YSH1_YARLI
ID YSH1_YARLI Reviewed; 827 AA.
AC Q6C2Z7;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Endoribonuclease YSH1;
DE EC=3.1.27.-;
DE AltName: Full=mRNA 3'-end-processing protein YSH1;
GN Name=YSH1; OrderedLocusNames=YALI0F03817g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
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; CR382132; CAG77772.2; -; Genomic_DNA.
DR RefSeq; XP_504965.2; XM_504965.2.
DR AlphaFoldDB; Q6C2Z7; -.
DR SMR; Q6C2Z7; -.
DR STRING; 4952.CAG77772; -.
DR EnsemblFungi; CAG77772; CAG77772; YALI0_F03817g.
DR GeneID; 2907714; -.
DR KEGG; yli:YALI0F03817g; -.
DR VEuPathDB; FungiDB:YALI0_F03817g; -.
DR HOGENOM; CLU_009673_2_3_1; -.
DR InParanoid; Q6C2Z7; -.
DR OMA; VMIPRRC; -.
DR Proteomes; UP000001300; Chromosome F.
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 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..827
FT /note="Endoribonuclease YSH1"
FT /id="PRO_0000238908"
FT REGION 583..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 426
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 448
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 827 AA; 92195 MW; 11220FA0F53ACDAA CRC64;
MARWSGQIMC FRVGHFLLVG HFLLVGNFLL TDDSDTFSFV ALGGGREVGR SCHVISFKGK
TIMLDAGVHP AHSGLASLPF YDEFDLSTID ILLISHFHLD HAASLPYVMQ KTNFKGRVFM
THPTKGIYRW LLSDFVRVTS GAESDPDLYS EADLTASFNK IETIDYHSTM EVNGVKFTAY
HAGHVLGAAM YTIEVGGVKV LFTGDYSREE DRHLNQAEVP PMKPDILICE STYGTGTHLP
RLEREQRLTG LIHSTLDKGG KCLLPVFALG RAQEILLILD EYWEAHPDLQ EFSIYYASAL
AKKCIAVYQT YINMMNDNIR RRFRDQKTNP FRFKYIKNIK NLDRFDDMGP CVMVASPGML
QSGVSRSLLE RWAPDPKNTL ILTGYSVEGT MAKQIINEPN EIPSAQNPDL KVPRRLAVEE
LSFAAHVDFQ QNSEFIDLVD SKNIILVHGE LNNMQRLKAA LLAKYRGLKN SPREKTIYNP
RNCEEVELAF KGVKVAKTVG KMAEEKPHVG QIISGVVVQK DFNYGLMGVA DLREHVGLST
SSVLERQTVT VNAGVDLVKY HLEQMFGYVE MRETENVKIE EMEDDVAEEE EDKEVKQEVE
DVTMEGEVKD ETAEEVKKEE EVAEEFKQEV EGDSDTSAGT TFVVMNSVTV KHTPTSCTIE
WVGSCLNDSI ADAVLAILLT VDNSRASVKM SSKQCAHSHG HEDGHSNSSL DERVLQLSSI
LKAQFGDSYI VSEDGKSANI KIDAMEATIS FSDLSVTGSP PPLVQRVQVA VDRAISLVAP
LAQKLSAVDL VEGFKAIENV KDREENGEVK AEDEEKVKAE EKVKEEE
