ID A0A177CUA0_9PLEO Unreviewed; 496 AA.
AC A0A177CUA0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Acid phosphatase/Vanadium-dependent haloperoxidase {ECO:0000313|EMBL:OAG10460.1};
GN ORFNames=CC84DRAFT_484908 {ECO:0000313|EMBL:OAG10460.1};
OS Paraphaeosphaeria sporulosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC Paraphaeosphaeria.
OX NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG10460.1, ECO:0000313|Proteomes:UP000077069};
RN [1] {ECO:0000313|EMBL:OAG10460.1, ECO:0000313|Proteomes:UP000077069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG10460.1,
RC ECO:0000313|Proteomes:UP000077069};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000256|ARBA:ARBA00008816}.
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DR EMBL; KV441549; OAG10460.1; -; Genomic_DNA.
DR RefSeq; XP_018040825.1; XM_018186461.1.
DR AlphaFoldDB; A0A177CUA0; -.
DR STRING; 1460663.A0A177CUA0; -.
DR GeneID; 28769947; -.
DR InParanoid; A0A177CUA0; -.
DR OrthoDB; 25293at2759; -.
DR Proteomes; UP000077069; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
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:SF35; RE23632P; 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 Oxidoreductase {ECO:0000313|EMBL:OAG10460.1};
KW Peroxidase {ECO:0000313|EMBL:OAG10460.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077069};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 74..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 129..150
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 208..226
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 238..259
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 131..283
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
FT REGION 316..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 496 AA; 54846 MW; CD88A33CC296BA06 CRC64;
MDQWNTNKLP ERLPFSKKRL PKRVIFSYIL DYVVIFVLLA VFMLVDKIEP FHQPFALENW
TLHYPYAKHE RVTVTMAAVF AIGFPIVIIT FYTMVIDGIF SHQTPMPAGR GGLKRLTGRY
RLKDRLWELN CGLLGLMLSV GAAFTITGAL KNAIGKPRPD IVDRCQVKEE VWKAFHDNYP
RVVMATVADC MQSDNYILQD GFKSFPSAHS SVSFGGLFYL SIYLAAKLHV LDSKGEVWKS
FIVLVPTLGA ALIAGSRIMD ARHHPFDVLS GSLMGILVAW GSYRQYFPPV SETWRKGRAY
PIRAWGKGPA MPPPTAVIAD DIQPLRPVRS ATDEERGTSS AIPGADGHSG NVFRQQISQS
QRRREEEFGG IQPSDTMSST YSSKVAGYQG QLPASNPFTE ASRRRQDNYE YSSSEDDDNI
ELQPSYSLSG RPLAGQRGAN YDPVAGRLTD TGYHPPQGIT PTPTPPPVRT TGDIAEARGG
PAPPPAHAVG TTTQQV
//
