ID A0A118K100_CYNCS Unreviewed; 465 AA.
AC A0A118K100;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=Ccrd_020196 {ECO:0000313|EMBL:KVI01531.1};
OS Cynara cardunculus var. scolymus (Globe artichoke) (Cynara scolymus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Carduoideae; Cardueae;
OC Carduinae; Cynara.
OX NCBI_TaxID=59895 {ECO:0000313|EMBL:KVI01531.1, ECO:0000313|Proteomes:UP000243975};
RN [1] {ECO:0000313|EMBL:KVI01531.1, ECO:0000313|Proteomes:UP000243975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2C {ECO:0000313|EMBL:KVI01531.1};
RX PubMed=26786968; DOI=10.1038/srep19427;
RA Scaglione D., Reyes-Chin-Wo S., Acquadro A., Froenicke L., Portis E.,
RA Beitel C., Tirone M., Mauro R., Lo Monaco A., Mauromicale G., Faccioli P.,
RA Cattivelli L., Rieseberg L., Michelmore R., Lanteri S.;
RT "The genome sequence of the outbreeding globe artichoke constructed de novo
RT incorporating a phase-aware low-pass sequencing strategy of F1 progeny.";
RL Sci. Rep. 6:19427-19427(2016).
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.
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:KVI01531.1}.
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DR EMBL; LEKV01003054; KVI01531.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A118K100; -.
DR STRING; 59895.A0A118K100; -.
DR EnsemblPlants; KVI01531; KVI01531; Ccrd_020196.
DR Gramene; KVI01531; KVI01531; Ccrd_020196.
DR OMA; MMEDKTL; -.
DR Proteomes; UP000243975; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR000222; PP2C_BS.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR PANTHER; PTHR47992; PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR47992:SF160; PROTEIN PHOSPHATASE 2C 77; 1.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR PROSITE; PS01032; PPM_1; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003465};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912,
KW ECO:0000256|RuleBase:RU003465};
KW Reference proteome {ECO:0000313|Proteomes:UP000243975}.
FT DOMAIN 160..455
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
SQ SEQUENCE 465 AA; 50842 MW; 99AD2A6C17C5BFB2 CRC64;
MEEMLPAVIV PLSLGNSICK TLILEETLVI ITGIQQTMAD KTSFFQNHPQ DSNYENDGNW
VASDSALQES EDELMSLEGD RIFDSSCTLS VVSDSSSLCG EDFIAFESIT SEIGTLGSQD
AEKNATVTGF EDVTTKIVIS EKVSSGTVAR SVFEIDCVPL WGFTSICGRR PEMEDAVATV
PRFLKVPIQM LTGDHDSDRL TMTKSLSHLT THFFGVYDGH GGSQEELEPL MDGDGSGISK
DNIVQDLWKK AFMNCFLKVD DEIGGKQANV EPVAPETVGS TAVVALICSS HIIVSNCGDS
RAVLCRGKEA MALSVDHKPN REDEYARIEA AGGKVIQWNG HRVFGVLAMS RSIGDRYLKP
WIIPDPEVTF IPRAKEDECL ILASDGLWDV MSNEEVCEIA RKRILVWHKK NGISSLPQER
GEGIDLAAQA AAESLSNRAL QKGSKDNITV IVIDLKAQRK FKTKT
//