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Conserved domains on  [gi|1901933173|dbj|GGR87269|]
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protein-tyrosine-phosphatase [Deinococcus sedimenti]

Protein Classification

tyrosine-protein phosphatase( domain architecture ID 11457164)

tyrosine-protein phosphatase catalyzes the dephosphorylation of O-phosphotyrosine groups in phosphoproteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Oca4 COG2365
Protein tyrosine/serine phosphatase Oca4 [Signal transduction mechanisms];
23-227 8.47e-50

Protein tyrosine/serine phosphatase Oca4 [Signal transduction mechanisms];


:

Pssm-ID: 441932 [Multi-domain]  Cd Length: 248  Bit Score: 162.82  E-value: 8.47e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901933173  23 RSDTLSRLTPDGRRDLKALNFSRIIDLRSRTERAADPPPYLGHAAYLNLPLLPWRHRAFNEASAAARSNADHMSAML--- 99
Cdd:COG2365    29 RSGALSRLTDADLARLADLGIRTVIDLRSPAEVARAPDRLPPGVRYVHLPVLPDDAEALLEELRDGDLTPGDAEEFMlel 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901933173 100 ------DHAPNQIVTVLGAILDAPPGPVLIHCHAGKDRTGLIAALCSELAGQTRDQTADDYTASGPALRDFYR----DMQ 169
Cdd:COG2365   109 yrafvdPDAADAYRAAFRALADAENGPVLFHCTAGKDRTGVAAALLLLALGVPRETIMADYLLTNEYLAPLRArllaALR 188

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1901933173 170 ARRTPEQWAQLAPFAPTRADDIRHTLTHIDHHWGTLDAYLTAH-GLPNTDLTALRDRLT 227
Cdd:COG2365   189 AALGDEDPELLAPLLGVRPEYLEAALDAIDERYGSVDAYLEEGlGLTDAELEALRARLL 247
 
Name Accession Description Interval E-value
Oca4 COG2365
Protein tyrosine/serine phosphatase Oca4 [Signal transduction mechanisms];
23-227 8.47e-50

Protein tyrosine/serine phosphatase Oca4 [Signal transduction mechanisms];


Pssm-ID: 441932 [Multi-domain]  Cd Length: 248  Bit Score: 162.82  E-value: 8.47e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901933173  23 RSDTLSRLTPDGRRDLKALNFSRIIDLRSRTERAADPPPYLGHAAYLNLPLLPWRHRAFNEASAAARSNADHMSAML--- 99
Cdd:COG2365    29 RSGALSRLTDADLARLADLGIRTVIDLRSPAEVARAPDRLPPGVRYVHLPVLPDDAEALLEELRDGDLTPGDAEEFMlel 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901933173 100 ------DHAPNQIVTVLGAILDAPPGPVLIHCHAGKDRTGLIAALCSELAGQTRDQTADDYTASGPALRDFYR----DMQ 169
Cdd:COG2365   109 yrafvdPDAADAYRAAFRALADAENGPVLFHCTAGKDRTGVAAALLLLALGVPRETIMADYLLTNEYLAPLRArllaALR 188

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1901933173 170 ARRTPEQWAQLAPFAPTRADDIRHTLTHIDHHWGTLDAYLTAH-GLPNTDLTALRDRLT 227
Cdd:COG2365   189 AALGDEDPELLAPLLGVRPEYLEAALDAIDERYGSVDAYLEEGlGLTDAELEALRARLL 247
Y_phosphatase3 pfam13350
Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 ...
 10-227 2.13e-42

Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 families.


Pssm-ID: 463853 [Multi-domain]  Cd Length: 243  Bit Score: 143.54  E-value: 2.13e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901933173  10 GLLNFR-----RSLPG-------LSRSDTLSRLTPDGRRDLKALNFSRIIDLRSRTERAADPP-PylgHAAYLNLPLLPW 76
Cdd:pfam13350   5 GVFNFRdlggyPTADGrtvrwgrLYRSGNLSRLTDADLATLADLGIRTVIDLRSPAERAAPGPaP---DVRYVHLPVADS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901933173  77 RHRAFNEASAAARSNADHMSAM-------LDHAPNQIVTVLGAILDaPPGPVLIHCHAGKDRTGLIAALCSELAGQTRDQ 149
Cdd:pfam13350  82 EASSPELLARRALDPDDGEEFMaelyrdmVTSARAAYRALFEALAD-NDGPVLFHCTAGKDRTGVAAALLLSLLGVPEDT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901933173 150 TADDYTASGPALRDFYRDMQARRTPEQWAQLAPFAP---TRADDIRHTLTHIDHHWGTLDAYLTAH-GLPNTDLTALRDR 225
Cdd:pfam13350 161 IVADYLLTNEYLEPLRERLLAAFREELLDDAEGIRPllsVRPEYLEAALDAIDERYGSVEGYLRDGlGLSDEDIEALRAR 240


                  ..
gi 1901933173 226 LT 227
Cdd:pfam13350 241 LL 242
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 10-167 2.35e-26

bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa TpbA; This subfamily contains bacterial protein tyrosine phosphatases (PTPs) and dual-specificity phosphatases (DUSPs) related to Pseudomonas aeruginosa TpbA, a DUSP that negatively regulates biofilm formation by converting extracellular quorum sensing signals and to Mycobacterium tuberculosis PtpB, a PTP virulence factor that attenuates host immune defenses by interfering with signal transduction pathways in macrophages. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides, while DUSPs function as protein-serine/threonine phosphatases (EC 3.1.3.16) and PTPs.


Pssm-ID: 350378 [Multi-domain]  Cd Length: 158  Bit Score: 99.76  E-value: 2.35e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901933173  10 GLLNFRRSLPG-LSRSDTLSRltPDGRRDLKALNFSRIIDLRSRTERAADPPPYL--GHAAYLNLPLLPWRhrafneasa 86
Cdd:cd14529     2 GANNFRDVTPYvLYRSAQLSP--DEDRALLKKLGIKTVIDLRGADERAASEEAAAkiDGVKYVNLPLSATR--------- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901933173  87 aarsnadhmsamLDHAPNQIVTVLGAILDAPpGPVLIHCHAGKDRTGLIAALCSELAGQTRDQTADDYTASGPALRDFYR 166
Cdd:cd14529    71 ------------PTESDVQSFLLIMDLKLAP-GPVLIHCKHGKDRTGLVSALYRIVYGGSKEEANEDYRLSNRHLEGLRS 137


                  .
gi 1901933173 167 D 167
Cdd:cd14529   138 G 138
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
119-153 1.17e-03

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 37.34  E-value: 1.17e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1901933173  119 GPVLIHCHAGKDRTGLIAALCSELAGQTRDQTADD 153
Cdd:smart00404  40 GPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVD 74
 
Name Accession Description Interval E-value
Oca4 COG2365
Protein tyrosine/serine phosphatase Oca4 [Signal transduction mechanisms];
23-227 8.47e-50

Protein tyrosine/serine phosphatase Oca4 [Signal transduction mechanisms];


Pssm-ID: 441932 [Multi-domain]  Cd Length: 248  Bit Score: 162.82  E-value: 8.47e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901933173  23 RSDTLSRLTPDGRRDLKALNFSRIIDLRSRTERAADPPPYLGHAAYLNLPLLPWRHRAFNEASAAARSNADHMSAML--- 99
Cdd:COG2365    29 RSGALSRLTDADLARLADLGIRTVIDLRSPAEVARAPDRLPPGVRYVHLPVLPDDAEALLEELRDGDLTPGDAEEFMlel 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901933173 100 ------DHAPNQIVTVLGAILDAPPGPVLIHCHAGKDRTGLIAALCSELAGQTRDQTADDYTASGPALRDFYR----DMQ 169
Cdd:COG2365   109 yrafvdPDAADAYRAAFRALADAENGPVLFHCTAGKDRTGVAAALLLLALGVPRETIMADYLLTNEYLAPLRArllaALR 188

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1901933173 170 ARRTPEQWAQLAPFAPTRADDIRHTLTHIDHHWGTLDAYLTAH-GLPNTDLTALRDRLT 227
Cdd:COG2365   189 AALGDEDPELLAPLLGVRPEYLEAALDAIDERYGSVDAYLEEGlGLTDAELEALRARLL 247
Y_phosphatase3 pfam13350
Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 ...
 10-227 2.13e-42

Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 families.


Pssm-ID: 463853 [Multi-domain]  Cd Length: 243  Bit Score: 143.54  E-value: 2.13e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901933173  10 GLLNFR-----RSLPG-------LSRSDTLSRLTPDGRRDLKALNFSRIIDLRSRTERAADPP-PylgHAAYLNLPLLPW 76
Cdd:pfam13350   5 GVFNFRdlggyPTADGrtvrwgrLYRSGNLSRLTDADLATLADLGIRTVIDLRSPAERAAPGPaP---DVRYVHLPVADS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901933173  77 RHRAFNEASAAARSNADHMSAM-------LDHAPNQIVTVLGAILDaPPGPVLIHCHAGKDRTGLIAALCSELAGQTRDQ 149
Cdd:pfam13350  82 EASSPELLARRALDPDDGEEFMaelyrdmVTSARAAYRALFEALAD-NDGPVLFHCTAGKDRTGVAAALLLSLLGVPEDT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901933173 150 TADDYTASGPALRDFYRDMQARRTPEQWAQLAPFAP---TRADDIRHTLTHIDHHWGTLDAYLTAH-GLPNTDLTALRDR 225
Cdd:pfam13350 161 IVADYLLTNEYLEPLRERLLAAFREELLDDAEGIRPllsVRPEYLEAALDAIDERYGSVEGYLRDGlGLSDEDIEALRAR 240


                  ..
gi 1901933173 226 LT 227
Cdd:pfam13350 241 LL 242
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 10-167 2.35e-26

bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa TpbA; This subfamily contains bacterial protein tyrosine phosphatases (PTPs) and dual-specificity phosphatases (DUSPs) related to Pseudomonas aeruginosa TpbA, a DUSP that negatively regulates biofilm formation by converting extracellular quorum sensing signals and to Mycobacterium tuberculosis PtpB, a PTP virulence factor that attenuates host immune defenses by interfering with signal transduction pathways in macrophages. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides, while DUSPs function as protein-serine/threonine phosphatases (EC 3.1.3.16) and PTPs.


Pssm-ID: 350378 [Multi-domain]  Cd Length: 158  Bit Score: 99.76  E-value: 2.35e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901933173  10 GLLNFRRSLPG-LSRSDTLSRltPDGRRDLKALNFSRIIDLRSRTERAADPPPYL--GHAAYLNLPLLPWRhrafneasa 86
Cdd:cd14529     2 GANNFRDVTPYvLYRSAQLSP--DEDRALLKKLGIKTVIDLRGADERAASEEAAAkiDGVKYVNLPLSATR--------- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901933173  87 aarsnadhmsamLDHAPNQIVTVLGAILDAPpGPVLIHCHAGKDRTGLIAALCSELAGQTRDQTADDYTASGPALRDFYR 166
Cdd:cd14529    71 ------------PTESDVQSFLLIMDLKLAP-GPVLIHCKHGKDRTGLVSALYRIVYGGSKEEANEDYRLSNRHLEGLRS 137


                  .
gi 1901933173 167 D 167
Cdd:cd14529   138 G 138
COG3453 COG3453
Predicted phosphohydrolase, protein tyrosine phosphatase (PTP) superfamily, DUF442 family ...
 24-138 2.66e-06

Predicted phosphohydrolase, protein tyrosine phosphatase (PTP) superfamily, DUF442 family [General function prediction only];


Pssm-ID: 442676 [Multi-domain]  Cd Length: 125  Bit Score: 45.21  E-value: 2.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901933173  24 SDTLS---RLTPDGRRDLKALNFSRIIDLRSRTERAADPPPYLGHAA-------YLNLPLlpwRHRAFNEASAAArsnad 93
Cdd:COG3453     5 TDRLSvsgQPTPEDLAALAAAGFKTVINLRPDGEEPDQPAAADEAAAaeaagleYVHIPV---TGGAITDEDVEA----- 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1901933173  94 hmsamldhapnqivtvLGAILDAPPGPVLIHCHAGKdRTGLIAAL 138
Cdd:COG3453    77 ----------------FAAALAAAPGPVLAHCRSGT-RSSALWAL 104
PFA-DSP_unk cd18538
unknown subfamily of atypical dual-specificity phosphatases from fungi; This uncharacterized ...
 12-163 8.36e-06

unknown subfamily of atypical dual-specificity phosphatases from fungi; This uncharacterized subfamily belongs to the plant and fungi atypical dual-specificity phosphatases (PFA-DSPs) group of atypical DSPs that present in plants, fungi, kinetoplastids, and slime molds. They share structural similarity with atypical- and lipid phosphatase DSPs from mammals. The PFA-DSP group is composed of active as well as inactive phosphatases. This unknown subgroup contains the conserved the CxxxxxR catalytic motif present in active cysteine phosphatases.


Pssm-ID: 350514 [Multi-domain]  Cd Length: 145  Bit Score: 44.28  E-value: 8.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901933173  12 LNFRRSLPGLSRSdtlSRLTPDGRRDLKALNFSRIIDLRSRTEraadPPPYLghaAYLnlpllpwRHRAFNEASAAARSN 91
Cdd:cd18538     4 PNFGVVVPGVYRS---SFPKPENFGFLKSLGLRTILTLVQEEY----SPEFL---NFL-------RENGIQHFHIAMLGN 66

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1901933173  92 ADHMSAMLDHAPNQIVTVlgaILDAPPGPVLIHCHAGKDRTGLIAALCSELAGQTRDQTADDY-TASGPALRD 163
Cdd:cd18538    67 KDPKVSIPDHTMNRILRI---ILDKENHPILVHCNKGKHRTGCVIACFRKLQGWDVENVLEEYlSYAHPKSRD 136
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
34-137 1.95e-05

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 43.04  E-value: 1.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901933173  34 GRRDLKALNFSRIIDLRSRTERAADPPPYLGHAaYLNLPLLpwrhrafneasaaarsnaDHmsamldHAP--NQIVTVLG 111
Cdd:COG2453    17 GEADLKREGIDAVVSLTEEEELLLGLLEEAGLE-YLHLPIP------------------DF------GAPddEQLQEAVD 71

                          90       100
                  ....*....|....*....|....*...
gi 1901933173 112 AILDAPP--GPVLIHCHAGKDRTGLIAA 137
Cdd:COG2453    72 FIDEALRegKKVLVHCRGGIGRTGTVAA 99
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 101-137 1.07e-04

dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as VH1-like phosphatase Z (VHZ) or low molecular mass dual specificity phosphatase 3 (LDP-3), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP23 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. It is able to enhance activation of JNK and p38 MAPK, and has been shown to dephosphorylate p44-ERK1 (MAPK3) in vitro. It has been associated with cell growth and human primary cancers. It has also been identified as a cell-cell adhesion regulatory protein; it promotes the dephosphorylation of beta-catenin at Tyr 142 and enhances the interaction between alpha- and beta-catenin.


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 41.11  E-value: 1.07e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1901933173 101 HAPN--QIVTVLGAILDAP--PGPVLIHCHAGKDRTGLIAA 137
Cdd:cd14504    61 TPPTleQIDEFLDIVEEANakNEAVLVHCLAGKGRTGTMLA 101
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 116-138 3.01e-04

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases.


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 39.26  E-value: 3.01e-04
                          10        20
                  ....*....|....*....|...
gi 1901933173 116 APPGPVLIHCHAGKDRTGLIAAL 138
Cdd:cd14494    54 KPGEPVLVHCKAGVGRTGTLVAC 76
Y_phosphatase2 pfam03162
Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 ...
 7-135 7.68e-04

Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 families.


Pssm-ID: 397328 [Multi-domain]  Cd Length: 150  Bit Score: 38.50  E-value: 7.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901933173   7 PPgglLNFRRSLPGLSRSDTlsrltPDgrrdlkALNFSRIIDLRSRTERAADPPPYlghaAYLNLPLLPWRHraFNEASA 86
Cdd:pfam03162   3 PP---LNFSPVEPGLYRSSY-----PR------ANNFSFLRSLRLKTIISLSPEPY----PQDNLQFLESEH--IKLYHI 62

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1901933173  87 AARSNADHMSAMLDHapnQIVTVLGAILDAPPGPVLIHCHAGKDRTGLI 135
Cdd:pfam03162  63 HMEGNKDPFVNIPSH---LLRRALKLLLNKDNYPVLIHCNRGKHRTGLV 108
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
119-153 1.17e-03

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 37.34  E-value: 1.17e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1901933173  119 GPVLIHCHAGKDRTGLIAALCSELAGQTRDQTADD 153
Cdd:smart00404  40 GPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVD 74
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 119-153 1.17e-03

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine phosphatases. Homologues detected by this profile and not by those of "PTPc" or "DSPc" are predicted to be protein phosphatases with a similar fold to DSPs and PTPs, yet with unpredicted specificities.


Pssm-ID: 214469 [Multi-domain]  Cd Length: 105  Bit Score: 37.34  E-value: 1.17e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1901933173  119 GPVLIHCHAGKDRTGLIAALCSELAGQTRDQTADD 153
Cdd:smart00012  40 GPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVD 74
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 92-137 5.42e-03

protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine phosphatase domain-containing protein 1 (PTPDC1) is an uncharacterized non-receptor class protein-tyrosine phosphatase (PTP). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Small interfering RNA (siRNA) knockdown of the ptpdc1 gene is associated with elongated cilia.


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 36.94  E-value: 5.42e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1901933173  92 ADHMSAMLDhapnqIVTVLGAILDAPpGPVLIHCHAGKDRTGLIAA 137
Cdd:cd14506    89 VPSLTTILD-----IVKVMAFALQEG-GKVAVHCHAGLGRTGVLIA 128
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 121-137 6.79e-03

cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of eukaryotic cyclin-dependent kinase inhibitor 3 (CDKN3) and related archaeal and bacterial proteins. CDKN3 is also known as kinase-associated phosphatase (KAP), CDK2-associated dual-specificity phosphatase, cyclin-dependent kinase interactor 1 (CDI1), or cyclin-dependent kinase-interacting protein 2 (CIP2). It has been characterized as dual-specificity phosphatase, which function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and protein-tyrosine-phosphatase (EC 3.1.3.48). It dephosphorylates CDK2 at a threonine residue in a cyclin-dependent manner, resulting in the inhibition of G1/S cell cycle progression. It also interacts with CDK1 and controls progression through mitosis by dephosphorylating CDC2. CDKN3 may also function as a tumor suppressor; its loss of function was found in a variety of cancers including glioblastoma and hepatocellular carcinoma. However, it has also been found over-expressed in many cancers such as breast, cervical, lung and prostate cancers, and may also have an oncogenic function.


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 36.09  E-value: 6.79e-03
                          10
                  ....*....|....*..
gi 1901933173 121 VLIHCHAGKDRTGLIAA 137
Cdd:cd14505   109 VLIHCKGGLGRTGLIAA 125
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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