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Database: UniProt
Entry: A0A168BGI1_CORDF
LinkDB: A0A168BGI1_CORDF
Original site: A0A168BGI1_CORDF 
ID   A0A168BGI1_CORDF        Unreviewed;       596 AA.
AC   A0A168BGI1;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Peptidase S33 tripeptidyl aminopeptidase-lik {ECO:0000313|EMBL:OAA70085.1};
GN   ORFNames=LEL_09901 {ECO:0000313|EMBL:OAA70085.1};
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:OAA70085.1, ECO:0000313|Proteomes:UP000076881};
RN   [1] {ECO:0000313|EMBL:OAA70085.1, ECO:0000313|Proteomes:UP000076881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA70085.1,
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:OAA70085.1}.
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DR   EMBL; AZHF01000010; OAA70085.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A168BGI1; -.
DR   STRING; 1081108.A0A168BGI1; -.
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:SF29; AB HYDROLASE-1 DOMAIN-CONTAINING PROTEIN; 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:OAA70085.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000313|EMBL:OAA70085.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076881};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..596
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007895667"
FT   DOMAIN          87..291
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
FT   DOMAIN          449..557
FT                   /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08386"
SQ   SEQUENCE   596 AA;  64917 MW;  D8D1C853B5DAD4F1 CRC64;
     MGPIVGCLLI AALSLPSQAA TSISSFDWDQ VTPSASLNYT PCYQNHKCAR LLLPLDWLNP
     ENGANTTVAI IARPAVVSET DPSFGGTIIV NPGGPGASGI DFLLGAGALI QAMAHGNKKF
     EILSFDPRGV GRTTPSADCY RNEYARGNGL IMERAIGTLG AGEAVLKRKL AQAKGFAEMC
     AKRGRADDVR NFMSTTSVAR DMAKIVDELH VLRHAHDADQ DQGDTDARVE LRSEKQETSA
     RLNYWGWSYG TDLGNYFASM FPGRVERMIL EGVQDVRDYA DGTWLKFGDA EKTFDYFWDA
     CYGAGKSCAL YQELDTDAGD ARARFDAFIE EVNQDPPSYV GPDGTIASIM EEDVMLVIFA
     ALLQPILTFP SLAETLMEAM AGNFSTLYGQ LGQPSAESCP LPIPGTFTWT ADARIGIACG
     DGEPQNNMTL AAYQDYMAGI AADAPNFWPF MADIRLPCVH WPFRPKDRFK GPWVTPKSDP
     SRVPGRPTAP LLFISSRYDL LTPPSRAVEM SRFHPGSTVL VQENYGHGTI ATPSKCRDDH
     VKKYFDAGEV PPDGAVCDSD CVPFHDCPGD ADVKKAWLGH AEYSVADRRL PPSGWF
//
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