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
//