ID A0A1J9PBF3_9EURO Unreviewed; 386 AA.
AC A0A1J9PBF3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN ORFNames=ACJ73_09221 {ECO:0000313|EMBL:OJD13290.1};
OS Blastomyces percursus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=1658174 {ECO:0000313|EMBL:OJD13290.1, ECO:0000313|Proteomes:UP000242791};
RN [1] {ECO:0000313|EMBL:OJD13290.1, ECO:0000313|Proteomes:UP000242791}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EI222 {ECO:0000313|EMBL:OJD13290.1,
RC ECO:0000313|Proteomes:UP000242791};
RA Cuomo C.A., Schwartz I.S., Kenyon C., De Hoog G.S., Govender N.P.,
RA Botha A., Moreno L., De Vries M., Munoz J.F., Stielow J.B.;
RT "Emmonsia species relationships and genome sequence.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M28 family.
CC {ECO:0000256|RuleBase:RU361240}.
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:OJD13290.1}.
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DR EMBL; LGTZ01002495; OJD13290.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J9PBF3; -.
DR STRING; 1658174.A0A1J9PBF3; -.
DR VEuPathDB; FungiDB:ACJ73_09221; -.
DR OrthoDB; 3091175at2759; -.
DR Proteomes; UP000242791; Unassembled WGS sequence.
DR GO; GO:0016603; F:glutaminyl-peptide cyclotransferase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd03880; M28_QC_like; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR037457; M28_QC.
DR InterPro; IPR007484; Peptidase_M28.
DR InterPro; IPR040234; QC/QCL.
DR PANTHER; PTHR12283; GLUTAMINYL-PEPTIDE CYCLOTRANSFERASE; 1.
DR PANTHER; PTHR12283:SF6; GLUTAMINYL-PEPTIDE CYCLOTRANSFERASE; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Hydrolase {ECO:0000256|RuleBase:RU361240};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361240}; Protease {ECO:0000256|RuleBase:RU361240};
KW Reference proteome {ECO:0000313|Proteomes:UP000242791};
KW Signal {ECO:0000256|RuleBase:RU361240};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|RuleBase:RU361240}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|RuleBase:RU361240"
FT CHAIN 29..386
FT /note="Peptide hydrolase"
FT /evidence="ECO:0000256|RuleBase:RU361240"
FT /id="PRO_5011827546"
FT DOMAIN 125..358
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
SQ SEQUENCE 386 AA; 43153 MW; 88F7374DF661FAF2 CRC64;
MAKSIRHLAV SWLLFLLGTL FFAIPVQSYA TLSDGTLKSI PRPKNDFGIR NGALLAPILK
PRVPGTPGSL EVLEHFVDFF KNTLPEWTIE FQNSTSKTPV TGNKEVPFVN LIAYRDPPWS
NIGDTSRLTL AAHYDSKLEP AGFIGATDSA APCAIIMHSV RSIDAALTKK WDAMKGNPSH
ESLLDHQGIQ VLLLDGEEAF ASWTDTDSLY GSRSLAEAME GTFYPAASTY KSPLSAISLF
VLLDLLGEKD PRMPSYFKTT HWAYKNMATL ETRLRQLGQF KSAPSWKNGD NIWFVDSEKE
TFFPSGIGDD HIPFMERGVE ILHLITSPFP KVWHKITDDA EHLDLETVED WSTLLTAFVA
EWLELEDMLP KYEGSVPENE SKKTEL
//
