ID   A0A167JA23_CALVF        Unreviewed;       776 AA.
AC   A0A167JA23;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Metallo-hydrolase/oxidoreductase {ECO:0000313|EMBL:KZO93385.1};
GN   ORFNames=CALVIDRAFT_600826 {ECO:0000313|EMBL:KZO93385.1};
OS   Calocera viscosa (strain TUFC12733).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC   Dacrymycetales; Dacrymycetaceae; Calocera.
OX   NCBI_TaxID=1330018 {ECO:0000313|EMBL:KZO93385.1, ECO:0000313|Proteomes:UP000076738};
RN   [1] {ECO:0000313|EMBL:KZO93385.1, ECO:0000313|Proteomes:UP000076738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TUFC12733 {ECO:0000313|EMBL:KZO93385.1,
RC   ECO:0000313|Proteomes:UP000076738};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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}.
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DR   EMBL; KV417302; KZO93385.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A167JA23; -.
DR   STRING; 1330018.A0A167JA23; -.
DR   OrthoDB; 169081at2759; -.
DR   Proteomes; UP000076738; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
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   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; PF16661; Lactamase_B_6; 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:0000313|EMBL:KZO93385.1};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076738}.
FT   DOMAIN          22..240
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|SMART:SM00849"
FT   DOMAIN          251..377
FT                   /note="Beta-Casp"
FT                   /evidence="ECO:0000259|SMART:SM01027"
FT   DOMAIN          486..733
FT                   /note="Pre-mRNA 3'-end-processing endonuclease
FT                   polyadenylation factor C-term"
FT                   /evidence="ECO:0000259|SMART:SM01098"
FT   REGION          755..776
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   776 AA;  85939 MW;  6F1345825A318741 CRC64;
     MATSLTEPKL SITLLGAGQE VGRSCCVIQH AGITVVCDAG VHPAFHGMAA LPFIDDLDWS
     TVDALLITHF HLDHAASLTY IMEKTNFKDG KGKVYMTHPT KAVYRLMMQD YVRMSAAQST
     SAPPLFTPLD LSITLPLINA VSYATTTTVI PGLSFTPYPA GHVLGASMFL IQLADLRILY
     TGDYSREESR HLVRAEVPPG AGVDVLIVES TFGVQSTEGR REKEERFTSL IHRILLRGGH
     VLMPVFAVGG AQELLLILDD YFEKHPELHK FPIFYASALA RKCMAVYQGY VHVMNNNIRS
     RFANNQNPFV FRHVSHIPRS SGWEKKIGEG PPCVILASPG MMQSGASREL LEMWAPDRRN
     GVVITGYSVE GSMARNIMNE PDEITSMKGT SIPLRCTVDN ISFSAHVDYA QNREFIEAIG
     APHVVLVHGE QSQMFRLKAA LQAGYKERNE HITIHTPKNC EPLELIFRGE RVAKAIGTLA
     ERPPQTGAQL SGLLVSKDFT YTLLDPRDLR DFTGLSTSTI IQKQRMCIPG ITWELVKWHL
     EGLFGSVTQG ADAEGIRTMR VMGVLDVKGM REGLKEETDP FEAESGFPGG YLLLEWVSSG
     SNDMIADAAM ALIHGIDTSP ASVKLTSRPH THADHNHEEE DAKATTARRL TQLIEFLELY
     FGEVQFLDAQ GKELDDEDDE EGLELTEPAL RIRLDDQYAD INLITMTVKS VSQTFRRRVE
     DVLAMAITTF GSLTESYVSA DRSGWDGEQE FFIEGDRVEN GKDKSDEQTL GDGDTN
//