ID A0A0L1IY49_ASPNO Unreviewed; 552 AA.
AC A0A0L1IY49;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Putative penicillin-binding protein {ECO:0000313|EMBL:KNG84350.1};
GN ORFNames=ANOM_009494 {ECO:0000313|EMBL:KNG84350.1};
OS Aspergillus nomiae NRRL 13137.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG84350.1, ECO:0000313|Proteomes:UP000037505};
RN [1] {ECO:0000313|EMBL:KNG84350.1, ECO:0000313|Proteomes:UP000037505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG84350.1,
RC ECO:0000313|Proteomes:UP000037505};
RA Moore M.G., Shannon B.M., Brian M.M.;
RT "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL Submitted (JUN-2014) 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:KNG84350.1}.
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DR EMBL; JNOM01000213; KNG84350.1; -; Genomic_DNA.
DR RefSeq; XP_015405273.1; XM_015554750.1.
DR AlphaFoldDB; A0A0L1IY49; -.
DR GeneID; 26811298; -.
DR OrthoDB; 1931461at2759; -.
DR Proteomes; UP000037505; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022438};
KW Protease {ECO:0000256|ARBA:ARBA00022438};
KW Reference proteome {ECO:0000313|Proteomes:UP000037505}.
FT DOMAIN 32..349
FT /note="Beta-lactamase-related"
FT /evidence="ECO:0000259|Pfam:PF00144"
FT DOMAIN 371..549
FT /note="D-aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF07930"
SQ SEQUENCE 552 AA; 60750 MW; 214231BA885315D4 CRC64;
MEPFLYGTYS ILVPFIAMNP SIQDILENVS SVYRGPGGAA AVLKDGKLVG ERVWGYADLQ
KLVPMTPSTL MPICSITKQM VCMMLKDLER NPTPDMLRRG NISRQFSDTL LQMLHPDLAG
NTGLKLEHLC NNQSGIRDYW AMSMFWGAHP DGEFRLEEDA KKAMDRTRSL HFEPGTQYSY
CNLNFHILAR LIERVSGQSL DDLLAERLFS PARMTTARLC PDNGNLPPPC VGYEGSESSG
FIPAINRMQW SGDAGVVASL KDMTAYEDYL QTSWDDEQSL YRAIAQQPSF KDGTIARYGH
GLAYGNVRGV ATIGHGGALR GFRLHRIQAP SEKLAIVVML NHEADAEAVA QNIMQGVFNI
SKGKNPRLDL VNPSPDWFGT FYHPDAGLVV EVGHGRQGHL TVTYGGSGEA LACVEEGKAQ
SSNTTATING DTLTLHRLAD NHVIHAERAA TGQQPPKDLY VGEYYCAEVE STFRCSGKGG
MLYGNFEGYL GQGPPHLMRY IGQDIWLLSC PRGLDAPAPG NWTVVFQRDD HGDIASVVIG
CWLARKVAFA RQ
//
