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Database: UniProt
Entry: A0A2P5WF46_GOSBA
LinkDB: A0A2P5WF46_GOSBA
Original site: A0A2P5WF46_GOSBA 
ID   A0A2P5WF46_GOSBA        Unreviewed;       394 AA.
AC   A0A2P5WF46;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, 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=GOBAR_AA30984 {ECO:0000313|EMBL:PPR89707.1};
OS   Gossypium barbadense (Sea-island cotton) (Egyptian cotton).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=3634 {ECO:0000313|EMBL:PPR89707.1, ECO:0000313|Proteomes:UP000239757};
RN   [1] {ECO:0000313|EMBL:PPR89707.1, ECO:0000313|Proteomes:UP000239757}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Xinhai21 {ECO:0000313|Proteomes:UP000239757};
RC   TISSUE=Leaf {ECO:0000313|EMBL:PPR89707.1};
RA   Chen X., Liu X., Zhao B., Zheng H., Hu Y., Lu G., Yang C., Chen J.,
RA   Shan C., Zhang L., Zhou Y., Wang L., Guo W., Bai Y., Ruan J., Shangguan X.,
RA   Mao Y., Jiang J., Zhu Y., Lei J., Kang H., Chen S., He X., Wang R.,
RA   Wang Y., Chen J., Wang L., Yu S., Wang B., Wei J., Song S., Lu X., Gao Z.,
RA   Gu W., Deng X., Ma D., Wang S., Liang W., Fang L., Cai C., Zhu X., Zhou B.,
RA   Zhang Y., Chen Z., Xu S., Zhu R., Wang S., Zhang T., Zhao G.;
RT   "Genome of allotetraploid Gossypium barbadense reveals genomic plasticity
RT   and fiber elongation in cotton evolution.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; KZ667856; PPR89707.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P5WF46; -.
DR   Proteomes; UP000239757; 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:SF86; PROTEIN-SERINE_THREONINE PHOSPHATASE; 1.
DR   Pfam; PF00481; PP2C; 1.
DR   SMART; SM00331; PP2C_SIG; 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:UP000239757}.
FT   DOMAIN          138..390
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          38..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..64
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..92
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   394 AA;  42173 MW;  007E25230B13ECF5 CRC64;
     MSCSVAVSNS PAFSPSSSLF LNKTPIISPS TEALNLTLTH LKTSSSPASP SPSPSSPFRL
     RLPKPPPVSL LSSSSASNSS PSSGSGSAPG LGSGPVSTVL KRKRPARLEI PVVTEAMGLG
     IPATPCEVGK ELEREGDGYS VYCKRGRREA MEDRFSASVE LQGDSKKAIF GIFDGHGGAK
     AAEFAAQKLE KNILDQVITR RDNTAVMDAV KQGYLKTDAE FFKEDNAGGT CCLTALIQNG
     DLVVSNAGDC RAVLSRGGRA EPLTSDHRPS REDERSRIQN LGGYVDLCRG VWRIQSSLAV
     SRGIGDRHLK QWVIAEPETK IVSIEPDCEF LILASDGLWD KVSDQEAVDI ARPSFIGTDK
     PNLLFACKKL VDLSVSRGSF DDISVMLVHL GYYI
//
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