ID A0A168H005_CORDF Unreviewed; 585 AA.
AC A0A168H005;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Peptidase S33 tripeptidyl aminopeptidase-lik {ECO:0000313|EMBL:OAA77140.1};
GN ORFNames=LEL_03963 {ECO:0000313|EMBL:OAA77140.1};
OS Akanthomyces lecanii RCEF 1005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC Cordyceps confragosa.
OX NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA77140.1, ECO:0000313|Proteomes:UP000076881};
RN [1] {ECO:0000313|EMBL:OAA77140.1, ECO:0000313|Proteomes:UP000076881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA77140.1,
RC ECO:0000313|Proteomes:UP000076881};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
CC -!- SIMILARITY: Belongs to the peptidase S33 family.
CC {ECO:0000256|ARBA:ARBA00010088}.
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:OAA77140.1}.
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DR EMBL; AZHF01000003; OAA77140.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168H005; -.
DR STRING; 1081108.A0A168H005; -.
DR OrthoDB; 1833441at2759; -.
DR Proteomes; UP000076881; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR013595; Pept_S33_TAP-like_C.
DR PANTHER; PTHR43248; 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE; 1.
DR PANTHER; PTHR43248:SF25; PEPTIDASE S33 TRIPEPTIDYL AMINOPEPTIDASE-LIKE C-TERMINAL DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR Pfam; PF08386; Abhydrolase_4; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:OAA77140.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000313|EMBL:OAA77140.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076881}.
FT DOMAIN 104..255
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT DOMAIN 408..500
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08386"
FT REGION 523..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 585 AA; 63823 MW; 602220458886EB32 CRC64;
MSPKQILSIL SMIGMATTSS LHLQPRLDSK LDWGECNDPV INATLPADCA NFTVPLDYLS
EGGEEIQLQL ARIRAPVQPA KGTILLNFGG PGEEARATLT GPKAIQYLAL SGGRYDLAAF
DPRGVANTIP QKCFLTKQDK IEFLEAQTWH DQNETSLEKM WDRAKIDVEK CYEAHNKTQP
FLGTASVARD LMSVVDALGE DGMLRYWGFS YGTTLGATVA AMFPDKIDKM VIDGVQNPHE
YYHALADYEE WTDSDRVFSE IFRSCVRAGP QQCPMAAGNY TAEEMEMIAW RVANALKTNP
IQLGNGTEFD YPVIRGLFGL SLYGPDRWPL LMKILPYLAT NETDHPVFVK AASALVNQFT
ASVEIIPAVY GIHCSDRIPR LETLDEFRPV QARLSEISKV MDGSAALSMA CGLWKSDAKE
RYMGDFQVKT KNPILLSSNR YDGHTPLKSA YNVSSSFEGS SVLVVNGFGH STMSQASVCN
LKQTSAYWLN GTLPEKGFQC EVNAVPYGNY TWQNAITEVY GDGFGSPGGS NAQPQPVPGG
GNDNGNGSDN EANPKPTLPP VSRATSLISK INLAPALAVA LVCIL
//
