YSH1_ASHGO
ID YSH1_ASHGO Reviewed; 771 AA.
AC Q74ZC0;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Endoribonuclease YSH1;
DE EC=3.1.27.-;
DE AltName: Full=mRNA 3'-end-processing protein YSH1;
GN Name=YSH1; OrderedLocusNames=AGR279C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 82.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(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}.
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DR EMBL; AE016820; AAS54769.2; -; Genomic_DNA.
DR RefSeq; NP_986945.2; NM_212007.2.
DR AlphaFoldDB; Q74ZC0; -.
DR SMR; Q74ZC0; -.
DR STRING; 33169.AAS54769; -.
DR EnsemblFungi; AAS54769; AAS54769; AGOS_AGR279C.
DR GeneID; 4623247; -.
DR KEGG; ago:AGOS_AGR279C; -.
DR eggNOG; KOG1137; Eukaryota.
DR HOGENOM; CLU_009673_2_3_1; -.
DR InParanoid; Q74ZC0; -.
DR OMA; VMIPRRC; -.
DR Proteomes; UP000000591; Chromosome VII.
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: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..771
FT /note="Endoribonuclease YSH1"
FT /id="PRO_0000238896"
FT REGION 493..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 409
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
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 75
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="1"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 431
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 771 AA; 86338 MW; 17362B59B3B76A6A CRC64;
MTEEKLDTNS FRFFGLGGSN EVGRSCHILQ YKGKTVMLDA GVHPAHQGIA SLPFYDEFDL
SQVEVLLISH FHLDHAASLP YVMQRTNFQG RVFMTHPTKA IYRWLLSDFV KVTNIGNDNA
GGVSDENLYT DEDLAESFDR IETVDYHSTI DVNGIKFTAY HAGHVLGAAM FQVEIAGLRI
LFTGDYSREL DRHLNSAEIP TLPSDILIVE STFGTATHEP RTSKEKKLTQ LIHTTVSKGG
RVLLPVFALG RAQEIMLILD EYWSQHAEQL GNGQVPIFYA SNLARKCMSV FQTYVNMMND
KIRKKFRDSQ TNPFIFKNIS YLKNLDEFQD FGPSVMLASP GMLQNGLSRD LLEKWCPDEK
NLVLITGYSV EGTMAKFLML EPETIPSINN SDVSIPRRCQ VEEISFAAHV DFRENLEFVE
KIGAPNIILV HGESNPMGRL KSALLSNFSS LKGTEDEVRV YNPRNCVAVD LEFKGVKIAK
AVGNIVDEML PVVDEDKERP YNDPEDATSE EQPKEEPQDA DKLPEEREQP EVEEERVISG
ILVSDEKNFD LNLVSLSDLR EHHTDLSTTV LKERQTVHVD CRNELIFWHL CQMFGDIEVL
VDEEGATLTK VEEDEKNTKP GQLVVRVMGD IKLSVVDHVA TLEWTQNVIS DAVADSIVAI
LLSVDSSPAS VKRSSHSCNS NDHPGESETL WKIKQIAKLF NEQFGDSFTL LLDKESEHSD
NENIKGSVTI GKNYATVNFS KMAVEDCNSN PLKGRIESIL GIGADLVAPL C
