ID A0A165LRT7_9APHY Unreviewed; 220 AA.
AC A0A165LRT7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Vacuolar protein sorting-associated protein 29 {ECO:0000256|ARBA:ARBA00017767, ECO:0000256|RuleBase:RU362040};
GN ORFNames=DAEQUDRAFT_741072 {ECO:0000313|EMBL:KZT64774.1};
OS Daedalea quercina L-15889.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Daedalea.
OX NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT64774.1, ECO:0000313|Proteomes:UP000076727};
RN [1] {ECO:0000313|EMBL:KZT64774.1, ECO:0000313|Proteomes:UP000076727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-15889 {ECO:0000313|EMBL:KZT64774.1,
RC ECO:0000313|Proteomes:UP000076727};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the VPS29 family.
CC {ECO:0000256|ARBA:ARBA00005945, ECO:0000256|RuleBase:RU362040}.
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DR EMBL; KV429119; KZT64774.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165LRT7; -.
DR STRING; 1314783.A0A165LRT7; -.
DR OrthoDB; 5481532at2759; -.
DR Proteomes; UP000076727; 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:UP000076727};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 4..163
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF12850"
FT REGION 196..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 220 AA; 24403 MW; 83A0A9999C21918E CRC64;
MVLVLVIGDL HIPHRVHDLP AKFKKLLVPG KIQQILCTGN VCDRETYEYL RSVAPDVHVV
RGDYDESNFP LSVTVTHSPI RIGVIHGHQC IPTGDLDSLS ALARQLDVDV LISGHTHTFQ
AVEYDSRFFV NPGSATGAWI GSVHGPTDER RSDPTPTFAL MDIQGPVVVT YVYQLVEGEV
RVEKIEYRKD TEAFKEAPRS TVMPQSIPSS PAPPQQQSVW
//
