PRP8_DICDI
ID PRP8_DICDI Reviewed; 2327 AA.
AC Q8T295; Q554T3;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Pre-mRNA-processing-splicing factor 8 homolog;
DE AltName: Full=Splicing factor Prp8;
GN Name=prpf8; Synonyms=prp8; ORFNames=DDB_G0274229;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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 speckle {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. {ECO:0000250}.
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; AAFI02000012; EAL70007.1; -; Genomic_DNA.
DR RefSeq; XP_644240.1; XM_639148.1.
DR AlphaFoldDB; Q8T295; -.
DR SMR; Q8T295; -.
DR STRING; 44689.DDB0233128; -.
DR PaxDb; Q8T295; -.
DR PRIDE; Q8T295; -.
DR EnsemblProtists; EAL70007; EAL70007; DDB_G0274229.
DR GeneID; 8619668; -.
DR KEGG; ddi:DDB_G0274229; -.
DR dictyBase; DDB_G0274229; prpf8.
DR eggNOG; KOG1795; Eukaryota.
DR HOGENOM; CLU_000380_3_0_1; -.
DR InParanoid; Q8T295; -.
DR OMA; VCMRREK; -.
DR PhylomeDB; Q8T295; -.
DR Reactome; R-DDI-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-DDI-72165; mRNA Splicing - Minor Pathway.
DR PRO; PR:Q8T295; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
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:0006397; P:mRNA processing; ISS:dictyBase.
DR GO; GO:0008380; P:RNA splicing; ISS:dictyBase.
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 3: Inferred from homology;
KW mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW Ribonucleoprotein; RNA-binding; Spliceosome.
FT CHAIN 1..2327
FT /note="Pre-mRNA-processing-splicing factor 8 homolog"
FT /id="PRO_0000327448"
FT DOMAIN 2093..2223
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 801..1292
FT /note="Reverse transcriptase homology domain"
FT REGION 1293..1566
FT /note="Linker"
FT REGION 1502..1515
FT /note="Important for branch point selection"
FT /evidence="ECO:0000250"
FT REGION 1570..1740
FT /note="Restriction endonuclease homology domain"
FT REGION 1657..2023
FT /note="Involved in interaction with pre-mRNA 5' splice
FT site"
FT /evidence="ECO:0000250"
FT REGION 1755..2008
FT /note="RNase H homology domain"
SQ SEQUENCE 2327 AA; 272196 MW; F2B761E99EEF5EA9 CRC64;
MDDTNSNINQ SNESQHLEEK AKKWIQLNNK KYSEKRKFGA VEIRKEDMPP EHLRKIIKDH
GDMSNRRFRD DKRVYLGALK YMPHAILKLL ENIPMPWEQV KYVKVLYHLS GAITFVNEIP
FVIEPIYIAQ WATMWVTMRR EKRDRTHFRR MKFPLFDDEE PPLDYSDNIL DNEVEDPIQM
ELDENDDSEV IDWLYDSKPL VNTKFVNGSS YRKWRLNLPI MSTLFRLASP LLSDLTDSNY
FYLFDDNSFF TSKALNMAIP GGPKFEPLFR DVDDDDEDWN EFNDINKVII RNKIRTEYKI
AFPYLYNSRP RKVKTPTYHT PNNCYIKNDS PDLPGFYFGA ALNPIPSYKT SGNKNEQSEY
GTEDDEFQLP EEIETILSKT EIEHDNLANG IQLYWAPRPF SLRSGTTRRA EDIPLVKSWY
KEHCPSEHPV KVRVSYQKLL KCHVLNKLHH RKPKAQTKRN LFKSLKATKF FQSTEIDWVE
AGLQVCRQGY NMLNLLIHRK NLNYLHLDYN FYLKPIKTLT TKERKKSRFG NAFHLCREIL
RLTKLVVDVH VKFRLGDADA FQLADAIQYL FSHLGLLTGM YKYKYRLMRQ IRMCKDLKHL
IYYRFNTGAV GKGPGCGFWA PMWRVWLFFL RGIVPLLERW LGNLLARQFE GRQTKGMAKT
VTKQRVESHF DYELRAAVMH DILDMMPEGI KANKSRIILQ HLSEAWRCWK SNIPWKVPGL
PIPIENMILR YVKSKADWWT NIAHYNRERI KRGATIDKTA SKKNLGRLTR LWLKAEQERQ
HNYLKDGPYV SAEEAVAIYT TTVHWLEKRR FSAIPFPQTS YKHDIKILTL ALERLKEAYS
VKSRLNQSQR EELSLVEQAY DNPHDALARI KRHLLTQRTF KEVGIEFMDM YTHLVPIYDV
DPFEKITDAY LDQYLWYEAD KRQLFPNWVK PSDNEPPPVL IHKWCQGINN LDQVWETSQG
ECVVLLETQF SKVYEKMDLT LMNRLLRLIV DQNIADYMSG KNNVVINYKD MNHTNSYGLI
RGLQFASFIF QYYGLVLDLL VLGLERASAL AGPPNLPNSF LTFPSVQTET AHPIRLYSRY
VDRIHVLYKF TADEARKLIQ KYMSEHPDPN NENVVGYNNK KCWPRDCRMR LMKHDVNLGR
AVFWQIKNRL PRSLTTIDWE DSFVSVYSKD NPNLLMNMAG FDIRILPKCR TPLDQLAPKD
AVWSLQNVNT KERTAQAFLR VDTESQERFE NRIRMILMAS GSTTFTKIVN KWNTALIGLM
TYYREAVVTT REMLDILVRC ENKIQTRVKI GLNSKMPNRF PPVVFYTPKE LGGLGMLSMG
HVLIPQSDLK YSKQTDTGIT HFTSGMSHDE DQLIPNLYRY IQPWEQEIKD SQRVWAEYAI
KYEEAKSQNK NLTLEDLEDS WDRGIPRINT LFQKSRHTLA YDKGWRVRTD WKQYQVLKNN
PFWWTNQRHD GKLWNLNNYR TDIIQALGGV EGILEHTLFK GTYFPTWEGL FWEKASGFEE
SMKYKKLTHA QRSGLNQIPN RRFTLWWSPT INRKNVYVGF QVQLDLTGIF MHGKIPTLKI
SLIQIFRAHL WQKIHESLVM DLCQVFDQEL DNLEISVVNK EAIHPRKSYK MNSSCADILL
RATHKWQVSR PSLLNDNRDT YDNTTTQYWL DVQLKWGDFD SHDIERYSRA KFLDYTTDSM
SLYPSPTGCL IGLDLAYNIY SSFGNWFLGV KPLVQKAMAK ILKSNPALYV LRERIRKGLQ
LYSSEPTEPY LSSQNFGELF SNKIMWFVDD SNVYRVTIHK TFEGNLTTKP INGAIFIFNP
RTGQLFLKII HTDVWLGQKR LGQLAKWKTA EEVAALIRSL PVEEQPKQII ATRKGMMDPL
EVHLLDFPNI VIQGSELQLP FQACLKVEKF GDLILKATEP KMVLFNIYDD WLSTIHSYTA
FLRLILILRA LHVNLERTKI ILKPNKNVIT QPHHIWPTLT EQEWLTVEGS LKDLILADFG
KRNNVNVASL TQSEIRDIIL GMEISAPSQQ REDQIAEIEK QKTEASHLTA VTVRSTNIHG
EEIITTATSP HEQKVFSSKT DWRVRAISAT NLHLRTNQIY VNSDNAKETG GFTYVFPKNI
LKKFITIADL RTQIMGYCYG ISPPDNPSVK EIRCIVMPPQ WGTPVHVTVP NQLPEHEYLK
DLEPLGWIHT QPTELPQLSP QDVITHSKIM SDNKSWDGEK TVIISVSVAW PCTLTAYHLT
PSGFEWGKNN KDSLNYQGYQ PQFYEKVQML LSDRFLGFYM VPDRGSWNYN FMGVKHSTNM
TYGLKLDYPK NFYDESHRPA HFQNWTQMAP SANDDEENQP ENENLFE
