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Database: UniProt
Entry: A0A137PB83_CONC2
LinkDB: A0A137PB83_CONC2
Original site: A0A137PB83_CONC2 
ID   A0A137PB83_CONC2        Unreviewed;       473 AA.
AC   A0A137PB83;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=CNDP dipeptidase {ECO:0000313|EMBL:KXN72265.1};
GN   ORFNames=CONCODRAFT_16272 {ECO:0000313|EMBL:KXN72265.1};
OS   Conidiobolus coronatus (strain ATCC 28846 / CBS 209.66 / NRRL 28638)
OS   (Delacroixia coronata).
OC   Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota;
OC   Entomophthoromycotina; Entomophthoromycetes; Entomophthorales;
OC   Ancylistaceae; Conidiobolus.
OX   NCBI_TaxID=796925 {ECO:0000313|EMBL:KXN72265.1, ECO:0000313|Proteomes:UP000070444};
RN   [1] {ECO:0000313|EMBL:KXN72265.1, ECO:0000313|Proteomes:UP000070444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 28638 {ECO:0000313|EMBL:KXN72265.1,
RC   ECO:0000313|Proteomes:UP000070444};
RX   PubMed=25977457; DOI=10.1093/gbe/evv090;
RA   Chang Y., Wang S., Sekimoto S., Aerts A.L., Choi C., Clum A., LaButti K.M.,
RA   Lindquist E.A., Yee Ngan C., Ohm R.A., Salamov A.A., Grigoriev I.V.,
RA   Spatafora J.W., Berbee M.L.;
RT   "Phylogenomic Analyses Indicate that Early Fungi Evolved Digesting Cell
RT   Walls of Algal Ancestors of Land Plants.";
RL   Genome Biol. Evol. 7:1590-1601(2015).
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRSR:PIRSR037242-3};
CC       Note=Binds 2 manganese ions per subunit.
CC       {ECO:0000256|PIRSR:PIRSR037242-3};
CC   -!- SIMILARITY: Belongs to the peptidase M20A family.
CC       {ECO:0000256|ARBA:ARBA00006247}.
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DR   EMBL; KQ964456; KXN72265.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A137PB83; -.
DR   STRING; 796925.A0A137PB83; -.
DR   EnsemblFungi; KXN72265; KXN72265; CONCODRAFT_16272.
DR   OMA; HITIPGF; -.
DR   OrthoDB; 177966at2759; -.
DR   Proteomes; UP000070444; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070573; F:metallodipeptidase activity; IEA:EnsemblFungi.
DR   GO; GO:0008242; F:omega peptidase activity; IEA:EnsemblFungi.
DR   GO; GO:0006751; P:glutathione catabolic process; IEA:EnsemblFungi.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05676; M20_dipept_like_CNDP; 1.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR017153; CNDP/DUG1.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   PANTHER; PTHR43270; BETA-ALA-HIS DIPEPTIDASE; 1.
DR   PANTHER; PTHR43270:SF4; CARNOSINE DIPEPTIDASE 2, ISOFORM A; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF037242; CNDP_dipeptidase; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Manganese {ECO:0000256|PIRSR:PIRSR037242-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR037242-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070444}.
FT   DOMAIN          205..363
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
FT   ACT_SITE        97
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037242-1"
FT   ACT_SITE        163
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037242-1"
FT   BINDING         95
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT   BINDING         129
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT   BINDING         129
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT   BINDING         164
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT   BINDING         192
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT   BINDING         192
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037242-2"
FT   BINDING         225
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037242-2"
FT   BINDING         327
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037242-2"
FT   BINDING         340
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037242-2"
FT   BINDING         414
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037242-2"
FT   BINDING         442
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT   BINDING         442
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037242-2"
FT   SITE            225
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037242-4"
SQ   SEQUENCE   473 AA;  52719 MW;  77D67825D1FA1F81 CRC64;
     MEAVYQYIDE NQQNFIQKLR EAVAIPSVSS SVPHRPEVIR MGEWLIKELE ALGATTKRIE
     LGDHELEGQT IPLPPVVLAR YGEDPKKKTL LVYGHYDVQP ALKEDGWNTD PFELVHDDKD
     RLVGRGATDD KGPVLGWLLA LEAFQKTNTD FPVNLLCCFE GMEESGSEGL DDVVIQQANE
     WFKDTDCVCI SDNYWLGTTK PCLTYGLRGV SYFSLVVKGP AVDLHSGLFG GTVHEPMTDL
     VHLMGKLVNP QGEILVPGIM DQVAPLTEEE SQTYDALDFD MNVLHDSLGN TNSIHDSAKK
     TLMHRWRYPS LSLHGIEGAF YSPGAKTVIP AKVTGKFSIR TVPDMEPEKV TELVVKYVKD
     EFAKLGSKNE IDVFCQHAGK SWVSSFNHWN FQAAIKAVKQ VFQVEPDLTR EGGSIPVTLT
     FEQALGKNVL LLPMGSNDDG AHSTNEKIDR RNFIEGIKLL STYMYELSQT TEA
//
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