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Database: UniProt
Entry: A0A158NC83_ATTCE
LinkDB: A0A158NC83_ATTCE
Original site: A0A158NC83_ATTCE 
ID   A0A158NC83_ATTCE        Unreviewed;       376 AA.
AC   A0A158NC83;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=PPM-type phosphatase domain-containing protein {ECO:0000259|PROSITE:PS51746};
GN   Name=105618209 {ECO:0000313|EnsemblMetazoa:XP_012055141.1};
OS   Atta cephalotes (Leafcutter ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Atta.
OX   NCBI_TaxID=12957 {ECO:0000313|EnsemblMetazoa:XP_012055141.1, ECO:0000313|Proteomes:UP000005205};
RN   [1] {ECO:0000313|Proteomes:UP000005205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21347285; DOI=10.1371/journal.pgen.1002007;
RA   Suen G., Teiling C., Li L., Holt C., Abouheif E., Bornberg-Bauer E.,
RA   Bouffard P., Caldera E.J., Cash E., Cavanaugh A., Denas O., Elhaik E.,
RA   Fave M.J., Gadau J., Gibson J.D., Graur D., Grubbs K.J., Hagen D.E.,
RA   Harkins T.T., Helmkampf M., Hu H., Johnson B.R., Kim J., Marsh S.E.,
RA   Moeller J.A., Munoz-Torres M.C., Murphy M.C., Naughton M.C., Nigam S.,
RA   Overson R., Rajakumar R., Reese J.T., Scott J.J., Smith C.R., Tao S.,
RA   Tsutsui N.D., Viljakainen L., Wissler L., Yandell M.D., Zimmer F.,
RA   Taylor J., Slater S.C., Clifton S.W., Warren W.C., Elsik C.G., Smith C.D.,
RA   Weinstock G.M., Gerardo N.M., Currie C.R.;
RT   "The genome sequence of the leaf-cutter ant Atta cephalotes reveals
RT   insights into its obligate symbiotic lifestyle.";
RL   PLoS Genet. 7:e1002007-e1002007(2011).
RN   [2] {ECO:0000313|EnsemblMetazoa:XP_012055141.1}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (APR-2016) to UniProtKB.
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   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|ARBA:ARBA00004514}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor
CC       {ECO:0000256|ARBA:ARBA00004635}.
CC   -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000256|ARBA:ARBA00006702,
CC       ECO:0000256|RuleBase:RU003465}.
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DR   EMBL; ADTU01011738; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADTU01011739; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_012055141.1; XM_012199751.1.
DR   AlphaFoldDB; A0A158NC83; -.
DR   STRING; 12957.A0A158NC83; -.
DR   EnsemblMetazoa; XM_012199751.1; XP_012055141.1; LOC105618209.
DR   GeneID; 105618209; -.
DR   KEGG; acep:105618209; -.
DR   eggNOG; KOG0697; Eukaryota.
DR   InParanoid; A0A158NC83; -.
DR   OMA; QDNRVNG; -.
DR   OrthoDB; 11028at2759; -.
DR   Proteomes; UP000005205; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro.
DR   CDD; cd00143; PP2Cc; 1.
DR   Gene3D; 1.10.10.430; Phosphatase 2C, C-terminal domain suprefamily; 1.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   InterPro; IPR015655; PP2C.
DR   InterPro; IPR000222; PP2C_BS.
DR   InterPro; IPR012911; PP2C_C.
DR   InterPro; IPR036580; PP2C_C_sf.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   PANTHER; PTHR47992:SF267; ALPHABET, ISOFORM E; 1.
DR   PANTHER; PTHR47992; PROTEIN PHOSPHATASE; 1.
DR   Pfam; PF00481; PP2C; 1.
DR   Pfam; PF07830; PP2C_C; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   SUPFAM; SSF81601; Protein serine/threonine phosphatase 2C, C-terminal domain; 1.
DR   PROSITE; PS01032; PPM_1; 1.
DR   PROSITE; PS51746; PPM_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003465};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Myristate {ECO:0000256|ARBA:ARBA00022707};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912,
KW   ECO:0000256|RuleBase:RU003465};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005205}.
FT   DOMAIN          23..284
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
SQ   SEQUENCE   376 AA;  41720 MW;  F4BDF7E88324594D CRC64;
     MGAFLDTPNT EKCNEHGTGN GLRYGVASMQ GWRMEMEDAH RAIPCLDGGL SDWSYFAVFD
     GHAGALVSAH SAEHLLECIM QTQEFKAEDV IKGIHSGFLR LDDEMRDLPA MSAGMDKSGS
     TAVCAFISPK NIYIANCGDS RAVLCRSGLP VFSTRDHKPV LPAEKERIQN AGGSVMIQRV
     NGSLAVSRAL GDYEYKNLKD RGPCEQLVSP EPEIFMLDRD DEHDEFLVLA CDGIWDVMNN
     EDLCNFIHSR LQLTDDLEAV TNLVVDTCLY KGSRDNMSIV LVTFPAAPKP NPEAQRQEAE
     LEMAIARKIK EIVAQEEDKS EFDYLKMLEL LRGSDHFPYL PPGGGLHAKQ PFIEKMFREM
     CPSKAHSVSV GYIPLT
//
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