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Database: UniProt
Entry: A0A178ASZ6_9PLEO
LinkDB: A0A178ASZ6_9PLEO
Original site: A0A178ASZ6_9PLEO 
ID   A0A178ASZ6_9PLEO        Unreviewed;       414 AA.
AC   A0A178ASZ6;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Zn-dependent exopeptidase {ECO:0000313|EMBL:OAL00269.1};
GN   ORFNames=IQ06DRAFT_377122 {ECO:0000313|EMBL:OAL00269.1};
OS   Stagonospora sp. SRC1lsM3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX   NCBI_TaxID=765868 {ECO:0000313|EMBL:OAL00269.1, ECO:0000313|Proteomes:UP000077206};
RN   [1] {ECO:0000313|EMBL:OAL00269.1, ECO:0000313|Proteomes:UP000077206}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAL00269.1,
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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; KV441712; OAL00269.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178ASZ6; -.
DR   STRING; 765868.A0A178ASZ6; -.
DR   InParanoid; A0A178ASZ6; -.
DR   OrthoDB; 2875217at2759; -.
DR   Proteomes; UP000077206; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05652; M20_ArgE_DapE-like_fungal; 1.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR001261; ArgE/DapE_CS.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR   PANTHER; PTHR43808:SF8; M20_DIMER DOMAIN-CONTAINING PROTEIN; 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.
DR   PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077206};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..414
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008082161"
FT   DOMAIN          217..313
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
FT   REGION          23..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..44
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   414 AA;  44252 MW;  8534FD6A0F9C5E14 CRC64;
     MVSRFASLGL LLLSSVRAAP QAAPSPASLS TSTPTSSPSA VPSLTTEERD ELFELHEELV
     NIPSISGEEQ ECADYIAEYL EELGYYVEKV PVEETGSYNV FAYSTALREE GGWPEVLITS
     HIDTVPPFYP FERREENGTV FHYGRGTVDA KGPIATMIIA SHKFLESRTD TPSLGMLFVV
     SEEVGGTGMK AFASYASNTT FRAGIFGEPT EGKLASGHKG SQRLDIDIKG KSSHSAYPWL
     GVSAINYLAE AIVAMNALEP ALPSSELLGA TTLNAGVITG GVAGNVVPEA ANASVVIRIA
     RSEDDAVENV RNMVNGMLSP IKMKAEEANA TFELIWSNAS YPAPILDTDV DGLEVAPVFY
     GTDIPSLPQV EKKYLFGTGT IEVAHTPDEG LSQDELVEAA EAYGLILQSL FPSE
//
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