ID A0A091RYA9_MERNU Unreviewed; 839 AA.
AC A0A091RYA9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 08-NOV-2023, entry version 34.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
DE Flags: Fragment;
GN ORFNames=N331_08520 {ECO:0000313|EMBL:KFQ33352.1};
OS Merops nubicus (Northern carmine bee-eater).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Coraciiformes; Meropidae; Merops.
OX NCBI_TaxID=57421 {ECO:0000313|EMBL:KFQ33352.1, ECO:0000313|Proteomes:UP000052967};
RN [1] {ECO:0000313|EMBL:KFQ33352.1, ECO:0000313|Proteomes:UP000052967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N331 {ECO:0000313|EMBL:KFQ33352.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 protein-tyrosine phosphatase family.
CC {ECO:0000256|ARBA:ARBA00009580}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KK711090; KFQ33352.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091RYA9; -.
DR Proteomes; UP000052967; Unassembled WGS sequence.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; IEA:InterPro.
DR CDD; cd14569; DSP_slingshot_2; 1.
DR CDD; cd11652; SSH-N; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR InterPro; IPR014876; DEK_C.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR043587; Phosphatase_SSH-like.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR043588; SSH-N.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR45864:SF3; PROTEIN PHOSPHATASE SLINGSHOT HOMOLOG 2; 1.
DR PANTHER; PTHR45864; SLINGSHOT PROTEIN PHOSPHATASE HOMOLOG; 1.
DR Pfam; PF08766; DEK_C; 1.
DR Pfam; PF00782; DSPc; 1.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR PROSITE; PS51998; DEK_C; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000052967}.
FT DOMAIN 213..268
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT DOMAIN 272..413
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 337..391
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 587..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..611
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..750
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..811
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ33352.1"
FT NON_TER 839
FT /evidence="ECO:0000313|EMBL:KFQ33352.1"
SQ SEQUENCE 839 AA; 94647 MW; 6E68B7ED7AEA55F4 CRC64;
SISESFLTVK GAALFLPRGN GSSTPRISHR RNKHAGDLQQ HLQAMFILLR PEDNIRLAVR
LESTYQNRTR YMVVVSTNGR QDTEESIVLG MDFSSNDSST CTMGLVLPLW SDTLIHLDGD
GGFSVSTDNR VHIFKPVSVQ AMWSALQSLH KACEVARSNN YYPGSLFLTW VSYYESHINS
DQSSVNEWNA MQDVQSHRPD SPALFTDVPT ERERTERLIK TKLREIMMQK DLENITSKEI
RTELEMQMVC NLREFKEFID NEMIVILGQM DSPTQIFDHV FLGSEWNASN LEDLQNRGVR
YILNVTREID NFFPGLFEYH NIRVYDEEAT DLLAYWNDTY KFISKAKKNG SKCLVHCKMG
VSRSASTVIA YAMKEYGWNL DRAYDYVKER RTVTKPNPSF MRQLEEYQGI LLASKQRHNK
LWRSHSDSDL SDHHEPICKT GLELNKKEIT TSADQISEAK TNDNQQPMSP IYSAELEREQ
QLPEDAGTIE EMCVKEGIHL EFTCRDFHAE QMEDKLNLNN INGYTAGCCV DSVPPDNCHA
SEALMQLQHP LEISEFPDLT VDDLEKDALK PDMNVHLVPM EEFTSCLKDF PQSPNQNSPS
LQQNPQPEVT DLSSDRIDFF SALEKFVELS QESRPRTCSH SRAEEQGSGR NGVSRVPVLE
VLPAADGAAD AQRNSSANSP QASDDSSTEE EQQKEVPELP STACLTRSHS ENAISVKEII
TEIESINQGA GPAQQKEGST SLTQTPKRNT VHDLPVEAIW ASERAEQSEG ACAGHQEKDP
LQAEQEAAPA LQLSSGRSDL EESSPGGEQQ EPRGTINPEP KWCPGSVRRA TLEFEERLR
//
