ID Q0TXK9_PHANO Unreviewed; 462 AA.
AC Q0TXK9;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=AB hydrolase-1 domain-containing protein {ECO:0000259|Pfam:PF00561};
GN ORFNames=SNOG_15764 {ECO:0000313|EMBL:EAT76859.1};
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT76859.1, ECO:0000313|Proteomes:UP000001055};
RN [1] {ECO:0000313|Proteomes:UP000001055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC {ECO:0000313|Proteomes:UP000001055};
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
CC -!- SIMILARITY: Belongs to the peptidase S33 family.
CC {ECO:0000256|ARBA:ARBA00010088}.
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DR EMBL; CH445364; EAT76859.1; -; Genomic_DNA.
DR RefSeq; XP_001805902.1; XM_001805850.1.
DR AlphaFoldDB; Q0TXK9; -.
DR EnsemblFungi; SNOT_15764; SNOT_15764; SNOG_15764.
DR GeneID; 5982832; -.
DR KEGG; pno:SNOG_15764; -.
DR VEuPathDB; FungiDB:JI435_157640; -.
DR eggNOG; ENOG502QSNW; Eukaryota.
DR HOGENOM; CLU_024518_2_1_1; -.
DR InParanoid; Q0TXK9; -.
DR OMA; TNEYEHN; -.
DR OrthoDB; 2385117at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR002410; Peptidase_S33.
DR PANTHER; PTHR43248; 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE; 1.
DR PANTHER; PTHR43248:SF2; PROLYL AMINOPEPTIDASE; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PRINTS; PR00793; PROAMNOPTASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000001055}.
FT DOMAIN 70..233
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
SQ SEQUENCE 462 AA; 52802 MW; 26E362BFC7027ACF CRC64;
MIQAAKILEQ RSHLVPGKLR ITEHFFQVPR DYSNPASGTI QLFSRSALKA EKPADYPSES
SKDPKKTQLP WLVYLQGGPG FECRSPQSVS WVPTILDKGY RVLLLDQRGT GLSTAISQSS
LQLRGDEKVQ AEYMKSFRAD SIIKDCEAIR QALTADYPED KKKWSIMGQS FGGFCCSTYL
SFYPEGVKEA FVFGGLPPLR NNADEVYERL YERVKQRNES YYEKYPEDVG RVHRIIKLLS
RFGDNTVRVQ GGEGALSARR FMQLGIYFGK HGGIDEVHQM VLRADTDLTQ FGHLTRPTVL
ALEMAQSWDT NVIYALLHEP LYCQGEAANW SAERLLEKYP EFSLKNVESD KPVYFTGEMI
YPFMFDDYPE LKKLKTVGQL LAEEKDWPNL YDVEQLKKNE VPMYAAAYVD DMYVDFDLSM
ETARTIKGCK PFVTNSMYHN AIGAKTDEVL KELFARRDDV ID
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