ID A0A2P5EBJ1_TREOI Unreviewed; 436 AA.
AC A0A2P5EBJ1;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:PON82917.1};
GN ORFNames=TorRG33x02_213280 {ECO:0000313|EMBL:PON82917.1};
OS Trema orientale (Charcoal tree) (Celtis orientalis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Cannabaceae; Trema.
OX NCBI_TaxID=63057 {ECO:0000313|EMBL:PON82917.1, ECO:0000313|Proteomes:UP000237000};
RN [1] {ECO:0000313|Proteomes:UP000237000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. RG33-2 {ECO:0000313|Proteomes:UP000237000};
RA Van Velzen R., Holmer R., Bu F., Rutten L., Van Zeijl A., Liu W.,
RA Santuari L., Cao Q., Sharma T., Shen D., Roswanjaya Y., Wardhani T.,
RA Kalhor M.S., Jansen J., Van den Hoogen J., Gungor B., Hartog M.,
RA Hontelez J., Verver J., Yang W.-C., Schijlen E., Repin R., Schilthuizen M.,
RA Schranz E., Heidstra R., Miyata K., Fedorova E., Kohlen W., Bisseling T.,
RA Smit S., Geurts R.;
RT "Parallel loss of symbiosis genes in relatives of nitrogen-fixing non-
RT legume Parasponia.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M20 family.
CC {ECO:0000256|ARBA:ARBA00006153}.
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:PON82917.1}.
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DR EMBL; JXTC01000187; PON82917.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P5EBJ1; -.
DR STRING; 63057.A0A2P5EBJ1; -.
DR InParanoid; A0A2P5EBJ1; -.
DR OrthoDB; 3684955at2759; -.
DR Proteomes; UP000237000; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0009850; P:auxin metabolic process; IEA:InterPro.
DR CDD; cd08017; M20_IAA_Hyd; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR017439; Amidohydrolase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR044757; ILR1-like_Hyd.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR NCBIfam; TIGR01891; amidohydrolases; 1.
DR PANTHER; PTHR11014:SF63; METALLOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G09600)-RELATED; 1.
DR PANTHER; PTHR11014; PEPTIDASE M20 FAMILY MEMBER; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:PON82917.1};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Reference proteome {ECO:0000313|Proteomes:UP000237000};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..436
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015176332"
FT DOMAIN 217..316
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 436 AA; 48054 MW; D03A0684C956E7C2 CRC64;
MEWVLLCLFT LSTLTCGCGV WSLETPTGSE LSQLTRELFD SARKPEFSDW LKKIRRRIHE
NPELSFEEFE TSQLIRSELD SLGIQYTWPV AKTGVVASIG AGAQPWFGLR ADMDALPIQE
LVEWEHKSKK HGKMHACGHD AHVTMLLGAA KLLHQRSNQL KGTVKLVFQP AEEGPAGAYH
VLQEGALDKV QAIFGLHVDP KLPTGTIGSR PGPFFSGSSR FTVVIEGKGG HAAIPQVTRD
PILAASSAIL ALQHIISRET DPLEARVVSV GFIEGGQAGN VIPETVRFGG TFRSFTSEGL
SYLQQRIKEI VETQAEVHRC TAKVDFMLDK RRPYPATVND KTMYEHAKRV GEVLLGEPKV
QLLPMYMAAE DFSFYAQKMS AAFFVIGVRN ESFGSDIKDL HSPYFVIDEE ALPVGAALHA
AVAISFLENQ SHSVQI
//
