ID A0A2S7R517_9HELO Unreviewed; 773 AA.
AC A0A2S7R517;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Putative CTR1 suppressor protein {ECO:0000313|EMBL:PQE33903.1};
GN ORFNames=CJF32_00002764 {ECO:0000313|EMBL:PQE33903.1};
OS Rutstroemia sp. NJR-2017a WRK4.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Rutstroemiaceae; Rutstroemia.
OX NCBI_TaxID=2070412 {ECO:0000313|EMBL:PQE33903.1, ECO:0000313|Proteomes:UP000238813};
RN [1] {ECO:0000313|EMBL:PQE33903.1, ECO:0000313|Proteomes:UP000238813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJR-2017a WRK4 {ECO:0000313|EMBL:PQE33903.1,
RC ECO:0000313|Proteomes:UP000238813};
RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
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:PQE33903.1}.
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DR EMBL; NJPR01000003; PQE33903.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S7R517; -.
DR STRING; 2070412.A0A2S7R517; -.
DR InParanoid; A0A2S7R517; -.
DR OrthoDB; 2728187at2759; -.
DR Proteomes; UP000238813; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR CDD; cd07992; LPLAT_AAK14816-like; 1.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR31605; GLYCEROL-3-PHOSPHATE O-ACYLTRANSFERASE 1; 1.
DR PANTHER; PTHR31605:SF0; GLYCEROL-3-PHOSPHATE O-ACYLTRANSFERASE 1; 1.
DR Pfam; PF01553; Acyltransferase; 2.
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:UP000238813};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 26..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 446..466
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 497..520
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 532..555
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 61..299
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REGION 621..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..678
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..710
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 773 AA; 85302 MW; F3D0138BCC9F29C7 CRC64;
MANEQQVHEH MPQKAKHKEE FPMTNWIYDV FLWTFSILVD LFFREVHPRG SWKVPRRGPV
IFVAAPHANQ FVDPLILMRT LRNECHRRVA FLIAAKSMGQ FIVGWFARKV GAVPVGRALD
MVKPGSGTIY LPDPVNDPLL VRGIGTKFDS GEIQVGGLLV LPKVEGTTPG NAEIAEVISA
EELRLKKPFK GHIALTQLTG RDDVDENGKF KNESVKGTKE GFEGTKYKAA PKVDQTQVYD
AVFDRLSQGG AVGIFPEGGS HDRTELLPLK AGVAIMALGS LAANPDSGLK IVPCGMNYFH
AHKFRSRAVV EFGNPLEIPK ELVELYKSGE RREAVSQLLD TVYQALVAVT VTSPDYDTLM
LIQAVRRLYN PTGKKLPLPM VVELNRRLVK GYTHYKDDPR IVALKKSVLD YNKQLRYMNL
RDHQIEYAKF SLPKVIVLLF YRLGKLAVLS IGVIPGLVLF APVFAASKII SIKKSRQALA
ASTVKLQGRD VMATWKLLVA LAFAPVLYNF YTIGLAIWTY RNRVQGHMPD WVPLWAVFVS
GYIIFPAITF AALRFGEVGM DIAKSLRPLI ISLNPASSNV IYKLRERRAQ LSAQVTEVIN
TLGPELFPDF DASRIVADPF NRDGIRTPTS PSQSGIRRRD SNQSGLSELD SPPTIRRSQT
AGASIGGGSA MNGTLPRNES FGNLGNIALF ATRPPSRSES RSSSSGGAVG SSGFPLKGFS
ALDSKASFDE VSMKIRGAMK ERGQMRRRKS EAEAARDGDD VALSSDEDDR KHV
//
