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Database: UniProt
Entry: A0A178AKZ0_9PLEO
LinkDB: A0A178AKZ0_9PLEO
Original site: A0A178AKZ0_9PLEO 
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
//
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