ID V2YHS3_MONRO Unreviewed; 448 AA.
AC V2YHS3;
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=Histidine acid {ECO:0000313|EMBL:ESK91239.1};
GN ORFNames=Moror_2868 {ECO:0000313|EMBL:ESK91239.1};
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:ESK91239.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK91239.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK91239.1,
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 -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000256|ARBA:ARBA00005375}.
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:ESK91239.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AWSO01000361; ESK91239.1; -; Genomic_DNA.
DR RefSeq; XP_007849435.1; XM_007851244.1.
DR AlphaFoldDB; V2YHS3; -.
DR KEGG; mrr:Moror_2868; -.
DR HOGENOM; CLU_023111_2_1_1; -.
DR OrthoDB; 2315929at2759; -.
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; IPR000560; His_Pase_clade-2.
DR InterPro; IPR029033; His_PPase_superfam.
DR PANTHER; PTHR11567:SF142; -; 1.
DR PANTHER; PTHR11567; ACID PHOSPHATASE-RELATED; 1.
DR Pfam; PF00328; His_Phos_2; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE 3: Inferred from homology;
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 402..425
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 448 AA; 48655 MW; 29B223F5C56E96B0 CRC64;
MSDDSKVLGV LVLARHGDRQ GFYQNPSDYT PTNTQITPLG NVQEFRLGQY LRERYFNSLS
PTFISGVNST IANLNQVKVR ADAGGEGGVI ANSAMSLLQG LFPANANYTT TLANGTTIEG
PLNGYQSYLV ESVEPDNDIS LEGWTKCGTF DQATKAFYQS AEFKQKADES ASFLSQLPRY
LDGRPVSLEN MWNIFDFINV ENIHDSDFHN NIPATFVAQA RDLANWHEYG VFSDKELSGI
GNIPFRTMIP SVVESLQSIA DESDPLKFVH VAISYKPFIS LFNMTGVAQA HPELAGIVNY
AASVALEVRQ PSSGGDPVLR FNFKNGTDDV TYKTYSFFNA SGDVPLSTFV NYLNPAAINT
TAQWCTECNN SKDRGCGALA LAASQAQGQA HRQRISPVGA GFLGAGLTLF VAAAMLAVLF
FLGLLTFGKK GRKAQSVHSD DHSVEKAA
//
