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Database: UniProt
Entry: E2BIZ4_HARSA
LinkDB: E2BIZ4_HARSA
Original site: E2BIZ4_HARSA 
ID   E2BIZ4_HARSA            Unreviewed;       243 AA.
AC   E2BIZ4;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   ORFNames=EAI_13832 {ECO:0000313|EMBL:EFN84339.1};
OS   Harpegnathos saltator (Jerdon's jumping ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Ponerinae; Ponerini; Harpegnathos.
OX   NCBI_TaxID=610380 {ECO:0000313|Proteomes:UP000008237};
RN   [1] {ECO:0000313|EMBL:EFN84339.1, ECO:0000313|Proteomes:UP000008237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R22 G/1 {ECO:0000313|EMBL:EFN84339.1,
RC   ECO:0000313|Proteomes:UP000008237};
RX   PubMed=20798317; DOI=10.1126/science.1192428;
RA   Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA   Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA   Wang J., Liebig J.;
RT   "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT   saltator.";
RL   Science 329:1068-1071(2010).
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   -!- SIMILARITY: Belongs to the dullard family.
CC       {ECO:0000256|ARBA:ARBA00038346}.
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DR   EMBL; GL448543; EFN84339.1; -; Genomic_DNA.
DR   RefSeq; XP_011139706.1; XM_011141404.2.
DR   AlphaFoldDB; E2BIZ4; -.
DR   STRING; 610380.E2BIZ4; -.
DR   EnsemblMetazoa; XM_011141404.3; XP_011139706.1; LOC105183355.
DR   GeneID; 105183355; -.
DR   KEGG; hst:105183355; -.
DR   InParanoid; E2BIZ4; -.
DR   OMA; RIWGFFM; -.
DR   OrthoDB; 5473812at2759; -.
DR   PhylomeDB; E2BIZ4; -.
DR   Proteomes; UP000008237; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR   CDD; cd07521; HAD_FCP1-like; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR011948; Dullard_phosphatase.
DR   InterPro; IPR004274; FCP1_dom.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   NCBIfam; TIGR02251; HIF-SF_euk; 1.
DR   PANTHER; PTHR12210:SF70; CTD NUCLEAR ENVELOPE PHOSPHATASE 1; 1.
DR   PANTHER; PTHR12210; DULLARD PROTEIN PHOSPHATASE; 1.
DR   Pfam; PF03031; NIF; 1.
DR   SMART; SM00577; CPDc; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   PROSITE; PS50969; FCP1; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000008237}.
FT   DOMAIN          56..223
FT                   /note="FCP1 homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50969"
SQ   SEQUENCE   243 AA;  28018 MW;  6BE26CE7EBE56C92 CRC64;
     MLKQLQMGMR AFLLMASRVW TCICFLLKKQ VRTVSQMQPV KYEIFPLSPL SRHRLSIVKR
     KVLVLDLDET LIHSHHDGVA RPTVRPGTPP DFVLKVTIDR HPVRFFVHKR PHVDFFLDIV
     SQWYELVVFT ASMEIYGAAV ADKLDNNRGI LRRRYYRQHC TPEMGSYTKD LSAICSDLSS
     VFILDNSPGA YRAYPDNAIP IKSWFSDAGD TALLSLLPVL DALRFTQDVR SVLSRNLHLH
     HTW
//
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