SEB1_SCHPO
ID SEB1_SCHPO Reviewed; 620 AA.
AC Q9UTE3; O74176; Q9UTX2;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 3.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Rpb7-binding protein seb1;
GN Name=seb1; ORFNames=SPAC222.09;
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 418-604, 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 NUCLEOTIDE SEQUENCE [MRNA] OF 528-620.
RA Kawamukai M.;
RT "S.pombe hypothetical protein.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND INTERACTION WITH RPB7.
RX PubMed=12907709; DOI=10.1093/nar/gkg688;
RA Mitsuzawa H., Kanda E., Ishihama A.;
RT "Rpb7 subunit of RNA polymerase II interacts with an RNA-binding protein
RT involved in processing of transcripts.";
RL Nucleic Acids Res. 31:4696-4701(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Involved in the processing of pol II transcripts.
CC {ECO:0000269|PubMed:12907709}.
CC -!- SUBUNIT: Interacts with rpb7. {ECO:0000269|PubMed:12907709}.
CC -!- INTERACTION:
CC Q9UTE3; O14459: rpb7; NbExp=3; IntAct=EBI-608019, EBI-608029;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10759889}.
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DR EMBL; CU329670; CAB60701.1; -; Genomic_DNA.
DR EMBL; AB027948; BAA87252.1; -; Genomic_DNA.
DR EMBL; AB016219; BAA31743.1; -; mRNA.
DR PIR; T43388; T43388.
DR PIR; T50150; T50150.
DR RefSeq; NP_593148.1; NM_001018545.2.
DR PDB; 5MDT; X-ray; 1.62 A; A=1-152.
DR PDB; 5MDU; X-ray; 1.02 A; A=388-540.
DR PDB; 7MI2; X-ray; 1.40 A; A=388-539.
DR PDBsum; 5MDT; -.
DR PDBsum; 5MDU; -.
DR PDBsum; 7MI2; -.
DR AlphaFoldDB; Q9UTE3; -.
DR SMR; Q9UTE3; -.
DR BioGRID; 278429; 44.
DR IntAct; Q9UTE3; 4.
DR STRING; 4896.SPAC222.09.1; -.
DR iPTMnet; Q9UTE3; -.
DR MaxQB; Q9UTE3; -.
DR PaxDb; Q9UTE3; -.
DR PRIDE; Q9UTE3; -.
DR EnsemblFungi; SPAC222.09.1; SPAC222.09.1:pep; SPAC222.09.
DR GeneID; 2541942; -.
DR KEGG; spo:SPAC222.09; -.
DR PomBase; SPAC222.09; seb1.
DR VEuPathDB; FungiDB:SPAC222.09; -.
DR eggNOG; KOG0132; Eukaryota.
DR HOGENOM; CLU_016577_0_0_1; -.
DR InParanoid; Q9UTE3; -.
DR OMA; HAFIKMI; -.
DR PhylomeDB; Q9UTE3; -.
DR PRO; PR:Q9UTE3; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0033620; C:Mei2 nuclear dot complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; EXP:PomBase.
DR GO; GO:0106222; F:lncRNA binding; EXP:PomBase.
DR GO; GO:0003723; F:RNA binding; IDA:PomBase.
DR GO; GO:0099122; F:RNA polymerase II C-terminal domain binding; IPI:PomBase.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; EXP:PomBase.
DR GO; GO:0031124; P:mRNA 3'-end processing; IMP:PomBase.
DR GO; GO:0043628; P:small regulatory ncRNA 3'-end processing; EXP:PomBase.
DR GO; GO:0031126; P:sno(s)RNA 3'-end processing; IMP:PomBase.
DR GO; GO:0006369; P:termination of RNA polymerase II transcription; IMP:PomBase.
DR GO; GO:0030847; P:termination of RNA polymerase II transcription, exosome-dependent; ISO:PomBase.
DR GO; GO:0030846; P:termination of RNA polymerase II transcription, poly(A)-coupled; IMP:PomBase.
DR CDD; cd12331; RRM_NRD1_SEB1_like; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR006569; CID_dom.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR034894; Nrd1/Seb1_RRM.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF04818; CID; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00582; RPR; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS51391; CID; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Phosphoprotein; Reference proteome; RNA-binding.
FT CHAIN 1..620
FT /note="Rpb7-binding protein seb1"
FT /id="PRO_0000081902"
FT DOMAIN 1..151
FT /note="CID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00724"
FT DOMAIN 406..478
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 151..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..580
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT HELIX 4..16
FT /evidence="ECO:0007829|PDB:5MDT"
FT STRAND 17..20
FT /evidence="ECO:0007829|PDB:5MDT"
FT HELIX 23..35
FT /evidence="ECO:0007829|PDB:5MDT"
FT HELIX 36..39
FT /evidence="ECO:0007829|PDB:5MDT"
FT HELIX 40..53
FT /evidence="ECO:0007829|PDB:5MDT"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:5MDT"
FT HELIX 59..79
FT /evidence="ECO:0007829|PDB:5MDT"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:5MDT"
FT HELIX 92..113
FT /evidence="ECO:0007829|PDB:5MDT"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:5MDT"
FT HELIX 119..131
FT /evidence="ECO:0007829|PDB:5MDT"
FT HELIX 137..150
FT /evidence="ECO:0007829|PDB:5MDT"
FT STRAND 390..392
FT /evidence="ECO:0007829|PDB:5MDU"
FT STRAND 400..404
FT /evidence="ECO:0007829|PDB:5MDU"
FT STRAND 407..411
FT /evidence="ECO:0007829|PDB:5MDU"
FT HELIX 419..427
FT /evidence="ECO:0007829|PDB:5MDU"
FT STRAND 432..438
FT /evidence="ECO:0007829|PDB:5MDU"
FT HELIX 439..441
FT /evidence="ECO:0007829|PDB:5MDU"
FT STRAND 443..450
FT /evidence="ECO:0007829|PDB:5MDU"
FT HELIX 451..460
FT /evidence="ECO:0007829|PDB:5MDU"
FT STRAND 462..466
FT /evidence="ECO:0007829|PDB:5MDU"
FT STRAND 469..475
FT /evidence="ECO:0007829|PDB:5MDU"
FT HELIX 482..484
FT /evidence="ECO:0007829|PDB:5MDU"
FT TURN 487..489
FT /evidence="ECO:0007829|PDB:5MDU"
FT STRAND 490..495
FT /evidence="ECO:0007829|PDB:5MDU"
FT HELIX 496..498
FT /evidence="ECO:0007829|PDB:5MDU"
FT HELIX 501..509
FT /evidence="ECO:0007829|PDB:5MDU"
FT STRAND 511..513
FT /evidence="ECO:0007829|PDB:5MDU"
FT TURN 514..517
FT /evidence="ECO:0007829|PDB:7MI2"
FT STRAND 522..527
FT /evidence="ECO:0007829|PDB:5MDU"
SQ SEQUENCE 620 AA; 66440 MW; 20AE8CFC845B0E45 CRC64;
MSGIAEFDGI LDSLEHSKTG ISGSKILKLT NLSMENVSEN AQFVASVYKY AKRAPVTHKL
GALYILDSIV RSFQDGAKKN NESFENPVDA SFSGGWCKAA EITDSLVADA IQHAPSAHLP
KILKLCDIWE KASTFPPEKL ESLRSKLKDA MASTEPVSVD SAAAPSQSTN PEGNGGSVGS
QAAAPTSRPV ENDAASILEA LAAFAQKAPV PSAAEESVST PPQPAVAPSV SAVVPNLPVH
PATAINAQSQ SGNPLSNPLF QPSNVPQSIP SGPMGMKTGS VNDTQSQQIT LMNVLASQNV
PPAQIDSIMK AAFPNYNAPF QPAGVGSVPL PAPTSSQSLR LGSLHRSRSP SPRSGRPRRS
PSPSHLSIPS TLPPADGVPK PTPDGFPRRF ERDPTIPPDS IKVYSRTLFL GGITRSVREP
VLRSMFERFG SVQSLILNHN YRHGFLKMFR RDAAEKAQVA MENVPFADTT IRTKWGVGFG
PRECSDFSTG ISVIPIRLLT DADRTWLVTA EYGGTGGLPI TPGIALDEPD IEIGLGISSK
AISKRGKDFA MRRDERFRGR KPYRGGPPIH HGERHFDSGN DWHGNPSTVP PPTNPYNPGY
PYMDPNYSSG YVSQPPWQPQ
