ID B8M896_TALSN Unreviewed; 377 AA.
AC B8M896;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN ORFNames=TSTA_036350 {ECO:0000313|EMBL:EED20409.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED20409.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
CC -!- SIMILARITY: Belongs to the peptidase M28 family.
CC {ECO:0000256|RuleBase:RU361240}.
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DR EMBL; EQ962654; EED20409.1; -; Genomic_DNA.
DR RefSeq; XP_002480843.1; XM_002480798.1.
DR AlphaFoldDB; B8M896; -.
DR STRING; 441959.B8M896; -.
DR GeneID; 8101906; -.
DR VEuPathDB; FungiDB:TSTA_036350; -.
DR eggNOG; KOG3946; Eukaryota.
DR HOGENOM; CLU_045003_0_0_1; -.
DR InParanoid; B8M896; -.
DR OMA; GIQDDHI; -.
DR OrthoDB; 3091175at2759; -.
DR PhylomeDB; B8M896; -.
DR Proteomes; UP000001745; 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:UP000001745};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|RuleBase:RU361240}.
FT DOMAIN 105..350
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 377 AA; 42400 MW; 0DA08F722C2A314D CRC64;
MTSVPSLSQL SEETLKKLPR PGNDFDIHEG KLLAPILRTR IPGTPGSIAV LNHFNDFFKQ
TLPDWTVEFQ NSSARTPISG NKEVPFVNFI ASRDPPWASK GDVGRLTLVA HYDSKYEPKG
FIGAIDSAAP CAMIMHAMRS IDAALTRKWD DMQAKGDGLD SGLDAHTGIQ VLFLDGEEAF
KTWTDSDSLY GSRSLAETWD ETTHSAMSIF RTPLSSISLF MLLDLLGSKD PTIQSYFPTT
HWAYQNLASL EGRLRNLKQF KSSPNYDIKS GHVDEPQWLV DAEKSEHLLK SWTAIQDDHV
PFMRRGVDVL HIIDTPGRAN FPTVWHTIHD DGEHLDLPTV EDWSMLITAF AAEWMELEGY
FDAQDAAEKM YIRKTEL
//
