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
//