ID YSH1_CANAL Reviewed; 870 AA.
AC Q59P50; A0A1D8PHM3;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 13-SEP-2023, entry version 93.
DE RecName: Full=Endoribonuclease YSH1;
DE EC=3.1.27.-;
DE AltName: Full=mRNA 3'-end-processing protein YSH1;
GN Name=YSH1; OrderedLocusNames=CAALFM_C206230WA;
GN ORFNames=CaO19.12941, CaO19.5486;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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; CP017624; AOW27631.1; -; Genomic_DNA.
DR RefSeq; XP_711478.1; XM_706386.1.
DR AlphaFoldDB; Q59P50; -.
DR SMR; Q59P50; -.
DR STRING; 237561.Q59P50; -.
DR EnsemblFungi; C2_06230W_A-T; C2_06230W_A-T-p1; C2_06230W_A.
DR GeneID; 3646911; -.
DR KEGG; cal:CAALFM_C206230WA; -.
DR CGD; CAL0000178545; orf19.12941.
DR VEuPathDB; FungiDB:C2_06230W_A; -.
DR eggNOG; KOG1137; Eukaryota.
DR HOGENOM; CLU_009673_2_3_1; -.
DR InParanoid; Q59P50; -.
DR OrthoDB; 169081at2759; -.
DR PRO; PR:Q59P50; -.
DR Proteomes; UP000000559; Chromosome 2.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IBA:GO_Central.
DR GO; GO:0004534; F:5'-3' RNA exonuclease 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:0004521; F:RNA endonuclease activity; IBA:GO_Central.
DR GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
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 CDD; cd16292; CPSF3-like_MBL-fold; 1.
DR Gene3D; 3.40.50.10890; -; 1.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 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 PANTHER; PTHR11203; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR FAMILY MEMBER; 1.
DR PANTHER; PTHR11203:SF11; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR SUBUNIT 3; 1.
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; Metallo-hydrolase/oxidoreductase; 1.
PE 3: Inferred from homology;
KW Endonuclease; Hydrolase; Metal-binding; mRNA processing; Nuclease; Nucleus;
KW Reference proteome; Zinc.
FT CHAIN 1..870
FT /note="Endoribonuclease YSH1"
FT /id="PRO_0000238898"
FT REGION 598..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 499
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 256
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 277
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 277
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 521
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 870 AA; 97899 MW; D403C2942B7B87B7 CRC64;
MCIQPDSLED AYKIPRPVHR EEFTQLSPSF FQTATFQLEK TNEKNNIEEP KKNKAFLNSK
IIYKDLFEIR KLSNNFVNTS HPTCTETMNE QNEFSDEENF KFFGLGGCNE VGRSCHIIEY
KNKVIMLDSG MHPALSGHAS FPYFDEYDIS KVDILLISHF HVDHSASLPY VMQQSNFRGK
VFMTHATKAI YRWLMQDFVR VTSIGNSRSE DGGGGEGSNL YTDDDIMKSF DRIETIDYHS
TMEIDGIRFT AYHAGHVLGA CMYFIEIGGL KVLFTGDYSR EENRHLHAAE VPPLKPDILI
SESTFGTGTL EPRIELERKL TTHIHATIAK GGRVLLPVFA LGNAQELLLI LDEYWSQNED
LQNVNVFYAS NLAKKCMAVY ETYTGIMNDK IRLSSASSEK SNPFDFKYIK SIKDLSKFQD
MGPSVVVATP GMLQAGVSRQ LLEKWAPDGK NLVILTGYSV EGTMAKELLK EPTMIQSATN
PDMTIPRRIG IEEISFAAHV DFQQNSEFIE KVSPSKVILV HGDSVPMGRL KSALLSKYAS
RKGTDQEVKV YNPKNCEELI IGFKGLKIAK VLGSLAEEQL QVLKKIIQDE VSAENSKITE
LTEEKEEADE IKEDNGETDT TQKPNESSIN VLKTGQVVSG VLVSKDFNLN LLQLQDLHEF
TQLSTSIVKS KMHLKINADI SLMVWHLEQM FGYINVINDD DEEWECVIMD VVDVFIDRSK
GPGLFITVEW INDNLMADSL ADSVIAILYS IDSSPASVKL SSQNHNHGDN HIVKKEDSME
IDRPVEAHAK TDIKSRIERI ALLLKAQFGD SLKELPEEKA IIQIGKTVAN VDYKRLEVEC
SSKVLKDRVE NVIKRGCQLT APLSQNPKIA
//
