ID A0A0L9VB02_PHAAN Unreviewed; 539 AA.
AC A0A0L9VB02;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Serine/threonine-protein phosphatase 5 {ECO:0000256|ARBA:ARBA00020001};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=HKW66_Vig0181780 {ECO:0000313|EMBL:KAG2394444.1},
GN LR48_Vigan09g090400 {ECO:0000313|EMBL:KOM52245.1};
OS Phaseolus angularis (Azuki bean) (Vigna angularis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3914 {ECO:0000313|EMBL:KOM52245.1, ECO:0000313|Proteomes:UP000053144};
RN [1] {ECO:0000313|Proteomes:UP000053144}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Jingnong 6 {ECO:0000313|Proteomes:UP000053144};
RX PubMed=26460024; DOI=10.1073/pnas.1420949112;
RA Yang K., Tian Z., Chen C., Luo L., Zhao B., Wang Z., Yu L., Li Y., Sun Y.,
RA Li W., Chen Y., Li Y., Zhang Y., Ai D., Zhao J., Shang C., Ma Y., Wu B.,
RA Wang M., Gao L., Sun D., Zhang P., Guo F., Wang W., Li Y., Wang J.,
RA Varshney R.K., Wang J., Ling H.Q., Wan P.;
RT "Genome sequencing of adzuki bean (Vigna angularis) provides insight into
RT high starch and low fat accumulation and domestication.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13213-13218(2015).
RN [2] {ECO:0000313|EMBL:KOM52245.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Seedling {ECO:0000313|EMBL:KOM52245.1};
RA Chooi Y.-H.;
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAG2394444.1, ECO:0000313|Proteomes:UP000743370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Leaf {ECO:0000313|EMBL:KAG2394444.1};
RA Xiang H.;
RT "Vigna angularis (adzuki bean) Var. LongXiaoDou No. 4 denovo assembly.";
RL Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-5 (PP-T)
CC subfamily. {ECO:0000256|ARBA:ARBA00008786}.
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DR EMBL; JABFOF010000006; KAG2394444.1; -; Genomic_DNA.
DR EMBL; CM003379; KOM52245.1; -; Genomic_DNA.
DR RefSeq; XP_017436737.1; XM_017581248.1.
DR RefSeq; XP_017436738.1; XM_017581249.1.
DR RefSeq; XP_017436739.1; XM_017581250.1.
DR AlphaFoldDB; A0A0L9VB02; -.
DR STRING; 3914.A0A0L9VB02; -.
DR EnsemblPlants; KOM52245; KOM52245; LR48_Vigan09g090400.
DR GeneID; 108343155; -.
DR Gramene; KOM52245; KOM52245; LR48_Vigan09g090400.
DR KEGG; var:108343155; -.
DR OMA; NHFFMSR; -.
DR OrthoDB; 1107740at2759; -.
DR Proteomes; UP000053144; Chromosome 9.
DR Proteomes; UP000743370; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR CDD; cd07417; MPP_PP5_C; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR041753; PP5_C.
DR InterPro; IPR013235; PPP_dom.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR45668; SERINE/THREONINE-PROTEIN PHOSPHATASE 5-RELATED; 1.
DR PANTHER; PTHR45668:SF5; SERINE_THREONINE-PROTEIN PHOSPHATASE 5; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF08321; PPP5; 1.
DR Pfam; PF00515; TPR_1; 1.
DR Pfam; PF13432; TPR_16; 1.
DR PIRSF; PIRSF033096; PPPtase_5; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50005; TPR; 3.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000053144};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW ProRule:PRU00339}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 166..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 189..206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 11..44
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 45..78
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 79..112
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 245..521
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|SMART:SM00156"
SQ SEQUENCE 539 AA; 60384 MW; 503FA9607EFFE079 CRC64;
METEKSNISK AEELKTLANE AFNARKYSQA IDLYTQAIEL NGGNAVYYSN RAFAHLRLEE
YGSAIQDASK AIEVDPKYSK GYYRRGAAYI GLGKFKEALK DFQQVKKMCP NDPDATKKLK
ECEKAVMKLK FEEAIAAPES ERRSIAESID FHTIGKGRNS SVPTEVAIAA VVAVMAAAVM
LFRTSKTTIV IAIVVGLLLL LGAYWWSGHN TDVEPQYSGA RIEGDVVTLD FVKKMMEDFK
NQKFLHKRYA FQIVLQTREI LQSLPSLVDI HVPNGKRFTV CGDVHGQFYD LLNIFELNGL
PSEENPYLFN GDFVDRGSFS LEVILTLFAF KCLSPSAIYL ARGNHESKSM NKIYGFEGEV
RSKLNDTFVE LFAEVFCFLP LAHVINEKVF VVHGGLFSVD GVKLSDIRSI NRFCEPPEEG
LMCEILWSDP QPLPGRGPSK RGVGLSFGPD VTEQFLQENN LDLVVRSHEV KDEGYEIEHD
GKLITVFSAP NYCDQMGNKG AFIRFEAPDL KPNIVTFSAV SHPDVKPMAY ANNFLRMFS
//
