YSH1_EMENI
ID YSH1_EMENI Reviewed; 884 AA.
AC Q5BEP0; C8VU78;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, 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; ORFNames=AN0990;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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; AACD01000015; EAA65558.1; -; Genomic_DNA.
DR EMBL; BN001308; CBF88384.1; -; Genomic_DNA.
DR RefSeq; XP_658594.1; XM_653502.1.
DR AlphaFoldDB; Q5BEP0; -.
DR SMR; Q5BEP0; -.
DR STRING; 162425.CADANIAP00001661; -.
DR EnsemblFungi; CBF88384; CBF88384; ANIA_00990.
DR EnsemblFungi; EAA65558; EAA65558; AN0990.2.
DR GeneID; 2876766; -.
DR KEGG; ani:AN0990.2; -.
DR VEuPathDB; FungiDB:AN0990; -.
DR eggNOG; KOG1137; Eukaryota.
DR HOGENOM; CLU_009673_2_1_1; -.
DR InParanoid; Q5BEP0; -.
DR OMA; VMIPRRC; -.
DR OrthoDB; 218195at2759; -.
DR Proteomes; UP000000560; Chromosome VIII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
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..884
FT /note="Endoribonuclease ysh1"
FT /id="PRO_0000238902"
FT REGION 595..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..626
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 446
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 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 468
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 884 AA; 97685 MW; 63316AA7E7FD3334 CRC64;
MAAKRKAAAM NAVDDEPVDP SDELAFYCLG GGNEVGRSCH IIQYKGKTVM LDAGMHPAKE
GFSALPFFDE FDLSTVDILL ISHFHVDHSS ALPYVLSKTN FKGRVFMTHA TKAIYKWLIQ
DNVRVNNTAS SSDQRTTLYT EHDHLSTLPL IETIDFNTTH TINSIRITPY PAGHVLGAAM
FLISIAGLNI LFTGDYSREE DRHLIPATVP RGVKIDVLIT ESTFGISSNP PRLEREAALM
KSITGVLNRG GRVLMPVFAL GRAQELLLIL EEYWETHPEL QKIPIYYIGN TARRCMVVYQ
TYIGAMNDNI KRLFRQRMAE AEASGDKSVS AGPWDFKYVR SLRSLERFDD VGGCVMLASP
GMLQTGTSRE LLERWAPNER NGVVMTGYSV EGTMAKQLLN EPDQIHAVMS RAATGMGRTR
MNGNDEEQKI MIPRRCTVDE ISFAAHVDGV ENRNFIEEVS APVVILVHGE KHQMMRLKSK
LLSLNAEKTV KVKVYTPANC EEVRIPFRKD KIAKVVGKLA QTTLPTDNED GDGPLMAGVL
VQNGFDLSLM APDDLREYAG LATTTITCKQ HITLSSASMD LIKWALEGTF GAIEEIGTDE
DAEKEDQQSE SEEKQRMKEE ADEEIPMEKP QAYLVMGCVV IRYHPRTREV ELQWEGNMMN
DGIADAVMAV LLTVESSPAS VKQSAKHNKH HHHHHHDETD TLKFLNPHAA QDAEERFARL
LMMLEAQFGS DIAPIERPRV PSSTESATTT TNGNGNSKSD SEQLSSLESK TDGATPQDPD
TLSELEAAEL SRLHALGIPV PGIEIKVDKH VARVWLEDLE VECANAVLRD RVRVVIERAV
ETVASMWSVG RSSKTITNGG GKEIAGTGAD DVASKPGLEV AARA
