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Database: UniProt
Entry: A0A433D4U0_9FUNG
LinkDB: A0A433D4U0_9FUNG
Original site: A0A433D4U0_9FUNG 
ID   A0A433D4U0_9FUNG        Unreviewed;      2135 AA.
AC   A0A433D4U0;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   22-FEB-2023, entry version 10.
DE   SubName: Full=Lecithin:cholesterol acyltransferase-domain-containing protein {ECO:0000313|EMBL:RUP45845.1};
GN   ORFNames=BC936DRAFT_147669 {ECO:0000313|EMBL:RUP45845.1};
OS   Jimgerdemannia flammicorona.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Endogonomycetes; Endogonales; Endogonaceae; Jimgerdemannia.
OX   NCBI_TaxID=994334 {ECO:0000313|EMBL:RUP45845.1, ECO:0000313|Proteomes:UP000268093};
RN   [1] {ECO:0000313|EMBL:RUP45845.1, ECO:0000313|Proteomes:UP000268093}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GMNB39 {ECO:0000313|EMBL:RUP45845.1,
RC   ECO:0000313|Proteomes:UP000268093};
RX   PubMed=30485448;
RA   Chang Y., Desiro A., Na H., Sandor L., Lipzen A., Clum A., Barry K.,
RA   Grigoriev I.V., Martin F.M., Stajich J.E., Smith M.E., Bonito G.,
RA   Spatafora J.W.;
RT   "Phylogenomics of Endogonaceae and evolution of mycorrhizas within
RT   Mucoromycota.";
RL   New Phytol. 0:0-0(2018).
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:RUP45845.1}.
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DR   EMBL; RBNI01006700; RUP45845.1; -; Genomic_DNA.
DR   Proteomes; UP000268093; Unassembled WGS sequence.
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   Acyltransferase {ECO:0000313|EMBL:RUP45845.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000268093};
KW   Transferase {ECO:0000313|EMBL:RUP45845.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        74..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2052..2073
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          749..919
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          967..1018
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1141..1236
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1250..1407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1423..1469
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1518..1615
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1628..1719
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1752..1819
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1917..1942
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..45
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        749..871
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        890..919
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        972..1007
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1155..1170
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1198..1215
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1319..1342
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1563..1599
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1771..1807
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1917..1932
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2135 AA;  235928 MW;  1F298A5686BE9273 CRC64;
     MPTRRAKKSR APAPAPATAA TTATSFSTTI LTNRSNPSAS QRDANAGPEP LSPEDILSDS
     RIFEPARPFY KSRIFHFVFG VLAGVFIALS LYMAPPSARL QLEEFQHYIA LSFAELDLPT
     LLPQSLLVEE FMANLTNLLK PPPGSDGQPF QPALQLKEEL GLEPHFPVML IPGIVSSGLE
     SWSTSDCSAK IGWRARFHRG TLAKSCRMKM TLIVRQNYAA MFRAVLTDKE CWVKHLKLDP
     VTGLDPPGIK LRASQGLDAA DYFVPGYWIW GKIIENLAVV GYDSNNMHLA AYDWRLSFDN
     LEHRDHYFSR LKQDIEHSRQ WKGLKSVIIA HSMGSLVFYY FLKWVESPLG GNAGPNWTED
     HIESFINIAG PMMGVPKGLT ALLSGETRDT MDLGSYGAYI LEKFFSKNER ADLFRSWAGG
     SSMLPKGGEH IWGNLSWAPD DRHPHCRDVS YGNLLSFPSE VNYDVVDDPA LGREGTRDQA
     TIIRNHTALT GIELLHQSTS PEYHELLKNN YSFGITMSKK EIEKNEMDPR KWTNTVESRL
     PLAPSMRVYC FYGVGVETER SYFYTRSELE NGEVKLVCRA SEDEGEICER LNETNAMNLA
     HDEGESPKRP GEFTFPPKVY IDGRVHDPDS KINTGVHFGE GDGTVPLLSN GYMCASGWTT
     HADLYNPARS PIITREYLHE ASASALDIRG GNRASDHVNI LGNHEMTVCG LGADILKIVC
     NRPDGVDERY HSDMKEYGDR VNAMTSRRRA LSYGHNNPKT TRNLDDSQDT STPTPTNNHR
     PHSKPTISTP PHSSPRRASQ PTDLDLIPSR QTPSSLRSSP ASSTASLQNT LPSSLDSGPT
     SSDDRLSSKP HSARTSRALT STHQKQAKEN VNGAGWHTPE AGTGVARRQS VGGRRSNGSV
     TDLAGPQVGG STTLSPPQQE RIRAFDREKI GLAGKGFGSL LDEDRQEETI GELLGKISND
     DILKLTQLTK PHYPKPKSQS PATITSTSRK DGSPSKSNPN LATTTDDDSI PYDPDFHPSQ
     NTLALSRKFK NSLSQKYAYI FDTIARGEPY NPLQALRDRA VRAADSFAAD PLYASVYPQD
     ETRPSSHRQV RHTASGVLLG RRRKVSEWLV TTDEMEEDEA WRKANPQKEI LTLRASNPRA
     LLAASSSTSS QKQRVPRRSL EEDDRSSLEE LPRIQIQGSS SGVNIPPEMM VVLPQPPASP
     LSFQSFESEA SGGISSGGVD SPPRSPRPPN SHLVQPRPVR AQGLNFKLSH SASVSPVSSP
     SPSPPPSPKL DPRTGDGRFG ATNPLSRLVG LVSERENHSA LDVSTKERYE EEEEDENEVA
     HLPAQKEKRK TWHIPLFKKD KSSLLKKQHH RHTSLPHVNR LLEEDEPQTP TAPQEDARHS
     PGPQQIPPDG GEKMPRSESA SSSQNLSASD RIAATLGISL THDASSQSLP PPPRASNSLT
     TATAHGSRRR SSTTSVSLRP DLRSRTTSPV LRTLGDVAER PLFLGMDGTH PAPSQFAAME
     RDDASIIALP PTRRHSFDHT QRVETPVSAA ATEEAKKKGG RKKPYFLKVP GGDGTSASEE
     SAEDVTFRSD VEERESGGEK EKKNMWGFWK KEKSDVESDN SSSNRAGHGG PFSLEKRSSV
     EFFRGKFVPS GRSSFDDETR PSLSEIGARA SELAADGVEP STPRQSQIKK LQSHESGFLP
     GAAVVLPDEG PRDPGGTAGD ERELSRSQSP TQEIVEPVRR RVVQVDLEAV SSEVVGLVEK
     YRKLEGRVVQ VGKRRGRRRK GRGGFEDGED QGVSAETDDD EAETETETET ETEDDGDREE
     GDLDKDDEED ERAGKGNVVE VDASDADDIG FTKYVYFDDS LIHLHVSMLG ESDKDYKSKH
     GEMKGVLERF TTQIDLAEKA LTESEHFLTK HQDIMDDLCL NDLDEMGNWV ISRPETQQVY
     TSSPELSPPS SPHDVTTPRP DLYLPDKRAP SILLSTPYGR LNSFEYTLEE TELGVGALKT
     DIDLLERNVS DTQTLLQDMA KEMRITLDKF EDMTLEISEE YYHHLKLLED DVAAINAKRA
     QNPWLDAGYA TLSYVLTSIL PHLVIAFVFW FAVQLIKAGR AIAIFPRTLW TAYSEYLEDR
     KKTAMAVEAA AVPIPPRTLT SPRATTTVNG GRILE
//
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