ID V2XEQ2_MONRO Unreviewed; 624 AA.
AC V2XEQ2;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Acid phosphatase {ECO:0000313|EMBL:ESK92182.1};
GN ORFNames=Moror_4714 {ECO:0000313|EMBL:ESK92182.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK92182.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK92182.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK92182.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
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:ESK92182.1}.
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DR EMBL; AWSO01000299; ESK92182.1; -; Genomic_DNA.
DR RefSeq; XP_007848452.1; XM_007850261.1.
DR AlphaFoldDB; V2XEQ2; -.
DR KEGG; mrr:Moror_4714; -.
DR HOGENOM; CLU_020880_2_2_1; -.
DR OrthoDB; 2721627at2759; -.
DR Proteomes; UP000017559; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd07061; HP_HAP_like; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR InterPro; IPR033379; Acid_Pase_AS.
DR InterPro; IPR000560; His_Pase_clade-2.
DR InterPro; IPR029033; His_PPase_superfam.
DR PANTHER; PTHR20963; MULTIPLE INOSITOL POLYPHOSPHATE PHOSPHATASE-RELATED; 1.
DR PANTHER; PTHR20963:SF42; PUTATIVE-RELATED; 1.
DR Pfam; PF00328; His_Phos_2; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 49..70
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 23..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 624 AA; 69117 MW; 5E1462E27E5A1DC5 CRC64;
MSDIRGVVDA EREALLPTHI KQEQDDVDHV PLQPSPPSSS RITRRSFSLL HLTGAFAGGI
LACIVAQYAV CGQTCISPSN ISQNQNPDSA AALASPWAGS TEVHDFPPTS PTNAFPSLFP
TDVGYAGGTP TGAEAAVIAT APAYPLHTGA AQLVVPESLG GHGHKHSKFD LFKSWGNLSP
WYSVGNGAFG INSGPETPDT CRVTGLHFLH RHGARYPTAW ASYGGPANFS SRLHNVADQW
TTSGELEFMN DWTYKLGEEL LTPFGRQQLY DLGISMRLKY GFLLKNFTES NTVPVFRTES
QDRMLHSALN FAIGFFGYPF EGQYQQSITI EAANFNNTLA PYDTCPNANR RTVSDRGTWY
ASRWADKYLA SARKRLQKQI TGFELSVQDV FTMQQLCAYE TVAIGYSKFC ELFTEDEWEG
FDYALDLAFW YNSAFGSPVA RVQGAGWIQE MLHRLENRPV TEETNKFSMN FTLDGDTRTF
PVDQSLYVDA THEVVVLNII TALNLTSFAE DGPLPYDHIP KKRKFKVSQL APFATNIQFQ
LLSCTSRDGP QIRIIINDGV VPLTGIEGCP KNKDGMCPVD TFIKAQKKLL DKVDWDWACH
GNWEDKVGQG PEWETVTGDP PEKD
//
