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Database: UniProt
Entry: A0A061H4P1_9BASI
LinkDB: A0A061H4P1_9BASI
Original site: A0A061H4P1_9BASI 
ID   A0A061H4P1_9BASI        Unreviewed;      1251 AA.
AC   A0A061H4P1;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, 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=PFL1_04952 {ECO:0000313|EMBL:EPQ27414.1};
OS   Pseudozyma flocculosa PF-1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX   NCBI_TaxID=1277687 {ECO:0000313|EMBL:EPQ27414.1, ECO:0000313|Proteomes:UP000053664};
RN   [1] {ECO:0000313|EMBL:EPQ27414.1, ECO:0000313|Proteomes:UP000053664}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PF-1 {ECO:0000313|EMBL:EPQ27414.1,
RC   ECO:0000313|Proteomes:UP000053664};
RX   PubMed=23800965; DOI=10.1105/tpc.113.113969;
RA   Lefebvre F., Joly D.L., Labbe C., Teichmann B., Linning R., Belzile F.,
RA   Bakkeren G., Belanger R.R.;
RT   "The transition from a phytopathogenic smut ancestor to an anamorphic
RT   biocontrol agent deciphered by comparative whole-genome analysis.";
RL   Plant Cell 25:1946-1959(2013).
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DR   EMBL; KE361639; EPQ27414.1; -; Genomic_DNA.
DR   RefSeq; XP_007880673.1; XM_007882482.1.
DR   AlphaFoldDB; A0A061H4P1; -.
DR   GeneID; 19319052; -.
DR   KEGG; pfp:PFL1_04952; -.
DR   eggNOG; ENOG502S9ZP; Eukaryota.
DR   HOGENOM; CLU_265744_0_0_1; -.
DR   OrthoDB; 1421840at2759; -.
DR   Proteomes; UP000053664; 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:SF8; STERYL ACETYL HYDROLASE MUG81-RELATED; 1.
DR   Pfam; PF07859; Abhydrolase_3; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000053664}.
FT   DOMAIN          576..666
FT                   /note="Alpha/beta hydrolase fold-3"
FT                   /evidence="ECO:0000259|Pfam:PF07859"
FT   REGION          1..255
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          483..564
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          769..1153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1161..1180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..131
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        175..198
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..251
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        483..499
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        507..564
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        800..818
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        819..847
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        916..982
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1025..1044
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1084..1098
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1251 AA;  135417 MW;  004BF4B1FD290872 CRC64;
     MAPSSTSTET ESPRTRPREA LQASSAFKSY SAANGNVAPA PKREKGVFTS TSRTAALASD
     SDDDSVLGEV PGSSSGSSGD EAASRAAQSG QSSSSNKSRK AGKSSTSSKM TRLSKLFSPS
     SRPSSPSSTP QDKGKGKERS RPKTAVHAGR KLRATEIGPA TGNVALDSDE EEYPSEDERR
     ASVENMRELK EKQRRNVQSM DEAQVAGLQK AKEAPEKLDR MASQEADDRG RARTKAASED
     TPSEQRARDL SPGAKRNSLL ASKLPNLQLP EAITQKLTLP QFQIPIKDFP LQGSGKDSEF
     DQAHPVWAKQ PYKYLYYAYF GLSVGLYHLP AWSLTSAVKS KRGRKDWSWK RATMVKLFRH
     GTKLTFRTHT NLGRDLTKEV PHSKTVKSKF VWVDELADEY ISGELERAMK IQKIKALRTC
     GFWYGESGDG GVGQKAAPGE KVMFHLHGGA YWIGTAHESD VTAAVNTQAL RYMHEIYESQ
     KFADMSPTSS RNSTRSGDVR GEGGASGNGN GTASRSDLGS TIDAATGAER PASSSASSSS
     SSSSSSASKA AKAGPKVSTT DYTDPSAKAG RLLRTFSLDY RLCVPGKPQA GSYPAALLDA
     LAGYRYLIED LGFHPEDVIV AGDSAGGNLG IALCRYLRDE KVMPMPGSLL LMSPWADCSR
     SHSGPTGAPN LMSTAHRNIK SDIISPCLAF RNTAVSAFLG ELPARETYRN PYLSSISLQL
     PPHKGGKGPF WGFEGFPKRI YITTGSAEIS YDQHLTLAHR MAAGTKHGAP IYTGDKLSKG
     QDPAKLAGRY DYPRPKGLKI SLSSATTPGS TPGSETTPAE QEHENEERAA ASELFSDNDK
     DSDGQPEASI EELVSSAGEI VMRTRSKDGV SPSVNHRTDS DQVKMGAMRP VDSSRTDAAT
     SEKVDETMLP SQRQQQMEEK ELKQDLREAD ALPSHRREGE APRPRGEQRE LEDANAAQRE
     AIDVELARDE DRQTEEMAKV RRGQEGYSLA APAGRMTEEA TKKRKGSRGQ AGAGSAGAQE
     RRPDSGTCAQ HDEADDVIKA QDFIGDDNDD DDDAGSSSMS SQRATDGEGK QRRHRLKNKL
     FRREPSNTVP TTPQIRISPP ESEADAVDDD EGRTGRSGDG AGGGGGGSYF DLGRRRTNFP
     APPSGPRRRA YSEVSPLTPW MQASPSASAS SSHLDSLSNN GSTWSVASGA TATSSYHPEH
     DDRAQPHHEL EERVVILDEV KDAIHDYLLF SWFEPERSST WRRIAKWIHE A
//
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