ID A0A397GFM1_9EURO Unreviewed; 740 AA.
AC A0A397GFM1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=DUF676 domain-containing protein {ECO:0000259|Pfam:PF05057};
GN ORFNames=CDV56_100409 {ECO:0000313|EMBL:RHZ49822.1};
OS Aspergillus thermomutatus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=41047 {ECO:0000313|EMBL:RHZ49822.1, ECO:0000313|Proteomes:UP000215305};
RN [1] {ECO:0000313|EMBL:RHZ49822.1, ECO:0000313|Proteomes:UP000215305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 39 {ECO:0000313|EMBL:RHZ49822.1,
RC ECO:0000313|Proteomes:UP000215305};
RA Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA Perkins V., De Repentigny L., Dufresne S.F.;
RT "Draft genome sequence of azole-resistant Aspergillus thermomutatus
RT (Neosartorya pseudofischeri) strain HMR AF 39, isolated from a human nasal
RT aspirate.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the putative lipase ROG1 family.
CC {ECO:0000256|ARBA:ARBA00007920}.
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:RHZ49822.1}.
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DR EMBL; NKHU02000171; RHZ49822.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397GFM1; -.
DR VEuPathDB; FungiDB:CDV56_100409; -.
DR OrthoDB; 70376at2759; -.
DR Proteomes; UP000215305; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR007751; DUF676_lipase-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR48182; PROTEIN SERAC1; 1.
DR PANTHER; PTHR48182:SF2; PROTEIN SERAC1; 1.
DR Pfam; PF05057; DUF676; 1.
DR Pfam; PF13374; TPR_10; 1.
DR Pfam; PF13424; TPR_12; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF48452; TPR-like; 2.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000215305};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 25..168
FT /note="DUF676"
FT /evidence="ECO:0000259|Pfam:PF05057"
FT REGION 290..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..309
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 740 AA; 82362 MW; 219F783848ED6CCC CRC64;
METENEFPFL QEVYTPPSQP KIDFVFVHGL NPRGRNDHPY ETWRHQNGTF WPRDYLPQDI
PHARVFVYGY NSNVTNPQTM STAGVKDHAN TLLNLLDLER SPQLNTRPPK IVFIGHSLGG
LVIKQALLNA HEDPKYTAIR LATCGLVFFG TPHRGAKGVE VGKIAAKVAR FVSKGHASNE
LLDCLEYNSL FTRQMSSRFS HQLEDYRVVS FVEGKEVLLG GAGPASVSHL VVDEESAVLG
LPGNRETRLK LDADHSQMCK VGSRGPMYKL IKGNIKQIVD QVLVAEQGYI PQPSTSPHPG
PPLPPRMHTN SSSPYPNAAP QTNTPRVVGT MYAAVDSDPR SIQAAEHKNA GRWDQARNLE
YAIFQEHLRT LGPDHNSTIV AGYHLAEIDL EASYLAKATE WCKWVSDQSQ RTLGPRHPLT
LRAESLMGEI LCARGRYQES ESVCANVLAR QQMSIGDDDL DTLETRRRLS MAYSNLGQEQ
NAMSIAEKRH EALQRILGPQ HIRVLSSALD TIEVLITART SNGDKILEMR FSGEIAQTTS
QTGQIARELN DLLGPRHPLS IRALRLQGIL EMLAQNSTVA SETLRRALAT AEETLGPDHT
ESMALVATIG IMYTLHSDRG NYIAFVMPGS SNNKLEMAAP WLTRYLSWAE TRKGKDSGDV
QSMLDMLANL HFARQQYAEA HKYYDRLVES YQAAGMPVPQ LVATNLQTCR MHTMLLTQYS
PRGTGSAIEG ILNSFVKKRF
//