NCBI Conserved Domain Search

Fibronectin type III domain;

1480-1562

1.72e-12

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 64.74 E-value: 1.72e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049  1480 SPPSLMSFADIANTSLAITWKGPPDWT-DYNDFELQWLPRDALTVFNPYNNRKSEGR-IVYGLRPGRSYQFNVKTVSGDS 1557
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNgPITGYEVEYRPKNSGEPWNEITVPGTTTSvTLTGLKPGTEYEVRVQAVNGGG 80


                   ....*
gi 578824049  1558 WKTYS 1562
Cdd:pfam00041   81 EGPPS 85

fn3

Fibronectin type III domain;

1574-1653

1.18e-10

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 59.74 E-value: 1.18e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049  1574 DKIQNLHCRPQNSTAIACSWIPP---DSDFDGYSIECRKMDTQEVEFSRKLEKEKSLLNIMMLVPHKRYLVSIKVQSAGM 1650
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ...
gi 578824049  1651 TSE 1653
Cdd:pfam00041   81 EGP 83

fn3

Fibronectin type III domain;

950-1026

1.22e-10

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 59.74 E-value: 1.22e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049   950 DKVQGVSVSNsARSDYLRVSWVHAT---GDFDHYEVTIK--NKNNFIQTKSIPKSENECVFVQLVPGRLYSVTVTTKSGQ 1024
Cdd:pfam00041    1 SAPSNLTVTD-VTSTSLTVSWTPPPdgnGPITGYEVEYRpkNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ..
gi 578824049  1025 YE 1026
Cdd:pfam00041   80 GE 81

fn3

Fibronectin type III domain;

1126-1199

2.36e-10

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 58.97 E-value: 2.36e-10

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578824049  1126 SAVKNIHISPNGATdSLTVNWTP---GGGDVDSYTVSAF--RHSQKVDSQTIPKHVFEHTFHRLEAGEQYQIMIASVSG 1199
Cdd:pfam00041    1 SAPSNLTVTDVTST-SLTVSWTPppdGNGPITGYEVEYRpkNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78

fn3

Fibronectin type III domain;

331-407

5.45e-10

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 57.81 E-value: 5.45e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049   331 PARFGVSKEKTTSTSLHVWWTPS---SGKVTSYEVQLFDENNQKiQGVQIQESTSWNEYTFFNLTAGSKYNIAITAVSGG 407
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGE-PWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

fn3

Fibronectin type III domain;

1393-1466

3.80e-09

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 55.50 E-value: 3.80e-09

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578824049  1393 SVSHLRGSNRNTTdSLWFNWSPA---SGDFDFYELILYNPNGTKKENWK--DKDLTEWRFQGLVPGRKYVLWVVTHSGD 1466
Cdd:pfam00041    2 APSNLTVTDVTST-SLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEItvPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

fn3

Fibronectin type III domain;

1039-1112

1.78e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 53.57 E-value: 1.78e-08

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578824049  1039 PVKDLTLRNRSTEDLHVTWSGA---NGDVDQYEIQLL-FNDMKVFPPFHLVNTATEYRFTSLTPGRQYKILVLTISGD 1112
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRpKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

fn3

Fibronectin type III domain;

862-938

2.76e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 52.80 E-value: 2.76e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049   862 SSVSGVTVNNSGrNDYLSVSWLLAP---GDVDNYEVTLSH--DGKVVQSLVIAKSVRECSFSSLTPGRLYTVTITTRSGK 936
Cdd:pfam00041    1 SAPSNLTVTDVT-STSLTVSWTPPPdgnGPITGYEVEYRPknSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ..
gi 578824049   937 YE 938
Cdd:pfam00041   80 GE 81

fn3

Fibronectin type III domain;

687-765

4.41e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 52.42 E-value: 4.41e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049   687 AVLQLRVKHANETSLSIMWQTPV---AEWEKYIISLADRD--LLLIHKSLSKDAKEFTFTDLVPGRKYMATVTSISGDLK 761
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNsgEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ....
gi 578824049   762 NSSS 765
Cdd:pfam00041   82 GPPS 85

fn3

Fibronectin type III domain;

596-672

9.93e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 51.26 E-value: 9.93e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049   596 DKVANLEANNNGRmRSLVVSWSPPA---GDWEQYRILLF--NDSVVLLNITVGKEETQYVMddTGLVPGRQYEVEVIVES 670
Cdd:pfam00041    1 SAPSNLTVTDVTS-TSLTVSWTPPPdgnGPITGYEVEYRpkNSGEPWNEITVPGTTTSVTL--TGLKPGTEYEVRVQAVN 77


                   ..
gi 578824049   671 GN 672
Cdd:pfam00041   78 GG 79

FN3

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

507-582

1.09e-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: 51.73 E-value: 1.09e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049  507 PMEVSNLKVTNDGSlTSLKVKWQRPP---GNVDSYNITLSHKGTIKESRVLAPWITETHF--KELVPGRLYQVTVSCVSG 581
Cdd:cd00063     1 PSPPTNLRVTDVTS-TSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYtlTGLKPGTEYEFRVRAVNG 79


                  .
gi 578824049  582 E 582
Cdd:cd00063    80 G 80

FN3 super family

cl27307

Fibronectin type 3 domain [General function prediction only];

1093-1508

4.29e-07

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: 55.39 E-value: 4.29e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1093 FTSLTPGRQYKILVLTISGDVQQSAFIEGFTVPSAVKNIHISPNGATDSLTVNWTPGGGDVDSYTVSAFRHSQKVDSQTI 1172
Cdd:COG3401   108 NTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTV 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1173 PKHVFEHTFHRLEAGEQYQIMIASVS----GSLKNQINVV-GRTVPASVQGVIADNAYSSySLIVSWQKAAGV-AERYDI 1246
Cdd:COG3401   188 TSTTLVDGGGDIEPGTTYYYRVAATDtggeSAPSNEVSVTtPTTPPSAPTGLTATADTPG-SVTLSWDPVTESdATGYRV 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1247 LL-LTENGillrNTSEPATTKQHKFED--LTPGKKYKIQILTVSG----GLFSKEAQ-TEGRTVPAAVTDLRITENSTRH 1318
Cdd:COG3401   267 YRsNSGDG----PFTKVATVTTTSYTDtgLTNGTTYYYRVTAVDAagneSAPSNVVSvTTDLTPPAAPSGLTATAVGSSS 342

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1319 LSFRWTASEGE-LSWYNIflY---NPDGNLQERAQVDPlVQSFSFQNLLQGRM--YKMVIVTHSGELSNESF-IFGRTVP 1391
Cdd:COG3401   343 ITLSWTASSDAdVTGYNV--YrstSGGGTYTKIAETVT-TTSYTDTGLTPGTTyyYKVTAVDAAGNESAPSEeVSATTAS 419

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1392 ASVS-HLRGSNRNTTDSLWFNWSPASGDFDFYELILYNPNGTKKENWKDKDLTEW----RFQGLVPGRKYVLWVVTHSGD 1466
Cdd:COG3401   420 AASGeSLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSstvtATTTDTTTANLSVTTGSLVGG 499

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 578824049 1467 LSNKVTAESRTAPSPPSLMSFADIANTSLAITWKGPPDWTDY 1508
Cdd:COG3401   500 SGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGAS 541

fn3

Fibronectin type III domain;

774-847

3.80e-06

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 47.02 E-value: 3.80e-06

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578824049   774 QVTDLHVANQGmTSSLFTNWT---QAQGDVEFYQVLLIHENV--VIKNESISSETSRYSFHSLKSGSLYSVVVTTVSGG 847
Cdd:pfam00041    2 APSNLTVTDVT-STSLTVSWTpppDGNGPITGYEVEYRPKNSgePWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

fn3

Fibronectin type III domain;

255-316

2.18e-04

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 42.02 E-value: 2.18e-04

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578824049   255 SSHSVSIQWRIL----GSPCNFSLIYSSDTLGAALcPTFRIDNTTYGCNLQDLQAGTIYNFRIISL 316
Cdd:pfam00041   12 TSTSLTVSWTPPpdgnGPITGYEVEYRPKNSGEPW-NEITVPGTTTSVTLTGLKPGTEYEVRVQAV 76

FN3 super family

cl21522

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

422-488

9.47e-04

The actual alignment was detected with superfamily member pfam00041:

Pssm-ID: 473895 [Multi-domain] Cd Length: 85 Bit Score: 40.09 E-value: 9.47e-04

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578824049   422 SPVKDIGISTK-ANSLLISWS---HGSGNVERYRLML--MDKGILVHGGVVDKHATSYAFHGLTPGYLYNLTV 488
Cdd:pfam00041    1 SAPSNLTVTDVtSTSLTVSWTpppDGNGPITGYEVEYrpKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRV 73

Name

Accession

Description

Interval

E-value

R-PTPc-B

cd14617

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

1949-2176

4.44e-178

Pssm-ID: 350465 [Multi-domain] Cd Length: 228 Bit Score: 541.43 E-value: 4.44e-178

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1949 NRYNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 2028
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2029 KCDHYWPADQDSLYYGDLILQMLSESVLPEWTIREFKICGEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDY 2108
Cdd:cd14617    81 KCDHYWPADQDSLYYGDLIVQMLSESVLPEWTIREFKICSEEQLDAPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVRDY 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578824049 2109 INRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 2176
Cdd:cd14617   161 INRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228

PTPc

smart00194

Protein tyrosine phosphatase, catalytic domain;

1920-2178

9.68e-116

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 367.37 E-value: 9.68e-116

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049   1920 LLSKEYEELKDVGR-NQSCDIALLPENRGKNRYNNILPYDATRVKLSNvDDDPCSDYINASYIPGNNFRREYIVTQGPLP 1998
Cdd:smart00194    1 GLEEEFEKLDRLKPdDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKP-PPGEGSDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049   1999 GTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPADQ-DSLYYGDLILQMLSESVLPEWTIREFKICGEEQlDAHRL 2077
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEgEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGC-SETRT 158

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049   2078 IRHFHYTVWPDHGVPETTQSLIQFVRTVRDYinRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDL 2157
Cdd:smart00194  159 VTHYHYTNWPDHGVPESPESILDLIRAVRKS--QSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKEL 236

                           250       260
                    ....*....|....*....|.
gi 578824049   2158 RLHRVHMVQTECQYVYLHQCV 2178
Cdd:smart00194  237 RSQRPGMVQTEEQYIFLYRAI 257

Y_phosphatase

pfam00102

Protein-tyrosine phosphatase;

1945-2178

3.09e-101

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 324.97 E-value: 3.09e-101

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049  1945 NRGKNRYNNILPYDATRVKLSnvDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVE 2024
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049  2025 KGRVKCDHYWP-ADQDSLYYGDL-ILQMLSESVLPEWTIREFKICgEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFV 2102
Cdd:pfam00102   79 KGREKCAQYWPeEEGESLEYGDFtVTLKKEKEDEKDYTVRTLEVS-NGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLL 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578824049  2103 RTVRDYiNRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 2178
Cdd:pfam00102  158 RKVRKS-SLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232

beta-trefoil_Ricin_PTPRB-like

cd23409

ricin B-type lectin domain, beta-trefoil fold, found in receptor-type tyrosine-protein ...

18-134

1.15e-69

Pssm-ID: 467787 Cd Length: 117 Bit Score: 229.25 E-value: 1.15e-69

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049   18 SEGFQIVHVQKQQCLFKNEKVVVGSCNRTIQNQQWMWTEDEKLLHVKSALCLAISNSSRGPSRSAILDRCSQAPRWTCYD 97
Cdd:cd23409     1 SEGFLILHVQKQQCLFGNKTVSVGKCNATSPNQQWQWTEDGKLLHVKSGQCLGISNSSAFHSRRAILLDCSQAPRWTCHE 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 578824049   98 QEGFLEVENASLFLQKQGSRVVVKKARKYLHSWMKID 134
Cdd:cd23409    81 NEGLLEVANSSLFLTKQGQRVVVKQGKKYLHNWMKYE 117

PHA02742

protein tyrosine phosphatase; Provisional

1902-2190

1.17e-42

protein tyrosine phosphatase; Provisional

Pssm-ID: 165109 [Multi-domain] Cd Length: 303 Bit Score: 159.01 E-value: 1.17e-42

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1902 KINQFEGHFMKLQADSN--YLLSKEYEELKDVGRNQSCDIALLPENRGKNRYNNILPYDATRVKLSNvdDDPCSDYINAS 1979
Cdd:PHA02742    7 KKNSFAKNCEQLIEESNlaEILKEEHEHIMQEIVAFSCNESLELKNMKKCRYPDAPCFDRNRVILKI--EDGGDDFINAS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1980 YIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYW-PADQDSLYYGDLILQMLSESVLPE 2058
Cdd:PHA02742   85 YVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYWmPHERGKATHGEFKIKTKKIKSFRN 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2059 WTIREFKICGEEQ---LDahrlIRHFHYTVWPDHGVPETTQSLIQFVRTVR--DYINRSPGAG-------PTVVHCSAGV 2126
Cdd:PHA02742  165 YAVTNLCLTDTNTgasLD----IKHFAYEDWPHGGLPRDPNKFLDFVLAVReaDLKADVDIKGenivkepPILVHCSAGL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578824049 2127 GRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYlhqCVRDVLRARKLRSE 2190
Cdd:PHA02742  241 DRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIF---CYFIVLIFAKLMAD 301

COG5599

Protein tyrosine phosphatase [Signal transduction mechanisms];

1943-2171

2.23e-41

Protein tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 444335 [Multi-domain] Cd Length: 282 Bit Score: 154.86 E-value: 2.23e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1943 PENRGKNRYNNILPYDATRVKlsnvDDDPcsdYINASYIPGNNFRReYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQC 2022
Cdd:COG5599    40 INGSPLNRFRDIQPYKETALR----ANLG---YLNANYIQVIGNHR-YIATQYPLEEQLEDFFQMLFDNNTPVLVVLASD 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2023 VE--KGRVKCDHYWPADQDSLYYgDLILQMLSESVL-PEWTIREFKI----CGEEQLDahrlIRHFHYTVWPDHGVPETT 2095
Cdd:COG5599   112 DEisKPKVKMPVYFRQDGEYGKY-EVSSELTESIQLrDGIEARTYVLtikgTGQKKIE----IPVLHVKNWPDHGAISAE 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2096 QsLIQFVRTVRDYIN-RSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKD--SVDIYGAVHDLRLHR-VHMVQTECQY 2171
Cdd:COG5599   187 A-LKNLADLIDKKEKiKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRnGGMVQTSEQL 265

PTP_tm

pfam18861

TM proximal of protein tyrosine phosphatase, receptor type J; Protein tyrosine phosphatases ...

1691-1828

4.00e-33

Pssm-ID: 465889 Cd Length: 126 Bit Score: 125.41 E-value: 4.00e-33

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049  1691 VNCSWFSDTNGAVKYFTVVVREADgsDELKPEQQHPLPSYLEYRhNASIRVYQTNYFASKCAENPnSNSKSFNIKLGAEM 1770
Cdd:pfam18861    1 IQFSLFNSSNGPIKAYGVIVTTND--SLNRPLKEYLNKTYYDWK-YKKTDSYLATVTPNPFTSPR-SSSRSLTVPVGTGS 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 578824049  1771 ESlggkcdptqQKFCDGPLKPHTAYRISIRAFTQL-FDEDLKEFTKPLYSDTFFSLPIT 1828
Cdd:pfam18861   77 KW---------QGYCNGPLKPLGSYRFSVAAFTRLeFDDGLIDGEESYVSFTPFSEPIA 126

fn3

Fibronectin type III domain;

1480-1562

1.72e-12

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 64.74 E-value: 1.72e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049  1480 SPPSLMSFADIANTSLAITWKGPPDWT-DYNDFELQWLPRDALTVFNPYNNRKSEGR-IVYGLRPGRSYQFNVKTVSGDS 1557
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNgPITGYEVEYRPKNSGEPWNEITVPGTTTSvTLTGLKPGTEYEVRVQAVNGGG 80


                   ....*
gi 578824049  1558 WKTYS 1562
Cdd:pfam00041   81 EGPPS 85

fn3

Fibronectin type III domain;

1574-1653

1.18e-10

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 59.74 E-value: 1.18e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049  1574 DKIQNLHCRPQNSTAIACSWIPP---DSDFDGYSIECRKMDTQEVEFSRKLEKEKSLLNIMMLVPHKRYLVSIKVQSAGM 1650
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ...
gi 578824049  1651 TSE 1653
Cdd:pfam00041   81 EGP 83

fn3

Fibronectin type III domain;

950-1026

1.22e-10

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 59.74 E-value: 1.22e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049   950 DKVQGVSVSNsARSDYLRVSWVHAT---GDFDHYEVTIK--NKNNFIQTKSIPKSENECVFVQLVPGRLYSVTVTTKSGQ 1024
Cdd:pfam00041    1 SAPSNLTVTD-VTSTSLTVSWTPPPdgnGPITGYEVEYRpkNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ..
gi 578824049  1025 YE 1026
Cdd:pfam00041   80 GE 81

fn3

Fibronectin type III domain;

1126-1199

2.36e-10

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 58.97 E-value: 2.36e-10

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578824049  1126 SAVKNIHISPNGATdSLTVNWTP---GGGDVDSYTVSAF--RHSQKVDSQTIPKHVFEHTFHRLEAGEQYQIMIASVSG 1199
Cdd:pfam00041    1 SAPSNLTVTDVTST-SLTVSWTPppdGNGPITGYEVEYRpkNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78

fn3

Fibronectin type III domain;

331-407

5.45e-10

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 57.81 E-value: 5.45e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049   331 PARFGVSKEKTTSTSLHVWWTPS---SGKVTSYEVQLFDENNQKiQGVQIQESTSWNEYTFFNLTAGSKYNIAITAVSGG 407
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGE-PWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

fn3

Fibronectin type III domain;

1393-1466

3.80e-09

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 55.50 E-value: 3.80e-09

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578824049  1393 SVSHLRGSNRNTTdSLWFNWSPA---SGDFDFYELILYNPNGTKKENWK--DKDLTEWRFQGLVPGRKYVLWVVTHSGD 1466
Cdd:pfam00041    2 APSNLTVTDVTST-SLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEItvPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

FN3

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

328-419

5.98e-09

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 55.20 E-value: 5.98e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049  328 PLPPARFGVSKekTTSTSLHVWWTPSS---GKVTSYEVQLFDENNQKIQGVQIQESTSwNEYTFFNLTAGSKYNIAITAV 404
Cdd:cd00063     1 PSPPTNLRVTD--VTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSE-TSYTLTGLKPGTEYEFRVRAV 77

                          90
                  ....*....|....*.
gi 578824049  405 SGGKRS-FSVYTNGST 419
Cdd:cd00063    78 NGGGESpPSESVTVTT 93

fn3

Fibronectin type III domain;

1039-1112

1.78e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 53.57 E-value: 1.78e-08

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578824049  1039 PVKDLTLRNRSTEDLHVTWSGA---NGDVDQYEIQLL-FNDMKVFPPFHLVNTATEYRFTSLTPGRQYKILVLTISGD 1112
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRpKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

fn3

Fibronectin type III domain;

862-938

2.76e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 52.80 E-value: 2.76e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049   862 SSVSGVTVNNSGrNDYLSVSWLLAP---GDVDNYEVTLSH--DGKVVQSLVIAKSVRECSFSSLTPGRLYTVTITTRSGK 936
Cdd:pfam00041    1 SAPSNLTVTDVT-STSLTVSWTPPPdgnGPITGYEVEYRPknSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ..
gi 578824049   937 YE 938
Cdd:pfam00041   80 GE 81

fn3

Fibronectin type III domain;

687-765

4.41e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 52.42 E-value: 4.41e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049   687 AVLQLRVKHANETSLSIMWQTPV---AEWEKYIISLADRD--LLLIHKSLSKDAKEFTFTDLVPGRKYMATVTSISGDLK 761
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNsgEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ....
gi 578824049   762 NSSS 765
Cdd:pfam00041   82 GPPS 85

fn3

Fibronectin type III domain;

596-672

9.93e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 51.26 E-value: 9.93e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049   596 DKVANLEANNNGRmRSLVVSWSPPA---GDWEQYRILLF--NDSVVLLNITVGKEETQYVMddTGLVPGRQYEVEVIVES 670
Cdd:pfam00041    1 SAPSNLTVTDVTS-TSLTVSWTPPPdgnGPITGYEVEYRpkNSGEPWNEITVPGTTTSVTL--TGLKPGTEYEVRVQAVN 77


                   ..
gi 578824049   671 GN 672
Cdd:pfam00041   78 GG 79

FN3

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

507-582

1.09e-07

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 51.73 E-value: 1.09e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049  507 PMEVSNLKVTNDGSlTSLKVKWQRPP---GNVDSYNITLSHKGTIKESRVLAPWITETHF--KELVPGRLYQVTVSCVSG 581
Cdd:cd00063     1 PSPPTNLRVTDVTS-TSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYtlTGLKPGTEYEFRVRAVNG 79


                  .
gi 578824049  582 E 582
Cdd:cd00063    80 G 80

FN3

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

1573-1661

4.21e-07

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 49.80 E-value: 4.21e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1573 PDKIQNLHCRPQNSTAIACSWIPPDSD---FDGYSIECRKMDTQEVEFSRKLEKEKSLLNIMMLVPHKRYLVSIKVQSAG 1649
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDggpITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|..
gi 578824049 1650 MTSEVVEDSTIT 1661
Cdd:cd00063    81 GESPPSESVTVT 92

FN3

Fibronectin type 3 domain [General function prediction only];

1093-1508

4.29e-07

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 55.39 E-value: 4.29e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1093 FTSLTPGRQYKILVLTISGDVQQSAFIEGFTVPSAVKNIHISPNGATDSLTVNWTPGGGDVDSYTVSAFRHSQKVDSQTI 1172
Cdd:COG3401   108 NTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTV 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1173 PKHVFEHTFHRLEAGEQYQIMIASVS----GSLKNQINVV-GRTVPASVQGVIADNAYSSySLIVSWQKAAGV-AERYDI 1246
Cdd:COG3401   188 TSTTLVDGGGDIEPGTTYYYRVAATDtggeSAPSNEVSVTtPTTPPSAPTGLTATADTPG-SVTLSWDPVTESdATGYRV 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1247 LL-LTENGillrNTSEPATTKQHKFED--LTPGKKYKIQILTVSG----GLFSKEAQ-TEGRTVPAAVTDLRITENSTRH 1318
Cdd:COG3401   267 YRsNSGDG----PFTKVATVTTTSYTDtgLTNGTTYYYRVTAVDAagneSAPSNVVSvTTDLTPPAAPSGLTATAVGSSS 342

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1319 LSFRWTASEGE-LSWYNIflY---NPDGNLQERAQVDPlVQSFSFQNLLQGRM--YKMVIVTHSGELSNESF-IFGRTVP 1391
Cdd:COG3401   343 ITLSWTASSDAdVTGYNV--YrstSGGGTYTKIAETVT-TTSYTDTGLTPGTTyyYKVTAVDAAGNESAPSEeVSATTAS 419

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1392 ASVS-HLRGSNRNTTDSLWFNWSPASGDFDFYELILYNPNGTKKENWKDKDLTEW----RFQGLVPGRKYVLWVVTHSGD 1466
Cdd:COG3401   420 AASGeSLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSstvtATTTDTTTANLSVTTGSLVGG 499

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 578824049 1467 LSNKVTAESRTAPSPPSLMSFADIANTSLAITWKGPPDWTDY 1508
Cdd:COG3401   500 SGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGAS 541

FN3

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

328-410

7.39e-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: 7.39e-07

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049    328 PLPPARFGVSKekTTSTSLHVWWT-PSSGKVTSYEVQLFDENNQK-IQGVQIQESTSWNEYTFFNLTAGSKYNIAITAVS 405
Cdd:smart00060    1 PSPPSNLRVTD--VTSTSVTLSWEpPPDDGITGYIVGYRVEYREEgSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78


                    ....*
gi 578824049    406 GGKRS 410
Cdd:smart00060   79 GAGEG 83

fn3

Fibronectin type III domain;

1305-1378

9.04e-07

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 48.57 E-value: 9.04e-07

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578824049  1305 AVTDLRITENSTRHLSFRWTASE---GELSWYNIFLYNPDGNLQERAQVDPLVQ-SFSFQNLLQGRMYKMVIVTHSGE 1378
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNEITVPGTTtSVTLTGLKPGTEYEVRVQAVNGG 79

fn3

Fibronectin type III domain;

509-582

1.43e-06

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 48.18 E-value: 1.43e-06

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578824049   509 EVSNLKVTNDGSlTSLKVKWQRPP---GNVDSYNITLSHKGTIKE--SRVLAPWITETHFKELVPGRLYQVTVSCVSGE 582
Cdd:pfam00041    2 APSNLTVTDVTS-TSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPwnEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

fn3

Fibronectin type III domain;

774-847

3.80e-06

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 47.02 E-value: 3.80e-06

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578824049   774 QVTDLHVANQGmTSSLFTNWT---QAQGDVEFYQVLLIHENV--VIKNESISSETSRYSFHSLKSGSLYSVVVTTVSGG 847
Cdd:pfam00041    2 APSNLTVTDVT-STSLTVSWTpppDGNGPITGYEVEYRPKNSgePWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

FN3

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

1479-1571

1.17e-05

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 45.95 E-value: 1.17e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1479 PSPPSLMSFADIANTSLAITWKGPPDWTDYND-FELQWLPRDALTVFNPYNNRKSEGR-IVYGLRPGRSYQFNVKTVSGD 1556
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITgYVVEYREKGSGDWKEVEVTPGSETSyTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|....*
gi 578824049 1557 SWKTYSKPIfgSVRT 1571
Cdd:cd00063    81 GESPPSESV--TVTT 93

FN3

Fibronectin type 3 domain [General function prediction only];

302-452

1.73e-05

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 50.00 E-value: 1.73e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049  302 DLQAGTIYNFRIISLDEERT---------VVLQTDPLPPArfGVSKEKTTSTSLHVWWTPSSGK-VTSYEVQLFDENNQK 371
Cdd:COG3401   198 DIEPGTTYYYRVAATDTGGEsapsnevsvTTPTTPPSAPT--GLTATADTPGSVTLSWDPVTESdATGYRVYRSNSGDGP 275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049  372 IqgVQIQESTSwNEYTFFNLTAGSKYNIAITAV-SGGKRS-FSVY---TNGSTVPSPVKDI-GISTKANSLLISWSHGSG 445
Cdd:COG3401   276 F--TKVATVTT-TSYTDTGLTNGTTYYYRVTAVdAAGNESaPSNVvsvTTDLTPPAAPSGLtATAVGSSSITLSWTASSD 352


                  ....*...
gi 578824049  446 -NVERYRL 452
Cdd:COG3401   353 aDVTGYNV 360

FN3

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

1479-1558

3.66e-05

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 44.14 E-value: 3.66e-05

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049   1479 PSPPSLMSFADIANTSLAITWKGPPD--WTDYND-FELQWLPRDALTVFNPYNNRKSEGRIVyGLRPGRSYQFNVKTVSG 1555
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDdgITGYIVgYRVEYREEGSEWKEVNVTPSSTSYTLT-GLKPGTEYEFRVRAVNG 79


                    ...
gi 578824049   1556 DSW 1558
Cdd:smart00060   80 AGE 82

FN3

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

507-581

6.52e-05

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 43.37 E-value: 6.52e-05

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049    507 PMEVSNLKVTNDGSlTSLKVKWQRPP-GNVDSYNITLSHKGTIKESRVL----APWITETHFKELVPGRLYQVTVSCVSG 581
Cdd:smart00060    1 PSPPSNLRVTDVTS-TSVTLSWEPPPdDGITGYIVGYRVEYREEGSEWKevnvTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

FN3

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

595-672

6.79e-05

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 43.37 E-value: 6.79e-05

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049    595 PDKVANLEANNNGRmRSLVVSWSPPAGDWE-----QYRILLFNDSVVLLNITVGKEETQYVmdDTGLVPGRQYEVEVIVE 669
Cdd:smart00060    1 PSPPSNLRVTDVTS-TSVTLSWEPPPDDGItgyivGYRVEYREEGSEWKEVNVTPSSTSYT--LTGLKPGTEYEFRVRAV 77


                    ...
gi 578824049    670 SGN 672
Cdd:smart00060   78 NGA 80

FN3

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

1125-1199

8.34e-05

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 43.25 E-value: 8.34e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1125 PSAVKNIHISPNGATdSLTVNWTP---GGGDVDSYTVSaFRHSQKVDSQTIPKHVF---EHTFHRLEAGEQYQIMIASVS 1198
Cdd:cd00063     1 PSPPTNLRVTDVTST-SVTLSWTPpedDGGPITGYVVE-YREKGSGDWKEVEVTPGsetSYTLTGLKPGTEYEFRVRAVN 78


                  .
gi 578824049 1199 G 1199
Cdd:cd00063    79 G 79

fn3

Fibronectin type III domain;

255-316

2.18e-04

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 42.02 E-value: 2.18e-04

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578824049   255 SSHSVSIQWRIL----GSPCNFSLIYSSDTLGAALcPTFRIDNTTYGCNLQDLQAGTIYNFRIISL 316
Cdd:pfam00041   12 TSTSLTVSWTPPpdgnGPITGYEVEYRPKNSGEPW-NEITVPGTTTSVTLTGLKPGTEYEVRVQAV 76

FN3

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

949-1026

2.21e-04

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 42.10 E-value: 2.21e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049  949 PDKVQGVSVSNSArSDYLRVSWVHATGD---FDHYEVTIKNKN--NFIQTKSIPKSENECVFVQLVPGRLYSVTVTTKSG 1023
Cdd:cd00063     1 PSPPTNLRVTDVT-STSVTLSWTPPEDDggpITGYVVEYREKGsgDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79


                  ...
gi 578824049 1024 QYE 1026
Cdd:cd00063    80 GGE 82

FN3

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

1037-1112

2.44e-04

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 42.10 E-value: 2.44e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1037 PEPVKDLTLRNRSTEDLHVTWS---GANGDVDQYEIQL---LFNDMKVFPPFhlVNTATEYRFTSLTPGRQYKILVLTIS 1110
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTppeDDGGPITGYVVEYrekGSGDWKEVEVT--PGSETSYTLTGLKPGTEYEFRVRAVN 78


                  ..
gi 578824049 1111 GD 1112
Cdd:cd00063    79 GG 80

Ricin_B_lectin

pfam00652

Ricin-type beta-trefoil lectin domain;

22-93

4.52e-04

Ricin-type beta-trefoil lectin domain;

Pssm-ID: 395527 [Multi-domain] Cd Length: 126 Bit Score: 42.13 E-value: 4.52e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049    22 QIVHVQKQQCL-----FKNEKVVVGSCNRTIQNQQWMWTED-EKLLHVKSALCLAISNSSRGPSRsAILDRC-----SQa 90
Cdd:pfam00652   47 TIRSVASDLCLdvgstADGAKVVLWPCHPGNGNQRWRYDEDgTQIRNPQSGKCLDVSGAGTSNGK-VILWTCdsgnpNQ- 124


                   ...
gi 578824049    91 pRW 93
Cdd:pfam00652  125 -QW 126

fn3

Fibronectin type III domain;

422-488

9.47e-04

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 40.09 E-value: 9.47e-04

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578824049   422 SPVKDIGISTK-ANSLLISWS---HGSGNVERYRLML--MDKGILVHGGVVDKHATSYAFHGLTPGYLYNLTV 488
Cdd:pfam00041    1 SAPSNLTVTDVtSTSLTVSWTpppDGNGPITGYEVEYrpKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRV 73

FN3

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

949-1024

9.73e-04

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 39.91 E-value: 9.73e-04

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049    949 PDKVQGVSVSNSArSDYLRVSWVH-----ATGDFDHYEVTIKNKNNFIQTKSIPKSENECVFVQLVPGRLYSVTVTTKSG 1023
Cdd:smart00060    1 PSPPSNLRVTDVT-STSVTLSWEPppddgITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79


                    .
gi 578824049   1024 Q 1024
Cdd:smart00060   80 A 80

FN3

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

595-672

9.86e-04

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 40.17 E-value: 9.86e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049  595 PDKVANLEANNNGRmRSLVVSWSPPAGD---WEQYRILLF---NDSVVLLNITVGKEeTQYVMddTGLVPGRQYEVEVIV 668
Cdd:cd00063     1 PSPPTNLRVTDVTS-TSVTLSWTPPEDDggpITGYVVEYRekgSGDWKEVEVTPGSE-TSYTL--TGLKPGTEYEFRVRA 76


                  ....
gi 578824049  669 ESGN 672
Cdd:cd00063    77 VNGG 80

FN3

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

1037-1111

1.07e-03

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 39.91 E-value: 1.07e-03

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049   1037 PEPVKDLTLRNRSTEDLHVTWS-----GANGDVDQYEIQLLFNDMKVFPpFHLVNTATEYRFTSLTPGRQYKILVLTISG 1111
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEpppddGITGYIVGYRVEYREEGSEWKE-VNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

FN3

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

685-758

1.13e-03

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 39.91 E-value: 1.13e-03

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578824049    685 PLAVLQLRVKHANETSLSIMWQTPVAEWE-----KYIISLADRDLLLIHKSLSKDAKEFTFTDLVPGRKYMATVTSISG 758
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItgyivGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

FN3

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

1125-1199

1.47e-03

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 39.52 E-value: 1.47e-03

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049   1125 PSAVKNIHISPNGATdSLTVNWTP-----GGGDVDSYTVSAFRHSQKVDSQTIPKHVFEHTFHRLEAGEQYQIMIASVSG 1199
Cdd:smart00060    1 PSPPSNLRVTDVTST-SVTLSWEPppddgITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

FN3

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

685-770

2.78e-03

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 39.02 E-value: 2.78e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049  685 PLAVLQLRVKHANETSLSIMWQTPV---AEWEKYIISL--ADRDLLLIHKSLSKDAKEFTFTDLVPGRKYMATVTSISGD 759
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYreKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|...
gi 578824049  760 L--KNSSSVKGRT 770
Cdd:cd00063    81 GesPPSESVTVTT 93

FN3

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

1391-1465

3.55e-03

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 38.36 E-value: 3.55e-03

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049   1391 PASVSHLRGSNrNTTDSLWFNWSPASGDFDFYELILYNP-NGTKKENWK----DKDLTEWRFQGLVPGRKYVLWVVTHSG 1465
Cdd:smart00060    1 PSPPSNLRVTD-VTSTSVTLSWEPPPDDGITGYIVGYRVeYREEGSEWKevnvTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

RICIN

smart00458

Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.

22-94

5.59e-03

Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.

Pssm-ID: 214672 [Multi-domain] Cd Length: 118 Bit Score: 39.03 E-value: 5.59e-03

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578824049     22 QIVHVQKQQCLF----KNEKVVVGSCNRTIQNQQWMWTEDEKLLHVKSALCLAISNSSrgPSRSAILDRCSQAP--RWT 94
Cdd:smart00458   40 AIRIKDTDLCLTangnTGSTVTLYSCDGTNDNQYWEVNKDGTIRNPDSGKCLDVKDGN--TGTKVILWTCSGNPnqKWI 116

FN3

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

861-936

7.54e-03

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 37.59 E-value: 7.54e-03

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049    861 PSSVSGVTVNNSGRNdYLSVSWLLAPGD-----VDNYEVTLSHDGKVVQSLVIAKSVRECSFSSLTPGRLYTVTITTRSG 935
Cdd:smart00060    1 PSPPSNLRVTDVTST-SVTLSWEPPPDDgitgyIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79


                    .
gi 578824049    936 K 936
Cdd:smart00060   80 A 80

FN3

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

861-938

8.20e-03

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 37.86 E-value: 8.20e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049  861 PSSVSGVTVNNSGRNdYLSVSWLLAPGD---VDNYEVTLS--HDGKVVQSLVIAKSVRECSFSSLTPGRLYTVTITTRSG 935
Cdd:cd00063     1 PSPPTNLRVTDVTST-SVTLSWTPPEDDggpITGYVVEYRekGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79


                  ...
gi 578824049  936 KYE 938
Cdd:cd00063    80 GGE 82

FN3

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

421-491

8.48e-03

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 37.21 E-value: 8.48e-03

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578824049    421 PSPVKDIGIS-TKANSLLISWSH-----GSGNVERYRLMLMDKGILVHGGVVDKHATSYAFHGLTPGYLYNLTVMTE 491
Cdd:smart00060    1 PSPPSNLRVTdVTSTSVTLSWEPppddgITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77

Name

Accession

Description

Interval

E-value

R-PTPc-B

cd14617

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

1949-2176

4.44e-178

Pssm-ID: 350465 [Multi-domain] Cd Length: 228 Bit Score: 541.43 E-value: 4.44e-178

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1949 NRYNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 2028
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2029 KCDHYWPADQDSLYYGDLILQMLSESVLPEWTIREFKICGEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDY 2108
Cdd:cd14617    81 KCDHYWPADQDSLYYGDLIVQMLSESVLPEWTIREFKICSEEQLDAPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVRDY 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578824049 2109 INRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 2176
Cdd:cd14617   161 INRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228

R3-PTPc

cd14548

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

1950-2176

1.25e-142

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: 442.56 E-value: 1.25e-142

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1950 RYNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVK 2029
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2030 CDHYWPADQDSLYYGDLILQMLSESVLPEWTIREFKICGEEQldaHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDYI 2109
Cdd:cd14548    81 CDHYWPFDQDPVYYGDITVTMLSESVLPDWTIREFKLERGDE---VRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYI 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578824049 2110 NRspGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 2176
Cdd:cd14548   158 KQ--EKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222

PTPc

smart00194

Protein tyrosine phosphatase, catalytic domain;

1920-2178

9.68e-116

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 367.37 E-value: 9.68e-116

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049   1920 LLSKEYEELKDVGR-NQSCDIALLPENRGKNRYNNILPYDATRVKLSNvDDDPCSDYINASYIPGNNFRREYIVTQGPLP 1998
Cdd:smart00194    1 GLEEEFEKLDRLKPdDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKP-PPGEGSDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049   1999 GTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPADQ-DSLYYGDLILQMLSESVLPEWTIREFKICGEEQlDAHRL 2077
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEgEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGC-SETRT 158

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049   2078 IRHFHYTVWPDHGVPETTQSLIQFVRTVRDYinRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDL 2157
Cdd:smart00194  159 VTHYHYTNWPDHGVPESPESILDLIRAVRKS--QSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKEL 236

                           250       260
                    ....*....|....*....|.
gi 578824049   2158 RLHRVHMVQTECQYVYLHQCV 2178
Cdd:smart00194  237 RSQRPGMVQTEEQYIFLYRAI 257

R-PTPc-J

cd14615

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

1949-2180

4.19e-112

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: 355.66 E-value: 4.19e-112

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1949 NRYNNILPYDATRVKLSNvDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 2028
Cdd:cd14615     1 NRYNNVLPYDISRVKLSV-QSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2029 KCDHYWPADQdSLYYGDLILQMLSESVLPEWTIREFKICGEEQLDAHRlIRHFHYTVWPDHGVPETTQSLIQFVRTVRDY 2108
Cdd:cd14615    80 KCEEYWPSKQ-KKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRT-VRHFHFTSWPDHGVPETTDLLINFRHLVREY 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578824049 2109 INRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRD 2180
Cdd:cd14615   158 MKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229

R-PTPc-O

cd14614

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

1938-2179

4.04e-104

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: 333.39 E-value: 4.04e-104

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1938 DIALLPENRGKNRYNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIV 2017
Cdd:cd14614     5 FAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2018 MVTQCVEKGRVKCDHYWPADQDSLYYGDLILQMLSESVLPEWTIREFKIcgeEQLDAHRLIRHFHYTVWPDHGVP--ETT 2095
Cdd:cd14614    85 MLTQCNEKRRVKCDHYWPFTEEPVAYGDITVEMLSEEEQPDWAIREFRV---SYADEVQDVMHFNYTAWPDHGVPtaNAA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2096 QSLIQFVRTVRDYINRSPgaGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 2175
Cdd:cd14614   162 ESILQFVQMVRQQAVKSK--GPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIH 239


                  ....
gi 578824049 2176 QCVR 2179
Cdd:cd14614   240 QCVQ 243

Y_phosphatase

pfam00102

Protein-tyrosine phosphatase;

1945-2178

3.09e-101

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 324.97 E-value: 3.09e-101

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049  1945 NRGKNRYNNILPYDATRVKLSnvDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVE 2024
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049  2025 KGRVKCDHYWP-ADQDSLYYGDL-ILQMLSESVLPEWTIREFKICgEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFV 2102
Cdd:pfam00102   79 KGREKCAQYWPeEEGESLEYGDFtVTLKKEKEDEKDYTVRTLEVS-NGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLL 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578824049  2103 RTVRDYiNRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 2178
Cdd:pfam00102  158 RKVRKS-SLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232

R-PTPc-H

cd14619

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

1949-2182

3.08e-99

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: 319.14 E-value: 3.08e-99

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1949 NRYNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 2028
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2029 KCDHYWPADQDSLYYGDLILQMLSESVLPEWTIREFKICGEEQlDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDY 2108
Cdd:cd14619    81 KCEHYWPLDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEE-QKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQW 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578824049 2109 INRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRDVL 2182
Cdd:cd14619   160 LDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233

R-PTPc-V

cd14618

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

1949-2178

1.08e-96

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: 311.49 E-value: 1.08e-96

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1949 NRYNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 2028
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2029 KCDHYWPADQDSLYYGDLILQMLSESVLPEWTIREFKIcGEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDY 2108
Cdd:cd14618    81 LCDHYWPSESTPVSYGHITVHLLAQSSEDEWTRREFKL-WHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVREH 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2109 INRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 2178
Cdd:cd14618   160 VQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCI 229

R-PTPc-LAR-1

cd14553

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

1945-2178

7.41e-90

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: 292.38 E-value: 7.41e-90

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1945 NRGKNRYNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVE 2024
Cdd:cd14553     3 NKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2025 KGRVKCDHYWPADqDSLYYGDLILQMLSESVLPEWTIREFKICGEEQLDaHRLIRHFHYTVWPDHGVPETTQSLIQFVRT 2104
Cdd:cd14553    83 RSRVKCDQYWPTR-GTETYGLIQVTLLDTVELATYTVRTFALHKNGSSE-KREVRQFQFTAWPDHGVPEHPTPFLAFLRR 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578824049 2105 VRDYinRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 2178
Cdd:cd14553   161 VKAC--NPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDAL 232

PTPc

cd00047

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

1975-2176

8.19e-89

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: 287.64 E-value: 8.19e-89

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1975 YINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDS-LYYGDLILQMLSE 2053
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKpLEYGDITVTLVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2054 SVLPEWTIREFKICGEEQlDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDYinRSPGAGPTVVHCSAGVGRTGTFI 2133
Cdd:cd00047    81 EELSDYTIRTLELSPKGC-SESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKE--ARKPNGPIVVHCSAGVGRTGTFI 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 578824049 2134 ALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 2176
Cdd:cd00047   158 AIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200

PTPc-N9

cd14543

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

1923-2175

3.17e-84

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: 277.71 E-value: 3.17e-84

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1923 KEYEELKDVGRNQSCDIALLPENRGKNRYNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKD 2002
Cdd:cd14543     7 EEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2003 DFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDS-LYYGDLILQMLSESVLPEWTIREFKICGEEQlDAHRLIRHF 2081
Cdd:cd14543    87 DFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSsLRYGDLTVTNLSVENKEHYKKTTLEIHNTET-DESRQVTHF 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2082 HYTVWPDHGVPETTQSLIQFVRTVRDYINRS-----------PGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDI 2150
Cdd:cd14543   166 QFTSWPDFGVPSSAAALLDFLGEVRQQQALAvkamgdrwkghPPGPPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNV 245

                         250       260
                  ....*....|....*....|....*
gi 578824049 2151 YGAVHDLRLHRVHMVQTECQYVYLH 2175
Cdd:cd14543   246 MQTVRRMRTQRAFSIQTPDQYYFCY 270

R5-PTPc-1

cd14549

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

1975-2175

3.55e-83

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: 271.92 E-value: 3.55e-83

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1975 YINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPADqDSLYYGDLILQMLSES 2054
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKE-GTETYGNIQVTLLSTE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2055 VLPEWTIREF-----KICGEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDYinRSPGAGPTVVHCSAGVGRT 2129
Cdd:cd14549    80 VLATYTVRTFslknlKLKKVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAA--NPPGAGPIVVHCSAGVGRT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 578824049 2130 GTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 2175
Cdd:cd14549   158 GTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203

R-PTPc-Q

cd14616

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

1949-2176

6.20e-82

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: 269.08 E-value: 6.20e-82

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1949 NRYNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 2028
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2029 KCDHYWPADQDSL-YYGDLILQMLSESVLPEWTIREFKIcgeEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRd 2107
Cdd:cd14616    81 RCHQYWPEDNKPVtVFGDIVITKLMEDVQIDWTIRDLKI---ERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVR- 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578824049 2108 yINRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 2176
Cdd:cd14616   157 -ASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224

R-PTPc-F-1

cd14626

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

1909-2178

1.59e-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: 253.03 E-value: 1.59e-75

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1909 HFMKLQADSNYLLSKEYEELkDVGRNQSCDIALLPENRGKNRYNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRR 1988
Cdd:cd14626     6 NIERLKANDGLKFSQEYESI-DPGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYRKQN 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1989 EYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPAdQDSLYYGDLILQMLSESVLPEWTIREFKICg 2068
Cdd:cd14626    85 AYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPI-RGTETYGMIQVTLLDTVELATYSVRTFALY- 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2069 EEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRdyINRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSV 2148
Cdd:cd14626   163 KNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVK--ACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTV 240

                         250       260       270
                  ....*....|....*....|....*....|
gi 578824049 2149 DIYGAVHDLRLHRVHMVQTECQYVYLHQCV 2178
Cdd:cd14626   241 DIYGHVTCMRSQRNYMVQTEDQYIFIHEAL 270

R-PTPc-T-1

cd14630

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

1944-2178

9.24e-75

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: 249.17 E-value: 9.24e-75

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1944 ENRGKNRYNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCV 2023
Cdd:cd14630     2 ENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2024 EKGRVKCDHYWPADQDslYYGDLILQMLSESVLPEWTIREFKICGEEQLDAhRLIRHFHYTVWPDHGVPETTQSLIQFVR 2103
Cdd:cd14630    82 EVGRVKCVRYWPDDTE--VYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEI-REIRQFHFTSWPDHGVPCYATGLLGFVR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578824049 2104 TVRdYINrSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 2178
Cdd:cd14630   159 QVK-FLN-PPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAI 231

R-PTPc-G-1

cd17667

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

1922-2182

2.82e-74

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: 249.18 E-value: 2.82e-74

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1922 SKEYEELK--DVGRNQSCDIALLPENRGKNRYNNILPYDATRVKLSNV--DDDPCSDYINASYIPGNNFRREYIVTQGPL 1997
Cdd:cd17667     2 SEDFEEVQrcTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLpgKDSKHSDYINANYVDGYNKAKAYIATQGPL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1998 PGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPAdQDSLYYGDLILQMLSESVLPEWTIREFKICGEEQLDAH-- 2075
Cdd:cd17667    82 KSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPT-ENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKVKKGQkg 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2076 --------RLIRHFHYTVWPDHGVPETTQSLIQFVRtvRDYINRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDS 2147
Cdd:cd17667   161 npkgrqneRTVIQYHYTQWPDMGVPEYALPVLTFVR--RSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKST 238

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 578824049 2148 VDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRDVL 2182
Cdd:cd17667   239 VNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAI 273

PTPc-KIM

cd14547

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

1949-2176

4.60e-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: 246.54 E-value: 4.60e-74

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1949 NRYNNILPYDATRVKLSNVDDDPCSDYINASYIPG-NNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKgR 2027
Cdd:cd14547     1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGyDGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA-K 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2028 VKCDHYWPADQDSLYyGDLILQMLSESVLPEWTIREFKI-CGEEQldahRLIRHFHYTVWPDHGVPETTQSLIQFVRTVR 2106
Cdd:cd14547    80 EKCAQYWPEEENETY-GDFEVTVQSVKETDGYTVRKLTLkYGGEK----RYLKHYWYTSWPDHKTPEAAQPLLSLVQEVE 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2107 DYINRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 2176
Cdd:cd14547   155 EARQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224

PTPc-N11_6

cd14544

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

1945-2178

8.36e-73

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: 243.91 E-value: 8.36e-73

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1945 NRGKNRYNNILPYDATRVKLSNVDDD-PCSDYINASYI-PGNNFRRE------YIVTQGPLPGTKDDFWKMVWEQNVHNI 2016
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKDRDPNvPGSDYINANYIrNENEGPTTdenaktYIATQGCLENTVSDFWSMVWQENSRVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2017 VMVTQCVEKGRVKCDHYWPADQDSLYYGDLILQMLSESVLPEWTIREFKICGEEQLDAHRLIRHFHYTVWPDHGVPETTQ 2096
Cdd:cd14544    81 VMTTKEVERGKNKCVRYWPDEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDPIREIWHYQYLSWPDHGVPSDPG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2097 SLIQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKD---SVDIYGAVHDLRLHRVHMVQTECQYVY 2173
Cdd:cd14544   161 GVLNFLEDVNQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRSGMVQTEAQYKF 240


                  ....*
gi 578824049 2174 LHQCV 2178
Cdd:cd14544   241 IYVAV 245

R-PTPc-A-1

cd14621

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

1894-2178

7.32e-72

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: 243.01 E-value: 7.32e-72

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1894 NRKTScPIKINQFEGHFMKLQADSNYLLSKEYEELKDVGRNQSCDIALLPENRGKNRYNNILPYDATRVKLSNVDDDPCS 1973
Cdd:cd14621     2 NRKYP-PLPVDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1974 DYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPaDQDSLYYGDLILQMLSE 2053
Cdd:cd14621    81 DYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWP-DQGCWTYGNIRVSVEDV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2054 SVLPEWTIREFkiCGEEQLDA-----HRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRdyiNRSPG-AGPTVVHCSAGVG 2127
Cdd:cd14621   160 TVLVDYTVRKF--CIQQVGDVtnkkpQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVK---NCNPQyAGAIVVHCSAGVG 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578824049 2128 RTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 2178
Cdd:cd14621   235 RTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQAL 285

R-PTP-LAR-2

cd14554

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

1940-2176

8.67e-72

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: 240.50 E-value: 8.67e-72

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1940 ALLPENRGKNRYNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMV 2019
Cdd:cd14554     1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2020 TQCVEKGRVKCDHYWPADQdSLYYGDLILQMLSESVLPEWTIREFKICgEEQLDAHRLIRHFHYTVWPDHGVPETTQSLI 2099
Cdd:cd14554    81 TKLREMGREKCHQYWPAER-SARYQYFVVDPMAEYNMPQYILREFKVT-DARDGQSRTVRQFQFTDWPEQGVPKSGEGFI 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578824049 2100 QFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 2176
Cdd:cd14554   159 DFIGQVHKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYR 235

R-PTPc-M-1

cd14633

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

1909-2178

1.17e-70

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: 238.79 E-value: 1.17e-70

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1909 HFMKLQADSNYLLSKEYEELKDvGRNQSCDIALLPENRGKNRYNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRR 1988
Cdd:cd14633     5 HITQMKCAEGYGFKEEYESFFE-GQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYHRPN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1989 EYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDslYYGDLILQMLSESVLPEWTIREFKIcg 2068
Cdd:cd14633    84 HYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTE--IYKDIKVTLIETELLAEYVIRTFAV-- 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2069 eEQLDAH--RLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDyiNRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKD 2146
Cdd:cd14633   160 -EKRGVHeiREIRQFHFTGWPDHGVPYHATGLLGFVRQVKS--KSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREG 236

                         250       260       270
                  ....*....|....*....|....*....|..
gi 578824049 2147 SVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 2178
Cdd:cd14633   237 VVDIYNCVRELRSRRVNMVQTEEQYVFIHDAI 268

R-PTPc-D-1

cd14624

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

1900-2178

2.58e-70

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: 238.09 E-value: 2.58e-70

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1900 PIKINQFEGHFMKLQADSNYLLSKEYEELkDVGRNQSCDIALLPENRGKNRYNNILPYDATRVKLSNVDDDPCSDYINAS 1979
Cdd:cd14624     3 PIPILELADHIERLKANDNLKFSQEYESI-DPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINAN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1980 YIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPAdQDSLYYGDLILQMLSESVLPEW 2059
Cdd:cd14624    82 YIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPS-RGTETYGLIQVTLLDTVELATY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2060 TIREFKICgEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRdyINRSPGAGPTVVHCSAGVGRTGTFIALDRIL 2139
Cdd:cd14624   161 CVRTFALY-KNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVK--TCNPPDAGPMVVHCSAGVGRTGCFIVIDAML 237

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 578824049 2140 QQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 2178
Cdd:cd14624   238 ERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDAL 276

R-PTPc-S-1

cd14625

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

1900-2178

1.05e-69

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: 236.53 E-value: 1.05e-69

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1900 PIKINQFEGHFMKLQADSNYLLSKEYEELkDVGRNQSCDIALLPENRGKNRYNNILPYDATRVKLSNVDDDPCSDYINAS 1979
Cdd:cd14625     3 PIPISELAEHTERLKANDNLKLSQEYESI-DPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINAN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1980 YIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPaDQDSLYYGDLILQMLSESVLPEW 2059
Cdd:cd14625    82 YIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWP-SRGTETYGMIQVTLLDTIELATF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2060 TIREFKIcGEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRdyINRSPGAGPTVVHCSAGVGRTGTFIALDRIL 2139
Cdd:cd14625   161 CVRTFSL-HKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVK--TCNPPDAGPIVVHCSAGVGRTGCFIVIDAML 237

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 578824049 2140 QQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 2178
Cdd:cd14625   238 ERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDAL 276

beta-trefoil_Ricin_PTPRB-like

cd23409

ricin B-type lectin domain, beta-trefoil fold, found in receptor-type tyrosine-protein ...

18-134

1.15e-69

Pssm-ID: 467787 Cd Length: 117 Bit Score: 229.25 E-value: 1.15e-69

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049   18 SEGFQIVHVQKQQCLFKNEKVVVGSCNRTIQNQQWMWTEDEKLLHVKSALCLAISNSSRGPSRSAILDRCSQAPRWTCYD 97
Cdd:cd23409     1 SEGFLILHVQKQQCLFGNKTVSVGKCNATSPNQQWQWTEDGKLLHVKSGQCLGISNSSAFHSRRAILLDCSQAPRWTCHE 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 578824049   98 QEGFLEVENASLFLQKQGSRVVVKKARKYLHSWMKID 134
Cdd:cd23409    81 NEGLLEVANSSLFLTKQGQRVVVKQGKKYLHNWMKYE 117

PTP_fungal

cd18533

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

1975-2176

1.13e-67

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

Pssm-ID: 350509 [Multi-domain] Cd Length: 212 Bit Score: 227.52 E-value: 1.13e-67

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1975 YINASYI-PGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDSLYYGDLILQMLSE 2053
Cdd:cd18533     1 YINASYItLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEYGDLTVELVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2054 SVLPEW--TIREFKICGEEQldAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGT 2131
Cdd:cd18533    81 EENDDGgfIVREFELSKEDG--KVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSASLDPPIIVHCSAGVGRTGT 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578824049 2132 FIALDRILQQLDS--------KDSVD-IYGAVHDLRLHRVHMVQTECQYVYLHQ 2176
Cdd:cd18533   159 FIALDSLLDELKRglsdsqdlEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212

PTPc-N1

cd14608

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

1925-2174

5.33e-67

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: 228.37 E-value: 5.33e-67

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1925 YEELKDVGRNQSCDIALLPENRGKNRYNNILPYDATRVKLSNvdddPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDF 2004
Cdd:cd14608     5 YQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQ----EDNDYINASLIKMEEAQRSYILTQGPLPNTCGHF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2005 WKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDS-LYYGD--LILQMLSESVLPEWTIREFKIcgeEQLDAH--RLIR 2079
Cdd:cd14608    81 WEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKeMIFEDtnLKLTLISEDIKSYYTVRQLEL---ENLTTQetREIL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2080 HFHYTVWPDHGVPETTQSLIQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSK---DSVDIYGAVHD 2156
Cdd:cd14608   158 HFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRkdpSSVDIKKVLLE 237

                         250       260
                  ....*....|....*....|
gi 578824049 2157 LRLHRVHMVQT--ECQYVYL 2174
Cdd:cd14608   238 MRKFRMGLIQTadQLRFSYL 257

R-PTPc-E-1

cd14620

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

1951-2176

4.18e-66

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: 224.05 E-value: 4.18e-66

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1951 YNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKC 2030
Cdd:cd14620     1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2031 DHYWPaDQDSLYYGDLILQMLSESVLPEWTIREFkiCGEEQLD----AHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVR 2106
Cdd:cd14620    81 YQYWP-DQGCWTYGNIRVAVEDCVVLVDYTIRKF--CIQPQLPdgckAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVK 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578824049 2107 dyiNRSPG-AGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 2176
Cdd:cd14620   158 ---SVNPVhAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQ 225

PTPc-N6

cd14606

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

1943-2178

3.68e-65

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: 222.83 E-value: 3.68e-65

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1943 PENRGKNRYNNILPYDATRVKLSNVDDD-PCSDYINASYI------PGNNFRReYIVTQGPLPGTKDDFWKMVWEQNVHN 2015
Cdd:cd14606    16 PENKSKNRYKNILPFDHSRVILQGRDSNiPGSDYINANYVknqllgPDENAKT-YIASQGCLEATVNDFWQMAWQENSRV 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2016 IVMVTQCVEKGRVKCDHYWPADQDSLYYGDLILQMLSESVLPEWTIREFKICGEEQLDAHRLIRHFHYTVWPDHGVPETT 2095
Cdd:cd14606    95 IVMTTREVEKGRNKCVPYWPEVGMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGELIREIWHYQYLSWPDHGVPSEP 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2096 QSLIQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSK--DS-VDIYGAVHDLRLHRVHMVQTECQYV 2172
Cdd:cd14606   175 GGVLSFLDQINQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKglDCdIDIQKTIQMVRAQRSGMVQTEAQYK 254


                  ....*.
gi 578824049 2173 YLHQCV 2178
Cdd:cd14606   255 FIYVAI 260

R-PTPc-C-1

cd14557

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

1975-2176

7.15e-65

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: 219.31 E-value: 7.15e-65

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1975 YINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPA-DQDSLYYGDLILQMLSE 2053
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSmEEGSRAFGDVVVKINEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2054 SVLPEWTIREFKICGEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDYINRspGAGPTVVHCSAGVGRTGTFI 2133
Cdd:cd14557    81 KICPDYIIRKLNINNKKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNF--FSGPIVVHCSAGVGRTGTYI 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 578824049 2134 ALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 2176
Cdd:cd14557   159 GIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201

PTPc-N7

cd14612

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

1942-2175

1.61e-64

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: 220.09 E-value: 1.61e-64

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1942 LPENRGKNRYNNILPYDATRVKLSNV-DDDPCSDYINASYIPGNNFR-REYIVTQGPLPGTKDDFWKMVWEQNVHNIVMV 2019
Cdd:cd14612    12 IPGHASKDRYKTILPNPQSRVCLRRAgSQEEEGSYINANYIRGYDGKeKAYIATQGPMLNTVSDFWEMVWQEECPIIVMI 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2020 TQCVEKgRVKCDHYWPADQDSlyYGDLILQMLSESVLPEWTIREFKICGEEqldAHRLIRHFHYTVWPDHGVPETTQSLI 2099
Cdd:cd14612    92 TKLKEK-KEKCVHYWPEKEGT--YGRFEIRVQDMKECDGYTIRDLTIQLEE---ESRSVKHYWFSSWPDHQTPESAGPLL 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578824049 2100 QFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 2175
Cdd:cd14612   166 RLVAEVEESRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLH 241

R-PTPc-Z-1

cd17668

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

1975-2175

1.94e-64

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: 218.31 E-value: 1.94e-64

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1975 YINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPADqDSLYYGDLILQMLSES 2054
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPAD-GSEEYGNFLVTQKSVQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2055 VLPEWTIREF-------KICGEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDyiNRSPGAGPTVVHCSAGVG 2127
Cdd:cd17668    80 VLAYYTVRNFtlrntkiKKGSQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASY--AKRHAVGPVVVHCSAGVG 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 578824049 2128 RTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 2175
Cdd:cd17668   158 RTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 205

PTPc-N20_13

cd14538

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

1975-2182

2.61e-64

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: 217.63 E-value: 2.61e-64

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1975 YINASYI--PGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWP--ADQDSLYYGDLILQM 2050
Cdd:cd14538     1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPdsLNKPLICGGRLEVSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2051 LSESVLPEWTIREFKICGEEQLDAHRlIRHFHYTVWPDHGVPETTQSLIQFVRtvrdYINRSPGAGPTVVHCSAGVGRTG 2130
Cdd:cd14538    81 EKYQSLQDFVIRRISLRDKETGEVHH-ITHLNFTTWPDHGTPQSADPLLRFIR----YMRRIHNSGPIVVHCSAGIGRTG 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578824049 2131 TFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRDVL 2182
Cdd:cd14538   156 VLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207

PTPc-N18

cd14603

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

1943-2178

2.90e-64

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: 220.08 E-value: 2.90e-64

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1943 PENRGKNRYNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQC 2022
Cdd:cd14603    28 KENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMACRE 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2023 VEKGRVKCDHYWPADQDSLYYGDLILQMLSESVL-PEWTIREFKI--CGEEqldahRLIRHFHYTVWPDHGVPETTQSLI 2099
Cdd:cd14603   108 IEMGKKKCERYWAQEQEPLQTGPFTITLVKEKRLnEEVILRTLKVtfQKES-----RSVSHFQYMAWPDHGIPDSPDCML 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2100 QFVRTVRDYINRSPgaGPTVVHCSAGVGRTGTFIALDRILQQLDSK---DSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 2176
Cdd:cd14603   183 AMIELARRLQGSGP--EPLCVHCSAGCGRTGVICTVDYVRQLLLTQripPDFSIFDVVLEMRKQRPAAVQTEEQYEFLYH 260


                  ..
gi 578824049 2177 CV 2178
Cdd:cd14603   261 TV 262

PTPc-N2

cd14607

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

1933-2170

3.59e-64

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: 219.45 E-value: 3.59e-64

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1933 RNQSCD----IALLPENRGKNRYNNILPYDATRVKLSNVDDDpcsdYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMV 2008
Cdd:cd14607     8 RNESHDyphrVAKYPENRNRNRYRDVSPYDHSRVKLQNTEND----YINASLVVIEEAQRSYILTQGPLPNTCCHFWLMV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2009 WEQNVHNIVMVTQCVEKGRVKCDHYWPA-DQDSLYYGD--LILQMLSESVLPEWTIREFKI----CGEEqldahRLIRHF 2081
Cdd:cd14607    84 WQQKTKAVVMLNRIVEKDSVKCAQYWPTdEEEVLSFKEtgFSVKLLSEDVKSYYTVHLLQLeninSGET-----RTISHF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2082 HYTVWPDHGVPETTQSLIQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKD--SVDIYGAVHDLRL 2159
Cdd:cd14607   159 HYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRK 238

                         250
                  ....*....|.
gi 578824049 2160 HRVHMVQTECQ 2170
Cdd:cd14607   239 YRMGLIQTPDQ 249

PTPc-N1_2

cd14545

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

1948-2170

1.14e-63

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: 216.87 E-value: 1.14e-63

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1948 KNRYNNILPYDATRVKLSNVDDDpcSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGR 2027
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKLKQGD--NDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2028 VKCDHYWPADQDSLY---YGDLILQMLSESVLPEWTIREFKIcgeEQLDAH--RLIRHFHYTVWPDHGVPETTQSLIQFV 2102
Cdd:cd14545    79 IKCAQYWPQGEGNAMifeDTGLKVTLLSEEDKSYYTVRTLEL---ENLKTQetREVLHFHYTTWPDFGVPESPAAFLNFL 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2103 RTVRDYINRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKD--SVDIYGAVHDLRLHRVHMVQTECQ 2170
Cdd:cd14545   156 QKVRESGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNpsSVDVKKVLLEMRKYRMGLIQTPDQ 225

R-PTPc-typeIIb-1

cd14555

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

1975-2178

1.52e-63

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: 215.55 E-value: 1.52e-63

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1975 YINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDSlyYGDLILQMLSES 2054
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEV--YGDIKVTLVETE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2055 VLPEWTIREFKIcGEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRdyINRSPGAGPTVVHCSAGVGRTGTFIA 2134
Cdd:cd14555    79 PLAEYVVRTFAL-ERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVK--ASNPPSAGPIVVHCSAGAGRTGCYIV 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 578824049 2135 LDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 2178
Cdd:cd14555   156 IDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAI 199

R-PTPc-K-1

cd14631

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

1961-2178

9.80e-63

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: 213.73 E-value: 9.80e-63

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1961 RVKLSNVDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDs 2040
Cdd:cd14631     1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTE- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2041 lYYGDLILQMLSESVLPEWTIREFKIcGEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRdyINRSPGAGPTVV 2120
Cdd:cd14631    80 -VYGDFKVTCVEMEPLAEYVVRTFTL-ERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVK--LSNPPSAGPIVV 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578824049 2121 HCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 2178
Cdd:cd14631   156 HCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 213

PTPc-N3_4

cd14541

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

1974-2178

8.08e-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: 211.03 E-value: 8.08e-62

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1974 DYINASY----IPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDSLYYGDLILQ 2049
Cdd:cd14541     1 DYINANYvnmeIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETMQFGNLQIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2050 MLSESVLPEWTIREFKIC----GEEqldahRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDYinRSPGAGPTVVHCSAG 2125
Cdd:cd14541    81 CVSEEVTPSFAFREFILTntntGEE-----RHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQN--RVGMVEPTVVHCSAG 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 578824049 2126 VGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 2178
Cdd:cd14541   154 IGRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAI 206

PTPc-N13

cd14597

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

1944-2182

1.30e-61

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: 211.23 E-value: 1.30e-61

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1944 ENRGKNRYNNILPYDATRVKLSNVdddpcSDYINASYI--PGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQ 2021
Cdd:cd14597     2 ENRKKNRYKNILPYDTTRVPLGDE-----GGYINASFIkmPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2022 CVEKGRVKCDHYWPADQDSLYYGD--LILQMLSESVLPEWTIREFKIcGEEQLDAHRLIRHFHYTVWPDHGVPETTQSLI 2099
Cdd:cd14597    77 EVEGGKIKCQRYWPEILGKTTMVDnrLQLTLVRMQQLKNFVIRVLEL-EDIQTREVRHITHLNFTAWPDHDTPSQPEQLL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2100 QFVRTVRdYINRSpgaGPTVVHCSAGVGRTGTFIALDRILqQLDSKD-SVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 2178
Cdd:cd14597   156 TFISYMR-HIHKS---GPIITHCSAGIGRSGTLICIDVVL-GLISKDlDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVI 230


                  ....
gi 578824049 2179 RDVL 2182
Cdd:cd14597   231 LYVL 234

PTPc-N11

cd14605

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

1944-2179

1.48e-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: 209.10 E-value: 1.48e-60

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1944 ENRGKNRYNNILPYDATRVKLSNVD-DDPCSDYINASYI-PGNNF-------RREYIVTQGPLPGTKDDFWKMVWEQNVH 2014
Cdd:cd14605     1 ENKNKNRYKNILPFDHTRVVLHDGDpNEPVSDYINANIImPEFETkcnnskpKKSYIATQGCLQNTVNDFWRMVFQENSR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2015 NIVMVTQCVEKGRVKCDHYWPADQDSLYYGDLILQMLSESVLPEWTIREFKICGEEQLDAHRLIRHFHYTVWPDHGVPET 2094
Cdd:cd14605    81 VIVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYILRELKLSKVGQGNTERTVWQYHFRTWPDHGVPSD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2095 TQSLIQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKD---SVDIYGAVHDLRLHRVHMVQTECQY 2171
Cdd:cd14605   161 PGGVLDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGvdcDIDVPKTIQMVRSQRSGMVQTEAQY 240


                  ....*...
gi 578824049 2172 VYLHQCVR 2179
Cdd:cd14605   241 RFIYMAVQ 248

R-PTPc-U-1

cd14632

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

1975-2178

1.94e-60

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: 206.83 E-value: 1.94e-60

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1975 YINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDSlyYGDLILQMLSES 2054
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDT--YGDIKITLLKTE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2055 VLPEWTIREFKIcGEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDyiNRSPGAGPTVVHCSAGVGRTGTFIA 2134
Cdd:cd14632    79 TLAEYSVRTFAL-ERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKA--STPPDAGPVVVHCSAGAGRTGCYIV 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 578824049 2135 LDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 2178
Cdd:cd14632   156 LDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAI 199

R-PTP-S-2

cd14627

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

1940-2182

4.59e-60

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: 208.82 E-value: 4.59e-60

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1940 ALLPENRGKNRYNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMV 2019
Cdd:cd14627    48 ANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVML 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2020 TQCVEKGRVKCDHYWPADQdSLYYGDLILQMLSESVLPEWTIREFKICgEEQLDAHRLIRHFHYTVWPDHGVPETTQSLI 2099
Cdd:cd14627   128 TKLREMGREKCHQYWPAER-SARYQYFVVDPMAEYNMPQYILREFKVT-DARDGQSRTVRQFQFTDWPEQGVPKSGEGFI 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2100 QFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVR 2179
Cdd:cd14627   206 DFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAAL 285


                  ...
gi 578824049 2180 DVL 2182
Cdd:cd14627   286 EYL 288

R-PTP-D-2

cd14628

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

1940-2182

1.33e-59

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: 207.66 E-value: 1.33e-59

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1940 ALLPENRGKNRYNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMV 2019
Cdd:cd14628    47 ANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVML 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2020 TQCVEKGRVKCDHYWPADQdSLYYGDLILQMLSESVLPEWTIREFKICgEEQLDAHRLIRHFHYTVWPDHGVPETTQSLI 2099
Cdd:cd14628   127 TKLREMGREKCHQYWPAER-SARYQYFVVDPMAEYNMPQYILREFKVT-DARDGQSRTVRQFQFTDWPEQGVPKSGEGFI 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2100 QFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVR 2179
Cdd:cd14628   205 DFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAAL 284


                  ...
gi 578824049 2180 DVL 2182
Cdd:cd14628   285 EYL 287

R-PTPc-A-E-1

cd14551

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

1975-2176

2.68e-59

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: 203.22 E-value: 2.68e-59

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1975 YINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPaDQDSLYYGDLILQMLSES 2054
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWP-DQGCWTYGNLRVRVEDTV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2055 VLPEWTIREFkiCGEEQLD-----AHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDYInrSPGAGPTVVHCSAGVGRT 2129
Cdd:cd14551    80 VLVDYTTRKF--CIQKVNRgigekRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSAN--PPRAGPIVVHCSAGVGRT 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 578824049 2130 GTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 2176
Cdd:cd14551   156 GTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202

R-PTP-F-2

cd14629

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

1940-2182

3.02e-59

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

Pssm-ID: 350477 [Multi-domain] Cd Length: 291 Bit Score: 206.50 E-value: 3.02e-59

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1940 ALLPENRGKNRYNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMV 2019
Cdd:cd14629    48 ANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVML 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2020 TQCVEKGRVKCDHYWPADQdSLYYGDLILQMLSESVLPEWTIREFKICgEEQLDAHRLIRHFHYTVWPDHGVPETTQSLI 2099
Cdd:cd14629   128 TKLREMGREKCHQYWPAER-SARYQYFVVDPMAEYNMPQYILREFKVT-DARDGQSRTIRQFQFTDWPEQGVPKTGEGFI 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2100 QFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYvylHQCVR 2179
Cdd:cd14629   206 DFIGQVHKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQY---QLCYR 282


                  ...
gi 578824049 2180 DVL 2182
Cdd:cd14629   283 AAL 285

PTPc-N3

cd14600

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

1924-2183

5.32e-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: 205.08 E-value: 5.32e-59

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1924 EYEEL--KDVGRNQSCdiALLPENRGKNRYNNILPYDATRVKLSNVDDdpcsdYINASY----IPGNNFRREYIVTQGPL 1997
Cdd:cd14600    19 QFEQLyrKKPGLAITC--AKLPQNMDKNRYKDVLPYDATRVVLQGNED-----YINASYvnmeIPSANIVNKYIATQGPL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1998 PGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDSLYYGDLILQMLSESVLPEWTIREFKICGEEQLDAHRL 2077
Cdd:cd14600    92 PHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPDVMEYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTV 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2078 IrHFHYTVWPDHGVPETTQSLIQFVRTVRdyiNRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDL 2157
Cdd:cd14600   172 T-HLQYVAWPDHGVPDDSSDFLEFVNYVR---SKRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKM 247

                         250       260
                  ....*....|....*....|....*.
gi 578824049 2158 RLHRVHMVQTECQYVYLHQCVRDVLR 2183
Cdd:cd14600   248 RDQRAMMVQTSSQYKFVCEAILRVYE 273

R-PTPc-A-E-2

cd14552

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

1975-2178

2.34e-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: 194.80 E-value: 2.34e-56

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1975 YINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPADqDSLYYGDLILQMLSES 2054
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPED-GSVSSGDITVELKDQT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2055 VLPEWTIREFKICgEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDYINRSpGAGPTVVHCSAGVGRTGTFIA 2134
Cdd:cd14552    80 DYEDYTLRDFLVT-KGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQS-GNHPITVHCSAGAGRTGTFCA 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 578824049 2135 LDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 2178
Cdd:cd14552   158 LSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201

PTPc-N20

cd14596

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

1975-2183

9.99e-56

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: 193.04 E-value: 9.99e-56

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1975 YINASYI--PGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPAD-QDSLYYGDLILQML 2051
Cdd:cd14596     1 YINASYItmPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETlQEPMELENYQLRLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2052 SESVLPEWTIREFKICGEEQLDAHrLIRHFHYTVWPDHGVPETTQSLIQFVRtvrdYINRSPGAGPTVVHCSAGVGRTGT 2131
Cdd:cd14596    81 NYQALQYFIIRIIKLVEKETGENR-LIKHLQFTTWPDHGTPQSSDQLVKFIC----YMRKVHNTGPIVVHCSAGIGRAGV 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 578824049 2132 FIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRDVLR 2183
Cdd:cd14596   156 LICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207

R-PTPc-E-2

cd14622

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

1974-2180

1.33e-55

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

Pssm-ID: 350470 [Multi-domain] Cd Length: 205 Bit Score: 192.91 E-value: 1.33e-55

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1974 DYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPAdQDSLYYGDLILQMLSE 2053
Cdd:cd14622     1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPS-EGSVTHGEITIEIKND 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2054 SVLPEWTIREFkICGEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDYINRSpGAGPTVVHCSAGVGRTGTFI 2133
Cdd:cd14622    80 TLLETISIRDF-LVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQT-GNHPIVVHCSAGAGRTGTFI 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 578824049 2134 ALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRD 2180
Cdd:cd14622   158 ALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQD 204

PTPc-N22_18_12

cd14542

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

1975-2176

5.43e-53

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

Pssm-ID: 350390 [Multi-domain] Cd Length: 202 Bit Score: 185.32 E-value: 5.43e-53

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1975 YINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPADQ-DSLYYGDLILQMLSE 2053
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGeEQLQFGPFKISLEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2054 S-VLPEWTIREFKI-CGEEQldahRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDYinRSPGAGPTVVHCSAGVGRTGT 2131
Cdd:cd14542    81 KrVGPDFLIRTLKVtFQKES----RTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDY--QGSEDVPICVHCSAGCGRTGT 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 578824049 2132 FIALD---RILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 2176
Cdd:cd14542   155 ICAIDyvwNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202

R-PTPc-A-2

cd14623

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

1950-2180

9.04e-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: 185.63 E-value: 9.04e-53

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1950 RYNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVK 2029
Cdd:cd14623     1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2030 CDHYWPADqDSLYYGDLILQMLSESVLPEWTIREFKICGEEQlDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDYI 2109
Cdd:cd14623    81 CAQYWPSD-GSVSYGDITIELKKEEECESYTVRDLLVTNTRE-NKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQ 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578824049 2110 NRSpGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRD 2180
Cdd:cd14623   159 QQS-GNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228

PTPc-N22

cd14602

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

1948-2178

6.74e-52

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: 183.12 E-value: 6.74e-52

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1948 KNRYNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGR 2027
Cdd:cd14602     1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2028 VKCDHYWP-ADQDSLYYGDLILQMLSESVLPEWTIREFKI-CGEEQldahRLIRHFHYTVWPDHGVPETTQSLIQFVRTV 2105
Cdd:cd14602    81 KKCERYWAePGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVkFNSET----RTIYQFHYKNWPDHDVPSSIDPILELIWDV 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578824049 2106 RDYinRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLdsKDSV-----DIYGAVHDLRLHRVHMVQTECQYVYLHQCV 2178
Cdd:cd14602   157 RCY--QEDDSVPICIHCSAGCGRTGVICAIDYTWMLL--KDGIipenfSVFSLIQEMRTQRPSLVQTKEQYELVYNAV 230

PTPc-N5

cd14613

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

1948-2175

9.60e-52

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: 183.91 E-value: 9.60e-52

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1948 KNRYNNILPYDATRVKLSNVD-DDPCSDYINASYIPG-NNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEK 2025
Cdd:cd14613    28 KNRYKTILPNPHSRVCLTSPDqDDPLSSYINANYIRGyGGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2026 GRvKCDHYWPADQdSLYYGdliLQMLSESVLPE--WTIREFKI-CGEEQldahRLIRHFHYTVWPDHGVPETTQSLIQFV 2102
Cdd:cd14613   108 NE-KCTEYWPEEQ-VTYEG---IEITVKQVIHAddYRLRLITLkSGGEE----RGLKHYWYTSWPDQKTPDNAPPLLQLV 178

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578824049 2103 RTVRDYINRS-PGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 2175
Cdd:cd14613   179 QEVEEARQQAePNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVH 252

R-PTPc-R

cd14611

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

1948-2176

1.28e-51

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: 182.04 E-value: 1.28e-51

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1948 KNRYNNILPYDATRVKLSNVD-DDPCSDYINASYIPG-NNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEK 2025
Cdd:cd14611     2 KNRYKTILPNPHSRVCLKPKNsNDSLSTYINANYIRGyGGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2026 GRvKCDHYWPADQDslYYGDLILQMLSESVLPEWTIREFKIcgeEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTV 2105
Cdd:cd14611    82 NE-KCVLYWPEKRG--IYGKVEVLVNSVKECDNYTIRNLTL---KQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDV 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578824049 2106 RDYINRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 2176
Cdd:cd14611   156 EEDRLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVHH 226

PTPc-N12

cd14604

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

1904-2178

2.47e-51

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: 183.98 E-value: 2.47e-51

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1904 NQFEGHFMKLQAdsnylLSKEYEELK----DVGRNQscdiallpENRGKNRYNNILPYDATRVKLSNVDDDPCSDYINAS 1979
Cdd:cd14604    25 DNFASDFMRLRR-----LSTKYRTEKiyptATGEKE--------ENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINAN 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1980 YIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPA-DQDSLYYGDLILQMLSESVLPE 2058
Cdd:cd14604    92 FIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLyGEEPMTFGPFRISCEAEQARTD 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2059 WTIREFKIcgEEQLDAHRLIRhFHYTVWPDHGVPETTQSLIQFVRTVRDYINRSpgAGPTVVHCSAGVGRTGTFIALD-- 2136
Cdd:cd14604   172 YFIRTLLL--EFQNETRRLYQ-FHYVNWPDHDVPSSFDSILDMISLMRKYQEHE--DVPICIHCSAGCGRTGAICAIDyt 246

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 578824049 2137 -RILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 2178
Cdd:cd14604   247 wNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 289

PTPc-N21_14

cd14540

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

1975-2176

4.29e-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: 4.29e-51

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1975 YINASYIP---GNNFRReYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPA---DQDSLYYGDLIL 2048
Cdd:cd14540     1 YINASHITatvGGKQRF-YIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTlggEHDALTFGEYKV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2049 QMLSESVLPEWTIREFKIcGEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQF---VRTVRDYI-------NRSPgagPT 2118
Cdd:cd14540    80 STKFSVSSGCYTTTGLRV-KHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFleeINSVRRHTnqdvaghNRNP---PT 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578824049 2119 VVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 2176
Cdd:cd14540   156 LVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYN 213

R-PTP-N2

cd14610

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

1921-2173

8.83e-51

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: 181.79 E-value: 8.83e-51

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1921 LSKEYEELKDV-GRNQSCDIALLPENRGKNRYNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRR-EYIVTQGPLP 1998
Cdd:cd14610    19 LEKEWEALCAYqAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMDHDPRNpAYIATQGPLP 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1999 GTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPaDQDSLYYGDLILQMLSESVLPE-WTIREFKIcGEEQLDAHRL 2077
Cdd:cd14610    99 ATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWP-DEGSNLYHIYEVNLVSEHIWCEdFLVRSFYL-KNLQTNETRT 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2078 IRHFHYTVWPDHGVPETTQSLIQFVRTVRD-YINRSpgaGPTVVHCSAGVGRTGTFIALDRILQQL-DSKDSVDIYGAVH 2155
Cdd:cd14610   177 VTQFHFLSWNDQGVPASTRSLLDFRRKVNKcYRGRS---CPIIVHCSDGAGRSGTYILIDMVLNKMaKGAKEIDIAATLE 253

                         250
                  ....*....|....*...
gi 578824049 2156 DLRLHRVHMVQTECQYVY 2173
Cdd:cd14610   254 HLRDQRPGMVQTKEQFEF 271

R-PTP-N

cd14609

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

1921-2173

1.06e-48

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: 176.00 E-value: 1.06e-48

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1921 LSKEYEELKDV-GRNQSCDIALLPENRGKNRYNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRR-EYIVTQGPLP 1998
Cdd:cd14609    17 LAKEWQALCAYqAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIEHDPRMpAYIATQGPLS 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1999 GTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDSLYYgDLILQMLSESVLPE-WTIREFKIcGEEQLDAHRL 2077
Cdd:cd14609    97 HTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYH-IYEVNLVSEHIWCEdFLVRSFYL-KNVQTQETRT 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2078 IRHFHYTVWPDHGVPETTQSLIQFVRTV-RDYINRSpgaGPTVVHCSAGVGRTGTFIALDRILQQL-DSKDSVDIYGAVH 2155
Cdd:cd14609   175 LTQFHFLSWPAEGIPSSTRPLLDFRRKVnKCYRGRS---CPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLE 251

                         250
                  ....*....|....*...
gi 578824049 2156 DLRLHRVHMVQTECQYVY 2173
Cdd:cd14609   252 HVRDQRPGMVRTKDQFEF 269

PTPc-N4

cd14601

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

1974-2183

1.48e-48

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

Pssm-ID: 350449 [Multi-domain] Cd Length: 212 Bit Score: 172.82 E-value: 1.48e-48

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1974 DYINASYI----PGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDSLYYGDLILQ 2049
Cdd:cd14601     1 DYINANYInmeiPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSSSYGGFQVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2050 MLSESVLPEWTIREFKICGEEQLDAhRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDyiNRSPGAGPTVVHCSAGVGRT 2129
Cdd:cd14601    81 CHSEEGNPAYVFREMTLTNLEKNES-RPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRN--KRAGKDEPVVVHCSAGIGRT 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 578824049 2130 GTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRDVLR 2183
Cdd:cd14601   158 GVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVYE 211

PTPc-N14

cd14599

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

1924-2176

1.77e-48

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

Pssm-ID: 350447 [Multi-domain] Cd Length: 287 Bit Score: 175.57 E-value: 1.77e-48

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1924 EYEELKDVGRNQSCDIALLPENRGKNRYNNILPYDATRVKLSNVDDDPcSDYINASYIPGNNFRRE--YIVTQGPLPGTK 2001
Cdd:cd14599    17 EYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVPTKENN-TGYINASHIKVTVGGEEwhYIATQGPLPHTC 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2002 DDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWP---ADQDSLYYG--DLILQMLSESVLPEWTIREFK--ICGEEqlda 2074
Cdd:cd14599    96 HDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPklgSKHSSATYGkfKVTTKFRTDSGCYATTGLKVKhlLSGQE---- 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2075 hRLIRHFHYTVWPDHGVPETTQSLIQF---VRTVRDYINRSPGAG-----PTVVHCSAGVGRTGTFIALDRILQQLDSKD 2146
Cdd:cd14599   172 -RTVWHLQYTDWPDHGCPEEVQGFLSYleeIQSVRRHTNSMLDSTkncnpPIVVHCSAGVGRTGVVILTELMIGCLEHNE 250

                         250       260       270
                  ....*....|....*....|....*....|
gi 578824049 2147 SVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 2176
Cdd:cd14599   251 KVEVPVMLRHLREQRMFMIQTIAQYKFVYQ 280

R-PTP-C-2

cd14558

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

1975-2175

2.36e-47

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: 169.11 E-value: 2.36e-47

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1975 YINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDSlyYGDLILQMLSES 2054
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKT--YGDIEVELKDTE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2055 VLPEWTIREFKIcGEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVR----DYINRSPGAGPTVVHCSAGVGRTG 2130
Cdd:cd14558    79 KSPTYTVRVFEI-THLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKqklpYKNSKHGRSVPIVVHCSDGSSRTG 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 578824049 2131 TFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 2175
Cdd:cd14558   158 IFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202

R-PTPc-typeIIb-2

cd14556

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

1975-2176

5.09e-47

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: 167.97 E-value: 5.09e-47

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1975 YINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQcVEKGRVKCDHYWPaDQDSLYYGDLILQMLSES 2054
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQ-LDPKDQSCPQYWP-DEGSGTYGPIQVEFVSTT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2055 VLPEWTIREFKICGEEQL-DAHRLIRHFHYTVWPDHG-VPETTQSLIQFVRTVRDYINRSpGAGPTVVHCSAGVGRTGTF 2132
Cdd:cd14556    79 IDEDVISRIFRLQNTTRPqEGYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQEQS-GEGPIVVHCLNGVGRSGVF 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 578824049 2133 IALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 2176
Cdd:cd14556   158 CAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201

PTPc_plant_PTP1

cd17658

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

1975-2173

3.05e-44

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: 160.32 E-value: 3.05e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1975 YINASYIPGNNFRR--EYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGR-VKCDHYWPA-DQDSLYYGDLilqm 2050
Cdd:cd17658     1 YINASLVETPASESlpKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStAKCADYFPAeENESREFGRI---- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2051 lseSVLPEW--------TIREFKICGEEQLDAHRLIRHFHYTVWPDHGVPETTqsliqfvRTVRDYINRS----PGAGPT 2118
Cdd:cd17658    77 ---SVTNKKlkhsqhsiTLRVLEVQYIESEEPPLSVLHIQYPEWPDHGVPKDT-------RSVRELLKRLygipPSAGPI 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 578824049 2119 VVHCSAGVGRTGTFIALDRILQQLDSKD--SVDIYGAVHDLRLHRVHMVQTECQYVY 2173
Cdd:cd17658   147 VVHCSAGIGRTGAYCTIHNTIRRILEGDmsAVDLSKTVRKFRSQRIGMVQTQDQYIF 203

R-PTP-N-N2

cd14546

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

1975-2178

3.32e-44

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: 160.30 E-value: 3.32e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1975 YINASYIPGNNFRRE-YIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPaDQDSLYYGDLILQMLSE 2053
Cdd:cd14546     1 YINASTIYDHDPRNPaYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWP-EEGSEVYHIYEVHLVSE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2054 SVLPE-WTIREFKIcGEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTV-RDYINRSpgaGPTVVHCSAGVGRTGT 2131
Cdd:cd14546    80 HIWCDdYLVRSFYL-KNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVnKSYRGRS---CPIVVHCSDGAGRTGT 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 578824049 2132 FIALDRILQQL-DSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 2178
Cdd:cd14546   156 YILIDMVLNRMaKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAV 203

PTP-N23

cd14539

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

1975-2176

2.22e-43

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: 157.55 E-value: 2.22e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1975 YINASYIPG-NNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPADQ-DSLYYGDLILQMLS 2052
Cdd:cd14539     1 YINASLIEDlTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERgQALVYGAITVSLQS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2053 ESVLPEWTIREFKICGEEQlDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDYINRS-PGAGPTVVHCSAGVGRTGT 2131
Cdd:cd14539    81 VRTTPTHVERIISIQHKDT-RLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQrSLQTPIVVHCSSGVGRTGA 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 578824049 2132 FIALDRILQQLDSKDSV-DIYGAVHDLRLHRVHMVQTECQYVYLHQ 2176
Cdd:cd14539   160 FCLLYAAVQEIEAGNGIpDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205

PHA02742

protein tyrosine phosphatase; Provisional

1902-2190

1.17e-42

protein tyrosine phosphatase; Provisional

Pssm-ID: 165109 [Multi-domain] Cd Length: 303 Bit Score: 159.01 E-value: 1.17e-42

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1902 KINQFEGHFMKLQADSN--YLLSKEYEELKDVGRNQSCDIALLPENRGKNRYNNILPYDATRVKLSNvdDDPCSDYINAS 1979
Cdd:PHA02742    7 KKNSFAKNCEQLIEESNlaEILKEEHEHIMQEIVAFSCNESLELKNMKKCRYPDAPCFDRNRVILKI--EDGGDDFINAS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1980 YIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYW-PADQDSLYYGDLILQMLSESVLPE 2058
Cdd:PHA02742   85 YVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYWmPHERGKATHGEFKIKTKKIKSFRN 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2059 WTIREFKICGEEQ---LDahrlIRHFHYTVWPDHGVPETTQSLIQFVRTVR--DYINRSPGAG-------PTVVHCSAGV 2126
Cdd:PHA02742  165 YAVTNLCLTDTNTgasLD----IKHFAYEDWPHGGLPRDPNKFLDFVLAVReaDLKADVDIKGenivkepPILVHCSAGL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578824049 2127 GRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYlhqCVRDVLRARKLRSE 2190
Cdd:PHA02742  241 DRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIF---CYFIVLIFAKLMAD 301

COG5599

Protein tyrosine phosphatase [Signal transduction mechanisms];

1943-2171

2.23e-41

Protein tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 444335 [Multi-domain] Cd Length: 282 Bit Score: 154.86 E-value: 2.23e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1943 PENRGKNRYNNILPYDATRVKlsnvDDDPcsdYINASYIPGNNFRReYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQC 2022
Cdd:COG5599    40 INGSPLNRFRDIQPYKETALR----ANLG---YLNANYIQVIGNHR-YIATQYPLEEQLEDFFQMLFDNNTPVLVVLASD 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2023 VE--KGRVKCDHYWPADQDSLYYgDLILQMLSESVL-PEWTIREFKI----CGEEQLDahrlIRHFHYTVWPDHGVPETT 2095
Cdd:COG5599   112 DEisKPKVKMPVYFRQDGEYGKY-EVSSELTESIQLrDGIEARTYVLtikgTGQKKIE----IPVLHVKNWPDHGAISAE 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2096 QsLIQFVRTVRDYIN-RSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKD--SVDIYGAVHDLRLHR-VHMVQTECQY 2171
Cdd:COG5599   187 A-LKNLADLIDKKEKiKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRnGGMVQTSEQL 265

PTPc_DSPc

smart00012

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

2078-2178

5.70e-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: 5.70e-40

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049   2078 IRHFHYTVWPDHGVPETTQSLIQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDS-KDSVDIYGAVHD 2156
Cdd:smart00012    2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAeAGEVDIFDTVKE 81

                            90       100
                    ....*....|....*....|..
gi 578824049   2157 LRLHRVHMVQTECQYVYLHQCV 2178
Cdd:smart00012   82 LRSQRPGMVQTEEQYLFLYRAL 103

PTPc_motif

smart00404

Protein tyrosine phosphatase, catalytic domain motif;

2078-2178

5.70e-40

Protein tyrosine phosphatase, catalytic domain motif;

Pssm-ID: 214649 [Multi-domain] Cd Length: 105 Bit Score: 144.04 E-value: 5.70e-40

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049   2078 IRHFHYTVWPDHGVPETTQSLIQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDS-KDSVDIYGAVHD 2156
Cdd:smart00404    2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAeAGEVDIFDTVKE 81

                            90       100
                    ....*....|....*....|..
gi 578824049   2157 LRLHRVHMVQTECQYVYLHQCV 2178
Cdd:smart00404   82 LRSQRPGMVQTEEQYLFLYRAL 103

PHA02747

protein tyrosine phosphatase; Provisional

1943-2175

6.60e-39

protein tyrosine phosphatase; Provisional

Pssm-ID: 165114 [Multi-domain] Cd Length: 312 Bit Score: 148.61 E-value: 6.60e-39

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1943 PENRGKNRYNNILPYDATRVKLSNvDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQC 2022
Cdd:PHA02747   49 PENQPKNRYWDIPCWDHNRVILDS-GGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPT 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2023 -VEKGRVKCDHYW-PADQDSLYYGDLILQMLSESVLPEWTIREFKICgEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQ 2100
Cdd:PHA02747  128 kGTNGEEKCYQYWcLNEDGNIDMEDFRIETLKTSVRAKYILTLIEIT-DKILKDSRKISHFQCSEWFEDETPSDHPDFIK 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2101 FVRTV--------RDYINRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYV 2172
Cdd:PHA02747  207 FIKIIdinrkksgKLFNPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYL 286


                  ...
gi 578824049 2173 YLH 2175
Cdd:PHA02747  287 FIQ 289

PHA02738

hypothetical protein; Provisional

1945-2179

1.10e-38

hypothetical protein; Provisional

Pssm-ID: 222923 [Multi-domain] Cd Length: 320 Bit Score: 148.15 E-value: 1.10e-38

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1945 NRGKNRYNNILPYDATRVKLSNVDDDpcSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVE 2024
Cdd:PHA02738   49 NRKLNRYLDAVCFDHSRVILPAERNR--GDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKE 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2025 KGRVKCDHYWP-ADQDSLYYGDLILQMLSESVLPEWTirEFKICGEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVR 2103
Cdd:PHA02738  127 NGREKCFPYWSdVEQGSIRFGKFKITTTQVETHPHYV--KSTLLLTDGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVL 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2104 TVRD-----YINR------SPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYV 2172
Cdd:PHA02738  205 EVRQcqkelAQESlqighnRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYF 284


                  ....*..
gi 578824049 2173 YLHQCVR 2179
Cdd:PHA02738  285 FCYRAVK 291

PTPc-N21

cd14598

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

1975-2183

5.59e-38

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: 142.81 E-value: 5.59e-38

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1975 YINASYIPGNNFRRE--YIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWP---ADQDSLYYG--DLI 2047
Cdd:cd14598     1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlgSRHNTVTYGrfKIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2048 LQMLSESVLPEWTIREFK--ICGEEqldahRLIRHFHYTVWPDHGVPETTQSLIQF---VRTVRDYIN-----RSPGAgP 2117
Cdd:cd14598    81 TRFRTDSGCYATTGLKIKhlLTGQE-----RTVWHLQYTDWPEHGCPEDLKGFLSYleeIQSVRRHTNstidpKSPNP-P 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578824049 2118 TVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRDVLR 2183
Cdd:cd14598   155 VLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220

PHA02746

protein tyrosine phosphatase; Provisional

1920-2182

1.53e-37

protein tyrosine phosphatase; Provisional

Pssm-ID: 165113 [Multi-domain] Cd Length: 323 Bit Score: 145.17 E-value: 1.53e-37

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1920 LLSKEYEELKDVGRNQSCDIALLPENRGKNRYNNILPYDATRVKLSN-------------------VDDDPCSDYINASY 1980
Cdd:PHA02746   26 FVLLEHAEVMDIPIRGTTNHFLKKENLKKNRFHDIPCWDHSRVVINAheslkmfdvgdsdgkkievTSEDNAENYIHANF 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1981 IPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQcVEKGRVKCDHYWPADQDS-LYYGDLILQMLSESVLPEW 2059
Cdd:PHA02746  106 VDGFKEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTD-IDDDDEKCFELWTKEEDSeLAFGRFVAKILDIIEELSF 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2060 TIREFKICgEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFV--------RTVRDYINRSPGAGPTVVHCSAGVGRTGT 2131
Cdd:PHA02746  185 TKTRLMIT-DKISDTSREIHHFWFPDWPDNGIPTGMAEFLELInkvneeqaELIKQADNDPQTLGPIVVHCSAGIGRAGT 263

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578824049 2132 FIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRDVL 2182
Cdd:PHA02746  264 FCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKALKYAI 314

R5-PTP-2

cd14550

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

1975-2176

2.42e-34

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: 131.67 E-value: 2.42e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1975 YINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCdhYWPADQDSLYYGDLILQMLSES 2054
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPI--YWPTKEKPLECETFKVTLSGED 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2055 VLPEW-----TIREFKIcgEEQLDAHRL-IRHFHYTVWPDHGVP-ETTQSLIQFVRtvRDYINRSpgaGPTVVHCSAGVG 2127
Cdd:cd14550    79 HSCLSneirlIVRDFIL--ESTQDDYVLeVRQFQCPSWPNPCSPiHTVFELINTVQ--EWAQQRD---GPIVVHDRYGGV 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 578824049 2128 RTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 2176
Cdd:cd14550   152 QAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200

R-PTPc-T-2

cd14634

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

1975-2176

1.51e-33

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: 129.37 E-value: 1.51e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1975 YINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQcVEKGRVkCDHYWPaDQDSLYYGDLILQMLSES 2054
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNE-MDAAQL-CMQYWP-EKTSCCYGPIQVEFVSAD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2055 VLPEWTIREFKICGEEQ-LDAHRLIRHFHYTVWPDH-GVPETTQSLIQFVRTVRDYINRSPGA-GPTVVHCSAGVGRTGT 2131
Cdd:cd14634    78 IDEDIISRIFRICNMARpQDGYRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQYDGReGRTVVHCLNGGGRSGT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 578824049 2132 FIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 2176
Cdd:cd14634   158 FCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYE 202

PTP_tm

pfam18861

TM proximal of protein tyrosine phosphatase, receptor type J; Protein tyrosine phosphatases ...

1691-1828

4.00e-33

Pssm-ID: 465889 Cd Length: 126 Bit Score: 125.41 E-value: 4.00e-33

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049  1691 VNCSWFSDTNGAVKYFTVVVREADgsDELKPEQQHPLPSYLEYRhNASIRVYQTNYFASKCAENPnSNSKSFNIKLGAEM 1770
Cdd:pfam18861    1 IQFSLFNSSNGPIKAYGVIVTTND--SLNRPLKEYLNKTYYDWK-YKKTDSYLATVTPNPFTSPR-SSSRSLTVPVGTGS 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 578824049  1771 ESlggkcdptqQKFCDGPLKPHTAYRISIRAFTQL-FDEDLKEFTKPLYSDTFFSLPIT 1828
Cdd:pfam18861   77 KW---------QGYCNGPLKPLGSYRFSVAAFTRLeFDDGLIDGEESYVSFTPFSEPIA 126

R-PTPc-U-2

cd14637

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

1975-2178

4.33e-27

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: 111.15 E-value: 4.33e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1975 YINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV-KCDHYWPaDQDSLYYGDLILQMLSE 2053
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWP-EPGLQQYGPMEVEFVSG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2054 SVLPEWTIREFKICGEEQL-DAHRLIRHFHYTVW-PDHGVPETTQSLIQFVRTVRDYiNRSPGAGPTVVHCSAGVGRTGT 2131
Cdd:cd14637    80 SADEDIVTRLFRVQNITRLqEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKW-QRESGEGRTVVHCLNGGGRSGT 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 578824049 2132 FIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 2178
Cdd:cd14637   159 YCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIA 205

R-PTPc-K-2

cd14636

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

1975-2175

7.77e-27

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: 110.11 E-value: 7.77e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1975 YINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQC-VEKGrvkCDHYWPaDQDSLYYGDLILQMLSE 2053
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVdLAQG---CPQYWP-EEGMLRYGPIQVECMSC 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2054 SVLPEWTIREFKICG-EEQLDAHRLIRHFHYTVWPDH-GVPETTQSLIQFVRTVRDYINR-SPGAGPTVVHCSAGVGRTG 2130
Cdd:cd14636    77 SMDCDVISRIFRICNlTRPQEGYLMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEEcDEGEGRTIIHCLNGGGRSG 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 578824049 2131 TFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 2175
Cdd:cd14636   157 MFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCY 201

R-PTP-G-2

cd17670

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

1975-2178

7.80e-27

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: 110.15 E-value: 7.80e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1975 YINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQcvEKGRVKCDH-YWPADQDSLYYGDLILQMLSE 2053
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD--NQGLAEDEFvYWPSREESMNCEAFTVTLISK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2054 SVLPewtirefkICGEEQLDAHRLI------------RHFHYTVWPDHGVP-ETTQSLIQFVRtvRDYINRSpgaGPTVV 2120
Cdd:cd17670    79 DRLC--------LSNEEQIIIHDFIleatqddyvlevRHFQCPKWPNPDAPiSSTFELINVIK--EEALTRD---GPTIV 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 578824049 2121 HCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 2178
Cdd:cd17670   146 HDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAM 203

R-PTPc-M-2

cd14635

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

1975-2176

3.17e-25

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: 105.54 E-value: 3.17e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1975 YINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQcVEKGRVkCDHYWPaDQDSLYYGDLILQMLSES 2054
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLND-VDPAQL-CPQYWP-ENGVHRHGPIQVEFVSAD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2055 VLPEWTIREFKICGEEQ-LDAHRLIRHFHYTVWPDH-GVPETTQSLIQFVRTVRDYINRSPGA-GPTVVHCSAGVGRTGT 2131
Cdd:cd14635    78 LEEDIISRIFRIYNAARpQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEYNGGeGRTVVHCLNGGGRSGT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 578824049 2132 FIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 2176
Cdd:cd14635   158 FCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYE 202

R-PTP-Z-2

cd17669

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

1975-2178

2.39e-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: 103.15 E-value: 2.39e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1975 YINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCdHYWPADQDSLYYGDLILQMLSE- 2053
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWPNKDEPINCETFKVTLIAEe 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2054 ----SVLPEWTIREFkICGEEQLDAHRLIRHFHYTVWPDHGVP-ETTQSLIQFVRtvRDYINRSpgaGPTVVHCSAGVGR 2128
Cdd:cd17669    80 hkclSNEEKLIIQDF-ILEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELISIIK--EEAANRD---GPMIVHDEHGGVT 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 578824049 2129 TGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 2178
Cdd:cd17669   154 AGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203

beta-trefoil_Ricin_MRC-like

cd23385

ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) ...

19-132

1.62e-23

ricin B-type lectin domain, beta-trefoil fold, found in the macrophage mannose receptor (MRC) family; The MRC family includes MRC1-2, receptor-type tyrosine-protein phosphatase beta (PTPRB) isoform e, secretory phospholipase A2 receptor (PLA2R1), and lymphocyte antigen 75 (Ly-75). MRC1 mediates the endocytosis of glycoproteins by macrophages. It binds both sulfated and non-sulfated polysaccharide chains, and acts as a phagocytic receptor for bacteria, fungi, and other pathogens. It also acts as a receptor for Dengue virus envelope protein E. MRC2 may play a role as an endocytotic lectin receptor displaying calcium-dependent lectin activity. It internalizes glycosylated ligands from the extracellular space for release in an endosomal compartment via clathrin-mediated endocytosis. It may be involved in plasminogen activation system controlling the extracellular level of PLAUR/PLAU, and thus may regulate protease activity at the cell surface. It may contribute to cellular uptake, remodeling, and degradation of extracellular collagen matrices. It may play a role during cancer progression as well as in other chronic tissue destructive diseases acting on collagen turnover. It may participate in remodeling of extracellular matrix cooperating with the matrix metalloproteinases (MMPs). PTPRB (EC 3.1.3.48), also called protein-tyrosine phosphatase beta, plays an important role in blood vessel remodeling and angiogenesis. It is not necessary for the initial formation of the blood vessels but is essential for their maintenance and remodeling. It is also essential for the maintenance of endothelial cell contact integrity and for the adhesive function of VE-cadherin in endothelial cells that requires the presence of plakoglobin. PLA2R1 is a receptor for secretory phospholipase A2 (sPLA2). It acts as a receptor for phospholipase sPLA2-IB/PLA2G1B but not sPLA2-IIA/PLA2G2A. It can also bind to snake PA2-like toxins. It may be involved in responses in proinflammatory cytokine productions during endotoxic shock. It also has endocytic properties and rapidly internalizes sPLA2 ligands, which is particularly important for the clearance of extracellular sPLA2s to protect their potent enzymatic activities. Ly-75 acts as an endocytic receptor to direct captured antigens from the extracellular space to a specialized antigen-processing compartment. It causes reduced proliferation of B-lymphocytes. All family members contain a ricin B-type lectin domain at the N-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket. One member of this family, MRC1, is missing the gamma subdomain.

Pssm-ID: 467784 [Multi-domain] Cd Length: 119 Bit Score: 97.67 E-value: 1.62e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049   19 EGFQIVHVQKQQCLFKNE---KVVVGSCNRTIQNQQWMWTEDEKLLHVKSALCLAISNSSrgPSRSAILDRC---SQAPR 92
Cdd:cd23385     1 DSFLIYNEDLGKCLAARSsssKVSLSTCNPNSPNQQWKWTSGHRLFNVGTGKCLGVSSSS--PSSPLRLFECdseDELQK 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 578824049   93 WTCYDQEGFLEVENASLFLQ-KQGSRVVVKKARKYLHSWMK 132
Cdd:cd23385    79 WKCSKDGLLLLKGLGLLLLYdKSGKNVVVSKGSGLSSRWKI 119

PHA02740

protein tyrosine phosphatase; Provisional

1901-2176

5.14e-16

protein tyrosine phosphatase; Provisional

Pssm-ID: 165107 [Multi-domain] Cd Length: 298 Bit Score: 81.17 E-value: 5.14e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1901 IKINQFEGHFMKlqADSNYLLSKEYEEL---KDVGRNQSCDIAllpENRGKNRYN--NILPYDATRVKLSNVDDdpcsdY 1975
Cdd:PHA02740    9 INGMDFINFINK--PDLLSCIIKEYRAIvpeHEDEANKACAQA---ENKAKDENLalHITRLLHRRIKLFNDEK-----V 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1976 INASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKgrvKC-DHYWPADQDSL-YYGDLILQMLSE 2053
Cdd:PHA02740   79 LDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHADK---KCfNQFWSLKEGCViTSDKFQIETLEI 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2054 SVLPEWTIREFKIcgEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDY---INRSPG---AGPTVVHCSAGVG 2127
Cdd:PHA02740  156 IIKPHFNLTLLSL--TDKFGQAQKISHFQYTAWPADGFSHDPDAFIDFFCNIDDLcadLEKHKAdgkIAPIIIDCIDGIS 233

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 578824049 2128 RTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 2176
Cdd:PHA02740  234 SSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYH 282

fn3

Fibronectin type III domain;

1480-1562

1.72e-12

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 64.74 E-value: 1.72e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049  1480 SPPSLMSFADIANTSLAITWKGPPDWT-DYNDFELQWLPRDALTVFNPYNNRKSEGR-IVYGLRPGRSYQFNVKTVSGDS 1557
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNgPITGYEVEYRPKNSGEPWNEITVPGTTTSvTLTGLKPGTEYEVRVQAVNGGG 80


                   ....*
gi 578824049  1558 WKTYS 1562
Cdd:pfam00041   81 EGPPS 85

CDC14

COG2453

Protein-tyrosine phosphatase [Signal transduction mechanisms];

2078-2176

2.18e-11

Protein-tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 441989 [Multi-domain] Cd Length: 140 Bit Score: 63.45 E-value: 2.18e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2078 IRHFHYTvWPDHGVPETTQsLIQFVRTVRDYINRSpgaGPTVVHCSAGVGRTGTFIALDRILQQLDSKDsvdiygAVHDL 2157
Cdd:COG2453    48 LEYLHLP-IPDFGAPDDEQ-LQEAVDFIDEALREG---KKVLVHCRGGIGRTGTVAAAYLVLLGLSAEE------ALARV 116

                          90
                  ....*....|....*....
gi 578824049 2158 RLHRVHMVQTECQYVYLHQ 2176
Cdd:COG2453   117 RAARPGAVETPAQRAFLER 135

fn3

Fibronectin type III domain;

1574-1653

1.18e-10

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 59.74 E-value: 1.18e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049  1574 DKIQNLHCRPQNSTAIACSWIPP---DSDFDGYSIECRKMDTQEVEFSRKLEKEKSLLNIMMLVPHKRYLVSIKVQSAGM 1650
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ...
gi 578824049  1651 TSE 1653
Cdd:pfam00041   81 EGP 83

fn3

Fibronectin type III domain;

950-1026

1.22e-10

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 59.74 E-value: 1.22e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049   950 DKVQGVSVSNsARSDYLRVSWVHAT---GDFDHYEVTIK--NKNNFIQTKSIPKSENECVFVQLVPGRLYSVTVTTKSGQ 1024
Cdd:pfam00041    1 SAPSNLTVTD-VTSTSLTVSWTPPPdgnGPITGYEVEYRpkNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ..
gi 578824049  1025 YE 1026
Cdd:pfam00041   80 GE 81

fn3

Fibronectin type III domain;

1126-1199

2.36e-10

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 58.97 E-value: 2.36e-10

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578824049  1126 SAVKNIHISPNGATdSLTVNWTP---GGGDVDSYTVSAF--RHSQKVDSQTIPKHVFEHTFHRLEAGEQYQIMIASVSG 1199
Cdd:pfam00041    1 SAPSNLTVTDVTST-SLTVSWTPppdGNGPITGYEVEYRpkNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78

fn3

Fibronectin type III domain;

331-407

5.45e-10

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 57.81 E-value: 5.45e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049   331 PARFGVSKEKTTSTSLHVWWTPS---SGKVTSYEVQLFDENNQKiQGVQIQESTSWNEYTFFNLTAGSKYNIAITAVSGG 407
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGE-PWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

PTP_YopH-like

cd14559

YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...

2081-2174

1.90e-09

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

Pssm-ID: 350407 [Multi-domain] Cd Length: 227 Bit Score: 60.11 E-value: 1.90e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2081 FHYTVWPDHG-------------VPETTQSLIQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFIAldrILQQLDSKDS 2147
Cdd:cd14559   121 VHVTNWPDHTaisseglkeladlVNKSAEEKRNFYKSKGSSAINDKNKLLPVIHCRAGVGRTGQLAA---AMELNKSPNN 197

                          90       100
                  ....*....|....*....|....*...
gi 578824049 2148 VDIYGAVHDLRLHR-VHMVQTECQYVYL 2174
Cdd:cd14559   198 LSVEDIVSDMRTSRnGKMVQKDEQLDTL 225

fn3

Fibronectin type III domain;

1393-1466

3.80e-09

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 55.50 E-value: 3.80e-09

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578824049  1393 SVSHLRGSNRNTTdSLWFNWSPA---SGDFDFYELILYNPNGTKKENWK--DKDLTEWRFQGLVPGRKYVLWVVTHSGD 1466
Cdd:pfam00041    2 APSNLTVTDVTST-SLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEItvPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

FN3

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

328-419

5.98e-09

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 55.20 E-value: 5.98e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049  328 PLPPARFGVSKekTTSTSLHVWWTPSS---GKVTSYEVQLFDENNQKIQGVQIQESTSwNEYTFFNLTAGSKYNIAITAV 404
Cdd:cd00063     1 PSPPTNLRVTD--VTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSE-TSYTLTGLKPGTEYEFRVRAV 77

                          90
                  ....*....|....*.
gi 578824049  405 SGGKRS-FSVYTNGST 419
Cdd:cd00063    78 NGGGESpPSESVTVTT 93

fn3

Fibronectin type III domain;

1039-1112

1.78e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 53.57 E-value: 1.78e-08

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578824049  1039 PVKDLTLRNRSTEDLHVTWSGA---NGDVDQYEIQLL-FNDMKVFPPFHLVNTATEYRFTSLTPGRQYKILVLTISGD 1112
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRpKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

fn3

Fibronectin type III domain;

862-938

2.76e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 52.80 E-value: 2.76e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049   862 SSVSGVTVNNSGrNDYLSVSWLLAP---GDVDNYEVTLSH--DGKVVQSLVIAKSVRECSFSSLTPGRLYTVTITTRSGK 936
Cdd:pfam00041    1 SAPSNLTVTDVT-STSLTVSWTPPPdgnGPITGYEVEYRPknSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ..
gi 578824049   937 YE 938
Cdd:pfam00041   80 GE 81

fn3

Fibronectin type III domain;

687-765

4.41e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 52.42 E-value: 4.41e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049   687 AVLQLRVKHANETSLSIMWQTPV---AEWEKYIISLADRD--LLLIHKSLSKDAKEFTFTDLVPGRKYMATVTSISGDLK 761
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNsgEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ....
gi 578824049   762 NSSS 765
Cdd:pfam00041   82 GPPS 85

PTP_DSP_cys

cd14494

cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...

2100-2176

6.54e-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: 52.74 E-value: 6.54e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2100 QFVRTVRDYINR--SPGaGPTVVHCSAGVGRTGTFIALDRILQQLDS-KDSVDIYGavhdlRLHRVHMVQTECQYVYLHQ 2176
Cdd:cd14494    40 AMVDRFLEVLDQaeKPG-EPVLVHCKAGVGRTGTLVACYLVLLGGMSaEEAVRIVR-----LIRPGGIPQTIEQLDFLIK 113

fn3

Fibronectin type III domain;

596-672

9.93e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 51.26 E-value: 9.93e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049   596 DKVANLEANNNGRmRSLVVSWSPPA---GDWEQYRILLF--NDSVVLLNITVGKEETQYVMddTGLVPGRQYEVEVIVES 670
Cdd:pfam00041    1 SAPSNLTVTDVTS-TSLTVSWTPPPdgnGPITGYEVEYRpkNSGEPWNEITVPGTTTSVTL--TGLKPGTEYEVRVQAVN 77


                   ..
gi 578824049   671 GN 672
Cdd:pfam00041   78 GG 79

CDKN3-like

cd14505

cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...

2078-2176

9.97e-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: 53.81 E-value: 9.97e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2078 IRHFHYTVwPDHGVPETTQsliQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFIAldRILQQLDSKDSVDiyGAVHDL 2157
Cdd:cd14505    73 ITWHHLPI-PDGGVPSDIA---QWQELLEELLSALENGKKVLIHCKGGLGRTGLIAA--CLLLELGDTLDPE--QAIAAV 144

                          90
                  ....*....|....*....
gi 578824049 2158 RLHRVHMVQTECQYVYLHQ 2176
Cdd:cd14505   145 RALRPGAIQTPKQENFLHQ 163

FN3

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

507-582

1.09e-07

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 51.73 E-value: 1.09e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049  507 PMEVSNLKVTNDGSlTSLKVKWQRPP---GNVDSYNITLSHKGTIKESRVLAPWITETHF--KELVPGRLYQVTVSCVSG 581
Cdd:cd00063     1 PSPPTNLRVTDVTS-TSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYtlTGLKPGTEYEFRVRAVNG 79


                  .
gi 578824049  582 E 582
Cdd:cd00063    80 G 80

FN3

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

1573-1661

4.21e-07

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 49.80 E-value: 4.21e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1573 PDKIQNLHCRPQNSTAIACSWIPPDSD---FDGYSIECRKMDTQEVEFSRKLEKEKSLLNIMMLVPHKRYLVSIKVQSAG 1649
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDggpITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|..
gi 578824049 1650 MTSEVVEDSTIT 1661
Cdd:cd00063    81 GESPPSESVTVT 92

FN3

Fibronectin type 3 domain [General function prediction only];

1093-1508

4.29e-07

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 55.39 E-value: 4.29e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1093 FTSLTPGRQYKILVLTISGDVQQSAFIEGFTVPSAVKNIHISPNGATDSLTVNWTPGGGDVDSYTVSAFRHSQKVDSQTI 1172
Cdd:COG3401   108 NTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTV 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1173 PKHVFEHTFHRLEAGEQYQIMIASVS----GSLKNQINVV-GRTVPASVQGVIADNAYSSySLIVSWQKAAGV-AERYDI 1246
Cdd:COG3401   188 TSTTLVDGGGDIEPGTTYYYRVAATDtggeSAPSNEVSVTtPTTPPSAPTGLTATADTPG-SVTLSWDPVTESdATGYRV 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1247 LL-LTENGillrNTSEPATTKQHKFED--LTPGKKYKIQILTVSG----GLFSKEAQ-TEGRTVPAAVTDLRITENSTRH 1318
Cdd:COG3401   267 YRsNSGDG----PFTKVATVTTTSYTDtgLTNGTTYYYRVTAVDAagneSAPSNVVSvTTDLTPPAAPSGLTATAVGSSS 342

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1319 LSFRWTASEGE-LSWYNIflY---NPDGNLQERAQVDPlVQSFSFQNLLQGRM--YKMVIVTHSGELSNESF-IFGRTVP 1391
Cdd:COG3401   343 ITLSWTASSDAdVTGYNV--YrstSGGGTYTKIAETVT-TTSYTDTGLTPGTTyyYKVTAVDAAGNESAPSEeVSATTAS 419

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1392 ASVS-HLRGSNRNTTDSLWFNWSPASGDFDFYELILYNPNGTKKENWKDKDLTEW----RFQGLVPGRKYVLWVVTHSGD 1466
Cdd:COG3401   420 AASGeSLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSstvtATTTDTTTANLSVTTGSLVGG 499

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 578824049 1467 LSNKVTAESRTAPSPPSLMSFADIANTSLAITWKGPPDWTDY 1508
Cdd:COG3401   500 SGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGAS 541

FN3

Fibronectin type 3 domain [General function prediction only];

786-1153

5.59e-07

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 55.01 E-value: 5.59e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049  786 TSSLFTNWTQAQGDVEFYQVLLIHENVVIKNESISSETSRYSFHSLKSGSLYSVVVTTVSGGISSRQ----VVVEGRTVP 861
Cdd:COG3401    61 LSSGGGLGTGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTatavAGGAATAGT 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049  862 SSVSGVTVNNSGRNDYLSVSWLLAPGDVDNYEVTLSHDGKVVQSLVIAKSVRECSFSSLTPGRLYTVTITTRSGKYEN-- 939
Cdd:COG3401   141 YALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESap 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049  940 ---HSFSQERTVPDKVQGVSVSnSARSDYLRVSWV-HATGDFDHYEVTIKNKNNFIQTKSIPKSENECVFVQLVPGRLYS 1015
Cdd:COG3401   221 sneVSVTTPTTPPSAPTGLTAT-ADTPGSVTLSWDpVTESDATGYRVYRSNSGDGPFTKVATVTTTSYTDTGLTNGTTYY 299

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1016 VTVTTKSGQYEANEQGN------GRTIPEPVKDLTLRNRSTEDLHVTWSGA-NGDVDQYEIqllFNDMKVFPPFHLVN-- 1086
Cdd:COG3401   300 YRVTAVDAAGNESAPSNvvsvttDLTPPAAPSGLTATAVGSSSITLSWTASsDADVTGYNV---YRSTSGGGTYTKIAet 376

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578824049 1087 -TATEYRFTSLTPGRQYKILVLTISGDVQQSAFIEGFTVPSAVKNIHISPNGATDSLTVNWTPGGGDV 1153
Cdd:COG3401   377 vTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAA 444

FN3

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

328-410

7.39e-07

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 48.76 E-value: 7.39e-07

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049    328 PLPPARFGVSKekTTSTSLHVWWT-PSSGKVTSYEVQLFDENNQK-IQGVQIQESTSWNEYTFFNLTAGSKYNIAITAVS 405
Cdd:smart00060    1 PSPPSNLRVTD--VTSTSVTLSWEpPPDDGITGYIVGYRVEYREEgSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78


                    ....*
gi 578824049    406 GGKRS 410
Cdd:smart00060   79 GAGEG 83

fn3

Fibronectin type III domain;

1305-1378

9.04e-07

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 48.57 E-value: 9.04e-07

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578824049  1305 AVTDLRITENSTRHLSFRWTASE---GELSWYNIFLYNPDGNLQERAQVDPLVQ-SFSFQNLLQGRMYKMVIVTHSGE 1378
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNEITVPGTTtSVTLTGLKPGTEYEVRVQAVNGG 79

fn3

Fibronectin type III domain;

509-582

1.43e-06

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 48.18 E-value: 1.43e-06

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578824049   509 EVSNLKVTNDGSlTSLKVKWQRPP---GNVDSYNITLSHKGTIKE--SRVLAPWITETHFKELVPGRLYQVTVSCVSGE 582
Cdd:pfam00041    2 APSNLTVTDVTS-TSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPwnEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

PTP_PTEN

cd14509

protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...

2067-2153

2.85e-06

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: 49.12 E-value: 2.85e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2067 CGEEQLDAHRlirhFHYTV----WPDHGVPeTTQSLIQFVRTVRDYINRSPGAgPTVVHCSAGVGRTGTFIA--LDRILQ 2140
Cdd:cd14509    48 CSERSYDPSK----FNGRVaeypFDDHNPP-PLELIKPFCEDVDEWLKEDEKN-VAAVHCKAGKGRTGVMICcyLLYLGK 121

                          90
                  ....*....|...
gi 578824049 2141 QLDSKDSVDIYGA 2153
Cdd:cd14509   122 FPSAKEALDFYGA 134

fn3

Fibronectin type III domain;

774-847

3.80e-06

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 47.02 E-value: 3.80e-06

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578824049   774 QVTDLHVANQGmTSSLFTNWT---QAQGDVEFYQVLLIHENV--VIKNESISSETSRYSFHSLKSGSLYSVVVTTVSGG 847
Cdd:pfam00041    2 APSNLTVTDVT-STSLTVSWTpppDGNGPITGYEVEYRPKNSgePWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

fn3

Fibronectin type III domain;

1215-1294

3.88e-06

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 47.02 E-value: 3.88e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049  1215 SVQGVIADNAySSYSLIVSWQKAA---GVAERYDILLLTENGI-LLRNTSEPATTKQHKFEDLTPGKKYKIQILTVSGGL 1290
Cdd:pfam00041    2 APSNLTVTDV-TSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGePWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....
gi 578824049  1291 FSKE 1294
Cdd:pfam00041   81 EGPP 84

PTP_VSP_TPTE

cd14510

protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...

2064-2175

4.39e-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: 49.28 E-value: 4.39e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2064 FKICGEEQLDAhrliRHFHYTV----WPDHGVPeTTQSLIQFVRTVRDYINRSPgAGPTVVHCSAGVGRTGTFIA--LDR 2137
Cdd:cd14510    59 YNLCSERGYDP----KYFHNRVervpIDDHNVP-TLDEMLSFTAEVREWMAADP-KNVVAIHCKGGKGRTGTMVCawLIY 132

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 578824049 2138 ILQQLDSKDSVDIYGAVH-DLRL-HRVHMVQTECQYVYLH 2175
Cdd:cd14510   133 SGQFESAKEALEYFGERRtDKSVsSKFQGVETPSQSRYVG 172

beta-trefoil_Ricin_GALNT1-like

cd23433

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...

34-94

8.35e-06

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 1 (GALNT1)-like subfamily; The GALNT1-like subfamily includes GALNT1 and GALNT13. They catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT1 has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b and Muc7. GALNT13 has a much stronger activity than GALNT1 to transfer GalNAc to mucin peptides, such as Muc5Ac and Muc7. It can glycosylate SDC3. It may be responsible for the synthesis of Tn antigen in neuronal cells. Members of this subfamily comprise a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

Pssm-ID: 467311 [Multi-domain] Cd Length: 127 Bit Score: 47.31 E-value: 8.35e-06

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578824049   34 KNEKVVVGSCNRTIQNQQWMWTEDEK-LLHVKSALCLAISNSSrgPSRSAILDRCSQAP--RWT 94
Cdd:cd23433    63 KGGPVKLEKCHGMGGNQEWEYDKETKqIRHVNSGLCLTAPNED--DPNEPVLRPCDGGPsqKWE 124

FN3

Fibronectin type 3 domain [General function prediction only];

380-586

1.02e-05

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 50.77 E-value: 1.02e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049  380 STSWNEYTFFNLTAGSKYNIAITAVSGGKRS-----FSVYTNgSTVPSPVKDI-GISTKANSLLISWS-HGSGNVERYRL 452
Cdd:COG3401   188 TSTTLVDGGGDIEPGTTYYYRVAATDTGGESapsneVSVTTP-TTPPSAPTGLtATADTPGSVTLSWDpVTESDATGYRV 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049  453 --MLMDKGILVHggVVDKHATSYAFHGLTPG--YLYNLTVMTEA---AGLQNYRW-KLVRTAPMEVSNLKVTNDGSlTSL 524
Cdd:COG3401   267 yrSNSGDGPFTK--VATVTTTSYTDTGLTNGttYYYRVTAVDAAgneSAPSNVVSvTTDLTPPAAPSGLTATAVGS-SSI 343

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578824049  525 KVKWQRPPG-NVDSYNItlsHKGTIKES--RVLAPWITETHF--KELVPGRLYQVTVSCV--SGELSAQ 586
Cdd:COG3401   344 TLSWTASSDaDVTGYNV---YRSTSGGGtyTKIAETVTTTSYtdTGLTPGTTYYYKVTAVdaAGNESAP 409

FN3

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

1479-1571

1.17e-05

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 45.95 E-value: 1.17e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1479 PSPPSLMSFADIANTSLAITWKGPPDWTDYND-FELQWLPRDALTVFNPYNNRKSEGR-IVYGLRPGRSYQFNVKTVSGD 1556
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITgYVVEYREKGSGDWKEVEVTPGSETSyTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|....*
gi 578824049 1557 SWKTYSKPIfgSVRT 1571
Cdd:cd00063    81 GESPPSESV--TVTT 93

beta-trefoil_Ricin_MRC2

cd23408

ricin B-type lectin domain, beta-trefoil fold, found in macrophage mannose receptor 2 (MRC2) ...

21-109

1.27e-05

ricin B-type lectin domain, beta-trefoil fold, found in macrophage mannose receptor 2 (MRC2) and similar proteins; MRC2, also called C-type mannose receptor 2, C-type lectin domain family 13 member E (CLEC13E), endocytic receptor 180 (Endo180), urokinase-type plasminogen activator receptor-associated protein (UPARAP), UPAR-associated protein, urokinase receptor-associated protein, or CD280, may play a role as endocytotic lectin receptor displaying calcium-dependent lectin activity. It internalizes glycosylated ligands from the extracellular space for release in an endosomal compartment via clathrin-mediated endocytosis. It may be involved in plasminogen activation system controlling the extracellular level of PLAUR/PLAU, and thus may regulate protease activity at the cell surface. It may contribute to cellular uptake, remodeling, and degradation of extracellular collagen matrices. It may play a role during cancer progression as well as in other chronic tissue destructive diseases acting on collagen turnover. It may participate in remodeling of extracellular matrix cooperating with the matrix metalloproteinases (MMPs). MRC2 contains an atypical ricin B-type lectin domain at the N-terminus. The typical ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket. In contrast, the ninth, tenth and eleventh beta strands, comprising the gamma subdomain, are missing in the ricin B-type lectin domain of MRC2.

Pssm-ID: 467786 Cd Length: 124 Bit Score: 46.71 E-value: 1.27e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049   21 FQIVHVQKQQCLFKNEKVV--VGSCNRTIQNQQWMWTEDEKLLHVKSALCLAISNSSRGPSRSAI-LDRCSQAP---RWT 94
Cdd:cd23408     3 FLIYSDGAQGCLEVRDSVVrlSPACNTSSPAQQWKWVSRNRLFNLGSMQCLGVSGPNGSGTSATLgTYECDRESvnmRWH 82

                          90
                  ....*....|....*
gi 578824049   95 CydqEGFLEVENASL 109
Cdd:cd23408    83 C---RTLGEQLSQHL 94

FN3

Fibronectin type 3 domain [General function prediction only];

302-452

1.73e-05

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 50.00 E-value: 1.73e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049  302 DLQAGTIYNFRIISLDEERT---------VVLQTDPLPPArfGVSKEKTTSTSLHVWWTPSSGK-VTSYEVQLFDENNQK 371
Cdd:COG3401   198 DIEPGTTYYYRVAATDTGGEsapsnevsvTTPTTPPSAPT--GLTATADTPGSVTLSWDPVTESdATGYRVYRSNSGDGP 275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049  372 IqgVQIQESTSwNEYTFFNLTAGSKYNIAITAV-SGGKRS-FSVY---TNGSTVPSPVKDI-GISTKANSLLISWSHGSG 445
Cdd:COG3401   276 F--TKVATVTT-TSYTDTGLTNGTTYYYRVTAVdAAGNESaPSNVvsvTTDLTPPAAPSGLtATAVGSSSITLSWTASSD 352


                  ....*...
gi 578824049  446 -NVERYRL 452
Cdd:COG3401   353 aDVTGYNV 360

FN3

Fibronectin type 3 domain [General function prediction only];

639-960

2.42e-05

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 49.62 E-value: 2.42e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049  639 NITVGKEETQYVMDDTGLVPGRQYE--VEVIVESGNLKNSERC---QGRTVPLAVLQLRVKHANETSLSIMWqTPVAEW- 712
Cdd:COG3401   182 TTSLTVTSTTLVDGGGDIEPGTTYYyrVAATDTGGESAPSNEVsvtTPTTPPSAPTGLTATADTPGSVTLSW-DPVTESd 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049  713 -EKYIISLADRDllliHKSLSK----DAKEFTFTDLVPGRKYMATVTSISGDLKNS------SSVKGRTVPAQVTDLHVA 781
Cdd:COG3401   261 aTGYRVYRSNSG----DGPFTKvatvTTTSYTDTGLTNGTTYYYRVTAVDAAGNESapsnvvSVTTDLTPPAAPSGLTAT 336

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049  782 NQGMTS-SLftNWTQAQG-DVEFYQVL----------LIHENVviknesisSETSrYSFHSLKSGSLYSVVVTTV-SGGI 848
Cdd:COG3401   337 AVGSSSiTL--SWTASSDaDVTGYNVYrstsgggtytKIAETV--------TTTS-YTDTGLTPGTTYYYKVTAVdAAGN 405

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049  849 SSRQvvvegrtvPSSVSGVTVNNSGRNDYLSVSWLLAPGDVDNYEVTLSHDGKVVQSLVIAKSVRECSFSSLTPGRLYTV 928
Cdd:COG3401   406 ESAP--------SEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTV 477

                         330       340       350
                  ....*....|....*....|....*....|..
gi 578824049  929 TITTRSGKYENHSFSQERTVPDKVQGVSVSNS 960
Cdd:COG3401   478 TATTTDTTTANLSVTTGSLVGGSGASSVTNSV 509

beta-trefoil_Ricin_GALNT11

cd23440

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...

21-94

2.59e-05

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide N-acetylgalactosaminyltransferase 11 (GALNT11) and similar proteins; GALNT11 (EC 2.4.1.41), also called polypeptide GalNAc transferase 11, GalNAc-T11, pp-GaNTase 11, protein-UDP acetylgalactosaminyltransferase 11, or UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11, catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. It is involved in left/right asymmetry by mediating O-glycosylation of NOTCH1. O-glycosylation of NOTCH1 promotes its activation, modulating the balance between motile and immotile (sensory) cilia at the left-right organizer (LRO). GALNT11 displays the same enzyme activity toward MUC1, MUC4, and EA2 as GALNT1. It is not involved in glycosylation of erythropoietin (EPO). GALNT11 comprises a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

Pssm-ID: 467318 [Multi-domain] Cd Length: 127 Bit Score: 45.83 E-value: 2.59e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049   21 FQIVHVQKQQCLF-------KNEKVVVGSCNRTIQNQQWMWTEDEKLLhVKSALCLAISNSSRGPSRsaiLDRC-----S 88
Cdd:cd23440     6 GQLKHAGSGLCLVaedevsqKGSLLVLRPCSRNDKKQLWYYTEDGELR-LANLLCLDSSETSSDFPR---LMKChgsggS 81


                  ....*.
gi 578824049   89 QapRWT 94
Cdd:cd23440    82 Q--QWR 85

FN3

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

1479-1558

3.66e-05

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 44.14 E-value: 3.66e-05

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049   1479 PSPPSLMSFADIANTSLAITWKGPPD--WTDYND-FELQWLPRDALTVFNPYNNRKSEGRIVyGLRPGRSYQFNVKTVSG 1555
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDdgITGYIVgYRVEYREEGSEWKEVNVTPSSTSYTLT-GLKPGTEYEFRVRAVNG 79


                    ...
gi 578824049   1556 DSW 1558
Cdd:smart00060   80 AGE 82

beta-trefoil_Ricin_MRC1

cd23407

ricin B-type lectin domain, beta-trefoil fold, found in macrophage mannose receptor 1 (MRC1) ...

21-111

6.17e-05

ricin B-type lectin domain, beta-trefoil fold, found in macrophage mannose receptor 1 (MRC1) and similar proteins; MRC1, also called MMR, C-type lectin domain family 13 member D (CLEC13D), C-type lectin domain family 13 member D-like (CLEC13DL), macrophage mannose receptor 1-like protein 1 (MRC1L1), or CD206, mediates the endocytosis of glycoproteins by macrophages. It binds both sulfated and non-sulfated polysaccharide chains. MRC1 acts as phagocytic receptor for bacteria, fungi and other pathogens. It also acts as a receptor for Dengue virus envelope protein E. MRC1 contains a ricin B-type lectin domain at the N-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.

Pssm-ID: 467785 Cd Length: 123 Bit Score: 44.66 E-value: 6.17e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049   21 FQIVHVQKQQCL-FKNEKVVV-GSCNRTIQNQQWMWTEDEKLLHVKSALCLAISNSSRGpsrSAI-LDRCSQAP---RWT 94
Cdd:cd23407     3 FLIYNEDHNRCVqARSSSSVTtATCNPNAESQKFRWVSGSQILSVAFKLCLGVPSKKDW---VTVtLFPCNEKSelqKWE 79

                          90
                  ....*....|....*..
gi 578824049   95 CYDqEGFLEVENASLFL 111
Cdd:cd23407    80 CKN-DTLLALKGEDLYF 95

FN3

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

507-581

6.52e-05

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 43.37 E-value: 6.52e-05

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049    507 PMEVSNLKVTNDGSlTSLKVKWQRPP-GNVDSYNITLSHKGTIKESRVL----APWITETHFKELVPGRLYQVTVSCVSG 581
Cdd:smart00060    1 PSPPSNLRVTDVTS-TSVTLSWEPPPdDGITGYIVGYRVEYREEGSEWKevnvTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

FN3

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

595-672

6.79e-05

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 43.37 E-value: 6.79e-05

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049    595 PDKVANLEANNNGRmRSLVVSWSPPAGDWE-----QYRILLFNDSVVLLNITVGKEETQYVmdDTGLVPGRQYEVEVIVE 669
Cdd:smart00060    1 PSPPSNLRVTDVTS-TSVTLSWEPPPDDGItgyivGYRVEYREEGSEWKEVNVTPSSTSYT--LTGLKPGTEYEFRVRAV 77


                    ...
gi 578824049    670 SGN 672
Cdd:smart00060   78 NGA 80

FN3

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

1125-1199

8.34e-05

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 43.25 E-value: 8.34e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1125 PSAVKNIHISPNGATdSLTVNWTP---GGGDVDSYTVSaFRHSQKVDSQTIPKHVF---EHTFHRLEAGEQYQIMIASVS 1198
Cdd:cd00063     1 PSPPTNLRVTDVTST-SVTLSWTPpedDGGPITGYVVE-YREKGSGDWKEVEVTPGsetSYTLTGLKPGTEYEFRVRAVN 78


                  .
gi 578824049 1199 G 1199
Cdd:cd00063    79 G 79

DUSP23

cd14504

dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...

2067-2134

1.00e-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: 44.58 E-value: 1.00e-04

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578824049 2067 CGEEQLDAHRLIRHFHYTVwPDHGVPeTTQSLIQFVRTVRDYINRSpgaGPTVVHCSAGVGRTGTFIA 2134
Cdd:cd14504    39 PPPEHSDTCPGLRYHHIPI-EDYTPP-TLEQIDEFLDIVEEANAKN---EAVLVHCLAGKGRTGTMLA 101

fn3

Fibronectin type III domain;

255-316

2.18e-04

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 42.02 E-value: 2.18e-04

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578824049   255 SSHSVSIQWRIL----GSPCNFSLIYSSDTLGAALcPTFRIDNTTYGCNLQDLQAGTIYNFRIISL 316
Cdd:pfam00041   12 TSTSLTVSWTPPpdgnGPITGYEVEYRPKNSGEPW-NEITVPGTTTSVTLTGLKPGTEYEVRVQAV 76

FN3

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

949-1026

2.21e-04

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 42.10 E-value: 2.21e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049  949 PDKVQGVSVSNSArSDYLRVSWVHATGD---FDHYEVTIKNKN--NFIQTKSIPKSENECVFVQLVPGRLYSVTVTTKSG 1023
Cdd:cd00063     1 PSPPTNLRVTDVT-STSVTLSWTPPEDDggpITGYVVEYREKGsgDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79


                  ...
gi 578824049 1024 QYE 1026
Cdd:cd00063    80 GGE 82

FN3

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

1037-1112

2.44e-04

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 42.10 E-value: 2.44e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1037 PEPVKDLTLRNRSTEDLHVTWS---GANGDVDQYEIQL---LFNDMKVFPPFhlVNTATEYRFTSLTPGRQYKILVLTIS 1110
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTppeDDGGPITGYVVEYrekGSGDWKEVEVT--PGSETSYTLTGLKPGTEYEFRVRAVN 78


                  ..
gi 578824049 1111 GD 1112
Cdd:cd00063    79 GG 80

beta-trefoil_Ricin_GALNT11

cd23440

ricin B-type lectin domain, beta-trefoil fold, found in polypeptide ...

50-92

2.49e-04

Pssm-ID: 467318 [Multi-domain] Cd Length: 127 Bit Score: 43.14 E-value: 2.49e-04

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 578824049   50 QQWMWTEDEKLLHVKSALCLAISNSSRGPsrSAILDRCSQAPR 92
Cdd:cd23440    82 QQWRFKKDNRLYNPASGQCLAASKNGTSG--YVTMDICSDSPS 122

beta-trefoil_Ricin_LY75

cd23411

ricin B-type lectin domain, beta-trefoil fold, found in lymphocyte antigen 75 (Ly-75) and ...

21-75

3.33e-04

ricin B-type lectin domain, beta-trefoil fold, found in lymphocyte antigen 75 (Ly-75) and similar proteins; Ly-75, also called C-type lectin domain family 13 member B, DEC-205, gp200-MR6, or CD205, acts as an endocytic receptor to direct captured antigens from the extracellular space to a specialized antigen-processing compartment. It causes reduced proliferation of B-lymphocytes. Ly-75 contains a ricin B-type lectin domain at the N-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.

Pssm-ID: 467789 Cd Length: 116 Bit Score: 42.42 E-value: 3.33e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578824049   21 FQIVHVQKQQCL-FKNEKVVVGSCNRTIQNQQWMWTEDEKLLHVKSALCLAISNSS 75
Cdd:cd23411     5 FTIQHENSGKCLkVENSQISAVDCKQSSESLQWKWVSEHRLFNLGSKQCLGLDITK 60

beta-trefoil_Ricin_unchar

cd23412

ricin B-type lectin domain, beta-trefoil fold, found in uncharacterized macrophage mannose ...

20-124

3.67e-04

ricin B-type lectin domain, beta-trefoil fold, found in uncharacterized macrophage mannose receptor (MRC)-like proteins; The subfamily corresponds to a group of uncharacterized ricin B-type lectin beta-trefoil domain-containing proteins from Gnathostomata. They show high sequence similarity with macrophage mannose receptor (MRC) family proteins.

Pssm-ID: 467790 Cd Length: 127 Bit Score: 42.39 E-value: 3.67e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049   20 GFQIVHVQKQQCLF----KNEKVVVGSCNRTIQNQQWMWTEDEK-LLHVKSALCLAISNsSRGPSrSAILDRC----SQA 90
Cdd:cd23412     4 GFMIRNVQLEKCIQvdhgESERVSLAECKPHSEHQQWSWDPETRaLSSLHTGECLTVLK-IQEFG-SVRLEPCgsrePQA 81

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 578824049   91 prWTCyDQEGFLEVENASLFL--QKQGSRVVVKKAR 124
Cdd:cd23412    82 --WSC-SKKGHLTLQGLGLHLsaRHSSHKVFVSKEK 114

beta-trefoil_Ricin_GALNT14-like

cd23441

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide ...

27-94

3.87e-04

ricin B-type lectin domain, beta-trefoil fold, found in the polypeptide N-acetylgalactosaminyltransferase 14 (GALNT14)-like subfamily; The GALNT14-like subfamily includes GALNT14 and GALNT16. They act as GalNAc transferases (EC 2.4.1.41) that catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. GALNT14 displays activity toward mucin-derived peptide substrates such as Muc2, Muc5AC, Muc7, and Muc13 (-58). It may be involved in O-glycosylation in the kidney. Members of this subfamily comprise a glycosyltransferase region and a ricin B-type lectin domain. The glycosyltransferase region contains two conserved domains, domain A (also called GT1 motif) and domain B (also called Gal/GalNAc-T motif). This model corresponds to the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.

Pssm-ID: 467319 [Multi-domain] Cd Length: 122 Bit Score: 42.39 E-value: 3.87e-04

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578824049   27 QKQQCL-------FKNEKVVVGSCNRTIQNQQWMWTEDEKLLHvkSALCLAISNSSRGPsrSAILDRCSQAP--RWT 94
Cdd:cd23441    10 QGNLCLdsdeqlfQGPALLILAPCSNSSDSQEWSFTKDGQLQT--QGLCLTVDSSSKDL--PVVLETCSDDPkqKWT 82

Ricin_B_lectin

pfam00652

Ricin-type beta-trefoil lectin domain;

22-93

4.52e-04

Ricin-type beta-trefoil lectin domain;

Pssm-ID: 395527 [Multi-domain] Cd Length: 126 Bit Score: 42.13 E-value: 4.52e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049    22 QIVHVQKQQCL-----FKNEKVVVGSCNRTIQNQQWMWTED-EKLLHVKSALCLAISNSSRGPSRsAILDRC-----SQa 90
Cdd:pfam00652   47 TIRSVASDLCLdvgstADGAKVVLWPCHPGNGNQRWRYDEDgTQIRNPQSGKCLDVSGAGTSNGK-VILWTCdsgnpNQ- 124


                   ...
gi 578824049    91 pRW 93
Cdd:pfam00652  125 -QW 126

Ricin_B_lectin

pfam00652

Ricin-type beta-trefoil lectin domain;

21-100

5.64e-04

Ricin-type beta-trefoil lectin domain;

Pssm-ID: 395527 [Multi-domain] Cd Length: 126 Bit Score: 41.75 E-value: 5.64e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049    21 FQIVHVQKQQCL------FKNEKVVVGSCNRTIQNQQWMWTEDEKLLHVKSALCLAISNSSRGpsRSAILDRCSQAP--- 91
Cdd:pfam00652    3 GRIRNRASGKCLdvpggsSAGGPVGLYPCHGSNGNQLWTLTGDGTIRSVASDLCLDVGSTADG--AKVVLWPCHPGNgnq 80


                   ....*....
gi 578824049    92 RWTcYDQEG 100
Cdd:pfam00652   81 RWR-YDEDG 88

DSPc

smart00195

Dual specificity phosphatase, catalytic domain;

2080-2158

6.28e-04

Dual specificity phosphatase, catalytic domain;

Pssm-ID: 214551 [Multi-domain] Cd Length: 138 Bit Score: 41.88 E-value: 6.28e-04

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049   2080 HFHYTVWPdhgVPETTQSLI-QFVRTVRDYINRS-PGAGPTVVHCSAGVGRTGTFIAldRILQQLDSKDSVDIYGAVHDL 2157
Cdd:smart00195   44 DFTYLGVP---IDDNTETKIsPYFPEAVEFIEDAeSKGGKVLVHCQAGVSRSATLII--AYLMKTRNMSLNDAYDFVKDR 118


                    .
gi 578824049   2158 R 2158
Cdd:smart00195  119 R 119

fn3

Fibronectin type III domain;

422-488

9.47e-04

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 40.09 E-value: 9.47e-04

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578824049   422 SPVKDIGISTK-ANSLLISWS---HGSGNVERYRLML--MDKGILVHGGVVDKHATSYAFHGLTPGYLYNLTV 488
Cdd:pfam00041    1 SAPSNLTVTDVtSTSLTVSWTpppDGNGPITGYEVEYrpKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRV 73

FN3

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

949-1024

9.73e-04

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 39.91 E-value: 9.73e-04

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049    949 PDKVQGVSVSNSArSDYLRVSWVH-----ATGDFDHYEVTIKNKNNFIQTKSIPKSENECVFVQLVPGRLYSVTVTTKSG 1023
Cdd:smart00060    1 PSPPSNLRVTDVT-STSVTLSWEPppddgITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79


                    .
gi 578824049   1024 Q 1024
Cdd:smart00060   80 A 80

FN3

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

595-672

9.86e-04

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 40.17 E-value: 9.86e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049  595 PDKVANLEANNNGRmRSLVVSWSPPAGD---WEQYRILLF---NDSVVLLNITVGKEeTQYVMddTGLVPGRQYEVEVIV 668
Cdd:cd00063     1 PSPPTNLRVTDVTS-TSVTLSWTPPEDDggpITGYVVEYRekgSGDWKEVEVTPGSE-TSYTL--TGLKPGTEYEFRVRA 76


                  ....
gi 578824049  669 ESGN 672
Cdd:cd00063    77 VNGG 80

PTP_PTEN-like

cd14497

protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...

2086-2134

9.90e-04

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: 41.80 E-value: 9.90e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 578824049 2086 WPDHGVPeTTQSLIQFVRTVRDYINRSPG--AgptVVHCSAGVGRTGTFIA 2134
Cdd:cd14497    68 FPDHHPP-PLGLLLEIVDDIDSWLSEDPNnvA---VVHCKAGKGRTGTVIC 114

FN3

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

1037-1111

1.07e-03

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 39.91 E-value: 1.07e-03

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049   1037 PEPVKDLTLRNRSTEDLHVTWS-----GANGDVDQYEIQLLFNDMKVFPpFHLVNTATEYRFTSLTPGRQYKILVLTISG 1111
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEpppddGITGYIVGYRVEYREEGSEWKE-VNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

FN3

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

685-758

1.13e-03

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 39.91 E-value: 1.13e-03

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578824049    685 PLAVLQLRVKHANETSLSIMWQTPVAEWE-----KYIISLADRDLLLIHKSLSKDAKEFTFTDLVPGRKYMATVTSISG 758
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItgyivGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

FN3

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

1125-1199

1.47e-03

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 39.52 E-value: 1.47e-03

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049   1125 PSAVKNIHISPNGATdSLTVNWTP-----GGGDVDSYTVSAFRHSQKVDSQTIPKHVFEHTFHRLEAGEQYQIMIASVSG 1199
Cdd:smart00060    1 PSPPSNLRVTDVTST-SVTLSWEPppddgITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

beta-trefoil_Ricin_laminarinase

cd23451

ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and ...

37-94

1.57e-03

ricin B-type lectin domain, beta-trefoil fold, found in glucan endo-1,3-beta-glucosidase and similar proteins; Glucan endo-1,3-beta-glucosidase (EC 3.2.1.39), also called (1->3)-beta-glucan endohydrolase, or (1->3)-beta-glucanase, or laminarinase, belongs to the glycosyl hydrolase 64 (GH64) family. It catalyzes hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans. It has been implicated in the defense against fungal pathogens. Glucan endo-1,3-beta-glucosidase contains a C-terminal ricin B-type lectin domain with a beta-trefoil fold, characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.

Pssm-ID: 467329 [Multi-domain] Cd Length: 125 Bit Score: 40.78 E-value: 1.57e-03

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049   37 KVVVGSCNRTIqNQQWMWTEDEKLLHVKSALCLAISNSSRGPSRSAILDRC--SQAPRWT 94
Cdd:cd23451    67 LVQLWDCNGTG-AQKWVPRADGTLYNPQSGKCLDAPGGSTTDGTQLQLYTCngTAAQQWT 125

TpbA-like

cd14529

bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...

2078-2159

1.81e-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: 41.21 E-value: 1.81e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2078 IRHFHYTVWPDHGVPETTQSLIQFVRTVRDYINRspgaGPTVVHCSAGVGRTGTFIALDRILQQLDSKDsvdiygAVHDL 2157
Cdd:cd14529    56 IDGVKYVNLPLSATRPTESDVQSFLLIMDLKLAP----GPVLIHCKHGKDRTGLVSALYRIVYGGSKEE------ANEDY 125


                  ..
gi 578824049 2158 RL 2159
Cdd:cd14529   126 RL 127

FN3

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

685-770

2.78e-03

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 39.02 E-value: 2.78e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049  685 PLAVLQLRVKHANETSLSIMWQTPV---AEWEKYIISL--ADRDLLLIHKSLSKDAKEFTFTDLVPGRKYMATVTSISGD 759
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYreKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|...
gi 578824049  760 L--KNSSSVKGRT 770
Cdd:cd00063    81 GesPPSESVTVTT 93

FN3

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

1391-1465

3.55e-03

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 38.36 E-value: 3.55e-03

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049   1391 PASVSHLRGSNrNTTDSLWFNWSPASGDFDFYELILYNP-NGTKKENWK----DKDLTEWRFQGLVPGRKYVLWVVTHSG 1465
Cdd:smart00060    1 PSPPSNLRVTD-VTSTSVTLSWEPPPDDGITGYIVGYRVeYREEGSEWKevnvTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

PTP_PTPDC1

cd14506

protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...

2078-2180

4.80e-03

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

Pssm-ID: 350356 [Multi-domain] Cd Length: 206 Bit Score: 40.80 E-value: 4.80e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 2078 IRHFHYTvWPDHGVPeTTQSLIQFVRTVRDYINRSpgaGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSvdiygAVHDL 2157
Cdd:cd14506    77 IYFYNFG-WKDYGVP-SLTTILDIVKVMAFALQEG---GKVAVHCHAGLGRTGVLIACYLVYALRMSADQ-----AIRLV 146

                          90       100
                  ....*....|....*....|...
gi 578824049 2158 RLHRVHMVQTECQYvylhQCVRD 2180
Cdd:cd14506   147 RSKRPNSIQTRGQV----LCVRE 165

RICIN

smart00458

Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.

22-94

5.59e-03

Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.

Pssm-ID: 214672 [Multi-domain] Cd Length: 118 Bit Score: 39.03 E-value: 5.59e-03

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578824049     22 QIVHVQKQQCLF----KNEKVVVGSCNRTIQNQQWMWTEDEKLLHVKSALCLAISNSSrgPSRSAILDRCSQAP--RWT 94
Cdd:smart00458   40 AIRIKDTDLCLTangnTGSTVTLYSCDGTNDNQYWEVNKDGTIRNPDSGKCLDVKDGN--TGTKVILWTCSGNPnqKWI 116

COG4733

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

1389-1557

6.00e-03

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

Pssm-ID: 443767 [Multi-domain] Cd Length: 978 Bit Score: 41.85 E-value: 6.00e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1389 TVPASVSHLRGSNRNTTDSLWFNWSPASGDFDfYELILYNPNGtkkeNWKDK---DLTEWRFQGLVPGRKYV-LWVVTHS 1464
Cdd:COG4733   535 NVTTSESLSVVAQGTAVTTLTVSWDAPAGAVA-YEVEWRRDDG----NWVSVprtSGTSFEVPGIYAGDYEVrVRAINAL 609

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1465 GDLSNKVTAESRT------APSPPSlmSF-ADIANTSLAITWKGPPDwTDYNDFELQWLPR----DALTVFNPYNNRKSe 1533
Cdd:COG4733   610 GVSSAWAASSETTvtgktaPPPAPT--GLtATGGLGGITLSWSFPVD-ADTLRTEIRYSTTgdwaSATVAQALYPGNTY- 685

                         170       180
                  ....*....|....*....|....*.
gi 578824049 1534 grIVYGLRPGRSYQFNVKTV--SGDS 1557
Cdd:COG4733   686 --TLAGLKAGQTYYYRARAVdrSGNV 709

FN3

Fibronectin type 3 domain [General function prediction only];

1435-1606

6.42e-03

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 41.53 E-value: 6.42e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1435 ENWKDKDLTEWRFQGLVPGRKYVLWVVthSGDLSNKVTAESRTAPSPPSLMSFADIANTSLAITWKGPPDWTDYNDFELQ 1514
Cdd:COG3401    91 ATGLTTLTGSGSVGGATNTGLTSSDEV--PSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGV 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049 1515 WLPRDALTVFNPYN-----NRKSEGRIVYGLRPGRSYQFNVKTVSGDSWKTYSKPIFGSV-RTKPDKIQNLHCRPQNSTA 1588
Cdd:COG3401   169 VVSPDTSATAAVATtsltvTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTpTTPPSAPTGLTATADTPGS 248

                         170
                  ....*....|....*....
gi 578824049 1589 IACSWIP-PDSDFDGYSIE 1606
Cdd:COG3401   249 VTLSWDPvTESDATGYRVY 267

FN3

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

861-936

7.54e-03

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 37.59 E-value: 7.54e-03

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049    861 PSSVSGVTVNNSGRNdYLSVSWLLAPGD-----VDNYEVTLSHDGKVVQSLVIAKSVRECSFSSLTPGRLYTVTITTRSG 935
Cdd:smart00060    1 PSPPSNLRVTDVTST-SVTLSWEPPPDDgitgyIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79


                    .
gi 578824049    936 K 936
Cdd:smart00060   80 A 80

CDC14_C

cd14499

C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...

2087-2135

7.78e-03

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: 39.36 E-value: 7.78e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 578824049 2087 PDHGVPeTTQSLIQFVRTVRdyinRSPGAgpTVVHCSAGVGRTGTFIAL 2135
Cdd:cd14499    88 PDGSTP-SDDIVKKFLDICE----NEKGA--IAVHCKAGLGRTGTLIAC 129

beta-trefoil_Ricin_XLN-like

cd23418

ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ...

37-94

7.93e-03

ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1,4-beta-xylanase and similar proteins; The family includes Streptomyces olivaceoviridis endo-1,4-beta-xylanase (XLN, EC 3.2.1.8), Streptomyces avermitilis beta-L-arabinopyranosidase (EC 3.2.1.185), and Streptomyces coelicolor extracellular exo-alpha-L-arabinofuranosidase (ABF, EC 3.2.1.55). XLN, also called xylanase, or 1,4-beta-D-xylan xylanohydrolase, belongs to the glycosyl hydrolase 10 (cellulase F) family. It contributes to hydrolyze hemicellulose, the major component of plant cell walls. XLN contains a (beta/alpha)8-barrel as a catalytic domain, a family 13 carbohydrate binding module (CBM13) as a xylan binding domain (XBD) and a Gly/Pro-rich linker between them. Beta-L-arabinopyranosidase belongs to the glycosyl hydrolase 27 (GH27) family. It has a GH27 catalytic domain, an antiparallel beta-domain containing Greek key motifs, another antiparallel beta-domain forming a jellyroll structure, and a CBM13 module. ScAraf62A, also called ABF, or arabinosidase, or arabinoxylan arabinofuranohydrolase, belongs to the glycosyl hydrolase 62 (GH62) family. It is involved in the degradation of xylan and is a key enzyme in the complete degradation of the plant cell wall. It has a specific arabinofuranose-debranching activity on xylan from gramineae. It acts synergistically with xylanases and binds specifically to xylan. ScAraf62A comprises a CBM13 module at its N-terminus and a catalytic domain at its C-terminus. This model corresponds to the CBM13 module, which is a ricin B-type lectin domain with a beta-trefoil fold, characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may contain a potential sugar-binding pocket.

Pssm-ID: 467297 [Multi-domain] Cd Length: 130 Bit Score: 38.87 E-value: 7.93e-03

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049   37 KVVVGSCNRTiQNQQWMWTEDEKLLHVKSALCLAISNSSRGPSRSAILDRCSQAP--RWT 94
Cdd:cd23418    71 PVVIWPCNGG-ANQKWRFNSDGTIRNVNSGLCLDVAGGGTANGTRLILWSCNGGSnqRWR 129

FN3

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

861-938

8.20e-03

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 37.86 E-value: 8.20e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578824049  861 PSSVSGVTVNNSGRNdYLSVSWLLAPGD---VDNYEVTLS--HDGKVVQSLVIAKSVRECSFSSLTPGRLYTVTITTRSG 935
Cdd:cd00063     1 PSPPTNLRVTDVTST-SVTLSWTPPEDDggpITGYVVEYRekGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79


                  ...
gi 578824049  936 KYE 938
Cdd:cd00063    80 GGE 82

FN3