YSH1_USTMA
ID YSH1_USTMA Reviewed; 880 AA.
AC Q4PEJ3; A0A0D1E796;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Endoribonuclease YSH1;
DE EC=3.1.27.-;
DE AltName: Full=mRNA 3'-end-processing protein YSH1;
GN Name=YSH1; ORFNames=UMAG_01470;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the cleavage factor I (CF I) involved in pre-
CC mRNA 3'-end processing. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA-
CC metabolizing metallo-beta-lactamase-like family. CPSF2/YSH1 subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM003142; KIS70295.1; -; Genomic_DNA.
DR RefSeq; XP_011387532.1; XM_011389230.1.
DR AlphaFoldDB; Q4PEJ3; -.
DR SMR; Q4PEJ3; -.
DR STRING; 5270.UM01470P0; -.
DR PRIDE; Q4PEJ3; -.
DR EnsemblFungi; KIS70295; KIS70295; UMAG_01470.
DR GeneID; 23562480; -.
DR KEGG; uma:UMAG_01470; -.
DR VEuPathDB; FungiDB:UMAG_01470; -.
DR eggNOG; KOG1137; Eukaryota.
DR HOGENOM; CLU_009673_2_0_1; -.
DR InParanoid; Q4PEJ3; -.
DR OMA; VMIPRRC; -.
DR OrthoDB; 218195at2759; -.
DR Proteomes; UP000000561; Chromosome 3.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IBA:GO_Central.
DR GO; GO:0008409; F:5'-3' exonuclease activity; IBA:GO_Central.
DR GO; GO:0004521; F:endoribonuclease activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006398; P:mRNA 3'-end processing by stem-loop binding and cleavage; IBA:GO_Central.
DR GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
DR GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IEA:EnsemblFungi.
DR GO; GO:0031126; P:sno(s)RNA 3'-end processing; IEA:EnsemblFungi.
DR GO; GO:0034247; P:snoRNA splicing; IEA:EnsemblFungi.
DR GO; GO:0006369; P:termination of RNA polymerase II transcription; IEA:EnsemblFungi.
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; PF00753; Lactamase_B; 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 Endonuclease; Hydrolase; Metal-binding; mRNA processing; Nuclease; Nucleus;
KW Reference proteome; Zinc.
FT CHAIN 1..880
FT /note="Endoribonuclease YSH1"
FT /id="PRO_0000238907"
FT REGION 618..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..751
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 413
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 435
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 880 AA; 97869 MW; 5741012284ABA7E3 CRC64;
MAPSVVPQSA AGGAALQASA DDQLTIEMLG AGQEVGRSCC VLKYRGKTIV CDTGVHPAFT
GIAALPFIDE LDWSTVDAIL ITHFHLDHAA ALTYIMEKTN FRDGHGKVYM THPTKAVYRF
LMSDFVRISN AGNDDNLFDE NEMLASWRQI EAVDFHQDVS IAGGLRFTSY HAGHVLGACM
FLIEIAGLRI LYTGDFSREE DRHLVQAEIP PVKPDVLICE STYGTQTHEP RLDKEHRFTS
QIHHIIKRGG RVLLPVFVLG RAQELLLLLD EYWAAHPELH SVPIYYASAL AKKCISVYQT
YIHTMNDHIR TRFNRRDNPF VFKHISNLRS LEKFEDRGPC VMMASPGFMQ SGVSRELLER
WAPDKRNGLI VSGYSVEGTM ARNILNEPDE IIGINGQKIP RRMSVDYISF SAHVDFAQNS
RFIDEIKAQH IVLVHGEQNN MSKLRAALQA RFTARGSDVK IHTPRNCEPL VLQFRAQRTA
KAIGTIAAKP PAQGDIVDGL LISKDFAYTI LDPKDLTDFT GLSTSTIVQR QRVALAVSWE
MVRWHLQGMY GRLQEGVDAE EGLRTLRIMG AVDVRQSARH ELLVEWVSSI ANDMVADSIV
ALLLGIDSAP SSVKMTMHNH HHHHHHHHHH HPGDAKAEET DDDAEATTED EEARTPTESA
ANLPMHPFSE AALVAESEVR AKAATDEAVH RDAYQLAKME HMAAFLEAHF GQVEELVIPE
APISEEIEES VPKVKVETER EAEKDEAGDE SMSTLQPEPD SVTDVDKPEL APPAEQATAS
PPISIASLFD GEARSALRVF LDEAEAVIDV ENLVILASSE SFRARVQHLC TLALRSFTSL
SDAFYLPQQM GTSLFQGKHS QLATIPEFGE ERPSKMVRSS
