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Database: UniProt
Entry: A0A0F4G580_9PEZI
LinkDB: A0A0F4G580_9PEZI
Original site: A0A0F4G580_9PEZI 
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
//
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