ID A0A2S7R1U8_9HELO Unreviewed; 424 AA.
AC A0A2S7R1U8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 28-JUN-2023, entry version 17.
DE RecName: Full=EH domain-containing protein {ECO:0000259|PROSITE:PS50031};
GN ORFNames=CJF32_00009642 {ECO:0000313|EMBL:PQE32758.1};
OS Rutstroemia sp. NJR-2017a WRK4.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Rutstroemiaceae; Rutstroemia.
OX NCBI_TaxID=2070412 {ECO:0000313|EMBL:PQE32758.1, ECO:0000313|Proteomes:UP000238813};
RN [1] {ECO:0000313|EMBL:PQE32758.1, ECO:0000313|Proteomes:UP000238813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJR-2017a WRK4 {ECO:0000313|EMBL:PQE32758.1,
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 -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000256|ARBA:ARBA00008655}.
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:PQE32758.1}.
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DR EMBL; NJPR01000022; PQE32758.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S7R1U8; -.
DR STRING; 2070412.A0A2S7R1U8; -.
DR InParanoid; A0A2S7R1U8; -.
DR OrthoDB; 2906776at2759; -.
DR Proteomes; UP000238813; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd07990; LPLAT_LCLAT1-like; 1.
DR InterPro; IPR032098; Acyltransf_C.
DR InterPro; IPR000261; EH_dom.
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; PF16076; Acyltransf_C; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR PROSITE; PS50031; EH; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000238813};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 393..414
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 372..424
FT /note="EH"
FT /evidence="ECO:0000259|PROSITE:PS50031"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 424 AA; 48946 MW; 8680A7D04E4F00B6 CRC64;
MSEPELKQRT TTRSRNMPAP VPDFGGGTKE KAVGEHPSGE VKHGYAAQIW RLLSFATYFW
ACCCTIQATQ ILGVPMYFIN KDIYYAWMAL TKQSFGLLVT TMTQWWSPTV VRISGDASVA
GQLRKTEDGR LECDFPERVV LIANHQLYTD WLYLWWVAYT NTPPTHGHIY IIAKESLKWV
PIIGWGMRFY GFIFMSRKME KDRPRMEHRL KQLRERHSGP LSGTPGLDPM WLLLFPEGTN
ASDNGRIKSA KWAEKIGVKD MEHVLLPRST GSFFCLNQLK GSVEYVYDCT MAYEGVPRGK
FGQDYFTLTS SYIEGRPPKS VNLYWRRFRI ADIPLDNAEE FDLWLREKWY EKDALMEQYM
TTGRFPPNAA SDKGAHEHEF IETEVKQKNW SDFLNIFVVL ATAGLIANLF AKVWNWALYG
NMKA
//
