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Database: UniProt
Entry: A0A178B3G2_9PLEO
LinkDB: A0A178B3G2_9PLEO
Original site: A0A178B3G2_9PLEO 
ID   A0A178B3G2_9PLEO        Unreviewed;       545 AA.
AC   A0A178B3G2;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Alpha/beta-hydrolase {ECO:0000313|EMBL:OAL04281.1};
GN   ORFNames=IQ06DRAFT_364844 {ECO:0000313|EMBL:OAL04281.1};
OS   Stagonospora sp. SRC1lsM3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX   NCBI_TaxID=765868 {ECO:0000313|EMBL:OAL04281.1, ECO:0000313|Proteomes:UP000077206};
RN   [1] {ECO:0000313|EMBL:OAL04281.1, ECO:0000313|Proteomes:UP000077206}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAL04281.1,
RC   ECO:0000313|Proteomes:UP000077206};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S33 family.
CC       {ECO:0000256|ARBA:ARBA00010088}.
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DR   EMBL; KV441707; OAL04281.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178B3G2; -.
DR   STRING; 765868.A0A178B3G2; -.
DR   InParanoid; A0A178B3G2; -.
DR   OrthoDB; 1833441at2759; -.
DR   Proteomes; UP000077206; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase 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; AB HYDROLASE-1 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   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:OAL04281.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077206};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..545
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008082581"
FT   DOMAIN          72..232
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
FT   DOMAIN          426..520
FT                   /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08386"
SQ   SEQUENCE   545 AA;  59605 MW;  DEE55BB9DE06481E CRC64;
     MTLSKVLTAL LLSQHVLSSP IREQAAIDAH GVPLYCSNLK VPLDYTDSRS NATLDLQLIK
     IEASKEPVKG SIIMNPGGPG ASGIEEISSN GPMYREVFGG QWNVIGFDAR GTGRTLPFAC
     NPVNKTSSSL ARRAENFTIP QNDMYDVLTR KAWNGAGLFV EACAETEGNK DIASLISTPF
     VVRDMVNIVD ALGEDGLLRF WGRSYSTTLG QTFAAMFPER VGRIMLDSVM RFQDYYDGTW
     SSAPRDTNLA VLSFFQACIQ AGPAWCPIAN FTGPDTTPES LNLELADIFQ ELLDKPEIGE
     TEIKLPTQAW WQPGTPLYQT IKMSFLSQTY RPNQFPALWA ISDLIFKRDW EGIITVLNTP
     AASPSNGTDQ GSSNTTLDLP WHLGLNALHG ISCSDTARRA EKPEEMYSLL QSQRAQGSWA
     DVLGPQTWVC PQWPFAAKER FTGPFIDLKT KNTILLISGS HDPITPLSGA WEASANLPDS
     RLLVHKGHGH GIMNHRSNCT IKAIHDYFND GTLPEVGTEC EPNQPAFELA IEAAEALAAA
     ADALP
//
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