDE; P34369; -.
DR EnsemblMetazoa; C50C3.6.1; C50C3.6.1; WBGene00004187.
DR GeneID; 176153; -.
DR KEGG; cel:CELE_C50C3.6; -.
DR UCSC; C50C3.6; c. elegans.
DR CTD; 176153; -.
DR WormBase; C50C3.6; CE00122; WBGene00004187; prp-8.
DR eggNOG; KOG1795; Eukaryota.
DR GeneTree; ENSGT00390000015210; -.
DR HOGENOM; CLU_000380_3_0_1; -.
DR InParanoid; P34369; -.
DR OMA; VCMRREK; -.
DR OrthoDB; 156083at2759; -.
DR PhylomeDB; P34369; -.
DR Reactome; R-CEL-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-CEL-72165; mRNA Splicing - Minor Pathway.
DR EvolutionaryTrace; P34369; -.
DR PRO; PR:P34369; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00004187; Expressed in embryo and 4 other tissues.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0005682; C:U5 snRNP; IBA:GO_Central.
DR GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR GO; GO:0097157; F:pre-mRNA intronic binding; IBA:GO_Central.
DR GO; GO:0030619; F:U1 snRNA binding; IBA:GO_Central.
DR GO; GO:0030620; F:U2 snRNA binding; IBA:GO_Central.
DR GO; GO:0030623; F:U5 snRNA binding; IBA:GO_Central.
DR GO; GO:0017070; F:U6 snRNA binding; IBA:GO_Central.
DR GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; IBA:GO_Central.
DR CDD; cd13838; RNase_H_like_Prp8_IV; 1.
DR Gene3D; 1.20.80.40; -; 1.
DR Gene3D; 3.30.420.230; -; 1.
DR Gene3D; 3.30.43.40; -; 1.
DR InterPro; IPR000555; JAMM/MPN+_dom.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR012591; PRO8NT.
DR InterPro; IPR012592; PROCN.
DR InterPro; IPR012984; PROCT.
DR InterPro; IPR027652; PRP8.
DR InterPro; IPR021983; PRP8_domainIV.
DR InterPro; IPR043173; Prp8_domainIV_fingers.
DR InterPro; IPR043172; Prp8_domainIV_palm.
DR InterPro; IPR019581; Prp8_U5-snRNA-bd.
DR InterPro; IPR042516; Prp8_U5-snRNA-bd_sf.
DR InterPro; IPR019580; Prp8_U6-snRNA-bd.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR019582; RRM_spliceosomal_PrP8.
DR PANTHER; PTHR11140; PTHR11140; 1.
DR Pfam; PF01398; JAB; 1.
DR Pfam; PF08082; PRO8NT; 1.
DR Pfam; PF08083; PROCN; 1.
DR Pfam; PF08084; PROCT; 1.
DR Pfam; PF12134; PRP8_domainIV; 1.
DR Pfam; PF10598; RRM_4; 1.
DR Pfam; PF10597; U5_2-snRNA_bdg; 1.
DR Pfam; PF10596; U6-snRNA_bdg; 1.
DR SMART; SM00232; JAB_MPN; 1.
DR SUPFAM; SSF53098; SSF53098; 2.
DR PROSITE; PS50249; MPN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW Ribonucleoprotein; RNA-binding; Spliceosome.
FT CHAIN 1..2329
FT /note="Pre-mRNA-splicing factor 8 homolog"
FT /id="PRO_0000097039"
FT DOMAIN 2096..2227
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 804..1295
FT /note="Reverse transcriptase homology domain"
FT REGION 1296..1570
FT /note="Linker"
FT REGION 1506..1519
FT /note="Important for branch point selection"
FT /evidence="ECO:0000250"
FT REGION 1574..1745
FT /note="Restriction endonuclease homology domain"
FT REGION 1760..2013
FT /note="RNase H homology domain"
FT COMPBIAS 16..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 2063..2073
FT /evidence="ECO:0007829|PDB:2P8R"
FT HELIX 2074..2081
FT /evidence="ECO:0007829|PDB:2P8R"
FT STRAND 2082..2085
FT /evidence="ECO:0007829|PDB:2P8R"
FT STRAND 2092..2094
FT /evidence="ECO:0007829|PDB:2P8R"
FT STRAND 2096..2100
FT /evidence="ECO:0007829|PDB:2P8R"
FT HELIX 2101..2109
FT /evidence="ECO:0007829|PDB:2P8R"
FT STRAND 2113..2115
FT /evidence="ECO:0007829|PDB:2P8R"
FT STRAND 2118..2124
FT /evidence="ECO:0007829|PDB:2P8R"
FT STRAND 2132..2139
FT /evidence="ECO:0007829|PDB:2P8R"
FT STRAND 2142..2145
FT /evidence="ECO:0007829|PDB:2P8R"
FT TURN 2160..2164
FT /evidence="ECO:0007829|PDB:2P8R"
FT STRAND 2165..2176
FT /evidence="ECO:0007829|PDB:2P8R"
FT HELIX 2183..2195
FT /evidence="ECO:0007829|PDB:2P8R"
FT TURN 2201..2203
FT /evidence="ECO:0007829|PDB:2P8R"
FT STRAND 2205..2212
FT /evidence="ECO:0007829|PDB:2P8R"
FT STRAND 2215..2223
FT /evidence="ECO:0007829|PDB:2P8R"
FT HELIX 2225..2233
FT /evidence="ECO:0007829|PDB:2P8R"
FT HELIX 2246..2248
FT /evidence="ECO:0007829|PDB:2P8R"
FT STRAND 2249..2257
FT /evidence="ECO:0007829|PDB:2P8R"
FT STRAND 2263..2267
FT /evidence="ECO:0007829|PDB:2P8R"
FT HELIX 2278..2280
FT /evidence="ECO:0007829|PDB:2P8R"
FT STRAND 2289..2291
FT /evidence="ECO:0007829|PDB:2P8R"
FT HELIX 2300..2302
FT /evidence="ECO:0007829|PDB:2P8R"
SQ SEQUENCE 2329 AA; 272028 MW; 626F9F97C800960C CRC64;
MANYGGHPQT EPHAIPDSIL EEKSRKWKQL QGKRYSEKKK FGMSDTQKEE MPPEHVRKVI
RDHGDMTSRK YRHDKRVYLG ALKYMPHAVL KLLENMPMPW EQIRDVKVLY HITGAITFVN
DIPRVIEPVY MAQWGTMWIM MRREKRDRRH FKRMRFPPFD DEEPPLDYAD NILDVEPLEP
IQMELDPEED GAVAEWFYDH KPLATTRFVN GPTYRKWAFS IPQMSTLYRL ANQLLTDLVD
DNYFYLFDMK SFFTAKALNV AIPGGPKFEP LVKDLHTDED WNEFNDINKV IIRAPIRTEY
RIAFPFMYNN LISSLPVQVS WYHTPSVVFI KTEDPDLPAF YYDPLINPIV LSNLKATEEN
LPEGEEEDEW ELPEDVRPIF EDVPLYTDNT ANGLALLWAP RPFNLRSGRT RRAVDVPLVK
SWYREHCPAG MPVKVRVSYQ KLLKVFVLNA LKHRPPKPQK RRYLFRSFKA TKFFQTTTLD
WVEAGLQVLR QGYNMLNLLI HRKNLNYLHL DYNFNLKPVK TLTTKERKKS RFGNAFHLCR
EILRLTKLVV DAHVQYRLNN VDAYQLADGL QYIFAHVGQL TGMYRYKYKL MRQVRMCKDL
KHLIYYRFNT GPVGKGPGCG FWAPGWRVWL FFLRGITPLL ERWLGNLLSR QFEGRHSKGV
AKTVTKQRVE SHFDLELRAA VMHDILDMMP DGIKQNKARV ILQHLSEAWR CWKANIPWKV
PGLPTPVENM ILRYVKAKAD WWTNSAHYNR ERVRRGATVD KTVCKKNLGR LTRLYLKSEQ
ERQHNYLKDG PYISAEEAVA IYTTTVHWLE SRRFSPIPFP PLSYKHDTKL LILALERLKE
SYSVKNRLNQ SQREELALIE QAYDNPHEAL SRIKRHMLTQ RAFKEVGIEF MDLYTHLIPV
YDIEPLEKVT DAYLDQYLWY EADKRRLFPA WVKPGDTEPP PLLTYKWCQG LNNLQDVWET
SEGECNVIME TKLEKIAEKM DLTLLNRLLR LIVDHNIADY MTSKNNVLIN YKDMNHTNSF
GIIRGLQFAS FIVQFYGLVL DLLVLGLRRA SEIAGPPQCP NEFLQFQDVA TEIGHPIRLY
CRYIDRVWIM FRFSADEARD LIQRYLTEHP DPNNENIVGY NNKKCWPRDA RMRLMKHDVN
LGRAVFWDIK NRLPRSITTV EWENSFVSVY SKDNPNMLFD MSGFECRILP KCRTANEEFV
HRDGVWNLQN EVTKERTAQC FLKVDEESLS KFHNRIRQIL MSSGSTTFTK IVNKWNTALI
GLMTYFREAV VNTQELLDLL VKCENKIQTR IKIGLNSKMP SRFPPVVFYT PKEIGGLGML
SMGHVLIPQS DLRWMQQTEA GGVTHFRSGM SHDEDQLIPN LYRYIQPWEA EFVDSVRVWA
EYALKRQEAN AQNRRLTLED LDDSWDRGIP RINTLFQKDR HTLAYDKGWR VRTEFKAYQI
LKQNPFWWTH QRHDGKLWNL NNYRTDMIQA LGGVEGILEH TLFRGTYFPT WEGLFWERAS
GFEESMKFKK LTNAQRSGLN QIPNRRFTLW WSPTINRANV YVGFQVQLDL TGIFMHGKIP
TLKISLIQIF RAHLWQKIHE SVVMDLCQVF DQELDALEIQ TVQKETIHPR KSYKMNSSCA
DVLLFAQYKW NVSRPSLMAD SKDVMDNTTT QKYWLDVQLR WGDYDSHDVE RYARAKFLDY
TTDNMSIYPS PTGVLIAIDL AYNLYSAYGN WFPGMKPLIR QAMAKIIKAN PAFYVLRERI
RKGLQLYSSE PTEPYLTSQN YGELFSNQII WFVDDTNVYR VTIHKTFEGN LTTKPINGAI
FIFNPRTGQL FLKIIHTSVW AGQKRLSQLA KWKTAEEVAA LIRSLPVEEQ PRQIIVTRKA
MLDPLEVHLL DFPNIVIKGS ELMLPFQAIM KVEKFGDLIL KATEPQMVLF NLYDDWLKTI
SSYTAFSRVV LIMRGMHINP DKTKVILKPD KTTITEPHHI WPTLSDDDWI KVELALKDMI
LADYGKKNNV NVASLTQSEV RDIILGMEIS APSQQRQQIA DIEKQTKEQS QVTATTTRTV
NKHGDEIITA TTSNYETASF ASRTEWRVRA ISSTNLHLRT QHIYVNSDDV KDTGYTYILP
KNILKKFITI SDLRTQIAGF MYGVSPPDNP QVKEIRCIVL VPQTGSHQQV NLPTQLPDHE
LLRDFEPLGW MHTQPNELPQ LSPQDVTTHA KLLTDNISWD GEKTVMITCS FTPGSVSLTA
YKLTPSGYEW GKANTDKGNN PKGYMPTHYE KVQMLLSDRF LGYFMVPSNG VWNYNFQGQR
WSPAMKFDVC LSNPKEYYHE DHRPVHFHNF KAFDDPLGTG SADREDAFA
