YSH1_SCHPO
ID YSH1_SCHPO Reviewed; 757 AA.
AC O13794;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Endoribonuclease ysh1;
DE EC=3.1.27.-;
DE AltName: Full=mRNA 3'-end-processing protein ysh1;
GN Name=ysh1; ORFNames=SPAC17G6.16c;
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 REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Component of the cleavage factor I (CF I) involved in pre-
CC mRNA 3'-end processing. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA-
CC metabolizing metallo-beta-lactamase-like family. CPSF2/YSH1 subfamily.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAB16227.2; -; Genomic_DNA.
DR PIR; T37848; T37848.
DR RefSeq; NP_594263.2; NM_001019686.2.
DR AlphaFoldDB; O13794; -.
DR SMR; O13794; -.
DR BioGRID; 278727; 15.
DR STRING; 4896.SPAC17G6.16c.1; -.
DR iPTMnet; O13794; -.
DR MaxQB; O13794; -.
DR PaxDb; O13794; -.
DR PRIDE; O13794; -.
DR EnsemblFungi; SPAC17G6.16c.1; SPAC17G6.16c.1:pep; SPAC17G6.16c.
DR GeneID; 2542258; -.
DR KEGG; spo:SPAC17G6.16c; -.
DR PomBase; SPAC17G6.16c; ysh1.
DR VEuPathDB; FungiDB:SPAC17G6.16c; -.
DR eggNOG; KOG1137; Eukaryota.
DR HOGENOM; CLU_009673_2_3_1; -.
DR InParanoid; O13794; -.
DR OMA; VMIPRRC; -.
DR Reactome; R-SPO-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-SPO-72187; mRNA 3'-end processing.
DR Reactome; R-SPO-77595; Processing of Intronless Pre-mRNAs.
DR PRO; PR:O13794; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0008409; F:5'-3' exonuclease activity; IBA:GO_Central.
DR GO; GO:0004521; F:endoribonuclease activity; ISO:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006379; P:mRNA cleavage; IC:PomBase.
DR GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR022712; Beta_Casp.
DR InterPro; IPR021718; CPSF73-100_C.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR011108; RMMBL.
DR Pfam; PF10996; Beta-Casp; 1.
DR Pfam; PF11718; CPSF73-100_C; 1.
DR Pfam; PF16661; Lactamase_B_6; 1.
DR Pfam; PF07521; RMMBL; 1.
DR SMART; SM01027; Beta-Casp; 1.
DR SMART; SM01098; CPSF73-100_C; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Endonuclease; Hydrolase; Metal-binding; mRNA processing;
KW Nuclease; Nucleus; Reference proteome; Zinc.
FT CHAIN 1..757
FT /note="Endoribonuclease ysh1"
FT /id="PRO_0000238906"
FT REGION 698..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..715
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..757
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 403
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 425
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 757 AA; 85990 MW; 95441DDF49CE8F61 CRC64;
MSKRKEFDED APVDPSDLLE FINLGAGNEV GRSCHVIQYK GKTVMLDAGV HPAYTGLSAL
PFFDEFDLST VDVLLISHFH LDHVASLPYV MQKTNFRGRV FMTHPTKAVC KWLLSDYVKV
SNVGMEDQLY DEKDLLAAFD RIEAVDYHST IEVEGIKFTP YHAGHVLGAC MYFVEMAGVN
ILFTGDYSRE EDRHLHVAEV PPKRPDVLIT ESTYGTASHQ PRLEKEARLL NIIHSTIRNG
GRVLMPVFAL GRAQELLLIL DEYWNNHLDL RSVPIYYASS LARKCMAIFQ TYVNMMNDNI
RKIFAERNPF IFRFVKSLRN LEKFDDIGPS VILASPGMLQ NGVSRTLLER WAPDPRNTLL
LTGYSVEGTM AKQITNEPIE IVSLSGQKIP RRMAVEELSF AAHVDYLQNS EFIDLVNADH
IILVHGEQTN MGRLKSALAS KFHNRKVDVK VYTPRNCVPL YLPFKGERLV RALGKVAVHK
PKEGDIMSGI LIQKDANYKL MSAEDLRDFS DLTTTVLTQK QVIPFFSSME LANFHLKQMF
GYVKQSKTKA GQPQYTVMDA ITLTLIQEHK LALEWVGNIM NDTIADSVIT ILLGIESSPA
SVKLTSHKCN HLHSHLDKPP KVSKEEDRIK KLMMFLDNQF GESMTKTEKG VEIKFEKYEA
SIDFSTMKVE CSNEALRSRV VHVLSRAINT ILPFSEASQN DVSEDDFENE ESDDDKIFEQ
QTKIEDDVKN ENKTEPVEEQ KSEEKNEQPN LKKEELS
