YSH1_CRYNB
ID YSH1_CRYNB Reviewed; 773 AA.
AC P0CM89; Q55IQ8; Q5KCZ0;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Endoribonuclease YSH1;
DE EC=3.1.27.-;
DE AltName: Full=mRNA 3'-end-processing protein YSH1;
GN Name=YSH1; OrderedLocusNames=CNBL2750;
OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=283643;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-3501A;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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; AAEY01000057; EAL17762.1; -; Genomic_DNA.
DR RefSeq; XP_772409.1; XM_767316.1.
DR AlphaFoldDB; P0CM89; -.
DR SMR; P0CM89; -.
DR EnsemblFungi; AAW45137; AAW45137; CNH02710.
DR EnsemblFungi; EAL17762; EAL17762; CNBL2750.
DR GeneID; 4939324; -.
DR KEGG; cnb:CNBL2750; -.
DR VEuPathDB; FungiDB:CNBL2750; -.
DR HOGENOM; CLU_009673_2_2_1; -.
DR Proteomes; UP000001435; Chromosome 12.
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 Zinc.
FT CHAIN 1..773
FT /note="Endoribonuclease YSH1"
FT /id="PRO_0000410047"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 421
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 443
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 773 AA; 85729 MW; F0CC85343EEA2D19 CRC64;
MIPRRHHFKP APQPTVQVLQ PPDEDAPSLT ITMLGAGQEV GRSCCVIEHR GKKIVCDAGL
HPAQPGIGAL PFIDELDWST VDAMLITHFH VDHAAALPYI MEKTNFKDGN GKVYMTHATK
AIYGLTMMDT VRLNDQNPDT SGRLYDEADV QSSWQSTIAV DYHQDIVIAG GLRFTPYHAG
HVLGASMFLI EIAGLKILYT GDYSREEDRH LVMAEIPPVK PDVMICESTF GVHTLPDRKE
KEEQFTTLVA NIVRRGGRCL MPIPSFGNGQ ELALLLDEYW NDHPELQNIP VYFASSLFQR
GMRVYKTYVH TMNANIRSRF ARRDNPFDFR FVKWLKDPQK LRENKGPCVI MSSPQFMSFG
LSRDLLEEWA PDSKNGVIVT GYSIEGTMAR TLLSEPDHIE SLKGGNVPRR LTVKEISFGA
HVDYAQNSKF IQEIGAQHVV LVHGEASQMG RLRAALRDTY AAKGQEINIH TPKNCEPLTL
TFRQERMVKA IGSLAATRPE HGTSVKGLLV SKDFSYTLLS PADLHDFTGL STSTIIQKQG
VAISVDWAVV RWYLEGMYGE VEEGVEEEGK AAFIIMNGVQ VVQISPTAVE LRWKSSSSND
MIADSALALL LGIDGSPATA KLTASPNKHA CNHSNSHSHT DLYPHTYPGD KSAKDVASNP
EFERLRMFLE AHFGHVEGPN LRPPLPPGAD GDGNDDKDKD GDDWLTMDVK LDNQTARIDL
ISMRVESESA ELQKRVETVL EMALTTVKSL SQTFLGGGLD VDMVKVEPNE SDS
