NCBI Conserved Domain Search

Fibronectin type III domain;

1172-1254

1.79e-12

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 64.74 E-value: 1.79e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999  1172 SPPSLMSFADIANTSLAITWKGPPDWT-DYNDFELQWLPRDALTVFNPYNNRKSEGR-IVYGLRPGRSYQFNVKTVSGDS 1249
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNgPITGYEVEYRPKNSGEPWNEITVPGTTTSvTLTGLKPGTEYEVRVQAVNGGG 80


                   ....*
gi 332800999  1250 WKTYS 1254
Cdd:pfam00041   81 EGPPS 85

fn3

Fibronectin type III domain;

1266-1345

1.17e-10

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 59.35 E-value: 1.17e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999  1266 DKIQNLHCRPQNSTAIACSWIPP---DSDFDGYSIECRKMDTQEVEFSRKLEKEKSLLNIMMLVPHKRYLVSIKVQSAGM 1342
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ...
gi 332800999  1343 TSE 1345
Cdd:pfam00041   81 EGP 83

fn3

Fibronectin type III domain;

642-718

1.28e-10

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 59.35 E-value: 1.28e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999   642 DKVQGVSVSNsARSDYLRVSWVHAT---GDFDHYEVTI--KNKNNFIQTKSIPKSENECVFVQLVPGRLYSVTVTTKSGQ 716
Cdd:pfam00041    1 SAPSNLTVTD-VTSTSLTVSWTPPPdgnGPITGYEVEYrpKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ..
gi 332800999   717 YE 718
Cdd:pfam00041   80 GE 81

fn3

Fibronectin type III domain;

818-891

2.37e-10

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 58.58 E-value: 2.37e-10

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332800999   818 SAVKNIHISPNGATdSLTVNWTP---GGGDVDSYTVSAF--RHSQKVDSQTIPKHVFEHTFHRLEAGEQYQIMIASVSG 891
Cdd:pfam00041    1 SAPSNLTVTDVTST-SLTVSWTPppdGNGPITGYEVEYRpkNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78

fn3

Fibronectin type III domain;

113-189

5.38e-10

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 57.81 E-value: 5.38e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999   113 PARFGVSKEKTTSTSLHVWWTPS---SGKVTSYEVQLFDENNQKiQGVQIQESTSWNEYTFFNLTAGSKYNIAITAVSGG 189
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGE-PWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

fn3

Fibronectin type III domain;

1085-1158

3.87e-09

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 55.11 E-value: 3.87e-09

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332800999  1085 SVSHLRGSNRNTTdSLWFNWSPA---SGDFDFYELILYNPNGTKKENWK--DKDLTEWRFQGLVPGRKYVLWVVTHSGD 1158
Cdd:pfam00041    2 APSNLTVTDVTST-SLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEItvPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

fn3

Fibronectin type III domain;

731-804

1.77e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 53.19 E-value: 1.77e-08

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332800999   731 PVKDLTLRNRSTEDLHVTWSGA---NGDVDQYEIQLL-FNDMKVFPPFHLVNTATEYRFTSLTPGRQYKILVLTISGD 804
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRpKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

fn3

Fibronectin type III domain;

554-630

2.73e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 52.80 E-value: 2.73e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999   554 SSVSGVTVNNSGrNDYLSVSWLLAP---GDVDNYEVTLSH--DGKVVQSLVIAKSVRECSFSSLTPGRLYTVTITTRSGK 628
Cdd:pfam00041    1 SAPSNLTVTDVT-STSLTVSWTPPPdgnGPITGYEVEYRPknSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ..
gi 332800999   629 YE 630
Cdd:pfam00041   80 GE 81

fn3

Fibronectin type III domain;

379-457

4.36e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 52.03 E-value: 4.36e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999   379 AVLQLRVKHANETSLSIMWQTPV---AEWEKYIISLADRD--LLLIHKSLSKDAKEFTFTDLVPGRKYMATVTSISGDLK 453
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNsgEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ....
gi 332800999   454 NSSS 457
Cdd:pfam00041   82 GPPS 85

FN3

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

289-364

1.25e-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: 51.34 E-value: 1.25e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999  289 PMEVSNLKVTNDGSlTSLKVKWQRPP---GNVDSYNITLSHKGTIKESRVLAPWITETHF--KELVPGRLYQVTVSCVSG 363
Cdd:cd00063     1 PSPPTNLRVTDVTS-TSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYtlTGLKPGTEYEFRVRAVNG 79


                  .
gi 332800999  364 E 364
Cdd:cd00063    80 G 80

fn3

Fibronectin type III domain;

997-1070

9.19e-07

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 48.57 E-value: 9.19e-07

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332800999   997 AVTDLRITENSTRHLSFRWTASE---GELSWYNIFLYNPDGNLQERAQVDPLVQ-SFSFQNLLQGRMYKMVIVTHSGE 1070
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNEITVPGTTtSVTLTGLKPGTEYEVRVQAVNGG 79

fn3

Fibronectin type III domain;

907-986

3.76e-06

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 46.64 E-value: 3.76e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999   907 SVQGVIADNAySSYSLIVSWQKAA---GVAERYDILLLTENGI-LLRNTSEPATTKQHKFEDLTPGKKYKIQILTVSGGL 982
Cdd:pfam00041    2 APSNLTVTDV-TSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGePWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....
gi 332800999   983 FSKE 986
Cdd:pfam00041   81 EGPP 84

fn3

Fibronectin type III domain;

466-539

3.83e-06

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 46.64 E-value: 3.83e-06

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332800999   466 QVTDLHVANQGmTSSLFTNWT---QAQGDVEFYQVLLIHEN--VVIKNESISSETSRYSFHSLKSGSLYSVVVTTVSGG 539
Cdd:pfam00041    2 APSNLTVTDVT-STSLTVSWTpppDGNGPITGYEVEYRPKNsgEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

fn3

Fibronectin type III domain;

37-98

2.15e-04

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 41.63 E-value: 2.15e-04

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332800999    37 SSHSVSIQWRIL----GSPCNFSLIYSSDTLGAALcPTFRIDNTTYGCNLQDLQAGTIYNFRIISL 98
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 ...

204-270

9.35e-04

The actual alignment was detected with superfamily member pfam00041:

Pssm-ID: 473895 [Multi-domain] Cd Length: 85 Bit Score: 40.09 E-value: 9.35e-04

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332800999   204 SPVKDIGISTK-ANSLLISWS---HGSGNVERYRLML--MDKGILVHGGVVDKHATSYAFHGLTPGYLYNLTV 270
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 ...

1641-1868

3.07e-179

Pssm-ID: 350465 [Multi-domain] Cd Length: 228 Bit Score: 540.28 E-value: 3.07e-179

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1641 NRYNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 1720
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1721 KCDHYWPADQDSLYYGDLILQMLSESVLPEWTIREFKICGEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDY 1800
Cdd:cd14617    81 KCDHYWPADQDSLYYGDLIVQMLSESVLPEWTIREFKICSEEQLDAPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVRDY 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332800999 1801 INRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 1868
Cdd:cd14617   161 INRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228

PTPc

smart00194

Protein tyrosine phosphatase, catalytic domain;

1612-1870

5.64e-116

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 367.75 E-value: 5.64e-116

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999   1612 LLSKEYEELKDVGR-NQSCDIALLPENRGKNRYNNILPYDATRVKLSNvDDDPCSDYINASYIPGNNFRREYIVTQGPLP 1690
Cdd:smart00194    1 GLEEEFEKLDRLKPdDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKP-PPGEGSDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999   1691 GTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPADQ-DSLYYGDLILQMLSESVLPEWTIREFKICGEEQlDAHRL 1769
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEgEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGC-SETRT 158

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999   1770 IRHFHYTVWPDHGVPETTQSLIQFVRTVRDYinRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDL 1849
Cdd:smart00194  159 VTHYHYTNWPDHGVPESPESILDLIRAVRKS--QSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKEL 236

                           250       260
                    ....*....|....*....|.
gi 332800999   1850 RLHRVHMVQTECQYVYLHQCV 1870
Cdd:smart00194  237 RSQRPGMVQTEEQYIFLYRAI 257

Y_phosphatase

pfam00102

Protein-tyrosine phosphatase;

1637-1870

2.12e-101

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 324.97 E-value: 2.12e-101

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999  1637 NRGKNRYNNILPYDATRVKLSnvDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVE 1716
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999  1717 KGRVKCDHYWP-ADQDSLYYGDL-ILQMLSESVLPEWTIREFKICgEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFV 1794
Cdd:pfam00102   79 KGREKCAQYWPeEEGESLEYGDFtVTLKKEKEDEKDYTVRTLEVS-NGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLL 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332800999  1795 RTVRDYiNRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 1870
Cdd:pfam00102  158 RKVRKS-SLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232

PHA02742

protein tyrosine phosphatase; Provisional

1594-1882

9.42e-43

protein tyrosine phosphatase; Provisional

Pssm-ID: 165109 [Multi-domain] Cd Length: 303 Bit Score: 159.40 E-value: 9.42e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1594 KINQFEGHFMKLQADSN--YLLSKEYEELKDVGRNQSCDIALLPENRGKNRYNNILPYDATRVKLSNvdDDPCSDYINAS 1671
Cdd:PHA02742    7 KKNSFAKNCEQLIEESNlaEILKEEHEHIMQEIVAFSCNESLELKNMKKCRYPDAPCFDRNRVILKI--EDGGDDFINAS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1672 YIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYW-PADQDSLYYGDLILQMLSESVLPE 1750
Cdd:PHA02742   85 YVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYWmPHERGKATHGEFKIKTKKIKSFRN 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1751 WTIREFKICGEEQ---LDahrlIRHFHYTVWPDHGVPETTQSLIQFVRTVR--DYINRSPGAG-------PTVVHCSAGV 1818
Cdd:PHA02742  165 YAVTNLCLTDTNTgasLD----IKHFAYEDWPHGGLPRDPNKFLDFVLAVReaDLKADVDIKGenivkepPILVHCSAGL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332800999 1819 GRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYlhqCVRDVLRARKLRSE 1882
Cdd:PHA02742  241 DRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIF---CYFIVLIFAKLMAD 301

COG5599

Protein tyrosine phosphatase [Signal transduction mechanisms];

1635-1863

1.25e-41

Protein tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 444335 [Multi-domain] Cd Length: 282 Bit Score: 155.25 E-value: 1.25e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1635 PENRGKNRYNNILPYDATRVKlsnvDDDPcsdYINASYIPGNNFRReYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQC 1714
Cdd:COG5599    40 INGSPLNRFRDIQPYKETALR----ANLG---YLNANYIQVIGNHR-YIATQYPLEEQLEDFFQMLFDNNTPVLVVLASD 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1715 VE--KGRVKCDHYWPADQDSLYYgDLILQMLSESVL-PEWTIREFKI----CGEEQLDahrlIRHFHYTVWPDHGVPETT 1787
Cdd:COG5599   112 DEisKPKVKMPVYFRQDGEYGKY-EVSSELTESIQLrDGIEARTYVLtikgTGQKKIE----IPVLHVKNWPDHGAISAE 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1788 QsLIQFVRTVRDYIN-RSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKD--SVDIYGAVHDLRLHR-VHMVQTECQY 1863
Cdd:COG5599   187 A-LKNLADLIDKKEKiKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRnGGMVQTSEQL 265

PTP_tm

pfam18861

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

1383-1520

6.15e-33

Pssm-ID: 465889 Cd Length: 126 Bit Score: 124.64 E-value: 6.15e-33

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999  1383 VNCSWFSDTNGAVKYFTVVVREADgsDELKPEQQHPLPSYLEYRhNASIRVYQTNYFASKCAENPnSNSKSFNIKLGAEM 1462
Cdd:pfam18861    1 IQFSLFNSSNGPIKAYGVIVTTND--SLNRPLKEYLNKTYYDWK-YKKTDSYLATVTPNPFTSPR-SSSRSLTVPVGTGS 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 332800999  1463 ESlggkcdptqQKFCDGPLKPHTAYRISIRAFTQL-FDEDLKEFTKPLYSDTFFSLPIT 1520
Cdd:pfam18861   77 KW---------QGYCNGPLKPLGSYRFSVAAFTRLeFDDGLIDGEESYVSFTPFSEPIA 126

fn3

Fibronectin type III domain;

1172-1254

1.79e-12

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 64.74 E-value: 1.79e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999  1172 SPPSLMSFADIANTSLAITWKGPPDWT-DYNDFELQWLPRDALTVFNPYNNRKSEGR-IVYGLRPGRSYQFNVKTVSGDS 1249
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNgPITGYEVEYRPKNSGEPWNEITVPGTTTSvTLTGLKPGTEYEVRVQAVNGGG 80


                   ....*
gi 332800999  1250 WKTYS 1254
Cdd:pfam00041   81 EGPPS 85

fn3

Fibronectin type III domain;

1266-1345

1.17e-10

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 59.35 E-value: 1.17e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999  1266 DKIQNLHCRPQNSTAIACSWIPP---DSDFDGYSIECRKMDTQEVEFSRKLEKEKSLLNIMMLVPHKRYLVSIKVQSAGM 1342
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ...
gi 332800999  1343 TSE 1345
Cdd:pfam00041   81 EGP 83

fn3

Fibronectin type III domain;

642-718

1.28e-10

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 59.35 E-value: 1.28e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999   642 DKVQGVSVSNsARSDYLRVSWVHAT---GDFDHYEVTI--KNKNNFIQTKSIPKSENECVFVQLVPGRLYSVTVTTKSGQ 716
Cdd:pfam00041    1 SAPSNLTVTD-VTSTSLTVSWTPPPdgnGPITGYEVEYrpKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ..
gi 332800999   717 YE 718
Cdd:pfam00041   80 GE 81

fn3

Fibronectin type III domain;

818-891

2.37e-10

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 58.58 E-value: 2.37e-10

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332800999   818 SAVKNIHISPNGATdSLTVNWTP---GGGDVDSYTVSAF--RHSQKVDSQTIPKHVFEHTFHRLEAGEQYQIMIASVSG 891
Cdd:pfam00041    1 SAPSNLTVTDVTST-SLTVSWTPppdGNGPITGYEVEYRpkNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78

fn3

Fibronectin type III domain;

113-189

5.38e-10

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 57.81 E-value: 5.38e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999   113 PARFGVSKEKTTSTSLHVWWTPS---SGKVTSYEVQLFDENNQKiQGVQIQESTSWNEYTFFNLTAGSKYNIAITAVSGG 189
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGE-PWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

fn3

Fibronectin type III domain;

1085-1158

3.87e-09

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 55.11 E-value: 3.87e-09

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332800999  1085 SVSHLRGSNRNTTdSLWFNWSPA---SGDFDFYELILYNPNGTKKENWK--DKDLTEWRFQGLVPGRKYVLWVVTHSGD 1158
Cdd:pfam00041    2 APSNLTVTDVTST-SLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEItvPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

FN3

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

110-201

6.64e-09

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 54.81 E-value: 6.64e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999  110 PLPPARFGVSKekTTSTSLHVWWTPSS---GKVTSYEVQLFDENNQKIQGVQIQESTSwNEYTFFNLTAGSKYNIAITAV 186
Cdd:cd00063     1 PSPPTNLRVTD--VTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSE-TSYTLTGLKPGTEYEFRVRAV 77

                          90
                  ....*....|....*.
gi 332800999  187 SGGKRS-FSVYTNGST 201
Cdd:cd00063    78 NGGGESpPSESVTVTT 93

fn3

Fibronectin type III domain;

731-804

1.77e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 53.19 E-value: 1.77e-08

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332800999   731 PVKDLTLRNRSTEDLHVTWSGA---NGDVDQYEIQLL-FNDMKVFPPFHLVNTATEYRFTSLTPGRQYKILVLTISGD 804
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRpKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

fn3

Fibronectin type III domain;

554-630

2.73e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 52.80 E-value: 2.73e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999   554 SSVSGVTVNNSGrNDYLSVSWLLAP---GDVDNYEVTLSH--DGKVVQSLVIAKSVRECSFSSLTPGRLYTVTITTRSGK 628
Cdd:pfam00041    1 SAPSNLTVTDVT-STSLTVSWTPPPdgnGPITGYEVEYRPknSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ..
gi 332800999   629 YE 630
Cdd:pfam00041   80 GE 81

fn3

Fibronectin type III domain;

379-457

4.36e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 52.03 E-value: 4.36e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999   379 AVLQLRVKHANETSLSIMWQTPV---AEWEKYIISLADRD--LLLIHKSLSKDAKEFTFTDLVPGRKYMATVTSISGDLK 453
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNsgEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ....
gi 332800999   454 NSSS 457
Cdd:pfam00041   82 GPPS 85

FN3

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

289-364

1.25e-07

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 51.34 E-value: 1.25e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999  289 PMEVSNLKVTNDGSlTSLKVKWQRPP---GNVDSYNITLSHKGTIKESRVLAPWITETHF--KELVPGRLYQVTVSCVSG 363
Cdd:cd00063     1 PSPPTNLRVTDVTS-TSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYtlTGLKPGTEYEFRVRAVNG 79


                  .
gi 332800999  364 E 364
Cdd:cd00063    80 G 80

FN3

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

1265-1353

4.49e-07

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 49.80 E-value: 4.49e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1265 PDKIQNLHCRPQNSTAIACSWIPPDSD---FDGYSIECRKMDTQEVEFSRKLEKEKSLLNIMMLVPHKRYLVSIKVQSAG 1341
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDggpITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|..
gi 332800999 1342 MTSEVVEDSTIT 1353
Cdd:cd00063    81 GESPPSESVTVT 92

FN3

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

110-192

7.45e-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: 7.45e-07

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999    110 PLPPARFGVSKekTTSTSLHVWWT-PSSGKVTSYEVQLFDENNQK-IQGVQIQESTSWNEYTFFNLTAGSKYNIAITAVS 187
Cdd:smart00060    1 PSPPSNLRVTD--VTSTSVTLSWEpPPDDGITGYIVGYRVEYREEgSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78


                    ....*
gi 332800999    188 GGKRS 192
Cdd:smart00060   79 GAGEG 83

fn3

Fibronectin type III domain;

997-1070

9.19e-07

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 48.57 E-value: 9.19e-07

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332800999   997 AVTDLRITENSTRHLSFRWTASE---GELSWYNIFLYNPDGNLQERAQVDPLVQ-SFSFQNLLQGRMYKMVIVTHSGE 1070
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNEITVPGTTtSVTLTGLKPGTEYEVRVQAVNGG 79

fn3

Fibronectin type III domain;

291-364

1.41e-06

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 47.79 E-value: 1.41e-06

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332800999   291 EVSNLKVTNDGSlTSLKVKWQRPP---GNVDSYNITLSHKGTIKE--SRVLAPWITETHFKELVPGRLYQVTVSCVSGE 364
Cdd:pfam00041    2 APSNLTVTDVTS-TSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPwnEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

fn3

Fibronectin type III domain;

907-986

3.76e-06

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 46.64 E-value: 3.76e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999   907 SVQGVIADNAySSYSLIVSWQKAA---GVAERYDILLLTENGI-LLRNTSEPATTKQHKFEDLTPGKKYKIQILTVSGGL 982
Cdd:pfam00041    2 APSNLTVTDV-TSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGePWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....
gi 332800999   983 FSKE 986
Cdd:pfam00041   81 EGPP 84

fn3

Fibronectin type III domain;

466-539

3.83e-06

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 46.64 E-value: 3.83e-06

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332800999   466 QVTDLHVANQGmTSSLFTNWT---QAQGDVEFYQVLLIHEN--VVIKNESISSETSRYSFHSLKSGSLYSVVVTTVSGG 539
Cdd:pfam00041    2 APSNLTVTDVT-STSLTVSWTpppDGNGPITGYEVEYRPKNsgEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

FN3

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

1171-1263

1.24e-05

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 45.57 E-value: 1.24e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1171 PSPPSLMSFADIANTSLAITWKGPPDWTDYND-FELQWLPRDALTVFNPYNNRKSEGR-IVYGLRPGRSYQFNVKTVSGD 1248
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITgYVVEYREKGSGDWKEVEVTPGSETSyTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|....*
gi 332800999 1249 SWKTYSKPIfgSVRT 1263
Cdd:cd00063    81 GESPPSESV--TVTT 93

FN3

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

1171-1250

3.73e-05

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 43.76 E-value: 3.73e-05

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999   1171 PSPPSLMSFADIANTSLAITWKGPPD--WTDYND-FELQWLPRDALTVFNPYNNRKSEGRIVyGLRPGRSYQFNVKTVSG 1247
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDdgITGYIVgYRVEYREEGSEWKEVNVTPSSTSYTLT-GLKPGTEYEFRVRAVNG 79


                    ...
gi 332800999   1248 DSW 1250
Cdd:smart00060   80 AGE 82

FN3

Fibronectin type 3 domain [General function prediction only];

84-234

3.86e-05

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 48.46 E-value: 3.86e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999   84 DLQAGTIYNFRIISLDEERT---------VVLQTDPLPPArfGVSKEKTTSTSLHVWWTPSSGK-VTSYEVQLFDENNQK 153
Cdd:COG3401   198 DIEPGTTYYYRVAATDTGGEsapsnevsvTTPTTPPSAPT--GLTATADTPGSVTLSWDPVTESdATGYRVYRSNSGDGP 275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999  154 IqgVQIQESTSwNEYTFFNLTAGSKYNIAITAV-SGGKRS-FSVY---TNGSTVPSPVKDI-GISTKANSLLISWSHGSG 227
Cdd:COG3401   276 F--TKVATVTT-TSYTDTGLTNGTTYYYRVTAVdAAGNESaPSNVvsvTTDLTPPAAPSGLtATAVGSSSITLSWTASSD 352


                  ....*...
gi 332800999  228 -NVERYRL 234
Cdd:COG3401   353 aDVTGYNV 360

FN3

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

289-363

6.64e-05

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 42.99 E-value: 6.64e-05

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999    289 PMEVSNLKVTNDGSlTSLKVKWQRPP-GNVDSYNITLSHKGTIKESRVL----APWITETHFKELVPGRLYQVTVSCVSG 363
Cdd:smart00060    1 PSPPSNLRVTDVTS-TSVTLSWEPPPdDGITGYIVGYRVEYREEGSEWKevnvTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

FN3

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

817-891

9.62e-05

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 42.87 E-value: 9.62e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999  817 PSAVKNIHISPNGATdSLTVNWTP---GGGDVDSYTVSaFRHSQKVDSQTIPKHVF---EHTFHRLEAGEQYQIMIASVS 890
Cdd:cd00063     1 PSPPTNLRVTDVTST-SVTLSWTPpedDGGPITGYVVE-YREKGSGDWKEVEVTPGsetSYTLTGLKPGTEYEFRVRAVN 78


                  .
gi 332800999  891 G 891
Cdd:cd00063    79 G 79

fn3

Fibronectin type III domain;

37-98

2.15e-04

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 41.63 E-value: 2.15e-04

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332800999    37 SSHSVSIQWRIL----GSPCNFSLIYSSDTLGAALcPTFRIDNTTYGCNLQDLQAGTIYNFRIISL 98
Cdd:pfam00041   12 TSTSLTVSWTPPpdgnGPITGYEVEYRPKNSGEPW-NEITVPGTTTSVTLTGLKPGTEYEVRVQAV 76

FN3

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

641-718

2.34e-04

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 41.71 E-value: 2.34e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999  641 PDKVQGVSVSNSaRSDYLRVSWVHATGD---FDHYEVTIKNKN--NFIQTKSIPKSENECVFVQLVPGRLYSVTVTTKSG 715
Cdd:cd00063     1 PSPPTNLRVTDV-TSTSVTLSWTPPEDDggpITGYVVEYREKGsgDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79


                  ...
gi 332800999  716 QYE 718
Cdd:cd00063    80 GGE 82

FN3

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

729-804

2.58e-04

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 41.71 E-value: 2.58e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999  729 PEPVKDLTLRNRSTEDLHVTWS---GANGDVDQYEIQL---LFNDMKVFPPFhlVNTATEYRFTSLTPGRQYKILVLTIS 802
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTppeDDGGPITGYVVEYrekGSGDWKEVEVT--PGSETSYTLTGLKPGTEYEFRVRAVN 78


                  ..
gi 332800999  803 GD 804
Cdd:cd00063    79 GG 80

fn3

Fibronectin type III domain;

204-270

9.35e-04

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 40.09 E-value: 9.35e-04

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332800999   204 SPVKDIGISTK-ANSLLISWS---HGSGNVERYRLML--MDKGILVHGGVVDKHATSYAFHGLTPGYLYNLTV 270
Cdd:pfam00041    1 SAPSNLTVTDVtSTSLTVSWTpppDGNGPITGYEVEYrpKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRV 73

FN3

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

641-716

9.71e-04

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 39.91 E-value: 9.71e-04

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999    641 PDKVQGVSVSNSArSDYLRVSWVH-----ATGDFDHYEVTIKNKNNFIQTKSIPKSENECVFVQLVPGRLYSVTVTTKSG 715
Cdd:smart00060    1 PSPPSNLRVTDVT-STSVTLSWEPppddgITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79


                    .
gi 332800999    716 Q 716
Cdd:smart00060   80 A 80

FN3

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

729-803

1.02e-03

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 39.91 E-value: 1.02e-03

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999    729 PEPVKDLTLRNRSTEDLHVTWS-----GANGDVDQYEIQLLFNDMKVFPpFHLVNTATEYRFTSLTPGRQYKILVLTISG 803
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEpppddGITGYIVGYRVEYREEGSEWKE-VNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

FN3

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

377-450

1.10e-03

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 39.52 E-value: 1.10e-03

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332800999    377 PLAVLQLRVKHANETSLSIMWQTPVAEWE-----KYIISLADRDLLLIHKSLSKDAKEFTFTDLVPGRKYMATVTSISG 450
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItgyivGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

FN3

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

817-891

1.39e-03

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 39.52 E-value: 1.39e-03

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999    817 PSAVKNIHISPNGATdSLTVNWTP-----GGGDVDSYTVSAFRHSQKVDSQTIPKHVFEHTFHRLEAGEQYQIMIASVSG 891
Cdd:smart00060    1 PSPPSNLRVTDVTST-SVTLSWEPppddgITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

FN3

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

377-462

2.85e-03

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 38.63 E-value: 2.85e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999  377 PLAVLQLRVKHANETSLSIMWQTPV---AEWEKYIISL--ADRDLLLIHKSLSKDAKEFTFTDLVPGRKYMATVTSISGD 451
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYreKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|...
gi 332800999  452 L--KNSSSVKGRT 462
Cdd:cd00063    81 GesPPSESVTVTT 93

FN3

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

1083-1157

3.64e-03

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 38.36 E-value: 3.64e-03

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999   1083 PASVSHLRGSNrNTTDSLWFNWSPASGDFDFYELILYNP-NGTKKENWK----DKDLTEWRFQGLVPGRKYVLWVVTHSG 1157
Cdd:smart00060    1 PSPPSNLRVTD-VTSTSVTLSWEPPPDDGITGYIVGYRVeYREEGSEWKevnvTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

FN3

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

553-628

7.67e-03

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 37.21 E-value: 7.67e-03

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999    553 PSSVSGVTVNNSGRNdYLSVSWLLAPGD-----VDNYEVTLSHDGKVVQSLVIAKSVRECSFSSLTPGRLYTVTITTRSG 627
Cdd:smart00060    1 PSPPSNLRVTDVTST-SVTLSWEPPPDDgitgyIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79


                    .
gi 332800999    628 K 628
Cdd:smart00060   80 A 80

FN3

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

203-273

8.54e-03

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 37.21 E-value: 8.54e-03

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332800999    203 PSPVKDIGIS-TKANSLLISWSH-----GSGNVERYRLMLMDKGILVHGGVVDKHATSYAFHGLTPGYLYNLTVMTE 273
Cdd:smart00060    1 PSPPSNLRVTdVTSTSVTLSWEPppddgITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77

FN3

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

553-630

8.58e-03

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 37.48 E-value: 8.58e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999  553 PSSVSGVTVNNSGRnDYLSVSWLLAPGD---VDNYEVTLS--HDGKVVQSLVIAKSVRECSFSSLTPGRLYTVTITTRSG 627
Cdd:cd00063     1 PSPPTNLRVTDVTS-TSVTLSWTPPEDDggpITGYVVEYRekGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79


                  ...
gi 332800999  628 KYE 630
Cdd:cd00063    80 GGE 82

FN3

Fibronectin type 3 domain [General function prediction only];

1143-1298

9.59e-03

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 40.76 E-value: 9.59e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1143 VPGRKYVLWVVTHSGDLSNKVTAESRTAPSPPSLMSFADIANTSLAITWKGPPDWTDYNDFELQWLPRDALTVFNPYN-- 1220
Cdd:COG3401   105 GATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATts 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1221 ---NRKSEGRIVYGLRPGRSYQFNVKTVSGDSWKTYSKPIFGSV-RTKPDKIQNLHCRPQNSTAIACSWIP-PDSDFDGY 1295
Cdd:COG3401   185 ltvTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTpTTPPSAPTGLTATADTPGSVTLSWDPvTESDATGY 264


                  ...
gi 332800999 1296 SIE 1298
Cdd:COG3401   265 RVY 267

Name

Accession

Description

Interval

E-value

R-PTPc-B

cd14617

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

1641-1868

3.07e-179

Pssm-ID: 350465 [Multi-domain] Cd Length: 228 Bit Score: 540.28 E-value: 3.07e-179

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1641 NRYNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 1720
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1721 KCDHYWPADQDSLYYGDLILQMLSESVLPEWTIREFKICGEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDY 1800
Cdd:cd14617    81 KCDHYWPADQDSLYYGDLIVQMLSESVLPEWTIREFKICSEEQLDAPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVRDY 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332800999 1801 INRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 1868
Cdd:cd14617   161 INRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228

R3-PTPc

cd14548

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

1642-1868

4.19e-143

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: 441.79 E-value: 4.19e-143

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1642 RYNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVK 1721
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1722 CDHYWPADQDSLYYGDLILQMLSESVLPEWTIREFKICGEEQldaHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDYI 1801
Cdd:cd14548    81 CDHYWPFDQDPVYYGDITVTMLSESVLPDWTIREFKLERGDE---VRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYI 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332800999 1802 NRspGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 1868
Cdd:cd14548   158 KQ--EKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222

PTPc

smart00194

Protein tyrosine phosphatase, catalytic domain;

1612-1870

5.64e-116

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 367.75 E-value: 5.64e-116

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999   1612 LLSKEYEELKDVGR-NQSCDIALLPENRGKNRYNNILPYDATRVKLSNvDDDPCSDYINASYIPGNNFRREYIVTQGPLP 1690
Cdd:smart00194    1 GLEEEFEKLDRLKPdDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKP-PPGEGSDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999   1691 GTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPADQ-DSLYYGDLILQMLSESVLPEWTIREFKICGEEQlDAHRL 1769
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEgEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGC-SETRT 158

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999   1770 IRHFHYTVWPDHGVPETTQSLIQFVRTVRDYinRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDL 1849
Cdd:smart00194  159 VTHYHYTNWPDHGVPESPESILDLIRAVRKS--QSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKEL 236

                           250       260
                    ....*....|....*....|.
gi 332800999   1850 RLHRVHMVQTECQYVYLHQCV 1870
Cdd:smart00194  237 RSQRPGMVQTEEQYIFLYRAI 257

R-PTPc-J

cd14615

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

1641-1872

4.40e-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: 355.28 E-value: 4.40e-112

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1641 NRYNNILPYDATRVKLSNvDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 1720
Cdd:cd14615     1 NRYNNVLPYDISRVKLSV-QSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1721 KCDHYWPADQdSLYYGDLILQMLSESVLPEWTIREFKICGEEQLDAHRlIRHFHYTVWPDHGVPETTQSLIQFVRTVRDY 1800
Cdd:cd14615    80 KCEEYWPSKQ-KKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRT-VRHFHFTSWPDHGVPETTDLLINFRHLVREY 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332800999 1801 INRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRD 1872
Cdd:cd14615   158 MKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229

R-PTPc-O

cd14614

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

1630-1871

3.51e-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: 3.51e-104

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1630 DIALLPENRGKNRYNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIV 1709
Cdd:cd14614     5 FAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1710 MVTQCVEKGRVKCDHYWPADQDSLYYGDLILQMLSESVLPEWTIREFKIcgeEQLDAHRLIRHFHYTVWPDHGVP--ETT 1787
Cdd:cd14614    85 MLTQCNEKRRVKCDHYWPFTEEPVAYGDITVEMLSEEEQPDWAIREFRV---SYADEVQDVMHFNYTAWPDHGVPtaNAA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1788 QSLIQFVRTVRDYINRSPgaGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 1867
Cdd:cd14614   162 ESILQFVQMVRQQAVKSK--GPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIH 239


                  ....
gi 332800999 1868 QCVR 1871
Cdd:cd14614   240 QCVQ 243

Y_phosphatase

pfam00102

Protein-tyrosine phosphatase;

1637-1870

2.12e-101

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 324.97 E-value: 2.12e-101

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999  1637 NRGKNRYNNILPYDATRVKLSnvDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVE 1716
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLT--GDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999  1717 KGRVKCDHYWP-ADQDSLYYGDL-ILQMLSESVLPEWTIREFKICgEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFV 1794
Cdd:pfam00102   79 KGREKCAQYWPeEEGESLEYGDFtVTLKKEKEDEKDYTVRTLEVS-NGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLL 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332800999  1795 RTVRDYiNRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 1870
Cdd:pfam00102  158 RKVRKS-SLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232

R-PTPc-H

cd14619

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

1641-1874

2.35e-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: 2.35e-99

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1641 NRYNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 1720
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1721 KCDHYWPADQDSLYYGDLILQMLSESVLPEWTIREFKICGEEQlDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDY 1800
Cdd:cd14619    81 KCEHYWPLDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEE-QKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQW 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332800999 1801 INRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRDVL 1874
Cdd:cd14619   160 LDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233

R-PTPc-V

cd14618

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

1641-1870

1.05e-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: 1.05e-96

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1641 NRYNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 1720
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1721 KCDHYWPADQDSLYYGDLILQMLSESVLPEWTIREFKIcGEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDY 1800
Cdd:cd14618    81 LCDHYWPSESTPVSYGHITVHLLAQSSEDEWTRREFKL-WHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVREH 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1801 INRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 1870
Cdd:cd14618   160 VQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCI 229

R-PTPc-LAR-1

cd14553

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

1637-1870

7.22e-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: 291.99 E-value: 7.22e-90

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1637 NRGKNRYNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVE 1716
Cdd:cd14553     3 NKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1717 KGRVKCDHYWPADqDSLYYGDLILQMLSESVLPEWTIREFKICGEEQLDaHRLIRHFHYTVWPDHGVPETTQSLIQFVRT 1796
Cdd:cd14553    83 RSRVKCDQYWPTR-GTETYGLIQVTLLDTVELATYTVRTFALHKNGSSE-KREVRQFQFTAWPDHGVPEHPTPFLAFLRR 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332800999 1797 VRDYinRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 1870
Cdd:cd14553   161 VKAC--NPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDAL 232

PTPc

cd00047

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

1667-1868

5.94e-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: 288.03 E-value: 5.94e-89

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1667 YINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDS-LYYGDLILQMLSE 1745
Cdd:cd00047     1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKpLEYGDITVTLVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1746 SVLPEWTIREFKICGEEQlDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDYinRSPGAGPTVVHCSAGVGRTGTFI 1825
Cdd:cd00047    81 EELSDYTIRTLELSPKGC-SESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKE--ARKPNGPIVVHCSAGVGRTGTFI 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 332800999 1826 ALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 1868
Cdd:cd00047   158 AIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200

PTPc-N9

cd14543

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

1615-1867

2.38e-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: 2.38e-84

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1615 KEYEELKDVGRNQSCDIALLPENRGKNRYNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKD 1694
Cdd:cd14543     7 EEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1695 DFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDS-LYYGDLILQMLSESVLPEWTIREFKICGEEQlDAHRLIRHF 1773
Cdd:cd14543    87 DFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSsLRYGDLTVTNLSVENKEHYKKTTLEIHNTET-DESRQVTHF 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1774 HYTVWPDHGVPETTQSLIQFVRTVRDYINRS-----------PGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDI 1842
Cdd:cd14543   166 QFTSWPDFGVPSSAAALLDFLGEVRQQQALAvkamgdrwkghPPGPPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNV 245

                         250       260
                  ....*....|....*....|....*
gi 332800999 1843 YGAVHDLRLHRVHMVQTECQYVYLH 1867
Cdd:cd14543   246 MQTVRRMRTQRAFSIQTPDQYYFCY 270

R5-PTPc-1

cd14549

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

1667-1867

3.54e-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: 271.53 E-value: 3.54e-83

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1667 YINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPADqDSLYYGDLILQMLSES 1746
Cdd:cd14549     1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKE-GTETYGNIQVTLLSTE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1747 VLPEWTIREF-----KICGEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDYinRSPGAGPTVVHCSAGVGRT 1821
Cdd:cd14549    80 VLATYTVRTFslknlKLKKVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAA--NPPGAGPIVVHCSAGVGRT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 332800999 1822 GTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 1867
Cdd:cd14549   158 GTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203

R-PTPc-Q

cd14616

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

1641-1868

7.28e-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: 268.70 E-value: 7.28e-82

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1641 NRYNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 1720
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1721 KCDHYWPADQDSL-YYGDLILQMLSESVLPEWTIREFKIcgeEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRd 1799
Cdd:cd14616    81 RCHQYWPEDNKPVtVFGDIVITKLMEDVQIDWTIRDLKI---ERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVR- 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332800999 1800 yINRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 1868
Cdd:cd14616   157 -ASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224

R-PTPc-F-1

cd14626

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

1601-1870

1.33e-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: 1.33e-75

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1601 HFMKLQADSNYLLSKEYEELkDVGRNQSCDIALLPENRGKNRYNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRR 1680
Cdd:cd14626     6 NIERLKANDGLKFSQEYESI-DPGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYRKQN 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1681 EYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPAdQDSLYYGDLILQMLSESVLPEWTIREFKICg 1760
Cdd:cd14626    85 AYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPI-RGTETYGMIQVTLLDTVELATYSVRTFALY- 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1761 EEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRdyINRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSV 1840
Cdd:cd14626   163 KNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVK--ACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTV 240

                         250       260       270
                  ....*....|....*....|....*....|
gi 332800999 1841 DIYGAVHDLRLHRVHMVQTECQYVYLHQCV 1870
Cdd:cd14626   241 DIYGHVTCMRSQRNYMVQTEDQYIFIHEAL 270

R-PTPc-T-1

cd14630

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

1636-1870

7.58e-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: 7.58e-75

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1636 ENRGKNRYNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCV 1715
Cdd:cd14630     2 ENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1716 EKGRVKCDHYWPADQDslYYGDLILQMLSESVLPEWTIREFKICGEEQLDAhRLIRHFHYTVWPDHGVPETTQSLIQFVR 1795
Cdd:cd14630    82 EVGRVKCVRYWPDDTE--VYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEI-REIRQFHFTSWPDHGVPCYATGLLGFVR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332800999 1796 TVRdYINrSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 1870
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 ...

1614-1874

2.40e-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: 2.40e-74

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1614 SKEYEELK--DVGRNQSCDIALLPENRGKNRYNNILPYDATRVKLSNV--DDDPCSDYINASYIPGNNFRREYIVTQGPL 1689
Cdd:cd17667     2 SEDFEEVQrcTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLpgKDSKHSDYINANYVDGYNKAKAYIATQGPL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1690 PGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPAdQDSLYYGDLILQMLSESVLPEWTIREFKICGEEQLDAH-- 1767
Cdd:cd17667    82 KSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPT-ENSEEYGNIIVTLKSTKIHACYTVRRFSIRNTKVKKGQkg 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1768 --------RLIRHFHYTVWPDHGVPETTQSLIQFVRtvRDYINRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDS 1839
Cdd:cd17667   161 npkgrqneRTVIQYHYTQWPDMGVPEYALPVLTFVR--RSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKST 238

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 332800999 1840 VDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRDVL 1874
Cdd:cd17667   239 VNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAI 273

PTPc-KIM

cd14547

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

1641-1868

3.89e-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: 3.89e-74

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1641 NRYNNILPYDATRVKLSNVDDDPCSDYINASYIPG-NNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKgR 1719
Cdd:cd14547     1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGyDGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA-K 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1720 VKCDHYWPADQDSLYyGDLILQMLSESVLPEWTIREFKI-CGEEQldahRLIRHFHYTVWPDHGVPETTQSLIQFVRTVR 1798
Cdd:cd14547    80 EKCAQYWPEEENETY-GDFEVTVQSVKETDGYTVRKLTLkYGGEK----RYLKHYWYTSWPDHKTPEAAQPLLSLVQEVE 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1799 DYINRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 1868
Cdd:cd14547   155 EARQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224

PTPc-N11_6

cd14544

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

1637-1870

6.28e-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: 244.29 E-value: 6.28e-73

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1637 NRGKNRYNNILPYDATRVKLSNVDDD-PCSDYINASYI-PGNNFRRE------YIVTQGPLPGTKDDFWKMVWEQNVHNI 1708
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILKDRDPNvPGSDYINANYIrNENEGPTTdenaktYIATQGCLENTVSDFWSMVWQENSRVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1709 VMVTQCVEKGRVKCDHYWPADQDSLYYGDLILQMLSESVLPEWTIREFKICGEEQLDAHRLIRHFHYTVWPDHGVPETTQ 1788
Cdd:cd14544    81 VMTTKEVERGKNKCVRYWPDEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDPIREIWHYQYLSWPDHGVPSDPG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1789 SLIQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKD---SVDIYGAVHDLRLHRVHMVQTECQYVY 1865
Cdd:cd14544   161 GVLNFLEDVNQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRSGMVQTEAQYKF 240


                  ....*
gi 332800999 1866 LHQCV 1870
Cdd:cd14544   241 IYVAV 245

R-PTPc-A-1

cd14621

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

1586-1870

4.10e-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: 243.78 E-value: 4.10e-72

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1586 NRKTScPIKINQFEGHFMKLQADSNYLLSKEYEELKDVGRNQSCDIALLPENRGKNRYNNILPYDATRVKLSNVDDDPCS 1665
Cdd:cd14621     2 NRKYP-PLPVDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1666 DYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPaDQDSLYYGDLILQMLSE 1745
Cdd:cd14621    81 DYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWP-DQGCWTYGNIRVSVEDV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1746 SVLPEWTIREFkiCGEEQLDA-----HRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRdyiNRSPG-AGPTVVHCSAGVG 1819
Cdd:cd14621   160 TVLVDYTVRKF--CIQQVGDVtnkkpQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVK---NCNPQyAGAIVVHCSAGVG 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 332800999 1820 RTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 1870
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 ...

1632-1868

6.77e-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: 6.77e-72

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1632 ALLPENRGKNRYNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMV 1711
Cdd:cd14554     1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1712 TQCVEKGRVKCDHYWPADQdSLYYGDLILQMLSESVLPEWTIREFKICgEEQLDAHRLIRHFHYTVWPDHGVPETTQSLI 1791
Cdd:cd14554    81 TKLREMGREKCHQYWPAER-SARYQYFVVDPMAEYNMPQYILREFKVT-DARDGQSRTVRQFQFTDWPEQGVPKSGEGFI 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332800999 1792 QFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 1868
Cdd:cd14554   159 DFIGQVHKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYR 235

R-PTPc-M-1

cd14633

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

1601-1870

1.05e-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: 1.05e-70

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1601 HFMKLQADSNYLLSKEYEELKDvGRNQSCDIALLPENRGKNRYNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRR 1680
Cdd:cd14633     5 HITQMKCAEGYGFKEEYESFFE-GQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYHRPN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1681 EYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDslYYGDLILQMLSESVLPEWTIREFKIcg 1760
Cdd:cd14633    84 HYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTE--IYKDIKVTLIETELLAEYVIRTFAV-- 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1761 eEQLDAH--RLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDyiNRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKD 1838
Cdd:cd14633   160 -EKRGVHeiREIRQFHFTGWPDHGVPYHATGLLGFVRQVKS--KSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREG 236

                         250       260       270
                  ....*....|....*....|....*....|..
gi 332800999 1839 SVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 1870
Cdd:cd14633   237 VVDIYNCVRELRSRRVNMVQTEEQYVFIHDAI 268

R-PTPc-D-1

cd14624

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

1592-1870

2.82e-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: 237.71 E-value: 2.82e-70

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1592 PIKINQFEGHFMKLQADSNYLLSKEYEELkDVGRNQSCDIALLPENRGKNRYNNILPYDATRVKLSNVDDDPCSDYINAS 1671
Cdd:cd14624     3 PIPILELADHIERLKANDNLKFSQEYESI-DPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINAN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1672 YIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPAdQDSLYYGDLILQMLSESVLPEW 1751
Cdd:cd14624    82 YIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPS-RGTETYGLIQVTLLDTVELATY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1752 TIREFKICgEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRdyINRSPGAGPTVVHCSAGVGRTGTFIALDRIL 1831
Cdd:cd14624   161 CVRTFALY-KNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVK--TCNPPDAGPMVVHCSAGVGRTGCFIVIDAML 237

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 332800999 1832 QQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 1870
Cdd:cd14624   238 ERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDAL 276

R-PTPc-S-1

cd14625

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

1592-1870

9.14e-70

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: 9.14e-70

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1592 PIKINQFEGHFMKLQADSNYLLSKEYEELkDVGRNQSCDIALLPENRGKNRYNNILPYDATRVKLSNVDDDPCSDYINAS 1671
Cdd:cd14625     3 PIPISELAEHTERLKANDNLKLSQEYESI-DPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINAN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1672 YIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPaDQDSLYYGDLILQMLSESVLPEW 1751
Cdd:cd14625    82 YIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWP-SRGTETYGMIQVTLLDTIELATF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1752 TIREFKIcGEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRdyINRSPGAGPTVVHCSAGVGRTGTFIALDRIL 1831
Cdd:cd14625   161 CVRTFSL-HKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVK--TCNPPDAGPIVVHCSAGVGRTGCFIVIDAML 237

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 332800999 1832 QQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 1870
Cdd:cd14625   238 ERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDAL 276

PTP_fungal

cd18533

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

1667-1868

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 332800999 1667 YINASYI-PGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDSLYYGDLILQMLSE 1745
Cdd:cd18533     1 YINASYItLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEYGDLTVELVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1746 SVLPEW--TIREFKICGEEQldAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGT 1823
Cdd:cd18533    81 EENDDGgfIVREFELSKEDG--KVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSASLDPPIIVHCSAGVGRTGT 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 332800999 1824 FIALDRILQQLDS--------KDSVD-IYGAVHDLRLHRVHMVQTECQYVYLHQ 1868
Cdd:cd18533   159 FIALDSLLDELKRglsdsqdlEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212

PTPc-N1

cd14608

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

1617-1866

4.48e-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: 4.48e-67

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1617 YEELKDVGRNQSCDIALLPENRGKNRYNNILPYDATRVKLSNvdddPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDF 1696
Cdd:cd14608     5 YQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQ----EDNDYINASLIKMEEAQRSYILTQGPLPNTCGHF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1697 WKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDS-LYYGD--LILQMLSESVLPEWTIREFKIcgeEQLDAH--RLIR 1771
Cdd:cd14608    81 WEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKeMIFEDtnLKLTLISEDIKSYYTVRQLEL---ENLTTQetREIL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1772 HFHYTVWPDHGVPETTQSLIQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSK---DSVDIYGAVHD 1848
Cdd:cd14608   158 HFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRkdpSSVDIKKVLLE 237

                         250       260
                  ....*....|....*....|
gi 332800999 1849 LRLHRVHMVQT--ECQYVYL 1866
Cdd:cd14608   238 MRKFRMGLIQTadQLRFSYL 257

R-PTPc-E-1

cd14620

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

1643-1868

4.20e-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: 223.66 E-value: 4.20e-66

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1643 YNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKC 1722
Cdd:cd14620     1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1723 DHYWPaDQDSLYYGDLILQMLSESVLPEWTIREFkiCGEEQLD----AHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVR 1798
Cdd:cd14620    81 YQYWP-DQGCWTYGNIRVAVEDCVVLVDYTIRKF--CIQPQLPdgckAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVK 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332800999 1799 dyiNRSPG-AGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 1868
Cdd:cd14620   158 ---SVNPVhAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQ 225

PTPc-N6

cd14606

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

1635-1870

1.86e-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: 223.22 E-value: 1.86e-65

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1635 PENRGKNRYNNILPYDATRVKLSNVDDD-PCSDYINASYI------PGNNFRReYIVTQGPLPGTKDDFWKMVWEQNVHN 1707
Cdd:cd14606    16 PENKSKNRYKNILPFDHSRVILQGRDSNiPGSDYINANYVknqllgPDENAKT-YIASQGCLEATVNDFWQMAWQENSRV 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1708 IVMVTQCVEKGRVKCDHYWPADQDSLYYGDLILQMLSESVLPEWTIREFKICGEEQLDAHRLIRHFHYTVWPDHGVPETT 1787
Cdd:cd14606    95 IVMTTREVEKGRNKCVPYWPEVGMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGELIREIWHYQYLSWPDHGVPSEP 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1788 QSLIQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSK--DS-VDIYGAVHDLRLHRVHMVQTECQYV 1864
Cdd:cd14606   175 GGVLSFLDQINQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKglDCdIDIQKTIQMVRAQRSGMVQTEAQYK 254


                  ....*.
gi 332800999 1865 YLHQCV 1870
Cdd:cd14606   255 FIYVAI 260

R-PTPc-C-1

cd14557

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

1667-1868

5.60e-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: 5.60e-65

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1667 YINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPA-DQDSLYYGDLILQMLSE 1745
Cdd:cd14557     1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSmEEGSRAFGDVVVKINEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1746 SVLPEWTIREFKICGEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDYINRspGAGPTVVHCSAGVGRTGTFI 1825
Cdd:cd14557    81 KICPDYIIRKLNINNKKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNF--FSGPIVVHCSAGVGRTGTYI 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 332800999 1826 ALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 1868
Cdd:cd14557   159 GIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201

PTPc-N7

cd14612

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

1634-1867

1.36e-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: 1.36e-64

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1634 LPENRGKNRYNNILPYDATRVKLSNV-DDDPCSDYINASYIPGNNFR-REYIVTQGPLPGTKDDFWKMVWEQNVHNIVMV 1711
Cdd:cd14612    12 IPGHASKDRYKTILPNPQSRVCLRRAgSQEEEGSYINANYIRGYDGKeKAYIATQGPMLNTVSDFWEMVWQEECPIIVMI 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1712 TQCVEKgRVKCDHYWPADQDSlyYGDLILQMLSESVLPEWTIREFKICGEEqldAHRLIRHFHYTVWPDHGVPETTQSLI 1791
Cdd:cd14612    92 TKLKEK-KEKCVHYWPEKEGT--YGRFEIRVQDMKECDGYTIRDLTIQLEE---ESRSVKHYWFSSWPDHQTPESAGPLL 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332800999 1792 QFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 1867
Cdd:cd14612   166 RLVAEVEESRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLH 241

R-PTPc-Z-1

cd17668

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

1667-1867

1.64e-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: 1.64e-64

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1667 YINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPADqDSLYYGDLILQMLSES 1746
Cdd:cd17668     1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPAD-GSEEYGNFLVTQKSVQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1747 VLPEWTIREF-------KICGEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDyiNRSPGAGPTVVHCSAGVG 1819
Cdd:cd17668    80 VLAYYTVRNFtlrntkiKKGSQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASY--AKRHAVGPVVVHCSAGVG 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 332800999 1820 RTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 1867
Cdd:cd17668   158 RTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 205

PTPc-N20_13

cd14538

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

1667-1874

2.21e-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: 2.21e-64

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1667 YINASYI--PGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWP--ADQDSLYYGDLILQM 1742
Cdd:cd14538     1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPdsLNKPLICGGRLEVSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1743 LSESVLPEWTIREFKICGEEQLDAHRlIRHFHYTVWPDHGVPETTQSLIQFVRtvrdYINRSPGAGPTVVHCSAGVGRTG 1822
Cdd:cd14538    81 EKYQSLQDFVIRRISLRDKETGEVHH-ITHLNFTTWPDHGTPQSADPLLRFIR----YMRRIHNSGPIVVHCSAGIGRTG 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 332800999 1823 TFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRDVL 1874
Cdd:cd14538   156 VLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207

PTPc-N18

cd14603

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

1635-1870

2.44e-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: 2.44e-64

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1635 PENRGKNRYNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQC 1714
Cdd:cd14603    28 KENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMACRE 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1715 VEKGRVKCDHYWPADQDSLYYGDLILQMLSESVL-PEWTIREFKI--CGEEqldahRLIRHFHYTVWPDHGVPETTQSLI 1791
Cdd:cd14603   108 IEMGKKKCERYWAQEQEPLQTGPFTITLVKEKRLnEEVILRTLKVtfQKES-----RSVSHFQYMAWPDHGIPDSPDCML 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1792 QFVRTVRDYINRSPgaGPTVVHCSAGVGRTGTFIALDRILQQLDSK---DSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 1868
Cdd:cd14603   183 AMIELARRLQGSGP--EPLCVHCSAGCGRTGVICTVDYVRQLLLTQripPDFSIFDVVLEMRKQRPAAVQTEEQYEFLYH 260


                  ..
gi 332800999 1869 CV 1870
Cdd:cd14603   261 TV 262

PTPc-N2

cd14607

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

1625-1862

2.67e-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: 2.67e-64

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1625 RNQSCD----IALLPENRGKNRYNNILPYDATRVKLSNVDDDpcsdYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMV 1700
Cdd:cd14607     8 RNESHDyphrVAKYPENRNRNRYRDVSPYDHSRVKLQNTEND----YINASLVVIEEAQRSYILTQGPLPNTCCHFWLMV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1701 WEQNVHNIVMVTQCVEKGRVKCDHYWPA-DQDSLYYGD--LILQMLSESVLPEWTIREFKI----CGEEqldahRLIRHF 1773
Cdd:cd14607    84 WQQKTKAVVMLNRIVEKDSVKCAQYWPTdEEEVLSFKEtgFSVKLLSEDVKSYYTVHLLQLeninSGET-----RTISHF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1774 HYTVWPDHGVPETTQSLIQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKD--SVDIYGAVHDLRL 1851
Cdd:cd14607   159 HYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRK 238

                         250
                  ....*....|.
gi 332800999 1852 HRVHMVQTECQ 1862
Cdd:cd14607   239 YRMGLIQTPDQ 249

PTPc-N1_2

cd14545

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

1640-1862

9.40e-64

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: 9.40e-64

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1640 KNRYNNILPYDATRVKLSNVDDDpcSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGR 1719
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKLKQGD--NDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1720 VKCDHYWPADQDSLY---YGDLILQMLSESVLPEWTIREFKIcgeEQLDAH--RLIRHFHYTVWPDHGVPETTQSLIQFV 1794
Cdd:cd14545    79 IKCAQYWPQGEGNAMifeDTGLKVTLLSEEDKSYYTVRTLEL---ENLKTQetREVLHFHYTTWPDFGVPESPAAFLNFL 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1795 RTVRDYINRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKD--SVDIYGAVHDLRLHRVHMVQTECQ 1862
Cdd:cd14545   156 QKVRESGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNpsSVDVKKVLLEMRKYRMGLIQTPDQ 225

R-PTPc-typeIIb-1

cd14555

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

1667-1870

1.41e-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: 1.41e-63

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1667 YINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDSlyYGDLILQMLSES 1746
Cdd:cd14555     1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEV--YGDIKVTLVETE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1747 VLPEWTIREFKIcGEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRdyINRSPGAGPTVVHCSAGVGRTGTFIA 1826
Cdd:cd14555    79 PLAEYVVRTFAL-ERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVK--ASNPPSAGPIVVHCSAGAGRTGCYIV 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 332800999 1827 LDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 1870
Cdd:cd14555   156 IDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAI 199

R-PTPc-K-1

cd14631

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

1653-1870

9.58e-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: 9.58e-63

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1653 RVKLSNVDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDs 1732
Cdd:cd14631     1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTE- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1733 lYYGDLILQMLSESVLPEWTIREFKIcGEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRdyINRSPGAGPTVV 1812
Cdd:cd14631    80 -VYGDFKVTCVEMEPLAEYVVRTFTL-ERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVK--LSNPPSAGPIVV 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 332800999 1813 HCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 1870
Cdd:cd14631   156 HCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 213

PTPc-N3_4

cd14541

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

1666-1870

4.97e-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: 211.42 E-value: 4.97e-62

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1666 DYINASY----IPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDSLYYGDLILQ 1741
Cdd:cd14541     1 DYINANYvnmeIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETMQFGNLQIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1742 MLSESVLPEWTIREFKIC----GEEqldahRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDYinRSPGAGPTVVHCSAG 1817
Cdd:cd14541    81 CVSEEVTPSFAFREFILTntntGEE-----RHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQN--RVGMVEPTVVHCSAG 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 332800999 1818 VGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 1870
Cdd:cd14541   154 IGRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAI 206

PTPc-N13

cd14597

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

1636-1874

1.07e-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: 1.07e-61

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1636 ENRGKNRYNNILPYDATRVKLSNVdddpcSDYINASYI--PGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQ 1713
Cdd:cd14597     2 ENRKKNRYKNILPYDTTRVPLGDE-----GGYINASFIkmPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1714 CVEKGRVKCDHYWPADQDSLYYGD--LILQMLSESVLPEWTIREFKIcGEEQLDAHRLIRHFHYTVWPDHGVPETTQSLI 1791
Cdd:cd14597    77 EVEGGKIKCQRYWPEILGKTTMVDnrLQLTLVRMQQLKNFVIRVLEL-EDIQTREVRHITHLNFTAWPDHDTPSQPEQLL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1792 QFVRTVRdYINRSpgaGPTVVHCSAGVGRTGTFIALDRILqQLDSKD-SVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 1870
Cdd:cd14597   156 TFISYMR-HIHKS---GPIITHCSAGIGRSGTLICIDVVL-GLISKDlDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVI 230


                  ....
gi 332800999 1871 RDVL 1874
Cdd:cd14597   231 LYVL 234

PTPc-N11

cd14605

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

1636-1871

1.25e-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: 1.25e-60

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1636 ENRGKNRYNNILPYDATRVKLSNVD-DDPCSDYINASYI-PGNNF-------RREYIVTQGPLPGTKDDFWKMVWEQNVH 1706
Cdd:cd14605     1 ENKNKNRYKNILPFDHTRVVLHDGDpNEPVSDYINANIImPEFETkcnnskpKKSYIATQGCLQNTVNDFWRMVFQENSR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1707 NIVMVTQCVEKGRVKCDHYWPADQDSLYYGDLILQMLSESVLPEWTIREFKICGEEQLDAHRLIRHFHYTVWPDHGVPET 1786
Cdd:cd14605    81 VIVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYILRELKLSKVGQGNTERTVWQYHFRTWPDHGVPSD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1787 TQSLIQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKD---SVDIYGAVHDLRLHRVHMVQTECQY 1863
Cdd:cd14605   161 PGGVLDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGvdcDIDVPKTIQMVRSQRSGMVQTEAQY 240


                  ....*...
gi 332800999 1864 VYLHQCVR 1871
Cdd:cd14605   241 RFIYMAVQ 248

R-PTPc-U-1

cd14632

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

1667-1870

1.64e-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: 1.64e-60

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1667 YINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDSlyYGDLILQMLSES 1746
Cdd:cd14632     1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDT--YGDIKITLLKTE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1747 VLPEWTIREFKIcGEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDyiNRSPGAGPTVVHCSAGVGRTGTFIA 1826
Cdd:cd14632    79 TLAEYSVRTFAL-ERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKA--STPPDAGPVVVHCSAGAGRTGCYIV 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 332800999 1827 LDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 1870
Cdd:cd14632   156 LDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAI 199

R-PTP-S-2

cd14627

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

1632-1874

2.65e-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: 209.59 E-value: 2.65e-60

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1632 ALLPENRGKNRYNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMV 1711
Cdd:cd14627    48 ANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVML 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1712 TQCVEKGRVKCDHYWPADQdSLYYGDLILQMLSESVLPEWTIREFKICgEEQLDAHRLIRHFHYTVWPDHGVPETTQSLI 1791
Cdd:cd14627   128 TKLREMGREKCHQYWPAER-SARYQYFVVDPMAEYNMPQYILREFKVT-DARDGQSRTVRQFQFTDWPEQGVPKSGEGFI 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1792 QFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVR 1871
Cdd:cd14627   206 DFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAAL 285


                  ...
gi 332800999 1872 DVL 1874
Cdd:cd14627   286 EYL 288

R-PTP-D-2

cd14628

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

1632-1874

9.03e-60

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: 208.05 E-value: 9.03e-60

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1632 ALLPENRGKNRYNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMV 1711
Cdd:cd14628    47 ANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVML 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1712 TQCVEKGRVKCDHYWPADQdSLYYGDLILQMLSESVLPEWTIREFKICgEEQLDAHRLIRHFHYTVWPDHGVPETTQSLI 1791
Cdd:cd14628   127 TKLREMGREKCHQYWPAER-SARYQYFVVDPMAEYNMPQYILREFKVT-DARDGQSRTVRQFQFTDWPEQGVPKSGEGFI 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1792 QFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVR 1871
Cdd:cd14628   205 DFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAAL 284


                  ...
gi 332800999 1872 DVL 1874
Cdd:cd14628   285 EYL 287

R-PTP-F-2

cd14629

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

1632-1874

2.01e-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: 206.89 E-value: 2.01e-59

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1632 ALLPENRGKNRYNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMV 1711
Cdd:cd14629    48 ANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVML 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1712 TQCVEKGRVKCDHYWPADQdSLYYGDLILQMLSESVLPEWTIREFKICgEEQLDAHRLIRHFHYTVWPDHGVPETTQSLI 1791
Cdd:cd14629   128 TKLREMGREKCHQYWPAER-SARYQYFVVDPMAEYNMPQYILREFKVT-DARDGQSRTIRQFQFTDWPEQGVPKTGEGFI 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1792 QFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYvylHQCVR 1871
Cdd:cd14629   206 DFIGQVHKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQY---QLCYR 282


                  ...
gi 332800999 1872 DVL 1874
Cdd:cd14629   283 AAL 285

R-PTPc-A-E-1

cd14551

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

1667-1868

2.12e-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: 2.12e-59

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1667 YINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPaDQDSLYYGDLILQMLSES 1746
Cdd:cd14551     1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWP-DQGCWTYGNLRVRVEDTV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1747 VLPEWTIREFkiCGEEQLD-----AHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDYInrSPGAGPTVVHCSAGVGRT 1821
Cdd:cd14551    80 VLVDYTTRKF--CIQKVNRgigekRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSAN--PPRAGPIVVHCSAGVGRT 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 332800999 1822 GTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 1868
Cdd:cd14551   156 GTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202

PTPc-N3

cd14600

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

1616-1875

2.76e-59

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

Pssm-ID: 350448 [Multi-domain] Cd Length: 274 Bit Score: 205.85 E-value: 2.76e-59

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1616 EYEEL--KDVGRNQSCdiALLPENRGKNRYNNILPYDATRVKLSNVDDdpcsdYINASY----IPGNNFRREYIVTQGPL 1689
Cdd:cd14600    19 QFEQLyrKKPGLAITC--AKLPQNMDKNRYKDVLPYDATRVVLQGNED-----YINASYvnmeIPSANIVNKYIATQGPL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1690 PGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDSLYYGDLILQMLSESVLPEWTIREFKICGEEQLDAHRL 1769
Cdd:cd14600    92 PHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPDVMEYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTV 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1770 IrHFHYTVWPDHGVPETTQSLIQFVRTVRdyiNRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDL 1849
Cdd:cd14600   172 T-HLQYVAWPDHGVPDDSSDFLEFVNYVR---SKRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKM 247

                         250       260
                  ....*....|....*....|....*.
gi 332800999 1850 RLHRVHMVQTECQYVYLHQCVRDVLR 1875
Cdd:cd14600   248 RDQRAMMVQTSSQYKFVCEAILRVYE 273

R-PTPc-A-E-2

cd14552

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

1667-1870

1.98e-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: 1.98e-56

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1667 YINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPADqDSLYYGDLILQMLSES 1746
Cdd:cd14552     1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPED-GSVSSGDITVELKDQT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1747 VLPEWTIREFKICgEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDYINRSpGAGPTVVHCSAGVGRTGTFIA 1826
Cdd:cd14552    80 DYEDYTLRDFLVT-KGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQS-GNHPITVHCSAGAGRTGTFCA 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 332800999 1827 LDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 1870
Cdd:cd14552   158 LSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201

PTPc-N20

cd14596

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

1667-1875

6.76e-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: 193.43 E-value: 6.76e-56

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1667 YINASYI--PGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPAD-QDSLYYGDLILQML 1743
Cdd:cd14596     1 YINASYItmPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETlQEPMELENYQLRLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1744 SESVLPEWTIREFKICGEEQLDAHrLIRHFHYTVWPDHGVPETTQSLIQFVRtvrdYINRSPGAGPTVVHCSAGVGRTGT 1823
Cdd:cd14596    81 NYQALQYFIIRIIKLVEKETGENR-LIKHLQFTTWPDHGTPQSSDQLVKFIC----YMRKVHNTGPIVVHCSAGIGRAGV 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 332800999 1824 FIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRDVLR 1875
Cdd:cd14596   156 LICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207

R-PTPc-E-2

cd14622

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

1666-1872

1.13e-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: 1.13e-55

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1666 DYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPAdQDSLYYGDLILQMLSE 1745
Cdd:cd14622     1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPS-EGSVTHGEITIEIKND 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1746 SVLPEWTIREFkICGEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDYINRSpGAGPTVVHCSAGVGRTGTFI 1825
Cdd:cd14622    80 TLLETISIRDF-LVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQT-GNHPIVVHCSAGAGRTGTFI 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 332800999 1826 ALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRD 1872
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; ...

1667-1868

3.31e-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: 185.70 E-value: 3.31e-53

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1667 YINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPADQ-DSLYYGDLILQMLSE 1745
Cdd:cd14542     1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGeEQLQFGPFKISLEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1746 S-VLPEWTIREFKI-CGEEQldahRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDYinRSPGAGPTVVHCSAGVGRTGT 1823
Cdd:cd14542    81 KrVGPDFLIRTLKVtFQKES----RTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDY--QGSEDVPICVHCSAGCGRTGT 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 332800999 1824 FIALD---RILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 1868
Cdd:cd14542   155 ICAIDyvwNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202

R-PTPc-A-2

cd14623

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

1642-1872

7.63e-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: 7.63e-53

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1642 RYNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVK 1721
Cdd:cd14623     1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1722 CDHYWPADqDSLYYGDLILQMLSESVLPEWTIREFKICGEEQlDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDYI 1801
Cdd:cd14623    81 CAQYWPSD-GSVSYGDITIELKKEEECESYTVRDLLVTNTRE-NKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQ 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332800999 1802 NRSpGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRD 1872
Cdd:cd14623   159 QQS-GNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228

PTPc-N22

cd14602

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

1640-1870

6.14e-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: 6.14e-52

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1640 KNRYNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGR 1719
Cdd:cd14602     1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1720 VKCDHYWP-ADQDSLYYGDLILQMLSESVLPEWTIREFKI-CGEEQldahRLIRHFHYTVWPDHGVPETTQSLIQFVRTV 1797
Cdd:cd14602    81 KKCERYWAePGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVkFNSET----RTIYQFHYKNWPDHDVPSSIDPILELIWDV 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332800999 1798 RDYinRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLdsKDSV-----DIYGAVHDLRLHRVHMVQTECQYVYLHQCV 1870
Cdd:cd14602   157 RCY--QEDDSVPICIHCSAGCGRTGVICAIDYTWMLL--KDGIipenfSVFSLIQEMRTQRPSLVQTKEQYELVYNAV 230

PTPc-N5

cd14613

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

1640-1867

6.29e-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: 6.29e-52

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1640 KNRYNNILPYDATRVKLSNVD-DDPCSDYINASYIPG-NNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEK 1717
Cdd:cd14613    28 KNRYKTILPNPHSRVCLTSPDqDDPLSSYINANYIRGyGGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1718 GRvKCDHYWPADQdSLYYGdliLQMLSESVLPE--WTIREFKI-CGEEQldahRLIRHFHYTVWPDHGVPETTQSLIQFV 1794
Cdd:cd14613   108 NE-KCTEYWPEEQ-VTYEG---IEITVKQVIHAddYRLRLITLkSGGEE----RGLKHYWYTSWPDQKTPDNAPPLLQLV 178

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332800999 1795 RTVRDYINRS-PGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 1867
Cdd:cd14613   179 QEVEEARQQAePNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVH 252

R-PTPc-R

cd14611

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

1640-1868

9.53e-52

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

Pssm-ID: 350459 [Multi-domain] Cd Length: 226 Bit Score: 182.43 E-value: 9.53e-52

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1640 KNRYNNILPYDATRVKLSNVD-DDPCSDYINASYIPG-NNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEK 1717
Cdd:cd14611     2 KNRYKTILPNPHSRVCLKPKNsNDSLSTYINANYIRGyGGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1718 GRvKCDHYWPADQDslYYGDLILQMLSESVLPEWTIREFKIcgeEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTV 1797
Cdd:cd14611    82 NE-KCVLYWPEKRG--IYGKVEVLVNSVKECDNYTIRNLTL---KQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDV 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332800999 1798 RDYINRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 1868
Cdd:cd14611   156 EEDRLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVHH 226

PTPc-N12

cd14604

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

1596-1870

2.07e-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: 2.07e-51

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1596 NQFEGHFMKLQAdsnylLSKEYEELK----DVGRNQscdiallpENRGKNRYNNILPYDATRVKLSNVDDDPCSDYINAS 1671
Cdd:cd14604    25 DNFASDFMRLRR-----LSTKYRTEKiyptATGEKE--------ENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINAN 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1672 YIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPA-DQDSLYYGDLILQMLSESVLPE 1750
Cdd:cd14604    92 FIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLyGEEPMTFGPFRISCEAEQARTD 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1751 WTIREFKIcgEEQLDAHRLIRhFHYTVWPDHGVPETTQSLIQFVRTVRDYINRSpgAGPTVVHCSAGVGRTGTFIALD-- 1828
Cdd:cd14604   172 YFIRTLLL--EFQNETRRLYQ-FHYVNWPDHDVPSSFDSILDMISLMRKYQEHE--DVPICIHCSAGCGRTGAICAIDyt 246

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 332800999 1829 -RILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 1870
Cdd:cd14604   247 wNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 289

PTPc-N21_14

cd14540

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

1667-1868

3.17e-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: 180.73 E-value: 3.17e-51

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1667 YINASYIP---GNNFRReYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPA---DQDSLYYGDLIL 1740
Cdd:cd14540     1 YINASHITatvGGKQRF-YIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTlggEHDALTFGEYKV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1741 QMLSESVLPEWTIREFKIcGEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQF---VRTVRDYI-------NRSPgagPT 1810
Cdd:cd14540    80 STKFSVSSGCYTTTGLRV-KHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFleeINSVRRHTnqdvaghNRNP---PT 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 332800999 1811 VVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 1868
Cdd:cd14540   156 LVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYN 213

R-PTP-N2

cd14610

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

1613-1865

7.42e-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: 7.42e-51

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1613 LSKEYEELKDV-GRNQSCDIALLPENRGKNRYNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRR-EYIVTQGPLP 1690
Cdd:cd14610    19 LEKEWEALCAYqAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMDHDPRNpAYIATQGPLP 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1691 GTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPaDQDSLYYGDLILQMLSESVLPE-WTIREFKIcGEEQLDAHRL 1769
Cdd:cd14610    99 ATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWP-DEGSNLYHIYEVNLVSEHIWCEdFLVRSFYL-KNLQTNETRT 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1770 IRHFHYTVWPDHGVPETTQSLIQFVRTVRD-YINRSpgaGPTVVHCSAGVGRTGTFIALDRILQQL-DSKDSVDIYGAVH 1847
Cdd:cd14610   177 VTQFHFLSWNDQGVPASTRSLLDFRRKVNKcYRGRS---CPIIVHCSDGAGRSGTYILIDMVLNKMaKGAKEIDIAATLE 253

                         250
                  ....*....|....*...
gi 332800999 1848 DLRLHRVHMVQTECQYVY 1865
Cdd:cd14610   254 HLRDQRPGMVQTKEQFEF 271

R-PTP-N

cd14609

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

1613-1865

8.93e-49

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: 8.93e-49

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1613 LSKEYEELKDV-GRNQSCDIALLPENRGKNRYNNILPYDATRVKLSNVDDDPCSDYINASYIPGNNFRR-EYIVTQGPLP 1690
Cdd:cd14609    17 LAKEWQALCAYqAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASPIIEHDPRMpAYIATQGPLS 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1691 GTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDSLYYgDLILQMLSESVLPE-WTIREFKIcGEEQLDAHRL 1769
Cdd:cd14609    97 HTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYH-IYEVNLVSEHIWCEdFLVRSFYL-KNVQTQETRT 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1770 IRHFHYTVWPDHGVPETTQSLIQFVRTV-RDYINRSpgaGPTVVHCSAGVGRTGTFIALDRILQQL-DSKDSVDIYGAVH 1847
Cdd:cd14609   175 LTQFHFLSWPAEGIPSSTRPLLDFRRKVnKCYRGRS---CPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATLE 251

                         250
                  ....*....|....*...
gi 332800999 1848 DLRLHRVHMVQTECQYVY 1865
Cdd:cd14609   252 HVRDQRPGMVRTKDQFEF 269

PTPc-N4

cd14601

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

1666-1875

1.05e-48

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

Pssm-ID: 350449 [Multi-domain] Cd Length: 212 Bit Score: 173.21 E-value: 1.05e-48

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1666 DYINASYI----PGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDSLYYGDLILQ 1741
Cdd:cd14601     1 DYINANYInmeiPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSSSYGGFQVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1742 MLSESVLPEWTIREFKICGEEQLDAhRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDyiNRSPGAGPTVVHCSAGVGRT 1821
Cdd:cd14601    81 CHSEEGNPAYVFREMTLTNLEKNES-RPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRN--KRAGKDEPVVVHCSAGIGRT 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 332800999 1822 GTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRDVLR 1875
Cdd:cd14601   158 GVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVYE 211

PTPc-N14

cd14599

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

1616-1868

1.48e-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: 1.48e-48

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1616 EYEELKDVGRNQSCDIALLPENRGKNRYNNILPYDATRVKLSNVDDDPcSDYINASYIPGNNFRRE--YIVTQGPLPGTK 1693
Cdd:cd14599    17 EYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVPTKENN-TGYINASHIKVTVGGEEwhYIATQGPLPHTC 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1694 DDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWP---ADQDSLYYG--DLILQMLSESVLPEWTIREFK--ICGEEqlda 1766
Cdd:cd14599    96 HDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPklgSKHSSATYGkfKVTTKFRTDSGCYATTGLKVKhlLSGQE---- 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1767 hRLIRHFHYTVWPDHGVPETTQSLIQF---VRTVRDYINRSPGAG-----PTVVHCSAGVGRTGTFIALDRILQQLDSKD 1838
Cdd:cd14599   172 -RTVWHLQYTDWPDHGCPEEVQGFLSYleeIQSVRRHTNSMLDSTkncnpPIVVHCSAGVGRTGVVILTELMIGCLEHNE 250

                         250       260       270
                  ....*....|....*....|....*....|
gi 332800999 1839 SVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 1868
Cdd:cd14599   251 KVEVPVMLRHLREQRMFMIQTIAQYKFVYQ 280

R-PTP-C-2

cd14558

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

1667-1867

1.66e-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: 1.66e-47

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1667 YINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDSlyYGDLILQMLSES 1746
Cdd:cd14558     1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKT--YGDIEVELKDTE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1747 VLPEWTIREFKIcGEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVR----DYINRSPGAGPTVVHCSAGVGRTG 1822
Cdd:cd14558    79 KSPTYTVRVFEI-THLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKqklpYKNSKHGRSVPIVVHCSDGSSRTG 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 332800999 1823 TFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 1867
Cdd:cd14558   158 IFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202

R-PTPc-typeIIb-2

cd14556

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

1667-1868

3.72e-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: 168.35 E-value: 3.72e-47

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1667 YINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQcVEKGRVKCDHYWPaDQDSLYYGDLILQMLSES 1746
Cdd:cd14556     1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQ-LDPKDQSCPQYWP-DEGSGTYGPIQVEFVSTT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1747 VLPEWTIREFKICGEEQL-DAHRLIRHFHYTVWPDHG-VPETTQSLIQFVRTVRDYINRSpGAGPTVVHCSAGVGRTGTF 1824
Cdd:cd14556    79 IDEDVISRIFRLQNTTRPqEGYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQEQS-GEGPIVVHCLNGVGRSGVF 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 332800999 1825 IALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 1868
Cdd:cd14556   158 CAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201

R-PTP-N-N2

cd14546

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

1667-1870

2.75e-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: 2.75e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1667 YINASYIPGNNFRRE-YIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPaDQDSLYYGDLILQMLSE 1745
Cdd:cd14546     1 YINASTIYDHDPRNPaYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWP-EEGSEVYHIYEVHLVSE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1746 SVLPE-WTIREFKIcGEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTV-RDYINRSpgaGPTVVHCSAGVGRTGT 1823
Cdd:cd14546    80 HIWCDdYLVRSFYL-KNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVnKSYRGRS---CPIVVHCSDGAGRTGT 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 332800999 1824 FIALDRILQQL-DSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 1870
Cdd:cd14546   156 YILIDMVLNRMaKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAV 203

PTPc_plant_PTP1

cd17658

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

1667-1865

3.61e-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: 159.94 E-value: 3.61e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1667 YINASYIPGNNFRR--EYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGR-VKCDHYWPA-DQDSLYYGDLilqm 1742
Cdd:cd17658     1 YINASLVETPASESlpKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStAKCADYFPAeENESREFGRI---- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1743 lseSVLPEW--------TIREFKICGEEQLDAHRLIRHFHYTVWPDHGVPETTqsliqfvRTVRDYINRS----PGAGPT 1810
Cdd:cd17658    77 ---SVTNKKlkhsqhsiTLRVLEVQYIESEEPPLSVLHIQYPEWPDHGVPKDT-------RSVRELLKRLygipPSAGPI 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 332800999 1811 VVHCSAGVGRTGTFIALDRILQQLDSKD--SVDIYGAVHDLRLHRVHMVQTECQYVY 1865
Cdd:cd17658   147 VVHCSAGIGRTGAYCTIHNTIRRILEGDmsAVDLSKTVRKFRSQRIGMVQTQDQYIF 203

PTP-N23

cd14539

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

1667-1868

1.72e-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: 157.93 E-value: 1.72e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1667 YINASYIPG-NNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWPADQ-DSLYYGDLILQMLS 1744
Cdd:cd14539     1 YINASLIEDlTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERgQALVYGAITVSLQS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1745 ESVLPEWTIREFKICGEEQlDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDYINRS-PGAGPTVVHCSAGVGRTGT 1823
Cdd:cd14539    81 VRTTPTHVERIISIQHKDT-RLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQrSLQTPIVVHCSSGVGRTGA 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 332800999 1824 FIALDRILQQLDSKDSV-DIYGAVHDLRLHRVHMVQTECQYVYLHQ 1868
Cdd:cd14539   160 FCLLYAAVQEIEAGNGIpDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205

PHA02742

protein tyrosine phosphatase; Provisional

1594-1882

9.42e-43

protein tyrosine phosphatase; Provisional

Pssm-ID: 165109 [Multi-domain] Cd Length: 303 Bit Score: 159.40 E-value: 9.42e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1594 KINQFEGHFMKLQADSN--YLLSKEYEELKDVGRNQSCDIALLPENRGKNRYNNILPYDATRVKLSNvdDDPCSDYINAS 1671
Cdd:PHA02742    7 KKNSFAKNCEQLIEESNlaEILKEEHEHIMQEIVAFSCNESLELKNMKKCRYPDAPCFDRNRVILKI--EDGGDDFINAS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1672 YIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYW-PADQDSLYYGDLILQMLSESVLPE 1750
Cdd:PHA02742   85 YVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYWmPHERGKATHGEFKIKTKKIKSFRN 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1751 WTIREFKICGEEQ---LDahrlIRHFHYTVWPDHGVPETTQSLIQFVRTVR--DYINRSPGAG-------PTVVHCSAGV 1818
Cdd:PHA02742  165 YAVTNLCLTDTNTgasLD----IKHFAYEDWPHGGLPRDPNKFLDFVLAVReaDLKADVDIKGenivkepPILVHCSAGL 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332800999 1819 GRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYlhqCVRDVLRARKLRSE 1882
Cdd:PHA02742  241 DRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIF---CYFIVLIFAKLMAD 301

COG5599

Protein tyrosine phosphatase [Signal transduction mechanisms];

1635-1863

1.25e-41

Protein tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 444335 [Multi-domain] Cd Length: 282 Bit Score: 155.25 E-value: 1.25e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1635 PENRGKNRYNNILPYDATRVKlsnvDDDPcsdYINASYIPGNNFRReYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQC 1714
Cdd:COG5599    40 INGSPLNRFRDIQPYKETALR----ANLG---YLNANYIQVIGNHR-YIATQYPLEEQLEDFFQMLFDNNTPVLVVLASD 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1715 VE--KGRVKCDHYWPADQDSLYYgDLILQMLSESVL-PEWTIREFKI----CGEEQLDahrlIRHFHYTVWPDHGVPETT 1787
Cdd:COG5599   112 DEisKPKVKMPVYFRQDGEYGKY-EVSSELTESIQLrDGIEARTYVLtikgTGQKKIE----IPVLHVKNWPDHGAISAE 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1788 QsLIQFVRTVRDYIN-RSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKD--SVDIYGAVHDLRLHR-VHMVQTECQY 1863
Cdd:COG5599   187 A-LKNLADLIDKKEKiKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRnGGMVQTSEQL 265

PTPc_motif

smart00404

Protein tyrosine phosphatase, catalytic domain motif;

1770-1870

5.10e-40

Protein tyrosine phosphatase, catalytic domain motif;

Pssm-ID: 214649 [Multi-domain] Cd Length: 105 Bit Score: 144.04 E-value: 5.10e-40

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999   1770 IRHFHYTVWPDHGVPETTQSLIQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDS-KDSVDIYGAVHD 1848
Cdd:smart00404    2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAeAGEVDIFDTVKE 81

                            90       100
                    ....*....|....*....|..
gi 332800999   1849 LRLHRVHMVQTECQYVYLHQCV 1870
Cdd:smart00404   82 LRSQRPGMVQTEEQYLFLYRAL 103

PTPc_DSPc

smart00012

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

1770-1870

5.10e-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: 5.10e-40

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999   1770 IRHFHYTVWPDHGVPETTQSLIQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDS-KDSVDIYGAVHD 1848
Cdd:smart00012    2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAeAGEVDIFDTVKE 81

                            90       100
                    ....*....|....*....|..
gi 332800999   1849 LRLHRVHMVQTECQYVYLHQCV 1870
Cdd:smart00012   82 LRSQRPGMVQTEEQYLFLYRAL 103

PHA02747

protein tyrosine phosphatase; Provisional

1635-1867

5.12e-39

protein tyrosine phosphatase; Provisional

Pssm-ID: 165114 [Multi-domain] Cd Length: 312 Bit Score: 148.61 E-value: 5.12e-39

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1635 PENRGKNRYNNILPYDATRVKLSNvDDDPCSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQC 1714
Cdd:PHA02747   49 PENQPKNRYWDIPCWDHNRVILDS-GGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPT 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1715 -VEKGRVKCDHYW-PADQDSLYYGDLILQMLSESVLPEWTIREFKICgEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQ 1792
Cdd:PHA02747  128 kGTNGEEKCYQYWcLNEDGNIDMEDFRIETLKTSVRAKYILTLIEIT-DKILKDSRKISHFQCSEWFEDETPSDHPDFIK 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1793 FVRTV--------RDYINRSPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYV 1864
Cdd:PHA02747  207 FIKIIdinrkksgKLFNPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYL 286


                  ...
gi 332800999 1865 YLH 1867
Cdd:PHA02747  287 FIQ 289

PHA02738

hypothetical protein; Provisional

1637-1871

8.97e-39

hypothetical protein; Provisional

Pssm-ID: 222923 [Multi-domain] Cd Length: 320 Bit Score: 148.15 E-value: 8.97e-39

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1637 NRGKNRYNNILPYDATRVKLSNVDDDpcSDYINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVE 1716
Cdd:PHA02738   49 NRKLNRYLDAVCFDHSRVILPAERNR--GDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKE 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1717 KGRVKCDHYWP-ADQDSLYYGDLILQMLSESVLPEWTirEFKICGEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVR 1795
Cdd:PHA02738  127 NGREKCFPYWSdVEQGSIRFGKFKITTTQVETHPHYV--KSTLLLTDGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVL 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1796 TVRD-----YINR------SPGAGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYV 1864
Cdd:PHA02738  205 EVRQcqkelAQESlqighnRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYF 284


                  ....*..
gi 332800999 1865 YLHQCVR 1871
Cdd:PHA02738  285 FCYRAVK 291

PTPc-N21

cd14598

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

1667-1875

4.33e-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: 4.33e-38

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1667 YINASYIPGNNFRRE--YIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCDHYWP---ADQDSLYYG--DLI 1739
Cdd:cd14598     1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlgSRHNTVTYGrfKIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1740 LQMLSESVLPEWTIREFK--ICGEEqldahRLIRHFHYTVWPDHGVPETTQSLIQF---VRTVRDYIN-----RSPGAgP 1809
Cdd:cd14598    81 TRFRTDSGCYATTGLKIKhlLTGQE-----RTVWHLQYTDWPEHGCPEDLKGFLSYleeIQSVRRHTNstidpKSPNP-P 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332800999 1810 TVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRDVLR 1875
Cdd:cd14598   155 VLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220

PHA02746

protein tyrosine phosphatase; Provisional

1612-1874

1.12e-37

protein tyrosine phosphatase; Provisional

Pssm-ID: 165113 [Multi-domain] Cd Length: 323 Bit Score: 145.17 E-value: 1.12e-37

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1612 LLSKEYEELKDVGRNQSCDIALLPENRGKNRYNNILPYDATRVKLSN-------------------VDDDPCSDYINASY 1672
Cdd:PHA02746   26 FVLLEHAEVMDIPIRGTTNHFLKKENLKKNRFHDIPCWDHSRVVINAheslkmfdvgdsdgkkievTSEDNAENYIHANF 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1673 IPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQcVEKGRVKCDHYWPADQDS-LYYGDLILQMLSESVLPEW 1751
Cdd:PHA02746  106 VDGFKEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTD-IDDDDEKCFELWTKEEDSeLAFGRFVAKILDIIEELSF 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1752 TIREFKICgEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFV--------RTVRDYINRSPGAGPTVVHCSAGVGRTGT 1823
Cdd:PHA02746  185 TKTRLMIT-DKISDTSREIHHFWFPDWPDNGIPTGMAEFLELInkvneeqaELIKQADNDPQTLGPIVVHCSAGIGRAGT 263

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 332800999 1824 FIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRDVL 1874
Cdd:PHA02746  264 FCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKALKYAI 314

R5-PTP-2

cd14550

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

1667-1868

2.37e-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: 131.29 E-value: 2.37e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1667 YINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCdhYWPADQDSLYYGDLILQMLSES 1746
Cdd:cd14550     1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPI--YWPTKEKPLECETFKVTLSGED 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1747 VLPEW-----TIREFKIcgEEQLDAHRL-IRHFHYTVWPDHGVP-ETTQSLIQFVRtvRDYINRSpgaGPTVVHCSAGVG 1819
Cdd:cd14550    79 HSCLSneirlIVRDFIL--ESTQDDYVLeVRQFQCPSWPNPCSPiHTVFELINTVQ--EWAQQRD---GPIVVHDRYGGV 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 332800999 1820 RTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 1868
Cdd:cd14550   152 QAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200

R-PTPc-T-2

cd14634

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

1667-1868

1.28e-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: 1.28e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1667 YINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQcVEKGRVkCDHYWPaDQDSLYYGDLILQMLSES 1746
Cdd:cd14634     1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNE-MDAAQL-CMQYWP-EKTSCCYGPIQVEFVSAD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1747 VLPEWTIREFKICGEEQ-LDAHRLIRHFHYTVWPDH-GVPETTQSLIQFVRTVRDYINRSPGA-GPTVVHCSAGVGRTGT 1823
Cdd:cd14634    78 IDEDIISRIFRICNMARpQDGYRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQYDGReGRTVVHCLNGGGRSGT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 332800999 1824 FIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 1868
Cdd:cd14634   158 FCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYE 202

PTP_tm

pfam18861

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

1383-1520

6.15e-33

Pssm-ID: 465889 Cd Length: 126 Bit Score: 124.64 E-value: 6.15e-33

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999  1383 VNCSWFSDTNGAVKYFTVVVREADgsDELKPEQQHPLPSYLEYRhNASIRVYQTNYFASKCAENPnSNSKSFNIKLGAEM 1462
Cdd:pfam18861    1 IQFSLFNSSNGPIKAYGVIVTTND--SLNRPLKEYLNKTYYDWK-YKKTDSYLATVTPNPFTSPR-SSSRSLTVPVGTGS 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 332800999  1463 ESlggkcdptqQKFCDGPLKPHTAYRISIRAFTQL-FDEDLKEFTKPLYSDTFFSLPIT 1520
Cdd:pfam18861   77 KW---------QGYCNGPLKPLGSYRFSVAAFTRLeFDDGLIDGEESYVSFTPFSEPIA 126

R-PTPc-U-2

cd14637

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

1667-1870

3.17e-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: 3.17e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1667 YINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV-KCDHYWPaDQDSLYYGDLILQMLSE 1745
Cdd:cd14637     1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWP-EPGLQQYGPMEVEFVSG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1746 SVLPEWTIREFKICGEEQL-DAHRLIRHFHYTVW-PDHGVPETTQSLIQFVRTVRDYiNRSPGAGPTVVHCSAGVGRTGT 1823
Cdd:cd14637    80 SADEDIVTRLFRVQNITRLqEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKW-QRESGEGRTVVHCLNGGGRSGT 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 332800999 1824 FIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 1870
Cdd:cd14637   159 YCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIA 205

R-PTPc-K-2

cd14636

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

1667-1867

6.57e-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: 6.57e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1667 YINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQC-VEKGrvkCDHYWPaDQDSLYYGDLILQMLSE 1745
Cdd:cd14636     1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVdLAQG---CPQYWP-EEGMLRYGPIQVECMSC 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1746 SVLPEWTIREFKICG-EEQLDAHRLIRHFHYTVWPDH-GVPETTQSLIQFVRTVRDYINR-SPGAGPTVVHCSAGVGRTG 1822
Cdd:cd14636    77 SMDCDVISRIFRICNlTRPQEGYLMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEEcDEGEGRTIIHCLNGGGRSG 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 332800999 1823 TFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 1867
Cdd:cd14636   157 MFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCY 201

R-PTP-G-2

cd17670

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

1667-1870

6.59e-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: 6.59e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1667 YINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQcvEKGRVKCDH-YWPADQDSLYYGDLILQMLSE 1745
Cdd:cd17670     1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD--NQGLAEDEFvYWPSREESMNCEAFTVTLISK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1746 SVLPewtirefkICGEEQLDAHRLI------------RHFHYTVWPDHGVP-ETTQSLIQFVRtvRDYINRSpgaGPTVV 1812
Cdd:cd17670    79 DRLC--------LSNEEQIIIHDFIleatqddyvlevRHFQCPKWPNPDAPiSSTFELINVIK--EEALTRD---GPTIV 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 332800999 1813 HCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 1870
Cdd:cd17670   146 HDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAM 203

R-PTPc-M-2

cd14635

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

1667-1868

2.63e-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: 2.63e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1667 YINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQcVEKGRVkCDHYWPaDQDSLYYGDLILQMLSES 1746
Cdd:cd14635     1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLND-VDPAQL-CPQYWP-ENGVHRHGPIQVEFVSAD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1747 VLPEWTIREFKICGEEQ-LDAHRLIRHFHYTVWPDH-GVPETTQSLIQFVRTVRDYINRSPGA-GPTVVHCSAGVGRTGT 1823
Cdd:cd14635    78 LEEDIISRIFRIYNAARpQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEYNGGeGRTVVHCLNGGGRSGT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 332800999 1824 FIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 1868
Cdd:cd14635   158 FCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYE 202

R-PTP-Z-2

cd17669

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

1667-1870

2.02e-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: 2.02e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1667 YINASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRVKCdHYWPADQDSLYYGDLILQMLSE- 1745
Cdd:cd17669     1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWPNKDEPINCETFKVTLIAEe 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1746 ----SVLPEWTIREFkICGEEQLDAHRLIRHFHYTVWPDHGVP-ETTQSLIQFVRtvRDYINRSpgaGPTVVHCSAGVGR 1820
Cdd:cd17669    80 hkclSNEEKLIIQDF-ILEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELISIIK--EEAANRD---GPMIVHDEHGGVT 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 332800999 1821 TGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 1870
Cdd:cd17669   154 AGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203

PHA02740

protein tyrosine phosphatase; Provisional

1593-1868

3.55e-16

protein tyrosine phosphatase; Provisional

Pssm-ID: 165107 [Multi-domain] Cd Length: 298 Bit Score: 81.55 E-value: 3.55e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1593 IKINQFEGHFMKlqADSNYLLSKEYEEL---KDVGRNQSCDIAllpENRGKNRYN--NILPYDATRVKLSNVDDdpcsdY 1667
Cdd:PHA02740    9 INGMDFINFINK--PDLLSCIIKEYRAIvpeHEDEANKACAQA---ENKAKDENLalHITRLLHRRIKLFNDEK-----V 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1668 INASYIPGNNFRREYIVTQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKgrvKC-DHYWPADQDSL-YYGDLILQMLSE 1745
Cdd:PHA02740   79 LDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHADK---KCfNQFWSLKEGCViTSDKFQIETLEI 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1746 SVLPEWTIREFKIcgEEQLDAHRLIRHFHYTVWPDHGVPETTQSLIQFVRTVRDY---INRSPG---AGPTVVHCSAGVG 1819
Cdd:PHA02740  156 IIKPHFNLTLLSL--TDKFGQAQKISHFQYTAWPADGFSHDPDAFIDFFCNIDDLcadLEKHKAdgkIAPIIIDCIDGIS 233

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 332800999 1820 RTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 1868
Cdd:PHA02740  234 SSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYH 282

fn3

Fibronectin type III domain;

1172-1254

1.79e-12

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 64.74 E-value: 1.79e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999  1172 SPPSLMSFADIANTSLAITWKGPPDWT-DYNDFELQWLPRDALTVFNPYNNRKSEGR-IVYGLRPGRSYQFNVKTVSGDS 1249
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNgPITGYEVEYRPKNSGEPWNEITVPGTTTSvTLTGLKPGTEYEVRVQAVNGGG 80


                   ....*
gi 332800999  1250 WKTYS 1254
Cdd:pfam00041   81 EGPPS 85

CDC14

COG2453

Protein-tyrosine phosphatase [Signal transduction mechanisms];

1770-1868

1.86e-11

Protein-tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 441989 [Multi-domain] Cd Length: 140 Bit Score: 63.45 E-value: 1.86e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1770 IRHFHYTvWPDHGVPETTQsLIQFVRTVRDYINRSpgaGPTVVHCSAGVGRTGTFIALDRILQQLDSKDsvdiygAVHDL 1849
Cdd:COG2453    48 LEYLHLP-IPDFGAPDDEQ-LQEAVDFIDEALREG---KKVLVHCRGGIGRTGTVAAAYLVLLGLSAEE------ALARV 116

                          90
                  ....*....|....*....
gi 332800999 1850 RLHRVHMVQTECQYVYLHQ 1868
Cdd:COG2453   117 RAARPGAVETPAQRAFLER 135

fn3

Fibronectin type III domain;

1266-1345

1.17e-10

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 59.35 E-value: 1.17e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999  1266 DKIQNLHCRPQNSTAIACSWIPP---DSDFDGYSIECRKMDTQEVEFSRKLEKEKSLLNIMMLVPHKRYLVSIKVQSAGM 1342
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ...
gi 332800999  1343 TSE 1345
Cdd:pfam00041   81 EGP 83

fn3

Fibronectin type III domain;

642-718

1.28e-10

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 59.35 E-value: 1.28e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999   642 DKVQGVSVSNsARSDYLRVSWVHAT---GDFDHYEVTI--KNKNNFIQTKSIPKSENECVFVQLVPGRLYSVTVTTKSGQ 716
Cdd:pfam00041    1 SAPSNLTVTD-VTSTSLTVSWTPPPdgnGPITGYEVEYrpKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ..
gi 332800999   717 YE 718
Cdd:pfam00041   80 GE 81

fn3

Fibronectin type III domain;

818-891

2.37e-10

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 58.58 E-value: 2.37e-10

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332800999   818 SAVKNIHISPNGATdSLTVNWTP---GGGDVDSYTVSAF--RHSQKVDSQTIPKHVFEHTFHRLEAGEQYQIMIASVSG 891
Cdd:pfam00041    1 SAPSNLTVTDVTST-SLTVSWTPppdGNGPITGYEVEYRpkNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78

fn3

Fibronectin type III domain;

113-189

5.38e-10

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 57.81 E-value: 5.38e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999   113 PARFGVSKEKTTSTSLHVWWTPS---SGKVTSYEVQLFDENNQKiQGVQIQESTSWNEYTFFNLTAGSKYNIAITAVSGG 189
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGE-PWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

PTP_YopH-like

cd14559

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

1773-1866

1.33e-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: 60.49 E-value: 1.33e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1773 FHYTVWPDHG-------------VPETTQSLIQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFIAldrILQQLDSKDS 1839
Cdd:cd14559   121 VHVTNWPDHTaisseglkeladlVNKSAEEKRNFYKSKGSSAINDKNKLLPVIHCRAGVGRTGQLAA---AMELNKSPNN 197

                          90       100
                  ....*....|....*....|....*...
gi 332800999 1840 VDIYGAVHDLRLHR-VHMVQTECQYVYL 1866
Cdd:cd14559   198 LSVEDIVSDMRTSRnGKMVQKDEQLDTL 225

fn3

Fibronectin type III domain;

1085-1158

3.87e-09

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 55.11 E-value: 3.87e-09

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332800999  1085 SVSHLRGSNRNTTdSLWFNWSPA---SGDFDFYELILYNPNGTKKENWK--DKDLTEWRFQGLVPGRKYVLWVVTHSGD 1158
Cdd:pfam00041    2 APSNLTVTDVTST-SLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEItvPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

FN3

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

110-201

6.64e-09

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 54.81 E-value: 6.64e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999  110 PLPPARFGVSKekTTSTSLHVWWTPSS---GKVTSYEVQLFDENNQKIQGVQIQESTSwNEYTFFNLTAGSKYNIAITAV 186
Cdd:cd00063     1 PSPPTNLRVTD--VTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSE-TSYTLTGLKPGTEYEFRVRAV 77

                          90
                  ....*....|....*.
gi 332800999  187 SGGKRS-FSVYTNGST 201
Cdd:cd00063    78 NGGGESpPSESVTVTT 93

fn3

Fibronectin type III domain;

731-804

1.77e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 53.19 E-value: 1.77e-08

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332800999   731 PVKDLTLRNRSTEDLHVTWSGA---NGDVDQYEIQLL-FNDMKVFPPFHLVNTATEYRFTSLTPGRQYKILVLTISGD 804
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRpKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

fn3

Fibronectin type III domain;

554-630

2.73e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 52.80 E-value: 2.73e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999   554 SSVSGVTVNNSGrNDYLSVSWLLAP---GDVDNYEVTLSH--DGKVVQSLVIAKSVRECSFSSLTPGRLYTVTITTRSGK 628
Cdd:pfam00041    1 SAPSNLTVTDVT-STSLTVSWTPPPdgnGPITGYEVEYRPknSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ..
gi 332800999   629 YE 630
Cdd:pfam00041   80 GE 81

fn3

Fibronectin type III domain;

379-457

4.36e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 52.03 E-value: 4.36e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999   379 AVLQLRVKHANETSLSIMWQTPV---AEWEKYIISLADRD--LLLIHKSLSKDAKEFTFTDLVPGRKYMATVTSISGDLK 453
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNsgEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ....
gi 332800999   454 NSSS 457
Cdd:pfam00041   82 GPPS 85

PTP_DSP_cys

cd14494

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

1792-1868

5.57e-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: 5.57e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1792 QFVRTVRDYINR--SPGaGPTVVHCSAGVGRTGTFIALDRILQQLDS-KDSVDIYGavhdlRLHRVHMVQTECQYVYLHQ 1868
Cdd:cd14494    40 AMVDRFLEVLDQaeKPG-EPVLVHCKAGVGRTGTLVACYLVLLGGMSaEEAVRIVR-----LIRPGGIPQTIEQLDFLIK 113

CDKN3-like

cd14505

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

1770-1868

8.46e-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: 8.46e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1770 IRHFHYTVwPDHGVPETTQsliQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFIAldRILQQLDSKDSVDiyGAVHDL 1849
Cdd:cd14505    73 ITWHHLPI-PDGGVPSDIA---QWQELLEELLSALENGKKVLIHCKGGLGRTGLIAA--CLLLELGDTLDPE--QAIAAV 144

                          90
                  ....*....|....*....
gi 332800999 1850 RLHRVHMVQTECQYVYLHQ 1868
Cdd:cd14505   145 RALRPGAIQTPKQENFLHQ 163

FN3

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

289-364

1.25e-07

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 51.34 E-value: 1.25e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999  289 PMEVSNLKVTNDGSlTSLKVKWQRPP---GNVDSYNITLSHKGTIKESRVLAPWITETHF--KELVPGRLYQVTVSCVSG 363
Cdd:cd00063     1 PSPPTNLRVTDVTS-TSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYtlTGLKPGTEYEFRVRAVNG 79


                  .
gi 332800999  364 E 364
Cdd:cd00063    80 G 80

FN3

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

1265-1353

4.49e-07

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 49.80 E-value: 4.49e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1265 PDKIQNLHCRPQNSTAIACSWIPPDSD---FDGYSIECRKMDTQEVEFSRKLEKEKSLLNIMMLVPHKRYLVSIKVQSAG 1341
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDggpITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|..
gi 332800999 1342 MTSEVVEDSTIT 1353
Cdd:cd00063    81 GESPPSESVTVT 92

FN3

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

110-192

7.45e-07

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 48.76 E-value: 7.45e-07

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999    110 PLPPARFGVSKekTTSTSLHVWWT-PSSGKVTSYEVQLFDENNQK-IQGVQIQESTSWNEYTFFNLTAGSKYNIAITAVS 187
Cdd:smart00060    1 PSPPSNLRVTD--VTSTSVTLSWEpPPDDGITGYIVGYRVEYREEgSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78


                    ....*
gi 332800999    188 GGKRS 192
Cdd:smart00060   79 GAGEG 83

fn3

Fibronectin type III domain;

997-1070

9.19e-07

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 48.57 E-value: 9.19e-07

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332800999   997 AVTDLRITENSTRHLSFRWTASE---GELSWYNIFLYNPDGNLQERAQVDPLVQ-SFSFQNLLQGRMYKMVIVTHSGE 1070
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNEITVPGTTtSVTLTGLKPGTEYEVRVQAVNGG 79

FN3

Fibronectin type 3 domain [General function prediction only];

478-845

1.18e-06

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 53.47 E-value: 1.18e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999  478 TSSLFTNWTQAQGDVEFYQVLLIHENVVIKNESISSETSRYSFHSLKSGSLYSVVVTTVSGGISSRQ----VVVEGRTVP 553
Cdd:COG3401    61 LSSGGGLGTGGRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTatavAGGAATAGT 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999  554 SSVSGVTVNNSGRNDYLSVSWLLAPGDVDNYEVTLSHDGKVVQSLVIAKSVRECSFSSLTPGRLYTVTITTRSGKYEN-- 631
Cdd:COG3401   141 YALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESap 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999  632 ---HSFSQERTVPDKVQGVSVSnSARSDYLRVSWV-HATGDFDHYEVTIKNKNNFIQTKSIPKSENECVFVQLVPGRLYS 707
Cdd:COG3401   221 sneVSVTTPTTPPSAPTGLTAT-ADTPGSVTLSWDpVTESDATGYRVYRSNSGDGPFTKVATVTTTSYTDTGLTNGTTYY 299

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999  708 VTVTTKSGQYEANEQGN------GRTIPEPVKDLTLRNRSTEDLHVTWSGA-NGDVDQYEIqllFNDMKVFPPFHLVN-- 778
Cdd:COG3401   300 YRVTAVDAAGNESAPSNvvsvttDLTPPAAPSGLTATAVGSSSITLSWTASsDADVTGYNV---YRSTSGGGTYTKIAet 376

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332800999  779 -TATEYRFTSLTPGRQYKILVLTISGDVQQSAFIEGFTVPSAVKNIHISPNGATDSLTVNWTPGGGDV 845
Cdd:COG3401   377 vTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAA 444

FN3

Fibronectin type 3 domain [General function prediction only];

785-1200

1.27e-06

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 53.47 E-value: 1.27e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999  785 FTSLTPGRQYKILVLTISGDVQQSAFIEGFTVPSAVKNIHISPNGATDSLTVNWTPGGGDVDSYTVSAFRHSQKVDSQTI 864
Cdd:COG3401   108 NTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTV 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999  865 PKHVFEHTFHRLEAGEQYQIMIASVS----GSLKNQINVV-GRTVPASVQGVIADNAYSSySLIVSWQKAAGV-AERYDI 938
Cdd:COG3401   188 TSTTLVDGGGDIEPGTTYYYRVAATDtggeSAPSNEVSVTtPTTPPSAPTGLTATADTPG-SVTLSWDPVTESdATGYRV 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999  939 LL-LTENGillrNTSEPATTKQHKFED--LTPGKKYKIQILTVSG----GLFSKEAQ-TEGRTVPAAVTDLRITENSTRH 1010
Cdd:COG3401   267 YRsNSGDG----PFTKVATVTTTSYTDtgLTNGTTYYYRVTAVDAagneSAPSNVVSvTTDLTPPAAPSGLTATAVGSSS 342

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1011 LSFRWTASEGE-LSWYNIflY---NPDGNLQERAQVDPlVQSFSFQNLLQGRM--YKMVIVTHSGELSNESF-IFGRTVP 1083
Cdd:COG3401   343 ITLSWTASSDAdVTGYNV--YrstSGGGTYTKIAETVT-TTSYTDTGLTPGTTyyYKVTAVDAAGNESAPSEeVSATTAS 419

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1084 ASVS-HLRGSNRNTTDSLWFNWSPASGDFDFYELILYNPNGTKKENWKDKDLTEW----RFQGLVPGRKYVLWVVTHSGD 1158
Cdd:COG3401   420 AASGeSLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSstvtATTTDTTTANLSVTTGSLVGG 499

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 332800999 1159 LSNKVTAESRTAPSPPSLMSFADIANTSLAITWKGPPDWTDY 1200
Cdd:COG3401   500 SGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGAS 541

fn3

Fibronectin type III domain;

291-364

1.41e-06

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 47.79 E-value: 1.41e-06

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332800999   291 EVSNLKVTNDGSlTSLKVKWQRPP---GNVDSYNITLSHKGTIKE--SRVLAPWITETHFKELVPGRLYQVTVSCVSGE 364
Cdd:pfam00041    2 APSNLTVTDVTS-TSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPwnEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

FN3

Fibronectin type 3 domain [General function prediction only];

157-652

1.78e-06

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 53.08 E-value: 1.78e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999  157 VQIQESTSWNEYTFFNLTAGSKYNIAITAVSGGKRSFS---VYTNGSTVPSPVKDIGISTKANSLLISWShGSGNVERYR 233
Cdd:COG3401     1 TGSSYLTSLDAGIAASAAANTAVNALSKAGGSGKTILVylaVVLSVTTKESPGTLLVAAGLSSGGGLGTG-GRAGTTSGV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999  234 LMLMDKGILVHGGVVDKHATSYAFHGLTPGYLYNLTVMTEAAGLQNYRWKLVRTAPMEVSNLKVTN-----DGSLTSLKV 308
Cdd:COG3401    80 AAVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAglygvDGANASGTT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999  309 KWQRPPGNVDSYNITLSHKGTIKESRVLAPWITETHFKELVPGRLYQVTVSCV-----SGELSAQKMAVGRTFPLAVLQL 383
Cdd:COG3401   160 ASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATdtggeSAPSNEVSVTTPTTPPSAPTGL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999  384 RVKHANETSLSIMWqTPVAEW--EKYIISLADRDllliHKSLSK----DAKEFTFTDLVPGRKYMATVTSISGDLKNS-- 455
Cdd:COG3401   240 TATADTPGSVTLSW-DPVTESdaTGYRVYRSNSG----DGPFTKvatvTTTSYTDTGLTNGTTYYYRVTAVDAAGNESap 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999  456 ----SSVKGRTVPAQVTDLHVANQGMTS-SLftNWTQAQG-DVEFYQVL----------LIHENVviknesisSETSrYS 519
Cdd:COG3401   315 snvvSVTTDLTPPAAPSGLTATAVGSSSiTL--SWTASSDaDVTGYNVYrstsgggtytKIAETV--------TTTS-YT 383

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999  520 FHSLKSGSLYSVVVTTV-SGGISSRQvvvegrtvPSSVSGVTVNNSGRNDYLSVSWLLAPGDVDNYEVTLSHDGKVVQSL 598
Cdd:COG3401   384 DTGLTPGTTYYYKVTAVdAAGNESAP--------SEEVSATTASAASGESLTASVDAVPLTDVAGATAAASAASNPGVSA 455

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 332800999  599 VIAKSVRECSFSSLTPGRLYTVTITTRSGKYENHSFSQERTVPDKVQGVSVSNS 652
Cdd:COG3401   456 AVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSV 509

PTP_PTEN

cd14509

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

1759-1845

2.61e-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: 2.61e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1759 CGEEQLDAHRlirhFHYTV----WPDHGVPeTTQSLIQFVRTVRDYINRSPGAgPTVVHCSAGVGRTGTFIA--LDRILQ 1832
Cdd:cd14509    48 CSERSYDPSK----FNGRVaeypFDDHNPP-PLELIKPFCEDVDEWLKEDEKN-VAAVHCKAGKGRTGVMICcyLLYLGK 121

                          90
                  ....*....|...
gi 332800999 1833 QLDSKDSVDIYGA 1845
Cdd:cd14509   122 FPSAKEALDFYGA 134

PTP_VSP_TPTE

cd14510

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

1756-1867

3.73e-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: 3.73e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1756 FKICGEEQLDAhrliRHFHYTV----WPDHGVPeTTQSLIQFVRTVRDYINRSPgAGPTVVHCSAGVGRTGTFIA--LDR 1829
Cdd:cd14510    59 YNLCSERGYDP----KYFHNRVervpIDDHNVP-TLDEMLSFTAEVREWMAADP-KNVVAIHCKGGKGRTGTMVCawLIY 132

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 332800999 1830 ILQQLDSKDSVDIYGAVH-DLRL-HRVHMVQTECQYVYLH 1867
Cdd:cd14510   133 SGQFESAKEALEYFGERRtDKSVsSKFQGVETPSQSRYVG 172

fn3

Fibronectin type III domain;

907-986

3.76e-06

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 46.64 E-value: 3.76e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999   907 SVQGVIADNAySSYSLIVSWQKAA---GVAERYDILLLTENGI-LLRNTSEPATTKQHKFEDLTPGKKYKIQILTVSGGL 982
Cdd:pfam00041    2 APSNLTVTDV-TSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGePWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....
gi 332800999   983 FSKE 986
Cdd:pfam00041   81 EGPP 84

fn3

Fibronectin type III domain;

466-539

3.83e-06

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 46.64 E-value: 3.83e-06

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332800999   466 QVTDLHVANQGmTSSLFTNWT---QAQGDVEFYQVLLIHEN--VVIKNESISSETSRYSFHSLKSGSLYSVVVTTVSGG 539
Cdd:pfam00041    2 APSNLTVTDVT-STSLTVSWTpppDGNGPITGYEVEYRPKNsgEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79

FN3

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

1171-1263

1.24e-05

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 45.57 E-value: 1.24e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1171 PSPPSLMSFADIANTSLAITWKGPPDWTDYND-FELQWLPRDALTVFNPYNNRKSEGR-IVYGLRPGRSYQFNVKTVSGD 1248
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITgYVVEYREKGSGDWKEVEVTPGSETSyTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|....*
gi 332800999 1249 SWKTYSKPIfgSVRT 1263
Cdd:cd00063    81 GESPPSESV--TVTT 93

FN3

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

1171-1250

3.73e-05

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 43.76 E-value: 3.73e-05

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999   1171 PSPPSLMSFADIANTSLAITWKGPPD--WTDYND-FELQWLPRDALTVFNPYNNRKSEGRIVyGLRPGRSYQFNVKTVSG 1247
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDdgITGYIVgYRVEYREEGSEWKEVNVTPSSTSYTLT-GLKPGTEYEFRVRAVNG 79


                    ...
gi 332800999   1248 DSW 1250
Cdd:smart00060   80 AGE 82

FN3

Fibronectin type 3 domain [General function prediction only];

84-234

3.86e-05

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 48.46 E-value: 3.86e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999   84 DLQAGTIYNFRIISLDEERT---------VVLQTDPLPPArfGVSKEKTTSTSLHVWWTPSSGK-VTSYEVQLFDENNQK 153
Cdd:COG3401   198 DIEPGTTYYYRVAATDTGGEsapsnevsvTTPTTPPSAPT--GLTATADTPGSVTLSWDPVTESdATGYRVYRSNSGDGP 275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999  154 IqgVQIQESTSwNEYTFFNLTAGSKYNIAITAV-SGGKRS-FSVY---TNGSTVPSPVKDI-GISTKANSLLISWSHGSG 227
Cdd:COG3401   276 F--TKVATVTT-TSYTDTGLTNGTTYYYRVTAVdAAGNESaPSNVvsvTTDLTPPAAPSGLtATAVGSSSITLSWTASSD 352


                  ....*...
gi 332800999  228 -NVERYRL 234
Cdd:COG3401   353 aDVTGYNV 360

FN3

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

289-363

6.64e-05

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 42.99 E-value: 6.64e-05

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999    289 PMEVSNLKVTNDGSlTSLKVKWQRPP-GNVDSYNITLSHKGTIKESRVL----APWITETHFKELVPGRLYQVTVSCVSG 363
Cdd:smart00060    1 PSPPSNLRVTDVTS-TSVTLSWEPPPdDGITGYIVGYRVEYREEGSEWKevnvTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

DUSP23

cd14504

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

1759-1826

8.52e-05

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: 8.52e-05

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332800999 1759 CGEEQLDAHRLIRHFHYTVwPDHGVPeTTQSLIQFVRTVRDYINRSpgaGPTVVHCSAGVGRTGTFIA 1826
Cdd:cd14504    39 PPPEHSDTCPGLRYHHIPI-EDYTPP-TLEQIDEFLDIVEEANAKN---EAVLVHCLAGKGRTGTMLA 101

FN3

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

817-891

9.62e-05

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 42.87 E-value: 9.62e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999  817 PSAVKNIHISPNGATdSLTVNWTP---GGGDVDSYTVSaFRHSQKVDSQTIPKHVF---EHTFHRLEAGEQYQIMIASVS 890
Cdd:cd00063     1 PSPPTNLRVTDVTST-SVTLSWTPpedDGGPITGYVVE-YREKGSGDWKEVEVTPGsetSYTLTGLKPGTEYEFRVRAVN 78


                  .
gi 332800999  891 G 891
Cdd:cd00063    79 G 79

fn3

Fibronectin type III domain;

37-98

2.15e-04

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 41.63 E-value: 2.15e-04

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332800999    37 SSHSVSIQWRIL----GSPCNFSLIYSSDTLGAALcPTFRIDNTTYGCNLQDLQAGTIYNFRIISL 98
Cdd:pfam00041   12 TSTSLTVSWTPPpdgnGPITGYEVEYRPKNSGEPW-NEITVPGTTTSVTLTGLKPGTEYEVRVQAV 76

FN3

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

641-718

2.34e-04

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 41.71 E-value: 2.34e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999  641 PDKVQGVSVSNSaRSDYLRVSWVHATGD---FDHYEVTIKNKN--NFIQTKSIPKSENECVFVQLVPGRLYSVTVTTKSG 715
Cdd:cd00063     1 PSPPTNLRVTDV-TSTSVTLSWTPPEDDggpITGYVVEYREKGsgDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79


                  ...
gi 332800999  716 QYE 718
Cdd:cd00063    80 GGE 82

FN3

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

729-804

2.58e-04

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 41.71 E-value: 2.58e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999  729 PEPVKDLTLRNRSTEDLHVTWS---GANGDVDQYEIQL---LFNDMKVFPPFhlVNTATEYRFTSLTPGRQYKILVLTIS 802
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTppeDDGGPITGYVVEYrekGSGDWKEVEVT--PGSETSYTLTGLKPGTEYEFRVRAVN 78


                  ..
gi 332800999  803 GD 804
Cdd:cd00063    79 GG 80

DSPc

smart00195

Dual specificity phosphatase, catalytic domain;

1772-1850

5.55e-04

Dual specificity phosphatase, catalytic domain;

Pssm-ID: 214551 [Multi-domain] Cd Length: 138 Bit Score: 41.88 E-value: 5.55e-04

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999   1772 HFHYTVWPdhgVPETTQSLI-QFVRTVRDYINRS-PGAGPTVVHCSAGVGRTGTFIAldRILQQLDSKDSVDIYGAVHDL 1849
Cdd:smart00195   44 DFTYLGVP---IDDNTETKIsPYFPEAVEFIEDAeSKGGKVLVHCQAGVSRSATLII--AYLMKTRNMSLNDAYDFVKDR 118


                    .
gi 332800999   1850 R 1850
Cdd:smart00195  119 R 119

PTP_PTEN-like

cd14497

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

1778-1826

9.33e-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: 9.33e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 332800999 1778 WPDHGVPeTTQSLIQFVRTVRDYINRSPG--AgptVVHCSAGVGRTGTFIA 1826
Cdd:cd14497    68 FPDHHPP-PLGLLLEIVDDIDSWLSEDPNnvA---VVHCKAGKGRTGTVIC 114

fn3

Fibronectin type III domain;

204-270

9.35e-04

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 40.09 E-value: 9.35e-04

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 332800999   204 SPVKDIGISTK-ANSLLISWS---HGSGNVERYRLML--MDKGILVHGGVVDKHATSYAFHGLTPGYLYNLTV 270
Cdd:pfam00041    1 SAPSNLTVTDVtSTSLTVSWTpppDGNGPITGYEVEYrpKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRV 73

FN3

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

641-716

9.71e-04

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 39.91 E-value: 9.71e-04

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999    641 PDKVQGVSVSNSArSDYLRVSWVH-----ATGDFDHYEVTIKNKNNFIQTKSIPKSENECVFVQLVPGRLYSVTVTTKSG 715
Cdd:smart00060    1 PSPPSNLRVTDVT-STSVTLSWEPppddgITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79


                    .
gi 332800999    716 Q 716
Cdd:smart00060   80 A 80

FN3

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

729-803

1.02e-03

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 39.91 E-value: 1.02e-03

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999    729 PEPVKDLTLRNRSTEDLHVTWS-----GANGDVDQYEIQLLFNDMKVFPpFHLVNTATEYRFTSLTPGRQYKILVLTISG 803
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEpppddGITGYIVGYRVEYREEGSEWKE-VNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

FN3

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

377-450

1.10e-03

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 39.52 E-value: 1.10e-03

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332800999    377 PLAVLQLRVKHANETSLSIMWQTPVAEWE-----KYIISLADRDLLLIHKSLSKDAKEFTFTDLVPGRKYMATVTSISG 450
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGItgyivGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

FN3

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

817-891

1.39e-03

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 39.52 E-value: 1.39e-03

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999    817 PSAVKNIHISPNGATdSLTVNWTP-----GGGDVDSYTVSAFRHSQKVDSQTIPKHVFEHTFHRLEAGEQYQIMIASVSG 891
Cdd:smart00060    1 PSPPSNLRVTDVTST-SVTLSWEPppddgITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

TpbA-like

cd14529

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

1770-1851

1.53e-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: 1.53e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1770 IRHFHYTVWPDHGVPETTQSLIQFVRTVRDYINRspgaGPTVVHCSAGVGRTGTFIALDRILQQLDSKDsvdiygAVHDL 1849
Cdd:cd14529    56 IDGVKYVNLPLSATRPTESDVQSFLLIMDLKLAP----GPVLIHCKHGKDRTGLVSALYRIVYGGSKEE------ANEDY 125


                  ..
gi 332800999 1850 RL 1851
Cdd:cd14529   126 RL 127

FN3

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

377-462

2.85e-03

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 38.63 E-value: 2.85e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999  377 PLAVLQLRVKHANETSLSIMWQTPV---AEWEKYIISL--ADRDLLLIHKSLSKDAKEFTFTDLVPGRKYMATVTSISGD 451
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYreKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|...
gi 332800999  452 L--KNSSSVKGRT 462
Cdd:cd00063    81 GesPPSESVTVTT 93

FN3

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

1083-1157

3.64e-03

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 38.36 E-value: 3.64e-03

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999   1083 PASVSHLRGSNrNTTDSLWFNWSPASGDFDFYELILYNP-NGTKKENWK----DKDLTEWRFQGLVPGRKYVLWVVTHSG 1157
Cdd:smart00060    1 PSPPSNLRVTD-VTSTSVTLSWEPPPDDGITGYIVGYRVeYREEGSEWKevnvTPSSTSYTLTGLKPGTEYEFRVRAVNG 79

PTP_PTPDC1

cd14506

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

1770-1872

4.07e-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: 4.07e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1770 IRHFHYTvWPDHGVPeTTQSLIQFVRTVRDYINRSpgaGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSvdiygAVHDL 1849
Cdd:cd14506    77 IYFYNFG-WKDYGVP-SLTTILDIVKVMAFALQEG---GKVAVHCHAGLGRTGVLIACYLVYALRMSADQ-----AIRLV 146

                          90       100
                  ....*....|....*....|...
gi 332800999 1850 RLHRVHMVQTECQYvylhQCVRD 1872
Cdd:cd14506   147 RSKRPNSIQTRGQV----LCVRE 165

COG4733

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

1081-1249

6.58e-03

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

Pssm-ID: 443767 [Multi-domain] Cd Length: 978 Bit Score: 41.47 E-value: 6.58e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1081 TVPASVSHLRGSNRNTTDSLWFNWSPASGDFDfYELILYNPNGtkkeNWKDK---DLTEWRFQGLVPGRKYV-LWVVTHS 1156
Cdd:COG4733   535 NVTTSESLSVVAQGTAVTTLTVSWDAPAGAVA-YEVEWRRDDG----NWVSVprtSGTSFEVPGIYAGDYEVrVRAINAL 609

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999 1157 GDLSNKVTAESRT------APSPPSlmSF-ADIANTSLAITWKGPPDwTDYNDFELQWLPR----DALTVFNPYNNRKSe 1225
Cdd:COG4733   610 GVSSAWAASSETTvtgktaPPPAPT--GLtATGGLGGITLSWSFPVD-ADTLRTEIRYSTTgdwaSATVAQALYPGNTY- 685

                         170       180
                  ....*....|....*....|....*.
gi 332800999 1226 grIVYGLRPGRSYQFNVKTV--SGDS 1249
Cdd:COG4733   686 --TLAGLKAGQTYYYRARAVdrSGNV 709

CDC14_C

cd14499

C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...

1779-1827

6.60e-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: 6.60e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 332800999 1779 PDHGVPeTTQSLIQFVRTVRdyinRSPGAgpTVVHCSAGVGRTGTFIAL 1827
Cdd:cd14499    88 PDGSTP-SDDIVKKFLDICE----NEKGA--IAVHCKAGLGRTGTLIAC 129

FN3

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

553-628

7.67e-03

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 37.21 E-value: 7.67e-03

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999    553 PSSVSGVTVNNSGRNdYLSVSWLLAPGD-----VDNYEVTLSHDGKVVQSLVIAKSVRECSFSSLTPGRLYTVTITTRSG 627
Cdd:smart00060    1 PSPPSNLRVTDVTST-SVTLSWEPPPDDgitgyIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79


                    .
gi 332800999    628 K 628
Cdd:smart00060   80 A 80

FN3

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

203-273

8.54e-03

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 37.21 E-value: 8.54e-03

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332800999    203 PSPVKDIGIS-TKANSLLISWSH-----GSGNVERYRLMLMDKGILVHGGVVDKHATSYAFHGLTPGYLYNLTVMTE 273
Cdd:smart00060    1 PSPPSNLRVTdVTSTSVTLSWEPppddgITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77

FN3

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

553-630

8.58e-03

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 37.48 E-value: 8.58e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332800999  553 PSSVSGVTVNNSGRnDYLSVSWLLAPGD---VDNYEVTLS--HDGKVVQSLVIAKSVRECSFSSLTPGRLYTVTITTRSG 627
Cdd:cd00063     1 PSPPTNLRVTDVTS-TSVTLSWTPPEDDggpITGYVVEYRekGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79


                  ...
gi 332800999  628 KYE 630
Cdd:cd00063    80 GGE 82

FN3