ID A0A091TV62_PHALP Unreviewed; 1350 AA.
AC A0A091TV62;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=N335_04064 {ECO:0000313|EMBL:KFQ82284.1};
OS Phaethon lepturus (White-tailed tropicbird).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Eurypygimorphae; Phaethontiformes;
OC Phaethontidae; Phaethon.
OX NCBI_TaxID=97097 {ECO:0000313|EMBL:KFQ82284.1, ECO:0000313|Proteomes:UP000053638};
RN [1] {ECO:0000313|EMBL:KFQ82284.1, ECO:0000313|Proteomes:UP000053638}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N335 {ECO:0000313|EMBL:KFQ82284.1};
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}.
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DR EMBL; KK466719; KFQ82284.1; -; Genomic_DNA.
DR PhylomeDB; A0A091TV62; -.
DR Proteomes; UP000053638; 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:UP000053638}.
FT DOMAIN 215..270
FT /note="DEK-C"
FT /evidence="ECO:0000259|PROSITE:PS51998"
FT DOMAIN 274..415
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 339..393
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 458..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..613
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..689
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..755
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..807
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..887
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ82284.1"
FT NON_TER 1350
FT /evidence="ECO:0000313|EMBL:KFQ82284.1"
SQ SEQUENCE 1350 AA; 149732 MW; 0C590D1F572F3862 CRC64;
PCSISESFLT VKGAALFLPR GNGSSTPRIS HRRNKHAGDL QQHLQAMFIL LRPEDNIRLA
VRLESTYQNR TRYMVVVSTN GRQDTEESIV LGMDFSSNDS STCTMGLVLP LWSDTLIHLD
GDGGFSVSTD NRVHIFKPVS VQAMWSALQS LHKACEVARS NNYYPGSLFL TWVSYYESHI
NSDQSSVNEW NAMQDVQSHR PDSPALFTDV PTERERTERL IKTKLREIMM QKDLENITSK
EIRTELEMQM VCNLREFKEF IDNEMIVILG QMDSPTQIFD HVFLGSEWNA SNLEDLQNRG
VRYILNVTRE IDNFFPGLFE YHNIRVYDEE ATDLLAYWND TYKFISKAKK NGSKCLVHCK
MGVSRSASTV IAYAMKEYGW NLDRAYDYVK ERRTVTKPNP SFMRQLEEYQ GILLASKQRH
NKLWRSHSDS DLSDHHEPIC KSGLELNKKE ITTSADQISE AKTNDNQQPM SPIYSAEPDR
EQQLPEDANM IEEMCVKERR IHVEFTCRDF HAEQMEDKLN LNNINGCTAG CCVDSVPPDN
CRASEALMQL QHPLEITEFP DLTVDDLEKD ALKPDMNVHL VPMEEFTSCL KDFPQSPNQN
SPSLQQNPQP EVTELSTDRI DFFSALEKFV ELSQESRSRA CSHSRTEEQG SGRNGVSRVP
VLEVPPAADG CADARRNSSG NSPQASDDSS TDEEQQKEVP ELPSAGHLTR SHSENAISVK
EIITEIESIN QGAGPAQQKE SSANLTQTPK GNTVHDLPLK QSEGACAGHQ EKEKDPLQAE
QEAVPSLQPS SGKSDLEESS PGGEQQEPRG SINAEPKWCP GSVRRATLEF EERLRQEQEH
QHVSPVCILP TRKNSRNDSP AAELLLRGKS EEPPLELAPE GDKARGLGAE ELLLPPRAEL
PAGRHLPGPF ASPAPESLPA EPSPGQEGAA PEHRTVVSFD GTEEPSLPSL LPKRIEIIEY
TPMVKPAECP DTSCEQGGLA AAIPPLDENL NPSLCSEKAP TCPRALTLVN LSLPEHAVHK
QPTFTVGSPS EEGGGLSFRL CAASPSAQVT SMPSASLDRS SYPYVIHLEG VTEQSTGTDD
EPVMPYGTEG DLTPLFRDSP KPLCRGGAGT LRQPRGEDFT SQRAENMDLL DISFLCYGLP
HSSSSHSVEE RSSSPGLVKQ RAKEIEARIR HAGLTTPSHM KRSASLAKLD CLDLCKDDLS
ERELASSDAN PVLLTCIALG QSFCGGRLER GSESVCGKHR LSSPEPAKHF VEQLRTAECI
AQSKPVERPL AQYAKECGSS QQSLFSSADP TWTSSEEGPP LLQVQVLDSL SPAQGLVVAP
RQQHGRTHPL RRLKKTNDKK RTTNPLYNTM
//
