YSH1_CANGA
ID YSH1_CANGA Reviewed; 771 AA.
AC Q6FUA5;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Endoribonuclease YSH1;
DE EC=3.1.27.-;
DE AltName: Full=mRNA 3'-end-processing protein YSH1;
GN Name=YSH1; OrderedLocusNames=CAGL0F05005g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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}.
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DR EMBL; CR380952; CAG59113.1; -; Genomic_DNA.
DR RefSeq; XP_446189.1; XM_446189.1.
DR AlphaFoldDB; Q6FUA5; -.
DR SMR; Q6FUA5; -.
DR STRING; 5478.XP_446189.1; -.
DR EnsemblFungi; CAG59113; CAG59113; CAGL0F05005g.
DR GeneID; 2887906; -.
DR KEGG; cgr:CAGL0F05005g; -.
DR CGD; CAL0131318; CAGL0F05005g.
DR VEuPathDB; FungiDB:CAGL0F05005g; -.
DR eggNOG; KOG1137; Eukaryota.
DR HOGENOM; CLU_009673_2_3_1; -.
DR InParanoid; Q6FUA5; -.
DR OMA; VMIPRRC; -.
DR Proteomes; UP000002428; Chromosome F.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IEA:EnsemblFungi.
DR GO; GO:0004521; F:endoribonuclease activity; IEA:EnsemblFungi.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006378; P:mRNA polyadenylation; IEA:EnsemblFungi.
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..771
FT /note="Endoribonuclease YSH1"
FT /id="PRO_0000238899"
FT ACT_SITE 407
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 429
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 771 AA; 86653 MW; D2B9D3BCF9A499A6 CRC64;
MDVKERSNQF RFFSLGGGNE VGRSCHIIQF KGKTIMLDAG IHPAYQGMAS LPFYDDFDLS
IVDVLLISHF HLDHAASLPY VMQKTNFKGR VFMTHPTKAI YRWLLRDFVR VTSIGSQSSN
AEDDNLYSNE DLIESFDKIE TIDYHSMIDV NGIKFTAFHA GHVLGAAMFQ IEIAGLRVLF
TGDYSREIDR HLNSAEVPPL PSDILIVEST FGTATHEPRL HREKKLTQLI HSTVNKGGRV
LMPVFALGRA QELMLILDEY WSQHKEELGS NQIPIFYASN LARKCLSVFQ TYVNMMNDNI
RKKFRDSQTN PFIFKNIAYI KNLDEFQDFG PSVMLASPGM LQNGLSRDLL ERWCPDEKNL
VLITGYSVEG TMAKYLLLEP DTIPSVSNPE VTIPRRCRVE ELSFAAHVDF QENLEFIEQI
NASNIILVHG EPNPMGRLKS ALLSNYASFK GTEDEVHVHN PRNCYELDIE CKGVKVAKAV
GNIVDEIKRT EEEVVKPEND AGQSKEGIEE FTGKTQDVRK DAEGEGAIIS SILVSDEKNF
DLNLVSLSDL REHHPELSTT VIRERQTIQV DCKKELIYWH ICQMFGDVSV LIDDDNVTNT
KETKLETSRG MLVLQIMGAI RLTVQHNKAI LEWTQGLISD TIADSIIAIL MSVDSAPVSV
KKSSNSCSHG HEHATPILSQ PSETDKIKQV AELFKTQFGD SFTLILNKDD DNDTAEEKED
DEFVKGLITI GKNTASINFT DMCVVECNSN PLKGRVESLL KIGIDMVSSL C
