ID A0A178EI82_9PLEO Unreviewed; 719 AA.
AC A0A178EI82;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Zn-dependent exopeptidase {ECO:0000313|EMBL:OAL55737.1};
GN ORFNames=IQ07DRAFT_583180 {ECO:0000313|EMBL:OAL55737.1};
OS Pyrenochaeta sp. DS3sAY3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC Pyrenochaeta.
OX NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL55737.1, ECO:0000313|Proteomes:UP000077535};
RN [1] {ECO:0000313|EMBL:OAL55737.1, ECO:0000313|Proteomes:UP000077535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL55737.1,
RC ECO:0000313|Proteomes:UP000077535};
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 -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC {ECO:0000256|ARBA:ARBA00005634}.
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DR EMBL; KV441637; OAL55737.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178EI82; -.
DR STRING; 765867.A0A178EI82; -.
DR InParanoid; A0A178EI82; -.
DR OrthoDB; 67337at2759; -.
DR Proteomes; UP000077535; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd08022; M28_PSMA_like; 1.
DR CDD; cd02121; PA_GCPII_like; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 1.20.930.40; Transferrin receptor-like, dimerisation domain; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR007484; Peptidase_M28.
DR InterPro; IPR039373; Peptidase_M28B.
DR InterPro; IPR007365; TFR-like_dimer_dom.
DR InterPro; IPR036757; TFR-like_dimer_dom_sf.
DR PANTHER; PTHR10404:SF46; GLUTAMATE CARBOXYPEPTIDASE 2 HOMOLOG; 1.
DR PANTHER; PTHR10404; N-ACETYLATED-ALPHA-LINKED ACIDIC DIPEPTIDASE; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR Pfam; PF04253; TFR_dimer; 1.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF47672; Transferrin receptor-like dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000077535};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..719
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008085430"
FT DOMAIN 161..234
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 346..536
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT DOMAIN 607..717
FT /note="Transferrin receptor-like dimerisation"
FT /evidence="ECO:0000259|Pfam:PF04253"
FT REGION 216..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 719 AA; 78863 MW; 5031177F04832A21 CRC64;
MATVWLLLLA LTQSSIACQR DLHLRDDIEH KQDLPLIPRQ LQPFPPQWSP NEKTLHTSIS
TASIEAWSSY YTHGDHIAGR NKSMAEETAK QWTANGVPSS LVEYEVFLNY PKEQALILKR
GNASIHQAQM YEDVLEEDET TGYPGAPPGF HGFSASGKVE AEYVYVGRGH KDDFAALKAA
NVNLTGKIAL AKYGGPFRGV KVQNAEANGM IGVVIFTDPG DDGPQEAKGD APYPKGPARQ
PSSIQRGSVA YINKYPGDPT TPGQPSKPGV KRVTPSNLPK IPSIPISYRD AIPILKALDG
QGIPGKSINR GGWLGGLNAT YSTGPAPGVT LSLTNIMEET ITPIWNVIGI INGTNANETV
IIGNHRDAWI IGGAADPNSG SAILVELTKA FGTLLKTGWK PRRNIIFASW DAEEYALVGS
TEWVEDHAPW LSATAISYLN IDIGVSGPLP GSSSTPELRA LALATMQKTV YGARTLLDAW
NALNQFRPED NGFGNLGSGS DYTAFMQLGI SSLDFGFDAD RSTPVYHYHS SYDSFAWMKS
RIDTDFAIHA TAARFLALLT YRLADDALLP LDMADWARNV NYYVRDLVVA TMNLGGDYSE
VQQQINITAL DEAAKRVRRV ADEWVERTGA EAFRRDEARV RRANGRMVEV LRLFVREGGL
PGRPFYTNAL VAPNRDDGYK AHTLPASMET LEDKKFDECR QWNLWIAERL NRAAELLVV
//