YSH1_ASPFU
ID YSH1_ASPFU Reviewed; 872 AA.
AC Q4WRC2;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Endoribonuclease ysh1;
DE EC=3.1.27.-;
DE AltName: Full=mRNA 3'-end-processing protein ysh1;
GN Name=ysh1; ORFNames=AFUA_1G16800;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(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; AAHF01000004; EAL91010.1; -; Genomic_DNA.
DR RefSeq; XP_753048.1; XM_747955.1.
DR AlphaFoldDB; Q4WRC2; -.
DR SMR; Q4WRC2; -.
DR STRING; 746128.CADAFUBP00001587; -.
DR EnsemblFungi; EAL91010; EAL91010; AFUA_1G16800.
DR GeneID; 3510074; -.
DR KEGG; afm:AFUA_1G16800; -.
DR VEuPathDB; FungiDB:Afu1g16800; -.
DR eggNOG; KOG1137; Eukaryota.
DR HOGENOM; CLU_009673_2_1_1; -.
DR InParanoid; Q4WRC2; -.
DR OMA; VMIPRRC; -.
DR OrthoDB; 218195at2759; -.
DR Proteomes; UP000002530; Chromosome 1.
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:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
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..872
FT /note="Endoribonuclease ysh1"
FT /id="PRO_0000238897"
FT REGION 682..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 447
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
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 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 469
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 872 AA; 96331 MW; 96B24FD4EB37B370 CRC64;
MATKRKASAL NAAVDDEPVD PSDELAFYCL GGGNEVGRSC HIIQYKGKTV MLDAGMHPAK
EGFSALPFFD EFDLSTVDIL LISHFHVDHS SALPYVLSKT NFKGRVFMTH ATKAIYKWLI
QDNVRVSNTA SSSDQRTTLY TEHDHLSTLP LIETIDFNTT HTVNSIRITP FPAGHVLGAA
MFLISIAGLN ILFTGDYSRE EDRHLIPAEV PKGIKIDVLI TESTFGISTN PPRLEREAAL
MKSITGILNR GGRVLMPVFA LGRAQELLLI LDEYWETHPE LQKIPIYYIG NTARRCMVVY
QTYIGAMNDN IKRLFRQRMA EAEASGDKSA SAGPWDFKFV RSLRSLERFD DVGGCVMLAS
PGMLQTGTSR ELLERWAPNE RNGVVMTGYS VEGTMAKQLL NEPEQIPAVM SRSAGGVSRR
GLAGTDEEQK IMIPRRCTVD EISFAAHVDG VENRNFIEEV AAPVVILVHG EKHQMMRLKS
KLLSLNADKA VKVKVYTPAN CDEVRIPFRK DKIAKVVGKL AQVAPPSDQD DGRLMSGVLV
QNGFDLSLMA PDDLREYAGL TTTTITCKQH ITLSSASMDL IRWALEGTFG AIEELGSNER
SKVKEESTKA VNGEQEIKEE PADEEIPMEE TQTYLVMGCV LIRYHSRTRE VELEWEGNMM
NDGVADAVMA VLLTVESSPA SVKQSAKLKH HHHHHSDLEL PNPHAHQGPE ETFENLLMML
EAQFGSNIAP IERPRIPSGI RANRTTKADP SVSAAVKTKS DAAGETPAES QEDESTEEIE
AAELARLQAL GIPYPGIEIK VDKHVARVWL ENFEVECANT VLRDRVRVVI ERAVETVSSM
WGEGHPAARA SNGTQGNKEV AVSKSNEIEA RA
