ID A0A0F4G580_9PEZI Unreviewed; 900 AA.
AC A0A0F4G580;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
GN ORFNames=TI39_contig5889g00004 {ECO:0000313|EMBL:KJX92217.1};
OS Zymoseptoria brevis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJX92217.1, ECO:0000313|Proteomes:UP000033647};
RN [1] {ECO:0000313|EMBL:KJX92217.1, ECO:0000313|Proteomes:UP000033647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zb18110 {ECO:0000313|EMBL:KJX92217.1,
RC ECO:0000313|Proteomes:UP000033647};
RA Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT "RNA-seq based gene annotation and comparative genomics of four
RT Zymoseptoria species reveal species-specific pathogenicity related genes
RT and transposable element activity.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJX92217.1}.
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DR EMBL; LAFY01005844; KJX92217.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4G580; -.
DR STRING; 1047168.A0A0F4G580; -.
DR OrthoDB; 3073733at2759; -.
DR Proteomes; UP000033647; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 2.40.70.10; Acid Proteases; 3.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11552:SF134; GMC_OXRDTASE_N DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00026; Asp; 2.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00623; GMC_OXRED_1; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|RuleBase:RU003968};
KW Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW Reference proteome {ECO:0000313|Proteomes:UP000033647}.
FT DOMAIN 583..887
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 601
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 778
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 900 AA; 96408 MW; 1CC436D39D5FD1EB CRC64;
MALTQSHYDF IIVGGGTAGC LLAHRLSHSA AARSVLLLEA GTKPSGPYLS APGHRYTAAF
ARSDLDHGYV SEPEPSLNGR ELPYARGKGL GGSSILNFGV YLYGSGEDYD RWADLVDDDD
WAWSSAQESF RTIEHYATES AAAYKHLADP ASGRHGTSGQ VTVSLPPVLE KSVAPQMASL
LAAGESLCLD PNAGDNIGVS LFPYSYGKSG RCTSAIAHLV DPPKNLEVWT DATVGKLFFD
GTSVIGVRTI DGREALSNKE VILCCGAIDT PRLLLLNGIG PKAELEALDV EVIKDLPGVG
KHLRDHVAGI MCVEVDGSFN DRTTFETDPK SVEEAQALWD QDHTGALSLQ HSSLWGGFLK
VPNLEKSSEF QNLAPADQEF LTRSKVPHFE FLNNALLWPP GSQLTPGNTY LSFTAALMNA
QSEGSVTLRS KNPTDKPLLR LNLLSHPYDV LVIREAIRRS WNMIIENPDM RPHVRKTLSG
PASLSDADID AYAKAEACPI WHANGTARMG KEADGGSVDS SGKVYGVQGL RVADLRVCPL
TTNNHTQATA YLVGQKIAEK MKDPTSGQTG DVPAEDIENN TEYLANVTIG TPGQTFALDF
DTGSADLWVW STELSVSTRN GNHGGNKHSI FDPKKSSTFK KSSGSLGKSN MEMAIELAKT
LSTQFASGPG DGLLGLAFGS INTVQPSPAQ TVVENMITQI DIPKNTELFT AYLGSTHPGS
SSDSSNGSAT TDATSFYPFG YIDQTALAGQ TPAYFPWTTR NEVGDKTINR SGNQSIADTG
TTLALVGDDL CEAVYGAIPG ATKSTQQQGW VFPTSTDLSS LPTVRLAIGD TLFTINPEEL
PFQDLGDGTF YGGIQSRGDQ TFDIYGDVFL RSVYAIFDQG NTRFGCTQRA STLSSNGEKY
//