SYF1_SCHPO
ID SYF1_SCHPO Reviewed; 790 AA.
AC Q9P7R9;
DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 146.
DE RecName: Full=Pre-mRNA-splicing factor cwf3;
DE AltName: Full=Complexed with cdc5 protein 3;
GN Name=cwf3; Synonyms=syf1; ORFNames=SPBC211.02c;
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 [GENOMIC DNA], AND PROTEIN SEQUENCE OF 9-27; 460-475
RP AND 511-535.
RX PubMed=10409726; DOI=10.1128/mcb.19.8.5352;
RA McDonald W.H., Ohi R., Smelkova N., Frendewey D., Gould K.L.;
RT "Myb-related fission yeast cdc5p is a component of a 40S snRNP-containing
RT complex and is essential for pre-mRNA splicing.";
RL Mol. Cell. Biol. 19:5352-5362(1999).
RN [2]
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 [3]
RP IDENTIFICATION IN THE CWF 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).
CC -!- FUNCTION: Involved in pre-mRNA splicing and cell cycle progression.
CC {ECO:0000250}.
CC -!- SUBUNIT: Belongs to the 40S cdc5-associated complex (or cwf complex), a
CC spliceosome sub-complex reminiscent of a late-stage spliceosome
CC composed of the U2, U5 and U6 snRNAs and at least brr2, cdc5,
CC cwf2/prp3, cwf3/syf1, cwf4/syf3, cwf5/ecm2, spp42/cwf6, cwf7/spf27,
CC cwf8, cwf9, cwf10, cwf11, cwf12, prp45/cwf13, cwf14, cwf15, cwf16,
CC cwf17, cwf18, cwf19, cwf20, cwf21, cwf22, cwf23, cwf24, cwf25, cwf26,
CC cyp7/cwf27, cwf28, cwf29/ist3, lea1, msl1, prp5/cwf1, prp10,
CC prp12/sap130, prp17, prp22, sap61, sap62, sap114, sap145, slu7, smb1,
CC smd1, smd3, smf1, smg1 and syf2. {ECO:0000269|PubMed:11884590}.
CC -!- INTERACTION:
CC Q9P7R9; P39964: cdc5; NbExp=7; IntAct=EBI-538809, EBI-538771;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the crooked-neck family. {ECO:0000305}.
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DR EMBL; AF251149; AAG01400.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB75410.1; -; Genomic_DNA.
DR PIR; T50337; T50337.
DR RefSeq; NP_596612.1; NM_001022533.2.
DR PDB; 3JB9; EM; 3.60 A; r=498-653.
DR PDBsum; 3JB9; -.
DR AlphaFoldDB; Q9P7R9; -.
DR SMR; Q9P7R9; -.
DR BioGRID; 277274; 27.
DR IntAct; Q9P7R9; 8.
DR STRING; 4896.SPBC211.02c.1; -.
DR MaxQB; Q9P7R9; -.
DR PaxDb; Q9P7R9; -.
DR PRIDE; Q9P7R9; -.
DR EnsemblFungi; SPBC211.02c.1; SPBC211.02c.1:pep; SPBC211.02c.
DR GeneID; 2540753; -.
DR KEGG; spo:SPBC211.02c; -.
DR PomBase; SPBC211.02c; cwf3.
DR VEuPathDB; FungiDB:SPBC211.02c; -.
DR eggNOG; KOG2047; Eukaryota.
DR HOGENOM; CLU_007736_0_0_1; -.
DR InParanoid; Q9P7R9; -.
DR OMA; FLMQQPL; -.
DR PhylomeDB; Q9P7R9; -.
DR Reactome; R-SPO-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-SPO-6782135; Dual incision in TC-NER.
DR Reactome; R-SPO-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR PRO; PR:Q9P7R9; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0071014; C:post-mRNA release spliceosomal complex; IDA:PomBase.
DR GO; GO:0000974; C:Prp19 complex; IDA:PomBase.
DR GO; GO:0005681; C:spliceosomal complex; IDA:PomBase.
DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IBA:GO_Central.
DR GO; GO:0071004; C:U2-type prespliceosome; ISO:PomBase.
DR GO; GO:0000349; P:generation of catalytic spliceosome for first transesterification step; IBA:GO_Central.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IC:PomBase.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR Gene3D; 1.25.40.10; -; 4.
DR InterPro; IPR003107; HAT.
DR InterPro; IPR008847; Suf.
DR InterPro; IPR045075; Syf1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR11246; PTHR11246; 1.
DR Pfam; PF05843; Suf; 1.
DR SMART; SM00386; HAT; 13.
DR SUPFAM; SSF48452; SSF48452; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; mRNA processing; mRNA splicing;
KW Nucleus; Reference proteome; Repeat; Spliceosome.
FT CHAIN 1..790
FT /note="Pre-mRNA-splicing factor cwf3"
FT /id="PRO_0000205734"
FT REPEAT 12..44
FT /note="HAT 1"
FT REPEAT 45..77
FT /note="HAT 2"
FT REPEAT 89..121
FT /note="HAT 3"
FT REPEAT 123..157
FT /note="HAT 4"
FT REPEAT 159..190
FT /note="HAT 5"
FT REPEAT 193..228
FT /note="HAT 6"
FT REPEAT 233..266
FT /note="HAT 7"
FT REPEAT 268..303
FT /note="HAT 8"
FT REPEAT 331..364
FT /note="HAT 9"
FT REPEAT 368..402
FT /note="HAT 10"
FT REPEAT 404..440
FT /note="HAT 11"
FT REPEAT 457..492
FT /note="HAT 12"
FT REPEAT 494..526
FT /note="HAT 13"
FT REPEAT 528..562
FT /note="HAT 14"
FT REPEAT 567..601
FT /note="HAT 15"
FT REPEAT 639..673
FT /note="HAT 16"
FT REPEAT 675..709
FT /note="HAT 17"
FT REGION 769..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 790 AA; 92637 MW; 4915D160DD83F324 CRC64;
MGDVIPLKVN FDLINVDDEP FELELLRDPY SLKSWLRYIK THEGSTLEKR VLLFERACSE
LPGSYKIWKS YLELRVAHVE HLNPYFHAEA FASVNDCFER SLILLHKMPV IWKLYLQFLM
KQPNVTKIRC TFNSALRALP VTQHDDIWDM FTKYAEDIGG LFCIHVYRRY IQVEPRAIEN
YIEILCKLGL WNEAARQYED ILNRPVFLSA KRKSNYQIWL EFSELVVQHP DHTQNIDVEK
VFRAGIKRFS DQAGKLWTYL AQYYIRIGDY EKARSTFYEG MNNIMTVRNF TIIFDAFVEF
EEQWLSARVE ASSGNANDEL SIDFHMAWLE KILDKRPLYI NDVLLRQNIN NVDEWLRRVK
FLEDDSEKVV QVYTDAIKNV NPKLAHGSLG KLFSEFARFY ENFDDLEQSR IIFEKATHVP
YKTVNELAQV WIDWAEMELR HQNFDAARKL IGDAVHAPRK SHISFFDESL SPQVRLHKSS
KIWMYYLDLE ESVGTIETTR KLYDRVFELK IATPQVVVNY ANLLEENAYF EDSFKIYERG
VALFSYPVAF ELWNLYLTKF VKRYQGTHME RTRDLFEQAL EGCPPEFSKS IYLLYADFEE
KFGKAKRSIS ILEKAADKVK TADRLAIYNV LLVKVALNYG VLATRTVYEK AIESLSDSEV
KDMCLRFAEM ETKLGEIDRA RLIYIHGSQY CDPRVETDYW KAWQEFEIRY GNPEETVKEM
LRIKRSVQTK FSTDSLHIAK RAAKIESAAA PMDPMEQLEM EKSEGPKALA GFVLSKSNPQ
ETSKITGEEN
