ID   A0A0F0II28_ASPPU        Unreviewed;       545 AA.
AC   A0A0F0II28;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=D-aminopeptidase domain C {ECO:0000313|EMBL:KJK67434.1};
GN   ORFNames=P875_00117193 {ECO:0000313|EMBL:KJK67434.1};
OS   Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK67434.1, ECO:0000313|Proteomes:UP000033540};
RN   [1] {ECO:0000313|EMBL:KJK67434.1, ECO:0000313|Proteomes:UP000033540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC   {ECO:0000313|Proteomes:UP000033540};
RA   Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA   Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT   "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S12 family.
CC       {ECO:0000256|ARBA:ARBA00038215}.
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:KJK67434.1}.
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DR   EMBL; JZEE01000194; KJK67434.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F0II28; -.
DR   Proteomes; UP000033540; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.128.50; -; 2.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   InterPro; IPR001466; Beta-lactam-related.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR027279; D_amino_pept/lipop_sf.
DR   InterPro; IPR012856; DAP_B_dom.
DR   PANTHER; PTHR46825; D-ALANYL-D-ALANINE-CARBOXYPEPTIDASE/ENDOPEPTIDASE AMPH; 1.
DR   PANTHER; PTHR46825:SF9; PROTEIN FLP; 1.
DR   Pfam; PF00144; Beta-lactamase; 1.
DR   Pfam; PF07930; DAP_B; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF50886; D-aminopeptidase, middle and C-terminal domains; 2.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW   ECO:0000313|EMBL:KJK67434.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022438, ECO:0000313|EMBL:KJK67434.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022438, ECO:0000313|EMBL:KJK67434.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033540}.
FT   DOMAIN          16..345
FT                   /note="Beta-lactamase-related"
FT                   /evidence="ECO:0000259|Pfam:PF00144"
FT   DOMAIN          364..542
FT                   /note="D-aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF07930"
SQ   SEQUENCE   545 AA;  60656 MW;  F4C62D7269A95B7A CRC64;
     MTSTKEDSIL VYDRIQDILE KIPSRYRGPG GALAVLSDGE LVAEHVWCYA DMQKLIPMTT
     STLMPICSIT KQMVCLILKD LERNPTPEMV KRGNVSRQFS DALHQMVHPD LTTNTGLKLE
     HLCHNQSGIR DYWAMSMFWG AHPDGVFRLE EDAKKALERT RSLHFEPGTQ YAYCNLNFYI
     LARLIENVSG QTLSDLLAER LFLPAKMKTA RLCADNANLP PPCVGYEGTE SSGFIPAINR
     MQWSGDAGVV ASLKDMIAYE HYLQTCWDDE KSVYRAIAQQ QSFKDGTIAQ YGYGLKHVTI
     RGIATIGHGG ALRGFRLHRI QAPSERVAVV VMLNHQADAE EVAQDILKSV LAIFVGQVPR
     LDPVNPSQDW FGTFYDPDAQ LVVDIRHGGQ GHVIVSYAGS DETLICDGEN IARSNNTVGI
     VDGGIPKLRR LVDNRVLDVK RVATGYQPHK DDYLGEYYCA EIESTFGCSG GGGMLYGYFE
     GYLGQGPPHL MRYIGRDIWM LSCPRGLDAP APGNWTVVFQ RADHGDITSV TISCWLARKV
     VFVKQ
//