ID Q0CYN3_ASPTN Unreviewed; 1211 AA.
AC Q0CYN3;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Alpha/beta hydrolase fold-3 domain-containing protein {ECO:0000259|Pfam:PF07859};
GN ORFNames=ATEG_01201 {ECO:0000313|EMBL:EAU37958.1};
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU37958.1, ECO:0000313|Proteomes:UP000007963};
RN [1] {ECO:0000313|Proteomes:UP000007963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963};
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the battenin family.
CC {ECO:0000256|ARBA:ARBA00007467}.
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DR EMBL; CH476595; EAU37958.1; -; Genomic_DNA.
DR RefSeq; XP_001208566.1; XM_001208566.1.
DR AlphaFoldDB; Q0CYN3; -.
DR STRING; 341663.Q0CYN3; -.
DR EnsemblFungi; EAU37958; EAU37958; ATEG_01201.
DR GeneID; 4315945; -.
DR VEuPathDB; FungiDB:ATEG_01201; -.
DR eggNOG; KOG3880; Eukaryota.
DR eggNOG; KOG4388; Eukaryota.
DR HOGENOM; CLU_003590_0_0_1; -.
DR OMA; KEPTNAW; -.
DR OrthoDB; 37251at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005773; C:vacuole; IEA:UniProt.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 2.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR InterPro; IPR003492; Battenin_disease_Cln3.
DR InterPro; IPR033140; Lipase_GDXG_put_SER_AS.
DR InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR23025:SF3; HORMONE-SENSITIVE LIPASE; 1.
DR PANTHER; PTHR23025; TRIACYLGLYCEROL LIPASE; 1.
DR Pfam; PF07859; Abhydrolase_3; 2.
DR Pfam; PF02487; CLN3; 2.
DR PRINTS; PR01315; BATTENIN.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR PROSITE; PS01174; LIPASE_GDXG_SER; 1.
PE 3: Inferred from homology;
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000007963};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 63..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 174..197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 209..227
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 331..351
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 357..380
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 392..416
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 428..445
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 680..852
FT /note="Alpha/beta hydrolase fold-3"
FT /evidence="ECO:0000259|Pfam:PF07859"
FT DOMAIN 902..981
FT /note="Alpha/beta hydrolase fold-3"
FT /evidence="ECO:0000259|Pfam:PF07859"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1054..1086
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1119..1144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1160..1193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1167..1193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 761
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10038"
SQ SEQUENCE 1211 AA; 132593 MW; 3C8DE7667230DEFE CRC64;
MPRSSLREET PMLPLPGAPS SSWAQFRQRL AATFHGADPR LVGDHHPGPS LTGSSRKCEC
TGLINNVLYV IILSAALDLV GPTVPKGVVL LADVLPSFGT KLVAPYFIHI VPYSVRVVIF
VLLSAIGMLL VALSPGYADG GTISTKIAGI ILASLSSGAG ELSFLGLTHF YGPFSLAAWG
SGTGAAGLVG AGAYALATTS LGLGVRNTLL ASACLPAVMV VSFFAILPRS PVHPLASVPA
EYRAIGTRDL LAEERGDDER DEREERVGER DGLLASVRED TQKGVSPTLL FPLASSPFAH
YRAFYPAYNA IYQVGVFISR SSTPFFRIHD LYFPSFLQIA NLVLLTLHAL FDFIPSVYII
FIVIFWEGLL GGLVYVNTFA EIGERVPKAD REFSLGATTV SDSAGICIAG FVSMVFEASI
TGAMHVTVNN YRVLLLILFV ILRIFPAPID LSHRTCNMID HVLGRPSTKF RKIQVCAVLL
FWSSLSPNAL TNELSGNKHG PPGIRNVSSR ISGKLTAWQT TVGVFLWLYV CRNFAKIVGL
ECPEPMANLY SRSFFRATWF MTALDAGFWT AMKIKPKWLR DIASLIFSIY YLFAAEQADD
KVRRVRATLT VDHLRVAWNK GTTPYLWALG KLARPRLTTY GPRAIRIPRP THSSYTEPTH
AWLYFDGPLS ALRDQTSVVL DFPGGGYVAM SPRAAEDRLL AWAGKTKVPI LSLDYKKAPE
YPYPYALHEC YDVYHMLVAT RGRCIGLSGH TRPHIVLSGD SAGGNLAVGT MLMLLQAGSE
DTPRWQPEHV LPRPAGLVLA YPSLNMRVES WMTEEQMALI QDKSARRTNE GIVRRKAADY
QRLTPGTSPV VSASDVRASA DSDPAAAPPV AAKPTKGTLA AQAAAVAEYH HPKQIRTRLA
VSSMISYVHD RILTPEMMRA MIILYIGPHN RPDFSTDFLL SPVLAPEALL ARFPKTYIIT
GERDPLVDDT VIFAGRLRQA KLRQFRERQE LGLEKSHREF NEKEHVEISL LPGVSHGFLH
IAGFFPESWK HIHRCGGWIV ELFAAATARG ERQLPEKAKA KEKSSAGFAP GSYDGGTGEM
RDAHGDGDYV RHHVRRLTGE SSGDEDRPLE MGVGKMTPAV QKGDMPLQDA RSGAVEDRGR
SVGGLRRKRR LAPSMRITMP SNEELPAEET VARRRRDPSL GSLPSEEDLL DRRMNGLAGG
LMGIGEGAQT P
//
