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Database: UniProt
Entry: A0A163HHY7_DIDRA
LinkDB: A0A163HHY7_DIDRA
Original site: A0A163HHY7_DIDRA 
ID   A0A163HHY7_DIDRA        Unreviewed;       711 AA.
AC   A0A163HHY7;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Transferase {ECO:0000313|EMBL:KZM25297.1};
GN   ORFNames=EKO05_0000609 {ECO:0000313|EMBL:UPX09932.1}, EKO05_000608
GN   {ECO:0000313|EMBL:KAF9712878.1}, ST47_g3533
GN   {ECO:0000313|EMBL:KZM25297.1};
OS   Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS   rabiei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX   NCBI_TaxID=5454 {ECO:0000313|EMBL:KZM25297.1, ECO:0000313|Proteomes:UP000076837};
RN   [1] {ECO:0000313|EMBL:KZM25297.1, ECO:0000313|Proteomes:UP000076837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ArDII {ECO:0000313|EMBL:KZM25297.1,
RC   ECO:0000313|Proteomes:UP000076837};
RX   PubMed=27091329; DOI=10.1038/srep24638;
RA   Verma S., Gazara R.K., Nizam S., Parween S., Chattopadhyay D., Verma P.K.;
RT   "Draft genome sequencing and secretome analysis of fungal phytopathogen
RT   Ascochyta rabiei provides insight into the necrotrophic effector
RT   repertoire.";
RL   Sci. Rep. 6:24638-24638(2016).
RN   [2] {ECO:0000313|EMBL:KAF9712878.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Me14 {ECO:0000313|EMBL:KAF9712878.1};
RA   Syme R.A., Farfan-Caceres L., Lichtenzveig J.;
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KAF9712878.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Me14 {ECO:0000313|EMBL:KAF9712878.1};
RX   PubMed=32345704; DOI=10.1534/g3.120.401265;
RA   Shah R.M., Williams A.H., Hane J.K., Lawrence J.A., Farfan-Caceres L.M.,
RA   Debler J.W., Oliver R.P., Lee R.C.;
RT   "Reference Genome Assembly for Australian Ascochyta rabiei Isolate
RT   ArME14.";
RL   G3 (Bethesda) 10:2131-2140(2020).
RN   [4] {ECO:0000313|EMBL:KAF9712878.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Me14 {ECO:0000313|EMBL:KAF9712878.1};
RA   Shah R.M., Williams A.H., Hane J.K., Lawrence J.A., Farfan-Caceres L.M.,
RA   Debler J.W., Oliver R.P., Lee R.C.;
RL   Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:UPX09932.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Me14 {ECO:0000313|EMBL:UPX09932.1};
RA   Mobegi F.M., Debler J.W.D., Lee R.C.L.;
RL   Submitted (MAR-2022) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC       acyltransferase family. {ECO:0000256|ARBA:ARBA00008655}.
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DR   EMBL; RYYQ01000002; KAF9712878.1; -; Genomic_DNA.
DR   EMBL; JYNV01000129; KZM25297.1; -; Genomic_DNA.
DR   EMBL; CP095288; UPX09932.1; -; Genomic_DNA.
DR   STRING; 5454.A0A163HHY7; -.
DR   OrthoDB; 2906776at2759; -.
DR   Proteomes; UP000076837; Unassembled WGS sequence.
DR   Proteomes; UP000617380; Chromosome 1.
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; 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.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076837};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KZM25297.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        42..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          129..251
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
FT   REGION          491..577
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          638..711
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        502..525
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   711 AA;  77481 MW;  0F65960F2AC12831 CRC64;
     MSPAIKKKKD DLGAGLRVSK DNIAAHPAGP PKYGELTQAE RAFTLASTFL SGVLAISASQ
     FLGAPLKLID PQFYEGYMAY TKECFAILIT CLTQWWAPTV VRVSGDSSMV GQLIQKKDGS
     LQCNFADRMV LMANHQLYTD WLYIWWIAYT NNMHGFIYII LKESLRNIPI IGWSAQFYNF
     IFLARNWEED QRRFKKALAR LNSATQPMWL IIFPEGTNLS ATTREKSKAW AAKNNLQDMK
     HQLLPRSTGL RFCLNELKDT TEWLYDCTIA YEGVPPGQFG QDIFTLRSTF FEGRPPKSVN
     MHWRRFHIND IPIQNTKAFE VWLRNRWREK DYMLEYFQKH SRFPAENFWK DHLDMGDRSS
     QGSQSIRSVP RPAVQIETEV KSGNWNEFVK IFAPISSVMM ALTVAYGANP ADIIPGGKEF
     FEQHMKTLLG GGGEMGGLPS PDQLEKMIEG AAKLGAAQAA DPQQVPQIAA LTQENLAKLV
     KETAIKSGAV MPGGMRRAST ALPQAPTRTL ATPTAVPTRA RSAVVTPSSA RKPAGATTKP
     KPATSGPAKP KAAPIKPKAA AKPKPTPPTG PMKEITLASG VSIKVPAPAV EDAKKTGATT
     IKTANGLILQ IGKKDVEKAQ EKKGDTIMTA SGIPIKVTSS GEIEVAKKPA SAKSSPAPKP
     AAKKPAATPA KAPSKLNGTA SAPKKLATPG PTKFAAKSST SQAKVPAKLA K
//
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