ID A0A2V5IZM7_9EURO Unreviewed; 439 AA.
AC A0A2V5IZM7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 9.
DE SubName: Full=PAP2-domain-containing protein {ECO:0000313|EMBL:PYI34610.1};
GN ORFNames=BP00DRAFT_56728 {ECO:0000313|EMBL:PYI34610.1};
OS Aspergillus indologenus CBS 114.80.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450541 {ECO:0000313|EMBL:PYI34610.1, ECO:0000313|Proteomes:UP000248817};
RN [1] {ECO:0000313|EMBL:PYI34610.1, ECO:0000313|Proteomes:UP000248817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114.80 {ECO:0000313|EMBL:PYI34610.1,
RC ECO:0000313|Proteomes:UP000248817};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; KZ825475; PYI34610.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V5IZM7; -.
DR Proteomes; UP000248817; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR CDD; cd03386; PAP2_Aur1_like; 1.
DR Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR InterPro; IPR026841; Aur1/Ipt1.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR PANTHER; PTHR31310; -; 1.
DR PANTHER; PTHR31310:SF11; INOSITOL PHOSPHORYLCERAMIDE SYNTHASE CATALYTIC SUBUNIT AUR1; 1.
DR Pfam; PF14378; PAP2_3; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 77..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 127..144
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 185..207
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 214..233
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 330..348
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 212..349
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
SQ SEQUENCE 439 AA; 49400 MW; 1A58629B4A5DD9E1 CRC64;
MNSSLPSWKD RTQNQFGKLQ IQVPWRSIQL LVPHRMRRKI RSKLRSRLSP TSSISTLQTS
FSPVDTLRSL QSHRWTLYDF QYLLLLIIGI FSLSMMGAPG PLAKTAVFTL LLISLLLPIT
RQFFLPFLPI AGWLIFFYAC QFIPSDWRPA IWVRVLPALE NILYGANISN ILSAHQNVVL
DVLAWIPYGL CHYGAPFVCS LIMFIFGPPG TVPLFARTFG YISMTAVTIQ LFFPCSPPWY
ENLYGLAPAD YSMPGNPAGL ARIDKLLGID LYTSGFRQSP VVFGAFPSLH AADSTLAALF
MSHVFPRLKP LFVTYTLWMW WATMYLSHHY AVDLVGGGLL ATVAFYFAKT RFLPRVQSDK
TYRWDYDYIE IGDSARAYGY DLASFDGDFN LDSDEWTVGS SSSVSSGSLS PVDDHYTWEG
ESLASPVTDI EAGRHVISP
//
