ID A0A168QKQ7_ABSGL Unreviewed; 475 AA.
AC A0A168QKQ7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN Name=ABSGL_10833.1 scaffold 12033 {ECO:0000313|EMBL:SAM04967.1};
OS Absidia glauca (Pin mould).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=4829 {ECO:0000313|EMBL:SAM04967.1};
RN [1] {ECO:0000313|EMBL:SAM04967.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAM04967.1};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-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}.
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DR EMBL; LT554417; SAM04967.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168QKQ7; -.
DR STRING; 4829.A0A168QKQ7; -.
DR InParanoid; A0A168QKQ7; -.
DR OMA; LYESNER; -.
DR OrthoDB; 19833at2759; -.
DR Proteomes; UP000078561; 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:UP000078561}.
FT DOMAIN 251..256
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS00125"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 44..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 475 AA; 52676 MW; BE8AE10A7044B167 CRC64;
MGNTSSRKRK DRPSVIRTEI PDNDYSNTTA TSINSILVNS SIQRNSVNSS NSRNGKGNSA
HQVPSAQQAF PNSQDTSPTH NRSPSSTMNT TKRDSGDLWP QANQQQAVDD QDSNQLTFTS
QNQLTATSMR SVGRNLDIDE CIDRLLDVGK SAKVSKSICF KNSEIVAICH AAQEVFVNQP
SLLELNPPVK ILGDIHGQYH DLIRLFEMGG FPPASNYLFL GDYVDRGKQS LETILLLFCY
KIKFPETFFL LRGNHESVYG FYDECKRRTN VKIWKTFVDV FNTLPIAALV AGKIFCVHGG
LSPSLNSMQD VRNIMRPTDV PEYGLLNDLL WSDPSDAVDL YESNERGVSV TFGKRVVNEF
LAKHDLDLVC RAHMVVEDGY EFFNDRTLVT VFSAPNYCGE FDNFGAIMSV NEELLCSFEL
LTPTDHPPPA TKLGSMNAPK ESHPVIMNTA ANGNGSKSSP PLVSSPQTTE LEQQV
//
