NCBI Conserved Domain Search

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...

2063-2266

4.66e-154

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: 474.10 E-value: 4.66e-154

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2063 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDEFVYWPNKDEPINCESFKVTLMAEEH 2142
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFVYWPNKDEPINCETFKVTLIAEEH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2143 KCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISVIKEEAANRDGPMIVHDEHGGVTAGTFCAL 2222
Cdd:cd17669     81 KCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCAL 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1609046161 2223 TTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVIL 2266
Cdd:cd17669    161 TTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204

alpha_CARP_receptor_like

cd03122

Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...

31-284

5.74e-113

Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related proteins (CARPs) are sequence similar to carbonic anhydrases. Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism. CARPs have lost conserved histidines involved in zinc binding and consequently their catalytic activity. This sub-family of carbonic anhydrase-related domains found in tyrosine phosphatase receptors may play a role in cell adhesion.

Pssm-ID: 239396 [Multi-domain] Cd Length: 253 Bit Score: 359.36 E-value: 5.74e-113

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161   31 NQKNWGKKYPTCNS-PKQSPINIDEDlTQVNVN-LKKLKFQGWDKTSLEnTFIHNTGKTVEINLTN---DYRVSGGVSEM 105
Cdd:cd03122      1 NPKHWAKKYPACGEgRQQSPIDIVED-TQVQRQgLQPLHFDGYEELTAS-TTLENTGKTVILRLEGnssDPFVSGGPLLG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  106 VFKASKITFHWGKCNmsSDGSEHSLEGQKFPLEMQIYCFDADRFSSFEeAVKGKGKLRALSILFEVGTEENLDFKAIIDG 185
Cdd:cd03122     79 RYKFSEITFHWGTCN--SDGSEHSIDGHKFPLEMQILHRNTDFFDSFE-AIKSPGGVLALAYLFELSHEDNPFLDPIIEG 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  186 VESVSRFGKQAALDPFILLNLLPNSTDKYYIYNGSLTSPPCTDTVDWIVFKDTVSISESQLAVFCEVLTMQQSGyVMLMD 265
Cdd:cd03122    156 LRNVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRQDG-VMSGD 234

                          250
                   ....*....|....*....
gi 1609046161  266 YLQNNFREQQYKFSRQVFS 284
Cdd:cd03122    235 YLPNNGRPQQPLGSRTVFS 253

fn3

pfam00041

Fibronectin type III domain;

299-387

1.60e-09

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 56.65 E-value: 1.60e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  299 SEPENVQADPENYTSLLVTWERPRVVYDTmIEKFAVLYQQLDGEDQtKHEFLTDGYQDlGAILNNLLPNMSYVLQIVAIC 378
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGP-ITGYEVEYRPKNSGEP-WNEITVPGTTT-SVTLTGLKPGTEYEVRVQAVN 77


                   ....*....
gi 1609046161  379 TNGlYGKYS 387
Cdd:pfam00041   78 GGG-EGPPS 85

Name

Accession

Description

Interval

E-value

R-PTPc-G-1

cd17667

catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...

1703-1980

2.13e-160

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: 494.94 E-value: 2.13e-160

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1703 FTEEFEtlkefyqEVQSCTVDLGITADSSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGKLTDYINANYVDGYNRPKA 1782
Cdd:cd17667      1 FSEDFE-------EVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKA 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1783 YIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQVLAYYTVRNFTLRNTK 1862
Cdd:cd17667     74 YIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTK 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1863 IKKGSQ---KGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQI 1939
Cdd:cd17667    154 VKKGQKgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQI 233

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1609046161 1940 QHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAIL 1980
Cdd:cd17667    234 KDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274

R-PTP-Z-2

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...

2063-2266

4.66e-154

Pssm-ID: 350507 [Multi-domain] Cd Length: 204 Bit Score: 474.10 E-value: 4.66e-154

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2063 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDEFVYWPNKDEPINCESFKVTLMAEEH 2142
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFVYWPNKDEPINCETFKVTLIAEEH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2143 KCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISVIKEEAANRDGPMIVHDEHGGVTAGTFCAL 2222
Cdd:cd17669     81 KCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCAL 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1609046161 2223 TTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVIL 2266
Cdd:cd17669    161 TTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204

PTPc

Protein tyrosine phosphatase, catalytic domain;

1702-1977

1.04e-118

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 375.84 E-value: 1.04e-118

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  1702 GFTEEFETLKEFYQEVQSCTVdlgitadsSNHPDNKHKNRYINIVAYDHSRVKLAQLaekDGKLTDYINANYVDGYNRPK 1781
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCTV--------AAFPENRDKNRYKDVLPYDHTRVKLKPP---PGEGSDYINASYIDGPNGPK 69

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  1782 AYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSE--EYGNFLVTQKSVQVLAYYTVRNFTLR 1859
Cdd:smart00194   70 AYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEplTYGDITVTLKSVEKVDDYTIRTLEVT 149

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  1860 NTkikkgsqkGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQI 1939
Cdd:smart00194  150 NT--------GCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQL 221

                           250       260       270
                    ....*....|....*....|....*....|....*...
gi 1609046161  1940 QHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1977
Cdd:smart00194  222 EAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259

alpha_CARP_receptor_like

cd03122

Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...

31-284

5.74e-113

Pssm-ID: 239396 [Multi-domain] Cd Length: 253 Bit Score: 359.36 E-value: 5.74e-113

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161   31 NQKNWGKKYPTCNS-PKQSPINIDEDlTQVNVN-LKKLKFQGWDKTSLEnTFIHNTGKTVEINLTN---DYRVSGGVSEM 105
Cdd:cd03122      1 NPKHWAKKYPACGEgRQQSPIDIVED-TQVQRQgLQPLHFDGYEELTAS-TTLENTGKTVILRLEGnssDPFVSGGPLLG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  106 VFKASKITFHWGKCNmsSDGSEHSLEGQKFPLEMQIYCFDADRFSSFEeAVKGKGKLRALSILFEVGTEENLDFKAIIDG 185
Cdd:cd03122     79 RYKFSEITFHWGTCN--SDGSEHSIDGHKFPLEMQILHRNTDFFDSFE-AIKSPGGVLALAYLFELSHEDNPFLDPIIEG 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  186 VESVSRFGKQAALDPFILLNLLPNSTDKYYIYNGSLTSPPCTDTVDWIVFKDTVSISESQLAVFCEVLTMQQSGyVMLMD 265
Cdd:cd03122    156 LRNVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRQDG-VMSGD 234

                          250
                   ....*....|....*....
gi 1609046161  266 YLQNNFREQQYKFSRQVFS 284
Cdd:cd03122    235 YLPNNGRPQQPLGSRTVFS 253

Y_phosphatase

Protein-tyrosine phosphatase;

1736-1977

1.06e-112

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 357.71 E-value: 1.06e-112

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1736 NKHKNRYINIVAYDHSRVKLaqlaEKDGKLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNL 1815
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKL----TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTEL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1816 VEKGRRKCDQYWP--ADGSEEYGNFLVT-QKSVQVLAYYTVRNFTLRNtkikkgsqKGRPSGRVVTQYHYTQWPDMGVPE 1892
Cdd:pfam00102   77 EEKGREKCAQYWPeeEGESLEYGDFTVTlKKEKEDEKDYTVRTLEVSN--------GGSEETRTVKHFHYTGWPDHGVPE 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1893 YSLPVLTFVRKAAYAKRHA-VGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFI 1971
Cdd:pfam00102  149 SPNSLLDLLRKVRKSSLDGrSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFL 228


                   ....*.
gi 1609046161 1972 HDTLVE 1977
Cdd:pfam00102  229 YDAILE 234

Carb_anhydrase

smart01057

Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...

24-281

5.84e-86

Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse the reversible hydration of carbon dioxide to bicarbonate.. CAs have essential roles in facilitating the transport of carbon dioxide and protons in the intracellular space, across biological membranes and in the layers of the extracellular space; they are also involved in many other processes, from respiration and photosynthesis in eukaryotes to cyanate degradation in prokaryotes. There are five known evolutionarily distinct CA families (alpha, beta, gamma, delta and epsilon) that have no significant sequence identity and have structurally distinct overall folds. Some CAs are membrane-bound, while others act in the cytosol; there are several related proteins that lack enzymatic activity. The active site of alpha-CAs is well described, consisting of a zinc ion coordinated through 3 histidine residues and a water molecule/hydroxide ion that acts as a potent nucleophile. The enzyme employs a two-step mechanism: in the first step, there is a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide; in the second step, the active site is regenerated by the ionisation of the zinc-bound water molecule and the removal of a proton from the active site. Beta- and gamma-CAs also employ a zinc hydroxide mechanism, although at least some beta-class enzymes do not have water directly coordinated to the metal ion.

Pssm-ID: 215000 [Multi-domain] Cd Length: 247 Bit Score: 281.51 E-value: 5.84e-86

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161    24 WSYTGALNQKNWGKKYPT-CNSPKQSPINIDEDLTQVNVNLKKLKFQgWDKTSleNTFIHNTGKTVEINL-TNDYRVSGG 101
Cdd:smart01057    1 WGYEGKNGPEHWGKLDPPfCGGKRQSPIDIVTAEAQYDPSLKPLKLS-YDQPT--AKRILNNGHTVQVNFdDDGSTLSGG 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161   102 VSEMVFKASKITFHWGKCNmsSDGSEHSLEGQKFPLEMQIYCFDADrfSSFEEAVKGKGKLRALSILFEVGTEENLDFKA 181
Cdd:smart01057   78 PLPGRYRLKQFHFHWGGSD--SEGSEHTIDGKRFPLELHLVHYNSK--GSFSEAVSKPGGLAVVAVFFKVGAEENPALQA 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161   182 IIDGVESVSRFGKQAALDPFILLNLLPNSTDKYYIYNGSLTSPPCTDTVDWIVFKDTVSISESQLAVFCEVLTMQQSgyv 261
Cdd:smart01057  154 ILDHLPLIKYKGQETELTPFDLSSLLPASTRHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLLPMEGN--- 230

                           250       260
                    ....*....|....*....|
gi 1609046161   262 mlmDYLQNNFREQQYKFSRQ 281
Cdd:smart01057  231 ---EPLVNNARPLQPLNGRV 247

Carb_anhydrase

pfam00194

Eukaryotic-type carbonic anhydrase;

30-286

5.86e-84

Eukaryotic-type carbonic anhydrase;

Pssm-ID: 459707 [Multi-domain] Cd Length: 252 Bit Score: 276.07 E-value: 5.86e-84

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161   30 LNQKNWGKKYPTCNSPKQSPINIDEDLTQVNVNLKKLKFQGWDKTSLENTfIHNTGKTVEINLTNDYR--VSGGVSEMVF 107
Cdd:pfam00194    1 LGPEHWGKVYPSCGGKRQSPINIDTRKVRYDPSLPPLTFQGYDVPPGKNT-LTNNGHTVQVSLDDGDPstISGGPLATRY 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  108 KASKITFHWGKCNmsSDGSEHSLEGQKFPLEMQIYCFDADRfSSFEEAVKGKGKLRALSILFEVGTEENLDFKAIIDGVE 187
Cdd:pfam00194   80 RLVQFHFHWGSTD--SRGSEHTIDGKRYPAELHIVHYNSKY-KSFDEAAKHPDGLAVLGVFFEVGDENNPYLQPIVSALD 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  188 SVSRFGKQAALDPFILLNLLPNSTDKYYIYNGSLTSPPCTDTVDWIVFKDTVSISESQLAVFCEVLTMQQSGYvmlMDYL 267
Cdd:pfam00194  157 NIKYKGKSVLLPPFDLSDLLPEDLTSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDGGEE---PRPL 233

                          250
                   ....*....|....*....
gi 1609046161  268 QNNFREQQYKFSRQVFSSY 286
Cdd:pfam00194  234 VNNFRPTQPLNGRVVFASF 252

PTPc

Protein tyrosine phosphatase, catalytic domain;

2008-2266

3.60e-78

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 259.90 E-value: 3.60e-78

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  2008 KLEKQFQLLSQSNIQQSDYSAALKQCNREKNRTSSIIPVERSRVGISSLSGEGTDYINASYIMGYYQSNEFIITQHPLLH 2087
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPLPS 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  2088 TIKDFWRMIWDHNAQLVVMI-PDGQNMAEDEFVYWPNK-DEPINCESFKVTLMAEEHKclsneEKLIIQDFILEATQDDY 2165
Cdd:smart00194   81 TVEDFWRMVWEQKVTVIVMLtELVEKGREKCAQYWPDEeGEPLTYGDITVTLKSVEKV-----DDYTIRTLEVTNTGCSE 155

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  2166 VLEVRHFQCPKWP---NPDSPISkTFELISVIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAK 2242
Cdd:smart00194  156 TRTVTHYHYTNWPdhgVPESPES-ILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVK 234

                           250       260
                    ....*....|....*....|....
gi 1609046161  2243 MINLMRPGVFADIEQYQFLYKVIL 2266
Cdd:smart00194  235 ELRSQRPGMVQTEEQYIFLYRAIL 258

Y_phosphatase

Protein-tyrosine phosphatase;

2034-2266

5.25e-76

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 252.55 E-value: 5.25e-76

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2034 NREKNRTSSIIPVERSRVGISSLSGeGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNM 2113
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPG-PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2114 A-EDEFVYWPNK-DEPINCESFKVTLMAEEhkclSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPN---PDSPISkTF 2188
Cdd:pfam00102   80 GrEKCAQYWPEEeGESLEYGDFTVTLKKEK----EDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDhgvPESPNS-LL 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1609046161 2189 ELISVIKE-EAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVIL 2266
Cdd:pfam00102  155 DLLRKVRKsSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233

PHA02738

hypothetical protein; Provisional

1708-1987

7.56e-54

hypothetical protein; Provisional

Pssm-ID: 222923 [Multi-domain] Cd Length: 320 Bit Score: 192.06 E-value: 7.56e-54

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1708 ETLKEFYQEVQSCTVDLGITADSSNhpdnKHKNRYINIVAYDHSRVKLAqlAEKDgkLTDYINANYVDGYNRPKAYIAAQ 1787
Cdd:PHA02738    25 EVITREHQKVISEKVDGTFNAEKKN----RKLNRYLDAVCFDHSRVILP--AERN--RGDYINANYVDGFEYKKKFICGQ 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1788 GPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWP--ADGSEEYGNFLVTQKSVQVLAYYTVRNFTLRNtkikk 1865
Cdd:PHA02738    97 APTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSdvEQGSIRFGKFKITTTQVETHPHYVKSTLLLTD----- 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1866 gsqkGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFV------RKAAYAKRHAVG-------PVVVHCSAGVGRTGTYIVL 1932
Cdd:PHA02738   172 ----GTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVlevrqcQKELAQESLQIGhnrlqppPIVVHCNAGLGRTPCYCVV 247

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1609046161 1933 DSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAILSKETEVL 1987
Cdd:PHA02738   248 DISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAVKRYVNLTVNKVS 302

COG5599

Protein tyrosine phosphatase [Signal transduction mechanisms];

1711-1971

5.41e-40

Protein tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 444335 [Multi-domain] Cd Length: 282 Bit Score: 150.63 E-value: 5.41e-40

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1711 KEFYQEVQSCTVDLGITADSSNHPDN---KHKNRYINIVAYDHSRVklaqlaEKDGKltdYINANYVDGYNrPKAYIAAQ 1787
Cdd:COG5599     14 EKINSRLSTLTNELAPSHNDPQYLQNingSPLNRFRDIQPYKETAL------RANLG---YLNANYIQVIG-NHRYIATQ 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1788 GPLKSTAEDFWRMIWEHNVEVIVMITNLVE--KGRRKCDQYWPADGseEYGNFLVTQKSVQVlaYYTVRNFTLRNTKIK- 1864
Cdd:COG5599     84 YPLEEQLEDFFQMLFDNNTPVLVVLASDDEisKPKVKMPVYFRQDG--EYGKYEVSSELTES--IQLRDGIEARTYVLTi 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1865 KGS-QKGRPsgrvVTQYHYTQWPDMGVP--EYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQ- 1940
Cdd:COG5599    160 KGTgQKKIE----IPVLHVKNWPDHGAIsaEALKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINa 235

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1609046161 1941 -HEGTVNIFGFLKHIRSQRNY-LVQTEEQYVFI 1971
Cdd:COG5599    236 lVQITLSVEEIVIDMRTSRNGgMVQTSEQLDVL 268

Cah

COG3338

Carbonic anhydrase [Inorganic ion transport and metabolism];

24-249

8.99e-32

Carbonic anhydrase [Inorganic ion transport and metabolism];

Pssm-ID: 442567 [Multi-domain] Cd Length: 247 Bit Score: 125.77 E-value: 8.99e-32

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161   24 WSYTGALNQKNWGK---KYPTCNS-PKQSPINIDedlTQVNVNLKKLKFQgWDKTSLEntfIHNTGKTVEINL-TNDYRV 98
Cdd:COG3338     28 WSYEGETGPEHWGElspEFATCATgKNQSPIDIR---TAIKADLPPLKFD-YKPTPLE---IVNNGHTIQVNVdPGSTLT 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161   99 SGGVsemVFKASKITFHwgkcnmssDGSEHSLEGQKFPLEMQiycF---DADrfssfeeavkgkGKLRALSILFEVGtEE 175
Cdd:COG3338    101 VDGK---RYELKQFHFH--------TPSEHTINGKSYPMEAH---LvhkDAD------------GELAVVGVLFEEG-AE 153

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1609046161  176 NLDFKAIIDGVESvsRFGKQAALD-PFILLNLLPNSTDkYYIYNGSLTSPPCTDTVDWIVFKDTVSISESQLAVF 249
Cdd:COG3338    154 NPALAKLWANLPL--EAGEEVALDaTIDLNDLLPEDRS-YYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQIEAF 225

PHA02747

protein tyrosine phosphatase; Provisional

2026-2270

8.39e-29

protein tyrosine phosphatase; Provisional

Pssm-ID: 165114 [Multi-domain] Cd Length: 312 Bit Score: 119.34 E-value: 8.39e-29

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2026 YSAALKQCNREKNRTSSIIPVERSRVGISSLSGEGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVV 2105
Cdd:PHA02747    43 IANFEKPENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIV 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2106 MI--PDGQNMAEDEFVYW-PNKDEPINCESFKVTLMAEEHKCLSNEEKLIIQDFILEATQddyvlEVRHFQCPKWPNPDS 2182
Cdd:PHA02747   123 MLtpTKGTNGEEKCYQYWcLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSR-----KISHFQCSEWFEDET 197

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2183 PiSKTFELISVIKEEAANRD-------------GPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRP 2249
Cdd:PHA02747   198 P-SDHPDFIKFIKIIDINRKksgklfnpkdallCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRH 276

                          250       260
                   ....*....|....*....|....
gi 1609046161 2250 GVFADIEQYQFL---YKVILSLVS 2270
Cdd:PHA02747   277 AGIMNFDDYLFIqpgYEVLHYFLS 300

fn3

pfam00041

Fibronectin type III domain;

299-387

1.60e-09

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 56.65 E-value: 1.60e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  299 SEPENVQADPENYTSLLVTWERPRVVYDTmIEKFAVLYQQLDGEDQtKHEFLTDGYQDlGAILNNLLPNMSYVLQIVAIC 378
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGP-ITGYEVEYRPKNSGEP-WNEITVPGTTT-SVTLTGLKPGTEYEVRVQAVN 77


                   ....*....
gi 1609046161  379 TNGlYGKYS 387
Cdd:pfam00041   78 GGG-EGPPS 85

PLN02179

carbonic anhydrase

35-239

7.39e-09

carbonic anhydrase

Pssm-ID: 177835 Cd Length: 235 Bit Score: 58.45 E-value: 7.39e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161   35 WGKKYP---TCNSPK-QSPInideDLTQVNVNLkkLKFQGWDKT-SLENTFIHNTGKTVEINLTNDyrvsggvsemvfkA 109
Cdd:PLN02179    50 WGKLNPqwkVCSTGKyQSPI----DLTDERVSL--IHDQALSRHyKPAPAVIQSRGHDVMVSWKGD-------------A 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  110 SKITFHWG-----KCNMSSDgSEHSLEGQKFPLEMQIYCFDAdrfssfeeavkgKGKLRALSILFEVGtEENLDFKAIID 184
Cdd:PLN02179   111 GKITIHQTdyklvQCHWHSP-SEHTINGTSYDLELHMVHTSA------------SGKTAVVGVLYKLG-EPDEFLTKLLN 176

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1609046161  185 GVESVsrfGKQ----AALDPfillNLLPNSTDKYYIYNGSLTSPPCTDTVDWIVFKDTV 239
Cdd:PLN02179   177 GIKGV---GKKeinlGIVDP----RDIRFETNNFYRYIGSLTIPPCTEGVIWTVVKRVV 228

FN3

cd00063

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...

299-392

1.43e-05

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 45.57 E-value: 1.43e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  299 SEPENVQADPENYTSLLVTWERPRvVYDTMIEKFAVLYQQLDGEDQTKHEflTDGYQDLGAILNNLLPNMSYVLQIVAIC 378
Cdd:cd00063      2 SPPTNLRVTDVTSTSVTLSWTPPE-DDGGPITGYVVEYREKGSGDWKEVE--VTPGSETSYTLTGLKPGTEYEFRVRAVN 78

                           90
                   ....*....|....
gi 1609046161  379 TNGlYGKYSDQLIV 392
Cdd:cd00063     79 GGG-ESPPSESVTV 91

FN3

smart00060

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...

299-381

2.21e-05

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 44.91 E-value: 2.21e-05

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161   299 SEPENVQADPENYTSLLVTWERPRvvyDTMIEKFAVLYQQLDGEDQTKHEFLTDGYQDLGAILNNLLPNMSYVLQIVAIC 378
Cdd:smart00060    2 SPPSNLRVTDVTSTSVTLSWEPPP---DDGITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78


                    ...
gi 1609046161   379 TNG 381
Cdd:smart00060   79 GAG 81

Name

Accession

Description

Interval

E-value

R-PTPc-G-1

cd17667

catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...

1703-1980

2.13e-160

Pssm-ID: 350505 [Multi-domain] Cd Length: 274 Bit Score: 494.94 E-value: 2.13e-160

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1703 FTEEFEtlkefyqEVQSCTVDLGITADSSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGKLTDYINANYVDGYNRPKA 1782
Cdd:cd17667      1 FSEDFE-------EVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKA 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1783 YIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQVLAYYTVRNFTLRNTK 1862
Cdd:cd17667     74 YIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTK 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1863 IKKGSQ---KGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQI 1939
Cdd:cd17667    154 VKKGQKgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQI 233

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1609046161 1940 QHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAIL 1980
Cdd:cd17667    234 KDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274

R-PTPc-Z-1

cd17668

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...

1768-1976

5.90e-155

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: 476.78 E-value: 5.90e-155

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1768 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 1847
Cdd:cd17668      1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1848 LAYYTVRNFTLRNTKIKKGSQKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGRTG 1927
Cdd:cd17668     81 LAYYTVRNFTLRNTKIKKGSQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVGPVVVHCSAGVGRTG 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1609046161 1928 TYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLV 1976
Cdd:cd17668    161 TYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209

R-PTP-Z-2

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...

2063-2266

4.66e-154

Pssm-ID: 350507 [Multi-domain] Cd Length: 204 Bit Score: 474.10 E-value: 4.66e-154

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2063 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDEFVYWPNKDEPINCESFKVTLMAEEH 2142
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFVYWPNKDEPINCETFKVTLIAEEH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2143 KCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISVIKEEAANRDGPMIVHDEHGGVTAGTFCAL 2222
Cdd:cd17669     81 KCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISIIKEEAANRDGPMIVHDEHGGVTAGTFCAL 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1609046161 2223 TTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVIL 2266
Cdd:cd17669    161 TTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204

R5-PTPc-1

cd14549

catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...

1768-1973

3.04e-143

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: 443.72 E-value: 3.04e-143

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1768 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 1847
Cdd:cd14549      1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTETYGNIQVTLLSTEV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1848 LAYYTVRNFTLRNTKIKKGsqKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGRTG 1927
Cdd:cd14549     81 LATYTVRTFSLKNLKLKKV--KGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAANPPGAGPIVVHCSAGVGRTG 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1609046161 1928 TYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHD 1973
Cdd:cd14549    159 TYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204

R-PTP-G-2

cd17670

PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...

2063-2267

2.08e-127

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: 398.67 E-value: 2.08e-127

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2063 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDEFVYWPNKDEPINCESFKVTLMAEEH 2142
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFVYWPSREESMNCEAFTVTLISKDR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2143 KCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISVIKEEAANRDGPMIVHDEHGGVTAGTFCAL 2222
Cdd:cd17670     81 LCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALTRDGPTIVHDEFGAVSAGTLCAL 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1609046161 2223 TTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVILS 2267
Cdd:cd17670    161 TTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAMLS 205

R5-PTP-2

cd14550

PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...

2063-2263

5.53e-126

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: 394.38 E-value: 5.53e-126

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2063 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQnMAEDEFVYWPNKDEPINCESFKVTLMAEEH 2142
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNE-LNEDEPIYWPTKEKPLECETFKVTLSGEDH 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2143 KCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTFELISVIKEEAANRDGPMIVHDEHGGVTAGTFCAL 2222
Cdd:cd14550     80 SCLSNEIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTVFELINTVQEWAQQRDGPIVVHDRYGGVQAATFCAL 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1609046161 2223 TTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYK 2263
Cdd:cd14550    160 TTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200

PTPc

Protein tyrosine phosphatase, catalytic domain;

1702-1977

1.04e-118

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 375.84 E-value: 1.04e-118

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  1702 GFTEEFETLKEFYQEVQSCTVdlgitadsSNHPDNKHKNRYINIVAYDHSRVKLAQLaekDGKLTDYINANYVDGYNRPK 1781
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCTV--------AAFPENRDKNRYKDVLPYDHTRVKLKPP---PGEGSDYINASYIDGPNGPK 69

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  1782 AYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSE--EYGNFLVTQKSVQVLAYYTVRNFTLR 1859
Cdd:smart00194   70 AYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEplTYGDITVTLKSVEKVDDYTIRTLEVT 149

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  1860 NTkikkgsqkGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQI 1939
Cdd:smart00194  150 NT--------GCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQL 221

                           250       260       270
                    ....*....|....*....|....*....|....*...
gi 1609046161  1940 QHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1977
Cdd:smart00194  222 EAGKEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259

alpha_CARP_receptor_like

cd03122

Carbonic anhydrase alpha related protein, receptor_like subfamily. Carbonic anhydrase related ...

31-284

5.74e-113

Pssm-ID: 239396 [Multi-domain] Cd Length: 253 Bit Score: 359.36 E-value: 5.74e-113

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161   31 NQKNWGKKYPTCNS-PKQSPINIDEDlTQVNVN-LKKLKFQGWDKTSLEnTFIHNTGKTVEINLTN---DYRVSGGVSEM 105
Cdd:cd03122      1 NPKHWAKKYPACGEgRQQSPIDIVED-TQVQRQgLQPLHFDGYEELTAS-TTLENTGKTVILRLEGnssDPFVSGGPLLG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  106 VFKASKITFHWGKCNmsSDGSEHSLEGQKFPLEMQIYCFDADRFSSFEeAVKGKGKLRALSILFEVGTEENLDFKAIIDG 185
Cdd:cd03122     79 RYKFSEITFHWGTCN--SDGSEHSIDGHKFPLEMQILHRNTDFFDSFE-AIKSPGGVLALAYLFELSHEDNPFLDPIIEG 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  186 VESVSRFGKQAALDPFILLNLLPNSTDKYYIYNGSLTSPPCTDTVDWIVFKDTVSISESQLAVFCEVLTMQQSGyVMLMD 265
Cdd:cd03122    156 LRNVSRPGKEVELPPFPLSDLLPPFTDKYYSYEGSLTTPPCSETVEWIVFREPVPISSRQLEAFRELLTRRQDG-VMSGD 234

                          250
                   ....*....|....*....
gi 1609046161  266 YLQNNFREQQYKFSRQVFS 284
Cdd:cd03122    235 YLPNNGRPQQPLGSRTVFS 253

Y_phosphatase

Protein-tyrosine phosphatase;

1736-1977

1.06e-112

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 357.71 E-value: 1.06e-112

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1736 NKHKNRYINIVAYDHSRVKLaqlaEKDGKLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNL 1815
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKL----TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTEL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1816 VEKGRRKCDQYWP--ADGSEEYGNFLVT-QKSVQVLAYYTVRNFTLRNtkikkgsqKGRPSGRVVTQYHYTQWPDMGVPE 1892
Cdd:pfam00102   77 EEKGREKCAQYWPeeEGESLEYGDFTVTlKKEKEDEKDYTVRTLEVSN--------GGSEETRTVKHFHYTGWPDHGVPE 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1893 YSLPVLTFVRKAAYAKRHA-VGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFI 1971
Cdd:pfam00102  149 SPNSLLDLLRKVRKSSLDGrSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFL 228


                   ....*.
gi 1609046161 1972 HDTLVE 1977
Cdd:pfam00102  229 YDAILE 234

R-PTPc-LAR-1

cd14553

catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...

1736-1981

2.45e-109

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: 348.23 E-value: 2.45e-109

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1736 NKHKNRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNL 1815
Cdd:cd14553      3 NKPKNRYANVIAYDHSRVILQPIEGVPG--SDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1816 VEKGRRKCDQYWPADGSEEYGNFLVTQKSVQVLAYYTVRNFTLRNTkikkgsqkGRPSGRVVTQYHYTQWPDMGVPEYSL 1895
Cdd:cd14553     81 EERSRVKCDQYWPTRGTETYGLIQVTLLDTVELATYTVRTFALHKN--------GSSEKREVRQFQFTAWPDHGVPEHPT 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1896 PVLTFVRKAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTL 1975
Cdd:cd14553    153 PFLAFLRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDAL 232


                   ....*.
gi 1609046161 1976 VEAILS 1981
Cdd:cd14553    233 LEAVTC 238

PTPc

cd00047

catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...

1768-1973

4.30e-96

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: 308.45 E-value: 4.30e-96

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1768 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSE--EYGNFLVTQKSV 1845
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKplEYGDITVTLVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1846 QVLAYYTVRNFTLRNTKIKKGsqkgrpsgRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGR 1925
Cdd:cd00047     81 EELSDYTIRTLELSPKGCSES--------REVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPNGPIVVHCSAGVGR 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1609046161 1926 TGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHD 1973
Cdd:cd00047    153 TGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200

R-PTPc-F-1

cd14626

catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...

1701-1979

5.13e-93

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: 303.11 E-value: 5.13e-93

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1701 SGFTEEFETLK-----EFYQEVQSCTVDLGITADSSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVD 1775
Cdd:cd14626      1 SDLADNIERLKandglKFSQEYESIDPGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPG--SDYINANYID 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1776 GYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQVLAYYTVRN 1855
Cdd:cd14626     79 GYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTETYGMIQVTLLDTVELATYSVRT 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1856 FTLRntkiKKGSQKGRPsgrvVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDSM 1935
Cdd:cd14626    159 FALY----KNGSSEKRE----VRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAM 230

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1609046161 1936 LQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAI 1979
Cdd:cd14626    231 LERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAA 274

R3-PTPc

cd14548

catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...

1741-1972

2.50e-92

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: 298.88 E-value: 2.50e-92

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1741 RYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGR 1820
Cdd:cd14548      1 RYTNILPYDHSRVKLIPINEEEG--SDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGR 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1821 RKCDQYWPADGSE-EYGNFLVTQKSVQVLAYYTVRNFTLrntkikkgsqKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLT 1899
Cdd:cd14548     79 VKCDHYWPFDQDPvYYGDITVTMLSESVLPDWTIREFKL----------ERGDEVRSVRQFHFTAWPDHGVPEAPDSLLR 148

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1609046161 1900 FVRKAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 1972
Cdd:cd14548    149 FVRLVRDYIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221

PTPc-N9

cd14543

catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...

1727-1972

4.24e-90

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: 294.66 E-value: 4.24e-90

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1727 TADSSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDgkLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNV 1806
Cdd:cd14543     20 TFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDE--RTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKV 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1807 EVIVMITNLVEKGRRKCDQYWP--ADGSEEYGNFLVTQKSVQVLAYYTVRNFTLRNTKIKkgsqkgrpSGRVVTQYHYTQ 1884
Cdd:cd14543     98 LVIVMTTRVVERGRVKCGQYWPleEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETD--------ESRQVTHFQFTS 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1885 WPDMGVPEYSLPVLTFVRKAAYAKRHAVG-------------PVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFL 1951
Cdd:cd14543    170 WPDFGVPSSAAALLDFLGEVRQQQALAVKamgdrwkghppgpPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTV 249

                          250       260
                   ....*....|....*....|.
gi 1609046161 1952 KHIRSQRNYLVQTEEQYVFIH 1972
Cdd:cd14543    250 RRMRTQRAFSIQTPDQYYFCY 270

R-PTPc-S-1

cd14625

catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...

1685-1979

3.31e-86

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: 283.91 E-value: 3.31e-86

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1685 IPIKHFPKHVADLHASsgfteefETLKeFYQEVQSCTVDLGITADSSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGk 1764
Cdd:cd14625      4 IPISELAEHTERLKAN-------DNLK-LSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMG- 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1765 lTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKS 1844
Cdd:cd14625     75 -SDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTETYGMIQVTLLD 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1845 VQVLAYYTVRNFTLRntkiKKGSQKGRPsgrvVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVG 1924
Cdd:cd14625    154 TIELATFCVRTFSLH----KNGSSEKRE----VRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVG 225

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1609046161 1925 RTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAI 1979
Cdd:cd14625    226 RTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAV 280

Carb_anhydrase

smart01057

Eukaryotic-type carbonic anhydrase; Carbonic anhydrases are zinc metalloenzymes which catalyse ...

24-281

5.84e-86

Pssm-ID: 215000 [Multi-domain] Cd Length: 247 Bit Score: 281.51 E-value: 5.84e-86

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161    24 WSYTGALNQKNWGKKYPT-CNSPKQSPINIDEDLTQVNVNLKKLKFQgWDKTSleNTFIHNTGKTVEINL-TNDYRVSGG 101
Cdd:smart01057    1 WGYEGKNGPEHWGKLDPPfCGGKRQSPIDIVTAEAQYDPSLKPLKLS-YDQPT--AKRILNNGHTVQVNFdDDGSTLSGG 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161   102 VSEMVFKASKITFHWGKCNmsSDGSEHSLEGQKFPLEMQIYCFDADrfSSFEEAVKGKGKLRALSILFEVGTEENLDFKA 181
Cdd:smart01057   78 PLPGRYRLKQFHFHWGGSD--SEGSEHTIDGKRFPLELHLVHYNSK--GSFSEAVSKPGGLAVVAVFFKVGAEENPALQA 153

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161   182 IIDGVESVSRFGKQAALDPFILLNLLPNSTDKYYIYNGSLTSPPCTDTVDWIVFKDTVSISESQLAVFCEVLTMQQSgyv 261
Cdd:smart01057  154 ILDHLPLIKYKGQETELTPFDLSSLLPASTRHYYTYNGSLTTPPCSEGVTWIVFKEPITISTEQLEKFRTLLPMEGN--- 230

                           250       260
                    ....*....|....*....|
gi 1609046161   262 mlmDYLQNNFREQQYKFSRQ 281
Cdd:smart01057  231 ---EPLVNNARPLQPLNGRV 247

R-PTPc-D-1

cd14624

catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...

1671-1979

4.45e-85

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: 280.85 E-value: 4.45e-85

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1671 PPTPIFPISDdvgaipikhfpkHVADLHASSGFteefetlkEFYQEVQSCTVDLGITADSSNHPDNKHKNRYINIVAYDH 1750
Cdd:cd14624      2 PPIPILELAD------------HIERLKANDNL--------KFSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDH 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1751 SRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPAD 1830
Cdd:cd14624     62 SRVLLSAIEGIPG--SDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSR 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1831 GSEEYGNFLVTQKSVQVLAYYTVRNFTLrntkIKKGSQKGRPsgrvVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRH 1910
Cdd:cd14624    140 GTETYGLIQVTLLDTVELATYCVRTFAL----YKNGSSEKRE----VRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCNPP 211

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1609046161 1911 AVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAI 1979
Cdd:cd14624    212 DAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAV 280

R-PTPc-T-1

cd14630

catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...

1735-1980

1.39e-84

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: 277.29 E-value: 1.39e-84

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1735 DNKHKNRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITN 1814
Cdd:cd14630      2 ENRNKNRYGNIISYDHSRVRLQLLDGDPH--SDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTN 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1815 LVEKGRRKCDQYWPaDGSEEYGNFLVTQKSVQVLAYYTVRNFTLRntkiKKGSQKGRPsgrvVTQYHYTQWPDMGVPEYS 1894
Cdd:cd14630     80 LVEVGRVKCVRYWP-DDTEVYGDIKVTLIETEPLAEYVIRTFTVQ----KKGYHEIRE----IRQFHFTSWPDHGVPCYA 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1895 LPVLTFVRKAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDT 1974
Cdd:cd14630    151 TGLLGFVRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDA 230


                   ....*.
gi 1609046161 1975 LVEAIL 1980
Cdd:cd14630    231 ILEACL 236

Carb_anhydrase

pfam00194

Eukaryotic-type carbonic anhydrase;

30-286

5.86e-84

Eukaryotic-type carbonic anhydrase;

Pssm-ID: 459707 [Multi-domain] Cd Length: 252 Bit Score: 276.07 E-value: 5.86e-84

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161   30 LNQKNWGKKYPTCNSPKQSPINIDEDLTQVNVNLKKLKFQGWDKTSLENTfIHNTGKTVEINLTNDYR--VSGGVSEMVF 107
Cdd:pfam00194    1 LGPEHWGKVYPSCGGKRQSPINIDTRKVRYDPSLPPLTFQGYDVPPGKNT-LTNNGHTVQVSLDDGDPstISGGPLATRY 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  108 KASKITFHWGKCNmsSDGSEHSLEGQKFPLEMQIYCFDADRfSSFEEAVKGKGKLRALSILFEVGTEENLDFKAIIDGVE 187
Cdd:pfam00194   80 RLVQFHFHWGSTD--SRGSEHTIDGKRYPAELHIVHYNSKY-KSFDEAAKHPDGLAVLGVFFEVGDENNPYLQPIVSALD 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  188 SVSRFGKQAALDPFILLNLLPNSTDKYYIYNGSLTSPPCTDTVDWIVFKDTVSISESQLAVFCEVLTMQQSGYvmlMDYL 267
Cdd:pfam00194  157 NIKYKGKSVLLPPFDLSDLLPEDLTSYYTYNGSLTTPPCSESVTWIVFKEPISISEEQLEAFRTLLFSDGGEE---PRPL 233

                          250
                   ....*....|....*....
gi 1609046161  268 QNNFREQQYKFSRQVFSSY 286
Cdd:pfam00194  234 VNNFRPTQPLNGRVVFASF 252

R-PTPc-J

cd14615

catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...

1740-1971

5.03e-81

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: 266.68 E-value: 5.03e-81

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1740 NRYINIVAYDHSRVKLAQLAEKdgkLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKG 1819
Cdd:cd14615      1 NRYNNVLPYDISRVKLSVQSHS---TDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1820 RRKCDQYWPADGSEEYGNFLVTQKSVQVLAYYTVRNFTLRNtkiKKGSQKgrpsgRVVTQYHYTQWPDMGVPEYSLPVLT 1899
Cdd:cd14615     78 RTKCEEYWPSKQKKDYGDITVTMTSEIVLPEWTIRDFTVKN---AQTNES-----RTVRHFHFTSWPDHGVPETTDLLIN 149

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1609046161 1900 F---VRKaaYAKRHAV-GPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFI 1971
Cdd:cd14615    150 FrhlVRE--YMKQNPPnSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFL 223

R-PTPc-A-1

cd14621

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...

1671-1986

1.37e-79

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: 265.35 E-value: 1.37e-79

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1671 PPTPIFPISDDVGaipikhfpKHVADlhASSGFTEEFETLKefyqevqSCTVDlgITADSSNHPDNKHKNRYINIVAYDH 1750
Cdd:cd14621      6 PPLPVDKLEEEIN--------RRMAD--DNKLFREEFNALP-------ACPIQ--ATCEAASKEENKEKNRYVNILPYDH 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1751 SRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPAD 1830
Cdd:cd14621     67 SRVHLTPVEGVPD--SDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQ 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1831 GSEEYGNFLVTQKSVQVLAYYTVRNFTLRNTkikkGSQKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRH 1910
Cdd:cd14621    145 GCWTYGNIRVSVEDVTVLVDYTVRKFCIQQV----GDVTNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQ 220

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1609046161 1911 AVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAILSKETEV 1986
Cdd:cd14621    221 YAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTEL 296

R-PTPc-M-1

cd14633

catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...

1692-1980

5.79e-79

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: 262.67 E-value: 5.79e-79

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1692 KHVADLHASSG--FTEEFETlkefYQEVQSCTvdlgitADSSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGklTDYI 1769
Cdd:cd14633      4 QHITQMKCAEGygFKEEYES----FFEGQSAP------WDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETS--SDYI 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1770 NANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPaDGSEEYGNFLVTQKSVQVLA 1849
Cdd:cd14633     72 NGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWP-DDTEIYKDIKVTLIETELLA 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1850 YYTVRNFTLRntkikkgsQKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGRTGTY 1929
Cdd:cd14633    151 EYVIRTFAVE--------KRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCF 222

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1609046161 1930 IVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAIL 1980
Cdd:cd14633    223 IVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 273

PTPc

Protein tyrosine phosphatase, catalytic domain;

2008-2266

3.60e-78

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 259.90 E-value: 3.60e-78

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  2008 KLEKQFQLLSQSNIQQSDYSAALKQCNREKNRTSSIIPVERSRVGISSLSGEGTDYINASYIMGYYQSNEFIITQHPLLH 2087
Cdd:smart00194    1 GLEEEFEKLDRLKPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGPNGPKAYIATQGPLPS 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  2088 TIKDFWRMIWDHNAQLVVMI-PDGQNMAEDEFVYWPNK-DEPINCESFKVTLMAEEHKclsneEKLIIQDFILEATQDDY 2165
Cdd:smart00194   81 TVEDFWRMVWEQKVTVIVMLtELVEKGREKCAQYWPDEeGEPLTYGDITVTLKSVEKV-----DDYTIRTLEVTNTGCSE 155

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  2166 VLEVRHFQCPKWP---NPDSPISkTFELISVIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAK 2242
Cdd:smart00194  156 TRTVTHYHYTNWPdhgVPESPES-ILDLIRAVRKSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVK 234

                           250       260
                    ....*....|....*....|....
gi 1609046161  2243 MINLMRPGVFADIEQYQFLYKVIL 2266
Cdd:smart00194  235 ELRSQRPGMVQTEEQYIFLYRAIL 258

R-PTPc-B

cd14617

catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...

1740-1972

2.69e-77

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: 256.00 E-value: 2.69e-77

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1740 NRYINIVAYDHSRVKLAQLaeKDGKLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKG 1819
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNV--DDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1820 RRKCDQYWPAD-GSEEYGNFLVTQKSVQVLAYYTVRNFtlrntKIKKGSQKGRPsgRVVTQYHYTQWPDMGVPEYSLPVL 1898
Cdd:cd14617     79 RVKCDHYWPADqDSLYYGDLIVQMLSESVLPEWTIREF-----KICSEEQLDAP--RLVRHFHYTVWPDHGVPETTQSLI 151

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1609046161 1899 TFVRKAA-YAKR-HAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 1972
Cdd:cd14617    152 QFVRTVRdYINRtPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 227

R-PTPc-typeIIb-1

cd14555

catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...

1768-1980

6.08e-77

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: 254.07 E-value: 6.08e-77

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1768 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADgSEEYGNFLVTQKSVQV 1847
Cdd:cd14555      1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDD-TEVYGDIKVTLVETEP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1848 LAYYTVRNFTLRntkikkgsQKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGRTG 1927
Cdd:cd14555     80 LAEYVVRTFALE--------RRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKASNPPSAGPIVVHCSAGAGRTG 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1609046161 1928 TYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAIL 1980
Cdd:cd14555    152 CYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILEACL 204

R-PTPc-H

cd14619

catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...

1740-1979

7.54e-77

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: 254.81 E-value: 7.54e-77

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1740 NRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKG 1819
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKPIHEEPG--SDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1820 RRKCDQYWPADGSE-EYGNFLVTQKSVQVLAYYTVRNFTLRNTKIKKgsqkgrpsGRVVTQYHYTQWPDMGVPEYSLPVL 1898
Cdd:cd14619     79 RVKCEHYWPLDYTPcTYGHLRVTVVSEEVMENWTVREFLLKQVEEQK--------TLSVRHFHFTAWPDHGVPSSTDTLL 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1899 TF---VRKAAYAKRHAvGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTL 1975
Cdd:cd14619    151 AFrrlLRQWLDQTMSG-GPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCI 229


                   ....
gi 1609046161 1976 VEAI 1979
Cdd:cd14619    230 LDFL 233

Y_phosphatase

Protein-tyrosine phosphatase;

2034-2266

5.25e-76

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 252.55 E-value: 5.25e-76

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2034 NREKNRTSSIIPVERSRVGISSLSGeGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNM 2113
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPG-PSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2114 A-EDEFVYWPNK-DEPINCESFKVTLMAEEhkclSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPN---PDSPISkTF 2188
Cdd:pfam00102   80 GrEKCAQYWPEEeGESLEYGDFTVTLKKEK----EDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDhgvPESPNS-LL 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1609046161 2189 ELISVIKE-EAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVIL 2266
Cdd:pfam00102  155 DLLRKVRKsSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233

R-PTPc-E-1

cd14620

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...

1742-1977

8.73e-76

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: 251.78 E-value: 8.73e-76

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1742 YINIVAYDHSRVKLAQLaekDGKL-TDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGR 1820
Cdd:cd14620      1 YPNILPYDHSRVILSQL---DGIPcSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1821 RKCDQYWPADGSEEYGNFLVTQKSVQVLAYYTVRNFTLRntkiKKGSQKGRPSgRVVTQYHYTQWPDMGVPEYSLPVLTF 1900
Cdd:cd14620     78 EKCYQYWPDQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQ----PQLPDGCKAP-RLVTQLHFTSWPDFGVPFTPIGMLKF 152

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1609046161 1901 VRKAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1977
Cdd:cd14620    153 LKKVKSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229

R-PTPc-K-1

cd14631

catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...

1761-1980

6.97e-74

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: 245.70 E-value: 6.97e-74

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1761 KDGKLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADgSEEYGNFLV 1840
Cdd:cd14631      8 EDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDD-TEVYGDFKV 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1841 TQKSVQVLAYYTVRNFTLrntkikkgSQKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVHCS 1920
Cdd:cd14631     87 TCVEMEPLAEYVVRTFTL--------ERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCS 158

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1921 AGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAIL 1980
Cdd:cd14631    159 AGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 218

R-PTP-LAR-2

cd14554

PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...

1731-1972

1.06e-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: 245.90 E-value: 1.06e-73

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1731 SNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIV 1810
Cdd:cd14554      1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEG--SDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1811 MITNLVEKGRRKCDQYWPADGSEEYGNFLvtqksVQVLAYYTVRNFTLRNTKIKKGSQKgrpSGRVVTQYHYTQWPDMGV 1890
Cdd:cd14554     79 MLTKLREMGREKCHQYWPAERSARYQYFV-----VDPMAEYNMPQYILREFKVTDARDG---QSRTVRQFQFTDWPEQGV 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1891 PEYSLPVLTFVRKA--AYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQY 1968
Cdd:cd14554    151 PKSGEGFIDFIGQVhkTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQY 230


                   ....
gi 1609046161 1969 VFIH 1972
Cdd:cd14554    231 QFCY 234

alpha_CA

cd00326

Carbonic anhydrase alpha (vertebrate-like) group. Carbonic anhydrases (CAs) are ...

46-283

5.52e-73

Carbonic anhydrase alpha (vertebrate-like) group. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidine residues and a fourth conserved histidine plays a potential role in proton transfer.

Pssm-ID: 238200 Cd Length: 227 Bit Score: 243.34 E-value: 5.52e-73

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161   46 KQSPINIDEDLTQVNVNLKKLKFQGWDKTSLEntfIHNTGKTVEINL-TNDYRVSGGVSEMVFKASKITFHWGKCNmsSD 124
Cdd:cd00326      3 RQSPINIVTSAVVYDPSLPPLNFDYYPTTSLT---LVNNGHTVQVNFdDDGGTLSGGGLPGRYKLVQFHFHWGSEN--SP 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  125 GSEHSLEGQKFPLEMQIYCFDADRFSSfeEAVKGKGKLRALSILFEVGTEENLDFKAIIDGVESVSRFGKQAALDPFILL 204
Cdd:cd00326     78 GSEHTIDGKRYPLELHLVHYNSDYYSS--EAAKKPGGLAVLGVFFEVGEKENPFLKKILDALPKIKYKGKETTLPPFDLS 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1609046161  205 NLLPNSTDKYYIYNGSLTSPPCTDTVDWIVFKDTVSISESQLAVFCEVLTMQqsgyvmlMDYLQNNFREQQYKFSRQVF 283
Cdd:cd00326    156 DLLPSSLRDYYTYEGSLTTPPCSEGVTWIVFKEPITISKEQLEAFRSLLDRE-------GKPLVNNYRPVQPLNGRVVY 227

R-PTPc-A-E-1

cd14551

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...

1768-1972

1.90e-72

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: 240.97 E-value: 1.90e-72

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1768 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 1847
Cdd:cd14551      1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTYGNLRVRVEDTVV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1848 LAYYTVRNFTLRntkiKKGSQKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGRTG 1927
Cdd:cd14551     81 LVDYTTRKFCIQ----KVNRGIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANPPRAGPIVVHCSAGVGRTG 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1609046161 1928 TYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 1972
Cdd:cd14551    157 TFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201

PTPc-KIM

cd14547

catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...

1740-1972

6.26e-71

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: 237.68 E-value: 6.26e-71

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1740 NRYINIVAYDHSRVKLAQlaEKDGKLTDYINANYVDGYN-RPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEK 1818
Cdd:cd14547      1 NRYKTILPNEHSRVCLPS--VDDDPLSSYINANYIRGYDgEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1819 gRRKCDQYWPADGSEEYGNFLVTQKSVQVLAYYTVRNFTLRNtkikkGSQKgrpsgRVVTQYHYTQWPDMGVPEYSLPVL 1898
Cdd:cd14547     79 -KEKCAQYWPEEENETYGDFEVTVQSVKETDGYTVRKLTLKY-----GGEK-----RYLKHYWYTSWPDHKTPEAAQPLL 147

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1609046161 1899 TFVRKAAYAKRHAV--GPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 1972
Cdd:cd14547    148 SLVQEVEEARQTEPhrGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223

R-PTPc-U-1

cd14632

catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...

1768-1980

1.10e-70

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: 236.10 E-value: 1.10e-70

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1768 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPaDGSEEYGNFLVTQKSVQV 1847
Cdd:cd14632      1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP-DDSDTYGDIKITLLKTET 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1848 LAYYTVRNFTLRntkikkgsQKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGRTG 1927
Cdd:cd14632     80 LAEYSVRTFALE--------RRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPDAGPVVVHCSAGAGRTG 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1609046161 1928 TYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAIL 1980
Cdd:cd14632    152 CYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACL 204

PTPc-N11_6

cd14544

catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...

1736-1972

5.92e-70

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: 235.82 E-value: 5.92e-70

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1736 NKHKNRYINIVAYDHSRVKLaQLAEKDGKLTDYINANYVDGYN-------RPKAYIAAQGPLKSTAEDFWRMIWEHNVEV 1808
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVIL-KDRDPNVPGSDYINANYIRNENegpttdeNAKTYIATQGCLENTVSDFWSMVWQENSRV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1809 IVMITNLVEKGRRKCDQYWPADG-SEEYGNFlvtqkSVQVLAYYTVRNFTLRNTKIKKGSQKGRPsgRVVTQYHYTQWPD 1887
Cdd:cd14544     80 IVMTTKEVERGKNKCVRYWPDEGmQKQYGPY-----RVQNVSEHDTTDYTLRELQVSKLDQGDPI--REIWHYQYLSWPD 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1888 MGVPEYSLPVLTFVRKA--AYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEG---TVNIFGFLKHIRSQRNYLV 1962
Cdd:cd14544    153 HGVPSDPGGVLNFLEDVnqRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRSGMV 232

                          250
                   ....*....|
gi 1609046161 1963 QTEEQYVFIH 1972
Cdd:cd14544    233 QTEAQYKFIY 242

R-PTPc-O

cd14614

catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...

1726-1972

7.69e-70

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: 235.17 E-value: 7.69e-70

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1726 ITADSSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHN 1805
Cdd:cd14614      2 IPHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEG--SDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1806 VEVIVMITNLVEKGRRKCDQYWP-ADGSEEYGNFLVTQKSVQVLAYYTVRNFtlrntKIKKGSQKGRpsgrvVTQYHYTQ 1884
Cdd:cd14614     80 SQIIVMLTQCNEKRRVKCDHYWPfTEEPVAYGDITVEMLSEEEQPDWAIREF-----RVSYADEVQD-----VMHFNYTA 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1885 WPDMGVPEYSL--PVLTFVRKAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLV 1962
Cdd:cd14614    150 WPDHGVPTANAaeSILQFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMV 229

                          250
                   ....*....|
gi 1609046161 1963 QTEEQYVFIH 1972
Cdd:cd14614    230 QTEEQYIFIH 239

R-PTPc-V

cd14618

catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...

1740-1976

2.58e-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: 227.52 E-value: 2.58e-67

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1740 NRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKG 1819
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQLGGEPH--SDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1820 RRKCDQYWPADGSE-EYGnflvtQKSVQVLAYYTVRNFTLRNTKIKKGSQKGRpsgRVVTQYHYTQWPDMGVPEYSLPVL 1898
Cdd:cd14618     79 RVLCDHYWPSESTPvSYG-----HITVHLLAQSSEDEWTRREFKLWHEDLRKE---RRVKHLHYTAWPDHGIPESTSSLM 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1899 TF---VRKAAYAKRHAvGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTL 1975
Cdd:cd14618    151 AFrelVREHVQATKGK-GPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCI 229


                   .
gi 1609046161 1976 V 1976
Cdd:cd14618    230 L 230

PTP_fungal

cd18533

fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...

1768-1973

7.49e-67

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: 225.21 E-value: 7.49e-67

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1768 YINANYVD-GYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSE-EYGNFLVTQKSV 1845
Cdd:cd18533      1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEgEYGDLTVELVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1846 QVL--AYYTVRNFTLRNTKIKKgsqkgrpsgRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHA--VGPVVVHCSA 1921
Cdd:cd18533     81 EENddGGFIVREFELSKEDGKV---------KKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSAslDPPIIVHCSA 151

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1609046161 1922 GVGRTGTYIVLDSMLQQIQ--HEGTVN-------IFGFLKHIRSQRNYLVQTEEQYVFIHD 1973
Cdd:cd18533    152 GVGRTGTFIALDSLLDELKrgLSDSQDledsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212

R-PTP-D-2

cd14628

PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...

1730-1981

9.24e-67

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: 228.46 E-value: 9.24e-67

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1730 SSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVI 1809
Cdd:cd14628     46 SANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEG--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIV 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1810 VMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQksvqvLAYYTVRNFTLRNTKIKKgSQKGRpsGRVVTQYHYTQWPDMG 1889
Cdd:cd14628    124 VMLTKLREMGREKCHQYWPAERSARYQYFVVDP-----MAEYNMPQYILREFKVTD-ARDGQ--SRTVRQFQFTDWPEQG 195

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1890 VPEYSLPVLTFVRKAAYAKRH--AVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQ 1967
Cdd:cd14628    196 VPKSGEGFIDFIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQ 275

                          250
                   ....*....|....
gi 1609046161 1968 YVFIHDTLVEAILS 1981
Cdd:cd14628    276 YQFCYRAALEYLGS 289

R-PTPc-C-1

cd14557

catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...

1768-1972

8.07e-66

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: 222.01 E-value: 8.07e-66

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1768 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPA--DGSEEYGNFLVTQKSV 1845
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSmeEGSRAFGDVVVKINEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1846 QVLAYYTVRNFTLRNTKIKKgsqkgrpSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGR 1925
Cdd:cd14557     81 KICPDYIIRKLNINNKKEKG-------SGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFFSGPIVVHCSAGVGR 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1609046161 1926 TGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 1972
Cdd:cd14557    154 TGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIH 200

R-PTP-S-2

cd14627

PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...

1730-1977

8.26e-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: 225.38 E-value: 8.26e-66

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1730 SSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVI 1809
Cdd:cd14627     47 SANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEG--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIV 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1810 VMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQksvqvLAYYTVRNFTLRNTKIKKgSQKGRpsGRVVTQYHYTQWPDMG 1889
Cdd:cd14627    125 VMLTKLREMGREKCHQYWPAERSARYQYFVVDP-----MAEYNMPQYILREFKVTD-ARDGQ--SRTVRQFQFTDWPEQG 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1890 VPEYSLPVLTFVRKAAYAKRH--AVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQ 1967
Cdd:cd14627    197 VPKSGEGFIDFIGQVHKTKEQfgQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDE 276

                          250
                   ....*....|
gi 1609046161 1968 YVFIHDTLVE 1977
Cdd:cd14627    277 YQFCYQAALE 286

R-PTP-F-2

cd14629

PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...

1730-1981

5.83e-65

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: 223.06 E-value: 5.83e-65

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1730 SSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVI 1809
Cdd:cd14629     47 SANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEG--SDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIV 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1810 VMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQksvqvLAYYTVRNFTLRNTKIKKgSQKGRpsGRVVTQYHYTQWPDMG 1889
Cdd:cd14629    125 VMLTKLREMGREKCHQYWPAERSARYQYFVVDP-----MAEYNMPQYILREFKVTD-ARDGQ--SRTIRQFQFTDWPEQG 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1890 VPEYSLPVLTFVRKAAYAKRH--AVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQ 1967
Cdd:cd14629    197 VPKTGEGFIDFIGQVHKTKEQfgQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQ 276

                          250
                   ....*....|....
gi 1609046161 1968 YVFIHDTLVEAILS 1981
Cdd:cd14629    277 YQLCYRAALEYLGS 290

PTPc-N18

cd14603

catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...

1711-1977

7.81e-63

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: 215.84 E-value: 7.81e-63

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1711 KEFyQEVQSCTV----DLGITADSSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAA 1786
Cdd:cd14603      2 GEF-SEIRACSAafkaDYVCSTVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGH--SDYINANFIKGVDGSRAYIAT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1787 QGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWP-ADGSEEYGNFLVTQ-KSVQVLAYYTVRNFTLrntKIK 1864
Cdd:cd14603     79 QGPLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYWAqEQEPLQTGPFTITLvKEKRLNEEVILRTLKV---TFQ 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1865 KGSqkgrpsgRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDS-----MLQQI 1939
Cdd:cd14603    156 KES-------RSVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYvrqllLTQRI 228

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1609046161 1940 QHEgtVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1977
Cdd:cd14603    229 PPD--FSIFDVVLEMRKQRPAAVQTEEQYEFLYHTVAQ 264

PTPc-N20_13

cd14538

catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...

1768-1979

6.74e-62

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: 211.08 E-value: 6.74e-62

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1768 YINANYV--DGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPaDGSEE----YGNFLVT 1841
Cdd:cd14538      1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWP-DSLNKplicGGRLEVS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1842 QKSVQVLAYYTVRNFTLRNTKIKKGsqkgrpsgRVVTQYHYTQWPDMGVPEYSLPVLTFVRkaaYAKR-HAVGPVVVHCS 1920
Cdd:cd14538     80 LEKYQSLQDFVIRRISLRDKETGEV--------HHITHLNFTTWPDHGTPQSADPLLRFIR---YMRRiHNSGPIVVHCS 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1609046161 1921 AGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAI 1979
Cdd:cd14538    149 AGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207

PTPc-N6

cd14606

catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...

1729-1981

1.27e-61

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: 212.43 E-value: 1.27e-61

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1729 DSSNHPDNKHKNRYINIVAYDHSRVKLaQLAEKDGKLTDYINANYVDGY-----NRPKAYIAAQGPLKSTAEDFWRMIWE 1803
Cdd:cd14606     11 LEGQRPENKSKNRYKNILPFDHSRVIL-QGRDSNIPGSDYINANYVKNQllgpdENAKTYIASQGCLEATVNDFWQMAWQ 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1804 HNVEVIVMITNLVEKGRRKCDQYWPADGSE-EYGNFLVTQKSVQVLAYYTVRnfTLRNTKIKKGSQKgrpsgRVVTQYHY 1882
Cdd:cd14606     90 ENSRVIVMTTREVEKGRNKCVPYWPEVGMQrAYGPYSVTNCGEHDTTEYKLR--TLQVSPLDNGELI-----REIWHYQY 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1883 TQWPDMGVPEYSLPVLTF---VRKAAYAKRHAvGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGT---VNIFGFLKHIRS 1956
Cdd:cd14606    163 LSWPDHGVPSEPGGVLSFldqINQRQESLPHA-GPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRA 241

                          250       260
                   ....*....|....*....|....*
gi 1609046161 1957 QRNYLVQTEEQYVFIHDTLVEAILS 1981
Cdd:cd14606    242 QRSGMVQTEAQYKFIYVAIAQFIET 266

R-PTPc-Q

cd14616

catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...

1740-1972

7.95e-61

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: 208.61 E-value: 7.95e-61

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1740 NRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKG 1819
Cdd:cd14616      1 NRFPNIKPYNNNRVKLIADAGVPG--SDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKG 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1820 RRKCDQYWPADGS--EEYGNFLVTQksvqvLAYYTVRNFTLRNTKIKKGSQKgrpsgRVVTQYHYTQWPDMGVPEYSLPV 1897
Cdd:cd14616     79 RIRCHQYWPEDNKpvTVFGDIVITK-----LMEDVQIDWTIRDLKIERHGDY-----MMVRQCNFTSWPEHGVPESSAPL 148

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1609046161 1898 LTFVRKAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 1972
Cdd:cd14616    149 IHFVKLVRASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLH 223

R-PTPc-A-E-2

cd14552

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...

1768-1976

2.56e-60

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: 206.35 E-value: 2.56e-60

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1768 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 1847
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVSSGDITVELKDQTD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1848 LAYYTVRNFTLRNTKIKKgsqkgrpsGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHA-VGPVVVHCSAGVGRT 1926
Cdd:cd14552     81 YEDYTLRDFLVTKGKGGS--------TRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSgNHPITVHCSAGAGRT 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1927 GTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLV 1976
Cdd:cd14552    153 GTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVVQ 202

PTPc-N22_18_12

cd14542

catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...

1768-1972

3.06e-60

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: 206.12 E-value: 3.06e-60

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1768 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEE--YGNFLVTQKSV 1845
Cdd:cd14542      1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQlqFGPFKISLEKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1846 QVLAyytvRNFTLRNTKIKKGSQKgrpsgRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGR 1925
Cdd:cd14542     81 KRVG----PDFLIRTLKVTFQKES-----RTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDVPICVHCSAGCGR 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1926 TGTYIVLDSMLQQIQHEG---TVNIFGFLKHIRSQRNYLVQTEEQYVFIH 1972
Cdd:cd14542    152 TGTICAIDYVWNLLKTGKipeEFSLFDLVREMRKQRPAMVQTKEQYELVY 201

PTPc-N1_2

cd14545

catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...

1737-1970

6.67e-60

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: 206.09 E-value: 6.67e-60

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1737 KHKNRYINIVAYDHSRVKLaqlaeKDGKlTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLV 1816
Cdd:cd14545      1 LNRYRDRDPYDHDRSRVKL-----KQGD-NDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLM 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1817 EKGRRKCDQYWPADGSE----EYGNFLVTQKSVQVLAYYTVRNFTLRNTKIkkgsqkgrPSGRVVTQYHYTQWPDMGVPE 1892
Cdd:cd14545     75 EKGQIKCAQYWPQGEGNamifEDTGLKVTLLSEEDKSYYTVRTLELENLKT--------QETREVLHFHYTTWPDFGVPE 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1893 YSLPVLTF---VRKAAYAKRHaVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGT--VNIFGFLKHIRSQRNYLVQTEEQ 1967
Cdd:cd14545    147 SPAAFLNFlqkVRESGSLSSD-VGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQ 225


                   ...
gi 1609046161 1968 YVF 1970
Cdd:cd14545    226 LRF 228

PTPc-N7

cd14612

catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...

1726-1975

3.31e-59

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: 204.68 E-value: 3.31e-59

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1726 ITADSSNHPDNKHKNRYINIVAYDHSRVKLAQLAEKDgKLTDYINANYVDGYN-RPKAYIAAQGPLKSTAEDFWRMIWEH 1804
Cdd:cd14612      5 VSPEELDIPGHASKDRYKTILPNPQSRVCLRRAGSQE-EEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQE 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1805 NVEVIVMITNLVEKgRRKCDQYWPaDGSEEYGNFLVTQKSVQVLAYYTVRNFTlrntkIKKGSQKgrpsgRVVTQYHYTQ 1884
Cdd:cd14612     84 ECPIIVMITKLKEK-KEKCVHYWP-EKEGTYGRFEIRVQDMKECDGYTIRDLT-----IQLEEES-----RSVKHYWFSS 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1885 WPDMGVPEYSLPVLTFVRKAAYAKRHAV--GPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLV 1962
Cdd:cd14612    152 WPDHQTPESAGPLLRLVAEVEESRQTAAspGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMI 231

                          250
                   ....*....|...
gi 1609046161 1963 QTEEQYVFIHDTL 1975
Cdd:cd14612    232 QTSEQYQFLHHTL 244

PTPc-N3_4

cd14541

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...

1767-1981

7.83e-59

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: 202.17 E-value: 7.83e-59

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1767 DYINANYVDgYNRPKA-----YIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPA-DGSEEYGNFLV 1840
Cdd:cd14541      1 DYINANYVN-MEIPGSgivnrYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDlGETMQFGNLQI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1841 TQKSVQVLAYYTVRNFTLRNTKIKKgsqkgrpsGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVHCS 1920
Cdd:cd14541     80 TCVSEEVTPSFAFREFILTNTNTGE--------ERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVEPTVVHCS 151

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1609046161 1921 AGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIhdtlVEAILS 1981
Cdd:cd14541    152 AGIGRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFV----CEAILR 208

R-PTP-N

cd14609

PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...

1705-1979

1.53e-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: 204.12 E-value: 1.53e-58

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1705 EEFETLKEFYQEVQSCtvdlgitaDSSNHPDNKHKNRYINIVAYDHSRVKLAqlAEKDGKLTDYINAN-YVDGYNRPKAY 1783
Cdd:cd14609     19 KEWQALCAYQAEPNTC--------STAQGEANVKKNRNPDFVPYDHARIKLK--AESNPSRSDYINASpIIEHDPRMPAY 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1784 IAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQVLAY-YTVRNFTLRNTK 1862
Cdd:cd14609     89 IATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYHIYEVNLVSEHIWCEdFLVRSFYLKNVQ 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1863 IKKgsqkgrpsGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQhE 1942
Cdd:cd14609    169 TQE--------TRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMA-K 239

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1609046161 1943 GT--VNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAI 1979
Cdd:cd14609    240 GVkeIDIAATLEHVRDQRPGMVRTKDQFEFALTAVAEEV 278

PTPc

cd00047

catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...

2063-2263

2.67e-58

Pssm-ID: 350343 [Multi-domain] Cd Length: 200 Bit Score: 200.20 E-value: 2.67e-58

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2063 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPD----GQNMAEDefvYWPNK-DEPINCESFKVTL 2137
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNlvekGREKCER---YWPEEgGKPLEYGDITVTL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2138 MAEEHKclsneEKLIIQDFILEATQDDYVLEVRHFQCPKWPN---PDSPISkTFELISVIKEEAANRDGPMIVHDEHGGV 2214
Cdd:cd00047     78 VSEEEL-----SDYTIRTLELSPKGCSESREVTHLHYTGWPDhgvPSSPED-LLALVRRVRKEARKPNGPIVVHCSAGVG 151

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1609046161 2215 TAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYK 2263
Cdd:cd00047    152 RTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200

PTPc-N12

cd14604

catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...

1735-1972

3.49e-58

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: 204.01 E-value: 3.49e-58

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1735 DNKHKNRYINIVAYDHSRVKLA-QLAEKDgklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMIT 1813
Cdd:cd14604     56 ENVKKNRYKDILPFDHSRVKLTlKTSSQD---SDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMAC 132

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1814 NLVEKGRRKCDQYWPADGSE--EYGNFLVTQKSVQVLAYYTVRNFTLrntkikkgsqKGRPSGRVVTQYHYTQWPDMGVP 1891
Cdd:cd14604    133 REFEMGRKKCERYWPLYGEEpmTFGPFRISCEAEQARTDYFIRTLLL----------EFQNETRRLYQFHYVNWPDHDVP 202

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1892 EYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGRTGTYIVLD---SMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQY 1968
Cdd:cd14604    203 SSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDytwNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQY 282


                   ....
gi 1609046161 1969 VFIH 1972
Cdd:cd14604    283 ELVH 286

R-PTPc-A-2

cd14623

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...

1741-1977

3.97e-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: 201.04 E-value: 3.97e-58

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1741 RYINIVAYDHSRVKLAqlAEKDGKLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGR 1820
Cdd:cd14623      1 RVLQIIPYEFNRVIIP--VKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1821 RKCDQYWPADGSEEYGNFLVTQKSVQVLAYYTVRNFTLRNTKIKKgsqkgrpsGRVVTQYHYTQWPDMGVPEYSLPVLTF 1900
Cdd:cd14623     79 EKCAQYWPSDGSVSYGDITIELKKEEECESYTVRDLLVTNTRENK--------SRQIRQFHFHGWPEVGIPSDGKGMINI 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1901 VrkAAYAKRHAVG---PVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1977
Cdd:cd14623    151 I--AAVQKQQQQSgnhPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228

R-PTP-N2

cd14610

PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...

1705-1979

6.10e-58

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: 202.59 E-value: 6.10e-58

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1705 EEFETLKEFYQEVQSCTVDLgitadssnHPDNKHKNRYINIVAYDHSRVKLAqlAEKDGKLTDYINANYV-DGYNRPKAY 1783
Cdd:cd14610     21 KEWEALCAYQAEPNATNVAQ--------REENVQKNRSLAVLPYDHSRIILK--AENSHSHSDYINASPImDHDPRNPAY 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1784 IAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQVLAY-YTVRNFTLRNTK 1862
Cdd:cd14610     91 IATQGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYHIYEVNLVSEHIWCEdFLVRSFYLKNLQ 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1863 IKKgsqkgrpsGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQI-QH 1941
Cdd:cd14610    171 TNE--------TRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMaKG 242

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1609046161 1942 EGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAI 1979
Cdd:cd14610    243 AKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAVAEEV 280

alpha_CA_VI_IX_XII_XIV

cd03123

Carbonic anhydrase alpha, isozymes VI, IX, XII and XIV. Carbonic anhydrases (CAs) are ...

32-286

8.02e-58

Carbonic anhydrase alpha, isozymes VI, IX, XII and XIV. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Alpha CAs are mostly monomeric enzymes. The zinc ion is complexed by three histidine residues. This sub-family comprises the secreted CA VI, which is found in saliva, for example, and the membrane proteins CA IX, XII, and XIV.

Pssm-ID: 239397 [Multi-domain] Cd Length: 248 Bit Score: 201.00 E-value: 8.02e-58

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161   32 QKNWGKKYPTCNSPKQSPINIDEDLTQVNVNLKKLKFQGWDKTSLENTFIHNTGKTVEINLTNDYRVSGGVSEmVFKASK 111
Cdd:cd03123      2 EDHWPKKYPACGGKRQSPIDIQTDIVQFDPSLPPLELVGYDLPGTEEFTLTNNGHTVQLSLPPTMHIRGGPGT-EYTAAQ 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  112 ITFHWGKCNMSSdGSEHSLEGQKFPLEMQIYCFDADRFSSFEEAVKGKGKLRALSILFEVGTEENLDFKAIIDGVESVSR 191
Cdd:cd03123     81 LHLHWGGRGSLS-GSEHTIDGIRFAAELHIVHYNSDKYSSFDEAADKPDGLAVLAILIEVGYPENTYYEKIISHLHEIKY 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  192 FGKQAALDPFILLNLLPNSTDKYYIYNGSLTSPPCTDTVDWIVFKDTVSISESQLavfcevLTMQQSgyvmLMDY----L 267
Cdd:cd03123    160 KGQETTVPGFNVRELLPEDLSHYYRYEGSLTTPPCYESVLWTVFRDPVTLSKEQL------ETLENT----LMDThnktL 229

                          250
                   ....*....|....*....
gi 1609046161  268 QNNFREQQYKFSRQVFSSY 286
Cdd:cd03123    230 QNNYRATQPLNGRVVEASF 248

PTPc-N11

cd14605

catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...

1735-1972

9.75e-58

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: 201.01 E-value: 9.75e-58

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1735 DNKHKNRYINIVAYDHSRVKLAQlAEKDGKLTDYINANYVDGYN-------RPK-AYIAAQGPLKSTAEDFWRMIWEHNV 1806
Cdd:cd14605      1 ENKNKNRYKNILPFDHTRVVLHD-GDPNEPVSDYINANIIMPEFetkcnnsKPKkSYIATQGCLQNTVNDFWRMVFQENS 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1807 EVIVMITNLVEKGRRKCDQYWPADGS-EEYGNFLVTQKSVQVLAYYTVRNFTLrnTKIKKGSQKgrpsgRVVTQYHYTQW 1885
Cdd:cd14605     80 RVIVMTTKEVERGKSKCVKYWPDEYAlKEYGVMRVRNVKESAAHDYILRELKL--SKVGQGNTE-----RTVWQYHFRTW 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1886 PDMGVPEYSLPVLTFVRKAAYaKRHAV---GPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGT---VNIFGFLKHIRSQRN 1959
Cdd:cd14605    153 PDHGVPSDPGGVLDFLEEVHH-KQESImdaGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRS 231

                          250
                   ....*....|...
gi 1609046161 1960 YLVQTEEQYVFIH 1972
Cdd:cd14605    232 GMVQTEAQYRFIY 244

PTPc-N21_14

cd14540

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...

1768-1977

2.18e-57

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: 198.45 E-value: 2.18e-57

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1768 YINANYVDGY--NRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEE----YGNFLVT 1841
Cdd:cd14540      1 YINASHITATvgGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEHdaltFGEYKVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1842 QKSVQVLAYYTVRNFTLRNTkikkgsqkgrPSGRVVTQYH--YTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVG------ 1913
Cdd:cd14540     81 TKFSVSSGCYTTTGLRVKHT----------LSGQSRTVWHlqYTDWPDHGCPEDVSGFLDFLEEINSVRRHTNQdvaghn 150

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1609046161 1914 ---PVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1977
Cdd:cd14540    151 rnpPTLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQ 217

PTPc-N22

cd14602

catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...

1739-1977

4.82e-57

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: 198.14 E-value: 4.82e-57

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1739 KNRYINIVAYDHSRVKLAQLAEKDGklTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEK 1818
Cdd:cd14602      1 KNRYKDILPYDHSRVELSLITSDED--SDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEM 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1819 GRRKCDQYWPADGSE--EYGNFLVTQKSVQVLAYYTVRnfTLrntKIKKGSQKgrpsgRVVTQYHYTQWPDMGVPEYSLP 1896
Cdd:cd14602     79 GKKKCERYWAEPGEMqlEFGPFSVTCEAEKRKSDYIIR--TL---KVKFNSET-----RTIYQFHYKNWPDHDVPSSIDP 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1897 VLTFVRKAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQhEGTV----NIFGFLKHIRSQRNYLVQTEEQYVFIH 1972
Cdd:cd14602    149 ILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLK-DGIIpenfSVFSLIQEMRTQRPSLVQTKEQYELVY 227


                   ....*
gi 1609046161 1973 DTLVE 1977
Cdd:cd14602    228 NAVIE 232

PTPc-N3

cd14600

catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...

1734-1980

8.09e-57

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: 198.92 E-value: 8.09e-57

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1734 PDNKHKNRYINIVAYDHSRVKLaqlaekDGKlTDYINANYVD----GYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVI 1809
Cdd:cd14600     38 PQNMDKNRYKDVLPYDATRVVL------QGN-EDYINASYVNmeipSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLI 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1810 VMITNLVEKGRRKCDQYWPaDGSE--EYGNFLVTQKSVQVLAYYTVRNFTLrnTKIKKGSQkgrpsgRVVTQYHYTQWPD 1887
Cdd:cd14600    111 VMLTTLTERGRTKCHQYWP-DPPDvmEYGGFRVQCHSEDCTIAYVFREMLL--TNTQTGEE------RTVTHLQYVAWPD 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1888 MGVPEYSLPVLTFVrKAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQ 1967
Cdd:cd14600    182 HGVPDDSSDFLEFV-NYVRSKRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQ 260

                          250
                   ....*....|...
gi 1609046161 1968 YVFIhdtlVEAIL 1980
Cdd:cd14600    261 YKFV----CEAIL 269

R-PTP-N-N2

cd14546

PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...

1768-1979

2.45e-56

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: 194.97 E-value: 2.45e-56

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1768 YINANYVDGYN-RPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQ 1846
Cdd:cd14546      1 YINASTIYDHDpRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHIYEVHLVSEH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1847 VL-AYYTVRNFTLRNTKIKKgsqkgrpsGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGR 1925
Cdd:cd14546     81 IWcDDYLVRSFYLKNLQTSE--------TRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRGRSCPIVVHCSDGAGR 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1609046161 1926 TGTYIVLDSMLQQIQhEGT--VNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAI 1979
Cdd:cd14546    153 TGTYILIDMVLNRMA-KGAkeIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAEEV 207

PTPc-N5

cd14613

catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...

1739-1975

3.89e-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: 196.62 E-value: 3.89e-56

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1739 KNRYINIVAYDHSRVKLAQlAEKDGKLTDYINANYVDGYN-RPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVE 1817
Cdd:cd14613     28 KNRYKTILPNPHSRVCLTS-PDQDDPLSSYINANYIRGYGgEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEE 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1818 KGRrKCDQYWPADgSEEYGNFLVTQKSVQVLAYYTVRNFTLrntkiKKGSQKgrpsgRVVTQYHYTQWPDMGVPEYSLPV 1897
Cdd:cd14613    107 MNE-KCTEYWPEE-QVTYEGIEITVKQVIHADDYRLRLITL-----KSGGEE-----RGLKHYWYTSWPDQKTPDNAPPL 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1898 LTFVRKAAYAKRHA---VGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDT 1974
Cdd:cd14613    175 LQLVQEVEEARQQAepnCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHV 254


                   .
gi 1609046161 1975 L 1975
Cdd:cd14613    255 L 255

R-PTPc-R

cd14611

catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...

1739-1972

5.83e-56

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: 194.75 E-value: 5.83e-56

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1739 KNRYINIVAYDHSRVKLAQLAEKDgKLTDYINANYVDGY-NRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVE 1817
Cdd:cd14611      2 KNRYKTILPNPHSRVCLKPKNSND-SLSTYINANYIRGYgGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1818 KGRrKCDQYWPaDGSEEYGNFLVTQKSVQVLAYYTVRNFTLrntkiKKGSQKgrpsgRVVTQYHYTQWPDMGVPEYSLPV 1897
Cdd:cd14611     81 KNE-KCVLYWP-EKRGIYGKVEVLVNSVKECDNYTIRNLTL-----KQGSQS-----RSVKHYWYTSWPDHKTPDSAQPL 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1898 LTFV------RKAAYAKrhavGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFI 1971
Cdd:cd14611    149 LQLMldveedRLASPGR----GPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFV 224


                   .
gi 1609046161 1972 H 1972
Cdd:cd14611    225 H 225

R-PTPc-E-2

cd14622

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...

1767-1972

2.27e-54

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: 189.45 E-value: 2.27e-54

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1767 DYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQ 1846
Cdd:cd14622      1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVTHGEITIEIKNDT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1847 VLAYYTVRNFTLRNTKIKKgsqkgrpsGRVVTQYHYTQWPDMGVPEYSLPVLTFVrKAAYAKRHAVG--PVVVHCSAGVG 1924
Cdd:cd14622     81 LLETISIRDFLVTYNQEKQ--------TRLVRQFHFHGWPEIGIPAEGKGMIDLI-AAVQKQQQQTGnhPIVVHCSAGAG 151

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1609046161 1925 RTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 1972
Cdd:cd14622    152 RTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCY 199

PHA02738

hypothetical protein; Provisional

1708-1987

7.56e-54

hypothetical protein; Provisional

Pssm-ID: 222923 [Multi-domain] Cd Length: 320 Bit Score: 192.06 E-value: 7.56e-54

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1708 ETLKEFYQEVQSCTVDLGITADSSNhpdnKHKNRYINIVAYDHSRVKLAqlAEKDgkLTDYINANYVDGYNRPKAYIAAQ 1787
Cdd:PHA02738    25 EVITREHQKVISEKVDGTFNAEKKN----RKLNRYLDAVCFDHSRVILP--AERN--RGDYINANYVDGFEYKKKFICGQ 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1788 GPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWP--ADGSEEYGNFLVTQKSVQVLAYYTVRNFTLRNtkikk 1865
Cdd:PHA02738    97 APTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREKCFPYWSdvEQGSIRFGKFKITTTQVETHPHYVKSTLLLTD----- 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1866 gsqkGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFV------RKAAYAKRHAVG-------PVVVHCSAGVGRTGTYIVL 1932
Cdd:PHA02738   172 ----GTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVlevrqcQKELAQESLQIGhnrlqppPIVVHCNAGLGRTPCYCVV 247

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1609046161 1933 DSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAILSKETEVL 1987
Cdd:PHA02738   248 DISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAVKRYVNLTVNKVS 302

PTPc-N13

cd14597

catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...

1735-1970

1.59e-52

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: 185.03 E-value: 1.59e-52

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1735 DNKHKNRYINIVAYDHSRVKLAQlaekDGkltDYINANYVD---GyNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVM 1811
Cdd:cd14597      2 ENRKKNRYKNILPYDTTRVPLGD----EG---GYINASFIKmpvG-DEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAM 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1812 ITNLVEKGRRKCDQYWPadgsEEYGNFLVTQKSVQV--LAYYTVRNFTLRNTKIKKgSQKGRPsgRVVTQYHYTQWPDMG 1889
Cdd:cd14597     74 MTQEVEGGKIKCQRYWP----EILGKTTMVDNRLQLtlVRMQQLKNFVIRVLELED-IQTREV--RHITHLNFTAWPDHD 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1890 VPEYSLPVLTFVrkaAYAKR-HAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQY 1968
Cdd:cd14597    147 TPSQPEQLLTFI---SYMRHiHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQY 223


                   ..
gi 1609046161 1969 VF 1970
Cdd:cd14597    224 IF 225

PTPc-N1

cd14608

catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...

1714-1977

2.08e-52

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: 186.38 E-value: 2.08e-52

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1714 YQEVQSCTVDLgiTADSSNHPDNKHKNRYINIVAYDHSRVKLAQlaekdgKLTDYINANYVDGYNRPKAYIAAQGPLKST 1793
Cdd:cd14608      5 YQDIRHEASDF--PCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQ------EDNDYINASLIKMEEAQRSYILTQGPLPNT 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1794 AEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEY----GNFLVTQKSVQVLAYYTVRNFTLRNTKIKKgsqk 1869
Cdd:cd14608     77 CGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMifedTNLKLTLISEDIKSYYTVRQLELENLTTQE---- 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1870 grpsGRVVTQYHYTQWPDMGVPEYSLPVLTFVRK----AAYAKRHavGPVVVHCSAGVGRTGTYIVLDS---MLQQIQHE 1942
Cdd:cd14608    153 ----TREILHFHYTTWPDFGVPESPASFLNFLFKvresGSLSPEH--GPVVVHCSAGIGRSGTFCLADTcllLMDKRKDP 226

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1609046161 1943 GTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1977
Cdd:cd14608    227 SSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIE 261

PTPc-N2

cd14607

catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...

1714-1970

7.33e-52

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: 184.01 E-value: 7.33e-52

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1714 YQEVQSCTVDLGITAdsSNHPDNKHKNRYINIVAYDHSRVKLaQLAEkdgklTDYINANYVDGYNRPKAYIAAQGPLKST 1793
Cdd:cd14607      4 YLEIRNESHDYPHRV--AKYPENRNRNRYRDVSPYDHSRVKL-QNTE-----NDYINASLVVIEEAQRSYILTQGPLPNT 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1794 AEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYG----NFLVTQKSVQVLAYYTVRNFTLRNtkIKKGSQk 1869
Cdd:cd14607     76 CCHFWLMVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSfketGFSVKLLSEDVKSYYTVHLLQLEN--INSGET- 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1870 grpsgRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAV--GPVVVHCSAGVGRTGTYIVLDS--MLQQIQHEGTV 1945
Cdd:cd14607    153 -----RTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPehGPAVVHCSAGIGRSGTFSLVDTclVLMEKKDPDSV 227

                          250       260
                   ....*....|....*....|....*
gi 1609046161 1946 NIFGFLKHIRSQRNYLVQTEEQYVF 1970
Cdd:cd14607    228 DIKQVLLDMRKYRMGLIQTPDQLRF 252

alpha_CA_XII_XIV

cd03126

Carbonic anhydrase alpha, isozymes XII and XIV. Carbonic anhydrases (CAs) are zinc-containing ...

32-286

3.81e-51

Carbonic anhydrase alpha, isozymes XII and XIV. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidine residues. This sub-family comprises the membrane proteins CA XII and XIV.

Pssm-ID: 239400 Cd Length: 249 Bit Score: 181.57 E-value: 3.81e-51

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161   32 QKNWGKKYPTCNSPKQSPINIDEDLTQVNVNLKKLKFQGWDKTSLENTFIHNTGKTVEINLTNDYRVSGGVSEmvFKASK 111
Cdd:cd03126      2 ENSWPKKYPFCGGVAQSPIDIHTDILQYDSSLPPLEFHGYNVSGTEQFTLTNNGHTVQLSLPPTMHIGGLPFK--YTASQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  112 ITFHWGKCNmSSDGSEHSLEGQKFPLEMQIYCFDADRFSSFEEAVKGKGKLRALSILFEVGtEENLDFKAIIDGVESVSR 191
Cdd:cd03126     80 LHLHWGQRG-SPEGSEHTISGKHFAAELHIVHYNSDKYPDISTAMNKSQGLAVLGILIEVG-PFNPSYEKIFSHLHEVKY 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  192 FGKQAALDPFILLNLLPNSTDKYYIYNGSLTSPPCTDTVDWIVFKDTVSISESQLavfcevLTMQQSGYVMLMD---YLQ 268
Cdd:cd03126    158 KDQKVSVPGFNVQELLPKRLDEYYRYEGSLTTPPCYPSVLWTVFRNPVQISQEQL------LALETALYSTEEDesrEMV 231

                          250
                   ....*....|....*...
gi 1609046161  269 NNFREQQYKFSRQVFSSY 286
Cdd:cd03126    232 NNYRQVQPFNERLVFASF 249

R-PTP-C-2

cd14558

PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...

1768-1973

1.02e-50

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: 178.74 E-value: 1.02e-50

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1768 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPaDGSEEYGNFLVTQKSVQV 1847
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWG-DEKKTYGDIEVELKDTEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1848 LAYYTVRNFTLRNTKIKKgsqkgrpsGRVVTQYHYTQWPDMGVPEYSLPVLTFVRKA------AYAKRHAVGPVVVHCSA 1921
Cdd:cd14558     80 SPTYTVRVFEITHLKRKD--------SRTVYQYQYHKWKGEELPEKPKDLVDMIKSIkqklpyKNSKHGRSVPIVVHCSD 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1609046161 1922 GVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHD 1973
Cdd:cd14558    152 GSSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203

alpha_CA_IV_XV_like

cd03117

Carbonic anhydrase alpha, CA_IV, CA_XV, like isozymes. Carbonic anhydrases (CAs) are ...

45-284

1.03e-50

Carbonic anhydrase alpha, CA_IV, CA_XV, like isozymes. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidine residues. This subgroup, restricted to animals, contains isozyme IV and similar proteins such as mouse CA XV. Isozymes IV is attached to membranes via a glycosylphosphatidylinositol (GPI) tail. In mammals, Isozyme IV plays crucial roles in kidney and lung function, amongst others. This subgroup also contains the dual domain CA from the giant clam, Tridacna gigas. T. gigas CA plays a role in the movement of inorganic carbon from the surrounding seawater to the symbiotic algae found in the clam's tissues. CA XV is expressed in several species but not in humans or chimps. Similar to isozyme CA IV, CA XV attaches to membranes via a GPI tail.

Pssm-ID: 239391 Cd Length: 234 Bit Score: 179.77 E-value: 1.03e-50

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161   45 PKQSPINIDEDLTQVNVNLKKLKFQGWDKTSLeNTFIHNTGKTVEINLTNDYRVSGGVSEMVFKASKITFHWGkcNMSSD 124
Cdd:cd03117      2 KRQSPINIVTKKVQYDENLTPFTFTGYDDTTT-NWTITNNGHTVQVTLPDGAKISGGGLPGTYKALQFHFHWG--SNGSP 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  125 GSEHSLEGQKFPLEMQIYCFDADrFSSFEEAVKGKGKLRALSILFEVGTEENLDFKAIIDGVESVSRFGKQAALDPFILL 204
Cdd:cd03117     79 GSEHTIDGERYPMELHIVHIKES-YNSLLEALKDSDGLAVLGFFIEEGEEENTNFDPLISALSNIPQKGGSTNLTPFSLR 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  205 NLLP-NSTDKYYIYNGSLTSPPCTDTVDWIVFKDTVSISESQLAVFCEVLTMQQSGYVMLMdylqNNFREQQYKFSRQVF 283
Cdd:cd03117    158 SLLPsVLLTKYYRYNGSLTTPGCNEAVIWTVFEEPIPISRAQLDAFSTVLFFDTDNGQPMV----NNFRPVQPLNGRVVY 233


                   .
gi 1609046161  284 S 284
Cdd:cd03117    234 A 234

PTPc-N20

cd14596

catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...

1768-1979

5.69e-50

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: 176.86 E-value: 5.69e-50

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1768 YINANYVDGYNRPKA--YIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWP--ADGSEEYGNFLVTQK 1843
Cdd:cd14596      1 YINASYITMPVGEEElfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPetLQEPMELENYQLRLE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1844 SVQVLAYYTVRNFTLrntkikkgSQKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFVRkaaYAKR-HAVGPVVVHCSAG 1922
Cdd:cd14596     81 NYQALQYFIIRIIKL--------VEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFIC---YMRKvHNTGPIVVHCSAG 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1609046161 1923 VGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAI 1979
Cdd:cd14596    150 IGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVL 206

PTPc-N4

cd14601

catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...

1767-1980

1.08e-48

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: 173.21 E-value: 1.08e-48

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1767 DYINANYVDG-------YNRpkaYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWP-ADGSEEYGNF 1838
Cdd:cd14601      1 DYINANYINMeipsssiINR---YIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPePSGSSSYGGF 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1839 LVTQKSVQVLAYYTVRNFTLRNTKikkgSQKGRPsgrvVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVGPVVVH 1918
Cdd:cd14601     78 QVTCHSEEGNPAYVFREMTLTNLE----KNESRP----LTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEPVVVH 149

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1609046161 1919 CSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIhdtlVEAIL 1980
Cdd:cd14601    150 CSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFV----CEAIL 207

PTPc-N14

cd14599

catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...

1734-1977

1.11e-48

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: 175.96 E-value: 1.11e-48

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1734 PDNKHKNRYINIVAYDHSRVKLAQLAEKDgklTDYINANYVDGYNRPKA--YIAAQGPLKSTAEDFWRMIWEHNVEVIVM 1811
Cdd:cd14599     36 PENAERNRIREVVPYEENRVELVPTKENN---TGYINASHIKVTVGGEEwhYIATQGPLPHTCHDFWQMVWEQGVNVIAM 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1812 ITNLVEKGRRKCDQYWPADG----SEEYGNFLVTQKSVQVLAYYTVRNFTLRNtkIKKGSQkgrpsgRVVTQYHYTQWPD 1887
Cdd:cd14599    113 VTAEEEGGRSKSHRYWPKLGskhsSATYGKFKVTTKFRTDSGCYATTGLKVKH--LLSGQE------RTVWHLQYTDWPD 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1888 MGVPEYSLPVLTFVRKAAYAKRHAVG----------PVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQ 1957
Cdd:cd14599    185 HGCPEEVQGFLSYLEEIQSVRRHTNSmldstkncnpPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRHLREQ 264

                          250       260
                   ....*....|....*....|
gi 1609046161 1958 RNYLVQTEEQYVFIHDTLVE 1977
Cdd:cd14599    265 RMFMIQTIAQYKFVYQVLIQ 284

R-PTP-D-2

cd14628

PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...

1984-2271

1.02e-46

Pssm-ID: 350476 [Multi-domain] Cd Length: 292 Bit Score: 170.68 E-value: 1.02e-46

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1984 TEVLDSHIHAYVNALL-IPGPAGKTKLEKQFQLLSQSNIQQSDYSAALKQCNREKNRTSSIIPVERSRVGISSLSG-EGT 2061
Cdd:cd14628      1 TEVPARNLYAYIQKLTqIETGENVTGMELEFKRLASSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGvEGS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2062 DYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDE-FVYWPnKDEPINCESFKVTLMAE 2140
Cdd:cd14628     81 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKcHQYWP-AERSARYQYFVVDPMAE 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2141 ehkclSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISVI--KEEAANRDGPMIVHDEHGGVTA 2216
Cdd:cd14628    160 -----YNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEgfIDFIGQVhkTKEQFGQDGPISVHCSAGVGRT 234

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1609046161 2217 GTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVILSLVST 2271
Cdd:cd14628    235 GVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYLGS 289

PTP-N23

cd14539

PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...

1768-1973

1.21e-46

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: 167.18 E-value: 1.21e-46

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1768 YINANYVDGY-NRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPAD-GSE-EYGNFLVTQKS 1844
Cdd:cd14539      1 YINASLIEDLtPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErGQAlVYGAITVSLQS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1845 VQVLAYYTVRNFTlrntkIKKGSQKGRpsgRVVTQYHYTQWPDMGVPEYSLPVLTF---VRKAAYAKRHAVGPVVVHCSA 1921
Cdd:cd14539     81 VRTTPTHVERIIS-----IQHKDTRLS---RSVVHLQFTTWPELGLPDSPNPLLRFieeVHSHYLQQRSLQTPIVVHCSS 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1609046161 1922 GVGRTGTYIVLDSMLQQIQHE-GTVNIFGFLKHIRSQRNYLVQTEEQYVFIHD 1973
Cdd:cd14539    153 GVGRTGAFCLLYAAVQEIEAGnGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205

R-PTP-LAR-2

cd14554

PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...

2033-2266

6.13e-46

Pssm-ID: 350402 [Multi-domain] Cd Length: 238 Bit Score: 166.55 E-value: 6.13e-46

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2033 CNREKNRTSSIIPVERSRVGISSLSG-EGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQ 2111
Cdd:cd14554      5 CNKFKNRLVNILPYESTRVCLQPIRGvEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLR 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2112 NMAEDE-FVYWPNkDEPINCESFKVTLMAEehkclSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPisKTFE- 2189
Cdd:cd14554     85 EMGREKcHQYWPA-ERSARYQYFVVDPMAE-----YNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVP--KSGEg 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2190 LISVIKE-----EAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKV 2264
Cdd:cd14554    157 FIDFIGQvhktkEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236


                   ..
gi 1609046161 2265 IL 2266
Cdd:cd14554    237 AL 238

PHA02747

protein tyrosine phosphatase; Provisional

1727-1972

6.60e-46

protein tyrosine phosphatase; Provisional

Pssm-ID: 165114 [Multi-domain] Cd Length: 312 Bit Score: 169.03 E-value: 6.60e-46

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1727 TADSSNHPDNKHKNRYINIVAYDHSRVKLAQlaeKDGKLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNV 1806
Cdd:PHA02747    42 LIANFEKPENQPKNRYWDIPCWDHNRVILDS---GGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHC 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1807 EVIVMIT-NLVEKGRRKCDQYW--PADGSEEYGNFLVTQKSVQVLAYYTVRNFTLRNtKIKKGSQKgrpsgrvVTQYHYT 1883
Cdd:PHA02747   119 SIIVMLTpTKGTNGEEKCYQYWclNEDGNIDMEDFRIETLKTSVRAKYILTLIEITD-KILKDSRK-------ISHFQCS 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1884 QWPDMGVPEYSLPVLTFVR----------KAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKH 1953
Cdd:PHA02747   191 EWFEDETPSDHPDFIKFIKiidinrkksgKLFNPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEK 270

                          250
                   ....*....|....*....
gi 1609046161 1954 IRSQRNYLVQTEEQYVFIH 1972
Cdd:PHA02747   271 IREQRHAGIMNFDDYLFIQ 289

PTPc_plant_PTP1

cd17658

protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...

1768-1972

7.15e-46

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: 164.94 E-value: 7.15e-46

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1768 YINANYV---DGYNRPKaYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRR-KCDQYWPAD--GSEEYGNFLVT 1841
Cdd:cd17658      1 YINASLVetpASESLPK-FIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEenESREFGRISVT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1842 QKSVQvlayYTVRNFTLRNTKIKKGSQKGRPsgRVVTQYHYTQWPDMGVPEYSLPVLTFVrKAAYAKRHAVGPVVVHCSA 1921
Cdd:cd17658     80 NKKLK----HSQHSITLRVLEVQYIESEEPP--LSVLHIQYPEWPDHGVPKDTRSVRELL-KRLYGIPPSAGPIVVHCSA 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1609046161 1922 GVGRTGTYIVLDSMLQQIQhEG---TVNIFGFLKHIRSQRNYLVQTEEQYVFIH 1972
Cdd:cd17658    153 GIGRTGAYCTIHNTIRRIL-EGdmsAVDLSKTVRKFRSQRIGMVQTQDQYIFCY 205

R-PTPc-typeIIb-2

cd14556

PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...

1768-1973

1.64e-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: 163.73 E-value: 1.64e-45

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1768 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMItNLVEKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 1847
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVML-NQLDPKDQSCPQYWPDEGSGTYGPIQVEFVSTTI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1848 LAYYTVRNFTLRNTKikkgsqkgRPS--GRVVTQYHYTQWPDMG----VPEYSLPVLTFVRKaaYAKRHAVGPVVVHCSA 1921
Cdd:cd14556     80 DEDVISRIFRLQNTT--------RPQegYRMVQQFQFLGWPRDRdtppSKRALLKLLSEVEK--WQEQSGEGPIVVHCLN 149

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1609046161 1922 GVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHD 1973
Cdd:cd14556    150 GVGRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201

R-PTP-S-2

cd14627

PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...

1984-2271

1.74e-45

Pssm-ID: 350475 [Multi-domain] Cd Length: 290 Bit Score: 166.83 E-value: 1.74e-45

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1984 TEVLDSHIHAYVNALLIPGPAGK-TKLEKQFQLLSQSNIQQSDYSAALKQCNREKNRTSSIIPVERSRVGISSLSG-EGT 2061
Cdd:cd14627      2 TEVPARNLYSYIQKLAQVEVGEHvTGMELEFKRLANSKAHTSRFISANLPCNKFKNRLVNIMPYETTRVCLQPIRGvEGS 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2062 DYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDE-FVYWPnKDEPINCESFKVTLMAE 2140
Cdd:cd14627     82 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKcHQYWP-AERSARYQYFVVDPMAE 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2141 ehkclSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISVI--KEEAANRDGPMIVHDEHGGVTA 2216
Cdd:cd14627    161 -----YNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEgfIDFIGQVhkTKEQFGQDGPISVHCSAGVGRT 235

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1609046161 2217 GTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVILSLVST 2271
Cdd:cd14627    236 GVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYLGS 290

PHA02742

protein tyrosine phosphatase; Provisional

1736-1977

3.28e-45

protein tyrosine phosphatase; Provisional

Pssm-ID: 165109 [Multi-domain] Cd Length: 303 Bit Score: 166.72 E-value: 3.28e-45

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1736 NKHKNRYINIVAYDHSRVKLAQlaeKDGkLTDYINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNL 1815
Cdd:PHA02742    52 NMKKCRYPDAPCFDRNRVILKI---EDG-GDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKI 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1816 VEKGRRKCDQYWPAD--GSEEYGNFLVTQKSVQVLAYYTVRNFTLRNTKikkgsqkgrpSGRV--VTQYHYTQWPDMGVP 1891
Cdd:PHA02742   128 MEDGKEACYPYWMPHerGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTN----------TGASldIKHFAYEDWPHGGLP 197

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1892 EYSLPVLTFVRKAAYAK-----------RHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNY 1960
Cdd:PHA02742   198 RDPNKFLDFVLAVREADlkadvdikgenIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHN 277

                          250
                   ....*....|....*..
gi 1609046161 1961 LVQTEEQYVFIHDTLVE 1977
Cdd:PHA02742   278 CLSLPQQYIFCYFIVLI 294

R-PTP-F-2

cd14629

PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...

1984-2271

6.20e-45

Pssm-ID: 350477 [Multi-domain] Cd Length: 291 Bit Score: 165.28 E-value: 6.20e-45

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1984 TEVLDSHIHAYVNAL-LIPGPAGKTKLEKQFQLLSQSNIQQSDYSAALKQCNREKNRTSSIIPVERSRVGISSLSG-EGT 2061
Cdd:cd14629      2 TEVPARNLYAHIQKLtQVPPGESVTAMELEFKLLANSKAHTSRFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGvEGS 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2062 DYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDE-FVYWPnKDEPINCESFKVTLMAE 2140
Cdd:cd14629     82 DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKcHQYWP-AERSARYQYFVVDPMAE 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2141 ehkclSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPisKTFE-LISVIKE-----EAANRDGPMIVHDEHGGV 2214
Cdd:cd14629    161 -----YNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVP--KTGEgFIDFIGQvhktkEQFGQDGPITVHCSAGVG 233

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1609046161 2215 TAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVILSLVST 2271
Cdd:cd14629    234 RTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEYLGS 290

PHA02746

protein tyrosine phosphatase; Provisional

1727-1980

1.79e-44

protein tyrosine phosphatase; Provisional

Pssm-ID: 165113 [Multi-domain] Cd Length: 323 Bit Score: 165.20 E-value: 1.79e-44

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1727 TADSSNHPDNKHKNRYINIVAYDHSRV--------KLAQLAEKDGKL---------TDYINANYVDGYNRPKAYIAAQGP 1789
Cdd:PHA02746    42 TTNHFLKKENLKKNRFHDIPCWDHSRVvinaheslKMFDVGDSDGKKievtsednaENYIHANFVDGFKEANKFICAQGP 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1790 LKSTAEDFWRMIWEHNVEVIVMITNlVEKGRRKCDQYW--PADGSEEYGNFLvtqksVQVLAYYTVRNFTLRNTKIkkgS 1867
Cdd:PHA02746   122 KEDTSEDFFKLISEHESQVIVSLTD-IDDDDEKCFELWtkEEDSELAFGRFV-----AKILDIIEELSFTKTRLMI---T 192

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1868 QKGRPSGRVVTQYHYTQWPDMGVPEYSLPVLTFV----------RKAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQ 1937
Cdd:PHA02746   193 DKISDTSREIHHFWFPDWPDNGIPTGMAEFLELInkvneeqaelIKQADNDPQTLGPIVVHCSAGIGRAGTFCAIDNALE 272

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1609046161 1938 QIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVEAIL 1980
Cdd:PHA02746   273 QLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKALKYAII 315

R3-PTPc

cd14548

catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...

2039-2263

6.66e-44

Pssm-ID: 350396 [Multi-domain] Cd Length: 222 Bit Score: 159.83 E-value: 6.66e-44

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2039 RTSSIIPVERSRVGISSLSG-EGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdgQNMAEDE 2117
Cdd:cd14548      1 RYTNILPYDHSRVKLIPINEeEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVML---TQCMEKG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2118 FV----YWPNKDEPINCESFKVTLMAEEHkclsnEEKLIIQDFILEatQDDYVLEVRHFQCPKWPN---PDSPISkTFEL 2190
Cdd:cd14548     78 RVkcdhYWPFDQDPVYYGDITVTMLSESV-----LPDWTIREFKLE--RGDEVRSVRQFHFTAWPDhgvPEAPDS-LLRF 149

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1609046161 2191 ISVIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYK 2263
Cdd:cd14548    150 VRLVRDYIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222

R-PTPc-typeIIb-2

cd14556

PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...

2063-2262

1.26e-42

Pssm-ID: 350404 [Multi-domain] Cd Length: 201 Bit Score: 155.26 E-value: 1.26e-42

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2063 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDEFVYWPNKdepincESFKVTLMAEEH 2142
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQSCPQYWPDE------GSGTYGPIQVEF 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2143 KCLSNEEKLIIQDFILEAT---QDDYVLeVRHFQCPKWP-NPDSPISKT--FELIS-VIKEEAANRDGPMIVHDEHGGVT 2215
Cdd:cd14556     75 VSTTIDEDVISRIFRLQNTtrpQEGYRM-VQQFQFLGWPrDRDTPPSKRalLKLLSeVEKWQEQSGEGPIVVHCLNGVGR 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1609046161 2216 AGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLY 2262
Cdd:cd14556    154 SGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200

R-PTPc-A-2

cd14623

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...

2039-2265

7.58e-42

Pssm-ID: 350471 [Multi-domain] Cd Length: 228 Bit Score: 154.43 E-value: 7.58e-42

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2039 RTSSIIPVERSRVGISSLSGE-GTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDE 2117
Cdd:cd14623      1 RVLQIIPYEFNRVIIPVKRGEeNTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2118 FV-YWPNkDEPINCESFKVTLMAEEhKClsneEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELISVI-- 2194
Cdd:cd14623     81 CAqYWPS-DGSVSYGDITIELKKEE-EC----ESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIP-SDGKGMINIIaa 153

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1609046161 2195 --KEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVI 2265
Cdd:cd14623    154 vqKQQQQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVV 226

R-PTP-C-2

cd14558

PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...

2063-2262

5.02e-41

Pssm-ID: 350406 [Multi-domain] Cd Length: 203 Bit Score: 151.01 E-value: 5.02e-41

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2063 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPD-GQNMAEDEFVYWPNKDEpiNCESFKVTLMAEE 2141
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTElKEGDQEQCAQYWGDEKK--TYGDIEVELKDTE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2142 hkclsNEEKLIIQDFILEATQDDYVLEVRHFQCPKWpNPDSPISKTFELISVIKE---------EAANRDGPMIVHDEHG 2212
Cdd:cd14558     79 -----KSPTYTVRVFEITHLKRKDSRTVYQYQYHKW-KGEELPEKPKDLVDMIKSikqklpyknSKHGRSVPIVVHCSDG 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2213 GVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLY 2262
Cdd:cd14558    153 SSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202

R-PTPc-A-E-2

cd14552

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...

2063-2265

1.09e-40

Pssm-ID: 350400 [Multi-domain] Cd Length: 202 Bit Score: 150.11 E-value: 1.09e-40

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2063 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDE-FVYWPNkDEPINCESFKVTLMAEE 2141
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKcAQYWPE-DGSVSSGDITVELKDQT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2142 hkclsNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPI--SKTFELI-SVIKEEAANRDGPMIVHDEHGGVTAGT 2218
Cdd:cd14552     80 -----DYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDngKGMIDLIaAVQKQQQQSGNHPITVHCSAGAGRTGT 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1609046161 2219 FCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVI 2265
Cdd:cd14552    155 FCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201

PTPc-N21

cd14598

catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...

1768-1977

4.16e-40

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: 148.97 E-value: 4.16e-40

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1768 YINANYVDGYNRPKA--YIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEE----YGNFLVT 1841
Cdd:cd14598      1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSRHntvtYGRFKIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1842 QKSVQVLAYYTVRNFTLRNtkIKKGSQkgrpsgRVVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHAVG-------- 1913
Cdd:cd14598     81 TRFRTDSGCYATTGLKIKH--LLTGQE------RTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNStidpkspn 152

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1609046161 1914 -PVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1977
Cdd:cd14598    153 pPVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQ 217

COG5599

Protein tyrosine phosphatase [Signal transduction mechanisms];

1711-1971

5.41e-40

Protein tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 444335 [Multi-domain] Cd Length: 282 Bit Score: 150.63 E-value: 5.41e-40

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1711 KEFYQEVQSCTVDLGITADSSNHPDN---KHKNRYINIVAYDHSRVklaqlaEKDGKltdYINANYVDGYNrPKAYIAAQ 1787
Cdd:COG5599     14 EKINSRLSTLTNELAPSHNDPQYLQNingSPLNRFRDIQPYKETAL------RANLG---YLNANYIQVIG-NHRYIATQ 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1788 GPLKSTAEDFWRMIWEHNVEVIVMITNLVE--KGRRKCDQYWPADGseEYGNFLVTQKSVQVlaYYTVRNFTLRNTKIK- 1864
Cdd:COG5599     84 YPLEEQLEDFFQMLFDNNTPVLVVLASDDEisKPKVKMPVYFRQDG--EYGKYEVSSELTES--IQLRDGIEARTYVLTi 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1865 KGS-QKGRPsgrvVTQYHYTQWPDMGVP--EYSLPVLTFVRKAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQ- 1940
Cdd:COG5599    160 KGTgQKKIE----IPVLHVKNWPDHGAIsaEALKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINa 235

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1609046161 1941 -HEGTVNIFGFLKHIRSQRNY-LVQTEEQYVFI 1971
Cdd:COG5599    236 lVQITLSVEEIVIDMRTSRNGgMVQTSEQLDVL 268

alpha_CA_IX

cd03150

Carbonic anhydrase alpha, isozyme IX. Carbonic anhydrases (CAs) are zinc-containing enzymes ...

31-286

2.05e-39

Carbonic anhydrase alpha, isozyme IX. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Alpha CAs are strictly monomeric enzymes. The zinc ion is complexed by three histidine residues. This sub-family comprises the membrane protein CA IX. CA IX is functionally implicated in tumor growth and survival. CA IX is mainly present in solid tumors and its expression in normal tissues is limited to the mucosa of alimentary tract. CA IX is a transmembrane protein with two extracellular domains: carbonic anhydrase and, a proteoglycan-like segment mediating cell-cell adhesion. There is evidence for an involvement of the MAPK pathway in the regulation of CA9 expression.

Pssm-ID: 239403 Cd Length: 247 Bit Score: 147.79 E-value: 2.05e-39

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161   31 NQKNWGKKYPTCNSPKQSPINIDEDLTQVNVNLKKLKFQGWDKTSLENTFIHNTGKTVEINLTNDYRVSGGVSEmVFKAS 110
Cdd:cd03150      1 GQPPWPSVSPACAGRFQSPVDIRPHLVAFCPALRPLELLGFDLPPSPSLRLLNNGHTVQLSLPSGLRMALGPGQ-EYRAL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  111 KITFHWGKCNMSsdGSEHSLEGQKFPLEMQIYCFDAdRFSSFEEAVKGKGKLRALSILFEVGTEENLDFKAIIDGVESVS 190
Cdd:cd03150     80 QLHLHWGAAGRP--GSEHTVDGHRFPAEIHVVHLST-AFANLDEALGRPGGLAVLAAFLAEGLHENSAYEQLLSRLSEIS 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  191 RFGKQAALDPFILLNLLPNSTDKYYIYNGSLTSPPCTDTVDWIVFKDTVSISESQLAVFCEVLTMQQSgyvmlmDYLQNN 270
Cdd:cd03150    157 EEESETVVPGLDVSALLPSDLSRYFRYEGSLTTPPCAQGVIWTVFNQTVRLSAKQLHTLSDSLWGPHD------SRLQLN 230

                          250
                   ....*....|....*.
gi 1609046161  271 FREQQYKFSRQVFSSY 286
Cdd:cd03150    231 FRATQPLNGRKIEASF 246

PTPc_DSPc

smart00012

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...

1877-1977

4.52e-39

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: 141.34 E-value: 4.52e-39

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  1877 VTQYHYTQWPDMGVPEYSLPVLTFVR--KAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHE-GTVNIFGFLKH 1953
Cdd:smart00012    2 VKHYHYTGWPDHGVPESPDSILELLRavKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVKE 81

                            90       100
                    ....*....|....*....|....
gi 1609046161  1954 IRSQRNYLVQTEEQYVFIHDTLVE 1977
Cdd:smart00012   82 LRSQRPGMVQTEEQYLFLYRALLE 105

PTPc_motif

smart00404

Protein tyrosine phosphatase, catalytic domain motif;

1877-1977

4.52e-39

Protein tyrosine phosphatase, catalytic domain motif;

Pssm-ID: 214649 [Multi-domain] Cd Length: 105 Bit Score: 141.34 E-value: 4.52e-39

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  1877 VTQYHYTQWPDMGVPEYSLPVLTFVR--KAAYAKRHAVGPVVVHCSAGVGRTGTYIVLDSMLQQIQHE-GTVNIFGFLKH 1953
Cdd:smart00404    2 VKHYHYTGWPDHGVPESPDSILELLRavKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVKE 81

                            90       100
                    ....*....|....*....|....
gi 1609046161  1954 IRSQRNYLVQTEEQYVFIHDTLVE 1977
Cdd:smart00404   82 LRSQRPGMVQTEEQYLFLYRALLE 105

R-PTPc-V

cd14618

catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...

2038-2266

6.65e-39

Pssm-ID: 350466 [Multi-domain] Cd Length: 230 Bit Score: 145.86 E-value: 6.65e-39

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2038 NRTSSIIPVERSRVGISSLSGE-GTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIP----DGQN 2112
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQLGGEpHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTvgmeNGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2113 MAEDefvYWPNKDEPINCESFKVTLMAEEhkclsNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPN---PDSPISkTFE 2189
Cdd:cd14618     81 LCDH---YWPSESTPVSYGHITVHLLAQS-----SEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDhgiPESTSS-LMA 151

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1609046161 2190 LISVIKEE--AANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVIL 2266
Cdd:cd14618    152 FRELVREHvqATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230

alpha_CA_VI

cd03125

Carbonic anhydrase alpha, isozyme VI. Carbonic anhydrases (CAs) are zinc-containing enzymes ...

31-286

8.20e-39

Carbonic anhydrase alpha, isozyme VI. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidine residues. This sub-family comprises the secreted CA VI, which is found in saliva.

Pssm-ID: 239399 Cd Length: 249 Bit Score: 146.08 E-value: 8.20e-39

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161   31 NQKNWGKKYPTCNSPKQSPINIDEDLTQVNVNLKKLKFQGWDKTSLENTFIHNtGKTVEINLTNDYRVSGGVSEmVFKAS 110
Cdd:cd03125      1 DESHWPEKYPACGGKRQSPIDIQRREVRFNPSLLQLELVGYEKEQGEFTMTNN-GHTVQIDLPPTMSITTGDGT-VYTAV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  111 KITFHWGKCNMSSDGSEHSLEGQKFPLEMQIYCFDADrFSSFEEAVKGKGKLRALSILFEVGTE-ENLDFKAIIDGVESV 189
Cdd:cd03125     79 QMHFHWGGRDSEISGSEHTIDGMRYVAELHIVHYNSK-YKSYEEAKDKPDGLAVLAFLYKVGHYaENTYYSDFISKLAKI 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  190 SRFGKQAALDPFILLNLLPNSTDKYYIYNGSLTSPPCTDTVDWIVFKDTVSISESQlavfceVLTMQQSgyvmLMDY--- 266
Cdd:cd03125    158 KYAGQTTTLTSLDVRDMLPENLHHYYTYQGSLTTPPCTENVLWFVFDDPVTLSKTQ------IVKLENT----LMDHhnk 227

                          250       260
                   ....*....|....*....|.
gi 1609046161  267 -LQNNFREQQYKFSRQVFSSY 286
Cdd:cd03125    228 tIRNDYRRTQPLNHRVVEANF 248

R-PTPc-J

cd14615

catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...

2038-2266

2.54e-37

Pssm-ID: 350463 [Multi-domain] Cd Length: 229 Bit Score: 141.11 E-value: 2.54e-37

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2038 NRTSSIIPVERSRVGISSLSGEGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVM----IPDGQNM 2113
Cdd:cd14615      1 NRYNNVLPYDISRVKLSVQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMltkcVEQGRTK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2114 AEDefvYWPNKdEPINCESFKVTLMAEehkclSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWpnPDSPISKTFELI-- 2191
Cdd:cd14615     81 CEE---YWPSK-QKKDYGDITVTMTSE-----IVLPEWTIRDFTVKNAQTNESRTVRHFHFTSW--PDHGVPETTDLLin 149

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1609046161 2192 --SVIKE--EAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVIL 2266
Cdd:cd14615    150 frHLVREymKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCAL 228

R-PTPc-LAR-1

cd14553

catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...

2032-2270

1.40e-36

Pssm-ID: 350401 [Multi-domain] Cd Length: 238 Bit Score: 139.45 E-value: 1.40e-36

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2032 QCNREKNRTSSIIPVERSRVGISSLSG-EGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdg 2110
Cdd:cd14553      1 EVNKPKNRYANVIAYDHSRVILQPIEGvPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMM--- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2111 QNMAEDEFV----YWPNKDEPiNCESFKVTLMAEEHkcLSNeekLIIQDFILEATQDDYVLEVRHFQCPKWPN---PDSP 2183
Cdd:cd14553     78 TKLEERSRVkcdqYWPTRGTE-TYGLIQVTLLDTVE--LAT---YTVRTFALHKNGSSEKREVRQFQFTAWPDhgvPEHP 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2184 ISkTFELISVIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYK 2263
Cdd:cd14553    152 TP-FLAFLRRVKACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHD 230


                   ....*..
gi 1609046161 2264 VILSLVS 2270
Cdd:cd14553    231 ALLEAVT 237

R-PTPc-E-2

cd14622

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...

2062-2265

2.15e-36

Pssm-ID: 350470 [Multi-domain] Cd Length: 205 Bit Score: 137.83 E-value: 2.15e-36

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2062 DYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDE-FVYWPNKDEPINCEsfkVTLmae 2140
Cdd:cd14622      1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKcVQYWPSEGSVTHGE---ITI--- 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2141 EHKCLSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPIS--KTFELISVI-KEEAANRDGPMIVHDEHGGVTAG 2217
Cdd:cd14622     75 EIKNDTLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEgkGMIDLIAAVqKQQQQTGNHPIVVHCSAGAGRTG 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1609046161 2218 TFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVI 2265
Cdd:cd14622    155 TFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202

PTPc-N9

cd14543

catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...

2026-2263

8.14e-36

Pssm-ID: 350391 [Multi-domain] Cd Length: 271 Bit Score: 138.27 E-value: 8.14e-36

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2026 YSAALKQCNREKNRTSSIIPVERSRVGISSLSG-EGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLV 2104
Cdd:cd14543     21 FLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGdERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVI 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2105 VMIPD---------GQnmaedefvYWPNKDEpiNCESF-KVTLmaeEHKCLSNEEKLIIQDFILEATQDDYVLEVRHFQC 2174
Cdd:cd14543    101 VMTTRvvergrvkcGQ--------YWPLEEG--SSLRYgDLTV---TNLSVENKEHYKKTTLEIHNTETDESRQVTHFQF 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2175 PKWPN---PDSPISKTFELISVIKEEAAN------------RDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQ 2239
Cdd:cd14543    168 TSWPDfgvPSSAAALLDFLGEVRQQQALAvkamgdrwkghpPGPPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQ 247

                          250       260
                   ....*....|....*....|....
gi 1609046161 2240 VAKMINLMRPGVFADIEQYQFLYK 2263
Cdd:cd14543    248 TVRRMRTQRAFSIQTPDQYYFCYK 271

alpha_CA_I_II_III_XIII

cd03119

Carbonic anhydrase alpha, isozymes I, II, and III and XIII. Carbonic anhydrases (CAs) are ...

24-286

8.39e-36

Carbonic anhydrase alpha, isozymes I, II, and III and XIII. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidines. This vertebrate subgroup comprises isozymes I, II, and III, which are cytoplasmic enzymes. CA I, for example, is expressed in erythrocyes of many vertebrates; CA II is the most active cytosolic isozyme; while it is being expressed nearly ubiquitously, it comprises 95% of the renal carbonic anhydrase and is required for renal acidification; CA III has been implicated in protection from the damaging effect of oxidizing agents in hepatocytes. CAXIII may play important physiological roles in several organs.

Pssm-ID: 239393 [Multi-domain] Cd Length: 259 Bit Score: 137.96 E-value: 8.39e-36

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161   24 WSYTGALNQKNWGKKYPTCNSPKQSPINIDEDLTQVNVNLKKLKFQgWDKTSLENtfIHNTGKTVEINLTNDYRVS---G 100
Cdd:cd03119      5 WGYDSHNGPEHWHELFPIAKGDRQSPIDIKTKDAKHDPSLKPLSVS-YDPATAKT--ILNNGHSFNVEFDDTDDRSvlrG 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  101 GVSEMVFKASKITFHWGKCNmsSDGSEHSLEGQKFPLEMQIYCFDAdRFSSFEEAVKGKGKLRALSILFEVGtEENLDFK 180
Cdd:cd03119     82 GPLTGSYRLRQFHFHWGSSD--DHGSEHTVDGVKYAAELHLVHWNS-KYGSFGEAAKQPDGLAVVGVFLKVG-EANPELQ 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  181 AIIDGVESVSRFGKQAALDPFILLNLLPNSTDkYYIYNGSLTSPPCTDTVDWIVFKDTVSISESQLAVFCEVLTMQQSGY 260
Cdd:cd03119    158 KVLDALDSIKTKGKQAPFTNFDPSCLLPASLD-YWTYPGSLTTPPLLECVTWIVLKEPISVSSEQMAKFRSLLFNAEGEP 236

                          250       260
                   ....*....|....*....|....*.
gi 1609046161  261 VMLMdylQNNFREQQYKFSRQVFSSY 286
Cdd:cd03119    237 PCPM---VDNWRPPQPLKGRKVRASF 259

R-PTPc-O

cd14614

catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...

2034-2266

1.13e-35

Pssm-ID: 350462 [Multi-domain] Cd Length: 245 Bit Score: 136.94 E-value: 1.13e-35

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2034 NREKNRTSSIIPVERSRVGISSLSG-EGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIP---D 2109
Cdd:cd14614     12 NRCKNRYTNILPYDFSRVKLVSMHEeEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTqcnE 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2110 GQNMAEDEfvYWPNKDEPINCESFKVTLMAEEhkclsNEEKLIIQDFilEATQDDYVLEVRHFQCPKWPNPDSPISKTFE 2189
Cdd:cd14614     92 KRRVKCDH--YWPFTEEPVAYGDITVEMLSEE-----EQPDWAIREF--RVSYADEVQDVMHFNYTAWPDHGVPTANAAE 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2190 ----LISVIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVI 2265
Cdd:cd14614    163 silqFVQMVRQQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCV 242


                   .
gi 1609046161 2266 L 2266
Cdd:cd14614    243 Q 243

R-PTPc-H

cd14619

catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...

2038-2269

1.96e-35

Pssm-ID: 350467 [Multi-domain] Cd Length: 233 Bit Score: 135.79 E-value: 1.96e-35

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2038 NRTSSIIPVERSRVGISSLSGEGT-DYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdgQNMAED 2116
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKPIHEEPGsDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVML---TNCMEA 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2117 EFV----YWPNKDEPINCESFKVTLMAEEhkclsNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELIS 2192
Cdd:cd14619     78 GRVkcehYWPLDYTPCTYGHLRVTVVSEE-----VMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVP-SSTDTLLA 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2193 ---VIKE--EAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVILS 2267
Cdd:cd14619    152 frrLLRQwlDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILD 231


                   ..
gi 1609046161 2268 LV 2269
Cdd:cd14619    232 FL 233

R-PTPc-M-1

cd14633

catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...

2022-2266

6.06e-35

Pssm-ID: 350481 [Multi-domain] Cd Length: 273 Bit Score: 135.94 E-value: 6.06e-35

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2022 QQSDYSAALKQCNREKNRTSSIIPVERSRVGISSLSGE-GTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHN 2100
Cdd:cd14633     28 QSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGEtSSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHEN 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2101 AQLVVMIpdgQNMAEDEFV----YWPNKDEPIncESFKVTLMaeEHKCLSneeKLIIQDFILEATQDDYVLEVRHFQCPK 2176
Cdd:cd14633    108 TASIIMV---TNLVEVGRVkcckYWPDDTEIY--KDIKVTLI--ETELLA---EYVIRTFAVEKRGVHEIREIRQFHFTG 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2177 WPNPDSPISKT--FELISVIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFAD 2254
Cdd:cd14633    178 WPDHGVPYHATglLGFVRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQT 257

                          250
                   ....*....|..
gi 1609046161 2255 IEQYQFLYKVIL 2266
Cdd:cd14633    258 EEQYVFIHDAIL 269

PTPc-KIM

cd14547

catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...

2038-2262

1.29e-34

Pssm-ID: 350395 [Multi-domain] Cd Length: 224 Bit Score: 133.29 E-value: 1.29e-34

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2038 NRTSSIIPVERSRVGISSL-SGEGTDYINASYIMGY-YQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAE 2115
Cdd:cd14547      1 NRYKTILPNEHSRVCLPSVdDDPLSSYINANYIRGYdGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2116 DEFVYWPNKdEPINCESFKVTLMAEEHKclsneEKLIIQDFILEatqddYVLEVR---HFQCPKWPNPDSPiSKTFELIS 2192
Cdd:cd14547     81 KCAQYWPEE-ENETYGDFEVTVQSVKET-----DGYTVRKLTLK-----YGGEKRylkHYWYTSWPDHKTP-EAAQPLLS 148

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1609046161 2193 VIKE-----EAANRDGPMIVHDEHG-GVTaGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLY 2262
Cdd:cd14547    149 LVQEveearQTEPHRGPIVVHCSAGiGRT-GCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223

R5-PTP-2

cd14550

PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...

1768-1971

1.54e-34

Pssm-ID: 350398 [Multi-domain] Cd Length: 200 Bit Score: 132.06 E-value: 1.54e-34

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1768 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGrrKCDQYWPADGSE-EYGNFLVTQ---- 1842
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTKEKPlECETFKVTLsged 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1843 -KSVQVLAYYTVRNFTLRNTKikkgsqkgrpSGRVVT--QYHYTQWPDMGVPEYSlpVLTFVRKAAYAKRHAVGPVVVHC 1919
Cdd:cd14550     79 hSCLSNEIRLIVRDFILESTQ----------DDYVLEvrQFQCPSWPNPCSPIHT--VFELINTVQEWAQQRDGPIVVHD 146

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1609046161 1920 SAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFI 1971
Cdd:cd14550    147 RYGGVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFL 198

PTPc-N18

cd14603

catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...

2011-2265

3.23e-34

Pssm-ID: 350451 [Multi-domain] Cd Length: 266 Bit Score: 133.41 E-value: 3.23e-34

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2011 KQFQLL-SQSNIQQSDYS----AALKQCNREKNRTSSIIPVERSRVGISSLSGEG-TDYINASYIMGYYQSNEFIITQHP 2084
Cdd:cd14603      2 GEFSEIrACSAAFKADYVcstvAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGhSDYINANFIKGVDGSRAYIATQGP 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2085 LLHTIKDFWRMIWDHNAQLVVM----IPDGQNMAEdefVYWPNKDEPINCESFKVTLMAEEHkclSNEEkLIIQdfILEA 2160
Cdd:cd14603     82 LSHTVLDFWRMIWQYGVKVILMacreIEMGKKKCE---RYWAQEQEPLQTGPFTITLVKEKR---LNEE-VILR--TLKV 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2161 TQDDYVLEVRHFQCPKWPN---PDSPiSKTFELISVIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDV 2237
Cdd:cd14603    153 TFQKESRSVSHFQYMAWPDhgiPDSP-DCMLAMIELARRLQGSGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPPD 231

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1609046161 2238 YQVAKMINLM---RPGVFADIEQYQFLYKVI 2265
Cdd:cd14603    232 FSIFDVVLEMrkqRPAAVQTEEQYEFLYHTV 262

alpha_CA_V

cd03118

Carbonic anhydrase alpha, CA isozyme V_like subgroup. Carbonic anhydrases (CAs) are ...

46-286

4.58e-34

Carbonic anhydrase alpha, CA isozyme V_like subgroup. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidines. This vertebrate subgroup comprises isozyme V. CA V is the mitochondrial isozyme, which may play a role in gluconeogenesis and ureagenesis and possibly also in lipogenesis.

Pssm-ID: 239392 Cd Length: 236 Bit Score: 132.27 E-value: 4.58e-34

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161   46 KQSPINIDEDLTQVNVNLKKLKFQGWDKTSLentFIHNTGKTVEINL---TNDYRVSGGVSEMVFKASKITFHWGKCNms 122
Cdd:cd03118      3 RQSPINIQWRDSVYDPQLAPLRVSYDPATCL---YIWNNGYSFQVEFddsTDKSGISGGPLENHYRLKQFHFHWGANN-- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  123 SDGSEHSLEGQKFPLEMQIYCFDADRFSSFEEAVKGKGKLRALSILFEVGTEENlDFKAIIDGVESVSRFGKQAALDPFI 202
Cdd:cd03118     78 EWGSEHTVDGHTYPAELHLVHWNSVKYENFEEAVMEENGLAVIGVFLKLGAHHE-GLQKLVDALPEVRHKDTVVEFNPFD 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  203 LLNLLPNSTDkYYIYNGSLTSPPCTDTVDWIVFKDTVSISESQLAVFCEVLTmqqSGYVMLMDYLQNNFREQQYKFSRQV 282
Cdd:cd03118    157 PSCLLPACRD-YWTYPGSLTTPPLTESVTWIIQKQPIEVSPSQLSVFRTLLF---TSRGEEEKVMVNNFRPLQPLMNRKV 232


                   ....
gi 1609046161  283 FSSY 286
Cdd:cd03118    233 RSSF 236

R-PTPc-T-1

cd14630

catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...

2034-2266

1.26e-32

Pssm-ID: 350478 [Multi-domain] Cd Length: 237 Bit Score: 127.83 E-value: 1.26e-32

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2034 NREKNRTSSIIPVERSRVGISSLSGE-GTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQN 2112
Cdd:cd14630      3 NRNKNRYGNIISYDHSRVRLQLLDGDpHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2113 MAEDEFV-YWPNKDEPINceSFKVTLMAEEHKClsneeKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FE 2189
Cdd:cd14630     83 VGRVKCVrYWPDDTEVYG--DIKVTLIETEPLA-----EYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATglLG 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1609046161 2190 LISVIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVIL 2266
Cdd:cd14630    156 FVRQVKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAIL 232

PTPc-N7

cd14612

catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...

2037-2262

2.12e-32

Pssm-ID: 350460 [Multi-domain] Cd Length: 247 Bit Score: 127.64 E-value: 2.12e-32

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2037 KNRTSSIIPVERSRVGISSL--SGEGTDYINASYIMGYY-QSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNM 2113
Cdd:cd14612     18 KDRYKTILPNPQSRVCLRRAgsQEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKEK 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2114 AEDEFVYWPNKDEPINCESFKVTLMAEehkClsneEKLIIQDFILEATQDDYvlEVRHFQCPKWPNPDSPISKT--FELI 2191
Cdd:cd14612     98 KEKCVHYWPEKEGTYGRFEIRVQDMKE---C----DGYTIRDLTIQLEEESR--SVKHYWFSSWPDHQTPESAGplLRLV 168

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1609046161 2192 SVIKE--EAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLY 2262
Cdd:cd14612    169 AEVEEsrQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLH 241

PTPc-N22

cd14602

catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...

2037-2268

2.23e-32

Pssm-ID: 350450 [Multi-domain] Cd Length: 234 Bit Score: 127.26 E-value: 2.23e-32

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2037 KNRTSSIIPVERSRVGISSL-SGEGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAE 2115
Cdd:cd14602      1 KNRYKDILPYDHSRVELSLItSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2116 DEFV-YWPN-KDEPINCESFKVTLMAEEHKclsneEKLIIQdfILEATQDDYVLEVRHFQCPKWPNPDSP--ISKTFELI 2191
Cdd:cd14602     81 KKCErYWAEpGEMQLEFGPFSVTCEAEKRK-----SDYIIR--TLKVKFNSETRTIYQFHYKNWPDHDVPssIDPILELI 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2192 SVIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEK----ENsVDVYQVAKMINLMRPGVFADIEQYQFLYKVILS 2267
Cdd:cd14602    154 WDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDgiipEN-FSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIE 232


                   .
gi 1609046161 2268 L 2268
Cdd:cd14602    233 L 233

PTPc-N5

cd14613

catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...

2037-2268

5.99e-32

Pssm-ID: 350461 [Multi-domain] Cd Length: 258 Bit Score: 126.90 E-value: 5.99e-32

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2037 KNRTSSIIPVERSRVGISSLSGEG--TDYINASYIMGY-YQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNM 2113
Cdd:cd14613     28 KNRYKTILPNPHSRVCLTSPDQDDplSSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2114 AEDEFVYWPnkDEPINCESFKVTLMAEEHkclsnEEKLIIQDFILEATQDDYVLevRHFQCPKWPN---PDS--PISKTF 2188
Cdd:cd14613    108 NEKCTEYWP--EEQVTYEGIEITVKQVIH-----ADDYRLRLITLKSGGEERGL--KHYWYTSWPDqktPDNapPLLQLV 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2189 ELISVIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKViLSL 2268
Cdd:cd14613    179 QEVEEARQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHV-LSL 257

Cah

COG3338

Carbonic anhydrase [Inorganic ion transport and metabolism];

24-249

8.99e-32

Carbonic anhydrase [Inorganic ion transport and metabolism];

Pssm-ID: 442567 [Multi-domain] Cd Length: 247 Bit Score: 125.77 E-value: 8.99e-32

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161   24 WSYTGALNQKNWGK---KYPTCNS-PKQSPINIDedlTQVNVNLKKLKFQgWDKTSLEntfIHNTGKTVEINL-TNDYRV 98
Cdd:COG3338     28 WSYEGETGPEHWGElspEFATCATgKNQSPIDIR---TAIKADLPPLKFD-YKPTPLE---IVNNGHTIQVNVdPGSTLT 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161   99 SGGVsemVFKASKITFHwgkcnmssDGSEHSLEGQKFPLEMQiycF---DADrfssfeeavkgkGKLRALSILFEVGtEE 175
Cdd:COG3338    101 VDGK---RYELKQFHFH--------TPSEHTINGKSYPMEAH---LvhkDAD------------GELAVVGVLFEEG-AE 153

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1609046161  176 NLDFKAIIDGVESvsRFGKQAALD-PFILLNLLPNSTDkYYIYNGSLTSPPCTDTVDWIVFKDTVSISESQLAVF 249
Cdd:COG3338    154 NPALAKLWANLPL--EAGEEVALDaTIDLNDLLPEDRS-YYRYSGSLTTPPCSEGVLWIVLKQPITVSAEQIEAF 225

alpha_CA_prokaryotic_like

cd03124

Carbonic anhydrase alpha, prokaryotic-like subfamily. Carbonic anhydrases (CAs) are ...

31-249

1.84e-31

Carbonic anhydrase alpha, prokaryotic-like subfamily. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidines. This sub-family includes bacterial carbonic anhydrase alpha, as well as plant enzymes such as tobacco nectarin III and yam dioscorin and, carbonic anhydrases from molluscs, such as nacrein, which are part of the organic matrix layer in shells. Other members of this family may be involved in maintaining pH balance, in facilitating transport of carbon dioxide or carbonic acid, or in sensing carbon dioxide levels in the environment. Dioscorin is the major storage protein of yam tubers and may play a role as an antioxidant. Tobacco Nectarin may play a role in the maintenace of pH and oxidative balance in nectar. Mollusc nacrein may participate in calcium carbonate crystal formation of the nacreous layer. This subfamily also includes three alpha carbonic anhydrases from Chlamydomonas reinhardtii (CAH 1-3). CAHs1-2 are localized in the periplasmic space. CAH1 faciliates the movement of carbon dioxide across the plasma membrane when the medium is alkaline. CAH3 is localized to the thylakoid lumen and provides CO2 to Rubisco.

Pssm-ID: 239398 [Multi-domain] Cd Length: 216 Bit Score: 123.92 E-value: 1.84e-31

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161   31 NQKNWG---KKYPTCNS-PKQSPINIDEDLTQVNVnLKKLKFQgWDKTSLEntfIHNTGKTVEINLTNDyrvsGGVSE-- 104
Cdd:cd03124      1 GPEHWGnldPEFALCATgKNQSPIDITTKAVVSDK-LPPLNYN-YKPTSAT---LVNNGHTIQVNFEGN----GGTLTid 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  105 -MVFKASKITFHwgkcnmssDGSEHSLEGQKFPLEMQIycfdadrfsSFEEAvkgKGKLRALSILFEVGtEENLDFKAII 183
Cdd:cd03124     72 gETYQLLQFHFH--------SPSEHLINGKRYPLEAHL---------VHKSK---DGQLAVVAVLFEEG-KENPFLKKIL 130

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1609046161  184 DGVESvsRFGKQAALDPFILLN-LLPNSTDkYYIYNGSLTSPPCTDTVDWIVFKDTVSISESQLAVF 249
Cdd:cd03124    131 DNMPK--KEGTEVNLPAILDPNeLLPESRS-YYRYEGSLTTPPCSEGVRWIVLKQPITISKEQLAKF 194

R-PTPc-F-1

cd14626

catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...

2022-2270

2.49e-30

Pssm-ID: 350474 [Multi-domain] Cd Length: 276 Bit Score: 122.45 E-value: 2.49e-30

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2022 QQSDYSAALKQCNREKNRTSSIIPVERSRVGISSLSG-EGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHN 2100
Cdd:cd14626     29 QQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGvPGSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQR 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2101 AQLVVMIpdgQNMAEDEFV----YWPNKDEPiNCESFKVTLM-AEEHKCLSneekliIQDFILEATQDDYVLEVRHFQCP 2175
Cdd:cd14626    109 TATIVMM---TRLEEKSRVkcdqYWPIRGTE-TYGMIQVTLLdTVELATYS------VRTFALYKNGSSEKREVRQFQFM 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2176 KWPNPDSPISKTFELISVIKEEAAN--RDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFA 2253
Cdd:cd14626    179 AWPDHGVPEYPTPILAFLRRVKACNppDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQ 258

                          250
                   ....*....|....*..
gi 1609046161 2254 DIEQYQFLYKVILSLVS 2270
Cdd:cd14626    259 TEDQYIFIHEALLEAAT 275

R-PTPc-U-2

cd14637

PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...

2063-2266

2.87e-30

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: 120.01 E-value: 2.87e-30

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2063 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIP--DGQNMAEDEFVYWPnkdEPINCesfKVTLMAE 2140
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNqlNQSNSAWPCLQYWP---EPGLQ---QYGPMEV 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2141 EHKCLSNEEKLIIQDFILE--ATQDDYVLEVRHFQCPKWP----NPDSPISKTFELISVIKEEAANRDGPMIVHDEHGGV 2214
Cdd:cd14637     75 EFVSGSADEDIVTRLFRVQniTRLQEGHLMVRHFQFLRWSayrdTPDSKKAFLHLLASVEKWQRESGEGRTVVHCLNGGG 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1609046161 2215 TAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVIL 2266
Cdd:cd14637    155 RSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIAL 206

PTP_fungal

cd18533

fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...

2063-2262

3.75e-30

Pssm-ID: 350509 [Multi-domain] Cd Length: 212 Bit Score: 120.05 E-value: 3.75e-30

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2063 YINASYI-MGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMI-PDGQNMAEDEFVYWPNKDEPINCESFKVTLMAE 2140
Cdd:cd18533      1 YINASYItLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLtPLVENGREKCDQYWPSGEYEGEYGDLTVELVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2141 EHKclsNEEKLIIQDFILeATQDDYVLEVRHFQCPKWPN---PDSPISkTFELISVIKE--EAANRDGPMIVHDEHG-GV 2214
Cdd:cd18533     81 EEN---DDGGFIVREFEL-SKEDGKVKKVYHIQYKSWPDfgvPDSPED-LLTLIKLKRElnDSASLDPPIIVHCSAGvGR 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1609046161 2215 TaGTFCALTTLMHQLEK--------ENSVDVyqVAKMINLM---RPGVFADIEQYQFLY 2262
Cdd:cd18533    156 T-GTFIALDSLLDELKRglsdsqdlEDSEDP--VYEIVNQLrkqRMSMVQTLRQYIFLY 211

R-PTPc-B

cd14617

catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...

2038-2263

5.46e-30

Pssm-ID: 350465 [Multi-domain] Cd Length: 228 Bit Score: 120.02 E-value: 5.46e-30

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2038 NRTSSIIPVERSRVGISSLSGEG-TDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdgQNMAED 2116
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNVDDDPcSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMV---TQCVEK 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2117 EFV----YWPNKDEPINCESFKVTLMAEehkclSNEEKLIIQDF-ILEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELI 2191
Cdd:cd14617     78 GRVkcdhYWPADQDSLYYGDLIVQMLSE-----SVLPEWTIREFkICSEEQLDAPRLVRHFHYTVWPDHGVP-ETTQSLI 151

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1609046161 2192 SVIK--EEAANRD---GPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYK 2263
Cdd:cd14617    152 QFVRtvRDYINRTpgsGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228

alpha_CA_VII

cd03149

Carbonic anhydrase alpha, CA isozyme VII_like subgroup. Carbonic anhydrases (CAs) are ...

46-286

8.26e-30

Carbonic anhydrase alpha, CA isozyme VII_like subgroup. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. Most alpha CAs are monomeric enzymes. The zinc ion is complexed by three histidines. This vertebrate subgroup comprises isozyme VII. CA VII is the most active cytosolic enzyme after CA II, and may be highly expressed in the brain. Human CA VII may be a target of antiepileptic sulfonamides/sulfamates.

Pssm-ID: 239402 Cd Length: 236 Bit Score: 119.94 E-value: 8.26e-30

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161   46 KQSPINIDEDLTQVNVNLKKLKFQGWDKTSLEntfIHNTGKT--VEINLTNDYRV-SGGVSEMVFKASKITFHWGKcnMS 122
Cdd:cd03149      3 RQSPIDIVSSEAVYDPKLKPLSLSYDPCTSLS---ISNNGHSvmVEFDDSDDKTViTGGPLENPYRLKQFHFHWGA--KH 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  123 SDGSEHSLEGQKFPLEMQIYCFDADRFSSFEEAVKGKGKLRALSILFEVGtEENLDFKAIIDGVESVSRFGKQAALDPFI 202
Cdd:cd03149     78 GSGSEHTVDGKTFPSELHLVHWNAKKYKSFGEAAAAPDGLAVLGVFLETG-DEHPGLNRLTDALYMVRFKGTKAQFLDFN 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  203 LLNLLPNSTDkYYIYNGSLTSPPCTDTVDWIVFKDTVSISESQLAVFCEVLTMQQSGYVMLMdylQNNFREQQYKFSRQV 282
Cdd:cd03149    157 PKCLLPKSLD-YWTYPGSLTTPPLNESVTWIVLKEPIPVSEKQMGKFRELLFTSEEDQRNHM---VNNFRPPQPLKGRTV 232


                   ....
gi 1609046161  283 FSSY 286
Cdd:cd03149    233 RASF 236

R-PTPc-T-2

cd14634

PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...

1768-1977

8.43e-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: 8.43e-30

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1768 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLveKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 1847
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM--DAAQLCMQYWPEKTSCCYGPIQVEFVSADI 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1848 LAYYTVRNFTLRNTkikkgsqkGRPSG--RVVTQYHYTQWPDM-GVPEYSLPVLTFVRKAA-----YAKRHavGPVVVHC 1919
Cdd:cd14634     79 DEDIISRIFRICNM--------ARPQDgyRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEkwqeqYDGRE--GRTVVHC 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1609046161 1920 SAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1977
Cdd:cd14634    149 LNGGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206

PTPc-N12

cd14604

catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...

2031-2268

1.17e-29

Pssm-ID: 350452 [Multi-domain] Cd Length: 297 Bit Score: 121.19 E-value: 1.17e-29

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2031 KQCNREKNRTSSIIPVERSRVGIS-SLSGEGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPD 2109
Cdd:cd14604     54 KEENVKKNRYKDILPFDHSRVKLTlKTSSQDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACR 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2110 GQNMAEDEFV-YWPN-KDEPINCESFKVTLMAEEHKclsneEKLIIQDFILEATQDDYVLEVRHFQcpKWPNPDSPIS-- 2185
Cdd:cd14604    134 EFEMGRKKCErYWPLyGEEPMTFGPFRISCEAEQAR-----TDYFIRTLLLEFQNETRRLYQFHYV--NWPDHDVPSSfd 206

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2186 KTFELISVIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADI---EQYQFLY 2262
Cdd:cd14604    207 SILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVqtkEQYELVH 286


                   ....*.
gi 1609046161 2263 KVILSL 2268
Cdd:cd14604    287 RAIAQL 292

R-PTPc-Q

cd14616

catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...

2038-2263

1.45e-29

Pssm-ID: 350464 [Multi-domain] Cd Length: 224 Bit Score: 118.86 E-value: 1.45e-29

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2038 NRTSSIIPVERSRVGISSLSG-EGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPD----GQN 2112
Cdd:cd14616      1 NRFPNIKPYNNNRVKLIADAGvPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQcfekGRI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2113 MAEDefvYWPNKDEPINCES-FKVTLMAEEhkclsNEEKLIIQDFILEaTQDDYVLeVRHFQCPKWPNPDSPISkTFELI 2191
Cdd:cd14616     81 RCHQ---YWPEDNKPVTVFGdIVITKLMED-----VQIDWTIRDLKIE-RHGDYMM-VRQCNFTSWPEHGVPES-SAPLI 149

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1609046161 2192 SVIKEEAANRDG---PMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYK 2263
Cdd:cd14616    150 HFVKLVRASRAHdntPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224

R-PTPc-E-1

cd14620

catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...

2042-2266

1.56e-29

Pssm-ID: 350468 [Multi-domain] Cd Length: 229 Bit Score: 118.89 E-value: 1.56e-29

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2042 SIIPVERSRVGISSLSG-EGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDE-FV 2119
Cdd:cd14620      3 NILPYDHSRVILSQLDGiPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKcYQ 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2120 YWPNKdepiNCESF-KVTLMAEEHKCLSNeekLIIQDFILEATQDDYVLEVR-----HFQcpKWPN---PDSPISkTFEL 2190
Cdd:cd14620     83 YWPDQ----GCWTYgNIRVAVEDCVVLVD---YTIRKFCIQPQLPDGCKAPRlvtqlHFT--SWPDfgvPFTPIG-MLKF 152

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1609046161 2191 ISVIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVIL 2266
Cdd:cd14620    153 LKKVKSVNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALL 228

R-PTPc-A-1

cd14621

catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...

2009-2266

1.70e-29

Pssm-ID: 350469 [Multi-domain] Cd Length: 296 Bit Score: 120.90 E-value: 1.70e-29

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2009 LEKQFQLLSQSNIQQSdYSAALKQCNREKNRTSSIIPVERSRVGISSLSG-EGTDYINASYIMGYYQSNEFIITQHPLLH 2087
Cdd:cd14621     28 FREEFNALPACPIQAT-CEAASKEENKEKNRYVNILPYDHSRVHLTPVEGvPDSDYINASFINGYQEKNKFIAAQGPKEE 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2088 TIKDFWRMIWDHNAQLVVMIPDGQNMAEDEFV-YWPNKdepiNCESF-KVTLMAEEHKCLSNE--EKLIIQDfILEATQD 2163
Cdd:cd14621    107 TVNDFWRMIWEQNTATIVMVTNLKERKECKCAqYWPDQ----GCWTYgNIRVSVEDVTVLVDYtvRKFCIQQ-VGDVTNK 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2164 DYVLEVRHFQCPKWPN---PDSPISkTFELISVIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQV 2240
Cdd:cd14621    182 KPQRLITQFHFTSWPDfgvPFTPIG-MLKFLKKVKNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGF 260

                          250       260
                   ....*....|....*....|....*.
gi 1609046161 2241 AKMINLMRPGVFADIEQYQFLYKVIL 2266
Cdd:cd14621    261 VSRIRAQRCQMVQTDMQYVFIYQALL 286

R-PTPc-T-2

cd14634

PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...

2063-2266

6.01e-29

Pssm-ID: 350482 [Multi-domain] Cd Length: 206 Bit Score: 116.27 E-value: 6.01e-29

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2063 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDgQNMAEDEFVYWPNKDE----PINCESFKVTLm 2138
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNE-MDAAQLCMQYWPEKTSccygPIQVEFVSADI- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2139 aeehkclsnEEKLIIQDFI---LEATQDDYVLeVRHFQCPKWPN-PDSPISKTfELISVIK------EEAANRDGPMIVH 2208
Cdd:cd14634     79 ---------DEDIISRIFRicnMARPQDGYRI-VQHLQYIGWPAyRDTPPSKR-SILKVVRrlekwqEQYDGREGRTVVH 147

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1609046161 2209 DEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVIL 2266
Cdd:cd14634    148 CLNGGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVAL 205

R5-PTPc-1

cd14549

catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...

2063-2262

6.03e-29

Pssm-ID: 350397 [Multi-domain] Cd Length: 204 Bit Score: 116.30 E-value: 6.03e-29

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2063 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdgQNMAE------DEfvYWPNKDEPiNCESFKVT 2136
Cdd:cd14549      1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMI---TNLVErgrrkcDQ--YWPKEGTE-TYGNIQVT 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2137 LMAEEHkcLSNeekLIIQDFILEATQ------DDYVLEVRHFQCPKWPN---PDSPISK-TFelisVIKEEAANRD--GP 2204
Cdd:cd14549     75 LLSTEV--LAT---YTVRTFSLKNLKlkkvkgRSSERVVYQYHYTQWPDhgvPDYTLPVlSF----VRKSSAANPPgaGP 145

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1609046161 2205 MIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLY 2262
Cdd:cd14549    146 IVVHCSAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203

PHA02747

protein tyrosine phosphatase; Provisional

2026-2270

8.39e-29

protein tyrosine phosphatase; Provisional

Pssm-ID: 165114 [Multi-domain] Cd Length: 312 Bit Score: 119.34 E-value: 8.39e-29

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2026 YSAALKQCNREKNRTSSIIPVERSRVGISSLSGEGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVV 2105
Cdd:PHA02747    43 IANFEKPENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIV 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2106 MI--PDGQNMAEDEFVYW-PNKDEPINCESFKVTLMAEEHKCLSNEEKLIIQDFILEATQddyvlEVRHFQCPKWPNPDS 2182
Cdd:PHA02747   123 MLtpTKGTNGEEKCYQYWcLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSR-----KISHFQCSEWFEDET 197

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2183 PiSKTFELISVIKEEAANRD-------------GPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRP 2249
Cdd:PHA02747   198 P-SDHPDFIKFIKIIDINRKksgklfnpkdallCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRH 276

                          250       260
                   ....*....|....*....|....
gi 1609046161 2250 GVFADIEQYQFL---YKVILSLVS 2270
Cdd:PHA02747   277 AGIMNFDDYLFIqpgYEVLHYFLS 300

R-PTPc-typeIIb-1

cd14555

catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...

2063-2266

2.26e-28

Pssm-ID: 350403 [Multi-domain] Cd Length: 204 Bit Score: 114.63 E-value: 2.26e-28

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2063 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdgQNMAEDEFV----YWPNKDEPINceSFKVTLM 2138
Cdd:cd14555      1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMV---TNLVEVGRVkcsrYWPDDTEVYG--DIKVTLV 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2139 AEEHKClsneeKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISVIKEEAANRDGPMIVHDEHGGVTA 2216
Cdd:cd14555     76 ETEPLA-----EYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATglLGFIRRVKASNPPSAGPIVVHCSAGAGRT 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2217 GTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVIL 2266
Cdd:cd14555    151 GCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAIL 200

PHA02746

protein tyrosine phosphatase; Provisional

2027-2265

2.29e-28

protein tyrosine phosphatase; Provisional

Pssm-ID: 165113 [Multi-domain] Cd Length: 323 Bit Score: 118.21 E-value: 2.29e-28

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2027 SAALKQCNREKNRTSSIIPVERSRVGISS------------------LSGEGTD--YINASYIMGYYQSNEFIITQHPLL 2086
Cdd:PHA02746    44 NHFLKKENLKKNRFHDIPCWDHSRVVINAheslkmfdvgdsdgkkieVTSEDNAenYIHANFVDGFKEANKFICAQGPKE 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2087 HTIKDFWRMIWDHNAQLVVMIPDGQNMAEDEFVYWPN-KDEPINCESFKVTLMAEEHKCLSNEEKLIIQDFILEATQddy 2165
Cdd:PHA02746   124 DTSEDFFKLISEHESQVIVSLTDIDDDDEKCFELWTKeEDSELAFGRFVAKILDIIEELSFTKTRLMITDKISDTSR--- 200

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2166 vlEVRHFQCPKWP---NPDSPiSKTFELISVIKEEAA----------NRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKE 2232
Cdd:PHA02746   201 --EIHHFWFPDWPdngIPTGM-AEFLELINKVNEEQAelikqadndpQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKE 277

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1609046161 2233 NSVDVYQVAKMINLMRPGVFADIEQYQFLYKVI 2265
Cdd:PHA02746   278 KEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL 310

alpha_CARP_X_XI_like

cd03121

Carbonic anhydrase alpha related protein: groups X, XI and related proteins. This subgroup ...

35-282

3.13e-28

Carbonic anhydrase alpha related protein: groups X, XI and related proteins. This subgroup contains carbonic anhydrase related proteins (CARPs) X and XI, which have been implicated in various biological processes of the central nervous system. CARPs are sequence similar to carbonic anhydrases. Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism. CARPs have lost conserved histidines involved in zinc binding and consequently their catalytic activity. CARP XI plays a role in the development of gastrointestinal stromal tumors.

Pssm-ID: 239395 [Multi-domain] Cd Length: 256 Bit Score: 115.97 E-value: 3.13e-28

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161   35 WGKKYPT---CNSPK-QSPINIDEDLTQVNVNLKKLKFQGWDKTSLEntfIHNTGKTVEINLTNDYRV--SGGVSEMVFK 108
Cdd:cd03121      5 WGLVNSAwnlCSKGRrQSPVDIEPSRLLFDPFLTPLRIDTGRKVSGT---FYNTGRHVSFRPDKDPVVniSGGPLSYRYR 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  109 ASKITFHWGKCNmsSDGSEHSLEGQKFPLEMQIYCFDADRFSSFEEAVKGKGKLRALSILFEVGTEENLDFKAIIDGVES 188
Cdd:cd03121     82 LEEIRLHFGRED--EQGSEHTVNGQAFPGEVQLIHYNSELYPNFSEASKSPNGLVIVSLFVKIGETSNPELRRLTNRDTI 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  189 VS-RFGKQAALDPFILLNLLPNSTDKYYIYNGSLTSPPCTDTVDWIVFKDTVSISESQLAvfcEVLTMQQSGYVMLMDYL 267
Cdd:cd03121    160 TSiRYKGDAYFLQDLSIELLLPETDHYITYEGSLTSPGCHETVTWIILNKPIYITKEQMH---SLRLLSQNSPSQEKAPM 236

                          250
                   ....*....|....*
gi 1609046161  268 QNNFREQQYKFSRQV 282
Cdd:cd03121    237 SPNFRPVQPLNNRPV 251

alpha_CARP_VIII

cd03120

Carbonic anhydrase alpha related protein, group VIII. Carbonic anhydrase related proteins ...

35-275

1.61e-27

Carbonic anhydrase alpha related protein, group VIII. Carbonic anhydrase related proteins (CARPs) are sequence similar to carbonic anhydrases. Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism. CARPs have lost conserved histidines involved in zinc binding and consequently their catalytic activity. CARP VIII may play roles in various biological processes of the central nervous system, and could be involved in protein-protein interactions. CARP VIII has been shown to bind inositol 1,4,5-triphosphate (IP3) receptor type I (IP3RI), reducing the affinity of the receptor for IP3. IP3RI is an intracellular IP3-gated Ca2+ channel located on intracellular Ca2+ stores. IP3RI converts IP3 signaling into Ca2+ signaling thereby participating in a variety of cell functions.

Pssm-ID: 239394 Cd Length: 256 Bit Score: 113.80 E-value: 1.61e-27

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161   35 WGKKYPTCNSPKQSPINI-------DEDLTQVNVNLKKLKFQGWDKTslentfihNTGKTVEINLTNDYRVSGGV--SEM 105
Cdd:cd03120      4 WGLLFPEANGEYQSPINLnsrearyDPSLLEVRLSPNYVVCRDCEVI--------NDGHTIQIILKSKSVLSGGPlpQGH 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  106 VFKASKITFHWGKCNMSsdGSEHSLEGQKFPLEMQIYCFDADRFSSFEEAVKGKGKLRALSILFEVGtEENLDFKAIIDG 185
Cdd:cd03120     76 EFELAEVRFHWGRENQR--GSEHTVNFKAFPMELHLIHWNSTLYSSLEEAMGKPHGIAIIALFVQIG-KEHVGLKAVTEI 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  186 VESVSRFGKQAALDPFILLNLLPNSTDK-YYIYNGSLTSPPCTDTVDWIVFKDTVSISESQLAVFCEvLTMQQSGY--VM 262
Cdd:cd03120    153 LQDIQYKGKSKTIPCFNPNTLLPDPLLRdYWVYEGSLTTPPCSEGVTWILFRYPLTISQSQIEEFRR-LRTHVKGAelVE 231

                          250
                   ....*....|....
gi 1609046161  263 LMDY-LQNNFREQQ 275
Cdd:cd03120    232 GCDGlLGDNFRPTQ 245

PTPc-N1_2

cd14545

catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...

2035-2263

1.89e-27

Pssm-ID: 350393 [Multi-domain] Cd Length: 231 Bit Score: 112.87 E-value: 1.89e-27

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2035 REKNRTSSIIPVERSRVgisSLSGEGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVM----IPDG 2110
Cdd:cd14545      1 LNRYRDRDPYDHDRSRV---KLKQGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMlnklMEKG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2111 QNMAEDefvYWPNKDEPINC---ESFKVTLMAEEHKclsneEKLIIQDFILEATQDDYVLEVRHFQCPKWPN---PDSPI 2184
Cdd:cd14545     78 QIKCAQ---YWPQGEGNAMIfedTGLKVTLLSEEDK-----SYYTVRTLELENLKTQETREVLHFHYTTWPDfgvPESPA 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2185 SKTFELISVIKEEAANRD-GPMIVHDEHGGVTAGTFCALTTLMHQLEKEN--SVDVYQVAKMINLMRPGVFADIEQYQFL 2261
Cdd:cd14545    150 AFLNFLQKVRESGSLSSDvGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNpsSVDVKKVLLEMRKYRMGLIQTPDQLRFS 229


                   ..
gi 1609046161 2262 YK 2263
Cdd:cd14545    230 YL 231

R-PTPc-M-2

cd14635

PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...

2063-2266

1.93e-27

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: 112.09 E-value: 1.93e-27

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2063 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDgQNMAEDEFVYWP----NKDEPINCESFKVTLm 2138
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLND-VDPAQLCPQYWPengvHRHGPIQVEFVSADL- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2139 aeehkclsnEEKLIIQDF-ILEAT--QDDYVLeVRHFQCPKWP-NPDSPISKT--FELISVI---KEEAANRDGPMIVHD 2209
Cdd:cd14635     79 ---------EEDIISRIFrIYNAArpQDGYRM-VQQFQFLGWPmYRDTPVSKRsfLKLIRQVdkwQEEYNGGEGRTVVHC 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1609046161 2210 EHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVIL 2266
Cdd:cd14635    149 LNGGGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVAL 205

PTPc-N1

cd14608

catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...

2022-2266

2.25e-27

Pssm-ID: 350456 [Multi-domain] Cd Length: 277 Bit Score: 113.97 E-value: 2.25e-27

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2022 QQSDY--SAALKQCNREKNRTSSIIPVERSRVgisSLSGEGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDH 2099
Cdd:cd14608     11 EASDFpcRVAKLPKNKNRNRYRDVSPFDHSRI---KLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQ 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2100 NAQLVVMIpdgQNMAEDEFV----YWPNKDEP---INCESFKVTLMAEEHKCLSNEEKLIIQDFILEATQddyvlEVRHF 2172
Cdd:cd14608     88 KSRGVVML---NRVMEKGSLkcaqYWPQKEEKemiFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETR-----EILHF 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2173 QCPKWPN---PDSPISKTFELISVIKEEAANRD-GPMIVHDEHGGVTAGTFCALTT---LMHQLEKENSVDVYQVAKMIN 2245
Cdd:cd14608    160 HYTTWPDfgvPESPASFLNFLFKVRESGSLSPEhGPVVVHCSAGIGRSGTFCLADTcllLMDKRKDPSSVDIKKVLLEMR 239

                          250       260
                   ....*....|....*....|.
gi 1609046161 2246 LMRPGVFADIEQYQFLYKVIL 2266
Cdd:cd14608    240 KFRMGLIQTADQLRFSYLAVI 260

R-PTPc-K-1

cd14631

catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...

2061-2266

2.43e-27

Pssm-ID: 350479 [Multi-domain] Cd Length: 218 Bit Score: 112.04 E-value: 2.43e-27

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2061 TDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdgQNMAE----DEFVYWPNKDEPINceSFKVT 2136
Cdd:cd14631     13 SDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMV---TNLVEvgrvKCYKYWPDDTEVYG--DFKVT 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2137 LMAEEHKClsneeKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISVIKEEAANRDGPMIVHDEHGGV 2214
Cdd:cd14631     88 CVEMEPLA-----EYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATglLSFIRRVKLSNPPSAGPIVVHCSAGAG 162

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1609046161 2215 TAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVIL 2266
Cdd:cd14631    163 RTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAIL 214

PTPc-N22_18_12

cd14542

catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...

2063-2263

3.07e-27

Pssm-ID: 350390 [Multi-domain] Cd Length: 202 Bit Score: 111.36 E-value: 3.07e-27

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2063 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVM----IPDGQNMAEDefvYWPNK-DEPINCESFKVTL 2137
Cdd:cd14542      1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMacreFEMGKKKCER---YWPEEgEEQLQFGPFKISL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2138 MAEEHKClsneekliiQDFI---LEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISVIKEEAANRDGPMIVHDEHG 2212
Cdd:cd14542     78 EKEKRVG---------PDFLirtLKVTFQKESRTVYQFHYTAWPDHGVPSSVDpiLDLVRLVRDYQGSEDVPICVHCSAG 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1609046161 2213 GVTAGTFCALT---TLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYK 2263
Cdd:cd14542    149 CGRTGTICAIDyvwNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202

R-PTPc-D-1

cd14624

catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...

2022-2270

4.60e-27

Pssm-ID: 350472 [Multi-domain] Cd Length: 284 Bit Score: 113.29 E-value: 4.60e-27

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2022 QQSDYSAALKQCNREKNRTSSIIPVERSRVGISSLSG-EGTDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHN 2100
Cdd:cd14624     35 QQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGiPGSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQR 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2101 AQLVVMIPDGQNMAE---DEfvYWPNKDEPINcESFKVTLMAEEHKClsneeKLIIQDFILEATQDDYVLEVRHFQCPKW 2177
Cdd:cd14624    115 SATVVMMTKLEERSRvkcDQ--YWPSRGTETY-GLIQVTLLDTVELA-----TYCVRTFALYKNGSSEKREVRQFQFTAW 186

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2178 PNPDSPISKTFELISVIKEEAAN--RDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADI 2255
Cdd:cd14624    187 PDHGVPEHPTPFLAFLRRVKTCNppDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTE 266

                          250
                   ....*....|....*
gi 1609046161 2256 EQYQFLYKVILSLVS 2270
Cdd:cd14624    267 DQYIFIHDALLEAVT 281

R-PTPc-G-1

cd17667

catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...

2034-2269

6.22e-27

Pssm-ID: 350505 [Multi-domain] Cd Length: 274 Bit Score: 112.82 E-value: 6.22e-27

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2034 NREKNRTSSIIPVERSRVGISSLSGEGT---DYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdg 2110
Cdd:cd17667     27 NKHKNRYINILAYDHSRVKLRPLPGKDSkhsDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMI--- 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2111 QNMAE------DEfvYWPNKdepiNCESFK---VTLMAEE-HKCLSneekliIQDFILEATQDDYVLE-----------V 2169
Cdd:cd17667    104 TNLVEkgrrkcDQ--YWPTE----NSEEYGniiVTLKSTKiHACYT------VRRFSIRNTKVKKGQKgnpkgrqnertV 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2170 RHFQCPKWPNPDSPiSKTFELISVIKEEAANRD---GPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINL 2246
Cdd:cd17667    172 IQYHYTQWPDMGVP-EYALPVLTFVRRSSAARTpemGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRT 250

                          250       260
                   ....*....|....*....|...
gi 1609046161 2247 MRPGVFADIEQYQFLYKVILSLV 2269
Cdd:cd17667    251 QRNYLVQTEEQYIFIHDALLEAI 273

PTPc-N11_6

cd14544

catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...

2034-2265

7.45e-27

Pssm-ID: 350392 [Multi-domain] Cd Length: 251 Bit Score: 111.79 E-value: 7.45e-27

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2034 NREKNRTSSIIPVERSRVGISSL--SGEGTDYINASYIM-------GYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLV 2104
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILKDRdpNVPGSDYINANYIRnenegptTDENAKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2105 VMIPDGQNMAEDEFV-YWPnkDEpincesfkVTLMAEEHKCLSNEEKLIIQDFIL------EATQDDYVLEVRHFQCPKW 2177
Cdd:cd14544     81 VMTTKEVERGKNKCVrYWP--DE--------GMQKQYGPYRVQNVSEHDTTDYTLrelqvsKLDQGDPIREIWHYQYLSW 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2178 PNPDSPiSKTFELISVI-----KEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKEN---SVDVYQVAKMINLMRP 2249
Cdd:cd14544    151 PDHGVP-SDPGGVLNFLedvnqRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRS 229

                          250
                   ....*....|....*.
gi 1609046161 2250 GVFADIEQYQFLYKVI 2265
Cdd:cd14544    230 GMVQTEAQYKFIYVAV 245

R-PTPc-U-2

cd14637

PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...

1768-1977

8.86e-27

Pssm-ID: 350485 [Multi-domain] Cd Length: 207 Bit Score: 110.00 E-value: 8.86e-27

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1768 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRR-KCDQYWPADGSEEYGNFLVTQKSVQ 1846
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPGLQQYGPMEVEFVSGS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1847 VLAYYTVRNFTLRN-TKIKKGSqkgrpsgRVVTQYHYTQW-PDMGVPEYS---LPVLTFVRKaaYAKRHAVGPVVVHCSA 1921
Cdd:cd14637     81 ADEDIVTRLFRVQNiTRLQEGH-------LMVRHFQFLRWsAYRDTPDSKkafLHLLASVEK--WQRESGEGRTVVHCLN 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1609046161 1922 GVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1977
Cdd:cd14637    152 GGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207

R-PTP-N2

cd14610

PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...

2006-2260

9.47e-27

Pssm-ID: 350458 [Multi-domain] Cd Length: 283 Bit Score: 112.46 E-value: 9.47e-27

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2006 KTKLEKQFQLLSQSNIQQSDYSAALKQCNREKNRTSSIIPVERSRVGISSL-SGEGTDYINASYIMGYYQSN-EFIITQH 2083
Cdd:cd14610     16 KNRLEKEWEALCAYQAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAEnSHSHSDYINASPIMDHDPRNpAYIATQG 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2084 PLLHTIKDFWRMIWDHNAQLVVMI-PDGQNMAEDEFVYWPnkDEPINC-ESFKVTLMAEEHKClsneEKLIIQDFILEAT 2161
Cdd:cd14610     96 PLPATVADFWQMVWESGCVVIVMLtPLAENGVKQCYHYWP--DEGSNLyHIYEVNLVSEHIWC----EDFLVRSFYLKNL 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2162 QDDYVLEVRHFQCPKWPNPDSPIS--KTFELISVIKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEK-ENSVDVY 2238
Cdd:cd14610    170 QTNETRTVTQFHFLSWNDQGVPAStrSLLDFRRKVNKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMAKgAKEIDIA 249

                          250       260
                   ....*....|....*....|..
gi 1609046161 2239 QVAKMINLMRPGVFADIEQYQF 2260
Cdd:cd14610    250 ATLEHLRDQRPGMVQTKEQFEF 271

R-PTPc-S-1

cd14625

catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...

2008-2270

9.55e-27

Pssm-ID: 350473 [Multi-domain] Cd Length: 282 Bit Score: 112.49 E-value: 9.55e-27

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2008 KLEKQFQLLSQSniQQSDYSAALKQCNREKNRTSSIIPVERSRVGISSLSG-EGTDYINASYIMGYYQSNEFIITQHPLL 2086
Cdd:cd14625     23 KLSQEYESIDPG--QQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGiMGSDYINANYIDGYRKQNAYIATQGPLP 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2087 HTIKDFWRMIWDHNAQLVVM---IPDGQNMAEDEfvYWPNKdepiNCESF---KVTLMAEEHKClsneeKLIIQDFILEA 2160
Cdd:cd14625    101 ETFGDFWRMVWEQRSATVVMmtkLEEKSRIKCDQ--YWPSR----GTETYgmiQVTLLDTIELA-----TFCVRTFSLHK 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2161 TQDDYVLEVRHFQCPKWPNPDSPISKTFELISVIKEEAAN--RDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVY 2238
Cdd:cd14625    170 NGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNppDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIY 249

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1609046161 2239 QVAKMINLMRPGVFADIEQYQFLYKVILSLVS 2270
Cdd:cd14625    250 GHVTLMRSQRNYMVQTEDQYSFIHDALLEAVA 281

R-PTPc-M-2

cd14635

PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...

1768-1977

4.60e-26

Pssm-ID: 350483 [Multi-domain] Cd Length: 206 Bit Score: 107.85 E-value: 4.60e-26

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1768 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLveKGRRKCDQYWPADGSEEYGNFLVTQKSVQV 1847
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV--DPAQLCPQYWPENGVHRHGPIQVEFVSADL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1848 LAYYTVRNFTLRNTkikkgsqkGRPSG--RVVTQYHYTQWPDM-GVPEYSLPVLTFVRKAAYAKRH---AVGPVVVHCSA 1921
Cdd:cd14635     79 EEDIISRIFRIYNA--------ARPQDgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEyngGEGRTVVHCLN 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1609046161 1922 GVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1977
Cdd:cd14635    151 GGGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206

R-PTPc-R

cd14611

catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...

2037-2262

9.78e-26

Pssm-ID: 350459 [Multi-domain] Cd Length: 226 Bit Score: 107.70 E-value: 9.78e-26

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2037 KNRTSSIIPVERSRVGI--SSLSGEGTDYINASYIMGYY-QSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNM 2113
Cdd:cd14611      2 KNRYKTILPNPHSRVCLkpKNSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2114 AEDEFVYWPNKDEPINcesfKVTLMAeehKCLSNEEKLIIQDFILEatQDDYVLEVRHFQCPKWPNPDSPISKT--FELI 2191
Cdd:cd14611     82 NEKCVLYWPEKRGIYG----KVEVLV---NSVKECDNYTIRNLTLK--QGSQSRSVKHYWYTSWPDHKTPDSAQplLQLM 152

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1609046161 2192 SVIKEE--AANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLY 2262
Cdd:cd14611    153 LDVEEDrlASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225

R-PTP-N

cd14609

PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...

2006-2260

1.86e-25

Pssm-ID: 350457 [Multi-domain] Cd Length: 281 Bit Score: 108.59 E-value: 1.86e-25

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2006 KTKLEKQFQLLSQSNIQQSDYSAALKQCNREKNRTSSIIPVERSRVGI-SSLSGEGTDYINASYIMGY-YQSNEFIITQH 2083
Cdd:cd14609     14 RDRLAKEWQALCAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLkAESNPSRSDYINASPIIEHdPRMPAYIATQG 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2084 PLLHTIKDFWRMIWDHNAQLVVM----IPDGQNMAEDefvYWPNKDEPINcESFKVTLMAEEHKClsneEKLIIQDFILE 2159
Cdd:cd14609     94 PLSHTIADFWQMVWENGCTVIVMltplVEDGVKQCDR---YWPDEGSSLY-HIYEVNLVSEHIWC----EDFLVRSFYLK 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2160 ATQDDYVLEVRHFQCPKWPNPDSPiSKTFELISV---IKEEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKE-NSV 2235
Cdd:cd14609    166 NVQTQETRTLTQFHFLSWPAEGIP-SSTRPLLDFrrkVNKCYRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGvKEI 244

                          250       260
                   ....*....|....*....|....*
gi 1609046161 2236 DVYQVAKMINLMRPGVFADIEQYQF 2260
Cdd:cd14609    245 DIAATLEHVRDQRPGMVRTKDQFEF 269

R-PTPc-U-1

cd14632

catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...

2063-2266

1.98e-25

Pssm-ID: 350480 [Multi-domain] Cd Length: 205 Bit Score: 106.29 E-value: 1.98e-25

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2063 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdgQNMAEDEFV----YWPNKDEPINceSFKVTLM 2138
Cdd:cd14632      1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMI---TKLVEVGRVkcskYWPDDSDTYG--DIKITLL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2139 AEEhkclsNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKT--FELISVIKEEAANRDGPMIVHDEHGGVTA 2216
Cdd:cd14632     76 KTE-----TLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATglLAFIRRVKASTPPDAGPVVVHCSAGAGRT 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2217 GTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVIL 2266
Cdd:cd14632    151 GCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAIL 200

R-PTPc-K-2

cd14636

PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...

1768-1977

3.98e-25

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: 3.98e-25

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1768 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNL-VEKGrrkCDQYWPADGSEEYGNFLVTQKSVQ 1846
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVdLAQG---CPQYWPEEGMLRYGPIQVECMSCS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1847 VLAYYTVRNFTLRN-TKIKKGSQkgrpsgrVVTQYHYTQWPD-MGVPEYS---LPVLTFVRKAAYAKRHAVGPVVVHCSA 1921
Cdd:cd14636     78 MDCDVISRIFRICNlTRPQEGYL-------MVQQFQYLGWAShREVPGSKrsfLKLILQVEKWQEECDEGEGRTIIHCLN 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1609046161 1922 GVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLVE 1977
Cdd:cd14636    151 GGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206

PTPc-N13

cd14597

catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...

2034-2266

4.90e-25

Pssm-ID: 350445 [Multi-domain] Cd Length: 234 Bit Score: 106.07 E-value: 4.90e-25

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2034 NREKNRTSSIIPVERSRVgissLSGEGTDYINASYIMGYYQSNEF--IITQHPLLHTIKDFWRMIWDHNAQLVVMIpdgQ 2111
Cdd:cd14597      3 NRKKNRYKNILPYDTTRV----PLGDEGGYINASFIKMPVGDEEFvyIACQGPLPTTVADFWQMVWEQKSTVIAMM---T 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2112 NMAEDEFV----YWP---NKDEPINcESFKVTLMAEEHkclsnEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPi 2184
Cdd:cd14597     76 QEVEGGKIkcqrYWPeilGKTTMVD-NRLQLTLVRMQQ-----LKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTP- 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2185 SKTFELISVIK-EEAANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYK 2263
Cdd:cd14597    149 SQPEQLLTFISyMRHIHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQ 228


                   ...
gi 1609046161 2264 VIL 2266
Cdd:cd14597    229 VIL 231

R-PTPc-A-E-1

cd14551

catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...

2063-2263

1.53e-24

Pssm-ID: 350399 [Multi-domain] Cd Length: 202 Bit Score: 103.45 E-value: 1.53e-24

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2063 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDEFV-YWPNKdepiNCESFKVTLMaee 2141
Cdd:cd14551      1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSqYWPDQ----GCWTYGNLRV--- 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2142 hkCLSNEEKLI---IQDFILEATQDDY----VLEVRHFQCPKWPN---PDSPISkTFELISVIKEEAANRDGPMIVHDEH 2211
Cdd:cd14551     74 --RVEDTVVLVdytTRKFCIQKVNRGIgekrVRLVTQFHFTSWPDfgvPFTPIG-MLKFLKKVKSANPPRAGPIVVHCSA 150

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1609046161 2212 GGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYK 2263
Cdd:cd14551    151 GVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202

R-PTPc-K-2

cd14636

PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...

2063-2266

3.24e-24

Pssm-ID: 350484 [Multi-domain] Cd Length: 206 Bit Score: 102.80 E-value: 3.24e-24

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2063 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDgQNMAEDEFVYWPNKDE----PINCESFKVTLM 2138
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNE-VDLAQGCPQYWPEEGMlrygPIQVECMSCSMD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2139 AEehkCLSNeeklIIQDFILEATQDDYVLeVRHFQCPKWP-NPDSPISKT--FELISVI---KEEAANRDGPMIVHDEHG 2212
Cdd:cd14636     80 CD---VISR----IFRICNLTRPQEGYLM-VQQFQYLGWAsHREVPGSKRsfLKLILQVekwQEECDEGEGRTIIHCLNG 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1609046161 2213 GVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVIL 2266
Cdd:cd14636    152 GGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVAL 205

PTPc-N20_13

cd14538

catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...

2063-2266

1.27e-23

Pssm-ID: 350386 [Multi-domain] Cd Length: 207 Bit Score: 100.91 E-value: 1.27e-23

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2063 YINASYIMGYYQSNEF--IITQHPLLHTIKDFWRMIWDHNAQLVVMIPdgQNMaEDEFV----YWPnkdepincESFKVT 2136
Cdd:cd14538      1 YINASHIRIPVGGDTYhyIACQGPLPNTTGDFWQMVWEQKSEVIAMVT--QDV-EGGKVkchrYWP--------DSLNKP 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2137 LMAEEHKCLSNEEKLIIQDFI-----LEATQDDYVLEVRHFQCPKWPNPDSPISkTFELISVIKE-EAANRDGPMIVHDE 2210
Cdd:cd14538     70 LICGGRLEVSLEKYQSLQDFVirrisLRDKETGEVHHITHLNFTTWPDHGTPQS-ADPLLRFIRYmRRIHNSGPIVVHCS 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1609046161 2211 HGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVIL 2266
Cdd:cd14538    149 AGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACL 204

PTPc_DSPc

smart00012

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...

2168-2267

8.64e-23

Pssm-ID: 214469 [Multi-domain] Cd Length: 105 Bit Score: 95.12 E-value: 8.64e-23

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  2168 EVRHFQCPKWPNPDSPISKT--FELISVIKEE--AANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKE-NSVDVYQVAK 2242
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDsiLELLRAVKKNlnQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 1609046161  2243 MINLMRPGVFADIEQYQFLYKVILS 2267
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105

PTPc_motif

smart00404

Protein tyrosine phosphatase, catalytic domain motif;

2168-2267

8.64e-23

Protein tyrosine phosphatase, catalytic domain motif;

Pssm-ID: 214649 [Multi-domain] Cd Length: 105 Bit Score: 95.12 E-value: 8.64e-23

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161  2168 EVRHFQCPKWPNPDSPISKT--FELISVIKEE--AANRDGPMIVHDEHGGVTAGTFCALTTLMHQLEKE-NSVDVYQVAK 2242
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDsiLELLRAVKKNlnQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 1609046161  2243 MINLMRPGVFADIEQYQFLYKVILS 2267
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105

PTPc-N20

cd14596

catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...

2063-2266

8.87e-23

Pssm-ID: 350444 [Multi-domain] Cd Length: 207 Bit Score: 98.67 E-value: 8.87e-23

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2063 YINASYIMGYYQSNE--FIITQHPLLHTIKDFWRMIWDHNAQLVVMIPD----GQNMAEDefvYWPNK-DEPINCESFKV 2135
Cdd:cd14596      1 YINASYITMPVGEEElfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTReverGKVKCHR---YWPETlQEPMELENYQL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2136 TLmaEEHKCLsneEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSPISKTfELISVIK-EEAANRDGPMIVHDEHGGV 2214
Cdd:cd14596     78 RL--ENYQAL---QYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSD-QLVKFICyMRKVHNTGPIVVHCSAGIG 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1609046161 2215 TAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVIL 2266
Cdd:cd14596    152 RAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVL 203

R-PTP-G-2

cd17670

PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...

1768-1976

9.65e-23

Pssm-ID: 350508 [Multi-domain] Cd Length: 205 Bit Score: 98.60 E-value: 9.65e-23

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1768 YINANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITN---LVEkgrrkcDQ--YWPAdgSEEYGN---FL 1839
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDnqgLAE------DEfvYWPS--REESMNceaFT 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1840 VTQKSVQVLAYYT-----VRNFTLRNTKIKKGSQkgrpsgrvVTQYHYTQWPDMGVPEYSLPVLTFVRKAAYAKRHavGP 1914
Cdd:cd17670     73 VTLISKDRLCLSNeeqiiIHDFILEATQDDYVLE--------VRHFQCPKWPNPDAPISSTFELINVIKEEALTRD--GP 142

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1609046161 1915 VVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDTLV 1976
Cdd:cd17670    143 TIVHDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204

R-PTPc-Z-1

cd17668

catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...

2063-2266

1.22e-22

Pssm-ID: 350506 [Multi-domain] Cd Length: 209 Bit Score: 98.13 E-value: 1.22e-22

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2063 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIpdgQNMAE------DEfvYWPNKDEPiNCESFKVT 2136
Cdd:cd17668      1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMI---TNLVEkgrrkcDQ--YWPADGSE-EYGNFLVT 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2137 LmaeehKCLSNEEKLIIQDFILEATQDDYVLE--------VRHFQCPKWPNPDSPiSKTFELISVIKEEAANRD---GPM 2205
Cdd:cd17668     75 Q-----KSVQVLAYYTVRNFTLRNTKIKKGSQkgrpsgrvVTQYHYTQWPDMGVP-EYTLPVLTFVRKASYAKRhavGPV 148

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1609046161 2206 IVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYKVIL 2266
Cdd:cd17668    149 VVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209

PHA02740

protein tyrosine phosphatase; Provisional

1730-1987

3.01e-22

protein tyrosine phosphatase; Provisional

Pssm-ID: 165107 [Multi-domain] Cd Length: 298 Bit Score: 99.66 E-value: 3.01e-22

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1730 SSNHPDNKHK--NRYINIVAYDHSRVKLaqlaEKDGKLTDyinANYVDGYNRPKAYIAAQGPLKSTAEDFWRMIWEHNVE 1807
Cdd:PHA02740    45 ACAQAENKAKdeNLALHITRLLHRRIKL----FNDEKVLD---ARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQ 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1808 VIVMITNLVEKgrrKC-DQYWpadgSEEYGNFLVTQK-SVQVLAYYTVRNFTLrnTKIKKGSQKGRpsGRVVTQYHYTQW 1885
Cdd:PHA02740   118 IIVLISRHADK---KCfNQFW----SLKEGCVITSDKfQIETLEIIIKPHFNL--TLLSLTDKFGQ--AQKISHFQYTAW 186

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 1886 PDMGVPEYSLPVLTFV--RKAAYA--KRHA----VGPVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQ 1957
Cdd:PHA02740   187 PADGFSHDPDAFIDFFcnIDDLCAdlEKHKadgkIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQK 266

                          250       260       270
                   ....*....|....*....|....*....|
gi 1609046161 1958 RNYLVQTEEQYVFIHDtLVEAILSKETEVL 1987
Cdd:PHA02740   267 KYGCMNCLDDYVFCYH-LIAAYLKEKFDIL 295

PHA02738

hypothetical protein; Provisional

2023-2265

3.18e-22

hypothetical protein; Provisional

Pssm-ID: 222923 [Multi-domain] Cd Length: 320 Bit Score: 100.00 E-value: 3.18e-22

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2023 QSDYSAALKqcNREKNRTSSIIPVERSRVGISSLSGEGtDYINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQ 2102
Cdd:PHA02738    40 DGTFNAEKK--NRKLNRYLDAVCFDHSRVILPAERNRG-DYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQ 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2103 LVVMI-PDGQNMAEDEFVYWPNKDE-PINCESFKVTLMAEEHKCLSNEEKLIIQDFIlEATQddyvlEVRHFQCPKWPNP 2180
Cdd:PHA02738   117 IIVMLcKKKENGREKCFPYWSDVEQgSIRFGKFKITTTQVETHPHYVKSTLLLTDGT-SATQ-----TVTHFNFTAWPDH 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2181 DSPiSKTFELISVI-------KEEAANR---------DGPMIVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMI 2244
Cdd:PHA02738   191 DVP-KNTSEFLNFVlevrqcqKELAQESlqighnrlqPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSI 269

                          250       260
                   ....*....|....*....|.
gi 1609046161 2245 NLMRPGVFADIEQYQFLYKVI 2265
Cdd:PHA02738   270 RNQRYYSLFIPFQYFFCYRAV 290

R-PTPc-C-1

cd14557

catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...

2063-2263

3.19e-22

Pssm-ID: 350405 [Multi-domain] Cd Length: 201 Bit Score: 96.82 E-value: 3.19e-22

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2063 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLVVMIPDGQNMAEDE-FVYWPNKDEPINC-ESFKVTLMAE 2140
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKcAQYWPSMEEGSRAfGDVVVKINEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609046161 2141 EHkClsneEKLIIQDFILEATQDDY-VLEVRHFQCPKWPN---PDSPiSKTFELISVIKEEAANRDGPMIVHDEHGGVTA 2216
Cdd:cd14557     81 KI-C----PDYIIRKLNINNKKEKGsGREVTHIQFTSWPDhgvPEDP-HLLLKLRRRVNAFNNFFSGPIVVHCSAGVGRT 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1609046161 2217 GTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFADIEQYQFLYK 2263
Cdd:cd14557    155 GTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201

R-PTP-Z-2