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Database: UniProt
Entry: K5WNB3_PHACS
LinkDB: K5WNB3_PHACS
Original site: K5WNB3_PHACS 
ID   K5WNB3_PHACS            Unreviewed;       418 AA.
AC   K5WNB3;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   22-FEB-2023, entry version 27.
DE   RecName: Full=Phospholipid/glycerol acyltransferase domain-containing protein {ECO:0000259|SMART:SM00563};
GN   ORFNames=PHACADRAFT_247149 {ECO:0000313|EMBL:EKM60925.1};
OS   Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus) (Peniophora
OS   carnosa).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Phanerochaetaceae; Phanerochaete.
OX   NCBI_TaxID=650164 {ECO:0000313|EMBL:EKM60925.1, ECO:0000313|Proteomes:UP000008370};
RN   [1] {ECO:0000313|EMBL:EKM60925.1, ECO:0000313|Proteomes:UP000008370}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM60925.1,
RC   ECO:0000313|Proteomes:UP000008370};
RX   PubMed=22937793; DOI=10.1186/1471-2164-13-444;
RA   Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
RA   Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
RA   LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
RA   Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
RA   Grigoriev I.V., Master E.R.;
RT   "Comparative genomics of the white-rot fungi, Phanerochaete carnosa and P.
RT   chrysosporium, to elucidate the genetic basis of the distinct wood types
RT   they colonize.";
RL   BMC Genomics 13:444-444(2012).
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DR   EMBL; JH930468; EKM60925.1; -; Genomic_DNA.
DR   RefSeq; XP_007390366.1; XM_007390304.1.
DR   AlphaFoldDB; K5WNB3; -.
DR   STRING; 650164.K5WNB3; -.
DR   GeneID; 18914006; -.
DR   KEGG; pco:PHACADRAFT_247149; -.
DR   HOGENOM; CLU_041844_3_1_1; -.
DR   InParanoid; K5WNB3; -.
DR   OrthoDB; 2906776at2759; -.
DR   Proteomes; UP000008370; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR   CDD; cd07990; LPLAT_LCLAT1-like; 1.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   PANTHER; PTHR10983; 1-ACYLGLYCEROL-3-PHOSPHATE ACYLTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR10983:SF16; LYSOCARDIOLIPIN ACYLTRANSFERASE 1; 1.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   SMART; SM00563; PlsC; 1.
DR   SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008370};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        26..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        398..415
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          128..254
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   418 AA;  47805 MW;  5859BD6B60B89E61 CRC64;
     MAAPTELHTL EISQRPRKTW AQTFNAVLFF LVFNLGCLMI SGFQFACLLP LRLLPFPEAQ
     KWYDEGIRYS KGACGTLLVL VTQLFAPASL VVSFERNGPG AFSREELDRL VVRDGSGRVT
     ALQLPPKAVW IANHQMYADW WYVWCLTYFA GSYKDVFIVL KKSLKWLPII GWGMQLYNFI
     FLSRSWASDR LHLAKSLSWL SAQAEKRDTP LTFVLYPEGT LVSKHTRPLS KKYADKMGFP
     DNRNMLLPRS TGLQYSLRAL SPRIRSLQLI DVTVAYPGIP PLGYGQSYYT LRSIFMDGVP
     PPQVHMHVRK FDVSRDVPIG DLSKVNPSKL PNVSGGPMKE SAETDVPQDE KDKFDKWLRE
     LWTAKDHDVD RYLDCGSFVN DPSLRVEIPI AIRRKREILD AFCFFIPALL GWIFSRLK
//
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