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
//