ID A0A1X2HLR9_SYNRA Unreviewed; 363 AA.
AC A0A1X2HLR9;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN ORFNames=BCR43DRAFT_433340 {ECO:0000313|EMBL:ORZ00323.1};
OS Syncephalastrum racemosum (Filamentous fungus).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Syncephalastraceae; Syncephalastrum.
OX NCBI_TaxID=13706 {ECO:0000313|EMBL:ORZ00323.1, ECO:0000313|Proteomes:UP000242180};
RN [1] {ECO:0000313|EMBL:ORZ00323.1, ECO:0000313|Proteomes:UP000242180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 2496 {ECO:0000313|EMBL:ORZ00323.1,
RC ECO:0000313|Proteomes:UP000242180};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC Evidence={ECO:0000256|RuleBase:RU004273};
CC -!- SIMILARITY: Belongs to the PPP phosphatase family.
CC {ECO:0000256|RuleBase:RU004273}.
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:ORZ00323.1}.
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DR EMBL; MCGN01000002; ORZ00323.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X2HLR9; -.
DR STRING; 13706.A0A1X2HLR9; -.
DR InParanoid; A0A1X2HLR9; -.
DR OMA; WADPNEN; -.
DR OrthoDB; 19833at2759; -.
DR Proteomes; UP000242180; Unassembled WGS sequence.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR InterPro; IPR031675; STPPase_N.
DR PANTHER; PTHR11668; SERINE/THREONINE PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR11668:SF484; SERINE_THREONINE-PROTEIN PHOSPHATASE PP-Z1-RELATED; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF16891; STPPase_N; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU004273};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000242180}.
FT DOMAIN 166..171
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS00125"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 363 AA; 41199 MW; A8312D236C723DA2 CRC64;
MGNIGSKKRK QRPSIIREEI PDNEYSNVTA TSLNSILQEA MEQNEQNEQS MSSQDLNQLS
VMSQNQLTTT SMRSIGSNLD IDECINRLME VGISGKIHRT VCFRNSEIIA ICKAAQELFL
SQPGGYPPES NYLFLGDYVD RGKQSLETIL LLFCYKIKYP ENFFLLRGNH ECANVTRVYG
FYDECKRRTN VKIWRTFVDT FNTLPIAGLV AGKIFCVHGG LSPSLNSLDD VRNIVRPTDV
PEYGLLNDIL WSDPTDNTDD WEDSERGVSY CFGKRVVNEF LSKFDLDLVC RAHMVVEDGY
EFFNERTLVT VFSAPNYCGE FDNFGAIMSI NEELLCSFEL LTPTDHPPAK LAALHKGKGR
RPR
//
