ID A0A317VIX1_9EURO Unreviewed; 352 AA.
AC A0A317VIX1;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 10.
DE SubName: Full=Peptidase S66, LD-carboxypeptidase A {ECO:0000313|EMBL:PWY72978.1};
GN ORFNames=BO70DRAFT_341986 {ECO:0000313|EMBL:PWY72978.1};
OS Aspergillus heteromorphus CBS 117.55.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448321 {ECO:0000313|EMBL:PWY72978.1, ECO:0000313|Proteomes:UP000247233};
RN [1] {ECO:0000313|EMBL:PWY72978.1, ECO:0000313|Proteomes:UP000247233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 117.55 {ECO:0000313|EMBL:PWY72978.1,
RC ECO:0000313|Proteomes:UP000247233};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S66 family.
CC {ECO:0000256|ARBA:ARBA00010233}.
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:PWY72978.1}.
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DR EMBL; MSFL01000025; PWY72978.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317VIX1; -.
DR STRING; 1448321.A0A317VIX1; -.
DR VEuPathDB; FungiDB:BO70DRAFT_341986; -.
DR OrthoDB; 3132006at2759; -.
DR Proteomes; UP000247233; Unassembled WGS sequence.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR CDD; cd07062; Peptidase_S66_mccF_like; 1.
DR Gene3D; 3.40.50.10740; Class I glutamine amidotransferase-like; 1.
DR Gene3D; 3.50.30.60; LD-carboxypeptidase A C-terminal domain-like; 1.
DR InterPro; IPR027461; Carboxypeptidase_A_C_sf.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR027478; LdcA_N.
DR InterPro; IPR040449; Peptidase_S66_N.
DR InterPro; IPR040921; Peptidase_S66C.
DR InterPro; IPR003507; S66_fam.
DR PANTHER; PTHR30237:SF4; CARBOXYPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR30237; MURAMOYLTETRAPEPTIDE CARBOXYPEPTIDASE; 1.
DR Pfam; PF02016; Peptidase_S66; 1.
DR Pfam; PF17676; Peptidase_S66C; 1.
DR PIRSF; PIRSF028757; LD-carboxypeptidase; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF141986; LD-carboxypeptidase A C-terminal domain-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:PWY72978.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000313|EMBL:PWY72978.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000247233}.
FT DOMAIN 16..135
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 211..336
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
SQ SEQUENCE 352 AA; 38576 MW; 5C865AC7909500BE CRC64;
MPATILPKAL RKGDTIAFIS PSARLNHLFP IALERATAVF ESLGFQVKII YSTLPKDVSF
KESVKVRCEE LHSAFRDPAI AAIICTIGGA HCGEMLPHLD YDLIRSNPKI FVGYSDTTFL
HYAIESRTGL RTFYGPSILT DWSDLPNPVS FTVDHFLHVL AGTGGAVGAL PRSSVYTTAH
SDFMLTSDAS TKPRELTDAP AWRWLQNGCA TGRLYGGVVS CVVRLQGTLY APKSWKNKIM
FLECSMGDDM VSPYLVSRFR SALMDLALSD AFHDISGLVI GRCYKYDAQM QDELADVILG
VFETLVGRSD LPILMNVDFG HTSPLLTLPI GASVRLDSEN DEFVVLEAGV EA
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