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Database: UniProt/TrEMBL
Entry: H8X295_CANO9
LinkDB: H8X295_CANO9
Original site: H8X295_CANO9 
ID   H8X295_CANO9            Unreviewed;       675 AA.
AC   H8X295;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   SubName: Full=Lro1 protein {ECO:0000313|EMBL:CCG22817.1};
GN   ORFNames=CORT_0B11180 {ECO:0000313|EMBL:CCG22817.1};
OS   Candida orthopsilosis (strain 90-125) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=1136231 {ECO:0000313|EMBL:CCG22817.1, ECO:0000313|Proteomes:UP000005018};
RN   [1] {ECO:0000313|EMBL:CCG22817.1, ECO:0000313|Proteomes:UP000005018}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=90-125 {ECO:0000313|Proteomes:UP000005018};
RX   PubMed=22563396; DOI=10.1371/journal.pone.0035750;
RA   Riccombeni A., Vidanes G., Proux-Wera E., Wolfe K.H., Butler G.;
RT   "Sequence and analysis of the genome of the pathogenic yeast Candida
RT   orthopsilosis.";
RL   PLoS ONE 7:e35750-e35750(2012).
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DR   EMBL; HE681720; CCG22817.1; -; Genomic_DNA.
DR   RefSeq; XP_003868251.1; XM_003868203.1.
DR   AlphaFoldDB; H8X295; -.
DR   GeneID; 14539161; -.
DR   KEGG; cot:CORT_0B11180; -.
DR   eggNOG; KOG2369; Eukaryota.
DR   HOGENOM; CLU_016065_1_0_1; -.
DR   OrthoDB; 589269at2759; -.
DR   Proteomes; UP000005018; Chromosome 2.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008374; F:O-acyltransferase activity; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR003386; LACT/PDAT_acylTrfase.
DR   PANTHER; PTHR11440:SF97; BCDNA.GH02384; 1.
DR   PANTHER; PTHR11440; LECITHIN-CHOLESTEROL ACYLTRANSFERASE-RELATED; 1.
DR   Pfam; PF02450; LCAT; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        84..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..76
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   675 AA;  75430 MW;  6FB145F7CBA5104F CRC64;
     MSTHRKRKLS HEKEASRAND AHAQSTAINN NNLGSDGEDG VQEIDLTNDD DSKKHRRSSV
     GHHHHKKHHQ DTKSRKKIRE SRRFVFILGI IFGLVVTVFF STNKANFPTD LDQLVNLNFD
     NLNSLFEDWK GWKDVLPSGI QSYLQDAEGG DDSLHGSAES FSVGLRLRAA KNYTAKYNVV
     MVPGVISTGL ESWGTTTSGD CPSIGYFRKR LWGSFFMLRT MILDKTCWLK NIMLDTETGL
     DPPNVKVRAA QGFEAADFFV AGYWIWNKIL QNLAVIGYSP DNMLSASYDW RLTYIDLEKR
     DGYFSKLQKQ IEMTKKVGGE KSILVGHSMG SQVIFYFLKW VEAKGEYFGN GGPNWVNEYI
     EAVVDISGSS LGTPKAIPAL ISGEMKDTVQ LNALAVYGLE QFFSRRERVD MLRTFGGVAS
     MFPKGGDLIW GNLTNAPDDP INTLETNDTT RELGGPKNGS FGTFIKYTGK DGEERDVTIN
     ESLEQLLDEA PSWYSKRVRD NYSHGVAKTK KELDANNQIQ SKWVNPLEAA LPNAPDLKYY
     CFYGVGNPTE RAYKYVPADK SVKLDYVIDS ESSDGVMLGD GDGTVSLLTH TMCHEWQKGN
     KSRYNPGNVN VTIVEIKHEP DRFDLRGGAK TAEHVDILGS AELNELVLTV ASGNGGAIKD
     RYVSNLRQIV ERLDI
//
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