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Conserved domains on  [gi|1822521651|ref|XP_032868917|]
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receptor-type tyrosine-protein phosphatase H-like isoform X18 [Amblyraja radiata]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1030-1288 1.82e-116

Protein tyrosine phosphatase, catalytic domain;


:

Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 363.90  E-value: 1.82e-116
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  1030 GFAEEYQGLANVG-TNQSKEAFQVPDNKVKNRYTNIFPYDVARVKLdRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLP 1108
Cdd:smart00194    1 GLEEEFEKLDRLKpDDESCTVAAFPENRDKNRYKDVLPYDHTRVKL-KPPPGEGSDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  1109 NTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCL-YGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTI 1187
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLtYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTV 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  1188 TQFHFTSWPDHGVPKTTDKLLQFQRMMRDYlNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRM 1267
Cdd:smart00194  160 THYHYTNWPDHGVPESPESILDLIRAVRKS-QSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRS 238

                           250       260
                    ....*....|....*....|.
gi 1822521651  1268 SRTCMVQTENQYIFLHQCILD 1288
Cdd:smart00194  239 QRPGMVQTEEQYIFLYRAILE 259
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
357-845 3.68e-17

Fibronectin type 3 domain [General function prediction only];


:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 86.98  E-value: 3.68e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  357 SSTTVTSRGETTFKATGLQPGDQYLLSVQSVTPEDTWSTPVEVTNTTNPSPVTGLTVVNGTTHSLRIEWTPPTDTRATNY 436
Cdd:COG3401      1 TGSSYLTSLDAGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  437 TYKVTVTNVAGGVSSTTITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPVTGLSVVNGTTESLTI 516
Cdd:COG3401     81 AVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  517 EWTSPNDTRASNYIYNVTVTNVTGGVSWTQSTSKDETtftatRLQPGDQYQLSVQSVTP--EDTLSTPVEVT-STTNPSP 593
Cdd:COG3401    161 SSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGG-----DIEPGTTYYYRVAATDTggESAPSNEVSVTtPTTPPSA 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  594 VTGLSVVNGTTQSLTIEWTRPTDTRASNYT-YRVTvtnvTGGVSWSKSTSKGETTFTATGLQPGDQYQLSVQSVTPEDTL 672
Cdd:COG3401    236 PTGLTATADTPGSVTLSWDPVTESDATGYRvYRSN----SGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNE 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  673 STPVEVKSTT----DPSPVTGLSVVNSTTQSLRIEWTTPNNIRASNYtyNVTVTNVTDGASSTTITSKGETTFTVTGLQP 748
Cdd:COG3401    312 SAPSNVVSVTtdltPPAAPSGLTATAVGSSSITLSWTASSDADVTGY--NVYRSTSGGGTYTKIAETVTTTSYTDTGLTP 389

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  749 GDQYRLSVRSVT---PEDTWSTPAQVTSTSNPSPVSGLTVVNRTTVSIEVTWAAPTDARAPEYTYRITLANVTRRGRGAI 825
Cdd:COG3401    390 GTTYYYKVTAVDaagNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVP 469

                          490       500
                   ....*....|....*....|
gi 1822521651  826 DTGPGVTTFTVTNLVPGVEY 845
Cdd:COG3401    470 FTTTSSTVTATTTDTTTANL 489
FN3 super family cl27307
Fibronectin type 3 domain [General function prediction only];
34-558 1.04e-14

Fibronectin type 3 domain [General function prediction only];


The actual alignment was detected with superfamily member COG3401:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 78.89  E-value: 1.04e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651   34 SPVTGLSVVSRTTDSLRIEWTSPNDTRASNYTYNVTVTNVAGGVSSITTTGKNETTFTATGLQPGDQYLLSVRSVTPEDT 113
Cdd:COG3401     82 VAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTAS 161

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  114 LSTPVEVTSTTNPSPVIGLSVVNGTTQSLWIEWTSPTDTRATNYTYIVTVTNVTGgvswtkstnkdkttftatglqpgdq 193
Cdd:COG3401    162 SVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGG------------------------- 216

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  194 yqlsvrsvtpEDTLSTPVEVT-NTTNPSPVTGLSVVNGTTESLRIKWTRPTDTRASDYT-YRVTvtnvTGGVSWTESTSK 271
Cdd:COG3401    217 ----------ESAPSNEVSVTtPTTPPSAPTGLTATADTPGSVTLSWDPVTESDATGYRvYRSN----SGDGPFTKVATV 282

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  272 DKTTFTATGLQPGDQYQLSVQSVTPEDTVSSPLEV----TNTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRATNytYIV 347
Cdd:COG3401    283 TTTSYTDTGLTNGTTYYYRVTAVDAAGNESAPSNVvsvtTDLTPPAAPSGLTATAVGSSSITLSWTASSDADVTG--YNV 360

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  348 TVTNVTGGVSSTTVTSRGETTFKATGLQPGDQYLLSVQSVT---PEDTWSTPVEVTNTTNPSPVTGLTVVNGTTHSLRIE 424
Cdd:COG3401    361 YRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDaagNESAPSEEVSATTASAASGESLTASVDAVPLTDVAG 440

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  425 WT-------PPTDTRATNYTYKVTVTNVAGGVSSTTITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTN 497
Cdd:COG3401    441 ATaaasaasNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAV 520

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1822521651  498 PSPVTGLSVVNGTTE--------SLTIEWTSPNDTRASNYIYNVTVTNVTGGVSWTQSTSKDETTFTAT 558
Cdd:COG3401    521 GGAPDGTPNVTGASPvtvgastgDVLITDLVSLTTSASSSVSGAGLGSGNLYLITTLGGSLLTTTSTNT 589
FN3 super family cl21522
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 872-948 1.28e-03

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.


The actual alignment was detected with superfamily member pfam00041:

Pssm-ID: 473895 [Multi-domain]  Cd Length: 85  Bit Score: 38.94  E-value: 1.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  872 AISDFRCSGSTGYMVEAKWSQP---NGQFSMFKaLTY---DGEQLISNLSLGKEERSLTVDNLQPGRTYTLRVVTESGNT 945
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPpdgNGPITGYE-VEYrpkNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ...
gi 1822521651  946 SSQ 948
Cdd:pfam00041   81 EGP 83
 
Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1030-1288 1.82e-116

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 363.90  E-value: 1.82e-116
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  1030 GFAEEYQGLANVG-TNQSKEAFQVPDNKVKNRYTNIFPYDVARVKLdRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLP 1108
Cdd:smart00194    1 GLEEEFEKLDRLKpDDESCTVAAFPENRDKNRYKDVLPYDHTRVKL-KPPPGEGSDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  1109 NTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCL-YGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTI 1187
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLtYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTV 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  1188 TQFHFTSWPDHGVPKTTDKLLQFQRMMRDYlNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRM 1267
Cdd:smart00194  160 THYHYTNWPDHGVPESPESILDLIRAVRKS-QSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRS 238

                           250       260
                    ....*....|....*....|.
gi 1822521651  1268 SRTCMVQTENQYIFLHQCILD 1288
Cdd:smart00194  239 QRPGMVQTEEQYIFLYRAILE 259
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 1060-1284 5.34e-112

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: 350.50  E-value: 5.34e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1060 RYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVK 1139
Cdd:cd14548      1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1140 CERYWPMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGcpEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLN 1219
Cdd:cd14548     81 CDHYWPFDQDPVYYGDITVTMLSESVLPDWTIREFKLERGD--EVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIK 158

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1822521651 1220 KNrAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1284
Cdd:cd14548    159 QE-KGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1055-1288 6.58e-110

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 345.38  E-value: 6.58e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1055 NKVKNRYTNIFPYDVARVKLdrQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVE 1134
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKL--TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1135 QNRVKCERYWPMDMS-SCLYGDIVVNIVSEET-SPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQR 1212
Cdd:pfam00102   79 KGREKCAQYWPEEEGeSLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1822521651 1213 MMRDYLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1288
Cdd:pfam00102  159 KVRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
1043-1282 3.37e-43

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 159.10  E-value: 3.37e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1043 TNQSKEAFQVPDNKVKNRYTNIFPYDVARVkldrqpnSSSSDYINASY--MPGYHLdkaFIAAQGPLPNTVVDFWRMVWE 1120
Cdd:COG5599     30 SHNDPQYLQNINGSPLNRFRDIQPYKETAL-------RANLGYLNANYiqVIGNHR---YIATQYPLEEQLEDFFQMLFD 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1121 QKTKVIVMLTNCVE--QNRVKCERYWPMDMSsclYGDIVVNIVSEET---SPEWTTRKFNVKKTGC-PEPRTITQFHFTS 1194
Cdd:COG5599    100 NNTPVLVVLASDDEisKPKVKMPVYFRQDGE---YGKYEVSSELTESiqlRDGIEARTYVLTIKGTgQKKIEIPVLHVKN 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1195 WPDHGVPkTTDKLLQFQRMMRDYLNKNRA--GLPVVHCSAGVGRTGTLIALDYLLQRI--EKEAVVDVYGIVHNMRMSRT 1270
Cdd:COG5599    177 WPDHGAI-SAEALKNLADLIDKKEKIKDPdkLLPVVHCRAGVGRTGTLIACLALSKSInaLVQITLSVEEIVIDMRTSRN 255

                          250
                   ....*....|...
gi 1822521651 1271 C-MVQTENQYIFL 1282
Cdd:COG5599    256 GgMVQTSEQLDVL 268
PHA02738 PHA02738
hypothetical protein; Provisional
 1055-1311 9.08e-42

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 156.24  E-value: 9.08e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1055 NKVKNRYTNIFPYDVARVKLDRQPNSSssDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVE 1134
Cdd:PHA02738    49 NRKLNRYLDAVCFDHSRVILPAERNRG--DYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKE 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1135 QNRVKCERYWP-MDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKtGCPEPRTITQFHFTSWPDHGVPKTTDKLLQF--- 1210
Cdd:PHA02738   127 NGREKCFPYWSdVEQGSIRFGKFKITTTQVETHPHYVKSTLLLTD-GTSATQTVTHFNFTAWPDHDVPKNTSEFLNFvle 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1211 ----QRMM---RDYLNKNRAGLP--VVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIF 1281
Cdd:PHA02738   206 vrqcQKELaqeSLQIGHNRLQPPpiVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFF 285

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1822521651 1282 LHQCI---LDVTGDKSIDEPIYENQADLIYENV 1311
Cdd:PHA02738   286 CYRAVkryVNLTVNKVSKKLIPNVQTVSFNKNL 318
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
357-845 3.68e-17

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 86.98  E-value: 3.68e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  357 SSTTVTSRGETTFKATGLQPGDQYLLSVQSVTPEDTWSTPVEVTNTTNPSPVTGLTVVNGTTHSLRIEWTPPTDTRATNY 436
Cdd:COG3401      1 TGSSYLTSLDAGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  437 TYKVTVTNVAGGVSSTTITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPVTGLSVVNGTTESLTI 516
Cdd:COG3401     81 AVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  517 EWTSPNDTRASNYIYNVTVTNVTGGVSWTQSTSKDETtftatRLQPGDQYQLSVQSVTP--EDTLSTPVEVT-STTNPSP 593
Cdd:COG3401    161 SSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGG-----DIEPGTTYYYRVAATDTggESAPSNEVSVTtPTTPPSA 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  594 VTGLSVVNGTTQSLTIEWTRPTDTRASNYT-YRVTvtnvTGGVSWSKSTSKGETTFTATGLQPGDQYQLSVQSVTPEDTL 672
Cdd:COG3401    236 PTGLTATADTPGSVTLSWDPVTESDATGYRvYRSN----SGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNE 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  673 STPVEVKSTT----DPSPVTGLSVVNSTTQSLRIEWTTPNNIRASNYtyNVTVTNVTDGASSTTITSKGETTFTVTGLQP 748
Cdd:COG3401    312 SAPSNVVSVTtdltPPAAPSGLTATAVGSSSITLSWTASSDADVTGY--NVYRSTSGGGTYTKIAETVTTTSYTDTGLTP 389

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  749 GDQYRLSVRSVT---PEDTWSTPAQVTSTSNPSPVSGLTVVNRTTVSIEVTWAAPTDARAPEYTYRITLANVTRRGRGAI 825
Cdd:COG3401    390 GTTYYYKVTAVDaagNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVP 469

                          490       500
                   ....*....|....*....|
gi 1822521651  826 DTGPGVTTFTVTNLVPGVEY 845
Cdd:COG3401    470 FTTTSSTVTATTTDTTTANL 489
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
34-558 1.04e-14

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 78.89  E-value: 1.04e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651   34 SPVTGLSVVSRTTDSLRIEWTSPNDTRASNYTYNVTVTNVAGGVSSITTTGKNETTFTATGLQPGDQYLLSVRSVTPEDT 113
Cdd:COG3401     82 VAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTAS 161

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  114 LSTPVEVTSTTNPSPVIGLSVVNGTTQSLWIEWTSPTDTRATNYTYIVTVTNVTGgvswtkstnkdkttftatglqpgdq 193
Cdd:COG3401    162 SVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGG------------------------- 216

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  194 yqlsvrsvtpEDTLSTPVEVT-NTTNPSPVTGLSVVNGTTESLRIKWTRPTDTRASDYT-YRVTvtnvTGGVSWTESTSK 271
Cdd:COG3401    217 ----------ESAPSNEVSVTtPTTPPSAPTGLTATADTPGSVTLSWDPVTESDATGYRvYRSN----SGDGPFTKVATV 282

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  272 DKTTFTATGLQPGDQYQLSVQSVTPEDTVSSPLEV----TNTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRATNytYIV 347
Cdd:COG3401    283 TTTSYTDTGLTNGTTYYYRVTAVDAAGNESAPSNVvsvtTDLTPPAAPSGLTATAVGSSSITLSWTASSDADVTG--YNV 360

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  348 TVTNVTGGVSSTTVTSRGETTFKATGLQPGDQYLLSVQSVT---PEDTWSTPVEVTNTTNPSPVTGLTVVNGTTHSLRIE 424
Cdd:COG3401    361 YRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDaagNESAPSEEVSATTASAASGESLTASVDAVPLTDVAG 440

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  425 WT-------PPTDTRATNYTYKVTVTNVAGGVSSTTITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTN 497
Cdd:COG3401    441 ATaaasaasNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAV 520

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1822521651  498 PSPVTGLSVVNGTTE--------SLTIEWTSPNDTRASNYIYNVTVTNVTGGVSWTQSTSKDETTFTAT 558
Cdd:COG3401    521 GGAPDGTPNVTGASPvtvgastgDVLITDLVSLTTSASSSVSGAGLGSGNLYLITTLGGSLLTTTSTNT 589
fn3 pfam00041
Fibronectin type III domain;
220-295 3.02e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 55.11  E-value: 3.02e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521651  220 SPVTGLSVVNGTTESLRIKWTRPTDTRASDYTYRVTVTNVTGGVSWTEST-SKDKTTFTATGLQPGDQYQLSVQSVT 295
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITvPGTTTSVTLTGLKPGTEYEVRVQAVN 77
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 219-295 1.02e-08

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: 53.39  E-value: 1.02e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521651   219 PSPVTGLSVVNGTTESLRIKWTRPTDTRASDYTYRVTVTNVTGGVSWTE-STSKDKTTFTATGLQPGDQYQLSVQSVT 295
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEvNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 498-574 1.12e-08

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: 53.39  E-value: 1.12e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521651   498 PSPVTGLSVVNGTTESLTIEWTSPNDTRASNYIYNVTVTNVTGGVSWTQ-STSKDETTFTATRLQPGDQYQLSVQSVT 574
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEvNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78
fn3 pfam00041
Fibronectin type III domain;
778-856 2.47e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 52.42  E-value: 2.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  778 SPVSGLTVVNRTTVSIEVTWAAPTDARAPEYTYRITLANVTRRGRGA-IDTGPGVTTFTVTNLVPGVEYELRLQSVTPAG 856
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNeITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 777-865 3.24e-08

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: 52.50  E-value: 3.24e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  777 PSPVSGLTVVNRTTVSIEVTWAAPTDARAPEYTYRITLANVTRRGRGAIDTGPG-VTTFTVTNLVPGVEYELRLQSVTPA 855
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGsETSYTLTGLKPGTEYEFRVRAVNGG 80

                           90
                   ....*....|..
gi 1822521651  856 GT--RSSPETVR 865
Cdd:cd00063     81 GEspPSESVTVT 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 33-124 5.12e-08

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: 51.73  E-value: 5.12e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651   33 PSPVTGLSVVSRTTDSLRIEWTSPNDTRASNYTYNVTVTNV-AGGVSSITTTGKNETTFTATGLQPGDQYLLSVRSVTpE 111
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKgSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN-G 79

                           90
                   ....*....|...
gi 1822521651  112 DTLSTPVEVTSTT 124
Cdd:cd00063     80 GGESPPSESVTVT 92
fn3 pfam00041
Fibronectin type III domain;
872-948 1.28e-03

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 38.94  E-value: 1.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  872 AISDFRCSGSTGYMVEAKWSQP---NGQFSMFKaLTY---DGEQLISNLSLGKEERSLTVDNLQPGRTYTLRVVTESGNT 945
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPpdgNGPITGYE-VEYrpkNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ...
gi 1822521651  946 SSQ 948
Cdd:pfam00041   81 EGP 83
 
Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1030-1288 1.82e-116

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 363.90  E-value: 1.82e-116
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  1030 GFAEEYQGLANVG-TNQSKEAFQVPDNKVKNRYTNIFPYDVARVKLdRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLP 1108
Cdd:smart00194    1 GLEEEFEKLDRLKpDDESCTVAAFPENRDKNRYKDVLPYDHTRVKL-KPPPGEGSDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  1109 NTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCL-YGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTI 1187
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLtYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTV 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  1188 TQFHFTSWPDHGVPKTTDKLLQFQRMMRDYlNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRM 1267
Cdd:smart00194  160 THYHYTNWPDHGVPESPESILDLIRAVRKS-QSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRS 238

                           250       260
                    ....*....|....*....|.
gi 1822521651  1268 SRTCMVQTENQYIFLHQCILD 1288
Cdd:smart00194  239 QRPGMVQTEEQYIFLYRAILE 259
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 1060-1284 5.34e-112

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: 350.50  E-value: 5.34e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1060 RYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVK 1139
Cdd:cd14548      1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1140 CERYWPMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGcpEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLN 1219
Cdd:cd14548     81 CDHYWPFDQDPVYYGDITVTMLSESVLPDWTIREFKLERGD--EVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIK 158

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1822521651 1220 KNrAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1284
Cdd:cd14548    159 QE-KGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1055-1288 6.58e-110

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 345.38  E-value: 6.58e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1055 NKVKNRYTNIFPYDVARVKLdrQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVE 1134
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKL--TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1135 QNRVKCERYWPMDMS-SCLYGDIVVNIVSEET-SPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQR 1212
Cdd:pfam00102   79 KGREKCAQYWPEEEGeSLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1822521651 1213 MMRDYLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1288
Cdd:pfam00102  159 KVRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 1059-1288 6.97e-109

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: 342.18  E-value: 6.97e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1059 NRYTNIFPYDVARVKLDrQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRV 1138
Cdd:cd14615      1 NRYNNVLPYDISRVKLS-VQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1139 KCERYWPMDMSSClYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYL 1218
Cdd:cd14615     80 KCEEYWPSKQKKD-YGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREYM 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1822521651 1219 NKNRAGLPV-VHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1288
Cdd:cd14615    159 KQNPPNSPIlVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 1059-1288 5.29e-106

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: 334.55  E-value: 5.29e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1059 NRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRV 1138
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1139 KCERYWPMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYL 1218
Cdd:cd14619     81 KCEHYWPLDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQWL 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1822521651 1219 NKNRA-GLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1288
Cdd:cd14619    161 DQTMSgGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILD 231
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 1085-1284 2.21e-97

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: 309.60  E-value: 2.21e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1085 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCL-YGDIVVNIVSE 1163
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLeYGDITVTLVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1164 ETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKNRaGLPVVHCSAGVGRTGTLIAL 1243
Cdd:cd00047     81 EELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPN-GPIVVHCSAGVGRTGTFIAI 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1822521651 1244 DYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1284
Cdd:cd00047    160 DILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 1059-1284 7.19e-96

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: 306.85  E-value: 7.19e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1059 NRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRV 1138
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1139 KCERYWPMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVkktgCPE-----PRTITQFHFTSWPDHGVPKTTDKLLQFQRM 1213
Cdd:cd14617     81 KCDHYWPADQDSLYYGDLIVQMLSESVLPEWTIREFKI----CSEeqldaPRLVRHFHYTVWPDHGVPETTQSLIQFVRT 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1822521651 1214 MRDYLNK-NRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1284
Cdd:cd14617    157 VRDYINRtPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 1046-1287 2.93e-92

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: 297.57  E-value: 2.93e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1046 SKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKV 1125
Cdd:cd14614      3 PHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQI 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1126 IVMLTNCVEQNRVKCERYWPMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGcpEPRTITQFHFTSWPDHGVP--KT 1203
Cdd:cd14614     83 IVMLTQCNEKRRVKCDHYWPFTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYAD--EVQDVMHFNYTAWPDHGVPtaNA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1204 TDKLLQFQRMMRDYLNKnRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLH 1283
Cdd:cd14614    161 AESILQFVQMVRQQAVK-SKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIH 239


                   ....
gi 1822521651 1284 QCIL 1287
Cdd:cd14614    240 QCVQ 243
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 1055-1288 1.24e-91

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: 295.46  E-value: 1.24e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1055 NKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVE 1134
Cdd:cd14553      3 NKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1135 QNRVKCERYWPMDMSScLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMM 1214
Cdd:cd14553     83 RSRVKCDQYWPTRGTE-TYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRV 161

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1822521651 1215 RdYLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1288
Cdd:cd14553    162 K-ACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLE 234
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 1059-1287 1.03e-86

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: 281.45  E-value: 1.03e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1059 NRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRV 1138
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1139 KCERYWPMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYL 1218
Cdd:cd14618     81 LCDHYWPSESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVREHV 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1219 NKNRAGLPV-VHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCIL 1287
Cdd:cd14618    161 QATKGKGPTlVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 1085-1283 1.03e-81

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: 266.52  E-value: 1.03e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1085 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSClYGDIVVNIVSEE 1164
Cdd:cd14549      1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTET-YGNIQVTLLSTE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1165 TSPEWTTRKFNVK------KTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRmMRDYLNKNRAGLPVVHCSAGVGRTG 1238
Cdd:cd14549     80 VLATYTVRTFSLKnlklkkVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVR-KSSAANPPGAGPIVVHCSAGVGRTG 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1822521651 1239 TLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLH 1283
Cdd:cd14549    159 TYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 1059-1284 4.28e-80

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: 262.54  E-value: 4.28e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1059 NRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRV 1138
Cdd:cd14616      1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1139 KCERYWPMDMSS-CLYGDIVVNIVSEETSPEWTTRKFNVKKTGcpEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRdy 1217
Cdd:cd14616     81 RCHQYWPEDNKPvTVFGDIVITKLMEDVQIDWTIRDLKIERHG--DYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVR-- 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1218 lnKNRAGLP---VVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1284
Cdd:cd14616    157 --ASRAHDNtpmIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 1030-1283 8.53e-80

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: 263.84  E-value: 8.53e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1030 GFAEEYQGLAN---VGTNQSKEAfqvPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGP 1106
Cdd:cd14543      4 GIYEEYEDIRReppAGTFLCSLA---PANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1107 LPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCL-YGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPR 1185
Cdd:cd14543     81 LPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLrYGDLTVTNLSVENKEHYKKTTLEIHNTETDESR 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1186 TITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLN----------KNRAGLP--VVHCSAGVGRTGTLIALDYLLQRIEKE 1253
Cdd:cd14543    161 QVTHFQFTSWPDFGVPSSAAALLDFLGEVRQQQAlavkamgdrwKGHPPGPpiVVHCSAGIGRTGTFCTLDICLSQLEDV 240

                          250       260       270
                   ....*....|....*....|....*....|
gi 1822521651 1254 AVVDVYGIVHNMRMSRTCMVQTENQYIFLH 1283
Cdd:cd14543    241 GTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 1054-1288 6.39e-76

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: 251.48  E-value: 6.39e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1054 DNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCV 1133
Cdd:cd14630      2 ENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1134 EQNRVKCERYWPMDMSscLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRM 1213
Cdd:cd14630     82 EVGRVKCVRYWPDDTE--VYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVRQ 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1822521651 1214 MRdYLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1288
Cdd:cd14630    160 VK-FLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 1014-1288 4.24e-75

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: 250.72  E-value: 4.24e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1014 SEYKSYYQRKHADTDIGFAEEYQGLaNVGTNQSKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPG 1093
Cdd:cd14626      1 SDLADNIERLKANDGLKFSQEYESI-DPGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1094 YHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSClYGDIVVNIVSEETSPEWTTRK 1173
Cdd:cd14626     80 YRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTET-YGMIQVTLLDTVELATYSVRT 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1174 FNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDyLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKE 1253
Cdd:cd14626    159 FALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKA-CNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHE 237

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1822521651 1254 AVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1288
Cdd:cd14626    238 KTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLE 272
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 1059-1284 6.12e-74

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: 245.38  E-value: 6.12e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1059 NRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGY-HLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEqNR 1137
Cdd:cd14547      1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYdGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTE-AK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1138 VKCERYWPMDMSScLYGDIVVNIVSEETSPEWTTRKFNVKKTGcpEPRTITQFHFTSWPDHGVPKTTDKLLQFQR-MMRD 1216
Cdd:cd14547     80 EKCAQYWPEEENE-TYGDFEVTVQSVKETDGYTVRKLTLKYGG--EKRYLKHYWYTSWPDHKTPEAAQPLLSLVQeVEEA 156

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521651 1217 YLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1284
Cdd:cd14547    157 RQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 1030-1288 1.38e-73

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: 246.11  E-value: 1.38e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1030 GFAEEYQGLANvGTNQSKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPN 1109
Cdd:cd14633     16 GFKEEYESFFE-GQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYHRPNHYIATQGPMQE 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1110 TVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSscLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQ 1189
Cdd:cd14633     95 TIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTE--IYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQ 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1190 FHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKNrAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSR 1269
Cdd:cd14633    173 FHFTGWPDHGVPYHATGLLGFVRQVKSKSPPN-AGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRR 251

                          250
                   ....*....|....*....
gi 1822521651 1270 TCMVQTENQYIFLHQCILD 1288
Cdd:cd14633    252 VNMVQTEEQYVFIHDAILE 270
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 1008-1288 5.62e-73

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: 245.32  E-value: 5.62e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1008 FKPIPVSEYKSYYQRKHADTDIGFAEEYQGLANVGTNQSKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYIN 1087
Cdd:cd14621      5 YPPLPVDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYIN 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1088 ASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPmDMSSCLYGDIVVNIVSEETSP 1167
Cdd:cd14621     85 ASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWP-DQGCWTYGNIRVSVEDVTVLV 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1168 EWTTRKFNVKK----TGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDyLNKNRAGLPVVHCSAGVGRTGTLIAL 1243
Cdd:cd14621    164 DYTVRKFCIQQvgdvTNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKN-CNPQYAGAIVVHCSAGVGRTGTFIVI 242

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1822521651 1244 DYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1288
Cdd:cd14621    243 DAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLE 287
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 1010-1291 1.44e-72

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


Pssm-ID: 350473 [Multi-domain]  Cd Length: 282  Bit Score: 243.85  E-value: 1.44e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1010 PIPVSEYKSYYQRKHADTDIGFAEEYQGLaNVGTNQSKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINAS 1089
Cdd:cd14625      3 PIPISELAEHTERLKANDNLKLSQEYESI-DPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINAN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1090 YMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPmDMSSCLYGDIVVNIVSEETSPEW 1169
Cdd:cd14625     82 YIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWP-SRGTETYGMIQVTLLDTIELATF 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1170 TTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDyLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQR 1249
Cdd:cd14625    161 CVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKT-CNPPDAGPIVVHCSAGVGRTGCFIVIDAMLER 239

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1822521651 1250 IEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILDVTG 1291
Cdd:cd14625    240 IKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAVA 281
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 1031-1288 2.89e-72

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: 242.63  E-value: 2.89e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1031 FAEEYQGL--ANVGTNQSKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQP--NSSSSDYINASYMPGYHLDKAFIAAQGP 1106
Cdd:cd17667      1 FSEDFEEVqrCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPgkDSKHSDYINANYVDGYNKAKAYIATQGP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1107 LPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSScLYGDIVVNIVSEETSPEWTTRKFNVKKT------- 1179
Cdd:cd17667     81 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSE-EYGNIIVTLKSTKIHACYTVRRFSIRNTkvkkgqk 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1180 ----GCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRmmrdylNKNRAGLP-----VVHCSAGVGRTGTLIALDYLLQRI 1250
Cdd:cd17667    160 gnpkGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVR------RSSAARTPemgpvLVHCSAGVGRTGTYIVIDSMLQQI 233

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1822521651 1251 EKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1288
Cdd:cd17667    234 KDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 271
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 1052-1287 3.16e-71

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: 238.19  E-value: 3.16e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1052 VPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTN 1131
Cdd:cd14554      3 LPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTK 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1132 CVEQNRVKCERYWPMDmSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQF- 1210
Cdd:cd14554     83 LREMGREKCHQYWPAE-RSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFi 161

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521651 1211 QRMMRDYLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCIL 1287
Cdd:cd14554    162 GQVHKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRAAL 238
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 1010-1288 3.88e-71

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


Pssm-ID: 350472 [Multi-domain]  Cd Length: 284  Bit Score: 239.63  E-value: 3.88e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1010 PIPVSEYKSYYQRKHADTDIGFAEEYQGLaNVGTNQSKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINAS 1089
Cdd:cd14624      3 PIPILELADHIERLKANDNLKFSQEYESI-DPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINAN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1090 YMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPmDMSSCLYGDIVVNIVSEETSPEW 1169
Cdd:cd14624     82 YIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWP-SRGTETYGLIQVTLLDTVELATY 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1170 TTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDyLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQR 1249
Cdd:cd14624    161 CVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKT-CNPPDAGPMVVHCSAGVGRTGCFIVIDAMLER 239

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1822521651 1250 IEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1288
Cdd:cd14624    240 IKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLE 278
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 1085-1284 6.25e-71

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: 235.88  E-value: 6.25e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1085 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWP-MDMSSCLYGDIVVNIVSE 1163
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPsMEEGSRAFGDVVVKINEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1164 ETSPEWTTRKFNV--KKTGCPEpRTITQFHFTSWPDHGVPKTTDKLLQFQRMMrDYLNKNRAGLPVVHCSAGVGRTGTLI 1241
Cdd:cd14557     81 KICPDYIIRKLNInnKKEKGSG-REVTHIQFTSWPDHGVPEDPHLLLKLRRRV-NAFNNFFSGPIVVHCSAGVGRTGTYI 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1822521651 1242 ALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1284
Cdd:cd14557    159 GIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 1085-1288 1.09e-70

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: 235.20  E-value: 1.09e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1085 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDmsSCLYGDIVVNIVSEE 1164
Cdd:cd14555      1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDD--TEVYGDIKVTLVETE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1165 TSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRdYLNKNRAGLPVVHCSAGVGRTGTLIALD 1244
Cdd:cd14555     79 PLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVK-ASNPPSAGPIVVHCSAGAGRTGCYIVID 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1822521651 1245 YLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1288
Cdd:cd14555    158 IMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 1055-1286 8.60e-69

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: 231.58  E-value: 8.60e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1055 NKVKNRYTNIFPYDVARVKL-DRQPNSSSSDYINASYM-----PGYHLD--KAFIAAQGPLPNTVVDFWRMVWEQKTKVI 1126
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILkDRDPNVPGSDYINANYIrneneGPTTDEnaKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1127 VMLTNCVEQNRVKCERYWPMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEP-RTITQFHFTSWPDHGVPKTTD 1205
Cdd:cd14544     81 VMTTKEVERGKNKCVRYWPDEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDPiREIWHYQYLSWPDHGVPSDPG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1206 KLLQF-QRMMRDYLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAV---VDVYGIVHNMRMSRTCMVQTENQYIF 1281
Cdd:cd14544    161 GVLNFlEDVNQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQRSGMVQTEAQYKF 240


                   ....*
gi 1822521651 1282 LHQCI 1286
Cdd:cd14544    241 IYVAV 245
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 1061-1288 1.30e-68

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


Pssm-ID: 350468 [Multi-domain]  Cd Length: 229  Bit Score: 230.21  E-value: 1.30e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1061 YTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKC 1140
Cdd:cd14620      1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1141 ERYWPmDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKT---GCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDy 1217
Cdd:cd14620     81 YQYWP-DQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQPQlpdGCKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKS- 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1822521651 1218 LNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1288
Cdd:cd14620    159 VNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 1085-1284 2.81e-66

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: 222.89  E-value: 2.81e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1085 YINASYM-PGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCLYGDIVVNIVSE 1163
Cdd:cd18533      1 YINASYItLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEYGDLTVELVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1164 ET--SPEWTTRKFNVKKTGCPePRTITQFHFTSWPDHGVPKTTDKLLQfqrMMR--DYLNKN-RAGLP-VVHCSAGVGRT 1237
Cdd:cd18533     81 EEndDGGFIVREFELSKEDGK-VKKVYHIQYKSWPDFGVPDSPEDLLT---LIKlkRELNDSaSLDPPiIVHCSAGVGRT 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1822521651 1238 GTLIALDYLLQRIEKEAVVD---------VYGIVHNMRMSRTCMVQTENQYIFLHQ 1284
Cdd:cd18533    157 GTFIALDSLLDELKRGLSDSqdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 1071-1288 4.65e-66

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: 222.59  E-value: 4.65e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1071 RVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSs 1150
Cdd:cd14631      1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTE- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1151 cLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRdYLNKNRAGLPVVHC 1230
Cdd:cd14631     80 -VYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVK-LSNPPSAGPIVVHC 157

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521651 1231 SAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1288
Cdd:cd14631    158 SAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 1046-1286 5.75e-66

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


Pssm-ID: 350451 [Multi-domain]  Cd Length: 266  Bit Score: 224.32  E-value: 5.75e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1046 SKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKV 1125
Cdd:cd14603     21 STVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKV 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1126 IVMLTNCVEQNRVKCERYWPMDMSSCLYGDIVVNIVSEE-TSPEWTTRKFNVkkTGCPEPRTITQFHFTSWPDHGVPKTT 1204
Cdd:cd14603    101 ILMACREIEMGKKKCERYWAQEQEPLQTGPFTITLVKEKrLNEEVILRTLKV--TFQKESRSVSHFQYMAWPDHGIPDSP 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1205 DKLLQFQRMMRDYLNKNRAGLpVVHCSAGVGRTGTLIALDY-----LLQRIEKEavVDVYGIVHNMRMSRTCMVQTENQY 1279
Cdd:cd14603    179 DCMLAMIELARRLQGSGPEPL-CVHCSAGCGRTGVICTVDYvrqllLTQRIPPD--FSIFDVVLEMRKQRPAAVQTEEQY 255


                   ....*..
gi 1822521651 1280 IFLHQCI 1286
Cdd:cd14603    256 EFLYHTV 262
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 1054-1289 7.27e-66

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: 222.78  E-value: 7.27e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1054 DNKVKNRYTNIFPYDVARVKLdrqpnSSSSDYINASY--MPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTN 1131
Cdd:cd14597      2 ENRKKNRYKNILPYDTTRVPL-----GDEGGYINASFikMPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQ 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1132 CVEQNRVKCERYWPMDMSSCLYGD--IVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQ 1209
Cdd:cd14597     77 EVEGGKIKCQRYWPEILGKTTMVDnrLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLLT 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1210 FQRMMRdylNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILDV 1289
Cdd:cd14597    157 FISYMR---HIHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVILYV 233
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 1085-1284 7.97e-66

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: 221.32  E-value: 7.97e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1085 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPmDMSSCLYGDIVVNIVSEE 1164
Cdd:cd14551      1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWP-DQGCWTYGNLRVRVEDTV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1165 TSPEWTTRKFNVKK----TGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDyLNKNRAGLPVVHCSAGVGRTGTL 1240
Cdd:cd14551     80 VLVDYTTRKFCIQKvnrgIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKS-ANPPRAGPIVVHCSAGVGRTGTF 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1822521651 1241 IALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1284
Cdd:cd14551    159 IVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 1085-1284 1.11e-65

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: 220.76  E-value: 1.11e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1085 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCL-YGDIVVNIVSE 1163
Cdd:cd14542      1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLqFGPFKISLEKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1164 E-TSPEWTTRKFNVKKTGcpEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYlnKNRAGLPV-VHCSAGVGRTGTLI 1241
Cdd:cd14542     81 KrVGPDFLIRTLKVTFQK--ESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDY--QGSEDVPIcVHCSAGCGRTGTIC 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1822521651 1242 ALDY---LLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1284
Cdd:cd14542    157 AIDYvwnLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 1085-1289 4.58e-65

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


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 219.17  E-value: 4.58e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1085 YINASYM------PGYHldkaFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWP--MDMSSCLYGDI 1156
Cdd:cd14538      1 YINASHIripvggDTYH----YIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPdsLNKPLICGGRL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1157 VVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYlnkNRAGLPVVHCSAGVGR 1236
Cdd:cd14538     77 EVSLEKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRI---HNSGPIVVHCSAGIGR 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1822521651 1237 TGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILDV 1289
Cdd:cd14538    154 TGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEV 206
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 1085-1288 6.24e-65

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: 218.77  E-value: 6.24e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1085 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDmsSCLYGDIVVNIVSEE 1164
Cdd:cd14632      1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDD--SDTYGDIKITLLKTE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1165 TSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKNrAGLPVVHCSAGVGRTGTLIALD 1244
Cdd:cd14632     79 TLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPD-AGPVVVHCSAGAGRTGCYIVLD 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1822521651 1245 YLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1288
Cdd:cd14632    158 VMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 1011-1291 2.12e-62

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: 214.98  E-value: 2.12e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1011 IPVSEYKSYYQR----KHADTDIGFAEEYQGLANVGTNQSKE-AFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDY 1085
Cdd:cd14627      4 VPARNLYSYIQKlaqvEVGEHVTGMELEFKRLANSKAHTSRFiSANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDY 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1086 INASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSScLYGDIVVNIVSEET 1165
Cdd:cd14627     84 INASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPAERSA-RYQYFVVDPMAEYN 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1166 SPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKNRAGLPV-VHCSAGVGRTGTLIALD 1244
Cdd:cd14627    163 MPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPIsVHCSAGVGRTGVFITLS 242

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1822521651 1245 YLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILDVTG 1291
Cdd:cd14627    243 IVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYLG 289
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 1058-1281 4.14e-62

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: 211.87  E-value: 4.14e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1058 KNRYTNIFPYDVARVKLdrqpNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNR 1137
Cdd:cd14545      3 RYRDRDPYDHDRSRVKL----KQGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1138 VKCERYWPMDMSS---CLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMM 1214
Cdd:cd14545     79 IKCAQYWPQGEGNamiFEDTGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQKV 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1822521651 1215 RDY--LNKNrAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAV--VDVYGIVHNMRMSRTCMVQTENQYIF 1281
Cdd:cd14545    159 RESgsLSSD-VGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRF 228
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1084-1289 5.13e-62

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: 210.65  E-value: 5.13e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1084 DYINASY----MPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCLYGDIVVN 1159
Cdd:cd14541      1 DYINANYvnmeIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETMQFGNLQIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1160 IVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRdylnKNRAGL--P-VVHCSAGVGR 1236
Cdd:cd14541     81 CVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVR----QNRVGMvePtVVHCSAGIGR 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1822521651 1237 TGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILDV 1289
Cdd:cd14541    157 TGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRV 209
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 1085-1287 7.52e-62

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: 210.22  E-value: 7.52e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1085 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSScLYGDIVVNIVSEE 1164
Cdd:cd17668      1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSE-EYGNFLVTQKSVQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1165 TSPEWTTRKFNVKKT--------GCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRmMRDYLNKNRAGLPVVHCSAGVGR 1236
Cdd:cd17668     80 VLAYYTVRNFTLRNTkikkgsqkGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVR-KASYAKRHAVGPVVVHCSAGVGR 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1822521651 1237 TGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCIL 1287
Cdd:cd17668    159 TGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 1013-1286 7.74e-62

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: 213.64  E-value: 7.74e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1013 VSEYKSYYQRKHADTDiGFAEEYQGLANVGTNQSKEAF------QVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYI 1086
Cdd:cd14604     10 IERVQAMKSTDHNGED-NFASDFMRLRRLSTKYRTEKIyptatgEKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYI 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1087 NASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCL-YGDIVVNIVSEET 1165
Cdd:cd14604     89 NANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLYGEEPMtFGPFRISCEAEQA 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1166 SPEWTTRKFNVKKTGcpEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYlnKNRAGLPV-VHCSAGVGRTGTLIALD 1244
Cdd:cd14604    169 RTDYFIRTLLLEFQN--ETRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKY--QEHEDVPIcIHCSAGCGRTGAICAID 244

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1822521651 1245 Y---LLQ--RIEKEavVDVYGIVHNMRMSRTCMVQTENQYIFLHQCI 1286
Cdd:cd14604    245 YtwnLLKagKIPEE--FNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 289
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 1011-1291 2.74e-61

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: 211.90  E-value: 2.74e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1011 IPVSEYKSYYQR----KHADTDIGFAEEYQGLANVGTNQSKE-AFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDY 1085
Cdd:cd14628      3 VPARNLYAYIQKltqiETGENVTGMELEFKRLASSKAHTSRFiSANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDY 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1086 INASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSScLYGDIVVNIVSEET 1165
Cdd:cd14628     83 INASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSA-RYQYFVVDPMAEYN 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1166 SPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKNRAGLPV-VHCSAGVGRTGTLIALD 1244
Cdd:cd14628    162 MPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPIsVHCSAGVGRTGVFITLS 241

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1822521651 1245 YLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILDVTG 1291
Cdd:cd14628    242 IVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYLG 288
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 1034-1291 5.50e-61

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: 210.74  E-value: 5.50e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1034 EYQGLANVGTNQSKE-AFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVV 1112
Cdd:cd14629     31 EFKLLANSKAHTSRFiSANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTE 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1113 DFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSScLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHF 1192
Cdd:cd14629    111 DFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSA-RYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQF 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1193 TSWPDHGVPKTTDKLLQF-QRMMRDYLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTC 1271
Cdd:cd14629    190 TDWPEQGVPKTGEGFIDFiGQVHKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPA 269

                          250       260
                   ....*....|....*....|
gi 1822521651 1272 MVQTENQYIFLHQCILDVTG 1291
Cdd:cd14629    270 MVQTEDQYQLCYRAALEYLG 289
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 1020-1281 4.04e-60

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: 207.97  E-value: 4.04e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1020 YQRKHADTDIGFAEEYQGL-ANVGTNQSKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINAS-------YM 1091
Cdd:cd14609      6 YMEDHLRNRDRLAKEWQALcAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASpiiehdpRM 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1092 PgyhldkAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPmDMSSCLYGDIVVNIVSEET-SPEWT 1170
Cdd:cd14609     86 P------AYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWP-DEGSSLYHIYEVNLVSEHIwCEDFL 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1171 TRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLnKNRAGLPVVHCSAGVGRTGTLIALDYLLQRI 1250
Cdd:cd14609    159 VRSFYLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCY-RGRSCPIIVHCSDGAGRTGTYILIDMVLNRM 237

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1822521651 1251 EKEAV-VDVYGIVHNMRMSRTCMVQTENQYIF 1281
Cdd:cd14609    238 AKGVKeIDIAATLEHVRDQRPGMVRTKDQFEF 269
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 1054-1286 8.09e-60

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: 206.02  E-value: 8.09e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1054 DNKVKNRYTNIFPYDVARVKL-DRQPNSSSSDYINASY-MPGYHLD-------KAFIAAQGPLPNTVVDFWRMVWEQKTK 1124
Cdd:cd14605      1 ENKNKNRYKNILPFDHTRVVLhDGDPNEPVSDYINANIiMPEFETKcnnskpkKSYIATQGCLQNTVNDFWRMVFQENSR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1125 VIVMLTNCVEQNRVKCERYWPMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPE-PRTITQFHFTSWPDHGVPKT 1203
Cdd:cd14605     81 VIVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYILRELKLSKVGQGNtERTVWQYHFRTWPDHGVPSD 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1204 TDKLLQF-QRMMRDYLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAV---VDVYGIVHNMRMSRTCMVQTENQY 1279
Cdd:cd14605    161 PGGVLDFlEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQTEAQY 240


                   ....*..
gi 1822521651 1280 IFLHQCI 1286
Cdd:cd14605    241 RFIYMAV 247
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 1085-1283 1.85e-59

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: 203.01  E-value: 1.85e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1085 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSclYGDIVVNIVSEE 1164
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKT--YGDIEVELKDTE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1165 TSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKNRAGLP-----VVHCSAGVGRTGT 1239
Cdd:cd14558     79 KSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNSKHGrsvpiVVHCSDGSSRTGI 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1822521651 1240 LIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLH 1283
Cdd:cd14558    159 FCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 1051-1289 2.05e-59

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: 205.85  E-value: 2.05e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1051 QVPDNKVKNRYTNIFPYDVARVKLDrqpnsSSSDYINASYM----PGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVI 1126
Cdd:cd14600     36 KLPQNMDKNRYKDVLPYDATRVVLQ-----GNEDYINASYVnmeiPSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLI 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1127 VMLTNCVEQNRVKCERYWPMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDK 1206
Cdd:cd14600    111 VMLTTLTERGRTKCHQYWPDPPDVMEYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVPDDSSD 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1207 LLQFQRMMRdylNKNRAGLPV-VHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQC 1285
Cdd:cd14600    191 FLEFVNYVR---SKRVENEPVlVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEA 267


                   ....
gi 1822521651 1286 ILDV 1289
Cdd:cd14600    268 ILRV 271
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 1058-1289 3.86e-58

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: 200.45  E-value: 3.86e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1058 KNRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNR 1137
Cdd:cd14602      1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1138 VKCERYWP-MDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGcpEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRD 1216
Cdd:cd14602     81 KKCERYWAePGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNS--ETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRC 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521651 1217 YlnKNRAGLPV-VHCSAGVGRTGTLIALDYLLqRIEKEAVV----DVYGIVHNMRMSRTCMVQTENQYIFLHQCILDV 1289
Cdd:cd14602    159 Y--QEDDSVPIcIHCSAGCGRTGVICAIDYTW-MLLKDGIIpenfSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIEL 233
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 1043-1287 1.44e-57

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: 200.11  E-value: 1.44e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1043 TNQSKEAfQVPDNKVKNRYTNIFPYDVARVKLD-RQPNSSSSDYINASYMPGYHL-----DKAFIAAQGPLPNTVVDFWR 1116
Cdd:cd14606      7 LHQRLEG-QRPENKSKNRYKNILPFDHSRVILQgRDSNIPGSDYINANYVKNQLLgpdenAKTYIASQGCLEATVNDFWQ 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1117 MVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPE-PRTITQFHFTSW 1195
Cdd:cd14606     86 MAWQENSRVIVMTTREVEKGRNKCVPYWPEVGMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGElIREIWHYQYLSW 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1196 PDHGVPKTTDKLLQFQrmmrDYLNKNRAGLP-----VVHCSAGVGRTGTLIALDYLLQRIEKEAV---VDVYGIVHNMRM 1267
Cdd:cd14606    166 PDHGVPSEPGGVLSFL----DQINQRQESLPhagpiIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRA 241

                          250       260
                   ....*....|....*....|
gi 1822521651 1268 SRTCMVQTENQYIFLHQCIL 1287
Cdd:cd14606    242 QRSGMVQTEAQYKFIYVAIA 261
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 1046-1283 2.04e-56

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: 196.21  E-value: 2.04e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1046 SKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSS-SSDYINASYMPGYH-LDKAFIAAQGPLPNTVVDFWRMVWEQKT 1123
Cdd:cd14612      6 SPEELDIPGHASKDRYKTILPNPQSRVCLRRAGSQEeEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEEC 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1124 KVIVMLTNCVEQNRvKCERYWPMDMSSclYG--DIVVNIVSEetSPEWTTRKFNVKKTGcpEPRTITQFHFTSWPDHGVP 1201
Cdd:cd14612     86 PIIVMITKLKEKKE-KCVHYWPEKEGT--YGrfEIRVQDMKE--CDGYTIRDLTIQLEE--ESRSVKHYWFSSWPDHQTP 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1202 KTTDKLLQFQRMMRDYLNKNRA-GLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYI 1280
Cdd:cd14612    159 ESAGPLLRLVAEVEESRQTAASpGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQ 238


                   ...
gi 1822521651 1281 FLH 1283
Cdd:cd14612    239 FLH 241
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 1085-1286 4.27e-56

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: 193.25  E-value: 4.27e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1085 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDmSSCLYGDIVVNIVSEE 1164
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPED-GSVSSGDITVELKDQT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1165 TSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKNRAGLPVVHCSAGVGRTGTLIALD 1244
Cdd:cd14552     80 DYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSGNHPITVHCSAGAGRTGTFCALS 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1822521651 1245 YLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCI 1286
Cdd:cd14552    160 TVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 1051-1281 9.68e-56

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: 195.66  E-value: 9.68e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1051 QVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINAS-YMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVML 1129
Cdd:cd14610     40 QREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCVVIVML 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1130 TNCVEQNRVKCERYWPmDMSSCLYGDIVVNIVSEET-SPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLL 1208
Cdd:cd14610    120 TPLAENGVKQCYHYWP-DEGSNLYHIYEVNLVSEHIwCEDFLVRSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLL 198

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1822521651 1209 QFQRMMrDYLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAV-VDVYGIVHNMRMSRTCMVQTENQYIF 1281
Cdd:cd14610    199 DFRRKV-NKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMAKGAKeIDIAATLEHLRDQRPGMVQTKEQFEF 271
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 1044-1286 1.46e-54

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: 190.95  E-value: 1.46e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1044 NQSKE-AFQV---PDNKVKNRYTNIFPYDVARVKLDRQPNssssDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVW 1119
Cdd:cd14607      9 NESHDyPHRVakyPENRNRNRYRDVSPYDHSRVKLQNTEN----DYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVW 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1120 EQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCLY---GDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWP 1196
Cdd:cd14607     85 QQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSfkeTGFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYTTWP 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1197 DHGVPKTTDKLLQFQRMMRDYLNKN-RAGLPVVHCSAGVGRTGTLIALDYLLQRIEKE--AVVDVYGIVHNMRMSRTCMV 1273
Cdd:cd14607    165 DFGVPESPASFLNFLFKVRESGSLSpEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKdpDSVDIKQVLLDMRKYRMGLI 244

                          250
                   ....*....|...
gi 1822521651 1274 QTENQYIFLHQCI 1286
Cdd:cd14607    245 QTPDQLRFSYMAV 257
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 1085-1289 2.29e-54

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: 188.42  E-value: 2.29e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1085 YINASY--MPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCL-YGDIVVNIV 1161
Cdd:cd14596      1 YINASYitMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMeLENYQLRLE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1162 SEETSPEWTTRKFNV--KKTGcpEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKnraGLPVVHCSAGVGRTGT 1239
Cdd:cd14596     81 NYQALQYFIIRIIKLveKETG--ENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNT---GPIVVHCSAGIGRAGV 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1240 LIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILDV 1289
Cdd:cd14596    156 LICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEV 205
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 1058-1284 8.56e-54

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: 187.82  E-value: 8.56e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1058 KNRYTNIFPYDVARVKLD-RQPNSSSSDYINASYMPGYH-LDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQ 1135
Cdd:cd14611      2 KNRYKTILPNPHSRVCLKpKNSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1136 NRvKCERYWPMDMSscLYGDIVVNIVSEETSPEWTTRKFNVKKTGcpEPRTITQFHFTSWPDHGVPKTTDKLLQFQ-RMM 1214
Cdd:cd14611     82 NE-KCVLYWPEKRG--IYGKVEVLVNSVKECDNYTIRNLTLKQGS--QSRSVKHYWYTSWPDHKTPDSAQPLLQLMlDVE 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1215 RDYLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1284
Cdd:cd14611    157 EDRLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVHH 226
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 1060-1286 1.12e-53

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: 187.56  E-value: 1.12e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1060 RYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVK 1139
Cdd:cd14623      1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1140 CERYWPMDmSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLN 1219
Cdd:cd14623     81 CAQYWPSD-GSVSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQ 159

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521651 1220 KNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCI 1286
Cdd:cd14623    160 QSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVV 226
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 1031-1297 1.12e-53

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: 189.47  E-value: 1.12e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1031 FAEEYQGLANVGTNQSKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQPNssssDYINASYMPGYHLDKAFIAAQGPLPNT 1110
Cdd:cd14608      1 WAAIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDN----DYINASLIKMEEAQRSYILTQGPLPNT 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1111 VVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCLY---GDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTI 1187
Cdd:cd14608     77 CGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIfedTNLKLTLISEDIKSYYTVRQLELENLTTQETREI 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1188 TQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKN-RAGLPVVHCSAGVGRTGTLIALDYLLQRIEKE---AVVDVYGIVH 1263
Cdd:cd14608    157 LHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSpEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRkdpSSVDIKKVLL 236

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1822521651 1264 NMRMSRTCMVQTENQYIFLHQCILD----VTGDKSIDE 1297
Cdd:cd14608    237 EMRKFRMGLIQTADQLRFSYLAVIEgakfIMGDSSVQD 274
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 1084-1288 5.40e-53

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: 184.44  E-value: 5.40e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1084 DYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDmSSCLYGDIVVNIVSE 1163
Cdd:cd14622      1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSE-GSVTHGEITIEIKND 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1164 ETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKNRAGLPVVHCSAGVGRTGTLIAL 1243
Cdd:cd14622     80 TLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTGNHPIVVHCSAGAGRTGTFIAL 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1822521651 1244 DYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1288
Cdd:cd14622    160 SNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQD 204
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 1084-1289 5.84e-53

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: 184.76  E-value: 5.84e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1084 DYINASYM----PGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCLYGDIVVN 1159
Cdd:cd14601      1 DYINANYInmeiPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSSSYGGFQVT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1160 IVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRdylnKNRAGLP---VVHCSAGVGR 1236
Cdd:cd14601     81 CHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVR----NKRAGKDepvVVHCSAGIGR 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1822521651 1237 TGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILDV 1289
Cdd:cd14601    157 TGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKV 209
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 1085-1286 1.27e-52

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: 183.80  E-value: 1.27e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1085 YINASYMpgYHLD---KAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSClYGDIVVNIV 1161
Cdd:cd14546      1 YINASTI--YDHDprnPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEV-YHIYEVHLV 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1162 SEET-SPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMmrdyLNKNRAGLP---VVHCSAGVGRT 1237
Cdd:cd14546     78 SEHIwCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRK----VNKSYRGRScpiVVHCSDGAGRT 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1238 GTLIALDYLLQRIEKEAV-VDVYGIVHNMRMSRTCMVQTENQYIFLHQCI 1286
Cdd:cd14546    154 GTYILIDMVLNRMAKGAKeIDIAATLEHLRDQRPGMVKTKDQFEFVLTAV 203
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1085-1289 2.91e-51

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: 180.34  E-value: 2.91e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1085 YINASYMPGYHLDKA--FIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCL---YGDIVVN 1159
Cdd:cd14540      1 YINASHITATVGGKQrfYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEHDaltFGEYKVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1160 IVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQF--------QRMMRDYLNKNRAGLPVVHCS 1231
Cdd:cd14540     81 TKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFleeinsvrRHTNQDVAGHNRNPPTLVHCS 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521651 1232 AGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILDV 1289
Cdd:cd14540    161 AGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQY 218
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 1085-1284 1.04e-50

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: 177.96  E-value: 1.04e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1085 YINASYMPGY-HLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCL-YGDIVVNIVS 1162
Cdd:cd14539      1 YINASLIEDLtPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALvYGAITVSLQS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1163 EETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKNRA-GLP-VVHCSAGVGRTGTL 1240
Cdd:cd14539     81 VRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQRSlQTPiVVHCSSGVGRTGAF 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1822521651 1241 IALDYLLQRIEKE-AVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1284
Cdd:cd14539    161 CLLYAAVQEIEAGnGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 1047-1283 4.44e-50

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: 178.13  E-value: 4.44e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1047 KEAFQVPDNKV------------KNRYTNIFPYDVARVKL-DRQPNSSSSDYINASYMPGY-HLDKAFIAAQGPLPNTVV 1112
Cdd:cd14613      5 AEFFEIPMNFVdpkeydipglvrKNRYKTILPNPHSRVCLtSPDQDDPLSSYINANYIRGYgGEEKVYIATQGPTVNTVG 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1113 DFWRMVWEQKTKVIVMLTNCVEQNRvKCERYWPMDmsSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGcpEPRTITQFHF 1192
Cdd:cd14613     85 DFWRMVWQERSPIIVMITNIEEMNE-KCTEYWPEE--QVTYEGIEITVKQVIHADDYRLRLITLKSGG--EERGLKHYWY 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1193 TSWPDHGVPKTTDKLLQFQRMMRDYLNKNRA--GLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRT 1270
Cdd:cd14613    160 TSWPDQKTPDNAPPLLQLVQEVEEARQQAEPncGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRG 239

                          250
                   ....*....|...
gi 1822521651 1271 CMVQTENQYIFLH 1283
Cdd:cd14613    240 GMIQTCEQYQFVH 252
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 1085-1284 1.02e-44

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: 160.65  E-value: 1.02e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1085 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLtNCVEQNRVKCERYWPMDMSSClYGDIVVNIVSEE 1164
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVML-NQLDPKDQSCPQYWPDEGSGT-YGPIQVEFVSTT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1165 TSPEWTTRKFNVKKTGCPEP--RTITQFHFTSWPDHG-VPKTTDKLLQFQRMMRDYLNKNRAGLPVVHCSAGVGRTGTLI 1241
Cdd:cd14556     79 IDEDVISRIFRLQNTTRPQEgyRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQEQSGEGPIVVHCLNGVGRSGVFC 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1822521651 1242 ALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1284
Cdd:cd14556    159 AISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
1043-1282 3.37e-43

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 159.10  E-value: 3.37e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1043 TNQSKEAFQVPDNKVKNRYTNIFPYDVARVkldrqpnSSSSDYINASY--MPGYHLdkaFIAAQGPLPNTVVDFWRMVWE 1120
Cdd:COG5599     30 SHNDPQYLQNINGSPLNRFRDIQPYKETAL-------RANLGYLNANYiqVIGNHR---YIATQYPLEEQLEDFFQMLFD 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1121 QKTKVIVMLTNCVE--QNRVKCERYWPMDMSsclYGDIVVNIVSEET---SPEWTTRKFNVKKTGC-PEPRTITQFHFTS 1194
Cdd:COG5599    100 NNTPVLVVLASDDEisKPKVKMPVYFRQDGE---YGKYEVSSELTESiqlRDGIEARTYVLTIKGTgQKKIEIPVLHVKN 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1195 WPDHGVPkTTDKLLQFQRMMRDYLNKNRA--GLPVVHCSAGVGRTGTLIALDYLLQRI--EKEAVVDVYGIVHNMRMSRT 1270
Cdd:COG5599    177 WPDHGAI-SAEALKNLADLIDKKEKIKDPdkLLPVVHCRAGVGRTGTLIACLALSKSInaLVQITLSVEEIVIDMRTSRN 255

                          250
                   ....*....|...
gi 1822521651 1271 C-MVQTENQYIFL 1282
Cdd:COG5599    256 GgMVQTSEQLDVL 268
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 1052-1287 1.49e-42

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: 157.47  E-value: 1.49e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1052 VPDNKVKNRYTNIFPYDVARVKLdrQPN-SSSSDYINASYMP------GYHldkaFIAAQGPLPNTVVDFWRMVWEQKTK 1124
Cdd:cd14599     35 LPENAERNRIREVVPYEENRVEL--VPTkENNTGYINASHIKvtvggeEWH----YIATQGPLPHTCHDFWQMVWEQGVN 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1125 VIVMLTNCVEQNRVKCERYWP---MDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVP 1201
Cdd:cd14599    109 VIAMVTAEEEGGRSKSHRYWPklgSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPDHGCP 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1202 KTTDKLLQFQ---RMMRDYLN------KNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCM 1272
Cdd:cd14599    189 EEVQGFLSYLeeiQSVRRHTNsmldstKNCNPPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRHLREQRMFM 268

                          250
                   ....*....|....*
gi 1822521651 1273 VQTENQYIFLHQCIL 1287
Cdd:cd14599    269 IQTIAQYKFVYQVLI 283
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 1085-1281 1.60e-42

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: 154.54  E-value: 1.60e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1085 YINASYM--PGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNR-VKCERYWPM-DMSSCLYGDIVVNI 1160
Cdd:cd17658      1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStAKCADYFPAeENESREFGRISVTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1161 VSEETSPE-WTTRKFNVKKTGCPE-PRTITQFHFTSWPDHGVPKTTDKLLQFQRmmRDYLNKNRAGLPVVHCSAGVGRTG 1238
Cdd:cd17658     81 KKLKHSQHsITLRVLEVQYIESEEpPLSVLHIQYPEWPDHGVPKDTRSVRELLK--RLYGIPPSAGPIVVHCSAGIGRTG 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1822521651 1239 TLIALDYLLQRIEKEAV--VDVYGIVHNMRMSRTCMVQTENQYIF 1281
Cdd:cd17658    159 AYCTIHNTIRRILEGDMsaVDLSKTVRKFRSQRIGMVQTQDQYIF 203
PHA02738 PHA02738
hypothetical protein; Provisional
 1055-1311 9.08e-42

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 156.24  E-value: 9.08e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1055 NKVKNRYTNIFPYDVARVKLDRQPNSSssDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVE 1134
Cdd:PHA02738    49 NRKLNRYLDAVCFDHSRVILPAERNRG--DYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKE 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1135 QNRVKCERYWP-MDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKtGCPEPRTITQFHFTSWPDHGVPKTTDKLLQF--- 1210
Cdd:PHA02738   127 NGREKCFPYWSdVEQGSIRFGKFKITTTQVETHPHYVKSTLLLTD-GTSATQTVTHFNFTAWPDHDVPKNTSEFLNFvle 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1211 ----QRMM---RDYLNKNRAGLP--VVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIF 1281
Cdd:PHA02738   206 vrqcQKELaqeSLQIGHNRLQPPpiVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFF 285

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1822521651 1282 LHQCI---LDVTGDKSIDEPIYENQADLIYENV 1311
Cdd:PHA02738   286 CYRAVkryVNLTVNKVSKKLIPNVQTVSFNKNL 318
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1034-1318 4.74e-41

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 154.00  E-value: 4.74e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1034 EYQGLANVGTNQSKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQpNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVD 1113
Cdd:PHA02747    30 EHHQIILKPFDGLIANFEKPENQPKNRYWDIPCWDHNRVILDSG-GGSTSDYIHANWIDGFEDDKKFIATQGPFAETCAD 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1114 FWRMVWEQKTKVIVMLTNCVEQN-RVKCERYW-PMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFH 1191
Cdd:PHA02747   109 FWKAVWQEHCSIIVMLTPTKGTNgEEKCYQYWcLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKISHFQ 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1192 FTSWPDHGVPKTTDKLLQF--------QRMMRDYLNKNRAGLP-VVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIV 1262
Cdd:PHA02747   189 CSEWFEDETPSDHPDFIKFikiidinrKKSGKLFNPKDALLCPiVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTA 268

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1822521651 1263 HNMRMSRTCMVQTENQYIFLhqcildvtgdksidEPIYENQADLIYENVDAIKVAN 1318
Cdd:PHA02747   269 EKIREQRHAGIMNFDDYLFI--------------QPGYEVLHYFLSKIKAIDKIKF 310
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1186-1288 3.02e-40

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 144.04  E-value: 3.02e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  1186 TITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKNRAGLP-VVHCSAGVGRTGTLIALDYLLQRIEKEA-VVDVYGIVH 1263
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPvVVHCSAGVGRTGTFVAIDILLQQLEAEAgEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 1822521651  1264 NMRMSRTCMVQTENQYIFLHQCILD 1288
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1186-1288 3.02e-40

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: 144.04  E-value: 3.02e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  1186 TITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKNRAGLP-VVHCSAGVGRTGTLIALDYLLQRIEKEA-VVDVYGIVH 1263
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPvVVHCSAGVGRTGTFVAIDILLQQLEAEAgEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 1822521651  1264 NMRMSRTCMVQTENQYIFLHQCILD 1288
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 1055-1287 1.02e-37

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 143.99  E-value: 1.02e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1055 NKVKNRYTNIFPYDVARVKLDRQpnSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVE 1134
Cdd:PHA02742    52 NMKKCRYPDAPCFDRNRVILKIE--DGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIME 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1135 QNRVKCERYW-PMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRM 1213
Cdd:PHA02742   130 DGKEACYPYWmPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFVLA 209

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1214 MR--------DYLNKNRAGLP--VVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLH 1283
Cdd:PHA02742   210 VReadlkadvDIKGENIVKEPpiLVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCY 289


                   ....
gi 1822521651 1284 QCIL 1287
Cdd:PHA02742   290 FIVL 293
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 1085-1288 1.78e-36

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: 137.07  E-value: 1.78e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1085 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTncvEQNRVK-CERYWPmDMSSCLYGDIVVNIVSE 1163
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLN---EMDAAQlCMQYWP-EKTSCCYGPIQVEFVSA 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1164 ETSPEWTTRKFNVKKTGCPEP--RTITQFHFTSWPDH-GVPKTTDKLLQFQRMMRDYLNK--NRAGLPVVHCSAGVGRTG 1238
Cdd:cd14634     77 DIDEDIISRIFRICNMARPQDgyRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQydGREGRTVVHCLNGGGRSG 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1239 TLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1288
Cdd:cd14634    157 TFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 1085-1287 4.49e-35

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: 133.56  E-value: 4.49e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1085 YINASYMP----GYHLDkaFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMS---SCLYGDIV 1157
Cdd:cd14598      1 YINASHIKvtvgGKEWD--YIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSrhnTVTYGRFK 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1158 VNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQF-------QRMMRDYLNKNRAGLPV-VH 1229
Cdd:cd14598     79 ITTRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYleeiqsvRRHTNSTIDPKSPNPPVlVH 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521651 1230 CSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCIL 1287
Cdd:cd14598    159 CSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLI 216
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 1053-1286 2.89e-34

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 134.77  E-value: 2.89e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1053 PDNKVKNRYTNIFPYDVARVKL------------DRQPN-------SSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVD 1113
Cdd:PHA02746    49 KENLKKNRFHDIPCWDHSRVVInaheslkmfdvgDSDGKkievtseDNAENYIHANFVDGFKEANKFICAQGPKEDTSED 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1114 FWRMVWEQKTKVIVMLTNcVEQNRVKCERYWPMDMSSCL-YGDIVVNI--VSEETSpeWTTRKFNVKKTGCPEPRTITQF 1190
Cdd:PHA02746   129 FFKLISEHESQVIVSLTD-IDDDDEKCFELWTKEEDSELaFGRFVAKIldIIEELS--FTKTRLMITDKISDTSREIHHF 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1191 HFTSWPDHGVPKTTDKLLQF--------QRMMRDYLNKNRAGLP-VVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGI 1261
Cdd:PHA02746   206 WFPDWPDNGIPTGMAEFLELinkvneeqAELIKQADNDPQTLGPiVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEI 285

                          250       260
                   ....*....|....*....|....*
gi 1822521651 1262 VHNMRMSRTCMVQTENQYIFLHQCI 1286
Cdd:PHA02746   286 VLKIRKQRHSSVFLPEQYAFCYKAL 310
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 1085-1288 2.32e-28

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: 113.85  E-value: 2.32e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1085 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRV-KCERYWPmDMSSCLYGDIVVNIVSE 1163
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWP-EPGLQQYGPMEVEFVSG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1164 ETSPEWTTRKFNVKKTG--CPEPRTITQFHFTSW-PDHGVPKTTDKLLQFQRMMRDYLNKNRAGLPVVHCSAGVGRTGTL 1240
Cdd:cd14637     80 SADEDIVTRLFRVQNITrlQEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQRESGEGRTVVHCLNGGGRSGTY 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1822521651 1241 IALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1288
Cdd:cd14637    160 CASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 1085-1288 6.27e-28

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: 112.47  E-value: 6.27e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1085 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLtNCVEQNRVkCERYWPmDMSSCLYGDIVVNIVSEE 1164
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVML-NDVDPAQL-CPQYWP-ENGVHRHGPIQVEFVSAD 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1165 TSPEWTTRKFNVKKTGCPEP--RTITQFHFTSWPDH-GVPKTTDKLLQFQRMMRDYLNKNRA--GLPVVHCSAGVGRTGT 1239
Cdd:cd14635     78 LEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEYNGgeGRTVVHCLNGGGRSGT 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1822521651 1240 LIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1288
Cdd:cd14635    158 FCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 1085-1284 8.79e-28

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: 112.03  E-value: 8.79e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1085 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCveQNRVKCERYWPMDMSSCLYGDIVVNIVSEE 1164
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDN--ELNEDEPIYWPTKEKPLECETFKVTLSGED 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1165 TSPEW-----TTRKFNVKKTGCPEPRTITQFHFTSWPDHGVP-KTTDKLLQ-FQRmmrdyLNKNRAGLPVVHCSAGVGRT 1237
Cdd:cd14550     79 HSCLSneirlIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPiHTVFELINtVQE-----WAQQRDGPIVVHDRYGGVQA 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1822521651 1238 GTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1284
Cdd:cd14550    154 ATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 1085-1288 2.39e-26

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


Pssm-ID: 350484 [Multi-domain]  Cd Length: 206  Bit Score: 108.19  E-value: 2.39e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1085 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTncvEQNRVK-CERYWPmDMSSCLYGDIVVNIVSE 1163
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLN---EVDLAQgCPQYWP-EEGMLRYGPIQVECMSC 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1164 ETSPEWTTRKFNVKKTGCPEP--RTITQFHFTSWPDH-GVPKTTDKLLQFQRMMRDYLNK--NRAGLPVVHCSAGVGRTG 1238
Cdd:cd14636     77 SMDCDVISRIFRICNLTRPQEgyLMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEEcdEGEGRTIIHCLNGGGRSG 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1239 TLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1288
Cdd:cd14636    157 MFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 1085-1287 7.84e-24

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: 100.84  E-value: 7.84e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1085 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNcvEQNRVKCE-RYWPMDMSSCLYGDIVVNIVSE 1163
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPD--GQNMAEDEfVYWPNKDEPINCETFKVTLIAE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1164 E-----TSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPktTDKLLQFQRMMRDYlNKNRAGLPVVHCSAGVGRTG 1238
Cdd:cd17669     79 EhkclsNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSP--ISKTFELISIIKEE-AANRDGPMIVHDEHGGVTAG 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1822521651 1239 TLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCIL 1287
Cdd:cd17669    156 TFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 1085-1287 1.16e-23

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: 100.14  E-value: 1.16e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1085 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNcvEQNRVKCER-YWPMDMSSCLYGDIVVNIVSE 1163
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD--NQGLAEDEFvYWPSREESMNCEAFTVTLISK 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1164 E-----TSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTD----KLLQFQRMMRDylnknraGLPVVHCSAGV 1234
Cdd:cd17670     79 DrlclsNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTfeliNVIKEEALTRD-------GPTIVHDEFGA 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1822521651 1235 GRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCIL 1287
Cdd:cd17670    152 VSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 1059-1279 8.67e-20

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


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 89.77  E-value: 8.67e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1059 NRYTNIfpydVARVKLDRQPNssssdyINASYMP--GYHLdkaFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQN 1136
Cdd:cd14559      1 NRFTNI----QTRVSTPVGKN------LNANRVQigNKNV---AIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQ 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1137 RVKCERYWPMdmsSCLYGDIVVNivSEETSPEWTTRKFNVK----KTGCPEPR-TITQFHFTSWPDHG------------ 1199
Cdd:cd14559     68 RKGLPPYFRQ---SGTYGSVTVK--SKKTGKDELVDGLKADmynlKITDGNKTiTIPVVHVTNWPDHTaisseglkelad 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1200 -VPKTTDKLLQF--QRMMRDYLNKNRaGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDvygIVHNMRMSRTC-MVQT 1275
Cdd:cd14559    143 lVNKSAEEKRNFykSKGSSAINDKNK-LLPVIHCRAGVGRTGQLAAAMELNKSPNNLSVED---IVSDMRTSRNGkMVQK 218


                   ....
gi 1822521651 1276 ENQY 1279
Cdd:cd14559    219 DEQL 222
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
357-845 3.68e-17

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 86.98  E-value: 3.68e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  357 SSTTVTSRGETTFKATGLQPGDQYLLSVQSVTPEDTWSTPVEVTNTTNPSPVTGLTVVNGTTHSLRIEWTPPTDTRATNY 436
Cdd:COG3401      1 TGSSYLTSLDAGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  437 TYKVTVTNVAGGVSSTTITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPVTGLSVVNGTTESLTI 516
Cdd:COG3401     81 AVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  517 EWTSPNDTRASNYIYNVTVTNVTGGVSWTQSTSKDETtftatRLQPGDQYQLSVQSVTP--EDTLSTPVEVT-STTNPSP 593
Cdd:COG3401    161 SSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGG-----DIEPGTTYYYRVAATDTggESAPSNEVSVTtPTTPPSA 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  594 VTGLSVVNGTTQSLTIEWTRPTDTRASNYT-YRVTvtnvTGGVSWSKSTSKGETTFTATGLQPGDQYQLSVQSVTPEDTL 672
Cdd:COG3401    236 PTGLTATADTPGSVTLSWDPVTESDATGYRvYRSN----SGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNE 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  673 STPVEVKSTT----DPSPVTGLSVVNSTTQSLRIEWTTPNNIRASNYtyNVTVTNVTDGASSTTITSKGETTFTVTGLQP 748
Cdd:COG3401    312 SAPSNVVSVTtdltPPAAPSGLTATAVGSSSITLSWTASSDADVTGY--NVYRSTSGGGTYTKIAETVTTTSYTDTGLTP 389

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  749 GDQYRLSVRSVT---PEDTWSTPAQVTSTSNPSPVSGLTVVNRTTVSIEVTWAAPTDARAPEYTYRITLANVTRRGRGAI 825
Cdd:COG3401    390 GTTYYYKVTAVDaagNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVP 469

                          490       500
                   ....*....|....*....|
gi 1822521651  826 DTGPGVTTFTVTNLVPGVEY 845
Cdd:COG3401    470 FTTTSSTVTATTTDTTTANL 489
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
293-857 6.75e-17

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 85.82  E-value: 6.75e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  293 SVTPEDTVSSPLEVTNTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRATNYTYIVTVTNVTGGVSSTTVTSRGETTFKAT 372
Cdd:COG3401     30 GGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNT 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  373 GLQPGDQYL-LSVQSVTPEDTWSTPVEVTNTTNPSPVTGLTVVNGTTHSLRIEWTPPTDTRATNYTYKVTVTNVAGGVSS 451
Cdd:COG3401    110 GLTSSDEVPsPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTS 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  452 TTITNKGETAFTATGLQpgdqYQLSVQSVTPEDTLSTPVEVT-STTNPSPVTGLSVVNGTTESLTIEWTSPNDTRASNYi 530
Cdd:COG3401    190 TTLVDGGGDIEPGTTYY----YRVAATDTGGESAPSNEVSVTtPTTPPSAPTGLTATADTPGSVTLSWDPVTESDATGY- 264

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  531 yNVTVTNVTGGvSWTQSTSKDETTFTATRLQPGDQYQLSVQSVTPEDTLSTPVEV----TSTTNPSPVTGLSVVNGTTQS 606
Cdd:COG3401    265 -RVYRSNSGDG-PFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNESAPSNVvsvtTDLTPPAAPSGLTATAVGSSS 342

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  607 LTIEWTRPTDTRASNYT-YRVTvtnvTGGVSWSK-STSKGETTFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVKSTTDP 684
Cdd:COG3401    343 ITLSWTASSDADVTGYNvYRST----SGGGTYTKiAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTA 418

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  685 SPVTGLSVVNSTTqSLRIEWTTPNNIRASNYTYNVTVTNVTDGASSTTITSKGETTFTVTGLQPGDQYRlSVRSVTPEDT 764
Cdd:COG3401    419 SAASGESLTASVD-AVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTT-ANLSVTTGSL 496

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  765 WSTPAQVTSTSNPSPVSGLTVVNRTTVSIEVTWAAPTDARAPEYTYRITLANVTRRGRGAIDTGPGVTTFTVTNLVPGVE 844
Cdd:COG3401    497 VGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITT 576

                          570
                   ....*....|...
gi 1822521651  845 YELRLQSVTPAGT 857
Cdd:COG3401    577 LGGSLLTTTSTNT 589
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
181-740 1.92e-16

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 84.67  E-value: 1.92e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  181 TTFTATGLQPGDQYQLSVRSVTPEDTLSTPVEVTNTTNPSPVTGLSVVNGTTESLRIKWTRPTDTR-ASDYTYRVTVTNV 259
Cdd:COG3401      4 SYLTSLDAGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTgGRAGTTSGVAAVA 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  260 TGGVSWTESTSKDKTTFTATGLQPGDQYQLSVQSVTPEDTVSSPLEVTNTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTR 339
Cdd:COG3401     84 VAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSV 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  340 ATNYTYIVTVTNVTGGVSSTTVTSRGETTFKATG-LQPGDQYLLSVQSVTP--EDTWSTPVEVT-NTTNPSPVTGLTVVN 415
Cdd:COG3401    164 AGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGdIEPGTTYYYRVAATDTggESAPSNEVSVTtPTTPPSAPTGLTATA 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  416 GTTHSLRIEWTPPTDTRATNYTYKVTVTnvaGGVSSTTITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEV--- 492
Cdd:COG3401    244 DTPGSVTLSWDPVTESDATGYRVYRSNS---GDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNESAPSNVvsv 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  493 -TSTTNPSPVTGLSVVNGTTESLTIEWTSPNDTRASNyiYNVTVTNVTGGVSWTQSTSKDETTFTATRLQPGDQYQLSVQ 571
Cdd:COG3401    321 tTDLTPPAAPSGLTATAVGSSSITLSWTASSDADVTG--YNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVT 398

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  572 SVT---PEDTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTR-------PTDTRASNYTYRVTVTNVTGGVSWSKST 641
Cdd:COG3401    399 AVDaagNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAaasaasnPGVSAAVLADGGDTGNAVPFTTTSSTVT 478

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  642 SKGETTFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVKSTTDPSPVTGLSVVNSTTQSLRIEWTTPNNIRASNYTYNVTV 721
Cdd:COG3401    479 ATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSAS 558

                          570
                   ....*....|....*....
gi 1822521651  722 TNVTDGASSTTITSKGETT 740
Cdd:COG3401    559 SSVSGAGLGSGNLYLITTL 577
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
34-558 1.04e-14

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 78.89  E-value: 1.04e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651   34 SPVTGLSVVSRTTDSLRIEWTSPNDTRASNYTYNVTVTNVAGGVSSITTTGKNETTFTATGLQPGDQYLLSVRSVTPEDT 113
Cdd:COG3401     82 VAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTAS 161

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  114 LSTPVEVTSTTNPSPVIGLSVVNGTTQSLWIEWTSPTDTRATNYTYIVTVTNVTGgvswtkstnkdkttftatglqpgdq 193
Cdd:COG3401    162 SVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGG------------------------- 216

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  194 yqlsvrsvtpEDTLSTPVEVT-NTTNPSPVTGLSVVNGTTESLRIKWTRPTDTRASDYT-YRVTvtnvTGGVSWTESTSK 271
Cdd:COG3401    217 ----------ESAPSNEVSVTtPTTPPSAPTGLTATADTPGSVTLSWDPVTESDATGYRvYRSN----SGDGPFTKVATV 282

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  272 DKTTFTATGLQPGDQYQLSVQSVTPEDTVSSPLEV----TNTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRATNytYIV 347
Cdd:COG3401    283 TTTSYTDTGLTNGTTYYYRVTAVDAAGNESAPSNVvsvtTDLTPPAAPSGLTATAVGSSSITLSWTASSDADVTG--YNV 360

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  348 TVTNVTGGVSSTTVTSRGETTFKATGLQPGDQYLLSVQSVT---PEDTWSTPVEVTNTTNPSPVTGLTVVNGTTHSLRIE 424
Cdd:COG3401    361 YRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDaagNESAPSEEVSATTASAASGESLTASVDAVPLTDVAG 440

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  425 WT-------PPTDTRATNYTYKVTVTNVAGGVSSTTITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTN 497
Cdd:COG3401    441 ATaaasaasNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAV 520

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1822521651  498 PSPVTGLSVVNGTTE--------SLTIEWTSPNDTRASNYIYNVTVTNVTGGVSWTQSTSKDETTFTAT 558
Cdd:COG3401    521 GGAPDGTPNVTGASPvtvgastgDVLITDLVSLTTSASSSVSGAGLGSGNLYLITTLGGSLLTTTSTNT 589
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
59-651 1.84e-14

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 78.12  E-value: 1.84e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651   59 TRASNYTYNVTVTNVAGGVSSITTTGKNETTFTATGLQPGDQYLLSVRSVTPEDTLSTPVEVTSTTNPSPVIGLSVVNGT 138
Cdd:COG3401     12 GIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAAAPPTA 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  139 TQSLWIEWTSPTDTRATNYTYIVTVTNVTGGVSWTKSTNKDKTTFTATGLQPGDQYQLSVRSVTPEDTLSTPVEVTNTTN 218
Cdd:COG3401     92 TGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVS 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  219 PSPVTGLSVVNGTTESLRI--KWTRPTDTRASDYTYRVTVTNVTGGVSWTESTSKdkttftatglqpgdqyqlsvqsvtp 296
Cdd:COG3401    172 PDTSATAAVATTSLTVTSTtlVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSV------------------------- 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  297 edtvsspleVTNTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRATNytYIVTVTNVTGGvSSTTVTSRGETTFKATGLQP 376
Cdd:COG3401    227 ---------TTPTTPPSAPTGLTATADTPGSVTLSWDPVTESDATG--YRVYRSNSGDG-PFTKVATVTTTSYTDTGLTN 294

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  377 GDQYLLSVQSVTPEDTWSTPVEV----TNTTNPSPVTGLTVVNGTTHSLRIEWTPPTDTRATNytYKVTVTNVAGGVSST 452
Cdd:COG3401    295 GTTYYYRVTAVDAAGNESAPSNVvsvtTDLTPPAAPSGLTATAVGSSSITLSWTASSDADVTG--YNVYRSTSGGGTYTK 372

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  453 TITNKGETAFTATGLQPGDQYQLSVQSVT---PEDTLSTPVEVTSTTNPSPVTGLSVVNGTTESLTIEWT-------SPN 522
Cdd:COG3401    373 IAETVTTTSYTDTGLTPGTTYYYKVTAVDaagNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATaaasaasNPG 452

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  523 DTRASNYIYNVTVTNVTGGVSWTQSTSKDETTFTATRLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPVTGLSV--- 599
Cdd:COG3401    453 VSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNvtg 532

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521651  600 -----VNGTTQSLTIEWTRPTDTRASNYTYRVTVTNVTGGVSWSKSTSKGETTFTAT 651
Cdd:COG3401    533 aspvtVGASTGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITTLGGSLLTTTSTNT 589
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
27-363 1.76e-11

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 68.49  E-value: 1.76e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651   27 SQNVTDPSPVTGLSVVSRTTDSLRIEWTSPNDTRASNYTYNVTvTNVAGGVSSITTTgkNETTFTATGLQPGDQYLLSVR 106
Cdd:COG3401    227 TTPTTPPSAPTGLTATADTPGSVTLSWDPVTESDATGYRVYRS-NSGDGPFTKVATV--TTTSYTDTGLTNGTTYYYRVT 303

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  107 SVTPEDTLSTPVEV----TSTTNPSPVIGLSVVNGTTQSLWIEWTSPTDTRATNYtYIVTVTNVTGGVSWTKSTNKDkTT 182
Cdd:COG3401    304 AVDAAGNESAPSNVvsvtTDLTPPAAPSGLTATAVGSSSITLSWTASSDADVTGY-NVYRSTSGGGTYTKIAETVTT-TS 381

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  183 FTATGLQPGDQYQLSVRSVT---PEDTLSTPVEVTNTTNPSPVTGLSVVNGTTESLRIKWTRPT----DTRASDYTYRVT 255
Cdd:COG3401    382 YTDTGLTPGTTYYYKVTAVDaagNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAAsaasNPGVSAAVLADG 461

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  256 VTNVTGGVSWTESTSKDKTT---------FTATGLQPGDQYQLSVQSVTPEDTVSSPLEVTNTTNPSPVTGLSVVNGT-- 324
Cdd:COG3401    462 GDTGNAVPFTTTSSTVTATTtdtttanlsVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGas 541

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1822521651  325 TQSLTIEWTRPTDTRATNYTYIVTVTNVTGGVSSTTVTS 363
Cdd:COG3401    542 TGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITTLGGS 580
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
275-764 7.04e-11

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 66.89  E-value: 7.04e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  275 TFTATGLQPGDQYQLSVQSVTPEDTVSSPLEVTNTTNPSpvtgLSVVNGTT--QSLTIEWTRPTDtrATNYTYIVTVtnv 352
Cdd:COG4733    503 TYTITAVQHAPEKYAAIDAGAFDDVPPQWPPVNVTTSES----LSVVAQGTavTTLTVSWDAPAG--AVAYEVEWRR--- 573

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  353 tGGVSSTTVTSRGETTFKATGLQPGDqYLLSVQSVTPEDT---WSTPVEVT---NTTNPSPVTGLTVVNGTTHsLRIEWT 426
Cdd:COG4733    574 -DDGNWVSVPRTSGTSFEVPGIYAGD-YEVRVRAINALGVssaWAASSETTvtgKTAPPPAPTGLTATGGLGG-ITLSWS 650

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  427 PPTDTRATnyTYKVTVTNVAGGVSSTTITNKGET-AFTATGLQPGDQYQLSVQSVtpeDTL--STPVEVTSTTNPSPVTG 503
Cdd:COG4733    651 FPVDADTL--RTEIRYSTTGDWASATVAQALYPGnTYTLAGLKAGQTYYYRARAV---DRSgnVSAWWVSGQASADAAGI 725

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  504 LSVVNGttESLTIEWTSPNDTRASNYIYNVTVTNVTGGVSWTQSTSKDETTFTATrlqpgdqyqlSVQSVTPEDTLSTPV 583
Cdd:COG4733    726 LDAITG--QILETELGQELDAIIQNATVAEVVAATVTDVTAQIDTAVLFAGVATA----------AAIGAEARVAATVAE 793

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  584 EVTSTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYRVTVTNVTGGVSWskSTSKGETTFTATGLQPGDQYQLSV 663
Cdd:COG4733    794 SATAAAATGTAADAAGDASGGVTAGTSGTTGAGDTAASTTRVAAAVVLAGVVVY--GDAIIESGNTGDIVATGDIASAAA 871

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  664 QSVTPEDTLSTPVEVKSTTDPSpVTGLSVVNSTTQSLRIEWTTPNNIRASNYTYNVTVTNVTDGASSTTITSKGETTFTV 743
Cdd:COG4733    872 GAVATTVSGTTAADVSAVADST-AASLTAIVIAATTIIDAIGDGTTREPAGDIGASGGAQGFAVTIVGSFDGAGAVATVD 950

                          490       500
                   ....*....|....*....|.
gi 1822521651  744 TGLQPGDQYRLSVRSVTPEDT 764
Cdd:COG4733    951 AGQSVVDGVGTAVEAANGTET 971
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
30-501 7.52e-10

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 63.48  E-value: 7.52e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651   30 VTDPSPVTGLSVVSRTTDSLRIEWTSPNDTRASNYTYNVTVTNVAGGVSSITTTGKNETTFTATGLQPGDQYLLSVRSVT 109
Cdd:COG3401    149 GVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTT 228

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  110 PEDTLSTPVEVTSTTNPSPVIGLSvvngttqslwieWTSPTDTRATNytYIVTVTNVTGGvSWTKSTNKDKTTFTATGLQ 189
Cdd:COG3401    229 PTTPPSAPTGLTATADTPGSVTLS------------WDPVTESDATG--YRVYRSNSGDG-PFTKVATVTTTSYTDTGLT 293

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  190 PGDQYQLSVRSVTPEDTLSTPVEV----TNTTNPSPVTGLSVVNGTTESLRIKWTRPTDTRASdyTYRVTVTNVTGGVSW 265
Cdd:COG3401    294 NGTTYYYRVTAVDAAGNESAPSNVvsvtTDLTPPAAPSGLTATAVGSSSITLSWTASSDADVT--GYNVYRSTSGGGTYT 371

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  266 TESTSKDKTTFTATGLQPGDQYQLSVQSVTPEDTVSSPLEVTNTTNPSPVTGLSVVNGTTqsltiEWTRPTDTRATNYTY 345
Cdd:COG3401    372 KIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVD-----AVPLTDVAGATAAAS 446

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  346 IVTVTNVTGGVSSTTVTSRGETTFKATGLQPGDQYLLSVQSVTPEDTWSTPVEVTNTTNPSPVTGLTVVNGTTHSLRIEW 425
Cdd:COG3401    447 AASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDG 526

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1822521651  426 TPPTDTRATNYTYKVTVTNVAGGVSSTTITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPV 501
Cdd:COG3401    527 TPNVTGASPVTVGASTGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITTLGGSLLTTTSTNTNDVAGVHGGTLLV 602
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 1033-1286 1.91e-09

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 60.37  E-value: 1.91e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1033 EEYQGLANVGTNQSKEAFQVPDNKVK--NRYTNIFPYDVARVKLdrqpnSSSSDYINASYMPGYHLDKAFIAAQGPLPNT 1110
Cdd:PHA02740    29 KEYRAIVPEHEDEANKACAQAENKAKdeNLALHITRLLHRRIKL-----FNDEKVLDARFVDGYDFEQKFICIINLCEDA 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1111 VVDFWRMVWEQKTKVIVMLTNCVEQNRVkcERYWPMDmSSCLygdIVVNIVSEETSPEWTTRKFNVK------KTGcpEP 1184
Cdd:PHA02740   104 CDKFLQALSDNKVQIIVLISRHADKKCF--NQFWSLK-EGCV---ITSDKFQIETLEIIIKPHFNLTllsltdKFG--QA 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1185 RTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDY---LNKNRA----GLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVD 1257
Cdd:PHA02740   176 QKISHFQYTAWPADGFSHDPDAFIDFFCNIDDLcadLEKHKAdgkiAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLS 255

                          250       260
                   ....*....|....*....|....*....
gi 1822521651 1258 VYGIVHNMRMSRTCMVQTENQYIFLHQCI 1286
Cdd:PHA02740   256 IANALKKVRQKKYGCMNCLDDYVFCYHLI 284
fn3 pfam00041
Fibronectin type III domain;
220-295 3.02e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 55.11  E-value: 3.02e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521651  220 SPVTGLSVVNGTTESLRIKWTRPTDTRASDYTYRVTVTNVTGGVSWTEST-SKDKTTFTATGLQPGDQYQLSVQSVT 295
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITvPGTTTSVTLTGLKPGTEYEVRVQAVN 77
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 219-295 1.02e-08

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: 53.39  E-value: 1.02e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521651   219 PSPVTGLSVVNGTTESLRIKWTRPTDTRASDYTYRVTVTNVTGGVSWTE-STSKDKTTFTATGLQPGDQYQLSVQSVT 295
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEvNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 498-574 1.12e-08

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: 53.39  E-value: 1.12e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521651   498 PSPVTGLSVVNGTTESLTIEWTSPNDTRASNYIYNVTVTNVTGGVSWTQ-STSKDETTFTATRLQPGDQYQLSVQSVT 574
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEvNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 591-667 1.24e-08

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: 53.39  E-value: 1.24e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521651   591 PSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYRVTVTNVTGGVSWSK-STSKGETTFTATGLQPGDQYQLSVQSVT 667
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEvNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78
fn3 pfam00041
Fibronectin type III domain;
778-856 2.47e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 52.42  E-value: 2.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  778 SPVSGLTVVNRTTVSIEVTWAAPTDARAPEYTYRITLANVTRRGRGA-IDTGPGVTTFTVTNLVPGVEYELRLQSVTPAG 856
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNeITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 405-481 3.10e-08

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: 52.23  E-value: 3.10e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521651   405 PSPVTGLTVVNGTTHSLRIEWTPPTDTRATNYTYKVTVTNVAGGVSSTTITNKG-ETAFTATGLQPGDQYQLSVQSVT 481
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPsSTSYTLTGLKPGTEYEFRVRAVN 78
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 777-865 3.24e-08

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: 52.50  E-value: 3.24e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  777 PSPVSGLTVVNRTTVSIEVTWAAPTDARAPEYTYRITLANVTRRGRGAIDTGPG-VTTFTVTNLVPGVEYELRLQSVTPA 855
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGsETSYTLTGLKPGTEYEFRVRAVNGG 80

                           90
                   ....*....|..
gi 1822521651  856 GT--RSSPETVR 865
Cdd:cd00063     81 GEspPSESVTVT 92
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 126-202 3.48e-08

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: 51.85  E-value: 3.48e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521651   126 PSPVIGLSVVNGTTQSLWIEWTSPTDTRATNYTYIVTVTNVTGGVSWTK-STNKDKTTFTATGLQPGDQYQLSVRSVT 202
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEvNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 777-856 4.11e-08

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: 51.85  E-value: 4.11e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651   777 PSPVSGLTVVNRTTVSIEVTWAAPTDARAPEYTYRITLANVTRRGRGA-IDTGPGVTTFTVTNLVPGVEYELRLQSVTPA 855
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKeVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                    .
gi 1822521651   856 G 856
Cdd:smart00060   81 G 81
fn3 pfam00041
Fibronectin type III domain;
685-760 4.79e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 51.65  E-value: 4.79e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521651  685 SPVTGLSVVNSTTQSLRIEWTTPNNIRASNYTYNVTVTNVTDGASSTTIT-SKGETTFTVTGLQPGDQYRLSVRSVT 760
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITvPGTTTSVTLTGLKPGTEYEVRVQAVN 77
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 33-124 5.12e-08

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: 51.73  E-value: 5.12e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651   33 PSPVTGLSVVSRTTDSLRIEWTSPNDTRASNYTYNVTVTNV-AGGVSSITTTGKNETTFTATGLQPGDQYLLSVRSVTpE 111
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKgSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN-G 79

                           90
                   ....*....|...
gi 1822521651  112 DTLSTPVEVTSTT 124
Cdd:cd00063     80 GGESPPSESVTVT 92
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 684-760 7.61e-08

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: 51.08  E-value: 7.61e-08
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521651   684 PSPVTGLSVVNSTTQSLRIEWTTPNNIRASNYTYNVTVTNVTDGASSTTITSKG-ETTFTVTGLQPGDQYRLSVRSVT 760
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPsSTSYTLTGLKPGTEYEFRVRAVN 78
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1183-1284 8.68e-08

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 52.67  E-value: 8.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1183 EPRTITQFHFTsWPDHGVPKTTdkllQFQRMMRDYLNKNRAGLPV-VHCSAGVGRTGTLIALdYLLQR-IE-KEAVVDVy 1259
Cdd:COG2453     44 EEAGLEYLHLP-IPDFGAPDDE----QLQEAVDFIDEALREGKKVlVHCRGGIGRTGTVAAA-YLVLLgLSaEEALARV- 116

                           90       100
                   ....*....|....*....|....*
gi 1822521651 1260 givhnmRMSRTCMVQTENQYIFLHQ 1284
Cdd:COG2453    117 ------RAARPGAVETPAQRAFLER 135
fn3 pfam00041
Fibronectin type III domain;
592-667 8.86e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 50.88  E-value: 8.86e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521651  592 SPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYRVTVTNVTGGVSW-SKSTSKGETTFTATGLQPGDQYQLSVQSVT 667
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWnEITVPGTTTSVTLTGLKPGTEYEVRVQAVN 77
fn3 pfam00041
Fibronectin type III domain;
406-481 8.86e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 50.88  E-value: 8.86e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521651  406 SPVTGLTVVNGTTHSLRIEWTPPTDTRATNYTYKVTVTNVAGGVSSTTITNKG-ETAFTATGLQPGDQYQLSVQSVT 481
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGtTTSVTLTGLKPGTEYEVRVQAVN 77
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1207-1284 8.95e-08

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


Pssm-ID: 350344 [Multi-domain]  Cd Length: 113  Bit Score: 51.58  E-value: 8.95e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1207 LLQFQRMMRDYLNKNRAGLPV-VHCSAGVGRTGTLIALDYLLQRIEkeavvDVYGIVHNMRMSRT-CMVQTENQYIFLHQ 1284
Cdd:cd14494     39 LAMVDRFLEVLDQAEKPGEPVlVHCKAGVGRTGTLVACYLVLLGGM-----SAEEAVRIVRLIRPgGIPQTIEQLDFLIK 113
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 405-496 9.46e-08

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: 50.96  E-value: 9.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  405 PSPVTGLTVVNGTTHSLRIEWTPPTDTRATNYTYKVTVTNVAGGVSST-TITNKGETAFTATGLQPGDQYQLSVQSVTpE 483
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEvEVTPGSETSYTLTGLKPGTEYEFRVRAVN-G 79

                           90
                   ....*....|...
gi 1822521651  484 DTLSTPVEVTSTT 496
Cdd:cd00063     80 GGESPPSESVTVT 92
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 1187-1284 9.68e-08

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


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 53.04  E-value: 9.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1187 ITQFHFtSWPDHGVPkttDKLLQFQRMMRDYLNKNRAGLPVV-HCSAGVGRTGTLIA--LDYLLQRIEKEAVVDvygIVh 1263
Cdd:cd14505     73 ITWHHL-PIPDGGVP---SDIAQWQELLEELLSALENGKKVLiHCKGGLGRTGLIAAclLLELGDTLDPEQAIA---AV- 144

                           90       100
                   ....*....|....*....|.
gi 1822521651 1264 nmRMSRTCMVQTENQYIFLHQ 1284
Cdd:cd14505    145 --RALRPGAIQTPKQENFLHQ 163
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 684-773 1.17e-07

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: 50.96  E-value: 1.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  684 PSPVTGLSVVNSTTQSLRIEWTTPNNIRASNYTYNVTVTNVTDGASST-TITSKGETTFTVTGLQPGDQYRLSVRSVTpE 762
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEvEVTPGSETSYTLTGLKPGTEYEFRVRAVN-G 79

                           90
                   ....*....|.
gi 1822521651  763 DTWSTPAQVTS 773
Cdd:cd00063     80 GGESPPSESVT 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 312-403 1.34e-07

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: 50.57  E-value: 1.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  312 PSPVTGLSVVNGTTQSLTIEWTRPTDTRATNYTYIVTVTNVTGGVSST-TVTSRGETTFKATGLQPGDQYLLSVQSVTpE 390
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEvEVTPGSETSYTLTGLKPGTEYEFRVRAVN-G 79

                           90
                   ....*....|...
gi 1822521651  391 DTWSTPVEVTNTT 403
Cdd:cd00063     80 GGESPPSESVTVT 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 219-310 2.11e-07

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: 50.19  E-value: 2.11e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  219 PSPVTGLSVVNGTTESLRIKWTRPTDTRASDYTYRVTVTNVTGGVSWT-ESTSKDKTTFTATGLQPGDQYQLSVQSVTpE 297
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEvEVTPGSETSYTLTGLKPGTEYEFRVRAVN-G 79

                           90
                   ....*....|...
gi 1822521651  298 DTVSSPLEVTNTT 310
Cdd:cd00063     80 GGESPPSESVTVT 92
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 1183-1267 2.22e-07

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


Pssm-ID: 350347 [Multi-domain]  Cd Length: 160  Bit Score: 51.81  E-value: 2.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1183 EPRTITQFHFT----SWPDHGVPkTTDKLLQFQRMMRDYLNKNRAGLPVVHCSAGVGRTGTLIA--LDYLLQRI-EKEAV 1255
Cdd:cd14497     52 EYDDDSKFEGRvlhyGFPDHHPP-PLGLLLEIVDDIDSWLSEDPNNVAVVHCKAGKGRTGTVICayLLYYGQYStADEAL 130

                           90
                   ....*....|..
gi 1822521651 1256 VDVYgivhNMRM 1267
Cdd:cd14497    131 EYFA----KKRF 138
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 33-109 2.53e-07

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: 49.54  E-value: 2.53e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521651    33 PSPVTGLSVVSRTTDSLRIEWTSPNDTRASNYTYNVTVTNVAGGVSSIT-TTGKNETTFTATGLQPGDQYLLSVRSVT 109
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEvNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 312-388 4.92e-07

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: 48.76  E-value: 4.92e-07
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521651   312 PSPVTGLSVVNGTTQSLTIEWTRPTDTRATNYTYIVTVTNVTGGVSSTTV-TSRGETTFKATGLQPGDQYLLSVQSVT 388
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVnVTPSSTSYTLTGLKPGTEYEFRVRAVN 78
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 591-682 5.27e-07

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: 49.03  E-value: 5.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  591 PSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYRVTVTNVTGGvSWSK--STSKGETTFTATGLQPGDQYQLSVQSVTp 668
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSG-DWKEveVTPGSETSYTLTGLKPGTEYEFRVRAVN- 78

                           90
                   ....*....|....
gi 1822521651  669 EDTLSTPVEVKSTT 682
Cdd:cd00063     79 GGGESPPSESVTVT 92
FhaB COG3210
Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ...
 29-838 5.39e-07

Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442443 [Multi-domain]  Cd Length: 1698  Bit Score: 54.39  E-value: 5.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651   29 NVTDPSPVTGLSVVSRTTDSLRIEWTSPNDTRASNYTYNVTVTNVAGGVSSITTTGKNETTFTATGLQPGDQYLLSVRSV 108
Cdd:COG3210    820 TITINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATAASITVGSGGVATSTGTANAGTLTNL 899

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  109 TPEDTLSTPVEVTSTTNPSPVIGLSVVNGTTQSLWIEWTSPTDTRATNYTYIVTVTNVTGGVSWTKSTNKDKTTFTATGL 188
Cdd:COG3210    900 GTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTGAGNGTTALSGTQGNAGLSAASASDGAGDTGASSAAGSSAVGT 979

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  189 QPGDQYQLSVRSVTPEDTLSTPVEVTNTTNPSPVTGLSVVNGTTESLRIKWTRPTDTRASDYTYRVTVTNVTGGVSWTES 268
Cdd:COG3210    980 SANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAIVAGGNGVTGTTGTASATGTGTAATAGGQNGVGVNASGISGGNAA 1059

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  269 TSKDKTTFTATGLQPGDQYQLSVQSVTPEDTVSSPLEVTNTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRATNYTYIVT 348
Cdd:COG3210   1060 ALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGATGTSGGTTTSTGGVTASKVGGTTTVGATGTSTASTEA 1139

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  349 VTNVTGGVSSTTVTSRGETTFKATGLQPGDQYLLSVQSVTPEDTWSTPVEVTNTTNPSPVTGLTVVNGTTHSLRIEWTPP 428
Cdd:COG3210   1140 AGAGTLTGLVAVSAVAGGASSASAGDTTAVAAATTTTTGSAINGGADSAATEGTAGTDLKGGDSTGGSTTTIGTTNVTTT 1219

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  429 TDTRATNYTYKVTVTNVAGGVSSTTITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPVTGLSVVN 508
Cdd:COG3210   1220 TTLTASDTGNTTATGGSSAGQTGSFVAAGSASGTGDATTGATAGAVSNGATSTVAGNAGATATGSTVDIGSTSATSAGGS 1299

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  509 GTTESLTIEWTSPNDTRASNYIYNVTVTNVTGGVSWTQSTSKDETTFTATRLQPGDQYQLSVQSVTPEDTLSTPVEVTST 588
Cdd:COG3210   1300 LDTTGNTAGANGATVGTGIGGTTATGTAVAAVNSGGVNAGGGTINTTAANTGLNGGNGATDSAAGAGSGGAAGSLAATAG 1379

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  589 TNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYRVTVTNVTGGVSWSKSTSKGETTFTATGLQPGDQYQLSVQSVTP 668
Cdd:COG3210   1380 AGTVLTGAGNNTGAEGTNAGRDGGVTTSGTGVGNNGGVSGTTVAGTTGSSATTGTGGTGNTTGTSVAGAGGGNADASAIN 1459

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  669 EDTLSTPVEVKSTTDPSPVTGLSVVNSTTQSLRIEWTTPNNIRASNYTYNVTVTNVTDGASSTTITSKGETTFTVTGLQP 748
Cdd:COG3210   1460 TGNASSLGAGGSTAGNAVGGAVIGGTTTGGNGAGVAGATASNGGTSTGAGGTAGGTTAEVAKASLEGGEGTYGGSSVAEA 1539

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  749 GDQYRLSVRSVTPEDTWSTPAQVTSTSNPSPVSGLTVVNRTTVSIEVTWAAPTDARAPEYTYRITLANVTRRGRGAIDTG 828
Cdd:COG3210   1540 GTGGGILGAVSGAGSEGGAAGGVTGSVGVGGTDGAGGDTGGADDTGAQAPTAGNTATLTLSLAEGTNAEYGGTTNVTSGT 1619

                          810
                   ....*....|
gi 1822521651  829 PGVTTFTVTN 838
Cdd:COG3210   1620 AGNAGATGAN 1629
fn3 pfam00041
Fibronectin type III domain;
499-574 5.51e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 48.57  E-value: 5.51e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521651  499 SPVTGLSVVNGTTESLTIEWTSPNDTRASNYIYNVTVTNVTGGVSW-TQSTSKDETTFTATRLQPGDQYQLSVQSVT 574
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWnEITVPGTTTSVTLTGLKPGTEYEVRVQAVN 77
fn3 pfam00041
Fibronectin type III domain;
34-109 1.09e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 47.79  E-value: 1.09e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521651   34 SPVTGLSVVSRTTDSLRIEWTSPNDTRASNYTYNVTVTNVAGGVSSIT-TTGKNETTFTATGLQPGDQYLLSVRSVT 109
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEiTVPGTTTSVTLTGLKPGTEYEVRVQAVN 77
RhsA COG3209
Uncharacterized conserved protein RhaS, contains 28 RHS repeats [General function prediction ...
 27-718 1.26e-06

Uncharacterized conserved protein RhaS, contains 28 RHS repeats [General function prediction only];


Pssm-ID: 442442 [Multi-domain]  Cd Length: 1103  Bit Score: 53.22  E-value: 1.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651   27 SQNVTDPSPVTGLSVVSRTTDSLRIEWTSPNDTRASNYTYNVTVTNVAGGVSSITTTGKNETTFTATGLQPGDQYLLSVR 106
Cdd:COG3209     77 AGGVTALGDASAAGGGYVGGAAAGGGATLTGLAAATASAGRLVSTGAGAGGTVTAATGGTLGATAGSATTGSTDGGRGGV 156

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  107 SVTPEDTLSTPVEVTSTTNPSPVIGLSVVNGTTqSLWIEWTSPTDTRATNYTYIVTVTNVTGGVSWTKSTNKDKTTFTAT 186
Cdd:COG3209    157 AVTGLAGGGASAYGLTLGGAAAGPATGVGTGAV-TLATGLAGSALLALGSGAILGGLAGAYSGSATTATGTALGTPASVA 235

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  187 GLQPGDQYQLSVRSVTPEDTLSTPVEVTNTTNPSPVTGLSVVNGTTESLRIKWTRPTDTRASDYTYRVTVTNVTGGVSWT 266
Cdd:COG3209    236 ATVTGSATGAAGAGAAVATAATTLGGTTGAGTGASGAGLDASTGTGGAGGSNAAATAGGLGGAGLGSGGAGGGGTAGGTT 315

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  267 ESTSKDKTTFTATGLQPGDQYQLSVQSVTPEDTVSSPLEVTNTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRATNYTYI 346
Cdd:COG3209    316 TAAGTTGTAAVSGAADAGTTTTTGTGTGGTTTTVGGGGSLTLGGYGAAGGLTTSVGAGGGGSTSGSTTTVGGGGTATGSG 395

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  347 VTVTNVTGGVSSTTVTSRGETTFKATGLQPGDQYLLSVQSVTPEDTWSTPVEVTNTTNPSPVTGLTVVNGTTHSLRIEWT 426
Cdd:COG3209    396 GGSSTTGVGAGTTTTSTTGGDGGPATAAGALTAGGTATGTGTGGGGTTAGTDATTTTGGAGASGTLTTTGGAATGATTGG 475

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  427 PPTDTRATNYTYKVTVTNVAGGVSSTTITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPVTGLSV 506
Cdd:COG3209    476 GTEAGTGGGTLTSGSAGATTLGTDTTLDDTLGGTTTTTAGARGLVVTTGTTLTLGTTTTATLSATDATGTGDTTTTGTVG 555

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  507 VNGTTESLTIEWTSPNDTRASNYIYNVTVTNVTGGVSWTQSTSKDETTFTATRLQPGDQYQLSVQSVTPEDTLSTPVEVT 586
Cdd:COG3209    556 TGTSTGTGGTGTVTTTGDGTGGASTTTGTTGGTATTTTVTTTTTTSTAGTTTTTTSGYTRAGLTLTLGTGTASGLERATA 635

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  587 STTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYRVTVTNVTGGVSWSKSTSKGETTFTATGLQPGDQYQLSVQSV 666
Cdd:COG3209    636 STGSTTGGTTGTGVTTTGTTTTRATGTTGTGTGVTAGLTTLATGGTTVGGGTGTTSTATTGATTGGTETGTTVTTLAGGT 715

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1822521651  667 TPEDTLSTPVEVKSTTDPSPVTGLSVVNSTTQSlrieWTTPNNIRASNYTYN 718
Cdd:COG3209    716 TTRLGTTTTGGGGGTTTDGTGTGGTTGTLTTTS----TTTTTTAGALTYTYD 763
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 126-217 1.93e-06

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: 47.49  E-value: 1.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  126 PSPVIGLSVVNGTTQSLWIEWTSPTDTRATNYTYIVTVTNVTGGvSWTK--STNKDKTTFTATGLQPGDQYQLSVRSVTp 203
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSG-DWKEveVTPGSETSYTLTGLKPGTEYEFRVRAVN- 78

                           90
                   ....*....|....
gi 1822521651  204 EDTLSTPVEVTNTT 217
Cdd:cd00063     79 GGGESPPSESVTVT 92
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 498-589 2.09e-06

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: 47.11  E-value: 2.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  498 PSPVTGLSVVNGTTESLTIEWTSPNDTRASNYIYNVTVTNVTGGvSWTQ--STSKDETTFTATRLQPGDQYQLSVQSVTp 575
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSG-DWKEveVTPGSETSYTLTGLKPGTEYEFRVRAVN- 78

                           90
                   ....*....|....
gi 1822521651  576 EDTLSTPVEVTSTT 589
Cdd:cd00063     79 GGGESPPSESVTVT 92
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
572-948 2.16e-06

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 51.93  E-value: 2.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  572 SVTPEDTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTrptdtrASNYTYRVTVTNVTGGVSWSKSTSKGETTFTAT 651
Cdd:COG3401     30 GGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTG------GRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSV 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  652 GLQPGDQYQLSVQSVTPEDTLSTPVEVKSTTDPSPVTGLSVVNSTTQSLRIEWTTPNNIRASNYTYNVTVTNVTDGASST 731
Cdd:COG3401    104 GGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATT 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  732 TITSKGETTFTVTG-LQPGDQYRLSVRSVTPEDTWSTPAQV---TSTSNPSPVSGLTVVNRTTVSIEVTWAAPTDARAPE 807
Cdd:COG3401    184 SLTVTSTTLVDGGGdIEPGTTYYYRVAATDTGGESAPSNEVsvtTPTTPPSAPTGLTATADTPGSVTLSWDPVTESDATG 263

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  808 YT-YRITLANVTRRGRGAIDTgpgvTTFTVTNLVPGVEYELRLQSVTPAGTRSSP----ETVRNATIPAAISDFRCSGST 882
Cdd:COG3401    264 YRvYRSNSGDGPFTKVATVTT----TSYTDTGLTNGTTYYYRVTAVDAAGNESAPsnvvSVTTDLTPPAAPSGLTATAVG 339

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  883 GYMVEAKWSQPNGQFSMFKALTYDGEQLISNLSLGK--EERSLTVDNLQPGRTYTLRV--VTESGNTSSQ 948
Cdd:COG3401    340 SSSITLSWTASSDADVTGYNVYRSTSGGGTYTKIAEtvTTTSYTDTGLTPGTTYYYKVtaVDAAGNESAP 409
fn3 pfam00041
Fibronectin type III domain;
313-388 2.23e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 47.02  E-value: 2.23e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521651  313 SPVTGLSVVNGTTQSLTIEWTRPTDTRATNYTYIVTVTNVTGGVSSTTVT-SRGETTFKATGLQPGDQYLLSVQSVT 388
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITvPGTTTSVTLTGLKPGTEYEVRVQAVN 77
PRK15375 PRK15375
type III secretion system effector GTPase-activating protein SptP;
1108-1242 4.45e-06

type III secretion system effector GTPase-activating protein SptP;


Pssm-ID: 185273 [Multi-domain]  Cd Length: 535  Bit Score: 50.96  E-value: 4.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1108 PNTVVDFWRMVWEQKTKVIVMLTNcveQNRVKCERYWPMDMSSCLYGDIVVNIVSEETSPEW-TTRKFNVKKTGCPEPRT 1186
Cdd:PRK15375   346 PDALEAHMKMLLEKECSCLVVLTS---EDQMQAKQLPPYFRGSYTFGEVHTNSQKVSSASQGeAIDQYNMQLSCGEKRYT 422

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1822521651 1187 ITQFHFTSWPDHGVPKTTDKLLQFQRMMRdylNKNRAG----------LPVVHCSAGVGRTGTLIA 1242
Cdd:PRK15375   423 IPVLHVKNWPDHQPLPSTDQLEYLADRVK---NSNQNGapgrsssdkhLPMIHCLGGVGRTGTMAA 485
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 1190-1283 7.45e-06

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


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 48.50  E-value: 7.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1190 FHFTSWPDHGVPkTTDKLLQFQRMMRDYLNKnrAGLPVVHCSAGVGRTGTLIA--LDYLLQRIEKEAVVDVygivhnmRM 1267
Cdd:cd14506     79 FYNFGWKDYGVP-SLTTILDIVKVMAFALQE--GGKVAVHCHAGLGRTGVLIAcyLVYALRMSADQAIRLV-------RS 148

                           90
                   ....*....|....*.
gi 1822521651 1268 SRTCMVQTENQYIFLH 1283
Cdd:cd14506    149 KRPNSIQTRGQVLCVR 164
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 1196-1283 8.20e-06

protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase/transmembrane phosphatase with tensin homology; Voltage-sensitive phosphatase (VSP) proteins comprise a family of phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. This family is conserved in deuterostomes; VSP was first identified as a sperm flagellar plasma membrane protein in Ciona intestinalis. Gene duplication events in primates resulted in the presence of paralogs, transmembrane phosphatase with tensin homology (TPTE) and TPTE2, that retain protein domain architecture but, in the case of TPTE, have lost catalytic activity. TPTE, also called cancer/testis antigen 44 (CT44), may play a role in the signal transduction pathways of the endocrine or spermatogenic function of the testis. TPTE2, also called TPTE and PTEN homologous inositol lipid phosphatase (TPIP), occurs in several differentially spliced forms; TPIP alpha displays phosphoinositide 3-phosphatase activity and is localized on the endoplasmic reticulum, while TPIP beta is cytosolic and lacks detectable phosphatase activity. VSP/TPTE proteins contain an N-terminal voltage sensor consisting of four transmembrane segments, a protein tyrosine phosphatase (PTP)-like phosphoinositide phosphatase catalytic domain, followed by a regulatory C2 domain.


Pssm-ID: 350360 [Multi-domain]  Cd Length: 177  Bit Score: 47.74  E-value: 8.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1196 PDHGVPkTTDKLLQFQRMMRDYLNKNRAGLPVVHCSAGVGRTGTLIA---LDYLLQRIEKEAvVDVYGivhNMRMSRTCM 1272
Cdd:cd14510     82 DDHNVP-TLDEMLSFTAEVREWMAADPKNVVAIHCKGGKGRTGTMVCawlIYSGQFESAKEA-LEYFG---ERRTDKSVS 156

                           90
                   ....*....|....*.
gi 1822521651 1273 -----VQTENQYIFLH 1283
Cdd:cd14510    157 skfqgVETPSQSRYVG 172
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
29-280 1.09e-05

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 50.00  E-value: 1.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651   29 NVTDPSPVTGLSVVSRTTDSLRIEWTSPNDTRASNYtyNVTVTNVAGGVSSITTTGKNETTFTATGLQPGDQYLLSVRSV 108
Cdd:COG3401    323 DLTPPAAPSGLTATAVGSSSITLSWTASSDADVTGY--NVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAV 400

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  109 T---PEDTLSTPVEVTSTTNPSPVIGLSVVNGTTQSLWIEWTSPT----DTRATNYTYIVTVTNVTGGVSWTKSTNKDKT 181
Cdd:COG3401    401 DaagNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAAsaasNPGVSAAVLADGGDTGNAVPFTTTSSTVTAT 480

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  182 T---------FTATGLQPGDQYQLSVRSVTPEDTLSTPVEVTNTTNPSPVTGLSVVNGTTESLRIKWTRPTDTRASDYTY 252
Cdd:COG3401    481 TtdtttanlsVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSS 560

                          250       260
                   ....*....|....*....|....*...
gi 1822521651  253 RVTVTNVTGGVSWTESTSKDKTTFTATG 280
Cdd:COG3401    561 VSGAGLGSGNLYLITTLGGSLLTTTSTN 588
fn3 pfam00041
Fibronectin type III domain;
127-202 1.56e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 44.33  E-value: 1.56e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521651  127 SPVIGLSVVNGTTQSLWIEWTSPTDTRATNYTYIVTVTNVTGGVSW-TKSTNKDKTTFTATGLQPGDQYQLSVRSVT 202
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWnEITVPGTTTSVTLTGLKPGTEYEVRVQAVN 77
COG4625 COG4625
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ...
 254-745 2.89e-05

Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];


Pssm-ID: 443664 [Multi-domain]  Cd Length: 900  Bit Score: 48.62  E-value: 2.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  254 VTVTNVTGGVSWTESTSKDKTTFTATGLQPGDQYQLSVQSVTPEDTVSSPLEVTNTTNPSPVTGLSVVNGTTQSLTIEWT 333
Cdd:COG4625      7 GGGGGGGGGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGGGGGGGG 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  334 RPTDTRATNYTYIVTVTNVTGGVSSTTVTSRGETTFKATGLQPGDQYLLSVQSVTPEDTWSTPVEVTNTTNPSPVTGLTV 413
Cdd:COG4625     87 GGGTGGVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGAGGGGGG 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  414 VNGTTHSLRIEWTPPTDTRATNYTYKVTVTNVAGGVSSTTITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVT 493
Cdd:COG4625    167 GGGGGGGGGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 246

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  494 STTNPSPVTGLSVVNGTTESLTIEWTSPNDTRASNYIYNVTVTNVTGGVSWTQSTSKDETTFTATRLQPGDQYQLSVQSV 573
Cdd:COG4625    247 GAGGGGGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 326

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  574 TPEDTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYRVTVTNVTGGVSWSKSTSKGETTFTATGL 653
Cdd:COG4625    327 GGGGGGGAGGGGGSGGAGAGGGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAGGGGGGGGAG 406

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  654 QPGDQYQLSVQSVTPEDTLSTPVEVKSTTDPSPVTGLSVVNSTTQSLRIEWTTPNNIRASNYTYNVTVTNVTDGASS--- 730
Cdd:COG4625    407 GTGGGGAGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGSGAGTLTLTGNNTytg 486

                          490
                   ....*....|....*.
gi 1822521651  731 -TTITSKGETTFTVTG 745
Cdd:COG4625    487 tTTVNGGGNYTQSAGS 502
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
731-946 4.38e-05

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 48.02  E-value: 4.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  731 TTITSKGETTFTVTGLQPGDQYRLSVRSVTPEDTWSTPAQVTSTSNPSpvsgLTVVNRTTV--SIEVTWAAPTDARAPEY 808
Cdd:COG4733    494 VSIEENEDGTYTITAVQHAPEKYAAIDAGAFDDVPPQWPPVNVTTSES----LSVVAQGTAvtTLTVSWDAPAGAVAYEV 569

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  809 TYRITLANVTRRGRgaidtgPGVTTFTVTNLVPGvEYELRLQSVTPAGTRSSPETVRNATI------PAAISDFRCSGST 882
Cdd:COG4733    570 EWRRDDGNWVSVPR------TSGTSFEVPGIYAG-DYEVRVRAINALGVSSAWAASSETTVtgktapPPAPTGLTATGGL 642

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  883 GyMVEAKWSQPNG----QFSMFKALTYDGEQLISNLSLGKeERSLTVDNLQPGRTYTLRV--VTESGNTS 946
Cdd:COG4733    643 G-GITLSWSFPVDadtlRTEIRYSTTGDWASATVAQALYP-GNTYTLAGLKAGQTYYYRAraVDRSGNVS 710
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
71-671 6.10e-05

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 47.63  E-value: 6.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651   71 TNVAGGVSSITttGKNETTFTATGLQPGDQYLlsvRSVTPEDTlstPVEVTSTTNPSPVIGLSVVNGTTQSLWIEWTSPT 150
Cdd:COG4733    412 RRIGGRVSSVD--GRVVTLDRPVTMEAGDRYL---RVRLPDGT---SVARTVQSVAGRTLTVSTAYSETPEAGAVWAFGP 483

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  151 DTRATNYTYIVTVTNVTGGvswtkstnkdktTFTATGLQPGDQYQLSVRSVTPEDTLSTPVEVTNTTNPSpvtgLSVVNG 230
Cdd:COG4733    484 DELETQLFRVVSIEENEDG------------TYTITAVQHAPEKYAAIDAGAFDDVPPQWPPVNVTTSES----LSVVAQ 547

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  231 TTE--SLRIKWTRPTDT------------------------------RASDYTYRVTVTNVTGGVS-WTESTSkdkttFT 277
Cdd:COG4733    548 GTAvtTLTVSWDAPAGAvayevewrrddgnwvsvprtsgtsfevpgiYAGDYEVRVRAINALGVSSaWAASSE-----TT 622

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  278 ATGLqpgdqyqlsvqsvtpedtvssplevtnTTNPSPVTGLSVVNGTTQsLTIEWTRPTDTRATnYTYIVTVTNVTGGVS 357
Cdd:COG4733    623 VTGK---------------------------TAPPPAPTGLTATGGLGG-ITLSWSFPVDADTL-RTEIRYSTTGDWASA 673

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  358 STTVTSRGETTFKATGLQPGDQYLLSVQSVtpeDTWSTPVEVTNTTNPSPVTGLTVVNGTTHSLRIEWTPPTDTRATNYT 437
Cdd:COG4733    674 TVAQALYPGNTYTLAGLKAGQTYYYRARAV---DRSGNVSAWWVSGQASADAAGILDAITGQILETELGQELDAIIQNAT 750

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  438 YKVTVTNVAGGVSSTTITNKGETAFTATglqpgdqyqlSVQSVTPEDTLSTPVEVTSTTNPSPVTGLSVVNGTTESLTIE 517
Cdd:COG4733    751 VAEVVAATVTDVTAQIDTAVLFAGVATA----------AAIGAEARVAATVAESATAAAATGTAADAAGDASGGVTAGTS 820

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  518 WTSPNDTRASNYIYNVTVTNVTGGVSWTQSTSKDETTFtatrlQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPVTGL 597
Cdd:COG4733    821 GTTGAGDTAASTTRVAAAVVLAGVVVYGDAIIESGNTG-----DIVATGDIASAAAGAVATTVSGTTAADVSAVADSTAA 895

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1822521651  598 SVVNGTTQSLTIEWTRPTDTRASNYTYRVTVTNVTGGV--SWSKSTSKGETTFTATGLQPGDQYQLSVQSVTPEDT 671
Cdd:COG4733    896 SLTAIVIAATTIIDAIGDGTTREPAGDIGASGGAQGFAvtIVGSFDGAGAVATVDAGQSVVDGVGTAVEAANGTET 971
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 1189-1242 1.25e-04

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


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 43.42  E-value: 1.25e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1822521651 1189 QFHFTSWPDHGVPkTTDKLLQFQRMMRDYLNKNRAGLpvVHCSAGVGRTGTLIA 1242
Cdd:cd14504     51 RYHHIPIEDYTPP-TLEQIDEFLDIVEEANAKNEAVL--VHCLAGKGRTGTMLA 101
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 1228-1249 2.90e-04

C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division control protein 14 (CDC14) family is highly conserved in all eukaryotes, although the roles of its members seem to have diverged during evolution. Yeast Cdc14, the best characterized member of this family, is a dual-specificity phosphatase that plays key roles in cell cycle control. It preferentially dephosphorylates cyclin-dependent kinase (CDK) targets, which makes it the main antagonist of CDK in the cell. Cdc14 functions at the end of mitosis and it triggers the events that completely eliminates the activity of CDK and other mitotic kinases. It is also involved in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint, and in chromosome segregation. Cdc14 phosphatases also function in DNA replication, DNA damage checkpoint, and DNA repair. Vertebrates may contain more than one Cdc14 homolog; humans have three (CDC14A, CDC14B, and CDC14C). CDC14 family proteins contain a highly conserved N-terminal pseudophosphatase domain that contributes to substrate specificity and a C-terminal catalytic dual-specificity phosphatase domain with the PTP signature motif.


Pssm-ID: 350349 [Multi-domain]  Cd Length: 174  Bit Score: 43.21  E-value: 2.90e-04
                           10        20
                   ....*....|....*....|..
gi 1822521651 1228 VHCSAGVGRTGTLIALdYLLQR 1249
Cdd:cd14499    114 VHCKAGLGRTGTLIAC-YLMKH 134
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 270-777 4.70e-04

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 44.52  E-value: 4.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  270 SKDKTTFTATGLQPGDQYQLSVQSVTPEDtvssplevTNTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTR---------- 339
Cdd:pfam05109  312 SQDMPTNTTDITYVGDNATYSVPMVTSED--------ANSPNVTVTAFWAWPNNTETDFKCKWTLTSGTPsgcenisgaf 383

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  340 ATNYTYIVTVTNVtGGVSSTTVTSRGETTFKATGLQpgdqyllSVQSVTPEDTWSTP-VEVTNTTNPSPVTGLTvvnGTT 418
Cdd:pfam05109  384 ASNRTFDITVSGL-GTAPKTLIITRTATNATTTTHK-------VIFSKAPESTTTSPtLNTTGFAAPNTTTGLP---SST 452

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  419 HsLRIEWTPPTDTRATNYTYKVTVTNVAGGVS-STTITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTtn 497
Cdd:pfam05109  453 H-VPTNLTAPASTGPTVSTADVTSPTPAGTTSgASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPTPNATSPTPAVTT-- 529

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  498 PSPVTGLSVVNGTTESLTIEWTSPNDTRASNYIYNVTVTNVTGGVSWTQSTSKDET-TFTATRLQPGDQY-QLSVQSVTP 575
Cdd:pfam05109  530 PTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPTPNATIPTLGKTSPTSAVTTpTPNATSPTVGETSpQANTTNHTL 609

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  576 EDTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTRP----------TDTRASNYTYRVTVTNVTGGVSWSKSTSKGE 645
Cdd:pfam05109  610 GGTSSTPVVTSPPKNATSAVTTGQHNITSSSTSSMSLRPssisetlspsTSDNSTSHMPLLTSAHPTGGENITQVTPAST 689

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  646 TTFTATGLQPGDQYQLSVQSVTP--EDTLSTPVEVKSTTDPSPVTGLSVVNSTTQSLRIEWTTPNNIRASNYTYNVTVTN 723
Cdd:pfam05109  690 STHHVSTSSPAPRPGTTSQASGPgnSSTSTKPGEVNVTKGTPPKNATSPQAPSGQKTAVPTVTSTGGKANSTTGGKHTTG 769

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1822521651  724 VTDGASSTTITSKGETTFT-------VTGLQPGDQYRLSVR---SVTPEDTWSTPAQVTSTSNP 777
Cdd:pfam05109  770 HGARTSTEPTTDYGGDSTTprtrynaTTYLPPSTSSKLRPRwtfTSPPVTTAQATVPVPPTSQP 833
fn3 pfam00041
Fibronectin type III domain;
872-948 1.28e-03

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 38.94  E-value: 1.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  872 AISDFRCSGSTGYMVEAKWSQP---NGQFSMFKaLTY---DGEQLISNLSLGKEERSLTVDNLQPGRTYTLRVVTESGNT 945
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPpdgNGPITGYE-VEYrpkNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ...
gi 1822521651  946 SSQ 948
Cdd:pfam00041   81 EGP 83
PTP_PTEN cd14509
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...
 1196-1266 1.43e-03

protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; Phosphatase and tensin homolog (PTEN), also phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN or mutated in multiple advanced cancers 1 (MMAC1), is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It is a critical endogenous inhibitor of phosphoinositide signaling. It dephosphorylates phosphoinositide trisphosphate, and therefore, has the function of negatively regulating Akt. The PTEN/PI3K/AKT pathway regulates the signaling of multiple biological processes such as apoptosis, metabolism, cell proliferation, and cell growth. PTEN contains an N-terminal PIP-binding domain, a protein tyrosine phosphatase (PTP)-like catalytic domain, a regulatory C2 domain responsible for its cellular location, a C-tail containing phosphorylation sites, and a C-terminal PDZ domain.


Pssm-ID: 350359 [Multi-domain]  Cd Length: 158  Bit Score: 40.65  E-value: 1.43e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521651 1196 PDHGVPkTTDKLLQFQRMMRDYLNKNRAGLPVVHCSAGVGRTGTLIALdYLLQRIE----KEAvVDVYGI--VHNMR 1266
Cdd:cd14509     68 DDHNPP-PLELIKPFCEDVDEWLKEDEKNVAAVHCKAGKGRTGVMICC-YLLYLGKfpsaKEA-LDFYGAkrTKNKK 141
DSP_DUSP16 cd14646
dual specificity phosphatase domain of dual specificity protein phosphatase 16; Dual ...
 1181-1251 1.44e-03

dual specificity phosphatase domain of dual specificity protein phosphatase 16; Dual specificity protein phosphatase 16 (DUSP16), also called mitogen-activated protein kinase (MAPK) phosphatase 7 (MKP-7), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). Like other MKPs, it deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. It belongs to the class III subfamily and is a JNK/p38-selective cytoplasmic MKP. DUSP16/MKP-7 plays an essential role in perinatal survival and selectively controls the differentiation and cytokine production of myeloid cells. It is acetylated by Mycobacterium tuberculosis Eis protein, which leads to the inhibition of JNK-dependent autophagy, phagosome maturation, and ROS generation, and thus, initiating suppression of host immune responses. DUSP16/MKP-7 contains an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.


Pssm-ID: 350494 [Multi-domain]  Cd Length: 145  Bit Score: 40.39  E-value: 1.44e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1822521651 1181 CPEPRTITQFHFTSWPDHGvpKTTDKLLQFQRMMRDYLNKNRA--GLPVVHCSAGVGRTGTlIALDYLLQRIE 1251
Cdd:cd14646     39 CPKPDFIPESHFLRVPVND--SFCEKILPWLDKSVDFIEKAKAsnGRVLVHCLAGISRSAT-IAIAYIMKRMD 108
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
299-518 2.13e-03

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 42.43  E-value: 2.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  299 TVSSPLEVTNTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRATNYTYIVTVTNVTGGVSSTTVTSRGETTfkATGLQPGD 378
Cdd:COG3469      1 SSSVSTAASPTAGGASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTA--ATSSTTST 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  379 QYLLSV---QSVTPEDTWSTPVEVTNTTNPSPVTGLTVVNGTTHSLRIEWTPPTDTRATNYTYKVTVTNVAGGVSSTTIT 455
Cdd:COG3469     79 TATATAaaaAATSTSATLVATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTET 158

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1822521651  456 NKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPVTGLSVVNGTTESLTIEW 518
Cdd:COG3469    159 ATGGTTTTSTTTTTTSASTTPSATTTATATTASGATTPSATTTATTTGPPTPGLPKHVLVGYW 221
COG4625 COG4625
Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ...
 348-842 2.14e-03

Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function unknown];


Pssm-ID: 443664 [Multi-domain]  Cd Length: 900  Bit Score: 42.46  E-value: 2.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  348 TVTNVTGGVSSTTVTSRGETTFKATGLQPGDQYLLSVQSVTPEDTWSTPVEVTNTTNPSPVTGLTVVNGTTHslriewtp 427
Cdd:COG4625     12 GGGGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGGGGG-------- 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  428 pTDTRATNYTYKVTVTNVAGGVSSTTITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPVTGLSVV 507
Cdd:COG4625     84 -GGGGGGTGGVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGAGG 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  508 NGTTESLTIEWTSPNDTRASNYIYNVTVTNVTGGVSWTQSTSKDETTFTATrlqpgDQYQLSVQSVTPEDTLSTPVEVTS 587
Cdd:COG4625    163 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGGGGG-----AGGGGGGGGGGGGGGGGGGGGGGG 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  588 TTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYRVTVTNVTGGVSWSKSTSKGETTFTATGLQPGDQYQLSVQSVT 667
Cdd:COG4625    238 GGGGGGGGGGAGGGGGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  668 PEDTLSTPVEVKSTTDPSPVTGLSVVNSTTQSLRIEWTTPNNIRASNYTYNVTVTNVTDGASSTTITSKGETTFTVTGLQ 747
Cdd:COG4625    318 GGGGGGGGGGGGGGGGAGGGGGSGGAGAGGGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAG 397

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  748 PGDQYRLSVRSVTPEDTWSTPAQVTSTSNPSPVSGLTVVNRTTVSIEVTWAAPTDARAPEYTYRITLANVTRRGRGAIDT 827
Cdd:COG4625    398 GGGGGGGAGGTGGGGAGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGSGAGTLT 477

                          490
                   ....*....|....*
gi 1822521651  828 GPGVTTFTVTNLVPG 842
Cdd:COG4625    478 LTGNNTYTGTTTVNG 492
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
1203-1284 2.20e-03

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 39.96  E-value: 2.20e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  1203 TTDKLLQFQRMMRDYLN--KNRAGLPVVHCSAGVGRTGTLIALdYLLQRiEKEAVVDVYGIVhnmRMSRTCMVQTENqyi 1280
Cdd:smart00195   56 TETKISPYFPEAVEFIEdaESKGGKVLVHCQAGVSRSATLIIA-YLMKT-RNMSLNDAYDFV---KDRRPIISPNFG--- 127


                    ....
gi 1822521651  1281 FLHQ 1284
Cdd:smart00195  128 FLRQ 131
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 1203-1284 3.10e-03

Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The enzyme's tertiary fold is highly similar to that of tyrosine-specific phosphatases, except for a "recognition" region.


Pssm-ID: 395632 [Multi-domain]  Cd Length: 127  Bit Score: 39.17  E-value: 3.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1203 TTDKLLQFQRMMRDYLN--KNRAGLPVVHCSAGVGRTGTLIALdYLLQRiEKEAVVDVYGIVhnmRMSRTCMVQTENqyi 1280
Cdd:pfam00782   47 HETNISKYLEEAVEFIDdaRQKGGKVLVHCQAGISRSATLIIA-YLMKT-RNLSLNEAYSFV---KERRPGISPNFG--- 118


                   ....
gi 1822521651 1281 FLHQ 1284
Cdd:pfam00782  119 FKRQ 122
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 1184-1268 3.42e-03

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


Pssm-ID: 350378 [Multi-domain]  Cd Length: 158  Bit Score: 39.66  E-value: 3.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1184 PRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDylnKNRAGlPVV-HCSAGVGRTGTLIALdYLlqriekeavvDVYG-- 1260
Cdd:cd14529     53 AAKIDGVKYVNLPLSATRPTESDVQSFLLIMDL---KLAPG-PVLiHCKHGKDRTGLVSAL-YR----------IVYGgs 117

                           90
                   ....*....|.
gi 1822521651 1261 ---IVHNMRMS 1268
Cdd:cd14529    118 keeANEDYRLS 128
DSP_MKP cd14512
dual specificity phosphatase domain of mitogen-activated protein kinase phosphatase; ...
 1179-1249 4.32e-03

dual specificity phosphatase domain of mitogen-activated protein kinase phosphatase; Mitogen-activated protein kinase (MAPK) phosphatases (MKPs) are eukaryotic dual-specificity phosphatases (DUSPs) that act on MAPKs, which are involved in gene regulation, cell proliferation, programmed cell death and stress responses, as an important feedback control mechanism that limits MAPK cascades. MKPs, also referred to as typical DUSPs, function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). They deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. All MKPs contain an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain. Based on sequence homology, subcellular localization and substrate specificity, 10 MKPs can be subdivided into three subfamilies (class I-III).


Pssm-ID: 350362 [Multi-domain]  Cd Length: 136  Bit Score: 39.00  E-value: 4.32e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1822521651 1179 TGCPEPRTITQFHFTSWP--DHgvpkTTDKLLQFQRMMRDYLN--KNRAGLPVVHCSAGVGRTGTlIALDYLLQR 1249
Cdd:cd14512     35 NTCPNPDFIGLFHYKRIPvnDS----FCQNISPWFDEAIEFIEeaKASNGGVLVHCLAGISRSAT-IAIAYLMKR 104
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
113-332 4.41e-03

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 41.28  E-value: 4.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  113 TLSTPVEVTSTTNPSPVIGLSVVNGTTQSLWIEWTSPTDTRATNYTYIVTV-------TNVTGGVSWTKSTNKDKTTFTA 185
Cdd:COG3469      1 SSSVSTAASPTAGGASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVaasgsagSGTGTTAASSTAATSSTTSTTA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  186 TGLQPGDQYQLSVRSVTPEDTLSTPVEVTNTTNPSPVTGLSVVNGTTeslriKWTRPTDTRASDYTYRVTVTNVTGGVSW 265
Cdd:COG3469     81 TATAAAAAATSTSATLVATSTASGANTGTSTVTTTSTGAGSVTSTTS-----STAGSTTTSGASATSSAGSTTTTTTVSG 155

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521651  266 TESTSKDKTTFTATGLQPGDQYQLSVQSVTPeDTVSSPLEVTNTTNPSPVTGLSVVNGTTQSLTIEW 332
Cdd:COG3469    156 TETATGGTTTTSTTTTTTSASTTPSATTTAT-ATTASGATTPSATTTATTTGPPTPGLPKHVLVGYW 221
DUF4959 pfam16323
Domain of unknown function (DUF4959); This family consists of uncharacterized proteins around ...
 213-307 4.49e-03

Domain of unknown function (DUF4959); This family consists of uncharacterized proteins around 400 residues in length and is mainly found in various Bacteroides, Pedobacter and Parabacteroides species. Several proteins are annotated as Galactose-binding like proteins, but the specific function of this protein is unknown.


Pssm-ID: 465093 [Multi-domain]  Cd Length: 106  Bit Score: 38.00  E-value: 4.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651  213 VTNTTNPSPVTGLSVVNGTTESLrIKWTRPTDtraSDYTYRVTVTNVTGGVSWTESTSKDKTTFTATGLQPGDQYQLSVQ 292
Cdd:pfam16323   13 GTDGTAPGPVTNVKVKNIPGGAT-ISYTLPDD---PDLLYVKAVYTIRNGKEREVKASYYTDSLTVEGFGDTGEYEVKLY 88

                           90
                   ....*....|....*
gi 1822521651  293 SVTPEDTVSSPLEVT 307
Cdd:pfam16323   89 AVSRSENESEPVEVK 103
DSP_DUSP11 cd17665
dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar ...
 1196-1241 5.13e-03

dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar proteins; dual specificity protein phosphatase 11 (DUSP11), also known as RNA/RNP complex-1-interacting phosphatase or phosphatase that interacts with RNA/RNP complex 1 (PIR1), has RNA 5'-triphosphatase and diphosphatase activity, but only poor protein-tyrosine phosphatase activity. It has activity for short RNAs but is less active toward mononucleotide triphosphates, suggesting that its primary function in vivo is to dephosphorylate RNA 5'-ends. It may play a role in nuclear mRNA metabolism. Also included in this subfamily is baculovirus RNA 5'-triphosphatase for Autographa californica nuclear polyhedrosis virus.


Pssm-ID: 350503  Cd Length: 169  Bit Score: 39.18  E-value: 5.13e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1822521651 1196 PDHGVPKTtDKLLQFQRMMRDYLNKNRA--GLPVVHCSAGVGRTGTLI 1241
Cdd:cd17665     85 PGHQVPDD-KTIQSFKDAVKDFLEKNKDndKLIGVHCTHGLNRTGYLI 131
DSP_MKP_classIII cd14568
dual specificity phosphatase domain of class III mitogen-activated protein kinase phosphatase; ...
 1175-1266 5.91e-03

dual specificity phosphatase domain of class III mitogen-activated protein kinase phosphatase; Mitogen-activated protein kinase (MAPK) phosphatases (MKPs) are eukaryotic dual-specificity phosphatases (DUSPs) that act on MAPKs and function as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). They deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. Based on sequence homology, subcellular localization and substrate specificity, 10 MKPs can be subdivided into three subfamilies (class I-III). Class III MKPs consist of DUSP8, DUSP10/MKP-5 and DUSP16/MKP-7, and are JNK/p38-selective phosphatases, which are found in both the cell nucleus and cytoplasm. All MKPs contain an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain.


Pssm-ID: 350416 [Multi-domain]  Cd Length: 140  Bit Score: 38.55  E-value: 5.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521651 1175 NVKKTgCPEPRTITQFHFTSWPDHGVPKttDKLLQFQRMMRDYLNKNRA--GLPVVHCSAGVGRTGTlIALDYLLQRIeK 1252
Cdd:cd14568     32 NVSNT-CPKPDFIPDSHFLRIPVNDSYC--EKLLPWLDKAVEFIEKARAsnKRVLVHCLAGISRSAT-IAIAYIMKHM-R 106

                           90
                   ....*....|....
gi 1822521651 1253 EAVVDVYGIVHNMR 1266
Cdd:cd14568    107 MSLDDAYRFVKEKR 120
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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