ID M7SZ00_EUTLA Unreviewed; 327 AA.
AC M7SZ00;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Putative pap2 superfamily protein {ECO:0000313|EMBL:EMR69768.1};
GN ORFNames=UCREL1_3197 {ECO:0000313|EMBL:EMR69768.1};
OS Eutypa lata (strain UCR-EL1) (Grapevine dieback disease fungus) (Eutypa
OS armeniacae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Diatrypaceae; Eutypa.
OX NCBI_TaxID=1287681 {ECO:0000313|EMBL:EMR69768.1, ECO:0000313|Proteomes:UP000012174};
RN [1] {ECO:0000313|Proteomes:UP000012174}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-EL1 {ECO:0000313|Proteomes:UP000012174};
RX PubMed=23723393; DOI=10.1128/genomeA.00228-13;
RA Blanco-Ulate B., Rolshausen P.E., Cantu D.;
RT "Draft genome sequence of the grapevine dieback fungus Eutypa lata UCR-
RT EL1.";
RL Genome Announc. 1:E0022813-E0022813(2013).
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000256|ARBA:ARBA00008816}.
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DR EMBL; KB706016; EMR69768.1; -; Genomic_DNA.
DR RefSeq; XP_007791129.1; XM_007792938.1.
DR AlphaFoldDB; M7SZ00; -.
DR STRING; 1287681.M7SZ00; -.
DR KEGG; ela:UCREL1_3197; -.
DR eggNOG; KOG3030; Eukaryota.
DR HOGENOM; CLU_021458_0_2_1; -.
DR OMA; IPNYDNV; -.
DR OrthoDB; 25293at2759; -.
DR Proteomes; UP000012174; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR CDD; cd03390; PAP2_containing_1_like; 1.
DR Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR InterPro; IPR043216; PA_PP_rel.
DR PANTHER; PTHR10165; LIPID PHOSPHATE PHOSPHATASE; 1.
DR PANTHER; PTHR10165:SF84; PHOSPHATIDIC ACID PHOSPHATASE BETA; 1.
DR Pfam; PF01569; PAP2; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000012174};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 45..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 81..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 157..176
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 188..210
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 216..237
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 82..234
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
FT REGION 281..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 327 AA; 36173 MW; 40130E524803939A CRC64;
MIILAVISAM IYRLRPAATR TFPLTVLATG EVVYPQFAYP YRPQILAPWL DAFVAAAVPI
AVILAANAVR VRSFWDTNNG IVGLVYALLA SSCFQVFIKW IVGGLRPHFY DVCKPDPSLF
NAVGLNHGVG YQNYMFTPEV CTGSQESVRN ALESFPSGHA TTIFAGMVYL YLYLNAKLKV
FSNYHPAMWK LLVLYMPILG ACLIAGTLTI DHSHNWYDII AGAVIGTVFA FSAYRMVYAA
IWDYRMNHIP LNRSSAFIWS EGCEGSDMVF TREVGWGAGS LHGDDRDRSP THNGNDTNGR
SKNKNGQEDA DPGRNVRNSN VHGAEMV
//
