ID M5FPU8_DACPD Unreviewed; 780 AA.
AC M5FPU8;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Metallo-hydrolase/oxidoreductase {ECO:0000313|EMBL:EJT97328.1};
GN ORFNames=DACRYDRAFT_84872 {ECO:0000313|EMBL:EJT97328.1};
OS Dacryopinax primogenitus (strain DJM 731) (Brown rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Dacryopinax.
OX NCBI_TaxID=1858805 {ECO:0000313|EMBL:EJT97328.1, ECO:0000313|Proteomes:UP000030653};
RN [1] {ECO:0000313|EMBL:EJT97328.1, ECO:0000313|Proteomes:UP000030653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJM-731 SS1 {ECO:0000313|EMBL:EJT97328.1,
RC ECO:0000313|Proteomes:UP000030653};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
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; JH795877; EJT97328.1; -; Genomic_DNA.
DR AlphaFoldDB; M5FPU8; -.
DR STRING; 1858805.M5FPU8; -.
DR HOGENOM; CLU_009673_2_0_1; -.
DR OMA; CKQHITL; -.
DR OrthoDB; 169081at2759; -.
DR Proteomes; UP000030653; 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:EJT97328.1};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000030653}.
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 757..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 780 AA; 86606 MW; FCAAA31E7FD742D5 CRC64;
MATSLTEPKL SITLLGAGQE VGRSCCVIQH AGITVVCDAG VHPAFHGMAA LPFIDDLDWS
TVDALLITHF HLDHAASLTY IMEKTNFKDG KGKVYMTHPT KAVYRLMMQD YVRMSAAQST
SAPPLFTPLD LSITLPLINA VSFATTTTVI PGLSFTPYPA GHVLGASMFL IQLADLRILY
TGDYSREESR HLVRAEVPPG AGIDVLIIES TFGVQSTEGR REKEERFTSL IHRILMRGGH
VLMPVFAVGG AQELLLILDD FFEKHPELHK FPIYYASALA RKCMAVYQGY VHVMNNNIRQ
RFANNQNPFV FRHVSHIPRS SGWEKKIGEG PPCVILASPG MMQSGASREL LEMWAPDRRN
GIVLTGYSVE GSMARNIMNE PDEINAMKGT PIPLRCTVDN ISFSAHVDYA QNREFIEAIG
APHVVLVHGE QSQMFRLKAA LQAGYKERNE HITIHTPKNC ETLELIFRGE RVAKAIGTLA
EHAPQAGAQL SGLLVSKDFT YTLLDPRDLR DFTGLSTSTI VQKQRLCIPG LTWELVKWHL
EGLFGSVTEG VDAEGTRTMR AMGLLDVKGM RDAVKEEPTI SQEENGFPGG YIVLEWVSSG
SNDMIADAAM ALIHGIDASP ASVKLTSRRH IHADHVHEKE VPKAAANRRL TQLIEFLELY
FGQVQFLDAQ GKEMDEDEDE EGLELTEPAL RIRLDEQYAD INLITMTVKS ASQTFRRRIE
DVLAMALTTY GSLTESYISA DRSGWDGEQD FFIDGEAREN EVSKEMEQVS KEGVEARMKE
//
