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Database: UniProt
Entry: A0A1L9SDL4_9EURO
LinkDB: A0A1L9SDL4_9EURO
Original site: A0A1L9SDL4_9EURO 
ID   A0A1L9SDL4_9EURO        Unreviewed;       355 AA.
AC   A0A1L9SDL4;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Peptidase S66, LD-carboxypeptidase A {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ASPZODRAFT_17490 {ECO:0000313|EMBL:OJJ45271.1};
OS   Penicilliopsis zonata CBS 506.65.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicilliopsis.
OX   NCBI_TaxID=1073090 {ECO:0000313|EMBL:OJJ45271.1, ECO:0000313|Proteomes:UP000184188};
RN   [1] {ECO:0000313|Proteomes:UP000184188}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 506.65 {ECO:0000313|Proteomes:UP000184188};
RX   PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA   de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA   Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA   Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA   Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA   Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA   Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA   Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA   Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA   Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA   Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA   Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA   Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA   Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA   Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA   Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA   Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA   van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA   Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA   Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA   Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA   Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT   "Comparative genomics reveals high biological diversity and specific
RT   adaptations in the industrially and medically important fungal genus
RT   Aspergillus.";
RL   Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
CC   -!- SIMILARITY: Belongs to the peptidase S66 family.
CC       {ECO:0000256|ARBA:ARBA00010233}.
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DR   EMBL; KV878345; OJJ45271.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L9SDL4; -.
DR   STRING; 1073090.A0A1L9SDL4; -.
DR   VEuPathDB; FungiDB:ASPZODRAFT_17490; -.
DR   OrthoDB; 3132006at2759; -.
DR   Proteomes; UP000184188; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase 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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184188}.
FT   DOMAIN          17..134
FT                   /note="LD-carboxypeptidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02016"
FT   DOMAIN          210..338
FT                   /note="LD-carboxypeptidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17676"
SQ   SEQUENCE   355 AA;  38905 MW;  3D4F4D449024DF95 CRC64;
     MATATILPPA LKKGDTIAFV SPSARLNQVL PTPIERGKTF LESLGFKVKV IYTPVSSRMA
     ESVRVRCEEL HEAFRDEAVT AIICTIGGSH ANEMLPFLDY SLIQANPKIF VGYSDTTFLH
     YAIESRTGLR TFYGPSVLTD LSDSPHPIQF TVDHFLHVLG GTGEPVGPVP RSPTFSVEHN
     DFLLHGELSE QPRQMVESPP WRWVRKGRAT GHLYGGTASC VTRLHGTAYS PASWKGKVLF
     LESSMGDNTQ VPYSVDRFRG SLVDLALGGV LGDISGLVIG RGYKYDASMQ DELAEAITDV
     FELIVGRDRN DELPVLMNVD FGHTSPLLTL PMGALVRLDS ESDEFTILES GVHIN
//
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