ID A0A178AKZ0_9PLEO Unreviewed; 509 AA.
AC A0A178AKZ0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Amidase {ECO:0000313|EMBL:OAK98153.1};
GN ORFNames=IQ06DRAFT_318204 {ECO:0000313|EMBL:OAK98153.1};
OS Stagonospora sp. SRC1lsM3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX NCBI_TaxID=765868 {ECO:0000313|EMBL:OAK98153.1, ECO:0000313|Proteomes:UP000077206};
RN [1] {ECO:0000313|EMBL:OAK98153.1, ECO:0000313|Proteomes:UP000077206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAK98153.1,
RC ECO:0000313|Proteomes:UP000077206};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247}.
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DR EMBL; KV441716; OAK98153.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178AKZ0; -.
DR STRING; 765868.A0A178AKZ0; -.
DR InParanoid; A0A178AKZ0; -.
DR OrthoDB; 5491171at2759; -.
DR Proteomes; UP000077206; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd03884; M20_bAS; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR010158; Amidase_Cbmase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR NCBIfam; TIGR01879; hydantase; 1.
DR PANTHER; PTHR32494:SF5; ALLANTOATE AMIDOHYDROLASE; 1.
DR PANTHER; PTHR32494; ALLANTOATE DEIMINASE-RELATED; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000077206}.
FT DOMAIN 281..375
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 509 AA; 55775 MW; 22728BD494387B84 CRC64;
MALPASRCAS ALRVAGSRYP AWRPTAPCRS ALRYSQARSF ASSPRWLIRT KEMNDDMLKD
LKVNQARLME DIHHTCQWGM GERWGDAPTE TGMSRLALSD ADKAARDWFV STTEALGCKV
TVDAMGNTFA VRPGLRNDKP PTFVGSHLDT QPTGGRYDGI LGVTAGVEML RVLADNWTET
EYPVGVVNWT NEEGARFPKS MVSSGVWAGD IPVETAHNLR EVHPGTATMA EELKRIGYLG
ETPASHEAIP MAGHFELHIE QGPLLEMSNK KIGVVKGVQA YKWFTINVKG RDTHTGTTDL
KSRADALLTA SKMILHSHRL ATLNNALAST GILHLKPGST NTVPGSVTFS LDIRSPKDET
VAKMTELIKQ DFPKIAAGED VLDSNLGCTS GLPLSVEIVE DFSSPATNFH PDCITSVRQS
AHSVLGSNGH NLVMEMTSGA GHDSVYASKR CPTSMIFVPC REGVSHNPRE FCKEEDCALG
AQVLLQSVIR FDRMRDERRV SWKQEPYTI
//