NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1098626536|ref|XP_018805132|]
View 

PREDICTED: tyrosine-protein phosphatase non-receptor type 9 isoform X4 [Bactrocera latifrons]

Protein Classification

SEC14 family lipid-binding protein( domain architecture ID 12895005)

SEC14 family lipid-binding protein contains a lipid-binding domain that is found in secretory proteins and in lipid regulated proteins; similar to Drosophila melanogaster retinol-binding protein pinta, a retinoid-binding protein which shows highest affinity for all-trans retinol

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 299-566 0e+00

catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein phosphatase non-receptor type 9 (PTPN9), also called protein-tyrosine phosphatase MEG2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN9 plays an important role in promoting intracellular secretary vesicle fusion in hematopoietic cells and promotes the dephosphorylation of ErbB2 and EGFR in breast cancer cells, leading to impaired activation of STAT5 and STAT3. It also directly dephosphorylates STAT3 at the Tyr705 residue, resulting in its inactivation. PTPN9 has been found to be dysregulated in various human cancers, including breast, colorectal, and gastric cancer.


:

Pssm-ID: 350391 [Multi-domain]  Cd Length: 271  Bit Score: 524.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 299 GRKGLVKEYAEIRNRAPEGTFVYARMGNNLTKNRYTDVLCYDHSRVVLSREDGE---DYINANFVDGYKQKNAYISTQGP 375
Cdd:cd14543     1 QKRGIYEEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDertDYINANFMDGYKQKNAYIATQGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 376 LPKTSQDFWRMIWEQHCLVVVMTTRVKERGRVKCGQYWEPTENSSLEFGNFHVRTLSIEINEDYTVASLELKNLKTDEIR 455
Cdd:cd14543    81 LPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 456 NVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQASMVKALGDTWAGHPRGPPIVVHCSAGIGRTGTFITLDICISRLEDV 535
Cdd:cd14543   161 QVTHFQFTSWPDFGVPSSAAALLDFLGEVRQQQALAVKAMGDRWKGHPPGPPIVVHCSAGIGRTGTFCTLDICLSQLEDV 240

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1098626536 536 GTADIRGTVEKIRSQRAYSIQMPDQYVFCHL 566
Cdd:cd14543   241 GTLNVMQTVRRMRTQRAFSIQTPDQYYFCYK 271
SEC14 super family cl49645
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 12-70 5.80e-12

Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p) and in RhoGAPs, RhoGEFs and the RasGAP, neurofibromin (NF1). Lipid-binding domain. The SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


The actual alignment was detected with superfamily member smart00516:

Pssm-ID: 214706 [Multi-domain]  Cd Length: 158  Bit Score: 63.86  E-value: 5.80e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1098626536   12 YPARLKKVLIVTAPLWFKAPFKILRLFVREKLRERVFTVS---VPTLGLHVPLKALPLHLGG 70
Cdd:smart00516  94 YPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGndsKEELLEYIDKEQLPEELGG 155
 
Name Accession Description Interval E-value
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 299-566 0e+00

catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein phosphatase non-receptor type 9 (PTPN9), also called protein-tyrosine phosphatase MEG2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN9 plays an important role in promoting intracellular secretary vesicle fusion in hematopoietic cells and promotes the dephosphorylation of ErbB2 and EGFR in breast cancer cells, leading to impaired activation of STAT5 and STAT3. It also directly dephosphorylates STAT3 at the Tyr705 residue, resulting in its inactivation. PTPN9 has been found to be dysregulated in various human cancers, including breast, colorectal, and gastric cancer.


Pssm-ID: 350391 [Multi-domain]  Cd Length: 271  Bit Score: 524.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 299 GRKGLVKEYAEIRNRAPEGTFVYARMGNNLTKNRYTDVLCYDHSRVVLSREDGE---DYINANFVDGYKQKNAYISTQGP 375
Cdd:cd14543     1 QKRGIYEEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDertDYINANFMDGYKQKNAYIATQGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 376 LPKTSQDFWRMIWEQHCLVVVMTTRVKERGRVKCGQYWEPTENSSLEFGNFHVRTLSIEINEDYTVASLELKNLKTDEIR 455
Cdd:cd14543    81 LPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 456 NVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQASMVKALGDTWAGHPRGPPIVVHCSAGIGRTGTFITLDICISRLEDV 535
Cdd:cd14543   161 QVTHFQFTSWPDFGVPSSAAALLDFLGEVRQQQALAVKAMGDRWKGHPPGPPIVVHCSAGIGRTGTFCTLDICLSQLEDV 240

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1098626536 536 GTADIRGTVEKIRSQRAYSIQMPDQYVFCHL 566
Cdd:cd14543   241 GTLNVMQTVRRMRTQRAFSIQTPDQYYFCYK 271
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
327-570 1.08e-119

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 353.86  E-value: 1.08e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 327 NLTKNRYTDVLCYDHSRVVLS-REDGEDYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERG 405
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTgDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 406 RVKCGQYWEPTENSSLEFGNFHVRTLSIEINE-DYTVASLELKNLKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKV 484
Cdd:pfam00102  81 REKCAQYWPEEEGESLEYGDFTVTLKKEKEDEkDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLRKV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 485 REKQasmvkalgdtwaGHPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFC 564
Cdd:pfam00102 161 RKSS------------LDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFL 228


                  ....*.
gi 1098626536 565 HLALIE 570
Cdd:pfam00102 229 YDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
302-570 1.17e-117

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 349.65  E-value: 1.17e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536  302 GLVKEYAEI-RNRAPEGTFVYARMGNNLTKNRYTDVLCYDHSRVVLSREDGE--DYINANFVDGYKQKNAYISTQGPLPK 378
Cdd:smart00194   1 GLEEEFEKLdRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEgsDYINASYIDGPNGPKAYIATQGPLPS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536  379 TSQDFWRMIWEQHCLVVVMTTRVKERGRVKCGQYWEPTENSSLEFGNFHVRTLSIEINEDYTVASLELKNLKTDEIRNVS 458
Cdd:smart00194  81 TVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVT 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536  459 HWQFTSWPDYGVPSSAMAMLNFLQKVREKQASmvkalgdtwaghpRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTA 538
Cdd:smart00194 161 HYHYTNWPDHGVPESPESILDLIRAVRKSQST-------------STGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEV 227

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1098626536  539 DIRGTVEKIRSQRAYSIQMPDQYVFCHLALIE 570
Cdd:smart00194 228 DIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
PHA02738 PHA02738
hypothetical protein; Provisional
 305-571 1.78e-77

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 248.30  E-value: 1.78e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 305 KEYAEIRNRAPEGTFVYARMGNNLtkNRYTDVLCYDHSRVVLSREDGE-DYINANFVDGYKQKNAYISTQGPLPKTSQDF 383
Cdd:PHA02738   29 REHQKVISEKVDGTFNAEKKNRKL--NRYLDAVCFDHSRVILPAERNRgDYINANYVDGFEYKKKFICGQAPTRQTCYDF 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 384 WRMIWEQHCLVVVMTTRVKERGRVKCGQYWEPTENSSLEFGNFHVRTLSIEINEDYTVASLELKNlKTDEIRNVSHWQFT 463
Cdd:PHA02738  107 YRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSIRFGKFKITTTQVETHPHYVKSTLLLTD-GTSATQTVTHFNFT 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 464 SWPDYGVPSSAMAMLNFLQKVREKQASMvkALGDTWAGHPRG--PPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIR 541
Cdd:PHA02738  186 AWPDHDVPKNTSEFLNFVLEVRQCQKEL--AQESLQIGHNRLqpPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIP 263

                         250       260       270
                  ....*....|....*....|....*....|
gi 1098626536 542 GTVEKIRSQRAYSIQMPDQYVFCHLALIEY 571
Cdd:PHA02738  264 SIVSSIRNQRYYSLFIPFQYFFCYRAVKRY 293
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
326-576 7.81e-35

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 132.91  E-value: 7.81e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 326 NNLTKNRYTDVLCYDHSRVvlsREDGEdYINANFVDGyKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKE-- 403
Cdd:COG5599    41 NGSPLNRFRDIQPYKETAL---RANLG-YLNANYIQV-IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEis 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 404 RGRVKCGQYWEPTEnsslEFGNFHVRTL---SIEINEDYTVASLELKNLKTD-EIRNVSHWQFTSWPDYGVPSSAmAMLN 479
Cdd:COG5599   116 KPKVKMPVYFRQDG----EYGKYEVSSElteSIQLRDGIEARTYVLTIKGTGqKKIEIPVLHVKNWPDHGAISAE-ALKN 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 480 FLQKVREKQasmvkalgdTWAGHPRGPPiVVHCSAGIGRTGTFItLDICISRLEDVGTaDIRGTVEKI----RSQRAYSI 555
Cdd:COG5599   191 LADLIDKKE---------KIKDPDKLLP-VVHCRAGVGRTGTLI-ACLALSKSINALV-QITLSVEEIvidmRTSRNGGM 258

                         250       260
                  ....*....|....*....|..
gi 1098626536 556 -QMPDQYVFchlaLIEYAVSRG 576
Cdd:COG5599   259 vQTSEQLDV----LVKLAEQQI 276
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 12-70 5.80e-12

Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p) and in RhoGAPs, RhoGEFs and the RasGAP, neurofibromin (NF1). Lipid-binding domain. The SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 214706 [Multi-domain]  Cd Length: 158  Bit Score: 63.86  E-value: 5.80e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1098626536   12 YPARLKKVLIVTAPLWFKAPFKILRLFVREKLRERVFTVS---VPTLGLHVPLKALPLHLGG 70
Cdd:smart00516  94 YPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGndsKEELLEYIDKEQLPEELGG 155
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
 12-70 7.74e-12

Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory proteins, such as S. cerevisiae phosphatidylinositol transfer protein (Sec14p), and in lipid regulated proteins such as RhoGAPs, RhoGEFs and neurofibromin (NF1). SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 469559 [Multi-domain]  Cd Length: 156  Bit Score: 63.51  E-value: 7.74e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1098626536  12 YPARLKKVLIVTAPLWFKAPFKILRLFVREKLRERVFTVS--VPTLGLHVPLKALPLHLGG 70
Cdd:cd00170    95 YPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGsdLEELLEYIDPDQLPKELGG 155
CRAL_TRIO pfam00650
CRAL/TRIO domain;
1-70 4.37e-10

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 58.42  E-value: 4.37e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1098626536   1 MRINSTIEKGGYPARLKKVLIVTAPLWFKAPFKILRLFVREKLRERVF---TVSVPTLGLHVPLKALPLHLGG 70
Cdd:pfam00650  79 LKKIIKILQDNYPERLGKILIVNAPWIFNTIWKLIKPFLDPKTREKIVflkNSNEEELEKYIPPEQLPKEYGG 151
 
Name Accession Description Interval E-value
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 299-566 0e+00

catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein phosphatase non-receptor type 9 (PTPN9), also called protein-tyrosine phosphatase MEG2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN9 plays an important role in promoting intracellular secretary vesicle fusion in hematopoietic cells and promotes the dephosphorylation of ErbB2 and EGFR in breast cancer cells, leading to impaired activation of STAT5 and STAT3. It also directly dephosphorylates STAT3 at the Tyr705 residue, resulting in its inactivation. PTPN9 has been found to be dysregulated in various human cancers, including breast, colorectal, and gastric cancer.


Pssm-ID: 350391 [Multi-domain]  Cd Length: 271  Bit Score: 524.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 299 GRKGLVKEYAEIRNRAPEGTFVYARMGNNLTKNRYTDVLCYDHSRVVLSREDGE---DYINANFVDGYKQKNAYISTQGP 375
Cdd:cd14543     1 QKRGIYEEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDertDYINANFMDGYKQKNAYIATQGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 376 LPKTSQDFWRMIWEQHCLVVVMTTRVKERGRVKCGQYWEPTENSSLEFGNFHVRTLSIEINEDYTVASLELKNLKTDEIR 455
Cdd:cd14543    81 LPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 456 NVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQASMVKALGDTWAGHPRGPPIVVHCSAGIGRTGTFITLDICISRLEDV 535
Cdd:cd14543   161 QVTHFQFTSWPDFGVPSSAAALLDFLGEVRQQQALAVKAMGDRWKGHPPGPPIVVHCSAGIGRTGTFCTLDICLSQLEDV 240

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1098626536 536 GTADIRGTVEKIRSQRAYSIQMPDQYVFCHL 566
Cdd:cd14543   241 GTLNVMQTVRRMRTQRAFSIQTPDQYYFCYK 271
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
327-570 1.08e-119

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 353.86  E-value: 1.08e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 327 NLTKNRYTDVLCYDHSRVVLS-REDGEDYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERG 405
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTgDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 406 RVKCGQYWEPTENSSLEFGNFHVRTLSIEINE-DYTVASLELKNLKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKV 484
Cdd:pfam00102  81 REKCAQYWPEEEGESLEYGDFTVTLKKEKEDEkDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLRKV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 485 REKQasmvkalgdtwaGHPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFC 564
Cdd:pfam00102 161 RKSS------------LDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFL 228


                  ....*.
gi 1098626536 565 HLALIE 570
Cdd:pfam00102 229 YDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
302-570 1.17e-117

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 349.65  E-value: 1.17e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536  302 GLVKEYAEI-RNRAPEGTFVYARMGNNLTKNRYTDVLCYDHSRVVLSREDGE--DYINANFVDGYKQKNAYISTQGPLPK 378
Cdd:smart00194   1 GLEEEFEKLdRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEgsDYINASYIDGPNGPKAYIATQGPLPS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536  379 TSQDFWRMIWEQHCLVVVMTTRVKERGRVKCGQYWEPTENSSLEFGNFHVRTLSIEINEDYTVASLELKNLKTDEIRNVS 458
Cdd:smart00194  81 TVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVT 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536  459 HWQFTSWPDYGVPSSAMAMLNFLQKVREKQASmvkalgdtwaghpRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTA 538
Cdd:smart00194 161 HYHYTNWPDHGVPESPESILDLIRAVRKSQST-------------STGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEV 227

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1098626536  539 DIRGTVEKIRSQRAYSIQMPDQYVFCHLALIE 570
Cdd:smart00194 228 DIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 354-565 3.20e-93

catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. The depth of the active site cleft renders the enzyme specific for phosphorylated Tyr (pTyr) residues, instead of pSer or pThr. This family has a distinctive active site signature motif, HCSAGxGRxG, and are characterized as either transmembrane, receptor-like or non-transmembrane (soluble) PTPs. Receptor-like PTP domains tend to occur in two copies in the cytoplasmic region of the transmembrane proteins, only one copy may be active.


Pssm-ID: 350343 [Multi-domain]  Cd Length: 200  Bit Score: 284.56  E-value: 3.20e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 354 YINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGRVKCGQYWEPTENSSLEFGNFHVRTLSI 433
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGDITVTLVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 434 EINEDYTVASLELKNLKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQAsmvkalgdtwaghPRGPPIVVHCS 513
Cdd:cd00047    81 EELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEAR-------------KPNGPIVVHCS 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1098626536 514 AGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCH 565
Cdd:cd00047   148 AGVGRTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIY 199
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 327-574 6.10e-92

catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350401 [Multi-domain]  Cd Length: 238  Bit Score: 282.75  E-value: 6.10e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 327 NLTKNRYTDVLCYDHSRVVLSRED---GEDYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKE 403
Cdd:cd14553     3 NKPKNRYANVIAYDHSRVILQPIEgvpGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 404 RGRVKCGQYWePTENSSlEFGNFHVRTLSIEINEDYTVASLELKNLKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQK 483
Cdd:cd14553    83 RSRVKCDQYW-PTRGTE-TYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 484 VRekqasmvkalgdtwAGHPR-GPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYV 562
Cdd:cd14553   161 VK--------------ACNPPdAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYI 226

                         250
                  ....*....|..
gi 1098626536 563 FCHLALIEyAVS 574
Cdd:cd14553   227 FIHDALLE-AVT 237
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 332-565 6.37e-83

catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar proteins; R3 subfamily receptor-type phosphotyrosine phosphatases (RPTP) are characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. Vertebrate members include receptor-type tyrosine-protein phosphatase-like O (PTPRO), J (PTPRJ), Q (PTPRQ), B (PTPRB), V (PTPRV) and H (PTPRH). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Most members are PTPs, except for PTPRQ, which dephosphorylates phosphatidylinositide substrates. PTPRV is characterized only in rodents; its function has been lost in humans. Both vertebrate and invertebrate R3 subfamily RPTPs are involved in the control of a variety of cellular processes, including cell growth, differentiation, mitotic cycle and oncogenic transformation.


Pssm-ID: 350396 [Multi-domain]  Cd Length: 222  Bit Score: 258.82  E-value: 6.37e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 332 RYTDVLCYDHSRVVLS---REDGEDYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGRVK 408
Cdd:cd14548     1 RYTNILPYDHSRVKLIpinEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 409 CGQYWePTENSSLEFGNFHVRTLSIEINEDYTVASLELKNlkTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREkq 488
Cdd:cd14548    81 CDHYW-PFDQDPVYYGDITVTMLSESVLPDWTIREFKLER--GDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRD-- 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1098626536 489 asmvkalgdtWAGHPRGPPIvVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCH 565
Cdd:cd14548   156 ----------YIKQEKGPTI-VHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 354-565 5.97e-80

catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350397 [Multi-domain]  Cd Length: 204  Bit Score: 250.35  E-value: 5.97e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 354 YINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGRVKCGQYWePTENsSLEFGNFHVRTLSI 433
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYW-PKEG-TETYGNIQVTLLST 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 434 EINEDYTVASLELKNLK------TDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVrekqasmvkalgdTWAGHPRGPP 507
Cdd:cd14549    79 EVLATYTVRTFSLKNLKlkkvkgRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKS-------------SAANPPGAGP 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1098626536 508 IVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCH 565
Cdd:cd14549   146 IVVHCSAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
PHA02738 PHA02738
hypothetical protein; Provisional
 305-571 1.78e-77

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 248.30  E-value: 1.78e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 305 KEYAEIRNRAPEGTFVYARMGNNLtkNRYTDVLCYDHSRVVLSREDGE-DYINANFVDGYKQKNAYISTQGPLPKTSQDF 383
Cdd:PHA02738   29 REHQKVISEKVDGTFNAEKKNRKL--NRYLDAVCFDHSRVILPAERNRgDYINANYVDGFEYKKKFICGQAPTRQTCYDF 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 384 WRMIWEQHCLVVVMTTRVKERGRVKCGQYWEPTENSSLEFGNFHVRTLSIEINEDYTVASLELKNlKTDEIRNVSHWQFT 463
Cdd:PHA02738  107 YRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSIRFGKFKITTTQVETHPHYVKSTLLLTD-GTSATQTVTHFNFT 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 464 SWPDYGVPSSAMAMLNFLQKVREKQASMvkALGDTWAGHPRG--PPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIR 541
Cdd:PHA02738  186 AWPDHDVPKNTSEFLNFVLEVRQCQKEL--AQESLQIGHNRLqpPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIP 263

                         250       260       270
                  ....*....|....*....|....*....|
gi 1098626536 542 GTVEKIRSQRAYSIQMPDQYVFCHLALIEY 571
Cdd:PHA02738  264 SIVSSIRNQRYYSLFIPFQYFFCYRAVKRY 293
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 305-573 3.40e-77

catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350474 [Multi-domain]  Cd Length: 276  Bit Score: 246.10  E-value: 3.40e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 305 KEYAEIrNRAPEGTFVYARMGNNLTKNRYTDVLCYDHSRVVLSRED---GEDYINANFVDGYKQKNAYISTQGPLPKTSQ 381
Cdd:cd14626    20 QEYESI-DPGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDgvpGSDYINANYIDGYRKQNAYIATQGPLPETLS 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 382 DFWRMIWEQHCLVVVMTTRVKERGRVKCGQYWePTENSSlEFGNFHVRTLSIEINEDYTVASLELKNLKTDEIRNVSHWQ 461
Cdd:cd14626    99 DFWRMVWEQRTATIVMMTRLEEKSRVKCDQYW-PIRGTE-TYGMIQVTLLDTVELATYSVRTFALYKNGSSEKREVRQFQ 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 462 FTSWPDYGVPSSAMAMLNFLQKvrekqasmVKALGDTWAGhprgpPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIR 541
Cdd:cd14626   177 FMAWPDHGVPEYPTPILAFLRR--------VKACNPPDAG-----PMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIY 243

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1098626536 542 GTVEKIRSQRAYSIQMPDQYVFCHLALIEYAV 573
Cdd:cd14626   244 GHVTCMRSQRNYMVQTEDQYIFIHEALLEAAT 275
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 331-563 9.28e-77

catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type tyrosine-protein phosphatase J (PTPRJ or R-PTP-J), also known as receptor-type tyrosine-protein phosphatase eta (R-PTP-eta) or density-enhanced phosphatase 1 (DEP-1) OR CD148, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRJ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (eight in PTPRJ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed in various cell types including epithelial, hematopoietic, and endothelial cells. It plays a role in cell adhesion, migration, proliferation and differentiation. It dephosphorylates or contributes to the dephosphorylation of various substrates including protein kinases such as FLT3, PDGFRB, MET, RET (variant MEN2A), VEGFR-2, LYN, SRC, MAPK1, MAPK3, and EGFR, as well as PIK3R1 and PIK3R2.


Pssm-ID: 350463 [Multi-domain]  Cd Length: 229  Bit Score: 243.19  E-value: 9.28e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 331 NRYTDVLCYDHSRVVLSREDG--EDYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGRVK 408
Cdd:cd14615     1 NRYNNVLPYDISRVKLSVQSHstDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRTK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 409 CGQYWePTEnSSLEFGNFHVRTLSIEINEDYTVASLELKNLKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVRE-- 486
Cdd:cd14615    81 CEEYW-PSK-QKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREym 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1098626536 487 KQasmvkalgdtwagHPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVF 563
Cdd:cd14615   159 KQ-------------NPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVF 222
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 330-566 2.42e-76

catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1) type 2 (PTPN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases, (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1 (or PTP-1B) is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor. PTPN2 (or TCPTP), a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner.


Pssm-ID: 350393 [Multi-domain]  Cd Length: 231  Bit Score: 242.30  E-value: 2.42e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 330 KNRYTDVLCYDHSRVVLSREDGE-DYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGRVK 408
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKLKQGDnDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQIK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 409 CGQYWEPTENSS--LEFGNFHVRTLSIEINEDYTVASLELKNLKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVRE 486
Cdd:cd14545    81 CAQYWPQGEGNAmiFEDTGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQKVRE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 487 kQASMVKALGdtwaghprgpPIVVHCSAGIGRTGTFITLDICISRLE--DVGTADIRGTVEKIRSQRAYSIQMPDQYVFC 564
Cdd:cd14545   161 -SGSLSSDVG----------PPVVHCSAGIGRSGTFCLVDTCLVLIEkgNPSSVDVKKVLLEMRKYRMGLIQTPDQLRFS 229


                  ..
gi 1098626536 565 HL 566
Cdd:cd14545   230 YL 231
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 326-570 5.99e-75

catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG has four splicing isoforms: three transmembrane isoforms, PTPRG-A, B, and C, and one secretory isoform, PTPRG-S, which are expressed in many tissues including the brain. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350505 [Multi-domain]  Cd Length: 274  Bit Score: 240.32  E-value: 5.99e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 326 NNLTKNRYTDVLCYDHSRVVLSREDGED-----YINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTR 400
Cdd:cd17667    26 DNKHKNRYINILAYDHSRVKLRPLPGKDskhsdYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITN 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 401 VKERGRVKCGQYWePTENSSlEFGNFHVRTLSIEINEDYTVASLELKNLKTDEI-----------RNVSHWQFTSWPDYG 469
Cdd:cd17667   106 LVEKGRRKCDQYW-PTENSE-EYGNIIVTLKSTKIHACYTVRRFSIRNTKVKKGqkgnpkgrqneRTVIQYHYTQWPDMG 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 470 VPSSAMAMLNFlqkVREKQASMVKALGdtwaghprgpPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRS 549
Cdd:cd17667   184 VPEYALPVLTF---VRRSSAARTPEMG----------PVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRT 250

                         250       260
                  ....*....|....*....|.
gi 1098626536 550 QRAYSIQMPDQYVFCHLALIE 570
Cdd:cd17667   251 QRNYLVQTEEQYIFIHDALLE 271
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 307-572 7.22e-75

catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein phosphatase non-receptor type 1 (PTPN1), also called protein-tyrosine phosphatase 1B (PTP-1B), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN1/PTP-1B is the first PTP to be purified and characterized and is the prototypical intracellular PTP found in a wide variety of human tissues. It contains an N-terminal catalytic PTP domain, followed by two tandem proline-rich motifs that mediate interaction with SH3-domain-containing proteins, and a small hydrophobic stretch that localizes the enzyme to the endoplasmic reticulum (ER). It dephosphorylates and regulates the activity of a number of receptor tyrosine kinases, including the insulin receptor, the EGF receptor, and the PDGF receptor.


Pssm-ID: 350456 [Multi-domain]  Cd Length: 277  Bit Score: 239.93  E-value: 7.22e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 307 YAEIRNRAPEGTFVYARMGNNLTKNRYTDVLCYDHSRVVLSREDgEDYINANFVDGYKQKNAYISTQGPLPKTSQDFWRM 386
Cdd:cd14608     5 YQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQED-NDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEM 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 387 IWEQHCLVVVMTTRVKERGRVKCGQYWEPTENSSLEF--GNFHVRTLSIEINEDYTVASLELKNLKTDEIRNVSHWQFTS 464
Cdd:cd14608    84 VWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFedTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTT 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 465 WPDYGVPSSAMAMLNFLQKVREkQASMVKALGdtwaghprgpPIVVHCSAGIGRTGTFITLDICI---SRLEDVGTADIR 541
Cdd:cd14608   164 WPDFGVPESPASFLNFLFKVRE-SGSLSPEHG----------PVVVHCSAGIGRSGTFCLADTCLllmDKRKDPSSVDIK 232

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1098626536 542 GTVEKIRSQRAYSIQMPDQYVFCHLALIEYA 572
Cdd:cd14608   233 KVLLEMRKFRMGLIQTADQLRFSYLAVIEGA 263
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 327-571 3.65e-74

catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) and type 6 (PTPN6) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 and PTPN6, are also called SH2 domain-containing tyrosine phosphatase 2 (SHP2) and 1 (SHP1), respectively. They contain two tandem SH2 domains: a catalytic PTP domain, and a C-terminal tail with regulatory properties. Although structurally similar, they have different localization and different roles in signal transduction. PTPN11/SHP2 is expressed ubiquitously and plays a positive role in cell signaling, leading to cell activation, while PTPN6/SHP1 expression is restricted mainly to hematopoietic and epithelial cells and functions as a negative regulator of signaling events.


Pssm-ID: 350392 [Multi-domain]  Cd Length: 251  Bit Score: 237.36  E-value: 3.65e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 327 NLTKNRYTDVLCYDHSRVVLSRED----GEDYINANFV-------DGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVV 395
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKDRDpnvpGSDYINANYIrnenegpTTDENAKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 396 VMTTRVKERGRVKCGQYWePTENSSLEFGNFHVRTLSIEINEDYTVASLELKNLK-TDEIRNVSHWQFTSWPDYGVPSSA 474
Cdd:cd14544    81 VMTTKEVERGKNKCVRYW-PDEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDqGDPIREIWHYQYLSWPDHGVPSDP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 475 MAMLNFLQKVREKQASMvkalgdtwaghPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTA---DIRGTVEKIRSQR 551
Cdd:cd14544   160 GGVLNFLEDVNQRQESL-----------PHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLDcdiDIQKTIQMVRSQR 228

                         250       260
                  ....*....|....*....|
gi 1098626536 552 AYSIQMPDQYVFCHLALIEY 571
Cdd:cd14544   229 SGMVQTEAQYKFIYVAVAQY 248
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 322-567 3.43e-73

PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs) include three vertebrate members: LAR (or PTPRF), R-PTP-delta (or PTPRD), and R-PTP-sigma (or PTPRS). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules; they bind to distinct synaptic membrane proteins and are physiologically responsible for mediating presynaptic development by shaping various synaptic adhesion pathways. They play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. LAR-RPTPs contain an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2).


Pssm-ID: 350402 [Multi-domain]  Cd Length: 238  Bit Score: 234.34  E-value: 3.43e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 322 ARMGNNLTKNRYTDVLCYDHSRVVLSR---EDGEDYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMT 398
Cdd:cd14554     1 ANLPCNKFKNRLVNILPYESTRVCLQPirgVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 399 TRVKERGRVKCGQYWePTENSSlEFGNFHVRTLSIEINEDYTVASLELKNLKTDEIRNVSHWQFTSWPDYGVPSSAMAML 478
Cdd:cd14554    81 TKLREMGREKCHQYW-PAERSA-RYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 479 NFLQKVREkqasmvkalgdTWAGHPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMP 558
Cdd:cd14554   159 DFIGQVHK-----------TKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTE 227


                  ....*....
gi 1098626536 559 DQYVFCHLA 567
Cdd:cd14554   228 DQYQFCYRA 236
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 307-568 1.26e-72

catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein phosphatase non-receptor type 2 (PTPN2), also called T-cell protein-tyrosine phosphatase (TCPTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN2, a tumor suppressor, dephosphorylates and inactivates EGFRs, Src family kinases, Janus-activated kinases (JAKs)-1 and -3, and signal transducer and activators of transcription (STATs)-1, -3 and -5, in a cell type and context-dependent manner. It is deleted in 6% of all T-cell acute lymphoblastic leukemias and is associated with constitutive JAK1/STAT5 signaling and tumorigenesis.


Pssm-ID: 350455 [Multi-domain]  Cd Length: 257  Bit Score: 233.32  E-value: 1.26e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 307 YAEIRNRAPEGTFVYARMGNNLTKNRYTDVLCYDHSRVVLSREDgEDYINANFVDGYKQKNAYISTQGPLPKTSQDFWRM 386
Cdd:cd14607     4 YLEIRNESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTE-NDYINASLVVIEEAQRSYILTQGPLPNTCCHFWLM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 387 IWEQHCLVVVMTTRVKERGRVKCGQYWEPTENSSLEFGN--FHVRTLSIEINEDYTVASLELKNLKTDEIRNVSHWQFTS 464
Cdd:cd14607    83 VWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSFKEtgFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYTT 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 465 WPDYGVPSSAMAMLNFLQKVREKqasmvKALGdtwaghPRGPPIVVHCSAGIGRTGTFITLDICISRLE--DVGTADIRG 542
Cdd:cd14607   163 WPDFGVPESPASFLNFLFKVRES-----GSLS------PEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEkkDPDSVDIKQ 231

                         250       260
                  ....*....|....*....|....*.
gi 1098626536 543 TVEKIRSQRAYSIQMPDQYVFCHLAL 568
Cdd:cd14607   232 VLLDMRKYRMGLIQTPDQLRFSYMAV 257
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 303-570 4.28e-72

catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350473 [Multi-domain]  Cd Length: 282  Bit Score: 233.06  E-value: 4.28e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 303 LVKEYAEIrNRAPEGTFVYARMGNNLTKNRYTDVLCYDHSRVVLSREDG---EDYINANFVDGYKQKNAYISTQGPLPKT 379
Cdd:cd14625    24 LSQEYESI-DPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGimgSDYINANYIDGYRKQNAYIATQGPLPET 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 380 SQDFWRMIWEQHCLVVVMTTRVKERGRVKCGQYW-----------EPTENSSLEFGNFHVRTLSIEINedytvaslelkn 448
Cdd:cd14625   103 FGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWpsrgtetygmiQVTLLDTIELATFCVRTFSLHKN------------ 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 449 lKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREkqasmvkalgdtwAGHPRGPPIVVHCSAGIGRTGTFITLDIC 528
Cdd:cd14625   171 -GSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKT-------------CNPPDAGPIVVHCSAGVGRTGCFIVIDAM 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1098626536 529 ISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIE 570
Cdd:cd14625   237 LERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLE 278
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 292-576 3.73e-71

catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type tyrosine-protein phosphatase D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350472 [Multi-domain]  Cd Length: 284  Bit Score: 230.77  E-value: 3.73e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 292 VQMVKEQGRKGLVKEYAEIrNRAPEGTFVYARMGNNLTKNRYTDVLCYDHSRVVLSREDG---EDYINANFVDGYKQKNA 368
Cdd:cd14624    13 IERLKANDNLKFSQEYESI-DPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGipgSDYINANYIDGYRKQNA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 369 YISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGRVKCGQYWePTENSSLEfGNFHVRTLSIEINEDYTVASLELKN 448
Cdd:cd14624    92 YIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYW-PSRGTETY-GLIQVTLLDTVELATYCVRTFALYK 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 449 LKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREkqasmvkalgdtwAGHPRGPPIVVHCSAGIGRTGTFITLDIC 528
Cdd:cd14624   170 NGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKT-------------CNPPDAGPMVVHCSAGVGRTGCFIVIDAM 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1098626536 529 ISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIEyAVSRG 576
Cdd:cd14624   237 LERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLE-AVTCG 283
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 306-575 7.94e-71

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 231.07  E-value: 7.94e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 306 EYAEIRNRAPEGTFVYARMGNNLTKNRYTDVLCYDHSRVVL----------------------SREDGEDYINANFVDGY 363
Cdd:PHA02746   30 EHAEVMDIPIRGTTNHFLKKENLKKNRFHDIPCWDHSRVVInaheslkmfdvgdsdgkkievtSEDNAENYIHANFVDGF 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 364 KQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVkERGRVKCGQYWEPTENSSLEFGNFHVRTLSIEINEDYTVAS 443
Cdd:PHA02746  110 KEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTDI-DDDDEKCFELWTKEEDSELAFGRFVAKILDIIEELSFTKTR 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 444 LELKNLKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQASMVKalgdTWAGHPRGP-PIVVHCSAGIGRTGTF 522
Cdd:PHA02746  189 LMITDKISDTSREIHHFWFPDWPDNGIPTGMAEFLELINKVNEEQAELIK----QADNDPQTLgPIVVHCSAGIGRAGTF 264

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1098626536 523 ITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALiEYAVSR 575
Cdd:PHA02746  265 CAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL-KYAIIE 316
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 353-563 1.07e-70

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3) and type 4 (PTPN4) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 and PTPN4 are large modular proteins containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses.


Pssm-ID: 350389 [Multi-domain]  Cd Length: 212  Bit Score: 226.83  E-value: 1.07e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 353 DYINANFVD----GYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGRVKCGQYWePTENSSLEFGNFHV 428
Cdd:cd14541     1 DYINANYVNmeipGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYW-PDLGETMQFGNLQI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 429 RTLSIEINEDYTVASLELKNLKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQASMVkalgdtwaghprgPPI 508
Cdd:cd14541    80 TCVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMV-------------EPT 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1098626536 509 VVHCSAGIGRTGTFITLD--IC-ISRLEDVGTADIrgtVEKIRSQRAYSIQMPDQYVF 563
Cdd:cd14541   147 VVHCSAGIGRTGVLITMEtaMClIEANEPVYPLDI---VRTMRDQRAMLIQTPSQYRF 201
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 331-565 3.70e-70

catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; The kinase interaction motif (KIM) family of protein-tyrosine phosphatases (PTPs) includes tyrosine-protein phosphatases non-receptor type 7 (PTPN7) and non-receptor type 5 (PTPN5), and protein-tyrosine phosphatase receptor type R (PTPRR). PTPN7 is also called hematopoietic protein-tyrosine phosphatase (HePTP) while PTPN5 is also called striatal-enriched protein-tyrosine phosphatase (STEP). They belong to the family of classical tyrosine-specific PTPs (EC 3.1.3.48) that catalyze the dephosphorylation of phosphotyrosine peptides. KIM-PTPs are characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. They are highly specific to the MAPKs ERK1/2 (extracellular-signal-regulated kinase 1/2) and p38, over JNK (c-Jun N-terminal kinase); they dephosphorylate these kinases and thereby critically modulate cell proliferation and differentiation.


Pssm-ID: 350395 [Multi-domain]  Cd Length: 224  Bit Score: 225.74  E-value: 3.70e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 331 NRYTDVLCYDHSRVVLSREDGE---DYINANFVDGYKQKN-AYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERgR 406
Cdd:cd14547     1 NRYKTILPNEHSRVCLPSVDDDplsSYINANYIRGYDGEEkAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA-K 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 407 VKCGQYWEPTENSslEFGNFHVRTLSIEINEDYTVASLELKNlkTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVRE 486
Cdd:cd14547    80 EKCAQYWPEEENE--TYGDFEVTVQSVKETDGYTVRKLTLKY--GGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 487 -KQASmvkalgdtwaghPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCH 565
Cdd:cd14547   156 aRQTE------------PHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 331-565 3.79e-70

catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type tyrosine-protein phosphatase H (PTPRH or R-PTP-H), also known as stomach cancer-associated protein tyrosine phosphatase 1 (SAP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRH is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is localized specifically at microvilli of the brush border in gastrointestinal epithelial cells. It plays a role in intestinal immunity by regulating CEACAM20 through tyrosine dephosphorylation. It is also a negative regulator of integrin-mediated signaling and may contribute to contact inhibition of cell growth and motility.


Pssm-ID: 350467 [Multi-domain]  Cd Length: 233  Bit Score: 225.92  E-value: 3.79e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 331 NRYTDVLCYDHSRVVLSR---EDGEDYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGRV 407
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPiheEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 408 KCGQYWePTENSSLEFGNFHVRTLSIEINEDYTVASLELKNLKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREK 487
Cdd:cd14619    81 KCEHYW-PLDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQW 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1098626536 488 QASmvkalgdtwagHPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCH 565
Cdd:cd14619   160 LDQ-----------TMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLH 226
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 297-563 1.66e-68

catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein phosphatase non-receptor type 3 (PTPN3), also called protein-tyrosine phosphatase H1 (PTP-H1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN3 interacts with mitogen-activated protein kinase p38gamma and serves as its specific phosphatase. PTPN3 and p38gamma cooperate to promote Ras-induced oncogenesis. PTPN3 is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain. Its PDZ domain binds with the PDZ-binding motif of p38gamma and enables efficient tyrosine dephosphorylation.


Pssm-ID: 350448 [Multi-domain]  Cd Length: 274  Bit Score: 223.19  E-value: 1.66e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 297 EQGRKGLVK-----EYAEIRNRAPEGTFVYARMGNNLTKNRYTDVLCYDHSRVVLsrEDGEDYINANFVD----GYKQKN 367
Cdd:cd14600     5 AQLKKGLESgtvliQFEQLYRKKPGLAITCAKLPQNMDKNRYKDVLPYDATRVVL--QGNEDYINASYVNmeipSANIVN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 368 AYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGRVKCGQYWePTENSSLEFGNFHVRTLSIEINEDYTVASLELK 447
Cdd:cd14600    83 KYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYW-PDPPDVMEYGGFRVQCHSEDCTIAYVFREMLLT 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 448 NLKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQASMVkalgdtwaghprgpPIVVHCSAGIGRTGTFITLD- 526
Cdd:cd14600   162 NTQTGEERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRSKRVENE--------------PVLVHCSAGIGRTGVLVTMEt 227

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1098626536 527 -IC-ISRLEDVGTADIrgtVEKIRSQRAYSIQMPDQYVF 563
Cdd:cd14600   228 aMClTERNQPVYPLDI---VRKMRDQRAMMVQTSSQYKF 263
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 327-572 3.92e-68

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 223.34  E-value: 3.92e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 327 NLTKNRYTDVLCYDHSRVVLSREDG-EDYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERG 405
Cdd:PHA02742   52 NMKKCRYPDAPCFDRNRVILKIEDGgDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDG 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 406 RVKCGQYWEPTENSSLEFGNFHVRTLSIEINEDYTVASLELKNLKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVR 485
Cdd:PHA02742  132 KEACYPYWMPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFVLAVR 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 486 EKQASmvKALGDTWAGHPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCH 565
Cdd:PHA02742  212 EADLK--ADVDIKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCY 289


                  ....*..
gi 1098626536 566 LALIEYA 572
Cdd:PHA02742  290 FIVLIFA 296
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 322-565 8.61e-68

catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type tyrosine-protein phosphatase O (PTPRO or R-PTP-O), also known as glomerular epithelial protein 1 or protein tyrosine phosphatase U2 (PTP-U2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRO is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is essential for sustaining the structure and function of foot processes by regulating tyrosine phosphorylation of podocyte proteins. It has been identified as a synaptic cell adhesion molecule (CAM) that serves as a potent initiator of synapse formation. It is also a tumor suppressor in several types of cancer, such as hepatocellular carcinoma, lung cancer, and breast cancer.


Pssm-ID: 350462 [Multi-domain]  Cd Length: 245  Bit Score: 220.53  E-value: 8.61e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 322 ARMGNNLTKNRYTDVLCYDHSRVVL---SREDGEDYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMT 398
Cdd:cd14614     7 ADLPVNRCKNRYTNILPYDFSRVKLvsmHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVML 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 399 TRVKERGRVKCGQYWePTENSSLEFGNFHVRTLSIEINEDYTVASLELKnlKTDEIRNVSHWQFTSWPDYGVPS--SAMA 476
Cdd:cd14614    87 TQCNEKRRVKCDHYW-PFTEEPVAYGDITVEMLSEEEQPDWAIREFRVS--YADEVQDVMHFNYTAWPDHGVPTanAAES 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 477 MLNFLQKVREKQasmVKALGdtwaghprgpPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQ 556
Cdd:cd14614   164 ILQFVQMVRQQA---VKSKG----------PMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQ 230


                  ....*....
gi 1098626536 557 MPDQYVFCH 565
Cdd:cd14614   231 TEEQYIFIH 239
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 333-570 8.83e-68

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the first PTP domain (repeat 1).


Pssm-ID: 350468 [Multi-domain]  Cd Length: 229  Bit Score: 219.81  E-value: 8.83e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 333 YTDVLCYDHSRVVLSREDG---EDYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGRVKC 409
Cdd:cd14620     1 YPNILPYDHSRVILSQLDGipcSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 410 GQYWepTENSSLEFGNFHVRTLSIEINEDYTVASLELKNLKTDEI---RNVSHWQFTSWPDYGVPSSAMAMLNFLQKvre 486
Cdd:cd14620    81 YQYW--PDQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDGCkapRLVTQLHFTSWPDFGVPFTPIGMLKFLKK--- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 487 kqasmVKALGDTWAGhprgpPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHL 566
Cdd:cd14620   156 -----VKSVNPVHAG-----PIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQ 225


                  ....
gi 1098626536 567 ALIE 570
Cdd:cd14620   226 ALLE 229
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 331-569 3.42e-67

catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type tyrosine-protein phosphatase V (PTPRV or R-PTP-V), also known as embryonic stem cell protein-tyrosine phosphatase (ES cell phosphatase) or osteotesticular protein-tyrosine phosphatase (OST-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRV is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. In rodents, it may play a role in the maintenance of pluripotency and may function in signaling pathways during bone remodeling. It is the only PTP whose function has been lost between rodent and human. The human OST-PTP gene is a pseudogene.


Pssm-ID: 350466 [Multi-domain]  Cd Length: 230  Bit Score: 218.27  E-value: 3.42e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 331 NRYTDVLCYDHSRVVLSREDGE---DYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGRV 407
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEphsDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 408 KCGQYWePTENSSLEFGNFHVRTLSIEINEDYTVASLELKNLKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREk 487
Cdd:cd14618    81 LCDHYW-PSESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVRE- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 488 QASMVKALGdtwaghprgpPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLA 567
Cdd:cd14618   159 HVQATKGKG----------PTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSC 228


                  ..
gi 1098626536 568 LI 569
Cdd:cd14618   229 IL 230
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 305-570 2.13e-66

catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein phosphatase non-receptor type 18 (PTPN18), also called brain-derived phosphatase, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. The N-terminal catalytic PTP domain of PTPN18 blocks lysosomal routing and delays the degradation of HER2 by dephosphorylation, and its C-terminal PEST domain promotes K48-linked HER2 ubiquitination and its destruction via the proteasome pathway.


Pssm-ID: 350451 [Multi-domain]  Cd Length: 266  Bit Score: 217.39  E-value: 2.13e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 305 KEYAEIRNRAP----EGTFVYARMGN--NLTKNRYTDVLCYDHSRVVLS---REDGEDYINANFVDGYKQKNAYISTQGP 375
Cdd:cd14603     2 GEFSEIRACSAafkaDYVCSTVAGGRkeNVKKNRYKDILPYDQTRVILSllqEEGHSDYINANFIKGVDGSRAYIATQGP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 376 LPKTSQDFWRMIWEQHCLVVVMTTRVKERGRVKCGQYWePTENSSLEFGNFHVRTL-SIEINEDYTVASLELKnlKTDEI 454
Cdd:cd14603    82 LSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYW-AQEQEPLQTGPFTITLVkEKRLNEEVILRTLKVT--FQKES 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 455 RNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQASmvkalgDTwaghprgPPIVVHCSAGIGRTGTFITLDIcISRL-- 532
Cdd:cd14603   159 RSVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGS------GP-------EPLCVHCSAGCGRTGVICTVDY-VRQLll 224

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1098626536 533 -----EDVGTADIrgtVEKIRSQRAYSIQMPDQYVFCHLALIE 570
Cdd:cd14603   225 tqripPDFSIFDV---VLEMRKQRPAAVQTEEQYEFLYHTVAQ 264
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 354-569 6.32e-66

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the catalytic PTP domain (repeat 1).


Pssm-ID: 350506 [Multi-domain]  Cd Length: 209  Bit Score: 214.07  E-value: 6.32e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 354 YINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGRVKCGQYWePTENSSlEFGNFHVRTLSI 433
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYW-PADGSE-EYGNFLVTQKSV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 434 EINEDYTVASLELKNLKTDE--------IRNVSHWQFTSWPDYGVPSSAMAMLNFlqkVREKQASMVKALGdtwaghprg 505
Cdd:cd17668    79 QVLAYYTVRNFTLRNTKIKKgsqkgrpsGRVVTQYHYTQWPDMGVPEYTLPVLTF---VRKASYAKRHAVG--------- 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1098626536 506 pPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALI 569
Cdd:cd17668   147 -PVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 288-571 7.50e-66

PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type tyrosine-protein phosphatase S (PTPRS), also known as receptor-type tyrosine-protein phosphatase sigma (R-PTP-sigma), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRS is a receptor for glycosaminoglycans, including heparan sulfate proteoglycan and neural chondroitin sulfate proteoglycans (CSPGs), which present a barrier to axon regeneration. It also plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. PTPRS contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350475 [Multi-domain]  Cd Length: 290  Bit Score: 216.91  E-value: 7.50e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 288 IEQIVQMVKEQGRKGLVKEYAEIRN-RAPEGTFVYARMGNNLTKNRYTDVLCYDHSRVVLSR---EDGEDYINANFVDGY 363
Cdd:cd14627    13 IQKLAQVEVGEHVTGMELEFKRLANsKAHTSRFISANLPCNKFKNRLVNIMPYETTRVCLQPirgVEGSDYINASFIDGY 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 364 KQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGRVKCGQYWePTENSSlEFGNFHVRTLSIEINEDYTVAS 443
Cdd:cd14627    93 RQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYW-PAERSA-RYQYFVVDPMAEYNMPQYILRE 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 444 LELKNLKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQASMvkalgdtwaghPRGPPIVVHCSAGIGRTGTFI 523
Cdd:cd14627   171 FKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQF-----------GQDGPISVHCSAGVGRTGVFI 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1098626536 524 TLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIEY 571
Cdd:cd14627   240 TLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEY 287
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 331-566 2.62e-65

catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type tyrosine-protein phosphatase B (PTPRB), also known as receptor-type tyrosine-protein phosphatase beta (R-PTP-beta) or vascular endothelial protein tyrosine phosphatase(VE-PTP), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRB/VE-PTP is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It is expressed specifically in vascular endothelial cells and it plays an important role in blood vessel remodeling and angiogenesis.


Pssm-ID: 350465 [Multi-domain]  Cd Length: 228  Bit Score: 213.24  E-value: 2.62e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 331 NRYTDVLCYDHSRVVLSRED---GEDYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGRV 407
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDddpCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 408 KCGQYWePTENSSLEFGNFHVRTLSIEINEDYTVASLELKNL-KTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVRe 486
Cdd:cd14617    81 KCDHYW-PADQDSLYYGDLIVQMLSESVLPEWTIREFKICSEeQLDAPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVR- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 487 kqasmvkalgDTWAGHPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHL 566
Cdd:cd14617   159 ----------DYINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 354-570 2.97e-65

catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) and type 13 (PTPN13, also known as PTPL1) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization. Human PTPN13 is an important regulator of tumor aggressiveness.


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 212.23  E-value: 2.97e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 354 YINANFV--DGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGRVKCGQYW-EPTENSSLEFGNFHVRT 430
Cdd:cd14538     1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWpDSLNKPLICGGRLEVSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 431 LSIEINEDYTVASLELKNLKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREkqasmvkaLGDTWaghprgpPIVV 510
Cdd:cd14538    81 EKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRR--------IHNSG-------PIVV 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 511 HCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIE 570
Cdd:cd14538   146 HCSAGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLE 205
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 327-570 3.27e-65

catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350478 [Multi-domain]  Cd Length: 237  Bit Score: 213.35  E-value: 3.27e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 327 NLTKNRYTDVLCYDHSRVVLSREDGE---DYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKE 403
Cdd:cd14630     3 NRNKNRYGNIISYDHSRVRLQLLDGDphsDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 404 RGRVKCGQYWePTENSSleFGNFHVRTLSIEINEDYTVASLELKNLKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQK 483
Cdd:cd14630    83 VGRVKCVRYW-PDDTEV--YGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVRQ 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 484 VRekqasmvkalgdtWAGHPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVF 563
Cdd:cd14630   160 VK-------------FLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVF 226


                  ....*..
gi 1098626536 564 CHLALIE 570
Cdd:cd14630   227 VHDAILE 233
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 327-571 5.98e-65

catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein phosphatase non-receptor type 11 (PTPN11), also called SH2 domain-containing tyrosine phosphatase 2 (SHP-2 or SHP2), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN11 promotes the activation of the RAS/Mitogen-Activated Protein Kinases (MAPK) Extracellular-Regulated Kinases 1/2 (ERK1/2) pathway, a canonical signaling cascade that plays key roles in various cellular processes, including proliferation, survival, differentiation, migration, or metabolism. It also regulates the phosphoinositide 3-kinase (PI3K)/AKT pathway, a fundamental cascade that functions in cell survival, proliferation, migration, morphogenesis, and metabolism. PTPN11 dysregulation is associated with several developmental diseases and malignancies, such as Noonan syndrome and juvenile myelomonocytic leukemia. It contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350453 [Multi-domain]  Cd Length: 253  Bit Score: 213.34  E-value: 5.98e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 327 NLTKNRYTDVLCYDHSRVVLS----REDGEDYINANFV--------DGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLV 394
Cdd:cd14605     2 NKNKNRYKNILPFDHTRVVLHdgdpNEPVSDYINANIImpefetkcNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 395 VVMTTRVKERGRVKCGQYWePTENSSLEFGNFHVRTLSIEINEDYTVASLELKNL-KTDEIRNVSHWQFTSWPDYGVPSS 473
Cdd:cd14605    82 IVMTTKEVERGKSKCVKYW-PDEYALKEYGVMRVRNVKESAAHDYILRELKLSKVgQGNTERTVWQYHFRTWPDHGVPSD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 474 AMAMLNFLQKVREKQASMVKAlgdtwaghprgPPIVVHCSAGIGRTGTFITLDICISRLEDVGT---ADIRGTVEKIRSQ 550
Cdd:cd14605   161 PGGVLDFLEEVHHKQESIMDA-----------GPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQ 229

                         250       260
                  ....*....|....*....|.
gi 1098626536 551 RAYSIQMPDQYVFCHLALIEY 571
Cdd:cd14605   230 RSGMVQTEAQYRFIYMAVQHY 250
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 302-563 8.03e-65

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 214.87  E-value: 8.03e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 302 GLVK-EYAEIRNRAPEGTFVYARMGNNLTKNRYTDVLCYDHSRVVLSREDGE--DYINANFVDGYKQKNAYISTQGPLPK 378
Cdd:PHA02747   25 GIIRdEHHQIILKPFDGLIANFEKPENQPKNRYWDIPCWDHNRVILDSGGGStsDYIHANWIDGFEDDKKFIATQGPFAE 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 379 TSQDFWRMIWEQHCLVVVMTTRVKE-RGRVKCGQYWEPTENSSLEFGNFHVRTLSIEINEDYTVASLELKNLKTDEIRNV 457
Cdd:PHA02747  105 TCADFWKAVWQEHCSIIVMLTPTKGtNGEEKCYQYWCLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKI 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 458 SHWQFTSWPDYGVPSSA---MAMLNFLQKVREKQASMVKALGDTWAghprgpPIVVHCSAGIGRTGTFITLDICISRLED 534
Cdd:PHA02747  185 SHFQCSEWFEDETPSDHpdfIKFIKIIDINRKKSGKLFNPKDALLC------PIVVHCSDGVGKTGIFCAVDICLNQLVK 258

                         250       260
                  ....*....|....*....|....*....
gi 1098626536 535 VGTADIRGTVEKIRSQRAYSIQMPDQYVF 563
Cdd:PHA02747  259 RKAICLAKTAEKIREQRHAGIMNFDDYLF 287
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 288-571 1.30e-64

PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type tyrosine-protein phosphatase-like D (PTPRD), also known as receptor-type tyrosine-protein phosphatase delta (R-PTP-delta), belongs to the LAR (leukocyte common antigen-related) family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. LAR-RPTPs are synaptic adhesion molecules that play roles in various aspects of neuronal development, including axon guidance, neurite extension, and synapse formation and function. PTPRD is involved in pre-synaptic differentiation through interaction with SLITRK2. It contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350476 [Multi-domain]  Cd Length: 292  Bit Score: 213.82  E-value: 1.30e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 288 IEQIVQMVKEQGRKGLVKEYAEI-RNRAPEGTFVYARMGNNLTKNRYTDVLCYDHSRVVLSR---EDGEDYINANFVDGY 363
Cdd:cd14628    12 IQKLTQIETGENVTGMELEFKRLaSSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPirgVEGSDYINASFIDGY 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 364 KQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGRVKCGQYWePTENSSlEFGNFHVRTLSIEINEDYTVAS 443
Cdd:cd14628    92 RQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYW-PAERSA-RYQYFVVDPMAEYNMPQYILRE 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 444 LELKNLKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQASMvkalgdtwaghPRGPPIVVHCSAGIGRTGTFI 523
Cdd:cd14628   170 FKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQF-----------GQDGPISVHCSAGVGRTGVFI 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1098626536 524 TLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIEY 571
Cdd:cd14628   239 TLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEY 286
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 354-565 1.99e-63

fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae protein-tyrosine phosphatases 1 (PTP1) and 2 (PTP2), Schizosaccharomyces pombe PTP1, PTP2, and PTP3, and similar fungal proteins. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. PTP2, together with PTP3, is the major phosphatase that dephosphorylates and inactivates the MAP kinase HOG1 and also modulates its subcellular localization.


Pssm-ID: 350509 [Multi-domain]  Cd Length: 212  Bit Score: 207.49  E-value: 1.99e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 354 YINANFVD-GYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGRVKCGQYWePTENSSLEFGNFHVRTLS 432
Cdd:cd18533     1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYW-PSGEYEGEYGDLTVELVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 433 IEINED--YTVASLELKNlKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQASmvkalgdtwagHPRGPPIVV 510
Cdd:cd18533    80 EEENDDggFIVREFELSK-EDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDS-----------ASLDPPIIV 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1098626536 511 HCSAGIGRTGTFITLDICISRLEDVGTAD---------IRGTVEKIRSQRAYSIQMPDQYVFCH 565
Cdd:cd18533   148 HCSAGVGRTGTFIALDSLLDELKRGLSDSqdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLY 211
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 327-571 2.07e-63

catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein phosphatase non-receptor type 6 (PTPN6), also called SH2 domain-containing protein-tyrosine phosphatase 1 (SHP1 or SHP-1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN6 expression is restricted mainly to hematopoietic and epithelial cells. It is an important regulator of hematopoietic cells, downregulating pathways that promote cell growth, survival, adhesion, and activation. It regulates glucose homeostasis by modulating insulin signalling in the liver and muscle, and it also negatively regulates bone resorption, affecting both the formation and the function of osteoclasts. PTPN6 contains two tandem SH2 domains, a catalytic PTP domain, and a C-terminal tail with regulatory properties.


Pssm-ID: 350454 [Multi-domain]  Cd Length: 266  Bit Score: 209.74  E-value: 2.07e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 327 NLTKNRYTDVLCYDHSRVVLSRED----GEDYINANFV------DGYKQKNaYISTQGPLPKTSQDFWRMIWEQHCLVVV 396
Cdd:cd14606    18 NKSKNRYKNILPFDHSRVILQGRDsnipGSDYINANYVknqllgPDENAKT-YIASQGCLEATVNDFWQMAWQENSRVIV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 397 MTTRVKERGRVKCGQYWePTENSSLEFGNFHVRTLSIEINEDYTVASLELKNL-KTDEIRNVSHWQFTSWPDYGVPSSAM 475
Cdd:cd14606    97 MTTREVEKGRNKCVPYW-PEVGMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLdNGELIREIWHYQYLSWPDHGVPSEPG 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 476 AMLNFLQKVREKQASMvkalgdtwaghPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGT---ADIRGTVEKIRSQRA 552
Cdd:cd14606   176 GVLSFLDQINQRQESL-----------PHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRS 244

                         250
                  ....*....|....*....
gi 1098626536 553 YSIQMPDQYVFCHLALIEY 571
Cdd:cd14606   245 GMVQTEAQYKFIYVAIAQF 263
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 327-571 4.43e-63

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).


Pssm-ID: 350469 [Multi-domain]  Cd Length: 296  Bit Score: 209.88  E-value: 4.43e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 327 NLTKNRYTDVLCYDHSRVVLSREDG---EDYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKE 403
Cdd:cd14621    52 NKEKNRYVNILPYDHSRVHLTPVEGvpdSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKE 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 404 RGRVKCGQYWepTENSSLEFGNFHVRTLSIEINEDYTVASL------ELKNLKTDeiRNVSHWQFTSWPDYGVPSSAMAM 477
Cdd:cd14621   132 RKECKCAQYW--PDQGCWTYGNIRVSVEDVTVLVDYTVRKFciqqvgDVTNKKPQ--RLITQFHFTSWPDFGVPFTPIGM 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 478 LNFLQKvrekqasmVKALGDTWAGhprgpPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQM 557
Cdd:cd14621   208 LKFLKK--------VKNCNPQYAG-----AIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQT 274

                         250
                  ....*....|....
gi 1098626536 558 PDQYVFCHLALIEY 571
Cdd:cd14621   275 DMQYVFIYQALLEH 288
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 354-565 2.55e-62

catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 1.


Pssm-ID: 350405 [Multi-domain]  Cd Length: 201  Bit Score: 204.29  E-value: 2.55e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 354 YINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGRVKCGQYWEPTENSSLEFGNFHVRTLSI 433
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKINEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 434 EINEDYTVASLELKNLKTD-EIRNVSHWQFTSWPDYGVPSSAmamlNFLQKVREKqasmVKALGDTWAGhprgpPIVVHC 512
Cdd:cd14557    81 KICPDYIIRKLNINNKKEKgSGREVTHIQFTSWPDHGVPEDP----HLLLKLRRR----VNAFNNFFSG-----PIVVHC 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1098626536 513 SAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCH 565
Cdd:cd14557   148 SAGVGRTGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 354-572 3.83e-62

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21) and type 14 (PTPN14) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Both PTPN21 and PTPN14 contain an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350388 [Multi-domain]  Cd Length: 219  Bit Score: 204.61  E-value: 3.83e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 354 YINANFVD---GYKQKNaYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGRVKCGQYWePTENS---SLEFGNFH 427
Cdd:cd14540     1 YINASHITatvGGKQRF-YIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYW-PTLGGehdALTFGEYK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 428 VRTLSIEINEDYTVASLELKNLKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVRekqaSMVKALGDTWAGHPRGPP 507
Cdd:cd14540    79 VSTKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEIN----SVRRHTNQDVAGHNRNPP 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1098626536 508 IVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIEYA 572
Cdd:cd14540   155 TLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 312-571 7.17e-62

PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type tyrosine-protein phosphatase F (PTPRF), also known as leukocyte common antigen related (LAR), is the prototypical member of the LAR family of receptor-type tyrosine-protein phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRF/LAR plays a role for LAR in cadherin complexes where it associates with and dephosphorylates beta-catenin, a pathway which may be critical for cadherin complex stability and cell-cell association. It also regulates focal adhesions through cyclin-dependent kinase-1 and is involved in axon guidance in the developing nervous system. It also functions in regulating insulin signaling. PTPRF contains an extracellular region with three immunoglobulin-like (Ig) domains and four to eight fibronectin type III (FN3) repeats (determined by alternative splicing), a single transmembrane domain, followed by an intracellular region with a membrane-proximal catalytic PTP domain (repeat 1, also called D1) and a membrane-distal non-catalytic PTP-like domain (repeat 2, also called D2). This model represents the non-catalytic PTP-like domain (repeat 2). Although described as non-catalytic, this domain contains the catalytic cysteine and the active site signature motif, HCSAGxGRxG.


Pssm-ID: 350477 [Multi-domain]  Cd Length: 291  Bit Score: 206.50  E-value: 7.17e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 312 NRAPEGTFVYARMGNNLTKNRYTDVLCYDHSRVVLSR---EDGEDYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIW 388
Cdd:cd14629    38 SKAHTSRFISANLPCNKFKNRLVNIMPYELTRVCLQPirgVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLW 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 389 EQHCLVVVMTTRVKERGRVKCGQYWePTENSSlEFGNFHVRTLSIEINEDYTVASLELKNLKTDEIRNVSHWQFTSWPDY 468
Cdd:cd14629   118 EHNSTIVVMLTKLREMGREKCHQYW-PAERSA-RYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQ 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 469 GVPSSAMAMLNFLQKVREKQASMvkalgdtwaghPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIR 548
Cdd:cd14629   196 GVPKTGEGFIDFIGQVHKTKEQF-----------GQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLR 264

                         250       260
                  ....*....|....*....|...
gi 1098626536 549 SQRAYSIQMPDQYVFCHLALIEY 571
Cdd:cd14629   265 TQRPAMVQTEDQYQLCYRAALEY 287
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 329-571 1.87e-61

catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein phosphatase non-receptor type 7 (PTPN7), also called hematopoietic protein-tyrosine phosphatase (HePTP) or LC-PTP. belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN7/HePTP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. PTPN7/HePTP is found exclusively in the white blood cells in bone marrow, thymus, spleen, lymph nodes and all myeloid and lymphoid cell lines. It negatively regulates T-cell activation and proliferation, and is often dysregulated in the preleukemic disorder myelodysplastic syndrome, as well as in acute myelogenous leukemia.


Pssm-ID: 350460 [Multi-domain]  Cd Length: 247  Bit Score: 203.91  E-value: 1.87e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 329 TKNRYTDVLCYDHSRVVLSR----EDGEDYINANFVDGYKQK-NAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKE 403
Cdd:cd14612    17 SKDRYKTILPNPQSRVCLRRagsqEEEGSYINANYIRGYDGKeKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKE 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 404 RgRVKCGQYWePTENSSleFGNFHVRTLSIEINEDYTVASLELKNlkTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQK 483
Cdd:cd14612    97 K-KEKCVHYW-PEKEGT--YGRFEIRVQDMKECDGYTIRDLTIQL--EEESRSVKHYWFSSWPDHQTPESAGPLLRLVAE 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 484 VREKQASmvkalgdtwAGHPrgPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVF 563
Cdd:cd14612   171 VEESRQT---------AASP--GPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQF 239


                  ....*...
gi 1098626536 564 CHLALIEY 571
Cdd:cd14612   240 LHHTLALY 247
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 354-570 2.26e-61

catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The type II (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350403 [Multi-domain]  Cd Length: 204  Bit Score: 202.07  E-value: 2.26e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 354 YINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGRVKCGQYW-EPTENssleFGNFHVRTLS 432
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWpDDTEV----YGDIKVTLVE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 433 IEINEDYTVASLELKNLKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQAsmvkalgdtwaghPRGPPIVVHC 512
Cdd:cd14555    77 TEPLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNP-------------PSAGPIVVHC 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1098626536 513 SAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIE 570
Cdd:cd14555   144 SAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 315-570 2.37e-61

PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type tyrosine-protein phosphatase N2 (PTPRN2 or R-PTP-N2), also called islet cell autoantigen-related protein (IAR), ICAAR, phogrin, or IA-2beta, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. It is mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells. It may function as a phosphatidylinositol phosphatase to regulate insulin secretion. It is also required for normal accumulation of the neurotransmitters norepinephrine, dopamine and serotonin in the brain.


Pssm-ID: 350458 [Multi-domain]  Cd Length: 283  Bit Score: 204.91  E-value: 2.37e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 315 PEGTFVyARMGNNLTKNRYTDVLCYDHSRVVLSRE---DGEDYINANFVDGYKQKN-AYISTQGPLPKTSQDFWRMIWEQ 390
Cdd:cd14610    33 PNATNV-AQREENVQKNRSLAVLPYDHSRIILKAEnshSHSDYINASPIMDHDPRNpAYIATQGPLPATVADFWQMVWES 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 391 HCLVVVMTTRVKERGRVKCGQYWePTENSSLeFGNFHVRTLSIEI-NEDYTVASLELKNLKTDEIRNVSHWQFTSWPDYG 469
Cdd:cd14610   112 GCVVIVMLTPLAENGVKQCYHYW-PDEGSNL-YHIYEVNLVSEHIwCEDFLVRSFYLKNLQTNETRTVTQFHFLSWNDQG 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 470 VPSSAMAMLNFLQKVREkqasmvkalgdTWAGhpRGPPIVVHCSAGIGRTGTFITLDICISRL-EDVGTADIRGTVEKIR 548
Cdd:cd14610   190 VPASTRSLLDFRRKVNK-----------CYRG--RSCPIIVHCSDGAGRSGTYILIDMVLNKMaKGAKEIDIAATLEHLR 256

                         250       260
                  ....*....|....*....|..
gi 1098626536 549 SQRAYSIQMPDQYVFCHLALIE 570
Cdd:cd14610   257 DQRPGMVQTKEQFEFALTAVAE 278
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 288-570 2.67e-61

catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350481 [Multi-domain]  Cd Length: 273  Bit Score: 204.12  E-value: 2.67e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 288 IEQIVQMVKEQGRkGLVKEYaEIRNRAPEGTFVYARMGNNLTKNRYTDVLCYDHSRVVLSREDGE---DYINANFVDGYK 364
Cdd:cd14633     3 LQHITQMKCAEGY-GFKEEY-ESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGEtssDYINGNYIDGYH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 365 QKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGRVKCGQYWeptENSSLEFGNFHVRTLSIEINEDYTVASL 444
Cdd:cd14633    81 RPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYW---PDDTEIYKDIKVTLIETELLAEYVIRTF 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 445 ELKNLKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQAsmvkalgdtwaghPRGPPIVVHCSAGIGRTGTFIT 524
Cdd:cd14633   158 AVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSP-------------PNAGPLVVHCSAGAGRTGCFIV 224

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1098626536 525 LDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIE 570
Cdd:cd14633   225 IDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILE 270
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 354-568 4.77e-61

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350400 [Multi-domain]  Cd Length: 202  Bit Score: 200.96  E-value: 4.77e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 354 YINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGRVKCGQYWePTEnSSLEFGNFHVRTLSI 433
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYW-PED-GSVSSGDITVELKDQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 434 EINEDYTVASLELKNLKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQAsmvkalgdtwagHPRGPPIVVHCS 513
Cdd:cd14552    79 TDYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQ------------QSGNHPITVHCS 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1098626536 514 AGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLAL 568
Cdd:cd14552   147 AGAGRTGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 354-563 1.76e-60

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; Receptor-type tyrosine-protein phosphatase A (PTPRA) and E (PTPRE) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA and PTPRE share several functions including regulation of Src family kinases and voltage-gated potassium (Kv) channels. They both contain a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the first catalytic PTP domain (repeat 1).


Pssm-ID: 350399 [Multi-domain]  Cd Length: 202  Bit Score: 199.75  E-value: 1.76e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 354 YINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGRVKCGQYWepTENSSLEFGNFHVRTLSI 433
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYW--PDQGCWTYGNLRVRVEDT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 434 EINEDYTVASLELKNLKTD----EIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREkqasmvkalgdtwAGHPRGPPIV 509
Cdd:cd14551    79 VVLVDYTTRKFCIQKVNRGigekRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKS-------------ANPPRAGPIV 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1098626536 510 VHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVF 563
Cdd:cd14551   146 VHCSAGVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVF 199
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 298-570 2.27e-58

PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type tyrosine-protein phosphatase-like N (PTPRN or R-PTP-N), also called islet cell antigen 512 (ICA512) or PTP IA-2, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). It consists of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. PTPRN is located in secretory granules of neuroendocrine cells and is involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. It is a major autoantigen in type 1 diabetes and is involved in the regulation of insulin secretion.


Pssm-ID: 350457 [Multi-domain]  Cd Length: 281  Bit Score: 196.80  E-value: 2.27e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 298 QGRKGLVKEY-AEIRNRAPEGTFVYARMGNNLTKNRYTDVLCYDHSRVVLSREDG---EDYINAN-FVDGYKQKNAYIST 372
Cdd:cd14609    12 RNRDRLAKEWqALCAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNpsrSDYINASpIIEHDPRMPAYIAT 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 373 QGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGRVKCGQYWePTENSSLeFGNFHVRTLSIEI-NEDYTVASLELKNLKT 451
Cdd:cd14609    92 QGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYW-PDEGSSL-YHIYEVNLVSEHIwCEDFLVRSFYLKNVQT 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 452 DEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREkqasmvkalgdTWAGhpRGPPIVVHCSAGIGRTGTFITLDICISR 531
Cdd:cd14609   170 QETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNK-----------CYRG--RSCPIIVHCSDGAGRTGTYILIDMVLNR 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1098626536 532 L-EDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIE 570
Cdd:cd14609   237 MaKGVKEIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAE 276
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 354-570 3.64e-58

PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type tyrosine-protein phosphatase-like N (PTPRN) and N2 (PTPRN2) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). They consist of a large ectodomain that contains a RESP18HD (regulated endocrine-specific protein 18 homology domain), followed by a transmembrane segment, and a single, catalytically-impaired, PTP domain. They are mainly expressed in neuropeptidergic neurons and peptide-secreting endocrine cells, including insulin-producing pancreatic beta-cells, and are involved in involved in the generation, cargo storage, traffic, exocytosis and recycling of insulin secretory granules, as well as in beta-cell proliferation. They also are major autoantigens in type 1 diabetes and are involved in the regulation of insulin secretion.


Pssm-ID: 350394 [Multi-domain]  Cd Length: 208  Bit Score: 193.81  E-value: 3.64e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 354 YINANFVDGYKQKN-AYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGRVKCGQYWePTENSSLeFGNFHVRTLS 432
Cdd:cd14546     1 YINASTIYDHDPRNpAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYW-PEEGSEV-YHIYEVHLVS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 433 IEI-NEDYTVASLELKNLKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQasmvkalgdtwagHPRGPPIVVH 511
Cdd:cd14546    79 EHIwCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSY-------------RGRSCPIVVH 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 512 CSAGIGRTGTFITLDICISRL-EDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIE 570
Cdd:cd14546   146 CSDGAGRTGTYILIDMVLNRMaKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 331-565 4.38e-58

catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type tyrosine-protein phosphatase Q (PTPRQ or R-PTP-Q), also called phosphatidylinositol phosphatase PTPRQ, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRQ is a member of the R3 subfamily of receptor-type phosphotyrosine phosphatases (RPTP), characterized by a unique modular composition consisting of multiple extracellular fibronectin type III (FN3) repeats (18 in PTPRQ) and a single (most RPTP subtypes have two) cytoplasmic catalytic PTP domain. It displays low tyrosine-protein phosphatase activity; rather, it functions as a phosphatidylinositol phosphatase required for auditory processes. It regulates the levels of phosphatidylinositol 4,5-bisphosphate (PIP2) in the basal region of hair bundles. It can dephosphorylate a broad range of phosphatidylinositol phosphates, including phosphatidylinositol 3,4,5-trisphosphate and most phosphatidylinositol monophosphates and diphosphates.


Pssm-ID: 350464 [Multi-domain]  Cd Length: 224  Bit Score: 193.97  E-value: 4.38e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 331 NRYTDVLCYDHSRVVLSRE---DGEDYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGRV 407
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADagvPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 408 KCGQYWePTENSSLE-FGNFHVRTLSIEINEDYTVASLELKnlKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVRE 486
Cdd:cd14616    81 RCHQYW-PEDNKPVTvFGDIVITKLMEDVQIDWTIRDLKIE--RHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVRA 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1098626536 487 KQAsmvkalGDTwaghprgPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCH 565
Cdd:cd14616   158 SRA------HDN-------TPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 332-570 7.29e-58

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type tyrosine-protein phosphatase A (PTPRA), also known as receptor-type tyrosine-protein phosphatase alpha (R-PTP-alpha), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRA is a positive regulator of Src and Src family kinases via dephosphorylation of the Src-inhibitory tyrosine 527. Thus, it affects transformation and tumorigenesis, inhibition of proliferation, cell cycle arrest, integrin signaling, neuronal differentiation and outgrowth, and ion channel activity. It is also involved in interleukin-1 signaling in fibroblasts through its interaction with the focal adhesion targeting domain of focal adhesion kinase. PTPRA comprises a small extracellular domain, a transmembrane segment, and an intracellular region containing two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350471 [Multi-domain]  Cd Length: 228  Bit Score: 193.72  E-value: 7.29e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 332 RYTDVLCYDHSRVVLSREDGE---DYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGRVK 408
Cdd:cd14623     1 RVLQIIPYEFNRVIIPVKRGEentDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 409 CGQYWePTEnSSLEFGNFHVRTLSIEINEDYTVASLELKNLKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQ 488
Cdd:cd14623    81 CAQYW-PSD-GSVSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQ 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 489 ASMvkalgdtwAGHprgpPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLAL 568
Cdd:cd14623   159 QQS--------GNH----PITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVV 226


                  ..
gi 1098626536 569 IE 570
Cdd:cd14623   227 QE 228
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 327-565 1.26e-57

catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein phosphatase non-receptor type 13 (PTPN13, also known as PTPL1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN13 is an important regulator of tumor aggressiveness. It regulates breast cancer cell aggressiveness through direct inactivation of Src kinase. In hepatocellular carcinoma, PTPN13 is a tumor suppressor. PTPN13 contains a FERM domain, five PDZ domains, and a C-terminal catalytic PTP domain. With its PDZ domains, PTPN13 has numerous interacting partners that can actively participate in the regulation of its phosphatase activity or can permit direct or indirect recruitment of tyrosine phosphorylated substrates. Its FERM domain is necessary for localization to the membrane.


Pssm-ID: 350445 [Multi-domain]  Cd Length: 234  Bit Score: 193.12  E-value: 1.26e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 327 NLTKNRYTDVLCYDHSRVVLSREDGedYINANFVD---GyKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKE 403
Cdd:cd14597     3 NRKKNRYKNILPYDTTRVPLGDEGG--YINASFIKmpvG-DEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEVE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 404 RGRVKCGQYWEPTENSSLEFGN-FHVRTLSIEINEDYTVASLELKNLKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQ 482
Cdd:cd14597    80 GGKIKCQRYWPEILGKTTMVDNrLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLLTFIS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 483 KVREKqasmvkalgdtwagHPRGpPIVVHCSAGIGRTGTFITLDIC---ISRLEDVgtaDIRGTVEKIRSQRAYSIQMPD 559
Cdd:cd14597   160 YMRHI--------------HKSG-PIITHCSAGIGRSGTLICIDVVlglISKDLDF---DISDIVRTMRLQRHGMVQTED 221


                  ....*.
gi 1098626536 560 QYVFCH 565
Cdd:cd14597   222 QYIFCY 227
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 353-571 1.30e-57

catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein phosphatase non-receptor type 4 (PTPN4), also called protein-tyrosine phosphatase MEG1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN4 functions in TCR cell signaling, apoptosis, cerebellar synaptic plasticity, and innate immune responses. It specifically inhibits the TRIF-dependent TLR4 pathway by suppressing tyrosine phosphorylation of TRAM. It is a large modular protein containing an N-terminal FERM domain, a PDZ domain and a C-terminal catalytic PTP domain; the PDZ domain regulates the catalytic activity of PTPN4.


Pssm-ID: 350449 [Multi-domain]  Cd Length: 212  Bit Score: 192.47  E-value: 1.30e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 353 DYINANFVD----GYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGRVKCGQYW-EPTENSSleFGNFH 427
Cdd:cd14601     1 DYINANYINmeipSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWpEPSGSSS--YGGFQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 428 VRTLSIEINEDYTVASLELKNLKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQasmvkalgdtwAGHPRgpP 507
Cdd:cd14601    79 VTCHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKR-----------AGKDE--P 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1098626536 508 IVVHCSAGIGRTGTFITLDICISRLE---DVGTADIrgtVEKIRSQRAYSIQMPDQYVF-CHLALIEY 571
Cdd:cd14601   146 VVVHCSAGIGRTGVLITMETAMCLIEcnqPVYPLDI---VRTMRDQRAMMIQTPSQYRFvCEAILKVY 210
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 343-570 1.62e-57

catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350479 [Multi-domain]  Cd Length: 218  Bit Score: 192.54  E-value: 1.62e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 343 RVVLS---REDGEDYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGRVKCGQYWepTENS 419
Cdd:cd14631     1 RVILQpveDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYW--PDDT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 420 SLeFGNFHVRTLSIEINEDYTVASLELKNLKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVRekqasmvkalgdtW 499
Cdd:cd14631    79 EV-YGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVK-------------L 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1098626536 500 AGHPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIE 570
Cdd:cd14631   145 SNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 354-570 3.36e-57

catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350480 [Multi-domain]  Cd Length: 205  Bit Score: 191.03  E-value: 3.36e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 354 YINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGRVKCGQYWEPTENSsleFGNFHVRTLSI 433
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDT---YGDIKITLLKT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 434 EINEDYTVASLELKNLKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQAsmvkalgdtwaghPRGPPIVVHCS 513
Cdd:cd14632    78 ETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTP-------------PDAGPVVVHCS 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1098626536 514 AGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIE 570
Cdd:cd14632   145 AGAGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 354-570 7.31e-57

catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein phosphatase non-receptor type 20 (PTPN20) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN20 is a widely expressed phosphatase with a dynamic subcellular distribution that is targeted to sites of actin polymerization.


Pssm-ID: 350444 [Multi-domain]  Cd Length: 207  Bit Score: 190.34  E-value: 7.31e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 354 YINANFVDGY--KQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGRVKCGQYWEPTENSSLEFGNFHVRTL 431
Cdd:cd14596     1 YINASYITMPvgEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLRLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 432 SIEINEDYTVASLELKNLKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREkqasmVKALGdtwaghprgpPIVVH 511
Cdd:cd14596    81 NYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRK-----VHNTG----------PIVVH 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1098626536 512 CSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIE 570
Cdd:cd14596   146 CSAGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLE 204
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 306-571 1.34e-56

catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein phosphatase non-receptor type 14 (PTPN14), also called protein-tyrosine phosphatase pez, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN14 is a potential tumor suppressor and plays a regulatory role in the Hippo and Wnt/beta-catenin signaling pathways. It contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350447 [Multi-domain]  Cd Length: 287  Bit Score: 192.13  E-value: 1.34e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 306 EYAEIRNRAPEGTFVYARMGNNLTKNRYTDVLCYDHSRVVL--SREDGEDYINANF----VDGykQKNAYISTQGPLPKT 379
Cdd:cd14599    17 EYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELvpTKENNTGYINASHikvtVGG--EEWHYIATQGPLPHT 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 380 SQDFWRMIWEQHCLVVVMTTRVKERGRVKCGQYWEP--TENSSLEFGNFHVRTLSIEINEDYTVASLELKNLKTDEIRNV 457
Cdd:cd14599    95 CHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKlgSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTV 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 458 SHWQFTSWPDYGVPSSAMAMLNFL---QKVREKQASMVKALGDtwaghpRGPPIVVHCSAGIGRTGTFITLDICISRLED 534
Cdd:cd14599   175 WHLQYTDWPDHGCPEEVQGFLSYLeeiQSVRRHTNSMLDSTKN------CNPPIVVHCSAGVGRTGVVILTELMIGCLEH 248

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1098626536 535 VGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIEY 571
Cdd:cd14599   249 NEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQF 285
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 330-571 9.74e-56

catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein phosphatase non-receptor type 5 (PTPN5), also called striatum-enriched protein-tyrosine phosphatase (STEP) or neural-specific PTP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN5/STEP is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. It is a CNS-enriched protein that regulates key signaling proteins required for synaptic strengthening, as well as NMDA and AMPA receptor trafficking. PTPN5 is implicated in multiple neurologic and neuropsychiatric disorders, such as Alzheimer's disease, Parkinson's disease, schizophrenia, and fragile X syndrome.


Pssm-ID: 350461 [Multi-domain]  Cd Length: 258  Bit Score: 188.92  E-value: 9.74e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 330 KNRYTDVLCYDHSRVVLSREDGED----YINANFVDGY-KQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKER 404
Cdd:cd14613    28 KNRYKTILPNPHSRVCLTSPDQDDplssYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 405 GRvKCGQYWePTEnsSLEFGNFHVRTLSIEINEDYtvaSLELKNLKTD-EIRNVSHWQFTSWPDYGVPSSAMAMLNFLQK 483
Cdd:cd14613   108 NE-KCTEYW-PEE--QVTYEGIEITVKQVIHADDY---RLRLITLKSGgEERGLKHYWYTSWPDQKTPDNAPPLLQLVQE 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 484 VREKQASmvkalgdtwaGHPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVF 563
Cdd:cd14613   181 VEEARQQ----------AEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQF 250


                  ....*...
gi 1098626536 564 CHLALIEY 571
Cdd:cd14613   251 VHHVLSLY 258
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 330-570 2.20e-55

catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), also called lymphoid phosphatase (LyP), PEST-domain phosphatase (PEP), or hematopoietic cell protein-tyrosine phosphatase 70Z-PEP, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. Mutations in the PTPN22 gene are associated with multiple connective tissue and autoimmune diseases including type 1 diabetes mellitus, rheumatoid arthritis, and systemic lupus erythematosus. PTPN22 contains an N-terminal catalytic PTP domain and four proline-rich regions at the C-terminus.


Pssm-ID: 350450 [Multi-domain]  Cd Length: 234  Bit Score: 187.35  E-value: 2.20e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 330 KNRYTDVLCYDHSRVVLS---REDGEDYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGR 406
Cdd:cd14602     1 KNRYKDILPYDHSRVELSlitSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 407 VKCGQYWEPTENSSLEFGNFHVRTLSIEINEDYTVASLELKNLKtdEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVRE 486
Cdd:cd14602    81 KKCERYWAEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNS--ETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRC 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 487 KQasmvkalgdtwagHPRGPPIVVHCSAGIGRTGTFITLDICISRLED---VGTADIRGTVEKIRSQRAYSIQMPDQYVF 563
Cdd:cd14602   159 YQ-------------EDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDgiiPENFSVFSLIQEMRTQRPSLVQTKEQYEL 225


                  ....*..
gi 1098626536 564 CHLALIE 570
Cdd:cd14602   226 VYNAVIE 232
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 353-571 2.84e-55

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type tyrosine-protein phosphatase E (PTPRE), also known as receptor-type tyrosine-protein phosphatase epsilon (R-PTP-epsilon), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. The PTPRE gene contains two distinct promoters that generate the two major isoforms: transmembrane (receptor type RPTPe or PTPeM) and cytoplasmic (cyt-PTPe or PTPeC). Receptor type RPTPe plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells, and may also play a role in osteoclast formation and function. It also negatively regulates PDGFRbeta-mediated signaling pathways that are crucial for the pathogenesis of atherosclerosis. cyt-PTPe acts as a negative regulator of insulin receptor signaling in skeletal muscle. It regulates insulin-induced phosphorylation of proteins downstream of the insulin receptor. Receptor type RPTPe contains a small extracellular region, a single transmembrane segment, and an intracellular region two tandem catalytic PTP domains. This model represents the second PTP domain (repeat 2).


Pssm-ID: 350470 [Multi-domain]  Cd Length: 205  Bit Score: 185.98  E-value: 2.84e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 353 DYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGRVKCGQYWePTEnSSLEFGNFHVRTLS 432
Cdd:cd14622     1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYW-PSE-GSVTHGEITIEIKN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 433 IEINEDYTVASLELKNLKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQASMvkalgdtwAGHprgpPIVVHC 512
Cdd:cd14622    79 DTLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQT--------GNH----PIVVHC 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1098626536 513 SAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIEY 571
Cdd:cd14622   147 SAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 327-568 4.08e-54

catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein phosphatase non-receptor type 12 (PTPN12), also called PTP-PEST or protein-tyrosine phosphatase G1 (PTPG1), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling. It regulates various physiological processes, including cell migration, immune response, and neuronal activity, by dephosphorylating multiple substrates including HER2, FAK, PYK2, PSTPIP, WASP, p130Cas, paxillin, Shc, catenin, c-Abl, ArgBP2, p190RhoGAP, RhoGDI, cell adhesion kinase beta, and Rho GTPase.


Pssm-ID: 350452 [Multi-domain]  Cd Length: 297  Bit Score: 185.91  E-value: 4.08e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 327 NLTKNRYTDVLCYDHSRVVL----SREDgEDYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVK 402
Cdd:cd14604    57 NVKKNRYKDILPFDHSRVKLtlktSSQD-SDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREF 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 403 ERGRVKCGQYWEPTENSSLEFGNFHVRTLSIEINEDYTVASL--ELKNlktdEIRNVSHWQFTSWPDYGVPSSAMAMLNF 480
Cdd:cd14604   136 EMGRKKCERYWPLYGEEPMTFGPFRISCEAEQARTDYFIRTLllEFQN----ETRRLYQFHYVNWPDHDVPSSFDSILDM 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 481 LQKVREKQASmvkalgdtwaghpRGPPIVVHCSAGIGRTGTFITLDICISRL------EDVGTADIrgtVEKIRSQRAYS 554
Cdd:cd14604   212 ISLMRKYQEH-------------EDVPICIHCSAGCGRTGAICAIDYTWNLLkagkipEEFNVFNL---IQEMRTQRHSA 275

                         250
                  ....*....|....
gi 1098626536 555 IQMPDQYVFCHLAL 568
Cdd:cd14604   276 VQTKEQYELVHRAI 289
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 354-565 8.38e-54

protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis thaliana protein tyrosine phosphatase 1 (AtPTP1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. AtPTP1 dephosphorylates and inhibits MAP kinase 6 (MPK6) in non-oxidative stress conditions. Together with MAP kinase phosphatase 1 (MKP1) it expresses salicylic acid (SA) and camalexin biosynthesis, and therefore, modulating defense response.


Pssm-ID: 350496 [Multi-domain]  Cd Length: 206  Bit Score: 181.89  E-value: 8.38e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 354 YINANFVDGYKQKN--AYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGR-VKCGQYWEPTENSSLEFGNFHVRT 430
Cdd:cd17658     1 YINASLVETPASESlpKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStAKCADYFPAEENESREFGRISVTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 431 LSIEINED-YTVASLELKNLKTDE-IRNVSHWQFTSWPDYGVPSSAMAmlnflqkVREkqasMVKALgdtWAGHPRGPPI 508
Cdd:cd17658    81 KKLKHSQHsITLRVLEVQYIESEEpPLSVLHIQYPEWPDHGVPKDTRS-------VRE----LLKRL---YGIPPSAGPI 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1098626536 509 VVHCSAGIGRTGTFITLDICISR--LEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCH 565
Cdd:cd17658   147 VVHCSAGIGRTGAYCTIHNTIRRilEGDMSAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 354-565 2.32e-53

catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; Tyrosine-protein phosphatase non-receptor type 22 (PTPN22), type 18 (PTPN18) and type 12 (PTPN12) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN22 is expressed in hematopoietic cells and it functions as a key regulator of immune homeostasis by inhibiting T-cell receptor signaling through the direct dephosphorylation of Src family kinases (Lck and Fyn), ITAMs of the TCRz/CD3 complex, and other signaling molecules. TPN18 regulates HER2-mediated cellular functions through defining both its phosphorylation and ubiquitination states. PTPN12 is characterized as a tumor suppressor and a pivotal regulator of EGFR/HER2 signaling.


Pssm-ID: 350390 [Multi-domain]  Cd Length: 202  Bit Score: 180.70  E-value: 2.32e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 354 YINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGRVKCGQYWEPTENSSLEFGNFHVRTLSI 433
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLQFGPFKISLEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 434 E-INEDYTVASLELKnlKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQASmvkalgdtwaghpRGPPIVVHC 512
Cdd:cd14542    81 KrVGPDFLIRTLKVT--FQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGS-------------EDVPICVHC 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1098626536 513 SAGIGRTGTFITLDICISRL------EDVGTADIrgtVEKIRSQRAYSIQMPDQYVFCH 565
Cdd:cd14542   146 SAGCGRTGTICAIDYVWNLLktgkipEEFSLFDL---VREMRKQRPAMVQTKEQYELVY 201
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 329-565 2.95e-52

catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type tyrosine-protein phosphatase-like R (PTPRR or R-PTP-R), also called protein-tyrosine phosphatase PCPTP1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRR is a kinase interaction motif (KIM)-PTP, characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. The human and mouse PTPRR gene produces multiple neuronal protein isoforms of varying sizes (in human, PTPPBS-alpha, beta, gamma and delta). All isoforms contain the KIM motif and the catalytic PTP domain. PTPRR-deficient mice show significant defects in fine motor coordination and balance skills that are reminiscent of a mild ataxia.


Pssm-ID: 350459 [Multi-domain]  Cd Length: 226  Bit Score: 178.57  E-value: 2.95e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 329 TKNRYTDVLCYDHSRVVLSREDGED----YINANFVDGYK-QKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKE 403
Cdd:cd14611     1 TKNRYKTILPNPHSRVCLKPKNSNDslstYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 404 RGRvKCGQYWepTENSSLeFGNFHVRTLSIEINEDYTVASLELKNlkTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQK 483
Cdd:cd14611    81 KNE-KCVLYW--PEKRGI-YGKVEVLVNSVKECDNYTIRNLTLKQ--GSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLD 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 484 VREKQASmvkalgdtWAGhpRGPpIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVF 563
Cdd:cd14611   155 VEEDRLA--------SPG--RGP-VVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEF 223


                  ..
gi 1098626536 564 CH 565
Cdd:cd14611   224 VH 225
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 354-565 3.70e-48

PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 2.


Pssm-ID: 350406 [Multi-domain]  Cd Length: 203  Bit Score: 166.80  E-value: 3.70e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 354 YINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGRVKCGQYWEPTENSsleFGNFHVRTLSI 433
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKT---YGDIEVELKDT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 434 EINEDYTVASLELKNLKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQasmvkalGDTWAGHPRGPPIVVHCS 513
Cdd:cd14558    78 EKSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKL-------PYKNSKHGRSVPIVVHCS 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1098626536 514 AGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCH 565
Cdd:cd14558   151 DGSSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 354-565 9.28e-47

PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein phosphatase non-receptor type 23 (PTPN23), also called His domain-containing protein tyrosine phosphatase (HD-PTP) or protein tyrosine phosphatase TD14 (PTP-TD14), is a catalytically inactive member of the tyrosine-specific protein tyrosine phosphatase (PTP) family. Human PTPN23 may be involved in the regulation of small nuclear ribonucleoprotein assembly and pre-mRNA splicing by modifying the survival motor neuron (SMN) complex. It plays a role in ciliogenesis and is part of endosomal sorting complex required for transport (ESCRT) pathways. PTPN23 contains five domains: a BRO1-like domain that plays a role in endosomal sorting; a V-domain that interacts with Lys63-linked polyubiquitinated substrates; a central proline-rich region that might recruit SH3-containing proteins; a PTP-like domain; and a proteolytic degradation-targeting motif, also known as a PEST sequence.


Pssm-ID: 350387 [Multi-domain]  Cd Length: 205  Bit Score: 163.32  E-value: 9.28e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 354 YINANFVDGYKQKNA-YISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGRVKCGQYWePTE-NSSLEFGNFHVRTL 431
Cdd:cd14539     1 YINASLIEDLTPYCPrFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYW-PTErGQALVYGAITVSLQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 432 SIEINEDYTVASLELKNLKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVRE---KQASMVKalgdtwaghprgpPI 508
Cdd:cd14539    80 SVRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHShylQQRSLQT-------------PI 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1098626536 509 VVHCSAGIGRTGTFITLDICISRLE-DVGTADIRGTVEKIRSQRAYSIQMPDQYVFCH 565
Cdd:cd14539   147 VVHCSSGVGRTGAFCLLYAAVQEIEaGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCY 204
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 354-565 1.20e-45

PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The type IIb (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350404 [Multi-domain]  Cd Length: 201  Bit Score: 159.88  E-value: 1.20e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 354 YINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGRvKCGQYWepTENSSLEFGNFHVRTLSI 433
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQ-SCPQYW--PDEGSGTYGPIQVEFVST 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 434 EINEDYTVASLELKNLKTDE--IRNVSHWQFTSWPDYG-VPSSAMAMLNFLQKVrekqasmvkalgDTWAGHPRGPPIVV 510
Cdd:cd14556    78 TIDEDVISRIFRLQNTTRPQegYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEV------------EKWQEQSGEGPIVV 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1098626536 511 HCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCH 565
Cdd:cd14556   146 HCLNGVGRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 354-571 4.19e-43

catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21), also called protein-tyrosine phosphatase D1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN21 is a component of a multivalent scaffold complex nucleated by focal adhesion kinase (FAK) at specific intracellular sites. It promotes cytoskeleton events that induce cell adhesion and migration by modulating Src-FAK signaling. It can also selectively associate with and stimulate Tec family kinases and modulate Stat3 activation. Human PTPN21 may also play a pathologic role in gastrointestinal tract tumorigenesis. PTPN21 contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350446 [Multi-domain]  Cd Length: 220  Bit Score: 153.98  E-value: 4.19e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 354 YINANFVD---GYKQKNaYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGRVKCGQYWE--PTENSSLEFGNFHV 428
Cdd:cd14598     1 YINASHIKvtvGGKEWD-YIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlGSRHNTVTYGRFKI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 429 RTLSIEINEDYTVASLELKNLKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVRekqaSMVKALGDTWAGHPRGPPI 508
Cdd:cd14598    80 TTRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQ----SVRRHTNSTIDPKSPNPPV 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1098626536 509 VVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIEY 571
Cdd:cd14598   156 LVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQF 218
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 457-570 7.58e-36

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: 129.79  E-value: 7.58e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536  457 VSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQAsmvkalgdtwaGHPRGPPIVVHCSAGIGRTGTFITLDICISRLED-V 535
Cdd:smart00012   2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLN-----------QSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAeA 70

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1098626536  536 GTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIE 570
Cdd:smart00012  71 GEVDIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
457-570 7.58e-36

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 129.79  E-value: 7.58e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536  457 VSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQAsmvkalgdtwaGHPRGPPIVVHCSAGIGRTGTFITLDICISRLED-V 535
Cdd:smart00404   2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLN-----------QSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAeA 70

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1098626536  536 GTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIE 570
Cdd:smart00404  71 GEVDIFDTVKELRSQRPGMVQTEEQYLFLYRALLE 105
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
326-576 7.81e-35

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 132.91  E-value: 7.81e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 326 NNLTKNRYTDVLCYDHSRVvlsREDGEdYINANFVDGyKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKE-- 403
Cdd:COG5599    41 NGSPLNRFRDIQPYKETAL---RANLG-YLNANYIQV-IGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEis 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 404 RGRVKCGQYWEPTEnsslEFGNFHVRTL---SIEINEDYTVASLELKNLKTD-EIRNVSHWQFTSWPDYGVPSSAmAMLN 479
Cdd:COG5599   116 KPKVKMPVYFRQDG----EYGKYEVSSElteSIQLRDGIEARTYVLTIKGTGqKKIEIPVLHVKNWPDHGAISAE-ALKN 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 480 FLQKVREKQasmvkalgdTWAGHPRGPPiVVHCSAGIGRTGTFItLDICISRLEDVGTaDIRGTVEKI----RSQRAYSI 555
Cdd:COG5599   191 LADLIDKKE---------KIKDPDKLLP-VVHCRAGVGRTGTLI-ACLALSKSINALV-QITLSVEEIvidmRTSRNGGM 258

                         250       260
                  ....*....|....*....|..
gi 1098626536 556 -QMPDQYVFchlaLIEYAVSRG 576
Cdd:COG5599   259 vQTSEQLDV----LVKLAEQQI 276
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 354-563 8.54e-32

PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 subfamily of receptor-type phosphotyrosine phosphatases (RPTP) is composed of receptor-type tyrosine-protein phosphatase Z (PTPRZ) and G (PTPRG). They belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. They are type 1 integral membrane proteins consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350398 [Multi-domain]  Cd Length: 200  Bit Score: 122.04  E-value: 8.54e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 354 YINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGrvKCGQYWePTENSSLEFGNFHVR---- 429
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYW-PTKEKPLECETFKVTlsge 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 430 -TLSIEINEDYTVASLELKNLKTDEIRNVSHWQFTSWPDYGVPSSamAMLNFLQKVREKQASmvkalgdtwaghpRGPPI 508
Cdd:cd14550    78 dHSCLSNEIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIH--TVFELINTVQEWAQQ-------------RDGPI 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1098626536 509 VVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVF 563
Cdd:cd14550   143 VVHDRYGGVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQF 197
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 354-570 3.66e-31

PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350483 [Multi-domain]  Cd Length: 206  Bit Score: 120.56  E-value: 3.66e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 354 YINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGRvkCGQYWepTENSSLEFGNFHVRTLSI 433
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQL--CPQYW--PENGVHRHGPIQVEFVSA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 434 EINEDYTVASLELKNLK--TDEIRNVSHWQFTSWPDY-GVPSSAMAMLNFLQKVREKQASMVKALGDTwaghprgppiVV 510
Cdd:cd14635    77 DLEEDIISRIFRIYNAArpQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEYNGGEGRT----------VV 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 511 HCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIE 570
Cdd:cd14635   147 HCLNGGGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 303-571 6.32e-31

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 122.38  E-value: 6.32e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 303 LVKEYAEIRNRAPEGtfvyARMGNNLTKNRYTD------VLCYDHSRVVLsREDGEdYINANFVDGYKQKNAYISTQGPL 376
Cdd:PHA02740   27 IIKEYRAIVPEHEDE----ANKACAQAENKAKDenlalhITRLLHRRIKL-FNDEK-VLDARFVDGYDFEQKFICIINLC 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 377 PKTSQDFWRMIWEQHCLVVVMTTRVKERgrvKC-GQYWEPTENSSLEFGNFHVRTLSIEINEDYTVASLELKNLKTDEiR 455
Cdd:PHA02740  101 EDACDKFLQALSDNKVQIIVLISRHADK---KCfNQFWSLKEGCVITSDKFQIETLEIIIKPHFNLTLLSLTDKFGQA-Q 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 456 NVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQASMVKALGDTWAGhprgpPIVVHCSAGIGRTGTFITLDICISRLEDV 535
Cdd:PHA02740  177 KISHFQYTAWPADGFSHDPDAFIDFFCNIDDLCADLEKHKADGKIA-----PIIIDCIDGISSSAVFCVFDICATEFDKT 251

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1098626536 536 GTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIEY 571
Cdd:PHA02740  252 GMLSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAY 287
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 354-570 1.31e-30

PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type tyrosine-protein phosphatase T (PTPRT), also known as receptor-type tyrosine-protein phosphatase rho (RPTP-rho or PTPrho), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRT is highly expressed in the nervous system and it plays a critical role in regulation of synaptic formation and neuronal development. It dephosphorylates a specific tyrosine residue in syntaxin-binding protein 1, a key component of synaptic vesicle fusion machinery, and regulates its binding to syntaxin 1. PTPRT has been identified as a potential candidate gene for autism spectrum disorder (ASD) susceptibility. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350482 [Multi-domain]  Cd Length: 206  Bit Score: 118.97  E-value: 1.31e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 354 YINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGRvkCGQYWepTENSSLEFGNFHVRTLSI 433
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAAQL--CMQYW--PEKTSCCYGPIQVEFVSA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 434 EINEDYTVASLELKNLK--TDEIRNVSHWQFTSWPDY-GVPSSAMAMLNFLQKVREKQASMVKALGDTwaghprgppiVV 510
Cdd:cd14634    77 DIDEDIISRIFRICNMArpQDGYRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQYDGREGRT----------VV 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 511 HCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIE 570
Cdd:cd14634   147 HCLNGGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 354-565 7.34e-26

PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type tyrosine-protein phosphatase K (PTPRK), also known as receptor-type tyrosine-protein phosphatase kappa (RPTP-kappa or PTPkappa), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRK is widely expressed and has been shown to stimulate cell motility and neurite outgrowth. It is required for anti-proliferative and pro-migratory effects of TGF-beta, suggesting a role in regulation, maintenance, and restoration of cell adhesion. It is a potential tumour suppressor in primary central nervous system lymphomas, colorectal cancer, and breast cancer. It contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350484 [Multi-domain]  Cd Length: 206  Bit Score: 105.49  E-value: 7.34e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 354 YINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVK-ERGrvkCGQYWepTENSSLEFGNFHVRTLS 432
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDlAQG---CPQYW--PEEGMLRYGPIQVECMS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 433 IEINEDYTVASLELKNLKTDE--IRNVSHWQFTSWPDY-GVPSSAMAMLNFLQKVREKQASMVKALGDTwaghprgppiV 509
Cdd:cd14636    76 CSMDCDVISRIFRICNLTRPQegYLMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEECDEGEGRT----------I 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1098626536 510 VHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCH 565
Cdd:cd14636   146 IHCLNGGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCY 201
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 354-570 3.17e-25

PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type tyrosine-protein phosphatase U (PTPRU), also known as pancreatic carcinoma phosphatase 2 (PCP-2), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRU/PCP-2 is the most distant member of the type IIb subfamily and may have a distinct biological function other than cell-cell aggregation. It localizes to the adherens junctions and directly binds and dephosphorylates beta-catenin, and regulates the balance between signaling and adhesive beta-catenin. It plays an important role in the maintenance of epithelial integrity. PTPRU contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the second (repeat 2) PTP domain.


Pssm-ID: 350485 [Multi-domain]  Cd Length: 207  Bit Score: 103.45  E-value: 3.17e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 354 YINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGRV-KCGQYWepTENSSLEFGNFHVRTLS 432
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYW--PEPGLQQYGPMEVEFVS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 433 IEINEDYTVASLELKNLK--TDEIRNVSHWQFTSWPDY-GVPSSAMAMLNFLQKVrekqasmvkalgDTWAGHPRGPPIV 509
Cdd:cd14637    79 GSADEDIVTRLFRVQNITrlQEGHLMVRHFQFLRWSAYrDTPDSKKAFLHLLASV------------EKWQRESGEGRTV 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1098626536 510 VHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIE 570
Cdd:cd14637   147 VHCLNGGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 354-569 4.20e-21

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type tyrosine-protein phosphatase Z (PTPRZ), also called receptor-type tyrosine-protein phosphatase zeta (R-PTP-zeta), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Three isoforms are generated by alternative splicing from a single PTPRZ gene: two transmembrane isoforms, PTPRZ-A and PTPRZ-B, and one secretory isoform, PTPRZ-S (also known as phosphacan); all are preferentially expressed in the central nervous system (CNS) as chondroitin sulfate (CS) proteoglycans. PTPRZ isoforms play important roles in maintaining oligodendrocyte precursor cells in an undifferentiated state. PTPRZ is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350507 [Multi-domain]  Cd Length: 204  Bit Score: 91.59  E-value: 4.20e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 354 YINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGRVKCgQYWePTENSSLEFGNFHVRTLS- 432
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYW-PNKDEPINCETFKVTLIAe 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 433 ----IEINEDYTVASLELKNLKTDEIRNVSHWQFTSWPDYGVPSSamAMLNFLQKVREKQASmvkalgdtwaghpRGPPI 508
Cdd:cd17669    79 ehkcLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPIS--KTFELISIIKEEAAN-------------RDGPM 143

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1098626536 509 VVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALI 569
Cdd:cd17669   144 IVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 354-569 9.27e-21

PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type tyrosine-protein phosphatase G (PTPRG), also called protein-tyrosine phosphatase gamma (R-PTP-gamma), belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRG is an important tumor suppressor gene in multiple human cancers such as lung, ovarian, and breast cancers. It is widely expressed in many tissues, including the central nervous system, where it plays a role during neuroinflammation processes. It can dephosphorylate platelet-derived growth factor receptor beta (PDGFRB) and may play a role in PDGFRB-related infantile myofibromatosis. PTPRG is a type 1 integral membrane protein consisting of an extracellular region with a carbonic anhydrase-like (CAH) and a fibronectin type III (FN3) domains, and an intracellular region with a catalytic PTP domain (repeat 1) proximal to the membrane, and a catalytically inactive PTP-fold domain (repeat 2) distal to the membrane. This model represents the inactive PTP-like domain (repeat 2).


Pssm-ID: 350508 [Multi-domain]  Cd Length: 205  Bit Score: 90.89  E-value: 9.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 354 YINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVM---TTRVKERGRVkcgqYWePTENSSLEFGNFHVRT 430
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMlpdNQGLAEDEFV----YW-PSREESMNCEAFTVTL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 431 LS-----IEINEDYTVASLELKNLKTDEIRNVSHWQFTSWPDYGVP-SSAMAMLNFLqkvreKQASMVkalgdtwaghpR 504
Cdd:cd17670    76 ISkdrlcLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELINVI-----KEEALT-----------R 139

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1098626536 505 GPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALI 569
Cdd:cd17670   140 DGPTIVHDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
 12-70 5.80e-12

Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p) and in RhoGAPs, RhoGEFs and the RasGAP, neurofibromin (NF1). Lipid-binding domain. The SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 214706 [Multi-domain]  Cd Length: 158  Bit Score: 63.86  E-value: 5.80e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1098626536   12 YPARLKKVLIVTAPLWFKAPFKILRLFVREKLRERVFTVS---VPTLGLHVPLKALPLHLGG 70
Cdd:smart00516  94 YPERLGKVYIINPPWFFRVLWKIIKPFLDEKTREKIRFVGndsKEELLEYIDKEQLPEELGG 155
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
 12-70 7.74e-12

Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory proteins, such as S. cerevisiae phosphatidylinositol transfer protein (Sec14p), and in lipid regulated proteins such as RhoGAPs, RhoGEFs and neurofibromin (NF1). SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 469559 [Multi-domain]  Cd Length: 156  Bit Score: 63.51  E-value: 7.74e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1098626536  12 YPARLKKVLIVTAPLWFKAPFKILRLFVREKLRERVFTVS--VPTLGLHVPLKALPLHLGG 70
Cdd:cd00170    95 YPERLKKIYIVNAPWIFSALWKIVKPFLSEKTRKKIVFLGsdLEELLEYIDPDQLPKELGG 155
CRAL_TRIO pfam00650
CRAL/TRIO domain;
1-70 4.37e-10

CRAL/TRIO domain;


Pssm-ID: 459890 [Multi-domain]  Cd Length: 151  Bit Score: 58.42  E-value: 4.37e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1098626536   1 MRINSTIEKGGYPARLKKVLIVTAPLWFKAPFKILRLFVREKLRERVF---TVSVPTLGLHVPLKALPLHLGG 70
Cdd:pfam00650  79 LKKIIKILQDNYPERLGKILIVNAPWIFNTIWKLIKPFLDPKTREKIVflkNSNEEELEKYIPPEQLPKEYGG 151
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 331-523 1.92e-09

YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. YopH is an essential virulence determinant of the pathogenic bacterium by dephosphorylating several focal adhesion proteins including p130Cas in human epithelial cells, resulting in the disruption of focal adhesions and cell detachment from the extracellular matrix. It contains an N-terminal domain that contains signals required for TTSS-mediated delivery of YopH into host cells and a C-terminal catalytic PTP domain.


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 58.18  E-value: 1.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 331 NRYTDVlcydHSRVvlSREDGEDyINANFVDgYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVVVMTTRVKERGRVKCG 410
Cdd:cd14559     1 NRFTNI----QTRV--STPVGKN-LNANRVQ-IGNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 411 QYWEPTEnsslEFGNFHVRTLSIEINEDYTVASLELKNLKTDEIRN-----VSHwqFTSWPDYG-VPSSAMAML-NFLQK 483
Cdd:cd14559    73 PYFRQSG----TYGSVTVKSKKTGKDELVDGLKADMYNLKITDGNKtitipVVH--VTNWPDHTaISSEGLKELaDLVNK 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1098626536 484 VREKQASMVKALGDTWAGHPRGPPIVVHCSAGIGRTGTFI 523
Cdd:cd14559   147 SAEEKRNFYKSKGSSAINDKNKLLPVIHCRAGVGRTGQLA 186
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 504-565 3.66e-09

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: 54.66  E-value: 3.66e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1098626536 504 RGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTAdirgtVEKIRSQR-AYSIQMPDQYVFCH 565
Cdd:cd14494    55 PGEPVLVHCKAGVGRTGTLVACYLVLLGGMSAEEA-----VRIVRLIRpGGIPQTIEQLDFLI 112
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
465-563 2.77e-07

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 49.97  E-value: 2.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 465 WPDYGVPSsamamlnflqkvrekQASMVKALGDTWAGHPRGPPIVVHCSAGIGRTGTFItldICISRLEDVGTADIrgtV 544
Cdd:COG2453    55 IPDFGAPD---------------DEQLQEAVDFIDEALREGKKVLVHCRGGIGRTGTVA---AAYLVLLGLSAEEA---L 113

                          90
                  ....*....|....*....
gi 1098626536 545 EKIRSQRAYSIQMPDQYVF 563
Cdd:COG2453   114 ARVRAARPGAVETPAQRAF 132
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 455-565 2.11e-05

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: 45.80  E-value: 2.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 455 RNVSHWQFtSWPDYGVPSsamamLNFLQKVREKQASMVKALGDtwaghprgppIVVHCSAGIGRTGTFITldiCI-SRLE 533
Cdd:cd14506    75 AGIYFYNF-GWKDYGVPS-----LTTILDIVKVMAFALQEGGK----------VAVHCHAGLGRTGVLIA---CYlVYAL 135

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1098626536 534 DVGTADirgTVEKIRSQRAYSIQMPDQYVFCH 565
Cdd:cd14506   136 RMSADQ---AIRLVRSKRPNSIQTRGQVLCVR 164
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 466-565 4.95e-05

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: 43.79  E-value: 4.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 466 PDYGVPSSamamLNFLQKVREkqaSMVKALGDtwaghprGPPIVVHCSAGIGRTGTfitldICISRLEDVG-TADIRGTV 544
Cdd:cd14505    81 PDGGVPSD----IAQWQELLE---ELLSALEN-------GKKVLIHCKGGLGRTGL-----IAACLLLELGdTLDPEQAI 141

                          90       100
                  ....*....|....*....|.
gi 1098626536 545 EKIRSQRAYSIQMPDQYVFCH 565
Cdd:cd14505   142 AAVRALRPGAIQTPKQENFLH 162
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 466-560 1.25e-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: 42.26  E-value: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 466 PDYGVPSsamamlnflqkvREKQASMVKALGDTWAghpRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTAdirgtVE 545
Cdd:cd14504    58 EDYTPPT------------LEQIDEFLDIVEEANA---KNEAVLVHCLAGKGRTGTMLACYLVKTGKISAVDA-----IN 117

                          90
                  ....*....|....*
gi 1098626536 546 KIRSQRAYSIQMPDQ 560
Cdd:cd14504   118 EIRRIRPGSIETSEQ 132
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
 12-76 3.12e-04

Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain family. This family includes ECM25 that contains a divergent CRAL-TRIO domain identified by Gallego and colleagues.


Pssm-ID: 463965 [Multi-domain]  Cd Length: 140  Bit Score: 41.16  E-value: 3.12e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1098626536  12 YPARLKKVLIVTAPLWFKAPFKIL-RLFVREKLRERVFTVS-VPTLGLHVPLKALPLHLGGGLEIDH 76
Cdd:pfam13716  73 FKKNLKAVYVVHPSTFLRTFLKTLgSLLGSKKLRKKVHYVSsLSELWEGIDREQLPTELPGVLSYDE 139
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 424-523 5.28e-03

protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar proteins; Phosphatase and tensin homolog (PTEN) is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It dephosphorylates phosphoinositide trisphosphate. In addition to PTEN, this family includes tensins, voltage-sensitive phosphatases (VSPs), and auxilins. They all contain a protein tyrosine phosphatase-like domain although not all are active phosphatases. Tensins are intracellular proteins that act as links between the extracellular matrix and the cytoskeleton, and thereby mediate signaling for cell shape and motility, and they may or may not have phosphatase activity. VSPs are phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. Auxilins are J domain-containing proteins that facilitate Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles, and they do not exhibit phosphatase activity.


Pssm-ID: 350347 [Multi-domain]  Cd Length: 160  Bit Score: 37.94  E-value: 5.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1098626536 424 GNFHVRTLSIEINEDYTVasleLKNlktdeirNVSHWqftSWPDYGVPSsamamLNFLQKVrekqasmVKALgDTW-AGH 502
Cdd:cd14497    41 DHYMIFNLSEEEYDDDSK----FEG-------RVLHY---GFPDHHPPP-----LGLLLEI-------VDDI-DSWlSED 93

                          90       100
                  ....*....|....*....|.
gi 1098626536 503 PRGPpIVVHCSAGIGRTGTFI 523
Cdd:cd14497    94 PNNV-AVVHCKAGKGRTGTVI 113
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH