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Database: UniProt
Entry: K1VGD0_TRIAC
LinkDB: K1VGD0_TRIAC
Original site: K1VGD0_TRIAC 
ID   K1VGD0_TRIAC            Unreviewed;       627 AA.
AC   K1VGD0;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Alpha/beta hydrolase fold-3 domain-containing protein {ECO:0000259|Pfam:PF07859};
GN   ORFNames=A1Q2_07657 {ECO:0000313|EMBL:EKC98111.1};
OS   Trichosporon asahii var. asahii (strain CBS 8904) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Trichosporonales; Trichosporonaceae; Trichosporon.
OX   NCBI_TaxID=1220162 {ECO:0000313|EMBL:EKC98111.1, ECO:0000313|Proteomes:UP000006757};
RN   [1] {ECO:0000313|EMBL:EKC98111.1, ECO:0000313|Proteomes:UP000006757}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 8904 {ECO:0000313|EMBL:EKC98111.1,
RC   ECO:0000313|Proteomes:UP000006757};
RX   PubMed=23193141; DOI=10.1128/EC.00264-12;
RA   Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT   "Genome sequence of the Trichosporon asahii environmental strain CBS
RT   8904.";
RL   Eukaryot. Cell 11:1586-1587(2012).
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:EKC98111.1}.
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DR   EMBL; AMBO01000398; EKC98111.1; -; Genomic_DNA.
DR   AlphaFoldDB; K1VGD0; -.
DR   STRING; 1220162.K1VGD0; -.
DR   eggNOG; KOG1515; Eukaryota.
DR   HOGENOM; CLU_020372_0_0_1; -.
DR   InParanoid; K1VGD0; -.
DR   OMA; HEAGQAN; -.
DR   OrthoDB; 5491340at2759; -.
DR   Proteomes; UP000006757; 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; IPR013094; AB_hydrolase_3.
DR   PANTHER; PTHR48081; AB HYDROLASE SUPERFAMILY PROTEIN C4A8.06C; 1.
DR   PANTHER; PTHR48081:SF35; AB HYDROLASE SUPERFAMILY PROTEIN C4A8.06C; 1.
DR   Pfam; PF07859; Abhydrolase_3; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000006757}.
FT   DOMAIN          190..398
FT                   /note="Alpha/beta hydrolase fold-3"
FT                   /evidence="ECO:0000259|Pfam:PF07859"
FT   REGION          91..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          439..464
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          483..535
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          553..586
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        138..170
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        500..535
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        569..583
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   627 AA;  68797 MW;  1F3E6D72039B87C9 CRC64;
     MRNVANYTDF ADIVLIRRLI SITYLIPLPA DAVVTPITFV VPKRRADALR GFLREFDLLE
     SGTRELTGEW VVGNEVWKRL KSERRAKWHA ELRRRQGPGP SRLRDDMSDS GSSAAPTVPL
     LHGHPHPPRP GRRSYSGPRT HSRGNSLNGT ISGLPGSSAD STQQTPRQGA ATPEPEMEGE
     SPGRRERVIY YVHGGAYYVG NAATHRLITI GVSRACNARV FAITYRLAPE AAFPLPLLDV
     VQGYMRLLAP PLSIPPENIV VAGDSAGGGL SLALCMYLRD NDYPMPAGLV LLSPWVDLTM
     SCGSWEENGD SDVVPLPPLD SHLNPVGCYL GPDGVGAYVT HPYASPLFGD LRDLPPMLIQ
     SGDSEVLRDE ITLLAHKATL AGLNVTHELY EDMVHVFQMF TWLPATTASI NSIGRWVRQT
     LPRIEWEARQ NELHDLEEEP LHPPLHPHDA PHEHDEHEAG QANPYDAEED PFFAAFNSER
     RLRRSHTQHP LHVRSPTSPG PRSRAGSRAA SPSTLRRRRQ TASMHMSSPV SPVENHPFNV
     TTSGLASAFS TTGFDALSPT PSVRRRLRAP SSHPTTPSTR ARNHSHTDIF ELVEGYMEGG
     AANATVVYAP GGEIRSVGVL GDESDEE
//
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