ID F2PP79_TRIEC Unreviewed; 777 AA.
AC F2PP79;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Lipase/esterase family protein {ECO:0000313|EMBL:EGE03697.1};
GN ORFNames=TEQG_02729 {ECO:0000313|EMBL:EGE03697.1};
OS Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN [1] {ECO:0000313|Proteomes:UP000009169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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DR EMBL; DS995729; EGE03697.1; -; Genomic_DNA.
DR AlphaFoldDB; F2PP79; -.
DR VEuPathDB; FungiDB:TEQG_02729; -.
DR eggNOG; KOG1515; Eukaryota.
DR HOGENOM; CLU_004893_0_2_1; -.
DR Proteomes; UP000009169; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 2.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR InterPro; IPR002168; Lipase_GDXG_HIS_AS.
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.
DR PROSITE; PS01173; LIPASE_GDXG_HIS; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 232..282
FT /note="Alpha/beta hydrolase fold-3"
FT /evidence="ECO:0000259|Pfam:PF07859"
FT REGION 356..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..634
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..708
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..777
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 777 AA; 86057 MW; 8789B94AF43C634B CRC64;
MPFNILSVAF HASFTAVSTG VTHYLGKKPV KTEPAAHFSY HSGLKVVRRF LEHAARHTVE
ELQAFTGQKV PASYWVATGS VIIPAEQIES AAHILVAQLG PEGVSLVGGS KWWQWRDTEA
ALVAEWLETR RDYNDRRARK AKSNRIILYI HGGAYFFGSV ETHRYQLQRH ARKLKARVFA
RQACATAQSA HVEDYATSEL QESDGHRRNT QMLGELLRVE IDGATIEIKD QIHLYTTNKL
ISHPLVSPVL QPSLGGLPPL LVISGGGELL RDEQIYLAHK AANPEAYPPN DDILAKYDPD
RKILSQYKPT YVQLQVWNNI CHVAPTLSFT RPAKYMYRSV AQFSAWALSR AQESSIDIPD
SSPASSGDLL SNSEEKKASN KRTAEPELAQ HATIGKAGDP IPPFQNHMIR QLIDSEGHLL
PLPDEHDLPA LQVPRNHIGV PKPIPVRRWL AAKEEWDSKF IKEKRRLQKE RLKRIPMGID
DIAPGDRPPP SSRAARRGVA VSEVRQPTKK SVMLSFWNRL GAIHDAKIMQ KEKKNNVENK
FPTLWRGGVQ GEQRAAANVS RPSGQSKTQV VTDIGQSNES QRDFTTKPSR AIPEASVPQI
WRSPSSEELG RTRSPRRNSE SQGFVRDEGR GQNEETPVDS LLDEASIRTI RHSKGIISPP
PLSAAPLSDY ESVLQPGPYS GDDKTTVGVP TQKNEGTPGE SDAVSQNLPG GVVNRMDRNK
LPMFDFESAT GSNPRRELEP FPSLLNGSGG GARDNQSGYS SNYSQQSFSG PGNSGFH
//