ID A0A238F9E9_9BASI Unreviewed; 970 AA.
AC A0A238F9E9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=BQ2448_605 protein {ECO:0000313|EMBL:SCV68484.1};
GN ORFNames=BQ2448_605 {ECO:0000313|EMBL:SCV68484.1};
OS Microbotryum intermedium.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX NCBI_TaxID=269621 {ECO:0000313|EMBL:SCV68484.1, ECO:0000313|Proteomes:UP000198372};
RN [1] {ECO:0000313|Proteomes:UP000198372}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jeantristanb JTB J.-T., Ricardo R.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FMSP01000003; SCV68484.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238F9E9; -.
DR STRING; 269621.A0A238F9E9; -.
DR OrthoDB; 1943592at2759; -.
DR Proteomes; UP000198372; 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 InterPro; IPR002168; Lipase_GDXG_HIS_AS.
DR InterPro; IPR033140; Lipase_GDXG_put_SER_AS.
DR PANTHER; PTHR48081; AB HYDROLASE SUPERFAMILY PROTEIN C4A8.06C; 1.
DR PANTHER; PTHR48081:SF5; ABHYDROLASE_3 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF07859; Abhydrolase_3; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS01173; LIPASE_GDXG_HIS; 1.
DR PROSITE; PS01174; LIPASE_GDXG_SER; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000198372}.
FT DOMAIN 213..343
FT /note="Alpha/beta hydrolase fold-3"
FT /evidence="ECO:0000259|Pfam:PF07859"
FT REGION 180..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..439
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..840
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..874
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..891
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 294
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10038"
SQ SEQUENCE 970 AA; 108798 MW; 4DAA16BCE8F6F59C CRC64;
MDFLPLNPWT MSVSGLGMII YAGCRHFALH KKITSKQSAR GSFLFDEAFS VMKYFFVKAT
EHTVEEAQAF GNIFTPAPWW VCVVRVLIPL DTRLEANRIL IDTLGEDDIQ NVVGGKEWWQ
RCPNPDGALN GEWISMKKDW HGLDADEVDD DELETIKHEK VEAMKRKAED DRKRRYKLGR
EREERRAKGE DDPYGDDEGE PAYEHDLDEM RCILYIHGGA YFFGSPNTHR YSIWRYARKI
GGRAFALQYR LSPQFPFPCA LADALASYLY LIRPPIGAKH KPVDPKRLVI AGDSAGGGLT
LALSCLIRDA GLPAPAGIVL ISPWCDLTHS FPSILQNTET DVIPAFGLGL FKPSMLWPPP
PAEWQERADR STSIKGLKHA AEVIGKERRA NRKTSMFFNG SSRAHRKGEQ LLAEVEGFPV
EDPQRAEMTK TDEDGARDSS GGSAQENGEA KAEVGKVLKL KIDGEEVEVR DQIQLYATND
QLVYPFVSPV WQPSLGGLPS MYIMCGDKEV LRDEIVYMAH RAAHPDRYPV RQALLDANPE
RTKRHSEYPP TKVHLQIYDG ICHDLPLFAF TTPAKYCYRA ISSFVKFVTA DENKRGVDDE
VLASPVSNTG MELPVEILIK HEDAKLHHER IAESASPSRF SSLPQGIDTL PMPAPQIKID
TSVPTGQAAQ NGEAKEIRSS SSVAMKTHIN LAERVNDDSP SVQSDLSLSR YYTNLEKTIY
ASTQPSHRPA YVDNMVSERI SLTGVVRPLE PKEEVEVLKI PKDDLGLVKE GPVKRYLAGK
AKWDKKFKKT YEHVMRKRER ESPKSVGRAF INDELMTPQM TRSSEQLKKS MREEAERISA
QLKQRTLNKN ANFKTSAHTG STLMPSSTDG TDSPSRRTDS PKPMEDAEEE RDEHFHLGIW
ALPGEKPPPS SIAARKDTKE ARRLARVLDE RYSKLSALNV WNEVHRMANK VAEPPGRDLG
APHVGAAATS
//