ID   A0A9W8F1Q5_9FUNG        Unreviewed;       809 AA.
AC   A0A9W8F1Q5;
DT   08-NOV-2023, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2023, sequence version 1.
DT   05-FEB-2025, entry version 7.
DE   SubName: Full=Endoribonuclease ysh1 {ECO:0000313|EMBL:KAJ2487392.1};
GN   Name=YSH1 {ECO:0000313|EMBL:KAJ2487392.1};
GN   ORFNames=IWW37_005252 {ECO:0000313|EMBL:KAJ2487392.1};
OS   Coemansia sp. RSA 2050.
OC   Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC   Kickxellomycetes; Kickxellales; Kickxellaceae; Coemansia.
OX   NCBI_TaxID=2789361 {ECO:0000313|EMBL:KAJ2487392.1, ECO:0000313|Proteomes:UP001151568};
RN   [1] {ECO:0000313|EMBL:KAJ2487392.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=RSA 2050 {ECO:0000313|EMBL:KAJ2487392.1};
RA   Reynolds N.K., Stajich J.E., Barry K., Grigoriev I.V., Crous P.,
RA   Smith M.E.;
RT   "Phylogenomic reconstructions and comparative analyses of Kickxellomycotina
RT   fungi.";
RL   Submitted (JUL-2022) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA-
CC       metabolizing metallo-beta-lactamase-like family. CPSF2/YSH1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00010624}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KAJ2487392.1}.
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DR   EMBL; JANBSU010000150; KAJ2487392.1; -; Genomic_DNA.
DR   OrthoDB; 10249535at2759; -.
DR   Proteomes; UP001151568; Unassembled WGS sequence.
DR   GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IEA:TreeGrafter.
DR   GO; GO:0004534; F:5'-3' RNA exonuclease activity; IEA:TreeGrafter.
DR   GO; GO:0003723; F:RNA binding; IEA:TreeGrafter.
DR   GO; GO:0004521; F:RNA endonuclease activity; IEA:TreeGrafter.
DR   GO; GO:0006398; P:mRNA 3'-end processing by stem-loop binding and cleavage; IEA:TreeGrafter.
DR   CDD; cd16292; CPSF3-like_MBL-fold; 1.
DR   Gene3D; 3.40.50.10890; -; 1.
DR   Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 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   InterPro; IPR050698; RNA_Proc_MBL-domain.
DR   PANTHER; PTHR11203; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR FAMILY MEMBER; 1.
DR   PANTHER; PTHR11203:SF11; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR SUBUNIT 3; 1.
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; Metallo-hydrolase/oxidoreductase; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP001151568}.
FT   DOMAIN          32..243
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|SMART:SM00849"
FT   DOMAIN          256..380
FT                   /note="Beta-Casp"
FT                   /evidence="ECO:0000259|SMART:SM01027"
FT   DOMAIN          489..731
FT                   /note="Pre-mRNA 3'-end-processing endonuclease
FT                   polyadenylation factor C-term"
FT                   /evidence="ECO:0000259|SMART:SM01098"
FT   REGION          615..642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          760..809
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        620..629
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        764..775
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        777..800
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   809 AA;  89329 MW;  44FF49095F8813CB CRC64;
     MATKRKAEVS VPIEDENDQL TITPLGAGRE VGRSCIVVEY KGKKVMLDCG LHAGRNGPNS
     LPYFDEVDPA TIDVLLVTHF HIDHAAAVPY YLEHTSFKGR TFMTRPTKGV FRWLATDYIR
     VTNTSNSDTS ALYSEADLIS AHAKIEEIDV HQQVEVNGIK FTAYNAGHVL GAAMFLIEIA
     GVKVLYTGDY SREEDRHLVQ AENPGVSIHV LITESTYGVQ SHHPRAERER EFMTCVRDVV
     RRRGCCLMPV TALGRTQELL LILEEHWGRY AQELEGVPVF FISALGKTGT RLYQAYIMHM
     NQRIQRQFNR TGRNPFDFKY IKTRTNIAEV PDSGPCVVLA SPGMLQNGVS RQLLERWAPR
     PENGLIVTGY SVEGTLARTI VNAPDVIPAF AGGTIPRRMT VKNISFSAHV DYAQNSAFID
     EIRAPHVILV HGEENAMKQL RAKITDTYRG SDYEVAVHTP ANTHKVRLHF HGEKVARVMG
     SLASKVPREG DYASGILVER DFTYTLVDVA DLHEFTSIAP VVIEQQLCVP YASSYTLLRY
     HLEQMFGELV LTTERSGSGV AHILRIYDVV DVCHSSWKSH VEIEWEGNAM NDMVADSVVA
     IVLNIESSPA SVKLTQSSCS HDHGTKPDIS EADDASVDAS EAASQDLDSC GEALQARAGD
     CEKVIAKLAL FMQQQFTEVA VAGDGLSLIV TLNGQVAAID AHTLDIATES HMLRARIAPI
     IARVRRTMRP LGHHSLPLPE PVPASPLLEK LEELQLEAAV KPTNVDDDKD MHIDVASDIE
     DDEDDEDDDD EVYEDGDGGD SDTKSDPGS
//