YSH1_NEUCR
ID YSH1_NEUCR Reviewed; 850 AA.
AC Q8WZS6;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Endoribonuclease ysh-1;
DE EC=3.1.27.-;
DE AltName: Full=mRNA 3'-end-processing protein ysh-1;
GN Name=ysh-1; ORFNames=B8L21.110, NCU03479;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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; AL669989; CAD21097.1; -; Genomic_DNA.
DR EMBL; CM002237; EAA27132.1; -; Genomic_DNA.
DR RefSeq; XP_956368.1; XM_951275.2.
DR AlphaFoldDB; Q8WZS6; -.
DR SMR; Q8WZS6; -.
DR STRING; 5141.EFNCRP00000002675; -.
DR EnsemblFungi; EAA27132; EAA27132; NCU03479.
DR GeneID; 3872515; -.
DR KEGG; ncr:NCU03479; -.
DR VEuPathDB; FungiDB:NCU03479; -.
DR HOGENOM; CLU_009673_2_1_1; -.
DR InParanoid; Q8WZS6; -.
DR OMA; VMIPRRC; -.
DR Proteomes; UP000001805; Chromosome 6, Linkage Group II.
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..850
FT /note="Endoribonuclease ysh-1"
FT /id="PRO_0000238905"
FT REGION 685..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 442
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 464
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 850 AA; 94079 MW; 16448AE82BD7D46D CRC64;
MASKRKASAM ATEPEEPVDP ADELMFLNLG GGNEVGRSCH IIQYKGKTVM LDAGQHPAYD
GLAALPFFDD FDLSTVDVLL ISHFHIDHAA SLPYVLAKTN FRGRVFMTHA TKAIYKWLIQ
DSVRVGNTSS NPQSSLVYTE EDHLKTFPMI EAIDYNTTHT ISSIRITPYP AGHVLGAAMF
LIEIAGLKIF FTGDYSREED RHLISAKVPK GVKIDVLITE STYGIASHIP RPEREQALMK
SITGILNRGG RVLMPVFALG RAQELLLILD EYWGKHAEYQ KYPIYYASNL ARKCMLVYQT
YVGSMNDNIK RLFRERLAES ESSGDGAGKG GPWDFRFIRS LKSLDRFEDV GGCVMLASPG
MLQNGVSREL LERWAPSEKN GVIITGYSVE GTMAKQLLQE PEQIQAVMSR NIAGARRGPG
GDAEKVMIPR RCTVQEFSFA AHVDGVENRE FIEEVAAPVV ILVHGEVHNM MRLKSKLLSL
NATKEHKVKV FSPRNCEELR IPFKTDKVAK VVGKLASIPP SLKEAKTGHD GPLPSSTEPQ
LITGVLVQND FKMSLMAPED LREYAGLTTT TIACKQRLKL SAAGIDLIKW GLEGTFGAVE
ELPEVKPKLE IVKSENGDTK MEEADEELPH GDDVVAAYLV MGCVTVRYRA SGEVELEWEG
NMLNDGIADA VMAVLLGIES SPAAVKRSAT KNPHTHSPLP ADKNPHSHLT PEDRFFRLCM
FLEAQFGQDN VSPIVEPKLP PLSPTTKAIT SPSEETAKSS DVKSDADADA SMDVSEEDED
EQQLKARERA EVERLERMGI PKPGVRIKVD KMEAKVWLED LEVECANKIF RERVRAVVER
AVEVVAPLWG
