ID V2X205_MONRO Unreviewed; 222 AA.
AC V2X205;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Vacuolar protein sorting-associated protein 29 {ECO:0000256|ARBA:ARBA00017767, ECO:0000256|RuleBase:RU362040};
GN ORFNames=Moror_15130 {ECO:0000313|EMBL:ESK86801.1};
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:ESK86801.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK86801.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK86801.1,
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 VPS29 family.
CC {ECO:0000256|ARBA:ARBA00005945, ECO:0000256|RuleBase:RU362040}.
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:ESK86801.1}.
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DR EMBL; AWSO01000883; ESK86801.1; -; Genomic_DNA.
DR RefSeq; XP_007853890.1; XM_007855699.1.
DR AlphaFoldDB; V2X205; -.
DR STRING; 1381753.V2X205; -.
DR KEGG; mrr:Moror_15130; -.
DR HOGENOM; CLU_063749_0_1_1; -.
DR OrthoDB; 5481532at2759; -.
DR Proteomes; UP000017559; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0030904; C:retromer complex; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IEA:InterPro.
DR CDD; cd07394; MPP_Vps29; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR024654; Calcineurin-like_PHP_lpxH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR020935; PdiEstase_YfcE_CS.
DR InterPro; IPR000979; Phosphodiesterase_MJ0936/Vps29.
DR InterPro; IPR028661; Vps29.
DR NCBIfam; TIGR00040; yfcE; 1.
DR PANTHER; PTHR11124:SF12; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 29; 1.
DR PANTHER; PTHR11124; VACUOLAR SORTING PROTEIN VPS29; 1.
DR Pfam; PF12850; Metallophos_2; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS01269; UPF0025; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 4..158
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF12850"
FT REGION 187..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 222 AA; 23731 MW; CBA6F8095C814EAF CRC64;
MVLVLLIGDL HIPHRTHDLP TKFKKLLVPG KIQQILCTGN VCDKETYEYL RTISPDVGVV
RGDYDETPTY PSSLTVLHNP IKIGVIHGHQ CVPIGDLDAL SAIARQMDVD VLVSGHTHGV
QAIEYDNKFF VNPGSATGAW TGLVNGDITP SFALMDIQGP VVVTYVYQLV EGEVRVEKVE
YRKELETGGG VPRSTVLPQS IPSPTPGSPQ GAAVGAGGGG GW
//
