ID A0A2A9NN64_9AGAR Unreviewed; 598 AA.
AC A0A2A9NN64;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Peptidase S33 tripeptidyl aminopeptidase-like C-terminal domain-containing protein {ECO:0000259|Pfam:PF08386};
GN ORFNames=AMATHDRAFT_76363 {ECO:0000313|EMBL:PFH49122.1};
OS Amanita thiersii Skay4041.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Pluteineae; Amanitaceae; Amanita.
OX NCBI_TaxID=703135 {ECO:0000313|EMBL:PFH49122.1, ECO:0000313|Proteomes:UP000242287};
RN [1] {ECO:0000313|EMBL:PFH49122.1, ECO:0000313|Proteomes:UP000242287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKay4041 {ECO:0000313|EMBL:PFH49122.1,
RC ECO:0000313|Proteomes:UP000242287};
RG DOE Joint Genome Institute;
RA Hess J., Skrede I., Wolfe B., LaButti K., Ohm R.A., Grigoriev I.V.,
RA Pringle A.;
RT "Transposable element dynamics among asymbiotic and ectomycorrhizal Amanita
RT fungi.";
RL Submitted (FEB-2014) 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; KZ302038; PFH49122.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9NN64; -.
DR STRING; 703135.A0A2A9NN64; -.
DR OrthoDB; 50200at2759; -.
DR Proteomes; UP000242287; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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; PF08386; Abhydrolase_4; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000242287};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..598
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012428097"
FT TRANSMEM 255..274
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 461..561
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08386"
FT REGION 37..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 598 AA; 65503 MW; 1616D9B5324B261C CRC64;
MGLGRHALCL FVCTLFVLYS GLYAILPKSN WEALSMPQGV GSPGGEDERN GRGACRSTTS
SEEGVWTEIR ASEDLVWTDC YQGKDKRMQC ARLLVPLNYS APLSDSNQAS IALLRVPSAY
SSSHPSYLGP ILFNPGGPGG SGVDLILSVG DLLHQIVGKE FDVVGFDPRG VARSLPRVDL
FRDRVERAMW EAGEGIVDPE RERGVFGRKL ARAGVIGRLA ERVERSGGGY LRSIQTDHTA
RDMLRITEKQ GRDKLLYWGF SYGTILGATF AAMFPDKVGR LVIDGVADSE NYFATLWSNN
LIDTDKTMQW FFDSCYEAGP SNCPFYASSP EAISQRLTKL YDTLKMQPIP VVDPLSSSTG
MVDYPFLRTA IFTVLYKPYA FFPALAKALA DLEGGNASSI WSVMNSAQRR FRCSCGDDEE
HAFESISDAT PGIMCTDGKP ISGTLEDTEA HYREMKNMSG WADVWANIRV MCSSWPDFPR
THFQGPFEGN TSHPLLVIGN TADPVTPLWA AKKMSKGYPG SVVLTQDSPG HCSIAGPSVC
TINYVRDYFQ KGTLPPEGTV CPVLSPPIPT SQTRLGDENQ FYTSFGSLSE SSNLPLCL
//
