ID A0A3L6QK35_PANMI Unreviewed; 1066 AA.
AC A0A3L6QK35;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=C2845_PM12G09650 {ECO:0000313|EMBL:RLM79786.1};
OS Panicum miliaceum (Proso millet) (Broomcorn millet).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Panicinae; Panicum.
OX NCBI_TaxID=4540 {ECO:0000313|EMBL:RLM79786.1, ECO:0000313|Proteomes:UP000275267};
RN [1] {ECO:0000313|Proteomes:UP000275267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30683860; DOI=10.1038/s41467-019-08409-5;
RA Zou C., Miki D., Li D., Tang Q., Xiao L., Rajput S., Deng P., Jia W.,
RA Huang R., Zhang M., Sun Y., Hu J., Fu X., Schnable P.S., Li F., Zhang H.,
RA Feng B., Zhu X., Liu R., Schnable J.C., Zhu J.-K., Zhang H.;
RT "The genome of broomcorn millet.";
RL Nat. Commun. 10:436-436(2019).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC Evidence={ECO:0000256|ARBA:ARBA00001512};
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|ARBA:ARBA00001482};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000256|ARBA:ARBA00006702,
CC ECO:0000256|RuleBase:RU003465}.
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:RLM79786.1}.
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DR EMBL; PQIB02000012; RLM79786.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L6QK35; -.
DR STRING; 4540.A0A3L6QK35; -.
DR Proteomes; UP000275267; Chromosome 12.
DR GO; GO:0005524; F:ATP binding; 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 GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00038; CAP_ED; 2.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000222; PP2C_BS.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR24353; CYCLIC NUCLEOTIDE-DEPENDENT PROTEIN KINASE; 1.
DR PANTHER; PTHR24353:SF127; PROTEIN PHOSPHATASE 2C AND CYCLIC NUCLEOTIDE-BINDING_KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00027; cNMP_binding; 2.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00100; cNMP; 2.
DR SMART; SM00332; PP2Cc; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 2.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 2.
DR PROSITE; PS01032; PPM_1; 1.
DR PROSITE; PS51746; PPM_2; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003465};
KW Kinase {ECO:0000313|EMBL:RLM79786.1};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912,
KW ECO:0000256|RuleBase:RU003465};
KW Reference proteome {ECO:0000313|Proteomes:UP000275267};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 116..406
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT DOMAIN 499..578
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 595..719
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 747..1009
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 36..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1044..1066
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..61
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1066 AA; 118466 MW; 1CA9DDC07C3081C1 CRC64;
MLLPVLFSSS FADLCCPSKC CSQLKCSLFS NVCLSQTPDS PRESREKSSR GRGKADSTGS
DDSSDDLGED DDALNQMNTT RESTVGISRL SRVSSQFLPP NGSRKVQVPL GNYDLRYSFL
SQRGYYPESL DKPNQDSYCI HTPFGTSPDD HFFGVFDGHG EYGAQCSQFV KRRLCENLLR
DNRFRTDAVM ALHAAFVATN SQLHADNLDD SMSGTTAITI LVRGKTIYVA NTGDSRAVIA
EKRGDDIVAV DLSIDQTPYR FDELERVKEC GARVLTLDQI EGLKNPDVQC WGTEESDDGD
PPRLWVQNGM YPGTAFTRSI GDSVAESIGV IADPEIFVLD LNSKNPFFVL ASDGVFEFLS
SQTVVDMISK YKDPRDACAE IVAESYRLWL QYETRTDDIT IIVVHINGLT DMESTQTVTK
VSLQPSHQVV GVAGSESPLI VTSNTNNQRS RHDLSRARLR ALESSLENGQ LWVPPSPSHR
KTWEEQVSYK SEKGYRALQG GEGDCFYVVG SGEYEVLAIQ EEDGKEITKV LHRYTADKLS
SFGELALMHN KPLQASVRAV TSGTLWALKR EDFRGILMSE FSNIPSLKLL RSVELFTRLT
VLQLSQLAES LVEVSFADGQ TIVDKNDDVS ALYVIQRGRV RLILAADQMN SDTWDLVSAQ
TKQAQSSQQN DNYVVEIDEG GHFGEWALIG ETISFTAIAV ADVTCSTIAK EKFDTIVGPL
PKLSQADART KESLVTKKNV ADDDFPFRRV ELYDLEWKMC IYAADCSEIG LVQIKGSDKI
RSLKRFYIKR VQDLHKEVQV FEEKKLMKSL NQSTCVPQVL CTCADQSYLG ILLNCCLCCS
LASILHTPLN ESSAKFFAAS VVIALEELHQ KSIIYRGVSA DILMLDRSGH LQLVDFRFAK
KMEGERTYTI CGIADSLAPE IVLGRGHGFP ADWWALGVLI YFMLQSDMPF GSWRESELEP
VTKIAKGHLV IPSTFSAEVV DLITKLLVVD ENVRLGTSGA EAVKKHPWFD GIDWEQVASG
TYAVPDEITE RINSCIETLN EDLTASPSVP IEDPDDHTAP EWIQDW
//
