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Conserved domains on  [gi|2217276710|ref|XP_047281015|]
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paladin isoform X2 [Homo sapiens]

Protein Classification

PTP_paladin_1 and PTP_DSP_cys domain-containing protein( domain architecture ID 13026115)

PTP_paladin_1 and PTP_DSP_cys domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP_DSP_cys super family cl28904
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 477-733 8.53e-118

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.


The actual alignment was detected with superfamily member cd17660:

Pssm-ID: 475123  Cd Length: 216  Bit Score: 353.70  E-value: 8.53e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276710 477 DLIARGS--LREDDLVSPDALSTVREMDVANFRRVPRMPIYGTAQPSAKALGSILAYLTDAKRRLRKVVWVSLREEAVLE 554
Cdd:cd17660     2 DLITKGTrvLVEDERLSPDVLSTYKEMKVANFRRVPKMPIYGMAQPSSEALGVVLAYLTDAKRKHSKVLWVNLREELVLE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276710 555 CDGHTYSLRWPGPpvapdqletLEAQLKAhlsepppgkegpltyrfqtcltmqevfsqhrracpGLTYHRIPMPDFCAPR 634
Cdd:cd17660    82 ANGQTFSPREPGN---------LEQLIPV-----------------------------------GLTYRRIPIPDFCAPR 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276710 635 EEDFDQLLEALRAALSKDPGTGFVFSCLSGQGRTTTAMVVAVLAFWHIQGFPEVGEEELVSVPDAKFTKGEFQVVMKVVQ 714
Cdd:cd17660   118 EEDFDRLLEAMKSALAEDSGTAFVFNCLDGKGRTTTAMVIAVLTLWHFNGFPEGTEDEIVSVPDAKYTKGEFEVVMKVVR 197

                         250
                  ....*....|....*....
gi 2217276710 715 LLPDGHRVKKEVDAALDTV 733
Cdd:cd17660   198 LLPDGHRMKREVDAALDSV 216
PTP_paladin_1 cd17659
protein tyrosine phosphatase-like domain of paladin, repeat 1; Paladin is a putative ...
 91-382 1.08e-99

protein tyrosine phosphatase-like domain of paladin, repeat 1; Paladin is a putative phosphatase, which in mouse is expressed in endothelial cells during embryonic development and in arterial smooth muscle cells in adults. It has been suggested to be an antiphosphatase that regulates the activity of specific neural crest regulatory factors and thus, modulates neural crest cell formation and migration. Paladin contains two tyrosine-protein phosphatase domains. This model represents repeat 1.


:

Pssm-ID: 350497  Cd Length: 220  Bit Score: 306.78  E-value: 1.08e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276710  91 EHYLVQGRYFLVRDVTEKMDVLGTVGSCGAPNFRQVQGGLTVFGMGQPSLSGFRRVLQKLQKDGHRECVIFCVREEPVLF 170
Cdd:cd17659     1 EHYLIQGKYFLVKDVFSGIDILGTLKKYGAPNFRQAGGGYPVYGMGQPSLDGLKRVLEKLQTRGHKEIIFFNLREEPVLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276710 171 LRADEDFVSYTPRdkqnlhenlqglgpgvrveslelairkeihdfaqlsentyhvyhntedlwgephavaihgeddlhvt 250
Cdd:cd17659    81 LSLEEDFVPYSPR------------------------------------------------------------------- 93

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276710 251 eevykrplflqpTYRYHRLPLPEQGSPLEAQLDAFVSVLRETPSLLqlrDAHGPPPALVFSCQMGVGRTNLGMVLGTLIL 330
Cdd:cd17659    94 ------------AYRYHRLPLPEDGAPLEIQFDAFVNVLRENPSLS---DAIGLLPALLFSCQPGVGRTNLAMVLGTLVL 158

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217276710 331 LHRSGTTSQPEAAPTQAKPLPMEQFQVIQSFLRMV----------PQGRRMVEEVDRAITAC 382
Cdd:cd17659   159 GHKHGTTSEATNASDYENGEPKIIFQVIQVFINKLlpalifnchvPQGRTTVEEVDRAIILC 220
 
Name Accession Description Interval E-value
PTP_paladin_2 cd17660
protein tyrosine phosphatase-like domain of paladin, repeat 2; Paladin is a putative ...
 477-733 8.53e-118

protein tyrosine phosphatase-like domain of paladin, repeat 2; Paladin is a putative phosphatase, which in mouse is expressed in endothelial cells during embryonic development and in arterial smooth muscle cells in adults. It has been suggested to be an antiphosphatase that regulates the activity of specific neural crest regulatory factors and thus, modulates neural crest cell formation and migration. Paladin contains two tyrosine-protein phosphatase domains. This model represents repeat 2.


Pssm-ID: 350498  Cd Length: 216  Bit Score: 353.70  E-value: 8.53e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276710 477 DLIARGS--LREDDLVSPDALSTVREMDVANFRRVPRMPIYGTAQPSAKALGSILAYLTDAKRRLRKVVWVSLREEAVLE 554
Cdd:cd17660     2 DLITKGTrvLVEDERLSPDVLSTYKEMKVANFRRVPKMPIYGMAQPSSEALGVVLAYLTDAKRKHSKVLWVNLREELVLE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276710 555 CDGHTYSLRWPGPpvapdqletLEAQLKAhlsepppgkegpltyrfqtcltmqevfsqhrracpGLTYHRIPMPDFCAPR 634
Cdd:cd17660    82 ANGQTFSPREPGN---------LEQLIPV-----------------------------------GLTYRRIPIPDFCAPR 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276710 635 EEDFDQLLEALRAALSKDPGTGFVFSCLSGQGRTTTAMVVAVLAFWHIQGFPEVGEEELVSVPDAKFTKGEFQVVMKVVQ 714
Cdd:cd17660   118 EEDFDRLLEAMKSALAEDSGTAFVFNCLDGKGRTTTAMVIAVLTLWHFNGFPEGTEDEIVSVPDAKYTKGEFEVVMKVVR 197

                         250
                  ....*....|....*....
gi 2217276710 715 LLPDGHRVKKEVDAALDTV 733
Cdd:cd17660   198 LLPDGHRMKREVDAALDSV 216
PTP_paladin_1 cd17659
protein tyrosine phosphatase-like domain of paladin, repeat 1; Paladin is a putative ...
 91-382 1.08e-99

protein tyrosine phosphatase-like domain of paladin, repeat 1; Paladin is a putative phosphatase, which in mouse is expressed in endothelial cells during embryonic development and in arterial smooth muscle cells in adults. It has been suggested to be an antiphosphatase that regulates the activity of specific neural crest regulatory factors and thus, modulates neural crest cell formation and migration. Paladin contains two tyrosine-protein phosphatase domains. This model represents repeat 1.


Pssm-ID: 350497  Cd Length: 220  Bit Score: 306.78  E-value: 1.08e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276710  91 EHYLVQGRYFLVRDVTEKMDVLGTVGSCGAPNFRQVQGGLTVFGMGQPSLSGFRRVLQKLQKDGHRECVIFCVREEPVLF 170
Cdd:cd17659     1 EHYLIQGKYFLVKDVFSGIDILGTLKKYGAPNFRQAGGGYPVYGMGQPSLDGLKRVLEKLQTRGHKEIIFFNLREEPVLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276710 171 LRADEDFVSYTPRdkqnlhenlqglgpgvrveslelairkeihdfaqlsentyhvyhntedlwgephavaihgeddlhvt 250
Cdd:cd17659    81 LSLEEDFVPYSPR------------------------------------------------------------------- 93

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276710 251 eevykrplflqpTYRYHRLPLPEQGSPLEAQLDAFVSVLRETPSLLqlrDAHGPPPALVFSCQMGVGRTNLGMVLGTLIL 330
Cdd:cd17659    94 ------------AYRYHRLPLPEDGAPLEIQFDAFVNVLRENPSLS---DAIGLLPALLFSCQPGVGRTNLAMVLGTLVL 158

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217276710 331 LHRSGTTSQPEAAPTQAKPLPMEQFQVIQSFLRMV----------PQGRRMVEEVDRAITAC 382
Cdd:cd17659   159 GHKHGTTSEATNASDYENGEPKIIFQVIQVFINKLlpalifnchvPQGRTTVEEVDRAIILC 220
PTPlike_phytase pfam14566
Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in ...
 161-330 8.23e-51

Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in abundance in seeds and acting as an inorganic phosphate reservoir. Phytases are phosphatases that hydrolyze phytate to less-phosphorylated myo-inositol derivatives and inorganic phosphate. The active-site sequence (HCXXGXGR) of the phytase identified from the gut micro-organizm Selenomonas ruminantium forms a loop (P loop) at the base of a substrate binding pocket that is characteriztic of protein tyrosine phosphatases (PTPs). The depth of this pocket is an important determinant of the substrate specificity of PTPs. In humans this enzyme is thought to aid bone mineralization and salvage the inositol moiety prior to apoptosis.


Pssm-ID: 464208 [Multi-domain]  Cd Length: 157  Bit Score: 174.42  E-value: 8.23e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276710 161 FCVREEPVLFLradeDFVSYTPRDKQNLHENLQGLGP--GVRVESLELAIRKEIHDFAQLSENTYHVYHNTEDLWGEPHA 238
Cdd:pfam14566   1 VNLREEPVVYI----NGRPYVLREAEDPLNNLKEYPGisAERLERLEARLKEDVLAEAKKNGGRVLVHDETEDGIGVLTV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276710 239 VAIhGEDDLHVTEEVYKRPLFLQPTYRYHRLPLPEQGSPLEAQLDAFVSVLRETPSllqlrdahgpPPALVFSCQMGVGR 318
Cdd:pfam14566  77 VDV-WESDVQTPEEVYERLKAEGPGVDYRRIPITDEKAPLEEDFDALISIVKDAPE----------DTALVFNCQMGRGR 145

                         170
                  ....*....|..
gi 2217276710 319 TNLGMVLGTLIL 330
Cdd:pfam14566 146 TTTAMVIADLVR 157
PTPlike_phytase pfam14566
Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in ...
 545-677 4.79e-31

Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in abundance in seeds and acting as an inorganic phosphate reservoir. Phytases are phosphatases that hydrolyze phytate to less-phosphorylated myo-inositol derivatives and inorganic phosphate. The active-site sequence (HCXXGXGR) of the phytase identified from the gut micro-organizm Selenomonas ruminantium forms a loop (P loop) at the base of a substrate binding pocket that is characteriztic of protein tyrosine phosphatases (PTPs). The depth of this pocket is an important determinant of the substrate specificity of PTPs. In humans this enzyme is thought to aid bone mineralization and salvage the inositol moiety prior to apoptosis.


Pssm-ID: 464208 [Multi-domain]  Cd Length: 157  Bit Score: 118.95  E-value: 4.79e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276710 545 VSLREEAVLECDGHTYSLR---------WPGPPVAPDQLETLEAQLK----------------AHLSEPPPGKEGPLTYR 599
Cdd:pfam14566   1 VNLREEPVVYINGRPYVLReaedplnnlKEYPGISAERLERLEARLKedvlaeakknggrvlvHDETEDGIGVLTVVDVW 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217276710 600 FQTCLTMQEVFSQHRRACPGLTYHRIPMPDFCAPREEDFDQLLEALRAAlskDPGTGFVFSCLSGQGRTTTAMVVAVL 677
Cdd:pfam14566  81 ESDVQTPEEVYERLKAEGPGVDYRRIPITDEKAPLEEDFDALISIVKDA---PEDTALVFNCQMGRGRTTTAMVIADL 155
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
618-677 3.10e-09

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 56.13  E-value: 3.10e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276710 618 PGLTYHRIPMPDFCAPREEDFDQLLEALRAALSKdpGTGFVFSCLSGQGRTTTaMVVAVL 677
Cdd:COG2453    46 AGLEYLHLPIPDFGAPDDEQLQEAVDFIDEALRE--GKKVLVHCRGGIGRTGT-VAAAYL 102
 
Name Accession Description Interval E-value
PTP_paladin_2 cd17660
protein tyrosine phosphatase-like domain of paladin, repeat 2; Paladin is a putative ...
 477-733 8.53e-118

protein tyrosine phosphatase-like domain of paladin, repeat 2; Paladin is a putative phosphatase, which in mouse is expressed in endothelial cells during embryonic development and in arterial smooth muscle cells in adults. It has been suggested to be an antiphosphatase that regulates the activity of specific neural crest regulatory factors and thus, modulates neural crest cell formation and migration. Paladin contains two tyrosine-protein phosphatase domains. This model represents repeat 2.


Pssm-ID: 350498  Cd Length: 216  Bit Score: 353.70  E-value: 8.53e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276710 477 DLIARGS--LREDDLVSPDALSTVREMDVANFRRVPRMPIYGTAQPSAKALGSILAYLTDAKRRLRKVVWVSLREEAVLE 554
Cdd:cd17660     2 DLITKGTrvLVEDERLSPDVLSTYKEMKVANFRRVPKMPIYGMAQPSSEALGVVLAYLTDAKRKHSKVLWVNLREELVLE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276710 555 CDGHTYSLRWPGPpvapdqletLEAQLKAhlsepppgkegpltyrfqtcltmqevfsqhrracpGLTYHRIPMPDFCAPR 634
Cdd:cd17660    82 ANGQTFSPREPGN---------LEQLIPV-----------------------------------GLTYRRIPIPDFCAPR 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276710 635 EEDFDQLLEALRAALSKDPGTGFVFSCLSGQGRTTTAMVVAVLAFWHIQGFPEVGEEELVSVPDAKFTKGEFQVVMKVVQ 714
Cdd:cd17660   118 EEDFDRLLEAMKSALAEDSGTAFVFNCLDGKGRTTTAMVIAVLTLWHFNGFPEGTEDEIVSVPDAKYTKGEFEVVMKVVR 197

                         250
                  ....*....|....*....
gi 2217276710 715 LLPDGHRVKKEVDAALDTV 733
Cdd:cd17660   198 LLPDGHRMKREVDAALDSV 216
PTP_paladin_1 cd17659
protein tyrosine phosphatase-like domain of paladin, repeat 1; Paladin is a putative ...
 91-382 1.08e-99

protein tyrosine phosphatase-like domain of paladin, repeat 1; Paladin is a putative phosphatase, which in mouse is expressed in endothelial cells during embryonic development and in arterial smooth muscle cells in adults. It has been suggested to be an antiphosphatase that regulates the activity of specific neural crest regulatory factors and thus, modulates neural crest cell formation and migration. Paladin contains two tyrosine-protein phosphatase domains. This model represents repeat 1.


Pssm-ID: 350497  Cd Length: 220  Bit Score: 306.78  E-value: 1.08e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276710  91 EHYLVQGRYFLVRDVTEKMDVLGTVGSCGAPNFRQVQGGLTVFGMGQPSLSGFRRVLQKLQKDGHRECVIFCVREEPVLF 170
Cdd:cd17659     1 EHYLIQGKYFLVKDVFSGIDILGTLKKYGAPNFRQAGGGYPVYGMGQPSLDGLKRVLEKLQTRGHKEIIFFNLREEPVLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276710 171 LRADEDFVSYTPRdkqnlhenlqglgpgvrveslelairkeihdfaqlsentyhvyhntedlwgephavaihgeddlhvt 250
Cdd:cd17659    81 LSLEEDFVPYSPR------------------------------------------------------------------- 93

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276710 251 eevykrplflqpTYRYHRLPLPEQGSPLEAQLDAFVSVLRETPSLLqlrDAHGPPPALVFSCQMGVGRTNLGMVLGTLIL 330
Cdd:cd17659    94 ------------AYRYHRLPLPEDGAPLEIQFDAFVNVLRENPSLS---DAIGLLPALLFSCQPGVGRTNLAMVLGTLVL 158

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217276710 331 LHRSGTTSQPEAAPTQAKPLPMEQFQVIQSFLRMV----------PQGRRMVEEVDRAITAC 382
Cdd:cd17659   159 GHKHGTTSEATNASDYENGEPKIIFQVIQVFINKLlpalifnchvPQGRTTVEEVDRAIILC 220
PTPlike_phytase pfam14566
Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in ...
 161-330 8.23e-51

Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in abundance in seeds and acting as an inorganic phosphate reservoir. Phytases are phosphatases that hydrolyze phytate to less-phosphorylated myo-inositol derivatives and inorganic phosphate. The active-site sequence (HCXXGXGR) of the phytase identified from the gut micro-organizm Selenomonas ruminantium forms a loop (P loop) at the base of a substrate binding pocket that is characteriztic of protein tyrosine phosphatases (PTPs). The depth of this pocket is an important determinant of the substrate specificity of PTPs. In humans this enzyme is thought to aid bone mineralization and salvage the inositol moiety prior to apoptosis.


Pssm-ID: 464208 [Multi-domain]  Cd Length: 157  Bit Score: 174.42  E-value: 8.23e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276710 161 FCVREEPVLFLradeDFVSYTPRDKQNLHENLQGLGP--GVRVESLELAIRKEIHDFAQLSENTYHVYHNTEDLWGEPHA 238
Cdd:pfam14566   1 VNLREEPVVYI----NGRPYVLREAEDPLNNLKEYPGisAERLERLEARLKEDVLAEAKKNGGRVLVHDETEDGIGVLTV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276710 239 VAIhGEDDLHVTEEVYKRPLFLQPTYRYHRLPLPEQGSPLEAQLDAFVSVLRETPSllqlrdahgpPPALVFSCQMGVGR 318
Cdd:pfam14566  77 VDV-WESDVQTPEEVYERLKAEGPGVDYRRIPITDEKAPLEEDFDALISIVKDAPE----------DTALVFNCQMGRGR 145

                         170
                  ....*....|..
gi 2217276710 319 TNLGMVLGTLIL 330
Cdd:pfam14566 146 TTTAMVIADLVR 157
PTP_paladin cd14496
protein tyrosine phosphatase-like domains of paladin; Paladin is a putative phosphatase, which ...
 91-382 2.54e-50

protein tyrosine phosphatase-like domains of paladin; Paladin is a putative phosphatase, which in mouse is expressed in endothelial cells during embryonic development and in arterial smooth muscle cells in adults. It has been suggested to be an antiphosphatase that regulates the activity of specific neural crest regulatory factors and thus, modulates neural crest cell formation and migration. Paladin contains two protein tyrosine phosphatase (PTP)-like domains. This model represents both repeats.


Pssm-ID: 350346 [Multi-domain]  Cd Length: 185  Bit Score: 174.35  E-value: 2.54e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276710  91 EHYLVQGRYFLVRDVTEKMDVLGT--VGSCGAPNFRQVqGGLTVFGMGQPSLSGFRRVLQKLQ--KDGHRECVIFCVREE 166
Cdd:cd14496     1 RSGSVLGAGTILKSDHFPGCQSLTlpERVEGAPNFRRV-PGLPVYGVAQPTIDGIRRVLSRLGaaPDGRGRVVWVNLREE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276710 167 PVLFLRADEDFVSYTPRDkqnlhenlqglgpgvrveslelairkeihdfaqlsentyhvyhntedlwgephavaihgedd 246
Cdd:cd14496    80 PVVYINGRPFVLREVERR-------------------------------------------------------------- 97

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276710 247 lhvteevykrplflqptYRYHRLPLPEQGSPLEAQLDAFVSVLRETPsllqlrdahGPPPALVFSCQMGVGRTNLGMVLG 326
Cdd:cd14496    98 -----------------VDYHRIPITDEKAPEPGDFDALLEVILSTD---------DPTTAFVFNCQMGRGRTTTGMVIA 151

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217276710 327 TLIllhrsgttsqpeaaptqakplpMEQFQVIQSFLRMVPQGRRMVEEVDRAITAC 382
Cdd:cd14496   152 SLV----------------------RGEYVVIRKLVRVLDHGKEAKRLVDRAIDAC 185
PTP_paladin cd14496
protein tyrosine phosphatase-like domains of paladin; Paladin is a putative phosphatase, which ...
 497-733 5.22e-49

protein tyrosine phosphatase-like domains of paladin; Paladin is a putative phosphatase, which in mouse is expressed in endothelial cells during embryonic development and in arterial smooth muscle cells in adults. It has been suggested to be an antiphosphatase that regulates the activity of specific neural crest regulatory factors and thus, modulates neural crest cell formation and migration. Paladin contains two protein tyrosine phosphatase (PTP)-like domains. This model represents both repeats.


Pssm-ID: 350346 [Multi-domain]  Cd Length: 185  Bit Score: 170.50  E-value: 5.22e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276710 497 TVREMDVANFRRVPRMPIYGTAQPSAKALGSILAYLTDAKRRLRKVVWVSLREEAVLECDGHTYSLRwpgppvapdqlet 576
Cdd:cd14496    26 PERVEGAPNFRRVPGLPVYGVAQPTIDGIRRVLSRLGAAPDGRGRVVWVNLREEPVVYINGRPFVLR------------- 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276710 577 leaqlkahlsepppgkegpLTYRfqtcltmqevfsqhrracpGLTYHRIPMPDFCAPREEDFDQLLEALRAALskDPGTG 656
Cdd:cd14496    93 -------------------EVER-------------------RVDYHRIPITDEKAPEPGDFDALLEVILSTD--DPTTA 132

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217276710 657 FVFSCLSGQGRTTTAMVVAVLafwhiqgfpevgeeelvsvpdakfTKGEFQVVMKVVQLLPDGHRVKKEVDAALDTV 733
Cdd:cd14496   133 FVFNCQMGRGRTTTGMVIASL------------------------VRGEYVVIRKLVRVLDHGKEAKRLVDRAIDAC 185
PTPlike_phytase pfam14566
Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in ...
 545-677 4.79e-31

Inositol hexakisphosphate; Inositol hexakisphosphate, often called phytate, is found in abundance in seeds and acting as an inorganic phosphate reservoir. Phytases are phosphatases that hydrolyze phytate to less-phosphorylated myo-inositol derivatives and inorganic phosphate. The active-site sequence (HCXXGXGR) of the phytase identified from the gut micro-organizm Selenomonas ruminantium forms a loop (P loop) at the base of a substrate binding pocket that is characteriztic of protein tyrosine phosphatases (PTPs). The depth of this pocket is an important determinant of the substrate specificity of PTPs. In humans this enzyme is thought to aid bone mineralization and salvage the inositol moiety prior to apoptosis.


Pssm-ID: 464208 [Multi-domain]  Cd Length: 157  Bit Score: 118.95  E-value: 4.79e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276710 545 VSLREEAVLECDGHTYSLR---------WPGPPVAPDQLETLEAQLK----------------AHLSEPPPGKEGPLTYR 599
Cdd:pfam14566   1 VNLREEPVVYINGRPYVLReaedplnnlKEYPGISAERLERLEARLKedvlaeakknggrvlvHDETEDGIGVLTVVDVW 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217276710 600 FQTCLTMQEVFSQHRRACPGLTYHRIPMPDFCAPREEDFDQLLEALRAAlskDPGTGFVFSCLSGQGRTTTAMVVAVL 677
Cdd:pfam14566  81 ESDVQTPEEVYERLKAEGPGVDYRRIPITDEKAPLEEDFDALISIVKDA---PEDTALVFNCQMGRGRTTTAMVIADL 155
PTP_paladin_2 cd17660
protein tyrosine phosphatase-like domain of paladin, repeat 2; Paladin is a putative ...
 94-379 1.57e-22

protein tyrosine phosphatase-like domain of paladin, repeat 2; Paladin is a putative phosphatase, which in mouse is expressed in endothelial cells during embryonic development and in arterial smooth muscle cells in adults. It has been suggested to be an antiphosphatase that regulates the activity of specific neural crest regulatory factors and thus, modulates neural crest cell formation and migration. Paladin contains two tyrosine-protein phosphatase domains. This model represents repeat 2.


Pssm-ID: 350498  Cd Length: 216  Bit Score: 96.39  E-value: 1.57e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276710  94 LVQGRYFLVRDVTEKMDVLGTVGSCGAPNFRQVQGgLTVFGMGQPSLSGFRRVLQKL--QKDGHRECVIFCVREEpvLFL 171
Cdd:cd17660     4 ITKGTRVLVEDERLSPDVLSTYKEMKVANFRRVPK-MPIYGMAQPSSEALGVVLAYLtdAKRKHSKVLWVNLREE--LVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276710 172 RADEDfvSYTPRDKQNLHEnlqglgpgvrveslelairkeihdfaqlsentyhvyhntedlwgephavaihgeddlhvte 251
Cdd:cd17660    81 EANGQ--TFSPREPGNLEQ------------------------------------------------------------- 97

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276710 252 evykrPLFLQPTYRyhRLPLPEQGSPLEAQLDAFVSVLRETPsllqlrdAHGPPPALVFSCQMGVGRTNLGMVLGTLILL 331
Cdd:cd17660    98 -----LIPVGLTYR--RIPIPDFCAPREEDFDRLLEAMKSAL-------AEDSGTAFVFNCLDGKGRTTTAMVIAVLTLW 163

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2217276710 332 HRSG--TTSQPEAAPTQAKPLPMEQFQVIQSFLRMVPQGRRMVEEVDRAI 379
Cdd:cd17660   164 HFNGfpEGTEDEIVSVPDAKYTKGEFEVVMKVVRLLPDGHRMKREVDAAL 213
PTP_paladin_1 cd17659
protein tyrosine phosphatase-like domain of paladin, repeat 1; Paladin is a putative ...
 493-750 3.03e-13

protein tyrosine phosphatase-like domain of paladin, repeat 1; Paladin is a putative phosphatase, which in mouse is expressed in endothelial cells during embryonic development and in arterial smooth muscle cells in adults. It has been suggested to be an antiphosphatase that regulates the activity of specific neural crest regulatory factors and thus, modulates neural crest cell formation and migration. Paladin contains two tyrosine-protein phosphatase domains. This model represents repeat 1.


Pssm-ID: 350497  Cd Length: 220  Bit Score: 69.50  E-value: 3.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276710 493 DALSTVREMDVANFRRVP-RMPIYGTAQPSAKALGSILAYLTdaKRRLRKVVWVSLREEAV----LECDGHTYSLRwpgp 567
Cdd:cd17659    20 DILGTLKKYGAPNFRQAGgGYPVYGMGQPSLDGLKRVLEKLQ--TRGHKEIIFFNLREEPVlflsLEEDFVPYSPR---- 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276710 568 pvapdqletleaqlkahlsepppgkegplTYRfqtcltmqevfsqhrracpgltYHRIPMPDFCAPREEDFDQLLEALRA 647
Cdd:cd17659    94 -----------------------------AYR----------------------YHRLPLPEDGAPLEIQFDAFVNVLRE 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276710 648 ALSKDPGTG----FVFSCLSGQGRTTTAMVVAVLAFWHIQGFPevgeEELVSVPDakFTKGEFQVVMKVVQLLPDGHRVK 723
Cdd:cd17659   123 NPSLSDAIGllpaLLFSCQPGVGRTNLAMVLGTLVLGHKHGTT----SEATNASD--YENGEPKIIFQVIQVFINKLLPA 196

                         250       260
                  ....*....|....*....|....*..
gi 2217276710 724 KEVDAALDTvSETMTPMHYhlREIIIC 750
Cdd:cd17659   197 LIFNCHVPQ-GRTTVEEVD--RAIILC 220
PTPLP-like cd14495
Protein tyrosine phosphatase-like domains of phytases and similar domains; This subfamily ...
 516-673 8.69e-10

Protein tyrosine phosphatase-like domains of phytases and similar domains; This subfamily contains the tandem protein tyrosine phosphatase (PTP)-like domains of protein tyrosine phosphatase-like phytases (PTPLPs) and similar domains including the PTP domain of Pseudomonas syringae tyrosine-protein phosphatase hopPtoD2. PTPLPs, also known as cysteine phytases, are one of four known classes of phytases, enzymes that degrade phytate (inositol hexakisphosphate [InsP(6)]) to less-phosphorylated myo-inositol derivatives. Phytate is the most abundant cellular inositol phosphate and plays important roles in a broad scope of cellular processes, including DNA repair, RNA processing and export, development, apoptosis, and pathogenicity. PTPLPs adopt a PTP fold, including the active-site signature sequence (CX5R(S/T)) and utilize a classical PTP reaction mechanism. However, these enzymes display no catalytic activity against classical PTP substrates due to several unique structural features that confer specificity for myo-inositol polyphosphates.


Pssm-ID: 350345  Cd Length: 278  Bit Score: 60.47  E-value: 8.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276710 516 GTAQPSAKALGSILAYLtdaKRRLRKVVWV-SLREEAVLECDGHTYSLR----W-----PGPPVAPDQLETLEAQLKAHL 585
Cdd:cd14495    43 GSAQFSEKQLKAILKKL---KEKAKGPIYVvDLRQESHGFLNGIAVSWYgprdWanlgkSQSEVLADERNRLQALLGKKV 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276710 586 SEPPPGK------EGPLTYRFQTCLTMQEVFSQHrracpGLTYHRIPMPDFCAPREEDFDQLLEALRAaLSKDpgTGFVF 659
Cdd:cd14495   120 VSIPLGKdkkkspSQPKTVKVESVRTEEELVKKK-----GAHYVRIAATDHVWPDDEEIDAFVAFYRS-LPAD--AWLHF 191

                         170
                  ....*....|....
gi 2217276710 660 SCLSGQGRTTTAMV 673
Cdd:cd14495   192 HCRAGKGRTTTFMV 205
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
618-677 3.10e-09

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 56.13  E-value: 3.10e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217276710 618 PGLTYHRIPMPDFCAPREEDFDQLLEALRAALSKdpGTGFVFSCLSGQGRTTTaMVVAVL 677
Cdd:COG2453    46 AGLEYLHLPIPDFGAPDDEQLQEAVDFIDEALRE--GKKVLVHCRGGIGRTGT-VAAAYL 102
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 617-672 4.54e-08

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: 52.66  E-value: 4.54e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217276710 617 CPGLTYHRIPMPDFCAPREEDFDQLLEALRAALSKdpGTGFVFSCLSGQGRTTTAM 672
Cdd:cd14504    47 CPGLRYHHIPIEDYTPPTLEQIDEFLDIVEEANAK--NEAVLVHCLAGKGRTGTML 100
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 619-670 9.60e-04

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: 40.71  E-value: 9.60e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2217276710 619 GLTYHRIPMPDFCAPREEDFDQ-LLEALRAALSKdpGTGFVFSCLSGQGRTTT 670
Cdd:cd14505    72 GITWHHLPIPDGGVPSDIAQWQeLLEELLSALEN--GKKVLIHCKGGLGRTGL 122
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 279-336 1.49e-03

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: 38.87  E-value: 1.49e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217276710 279 EAQLDAFVSVLRETPSllqlrdahgPPPALVFSCQMGVGRTNLGMVLGTLILLHRSGT 336
Cdd:cd14494    39 LAMVDRFLEVLDQAEK---------PGEPVLVHCKAGVGRTGTLVACYLVLLGGMSAE 87
 
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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