NCBI Conserved Domain Search

Fibronectin type 3 domain [General function prediction only];

200-744

1.94e-16

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 84.67 E-value: 1.94e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  200 SVTPEDTLSTPVEVTNTTNPSPVTGLSVVNGTTESLRIKWT-RPTDTRASDYTYRVTVTNVTGGVSWTESTSKDKTTFTA 278
Cdd:COG3401     30 GGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGgRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNT 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  279 TGLQPGDQYQLSVQSVTPEDTVSSPLEVTNTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRATNYTYIVTVTNVTGGVSS 358
Cdd:COG3401    110 GLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTS 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  359 TTVTSRGETTFKATGLQpgdqYLLSVQSVTPEDTWSTPVEVT-NTTNPSPVTGLTVVNGTTHSLRIEWTPPTDTRATNYT 437
Cdd:COG3401    190 TTLVDGGGDIEPGTTYY----YRVAATDTGGESAPSNEVSVTtPTTPPSAPTGLTATADTPGSVTLSWDPVTESDATGYR 265

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  438 YKVTVTnvaGGVSSTTITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEV----TSTTNPSPVTGLSVVNGTTQS 513
Cdd:COG3401    266 VYRSNS---GDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNESAPSNVvsvtTDLTPPAAPSGLTATAVGSSS 342

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  514 LTIEWTSPNDTTASNyiYNVTVTNVTGGVSWTESTSKGETTFTATGLQPGDQYQLSVQSVT---PEDTLSTPEQVTNTTN 590
Cdd:COG3401    343 ITLSWTASSDADVTG--YNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDaagNESAPSEEVSATTASA 420

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  591 PSPVTGLSVVNGTTQSLGIEWT-------SPTDTRASNYTYIVTVTNVTGGGRSTTVTSKGETAFTATGLQPGDQYQLSV 663
Cdd:COG3401    421 ASGESLTASVDAVPLTDVAGATaaasaasNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGS 500

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  664 QSVTPEGTLSTPVEVTSTTNPSPVTGLSVVNGT--------TQSLTIEWTRPTDTRASNYTYNVTVTNVTGGVSWTQSTS 735
Cdd:COG3401    501 GASSVTNSVSVIGASAAAAVGGAPDGTPNVTGAspvtvgasTGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITTLGGS 580


                   ....*....
gi 1822521637  736 KDETTFTAT 744
Cdd:COG3401    581 LLTTTSTNT 589

FN3 super family

cl27307

Fibronectin type 3 domain [General function prediction only];

27-368

1.78e-10

Fibronectin type 3 domain [General function prediction only];

The actual alignment was detected with superfamily member COG3401:

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 65.41 E-value: 1.78e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637   27 SQNVTDPSPVTGLSVVSRTTDSLRIEWTSPNDTRASNYTYNVTvTNVAGGVSSITTTgkNETTFTATGLQPGDQYLLSVR 106
Cdd:COG3401    227 TTPTTPPSAPTGLTATADTPGSVTLSWDPVTESDATGYRVYRS-NSGDGPFTKVATV--TTTSYTDTGLTNGTTYYYRVT 303

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  107 SVTPEDTLSTPVEV----TSTTNPSPVIGLSVVNGTTQSLWIEWTSPTDTRATNytYIVTVTNVTGGVSWTKSTNKDKTT 182
Cdd:COG3401    304 AVDAAGNESAPSNVvsvtTDLTPPAAPSGLTATAVGSSSITLSWTASSDADVTG--YNVYRSTSGGGTYTKIAETVTTTS 381

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  183 FTATGLQPGDQYQLSVRSVTPEDTLSTPVEVTNTTNPSPVTGLSVVNGTTEslrikWTRPTDTRASDYTYRVTVTNVTGG 262
Cdd:COG3401    382 YTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDA-----VPLTDVAGATAAASAASNPGVSAA 456

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  263 VSWTESTSKDKTTFTATGLQPGDQYQLSVQSVTPEDTVSSPLEVTNTTNPSPVTGLSVVNGTTQSLTiewtrPTDTRATN 342
Cdd:COG3401    457 VLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGA-----PDGTPNVT 531

                          330       340
                   ....*....|....*....|....*.
gi 1822521637  343 YTYIVTVTNVTGGVSSTTVTSRGETT 368
Cdd:COG3401    532 GASPVTVGASTGDVLITDLVSLTTSA 557

fn3

Fibronectin type III domain;

871-949

3.68e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 52.03 E-value: 3.68e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  871 SPVSGLTVVNRTTVSIEVTWAAPTDARAPEYTYRITLANVTRRGRGA-IDTGPGVTTFTVTNLVPGVEYELRLQSVTPAG 949
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNeITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80

fn3

Fibronectin type III domain;

778-853

6.82e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 51.26 E-value: 6.82e-08

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521637  778 SPVTGLSVVNSTTQSLRIEWTTPNNIRASNYTYNVTVTNVTDGASSTTIT-SKGETTFTVTGLQPGDQYRLSVRSVT 853
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITvPGTTTSVTLTGLKPGTEYEVRVQAVN 77

FN3 super family

cl21522

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

965-1041

1.82e-03

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

The actual alignment was detected with superfamily member pfam00041:

Pssm-ID: 473895 [Multi-domain] Cd Length: 85 Bit Score: 38.94 E-value: 1.82e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  965 AISDFRCSGSTGYMVEAKWSQP---NGQFSMFKaLTY---DGEQLISNLSLGKEERSLTVDNLQPGRTYTLRVVTESGNT 1038
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPpdgNGPITGYE-VEYrpkNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ...
gi 1822521637 1039 SSQ 1041
Cdd:pfam00041   81 EGP 83

Name

Accession

Description

Interval

E-value

PTPc

smart00194

Protein tyrosine phosphatase, catalytic domain;

1123-1381

2.54e-116

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 365.06 E-value: 2.54e-116

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  1123 GFAEEYQGLANVG-TNQSKEAFQVPDNKVKNRYTNIFPYDVARVKLdRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLP 1201
Cdd:smart00194    1 GLEEEFEKLDRLKpDDESCTVAAFPENRDKNRYKDVLPYDHTRVKL-KPPPGEGSDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  1202 NTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCL-YGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTI 1280
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLtYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTV 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  1281 TQFHFTSWPDHGVPKTTDKLLQFQRMMRDYlNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRM 1360
Cdd:smart00194  160 THYHYTNWPDHGVPESPESILDLIRAVRKS-QSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRS 238

                           250       260
                    ....*....|....*....|.
gi 1822521637  1361 SRTCMVQTENQYIFLHQCILD 1381
Cdd:smart00194  239 QRPGMVQTEEQYIFLYRAILE 259

R3-PTPc

cd14548

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

1153-1377

9.50e-112

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

Pssm-ID: 350396 [Multi-domain] Cd Length: 222 Bit Score: 350.89 E-value: 9.50e-112

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1153 RYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVK 1232
Cdd:cd14548      1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1233 CERYWPMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGcpEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLN 1312
Cdd:cd14548     81 CDHYWPFDQDPVYYGDITVTMLSESVLPDWTIREFKLERGD--EVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIK 158

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1822521637 1313 KNrAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1377
Cdd:cd14548    159 QE-KGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222

Y_phosphatase

pfam00102

Protein-tyrosine phosphatase;

1148-1381

7.27e-110

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 346.15 E-value: 7.27e-110

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1148 NKVKNRYTNIFPYDVARVKLdrQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVE 1227
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKL--TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1228 QNRVKCERYWPMDMS-SCLYGDIVVNIVSEET-SPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQR 1305
Cdd:pfam00102   79 KGREKCAQYWPEEEGeSLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1822521637 1306 MMRDYLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1381
Cdd:pfam00102  159 KVRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234

COG5599

Protein tyrosine phosphatase [Signal transduction mechanisms];

1136-1375

3.79e-43

Protein tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 444335 [Multi-domain] Cd Length: 282 Bit Score: 159.10 E-value: 3.79e-43

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1136 TNQSKEAFQVPDNKVKNRYTNIFPYDVARVkldrqpnSSSSDYINASY--MPGYHLdkaFIAAQGPLPNTVVDFWRMVWE 1213
Cdd:COG5599     30 SHNDPQYLQNINGSPLNRFRDIQPYKETAL-------RANLGYLNANYiqVIGNHR---YIATQYPLEEQLEDFFQMLFD 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1214 QKTKVIVMLTNCVE--QNRVKCERYWPMDMSsclYGDIVVNIVSEET---SPEWTTRKFNVKKTGC-PEPRTITQFHFTS 1287
Cdd:COG5599    100 NNTPVLVVLASDDEisKPKVKMPVYFRQDGE---YGKYEVSSELTESiqlRDGIEARTYVLTIKGTgQKKIEIPVLHVKN 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1288 WPDHGVPkTTDKLLQFQRMMRDYLNKNRA--GLPVVHCSAGVGRTGTLIALDYLLQRI--EKEAVVDVYGIVHNMRMSRT 1363
Cdd:COG5599    177 WPDHGAI-SAEALKNLADLIDKKEKIKDPdkLLPVVHCRAGVGRTGTLIACLALSKSInaLVQITLSVEEIVIDMRTSRN 255

                          250
                   ....*....|...
gi 1822521637 1364 C-MVQTENQYIFL 1375
Cdd:COG5599    256 GgMVQTSEQLDVL 268

PHA02738

hypothetical protein; Provisional

1148-1404

7.69e-42

hypothetical protein; Provisional

Pssm-ID: 222923 [Multi-domain] Cd Length: 320 Bit Score: 156.62 E-value: 7.69e-42

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1148 NKVKNRYTNIFPYDVARVKLDRQPNSSssDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVE 1227
Cdd:PHA02738    49 NRKLNRYLDAVCFDHSRVILPAERNRG--DYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKE 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1228 QNRVKCERYWP-MDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKtGCPEPRTITQFHFTSWPDHGVPKTTDKLLQF--- 1303
Cdd:PHA02738   127 NGREKCFPYWSdVEQGSIRFGKFKITTTQVETHPHYVKSTLLLTD-GTSATQTVTHFNFTAWPDHDVPKNTSEFLNFvle 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1304 ----QRMM---RDYLNKNRAGLP--VVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIF 1374
Cdd:PHA02738   206 vrqcQKELaqeSLQIGHNRLQPPpiVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFF 285

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1822521637 1375 LHQCI---LDVTGDKSIDEPIYENQADLIYENV 1404
Cdd:PHA02738   286 CYRAVkryVNLTVNKVSKKLIPNVQTVSFNKNL 318

FN3

Fibronectin type 3 domain [General function prediction only];

200-744

1.94e-16

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 84.67 E-value: 1.94e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  200 SVTPEDTLSTPVEVTNTTNPSPVTGLSVVNGTTESLRIKWT-RPTDTRASDYTYRVTVTNVTGGVSWTESTSKDKTTFTA 278
Cdd:COG3401     30 GGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGgRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNT 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  279 TGLQPGDQYQLSVQSVTPEDTVSSPLEVTNTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRATNYTYIVTVTNVTGGVSS 358
Cdd:COG3401    110 GLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTS 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  359 TTVTSRGETTFKATGLQpgdqYLLSVQSVTPEDTWSTPVEVT-NTTNPSPVTGLTVVNGTTHSLRIEWTPPTDTRATNYT 437
Cdd:COG3401    190 TTLVDGGGDIEPGTTYY----YRVAATDTGGESAPSNEVSVTtPTTPPSAPTGLTATADTPGSVTLSWDPVTESDATGYR 265

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  438 YKVTVTnvaGGVSSTTITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEV----TSTTNPSPVTGLSVVNGTTQS 513
Cdd:COG3401    266 VYRSNS---GDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNESAPSNVvsvtTDLTPPAAPSGLTATAVGSSS 342

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  514 LTIEWTSPNDTTASNyiYNVTVTNVTGGVSWTESTSKGETTFTATGLQPGDQYQLSVQSVT---PEDTLSTPEQVTNTTN 590
Cdd:COG3401    343 ITLSWTASSDADVTG--YNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDaagNESAPSEEVSATTASA 420

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  591 PSPVTGLSVVNGTTQSLGIEWT-------SPTDTRASNYTYIVTVTNVTGGGRSTTVTSKGETAFTATGLQPGDQYQLSV 663
Cdd:COG3401    421 ASGESLTASVDAVPLTDVAGATaaasaasNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGS 500

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  664 QSVTPEGTLSTPVEVTSTTNPSPVTGLSVVNGT--------TQSLTIEWTRPTDTRASNYTYNVTVTNVTGGVSWTQSTS 735
Cdd:COG3401    501 GASSVTNSVSVIGASAAAAVGGAPDGTPNVTGAspvtvgasTGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITTLGGS 580


                   ....*....
gi 1822521637  736 KDETTFTAT 744
Cdd:COG3401    581 LLTTTSTNT 589

FN3

Fibronectin type 3 domain [General function prediction only];

27-368

1.78e-10

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 65.41 E-value: 1.78e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637   27 SQNVTDPSPVTGLSVVSRTTDSLRIEWTSPNDTRASNYTYNVTvTNVAGGVSSITTTgkNETTFTATGLQPGDQYLLSVR 106
Cdd:COG3401    227 TTPTTPPSAPTGLTATADTPGSVTLSWDPVTESDATGYRVYRS-NSGDGPFTKVATV--TTTSYTDTGLTNGTTYYYRVT 303

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  107 SVTPEDTLSTPVEV----TSTTNPSPVIGLSVVNGTTQSLWIEWTSPTDTRATNytYIVTVTNVTGGVSWTKSTNKDKTT 182
Cdd:COG3401    304 AVDAAGNESAPSNVvsvtTDLTPPAAPSGLTATAVGSSSITLSWTASSDADVTG--YNVYRSTSGGGTYTKIAETVTTTS 381

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  183 FTATGLQPGDQYQLSVRSVTPEDTLSTPVEVTNTTNPSPVTGLSVVNGTTEslrikWTRPTDTRASDYTYRVTVTNVTGG 262
Cdd:COG3401    382 YTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDA-----VPLTDVAGATAAASAASNPGVSAA 456

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  263 VSWTESTSKDKTTFTATGLQPGDQYQLSVQSVTPEDTVSSPLEVTNTTNPSPVTGLSVVNGTTQSLTiewtrPTDTRATN 342
Cdd:COG3401    457 VLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGA-----PDGTPNVT 531

                          330       340
                   ....*....|....*....|....*.
gi 1822521637  343 YTYIVTVTNVTGGVSSTTVTSRGETT 368
Cdd:COG3401    532 GASPVTVGASTGDVLITDLVSLTTSA 557

FN3

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

498-574

3.91e-09

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: 54.93 E-value: 3.91e-09

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521637   498 PSPVTGLSVVNGTTQSLTIEWTSPNDTTASNYIYNVTVTNVTGGVSWTE-STSKGETTFTATGLQPGDQYQLSVQSVT 574
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEvNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

fn3

Fibronectin type III domain;

220-295

4.43e-09

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 54.73 E-value: 4.43e-09

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521637  220 SPVTGLSVVNGTTESLRIKWTRPTDTRASDYTYRVTVTNVTGGVSWTEST-SKDKTTFTATGLQPGDQYQLSVQSVT 295
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITvPGTTTSVTLTGLKPGTEYEVRVQAVN 77

fn3

Fibronectin type III domain;

871-949

3.68e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 52.03 E-value: 3.68e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  871 SPVSGLTVVNRTTVSIEVTWAAPTDARAPEYTYRITLANVTRRGRGA-IDTGPGVTTFTVTNLVPGVEYELRLQSVTPAG 949
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNeITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80

FN3

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

870-958

4.65e-08

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 52.11 E-value: 4.65e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  870 PSPVSGLTVVNRTTVSIEVTWAAPTDARAPEYTYRITLANVTRRGRGAIDTGPG-VTTFTVTNLVPGVEYELRLQSVTPA 948
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGsETSYTLTGLKPGTEYEFRVRAVNGG 80

                           90
                   ....*....|..
gi 1822521637  949 GT--RSSPETVR 958
Cdd:cd00063     81 GEspPSESVTVT 92

FN3

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

126-202

4.82e-08

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 51.85 E-value: 4.82e-08

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521637   126 PSPVIGLSVVNGTTQSLWIEWTSPTDTRATNYTYIVTVTNVTGGVSWTK-STNKDKTTFTATGLQPGDQYQLSVRSVT 202
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEvNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

FN3

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

870-949

5.80e-08

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 51.46 E-value: 5.80e-08

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637   870 PSPVSGLTVVNRTTVSIEVTWAAPTDARAPEYTYRITLANVTRRGRGA-IDTGPGVTTFTVTNLVPGVEYELRLQSVTPA 948
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKeVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                    .
gi 1822521637   949 G 949
Cdd:smart00060   81 G 81

fn3

Fibronectin type III domain;

778-853

6.82e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 51.26 E-value: 6.82e-08

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521637  778 SPVTGLSVVNSTTQSLRIEWTTPNNIRASNYTYNVTVTNVTDGASSTTIT-SKGETTFTVTGLQPGDQYRLSVRSVT 853
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITvPGTTTSVTLTGLKPGTEYEVRVQAVN 77

FN3

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

33-124

7.72e-08

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 51.34 E-value: 7.72e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637   33 PSPVTGLSVVSRTTDSLRIEWTSPNDTRASNYTYNVTVTNV-AGGVSSITTTGKNETTFTATGLQPGDQYLLSVRSVTpE 111
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKgSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN-G 79

                           90
                   ....*....|...
gi 1822521637  112 DTLSTPVEVTSTT 124
Cdd:cd00063     80 GGESPPSESVTVT 92

FN3

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

777-853

1.03e-07

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 50.69 E-value: 1.03e-07

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521637   777 PSPVTGLSVVNSTTQSLRIEWTTPNNIRASNYTYNVTVTNVTDGASSTTITSKG-ETTFTVTGLQPGDQYRLSVRSVT 853
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPsSTSYTLTGLKPGTEYEFRVRAVN 78

FN3

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

405-496

1.37e-07

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 50.57 E-value: 1.37e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  405 PSPVTGLTVVNGTTHSLRIEWTPPTDTRATNYTYKVTVTNVAGGVSST-TITNKGETAFTATGLQPGDQYQLSVQSVTpE 483
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEvEVTPGSETSYTLTGLKPGTEYEFRVRAVN-G 79

                           90
                   ....*....|...
gi 1822521637  484 DTLSTPVEVTSTT 496
Cdd:cd00063     80 GGESPPSESVTVT 92

FN3

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

777-866

1.77e-07

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 50.57 E-value: 1.77e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  777 PSPVTGLSVVNSTTQSLRIEWTTPNNIRASNYTYNVTVTNVTDGASST-TITSKGETTFTVTGLQPGDQYRLSVRSVTpE 855
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEvEVTPGSETSYTLTGLKPGTEYEFRVRAVN-G 79

                           90
                   ....*....|.
gi 1822521637  856 DTWSTPAQVTS 866
Cdd:cd00063     80 GGESPPSESVT 90

fn3

Fibronectin type III domain;

34-109

1.51e-06

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 47.41 E-value: 1.51e-06

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521637   34 SPVTGLSVVSRTTDSLRIEWTSPNDTRASNYTYNVTVTNVAGGVSSIT-TTGKNETTFTATGLQPGDQYLLSVRSVT 109
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEiTVPGTTTSVTLTGLKPGTEYEVRVQAVN 77

fn3

Fibronectin type III domain;

965-1041

1.82e-03

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 38.94 E-value: 1.82e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  965 AISDFRCSGSTGYMVEAKWSQP---NGQFSMFKaLTY---DGEQLISNLSLGKEERSLTVDNLQPGRTYTLRVVTESGNT 1038
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPpdgNGPITGYE-VEYrpkNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ...
gi 1822521637 1039 SSQ 1041
Cdd:pfam00041   81 EGP 83

Name

Accession

Description

Interval

E-value

PTPc

smart00194

Protein tyrosine phosphatase, catalytic domain;

1123-1381

2.54e-116

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 365.06 E-value: 2.54e-116

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  1123 GFAEEYQGLANVG-TNQSKEAFQVPDNKVKNRYTNIFPYDVARVKLdRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLP 1201
Cdd:smart00194    1 GLEEEFEKLDRLKpDDESCTVAAFPENRDKNRYKDVLPYDHTRVKL-KPPPGEGSDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  1202 NTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCL-YGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTI 1280
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLtYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTV 159

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  1281 TQFHFTSWPDHGVPKTTDKLLQFQRMMRDYlNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRM 1360
Cdd:smart00194  160 THYHYTNWPDHGVPESPESILDLIRAVRKS-QSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRS 238

                           250       260
                    ....*....|....*....|.
gi 1822521637  1361 SRTCMVQTENQYIFLHQCILD 1381
Cdd:smart00194  239 QRPGMVQTEEQYIFLYRAILE 259

R3-PTPc

cd14548

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

1153-1377

9.50e-112

Pssm-ID: 350396 [Multi-domain] Cd Length: 222 Bit Score: 350.89 E-value: 9.50e-112

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1153 RYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVK 1232
Cdd:cd14548      1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1233 CERYWPMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGcpEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLN 1312
Cdd:cd14548     81 CDHYWPFDQDPVYYGDITVTMLSESVLPDWTIREFKLERGD--EVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYIK 158

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1822521637 1313 KNrAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1377
Cdd:cd14548    159 QE-KGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222

Y_phosphatase

pfam00102

Protein-tyrosine phosphatase;

1148-1381

7.27e-110

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 346.15 E-value: 7.27e-110

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1148 NKVKNRYTNIFPYDVARVKLdrQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVE 1227
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKL--TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1228 QNRVKCERYWPMDMS-SCLYGDIVVNIVSEET-SPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQR 1305
Cdd:pfam00102   79 KGREKCAQYWPEEEGeSLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1822521637 1306 MMRDYLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1381
Cdd:pfam00102  159 KVRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234

R-PTPc-J

cd14615

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

1152-1381

1.49e-108

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

Pssm-ID: 350463 [Multi-domain] Cd Length: 229 Bit Score: 342.57 E-value: 1.49e-108

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1152 NRYTNIFPYDVARVKLDrQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRV 1231
Cdd:cd14615      1 NRYNNVLPYDISRVKLS-VQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1232 KCERYWPMDMSSClYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYL 1311
Cdd:cd14615     80 KCEEYWPSKQKKD-YGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREYM 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1822521637 1312 NKNRAGLPV-VHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1381
Cdd:cd14615    159 KQNPPNSPIlVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229

R-PTPc-H

cd14619

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

1152-1381

1.49e-105

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

Pssm-ID: 350467 [Multi-domain] Cd Length: 233 Bit Score: 334.55 E-value: 1.49e-105

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1152 NRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRV 1231
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1232 KCERYWPMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYL 1311
Cdd:cd14619     81 KCEHYWPLDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQWL 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1822521637 1312 NKNRA-GLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1381
Cdd:cd14619    161 DQTMSgGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILD 231

PTPc

cd00047

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

1178-1377

2.35e-97

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

Pssm-ID: 350343 [Multi-domain] Cd Length: 200 Bit Score: 310.37 E-value: 2.35e-97

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1178 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCL-YGDIVVNIVSE 1256
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLeYGDITVTLVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1257 ETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKNRaGLPVVHCSAGVGRTGTLIAL 1336
Cdd:cd00047     81 EELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARKPN-GPIVVHCSAGVGRTGTFIAI 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1822521637 1337 DYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1377
Cdd:cd00047    160 DILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200

R-PTPc-B

cd14617

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

1152-1377

9.35e-96

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

Pssm-ID: 350465 [Multi-domain] Cd Length: 228 Bit Score: 307.23 E-value: 9.35e-96

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1152 NRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRV 1231
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1232 KCERYWPMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVkktgCPE-----PRTITQFHFTSWPDHGVPKTTDKLLQFQRM 1306
Cdd:cd14617     81 KCDHYWPADQDSLYYGDLIVQMLSESVLPEWTIREFKI----CSEeqldaPRLVRHFHYTVWPDHGVPETTQSLIQFVRT 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1822521637 1307 MRDYLNK-NRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1377
Cdd:cd14617    157 VRDYINRtPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228

R-PTPc-O

cd14614

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

1139-1380

4.09e-92

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

Pssm-ID: 350462 [Multi-domain] Cd Length: 245 Bit Score: 297.57 E-value: 4.09e-92

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1139 SKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKV 1218
Cdd:cd14614      3 PHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQI 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1219 IVMLTNCVEQNRVKCERYWPMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGcpEPRTITQFHFTSWPDHGVP--KT 1296
Cdd:cd14614     83 IVMLTQCNEKRRVKCDHYWPFTEEPVAYGDITVEMLSEEEQPDWAIREFRVSYAD--EVQDVMHFNYTAWPDHGVPtaNA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1297 TDKLLQFQRMMRDYLNKnRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLH 1376
Cdd:cd14614    161 AESILQFVQMVRQQAVK-SKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIH 239


                   ....
gi 1822521637 1377 QCIL 1380
Cdd:cd14614    240 QCVQ 243

R-PTPc-LAR-1

cd14553

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

1148-1381

1.86e-91

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

Pssm-ID: 350401 [Multi-domain] Cd Length: 238 Bit Score: 295.46 E-value: 1.86e-91

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1148 NKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVE 1227
Cdd:cd14553      3 NKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1228 QNRVKCERYWPMDMSScLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMM 1307
Cdd:cd14553     83 RSRVKCDQYWPTRGTE-TYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRV 161

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1822521637 1308 RdYLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1381
Cdd:cd14553    162 K-ACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLE 234

R-PTPc-V

cd14618

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

1152-1380

1.72e-86

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

Pssm-ID: 350466 [Multi-domain] Cd Length: 230 Bit Score: 281.45 E-value: 1.72e-86

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1152 NRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRV 1231
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1232 KCERYWPMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYL 1311
Cdd:cd14618     81 LCDHYWPSESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVREHV 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1312 NKNRAGLPV-VHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCIL 1380
Cdd:cd14618    161 QATKGKGPTlVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230

R5-PTPc-1

cd14549

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

1178-1376

1.37e-81

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

Pssm-ID: 350397 [Multi-domain] Cd Length: 204 Bit Score: 266.52 E-value: 1.37e-81

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1178 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSClYGDIVVNIVSEE 1257
Cdd:cd14549      1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTET-YGNIQVTLLSTE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1258 TSPEWTTRKFNVK------KTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRmMRDYLNKNRAGLPVVHCSAGVGRTG 1331
Cdd:cd14549     80 VLATYTVRTFSLKnlklkkVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVR-KSSAANPPGAGPIVVHCSAGVGRTG 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1822521637 1332 TLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLH 1376
Cdd:cd14549    159 TYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203

R-PTPc-Q

cd14616

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

1152-1377

4.21e-80

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

Pssm-ID: 350464 [Multi-domain] Cd Length: 224 Bit Score: 262.92 E-value: 4.21e-80

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1152 NRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRV 1231
Cdd:cd14616      1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1232 KCERYWPMDMSS-CLYGDIVVNIVSEETSPEWTTRKFNVKKTGcpEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRdy 1310
Cdd:cd14616     81 RCHQYWPEDNKPvTVFGDIVITKLMEDVQIDWTIRDLKIERHG--DYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVR-- 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1311 lnKNRAGLP---VVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1377
Cdd:cd14616    157 --ASRAHDNtpmIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224

PTPc-N9

cd14543

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

1123-1376

1.28e-79

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

Pssm-ID: 350391 [Multi-domain] Cd Length: 271 Bit Score: 263.46 E-value: 1.28e-79

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1123 GFAEEYQGLAN---VGTNQSKEAfqvPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGP 1199
Cdd:cd14543      4 GIYEEYEDIRReppAGTFLCSLA---PANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1200 LPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCL-YGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPR 1278
Cdd:cd14543     81 LPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLrYGDLTVTNLSVENKEHYKKTTLEIHNTETDESR 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1279 TITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLN----------KNRAGLP--VVHCSAGVGRTGTLIALDYLLQRIEKE 1346
Cdd:cd14543    161 QVTHFQFTSWPDFGVPSSAAALLDFLGEVRQQQAlavkamgdrwKGHPPGPpiVVHCSAGIGRTGTFCTLDICLSQLEDV 240

                          250       260       270
                   ....*....|....*....|....*....|
gi 1822521637 1347 AVVDVYGIVHNMRMSRTCMVQTENQYIFLH 1376
Cdd:cd14543    241 GTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270

R-PTPc-T-1

cd14630

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

1147-1381

4.35e-76

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

Pssm-ID: 350478 [Multi-domain] Cd Length: 237 Bit Score: 252.25 E-value: 4.35e-76

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1147 DNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCV 1226
Cdd:cd14630      2 ENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1227 EQNRVKCERYWPMDMSscLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRM 1306
Cdd:cd14630     82 EVGRVKCVRYWPDDTE--VYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVRQ 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1822521637 1307 MRdYLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1381
Cdd:cd14630    160 VK-FLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILE 233

R-PTPc-F-1

cd14626

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

1107-1381

4.09e-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: 251.11 E-value: 4.09e-75

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1107 SEYKSYYQRKHADTDIGFAEEYQGLaNVGTNQSKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPG 1186
Cdd:cd14626      1 SDLADNIERLKANDGLKFSQEYESI-DPGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1187 YHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSClYGDIVVNIVSEETSPEWTTRK 1266
Cdd:cd14626     80 YRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTET-YGMIQVTLLDTVELATYSVRT 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1267 FNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDyLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKE 1346
Cdd:cd14626    159 FALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKA-CNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHE 237

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1822521637 1347 AVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1381
Cdd:cd14626    238 KTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLE 272

PTPc-KIM

cd14547

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

1152-1377

6.26e-74

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

Pssm-ID: 350395 [Multi-domain] Cd Length: 224 Bit Score: 245.38 E-value: 6.26e-74

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1152 NRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGY-HLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEqNR 1230
Cdd:cd14547      1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGYdGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTE-AK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1231 VKCERYWPMDMSScLYGDIVVNIVSEETSPEWTTRKFNVKKTGcpEPRTITQFHFTSWPDHGVPKTTDKLLQFQR-MMRD 1309
Cdd:cd14547     80 EKCAQYWPEEENE-TYGDFEVTVQSVKETDGYTVRKLTLKYGG--EKRYLKHYWYTSWPDHKTPEAAQPLLSLVQeVEEA 156

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521637 1310 YLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1377
Cdd:cd14547    157 RQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224

R-PTPc-M-1

cd14633

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

1123-1381

1.02e-73

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

Pssm-ID: 350481 [Multi-domain] Cd Length: 273 Bit Score: 246.88 E-value: 1.02e-73

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1123 GFAEEYQGLANvGTNQSKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPN 1202
Cdd:cd14633     16 GFKEEYESFFE-GQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYHRPNHYIATQGPMQE 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1203 TVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSscLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQ 1282
Cdd:cd14633     95 TIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTE--IYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQ 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1283 FHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKNrAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSR 1362
Cdd:cd14633    173 FHFTGWPDHGVPYHATGLLGFVRQVKSKSPPN-AGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRR 251

                          250
                   ....*....|....*....
gi 1822521637 1363 TCMVQTENQYIFLHQCILD 1381
Cdd:cd14633    252 VNMVQTEEQYVFIHDAILE 270

R-PTPc-A-1

cd14621

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

1101-1381

5.19e-73

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

Pssm-ID: 350469 [Multi-domain] Cd Length: 296 Bit Score: 245.70 E-value: 5.19e-73

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1101 FKPIPVSEYKSYYQRKHADTDIGFAEEYQGLANVGTNQSKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYIN 1180
Cdd:cd14621      5 YPPLPVDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYIN 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1181 ASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPmDMSSCLYGDIVVNIVSEETSP 1260
Cdd:cd14621     85 ASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWP-DQGCWTYGNIRVSVEDVTVLV 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1261 EWTTRKFNVKK----TGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDyLNKNRAGLPVVHCSAGVGRTGTLIAL 1336
Cdd:cd14621    164 DYTVRKFCIQQvgdvTNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKN-CNPQYAGAIVVHCSAGVGRTGTFIVI 242

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1822521637 1337 DYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1381
Cdd:cd14621    243 DAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLE 287

R-PTPc-S-1

cd14625

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

1103-1384

1.68e-72

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

Pssm-ID: 350473 [Multi-domain] Cd Length: 282 Bit Score: 243.85 E-value: 1.68e-72

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1103 PIPVSEYKSYYQRKHADTDIGFAEEYQGLaNVGTNQSKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINAS 1182
Cdd:cd14625      3 PIPISELAEHTERLKANDNLKLSQEYESI-DPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINAN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1183 YMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPmDMSSCLYGDIVVNIVSEETSPEW 1262
Cdd:cd14625     82 YIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWP-SRGTETYGMIQVTLLDTIELATF 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1263 TTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDyLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQR 1342
Cdd:cd14625    161 CVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKT-CNPPDAGPIVVHCSAGVGRTGCFIVIDAMLER 239

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1822521637 1343 IEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILDVTG 1384
Cdd:cd14625    240 IKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAVA 281

R-PTPc-G-1

cd17667

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

1124-1381

2.87e-72

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

Pssm-ID: 350505 [Multi-domain] Cd Length: 274 Bit Score: 242.63 E-value: 2.87e-72

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1124 FAEEYQGL--ANVGTNQSKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQP--NSSSSDYINASYMPGYHLDKAFIAAQGP 1199
Cdd:cd17667      1 FSEDFEEVqrCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPgkDSKHSDYINANYVDGYNKAKAYIATQGP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1200 LPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSScLYGDIVVNIVSEETSPEWTTRKFNVKKT------- 1272
Cdd:cd17667     81 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSE-EYGNIIVTLKSTKIHACYTVRRFSIRNTkvkkgqk 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1273 ----GCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRmmrdylNKNRAGLP-----VVHCSAGVGRTGTLIALDYLLQRI 1343
Cdd:cd17667    160 gnpkGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVR------RSSAARTPemgpvLVHCSAGVGRTGTYIVIDSMLQQI 233

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1822521637 1344 EKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1381
Cdd:cd17667    234 KDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLE 271

R-PTP-LAR-2

cd14554

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

1145-1380

3.03e-71

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

Pssm-ID: 350402 [Multi-domain] Cd Length: 238 Bit Score: 238.19 E-value: 3.03e-71

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1145 VPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTN 1224
Cdd:cd14554      3 LPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTK 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1225 CVEQNRVKCERYWPMDmSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQF- 1303
Cdd:cd14554     83 LREMGREKCHQYWPAE-RSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFi 161

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521637 1304 QRMMRDYLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCIL 1380
Cdd:cd14554    162 GQVHKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRAAL 238

R-PTPc-C-1

cd14557

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

1178-1377

4.18e-71

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

Pssm-ID: 350405 [Multi-domain] Cd Length: 201 Bit Score: 236.26 E-value: 4.18e-71

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1178 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWP-MDMSSCLYGDIVVNIVSE 1256
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPsMEEGSRAFGDVVVKINEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1257 ETSPEWTTRKFNV--KKTGCPEpRTITQFHFTSWPDHGVPKTTDKLLQFQRMMrDYLNKNRAGLPVVHCSAGVGRTGTLI 1334
Cdd:cd14557     81 KICPDYIIRKLNInnKKEKGSG-REVTHIQFTSWPDHGVPEDPHLLLKLRRRV-NAFNNFFSGPIVVHCSAGVGRTGTYI 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1822521637 1335 ALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1377
Cdd:cd14557    159 GIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201

R-PTPc-D-1

cd14624

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

1103-1381

4.32e-71

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

Pssm-ID: 350472 [Multi-domain] Cd Length: 284 Bit Score: 239.63 E-value: 4.32e-71

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1103 PIPVSEYKSYYQRKHADTDIGFAEEYQGLaNVGTNQSKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINAS 1182
Cdd:cd14624      3 PIPILELADHIERLKANDNLKFSQEYESI-DPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINAN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1183 YMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPmDMSSCLYGDIVVNIVSEETSPEW 1262
Cdd:cd14624     82 YIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWP-SRGTETYGLIQVTLLDTVELATY 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1263 TTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDyLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQR 1342
Cdd:cd14624    161 CVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVKT-CNPPDAGPMVVHCSAGVGRTGCFIVIDAMLER 239

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1822521637 1343 IEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1381
Cdd:cd14624    240 IKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLE 278

R-PTPc-typeIIb-1

cd14555

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

1178-1381

8.88e-71

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

Pssm-ID: 350403 [Multi-domain] Cd Length: 204 Bit Score: 235.58 E-value: 8.88e-71

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1178 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDmsSCLYGDIVVNIVSEE 1257
Cdd:cd14555      1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDD--TEVYGDIKVTLVETE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1258 TSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRdYLNKNRAGLPVVHCSAGVGRTGTLIALD 1337
Cdd:cd14555     79 PLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVK-ASNPPSAGPIVVHCSAGAGRTGCYIVID 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1822521637 1338 YLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1381
Cdd:cd14555    158 IMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILE 201

PTPc-N11_6

cd14544

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

1148-1379

8.30e-69

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

Pssm-ID: 350392 [Multi-domain] Cd Length: 251 Bit Score: 231.97 E-value: 8.30e-69

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1148 NKVKNRYTNIFPYDVARVKL-DRQPNSSSSDYINASYM-----PGYHLD--KAFIAAQGPLPNTVVDFWRMVWEQKTKVI 1219
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILkDRDPNVPGSDYINANYIrneneGPTTDEnaKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1220 VMLTNCVEQNRVKCERYWPMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEP-RTITQFHFTSWPDHGVPKTTD 1298
Cdd:cd14544     81 VMTTKEVERGKNKCVRYWPDEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDPiREIWHYQYLSWPDHGVPSDPG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1299 KLLQF-QRMMRDYLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAV---VDVYGIVHNMRMSRTCMVQTENQYIF 1374
Cdd:cd14544    161 GVLNFlEDVNQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQRSGMVQTEAQYKF 240


                   ....*
gi 1822521637 1375 LHQCI 1379
Cdd:cd14544    241 IYVAV 245

R-PTPc-E-1

cd14620

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

1154-1381

1.08e-68

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

Pssm-ID: 350468 [Multi-domain] Cd Length: 229 Bit Score: 230.60 E-value: 1.08e-68

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1154 YTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKC 1233
Cdd:cd14620      1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1234 ERYWPmDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKT---GCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDy 1310
Cdd:cd14620     81 YQYWP-DQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQPQlpdGCKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKS- 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1822521637 1311 LNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1381
Cdd:cd14620    159 VNPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229

PTP_fungal

cd18533

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

1178-1377

2.29e-66

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

Pssm-ID: 350509 [Multi-domain] Cd Length: 212 Bit Score: 223.28 E-value: 2.29e-66

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1178 YINASYM-PGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCLYGDIVVNIVSE 1256
Cdd:cd18533      1 YINASYItLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEYGDLTVELVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1257 ET--SPEWTTRKFNVKKTGCPePRTITQFHFTSWPDHGVPKTTDKLLQfqrMMR--DYLNKN-RAGLP-VVHCSAGVGRT 1330
Cdd:cd18533     81 EEndDGGFIVREFELSKEDGK-VKKVYHIQYKSWPDFGVPDSPEDLLT---LIKlkRELNDSaSLDPPiIVHCSAGVGRT 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1822521637 1331 GTLIALDYLLQRIEKEAVVD---------VYGIVHNMRMSRTCMVQTENQYIFLHQ 1377
Cdd:cd18533    157 GTFIALDSLLDELKRGLSDSqdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212

R-PTPc-K-1

cd14631

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

1164-1381

3.13e-66

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

Pssm-ID: 350479 [Multi-domain] Cd Length: 218 Bit Score: 223.36 E-value: 3.13e-66

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1164 RVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSs 1243
Cdd:cd14631      1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTE- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1244 cLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRdYLNKNRAGLPVVHC 1323
Cdd:cd14631     80 -VYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVK-LSNPPSAGPIVVHC 157

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521637 1324 SAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1381
Cdd:cd14631    158 SAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILE 215

PTPc-N18

cd14603

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

1139-1379

4.38e-66

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

Pssm-ID: 350451 [Multi-domain] Cd Length: 266 Bit Score: 224.70 E-value: 4.38e-66

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1139 SKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKV 1218
Cdd:cd14603     21 STVAGGRKENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKV 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1219 IVMLTNCVEQNRVKCERYWPMDMSSCLYGDIVVNIVSEE-TSPEWTTRKFNVkkTGCPEPRTITQFHFTSWPDHGVPKTT 1297
Cdd:cd14603    101 ILMACREIEMGKKKCERYWAQEQEPLQTGPFTITLVKEKrLNEEVILRTLKV--TFQKESRSVSHFQYMAWPDHGIPDSP 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1298 DKLLQFQRMMRDYLNKNRAGLpVVHCSAGVGRTGTLIALDY-----LLQRIEKEavVDVYGIVHNMRMSRTCMVQTENQY 1372
Cdd:cd14603    179 DCMLAMIELARRLQGSGPEPL-CVHCSAGCGRTGVICTVDYvrqllLTQRIPPD--FSIFDVVLEMRKQRPAAVQTEEQY 255


                   ....*..
gi 1822521637 1373 IFLHQCI 1379
Cdd:cd14603    256 EFLYHTV 262

R-PTPc-A-E-1

cd14551

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

1178-1377

6.81e-66

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

Pssm-ID: 350399 [Multi-domain] Cd Length: 202 Bit Score: 221.71 E-value: 6.81e-66

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1178 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPmDMSSCLYGDIVVNIVSEE 1257
Cdd:cd14551      1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWP-DQGCWTYGNLRVRVEDTV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1258 TSPEWTTRKFNVKK----TGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDyLNKNRAGLPVVHCSAGVGRTGTL 1333
Cdd:cd14551     80 VLVDYTTRKFCIQKvnrgIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKS-ANPPRAGPIVVHCSAGVGRTGTF 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1822521637 1334 IALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1377
Cdd:cd14551    159 IVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202

PTPc-N13

cd14597

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

1147-1382

7.29e-66

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

Pssm-ID: 350445 [Multi-domain] Cd Length: 234 Bit Score: 222.78 E-value: 7.29e-66

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1147 DNKVKNRYTNIFPYDVARVKLdrqpnSSSSDYINASY--MPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTN 1224
Cdd:cd14597      2 ENRKKNRYKNILPYDTTRVPL-----GDEGGYINASFikMPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQ 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1225 CVEQNRVKCERYWPMDMSSCLYGD--IVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQ 1302
Cdd:cd14597     77 EVEGGKIKCQRYWPEILGKTTMVDnrLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLLT 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1303 FQRMMRdylNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILDV 1382
Cdd:cd14597    157 FISYMR---HIHKSGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVILYV 233

PTPc-N22_18_12

cd14542

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

1178-1377

9.66e-66

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: 221.14 E-value: 9.66e-66

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1178 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCL-YGDIVVNIVSE 1256
Cdd:cd14542      1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLqFGPFKISLEKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1257 E-TSPEWTTRKFNVKKTGcpEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYlnKNRAGLPV-VHCSAGVGRTGTLI 1334
Cdd:cd14542     81 KrVGPDFLIRTLKVTFQK--ESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDY--QGSEDVPIcVHCSAGCGRTGTIC 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1822521637 1335 ALDY---LLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1377
Cdd:cd14542    157 AIDYvwnLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202

PTPc-N20_13

cd14538

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

1178-1382

4.18e-65

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

Pssm-ID: 350386 [Multi-domain] Cd Length: 207 Bit Score: 219.55 E-value: 4.18e-65

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1178 YINASYM------PGYHldkaFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWP--MDMSSCLYGDI 1249
Cdd:cd14538      1 YINASHIripvggDTYH----YIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPdsLNKPLICGGRL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1250 VVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYlnkNRAGLPVVHCSAGVGR 1329
Cdd:cd14538     77 EVSLEKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRI---HNSGPIVVHCSAGIGR 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1822521637 1330 TGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILDV 1382
Cdd:cd14538    154 TGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEV 206

R-PTPc-U-1

cd14632

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

1178-1381

6.83e-65

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

Pssm-ID: 350480 [Multi-domain] Cd Length: 205 Bit Score: 218.77 E-value: 6.83e-65

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1178 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDmsSCLYGDIVVNIVSEE 1257
Cdd:cd14632      1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDD--SDTYGDIKITLLKTE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1258 TSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKNrAGLPVVHCSAGVGRTGTLIALD 1337
Cdd:cd14632     79 TLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPPD-AGPVVVHCSAGAGRTGCYIVLD 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1822521637 1338 YLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1381
Cdd:cd14632    158 VMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILE 201

R-PTP-S-2

cd14627

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

1104-1384

2.48e-62

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

Pssm-ID: 350475 [Multi-domain] Cd Length: 290 Bit Score: 214.98 E-value: 2.48e-62

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1104 IPVSEYKSYYQR----KHADTDIGFAEEYQGLANVGTNQSKE-AFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDY 1178
Cdd:cd14627      4 VPARNLYSYIQKlaqvEVGEHVTGMELEFKRLANSKAHTSRFiSANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDY 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1179 INASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSScLYGDIVVNIVSEET 1258
Cdd:cd14627     84 INASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPAERSA-RYQYFVVDPMAEYN 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1259 SPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKNRAGLPV-VHCSAGVGRTGTLIALD 1337
Cdd:cd14627    163 MPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPIsVHCSAGVGRTGVFITLS 242

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1822521637 1338 YLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILDVTG 1384
Cdd:cd14627    243 IVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYLG 289

PTPc-N1_2

cd14545

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

1151-1374

4.51e-62

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

Pssm-ID: 350393 [Multi-domain] Cd Length: 231 Bit Score: 211.87 E-value: 4.51e-62

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1151 KNRYTNIFPYDVARVKLdrqpNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNR 1230
Cdd:cd14545      3 RYRDRDPYDHDRSRVKL----KQGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1231 VKCERYWPMDMSS---CLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMM 1307
Cdd:cd14545     79 IKCAQYWPQGEGNamiFEDTGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQKV 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1822521637 1308 RDY--LNKNrAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAV--VDVYGIVHNMRMSRTCMVQTENQYIF 1374
Cdd:cd14545    159 RESgsLSSD-VGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRF 228

PTPc-N3_4

cd14541

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

1177-1382

5.27e-62

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

Pssm-ID: 350389 [Multi-domain] Cd Length: 212 Bit Score: 210.65 E-value: 5.27e-62

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1177 DYINASY----MPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCLYGDIVVN 1252
Cdd:cd14541      1 DYINANYvnmeIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETMQFGNLQIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1253 IVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRdylnKNRAGL--P-VVHCSAGVGR 1329
Cdd:cd14541     81 CVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVR----QNRVGMvePtVVHCSAGIGR 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1822521637 1330 TGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILDV 1382
Cdd:cd14541    157 TGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILRV 209

PTPc-N12

cd14604

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

1106-1379

8.48e-62

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

Pssm-ID: 350452 [Multi-domain] Cd Length: 297 Bit Score: 213.64 E-value: 8.48e-62

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1106 VSEYKSYYQRKHADTDiGFAEEYQGLANVGTNQSKEAF------QVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYI 1179
Cdd:cd14604     10 IERVQAMKSTDHNGED-NFASDFMRLRRLSTKYRTEKIyptatgEKEENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYI 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1180 NASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCL-YGDIVVNIVSEET 1258
Cdd:cd14604     89 NANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLYGEEPMtFGPFRISCEAEQA 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1259 SPEWTTRKFNVKKTGcpEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYlnKNRAGLPV-VHCSAGVGRTGTLIALD 1337
Cdd:cd14604    169 RTDYFIRTLLLEFQN--ETRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKY--QEHEDVPIcIHCSAGCGRTGAICAID 244

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1822521637 1338 Y---LLQ--RIEKEavVDVYGIVHNMRMSRTCMVQTENQYIFLHQCI 1379
Cdd:cd14604    245 YtwnLLKagKIPEE--FNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 289

R-PTPc-Z-1

cd17668

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

1178-1380

9.44e-62

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

Pssm-ID: 350506 [Multi-domain] Cd Length: 209 Bit Score: 209.83 E-value: 9.44e-62

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1178 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSScLYGDIVVNIVSEE 1257
Cdd:cd17668      1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSE-EYGNFLVTQKSVQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1258 TSPEWTTRKFNVKKT--------GCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRmMRDYLNKNRAGLPVVHCSAGVGR 1329
Cdd:cd17668     80 VLAYYTVRNFTLRNTkikkgsqkGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVR-KASYAKRHAVGPVVVHCSAGVGR 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1822521637 1330 TGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCIL 1380
Cdd:cd17668    159 TGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209

R-PTP-D-2

cd14628

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

1104-1384

3.05e-61

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

Pssm-ID: 350476 [Multi-domain] Cd Length: 292 Bit Score: 211.90 E-value: 3.05e-61

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1104 IPVSEYKSYYQR----KHADTDIGFAEEYQGLANVGTNQSKE-AFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDY 1178
Cdd:cd14628      3 VPARNLYAYIQKltqiETGENVTGMELEFKRLASSKAHTSRFiSANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDY 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1179 INASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSScLYGDIVVNIVSEET 1258
Cdd:cd14628     83 INASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSA-RYQYFVVDPMAEYN 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1259 SPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKNRAGLPV-VHCSAGVGRTGTLIALD 1337
Cdd:cd14628    162 MPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPIsVHCSAGVGRTGVFITLS 241

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1822521637 1338 YLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILDVTG 1384
Cdd:cd14628    242 IVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYLG 288

R-PTP-F-2

cd14629

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

1127-1384

6.42e-61

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

Pssm-ID: 350477 [Multi-domain] Cd Length: 291 Bit Score: 210.74 E-value: 6.42e-61

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1127 EYQGLANVGTNQSKE-AFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVV 1205
Cdd:cd14629     31 EFKLLANSKAHTSRFiSANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTE 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1206 DFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSScLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHF 1285
Cdd:cd14629    111 DFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSA-RYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQF 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1286 TSWPDHGVPKTTDKLLQF-QRMMRDYLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTC 1364
Cdd:cd14629    190 TDWPEQGVPKTGEGFIDFiGQVHKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPA 269

                          250       260
                   ....*....|....*....|
gi 1822521637 1365 MVQTENQYIFLHQCILDVTG 1384
Cdd:cd14629    270 MVQTEDQYQLCYRAALEYLG 289

R-PTP-N

cd14609

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

1113-1374

4.40e-60

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

Pssm-ID: 350457 [Multi-domain] Cd Length: 281 Bit Score: 207.97 E-value: 4.40e-60

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1113 YQRKHADTDIGFAEEYQGL-ANVGTNQSKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINAS-------YM 1184
Cdd:cd14609      6 YMEDHLRNRDRLAKEWQALcAYQAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSDYINASpiiehdpRM 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1185 PgyhldkAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPmDMSSCLYGDIVVNIVSEET-SPEWT 1263
Cdd:cd14609     86 P------AYIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWP-DEGSSLYHIYEVNLVSEHIwCEDFL 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1264 TRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLnKNRAGLPVVHCSAGVGRTGTLIALDYLLQRI 1343
Cdd:cd14609    159 VRSFYLKNVQTQETRTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCY-RGRSCPIIVHCSDGAGRTGTYILIDMVLNRM 237

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1822521637 1344 EKEAV-VDVYGIVHNMRMSRTCMVQTENQYIF 1374
Cdd:cd14609    238 AKGVKeIDIAATLEHVRDQRPGMVRTKDQFEF 269

PTPc-N11

cd14605

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

1147-1379

8.79e-60

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

Pssm-ID: 350453 [Multi-domain] Cd Length: 253 Bit Score: 206.02 E-value: 8.79e-60

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1147 DNKVKNRYTNIFPYDVARVKL-DRQPNSSSSDYINASY-MPGYHLD-------KAFIAAQGPLPNTVVDFWRMVWEQKTK 1217
Cdd:cd14605      1 ENKNKNRYKNILPFDHTRVVLhDGDPNEPVSDYINANIiMPEFETKcnnskpkKSYIATQGCLQNTVNDFWRMVFQENSR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1218 VIVMLTNCVEQNRVKCERYWPMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPE-PRTITQFHFTSWPDHGVPKT 1296
Cdd:cd14605     81 VIVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYILRELKLSKVGQGNtERTVWQYHFRTWPDHGVPSD 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1297 TDKLLQF-QRMMRDYLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAV---VDVYGIVHNMRMSRTCMVQTENQY 1372
Cdd:cd14605    161 PGGVLDFlEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQTEAQY 240


                   ....*..
gi 1822521637 1373 IFLHQCI 1379
Cdd:cd14605    241 RFIYMAV 247

R-PTP-C-2

cd14558

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

1178-1376

1.50e-59

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

Pssm-ID: 350406 [Multi-domain] Cd Length: 203 Bit Score: 203.39 E-value: 1.50e-59

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1178 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSclYGDIVVNIVSEE 1257
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKT--YGDIEVELKDTE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1258 TSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKNRAGLP-----VVHCSAGVGRTGT 1332
Cdd:cd14558     79 KSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNSKHGrsvpiVVHCSDGSSRTGI 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1822521637 1333 LIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLH 1376
Cdd:cd14558    159 FCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202

PTPc-N3

cd14600

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

1144-1382

2.20e-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: 2.20e-59

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1144 QVPDNKVKNRYTNIFPYDVARVKLDrqpnsSSSDYINASYM----PGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVI 1219
Cdd:cd14600     36 KLPQNMDKNRYKDVLPYDATRVVLQ-----GNEDYINASYVnmeiPSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLI 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1220 VMLTNCVEQNRVKCERYWPMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDK 1299
Cdd:cd14600    111 VMLTTLTERGRTKCHQYWPDPPDVMEYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVPDDSSD 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1300 LLQFQRMMRdylNKNRAGLPV-VHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQC 1378
Cdd:cd14600    191 FLEFVNYVR---SKRVENEPVlVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEA 267


                   ....
gi 1822521637 1379 ILDV 1382
Cdd:cd14600    268 ILRV 271

PTPc-N22

cd14602

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

1151-1382

2.17e-58

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

Pssm-ID: 350450 [Multi-domain] Cd Length: 234 Bit Score: 201.22 E-value: 2.17e-58

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1151 KNRYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNR 1230
Cdd:cd14602      1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1231 VKCERYWP-MDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGcpEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRD 1309
Cdd:cd14602     81 KKCERYWAePGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKFNS--ETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRC 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521637 1310 YlnKNRAGLPV-VHCSAGVGRTGTLIALDYLLqRIEKEAVV----DVYGIVHNMRMSRTCMVQTENQYIFLHQCILDV 1382
Cdd:cd14602    159 Y--QEDDSVPIcIHCSAGCGRTGVICAIDYTW-MLLKDGIIpenfSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIEL 233

PTPc-N6

cd14606

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

1136-1380

1.26e-57

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

Pssm-ID: 350454 [Multi-domain] Cd Length: 266 Bit Score: 200.49 E-value: 1.26e-57

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1136 TNQSKEAfQVPDNKVKNRYTNIFPYDVARVKLD-RQPNSSSSDYINASYMPGYHL-----DKAFIAAQGPLPNTVVDFWR 1209
Cdd:cd14606      7 LHQRLEG-QRPENKSKNRYKNILPFDHSRVILQgRDSNIPGSDYINANYVKNQLLgpdenAKTYIASQGCLEATVNDFWQ 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1210 MVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPE-PRTITQFHFTSW 1288
Cdd:cd14606     86 MAWQENSRVIVMTTREVEKGRNKCVPYWPEVGMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGElIREIWHYQYLSW 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1289 PDHGVPKTTDKLLQFQrmmrDYLNKNRAGLP-----VVHCSAGVGRTGTLIALDYLLQRIEKEAV---VDVYGIVHNMRM 1360
Cdd:cd14606    166 PDHGVPSEPGGVLSFL----DQINQRQESLPhagpiIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRA 241

                          250       260
                   ....*....|....*....|
gi 1822521637 1361 SRTCMVQTENQYIFLHQCIL 1380
Cdd:cd14606    242 QRSGMVQTEAQYKFIYVAIA 261

PTPc-N7

cd14612

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

1139-1376

2.34e-56

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

Pssm-ID: 350460 [Multi-domain] Cd Length: 247 Bit Score: 195.82 E-value: 2.34e-56

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1139 SKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQPNSS-SSDYINASYMPGYH-LDKAFIAAQGPLPNTVVDFWRMVWEQKT 1216
Cdd:cd14612      6 SPEELDIPGHASKDRYKTILPNPQSRVCLRRAGSQEeEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEEC 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1217 KVIVMLTNCVEQNRvKCERYWPMDMSSclYG--DIVVNIVSEetSPEWTTRKFNVKKTGcpEPRTITQFHFTSWPDHGVP 1294
Cdd:cd14612     86 PIIVMITKLKEKKE-KCVHYWPEKEGT--YGrfEIRVQDMKE--CDGYTIRDLTIQLEE--ESRSVKHYWFSSWPDHQTP 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1295 KTTDKLLQFQRMMRDYLNKNRA-GLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYI 1373
Cdd:cd14612    159 ESAGPLLRLVAEVEESRQTAASpGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQ 238


                   ...
gi 1822521637 1374 FLH 1376
Cdd:cd14612    239 FLH 241

R-PTPc-A-E-2

cd14552

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

1178-1379

5.65e-56

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

Pssm-ID: 350400 [Multi-domain] Cd Length: 202 Bit Score: 193.25 E-value: 5.65e-56

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1178 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDmSSCLYGDIVVNIVSEE 1257
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPED-GSVSSGDITVELKDQT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1258 TSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKNRAGLPVVHCSAGVGRTGTLIALD 1337
Cdd:cd14552     80 DYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSGNHPITVHCSAGAGRTGTFCALS 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1822521637 1338 YLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCI 1379
Cdd:cd14552    160 TVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201

R-PTP-N2

cd14610

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

1144-1374

1.05e-55

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

Pssm-ID: 350458 [Multi-domain] Cd Length: 283 Bit Score: 195.66 E-value: 1.05e-55

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1144 QVPDNKVKNRYTNIFPYDVARVKLDRQPNSSSSDYINAS-YMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVML 1222
Cdd:cd14610     40 QREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASpIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCVVIVML 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1223 TNCVEQNRVKCERYWPmDMSSCLYGDIVVNIVSEET-SPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLL 1301
Cdd:cd14610    120 TPLAENGVKQCYHYWP-DEGSNLYHIYEVNLVSEHIwCEDFLVRSFYLKNLQTNETRTVTQFHFLSWNDQGVPASTRSLL 198

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1822521637 1302 QFQRMMrDYLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAV-VDVYGIVHNMRMSRTCMVQTENQYIF 1374
Cdd:cd14610    199 DFRRKV-NKCYRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMAKGAKeIDIAATLEHLRDQRPGMVQTKEQFEF 271

PTPc-N2

cd14607

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

1137-1379

1.10e-54

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

Pssm-ID: 350455 [Multi-domain] Cd Length: 257 Bit Score: 191.72 E-value: 1.10e-54

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1137 NQSKE-AFQV---PDNKVKNRYTNIFPYDVARVKLDRQPNssssDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVW 1212
Cdd:cd14607      9 NESHDyPHRVakyPENRNRNRYRDVSPYDHSRVKLQNTEN----DYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVW 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1213 EQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCLY---GDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWP 1289
Cdd:cd14607     85 QQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSfkeTGFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYTTWP 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1290 DHGVPKTTDKLLQFQRMMRDYLNKN-RAGLPVVHCSAGVGRTGTLIALDYLLQRIEKE--AVVDVYGIVHNMRMSRTCMV 1366
Cdd:cd14607    165 DFGVPESPASFLNFLFKVRESGSLSpEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKdpDSVDIKQVLLDMRKYRMGLI 244

                          250
                   ....*....|...
gi 1822521637 1367 QTENQYIFLHQCI 1379
Cdd:cd14607    245 QTPDQLRFSYMAV 257

PTPc-N20

cd14596

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

1178-1382

1.94e-54

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

Pssm-ID: 350444 [Multi-domain] Cd Length: 207 Bit Score: 188.80 E-value: 1.94e-54

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1178 YINASY--MPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCL-YGDIVVNIV 1254
Cdd:cd14596      1 YINASYitMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMeLENYQLRLE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1255 SEETSPEWTTRKFNV--KKTGcpEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKnraGLPVVHCSAGVGRTGT 1332
Cdd:cd14596     81 NYQALQYFIIRIIKLveKETG--ENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNT---GPIVVHCSAGIGRAGV 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1333 LIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILDV 1382
Cdd:cd14596    156 LICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEV 205

R-PTPc-R

cd14611

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

1151-1377

1.01e-53

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

Pssm-ID: 350459 [Multi-domain] Cd Length: 226 Bit Score: 187.43 E-value: 1.01e-53

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1151 KNRYTNIFPYDVARVKLD-RQPNSSSSDYINASYMPGYH-LDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQ 1228
Cdd:cd14611      2 KNRYKTILPNPHSRVCLKpKNSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1229 NRvKCERYWPMDMSscLYGDIVVNIVSEETSPEWTTRKFNVKKTGcpEPRTITQFHFTSWPDHGVPKTTDKLLQFQ-RMM 1307
Cdd:cd14611     82 NE-KCVLYWPEKRG--IYGKVEVLVNSVKECDNYTIRNLTLKQGS--QSRSVKHYWYTSWPDHKTPDSAQPLLQLMlDVE 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1308 RDYLNKNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1377
Cdd:cd14611    157 EDRLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVHH 226

R-PTPc-A-2

cd14623

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

1153-1379

1.12e-53

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

Pssm-ID: 350471 [Multi-domain] Cd Length: 228 Bit Score: 187.56 E-value: 1.12e-53

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1153 RYTNIFPYDVARVKLDRQPNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVK 1232
Cdd:cd14623      1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1233 CERYWPMDmSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLN 1312
Cdd:cd14623     81 CAQYWPSD-GSVSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQ 159

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521637 1313 KNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCI 1379
Cdd:cd14623    160 QSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVV 226

PTPc-N1

cd14608

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

1124-1390

1.22e-53

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

Pssm-ID: 350456 [Multi-domain] Cd Length: 277 Bit Score: 189.47 E-value: 1.22e-53

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1124 FAEEYQGLANVGTNQSKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQPNssssDYINASYMPGYHLDKAFIAAQGPLPNT 1203
Cdd:cd14608      1 WAAIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDN----DYINASLIKMEEAQRSYILTQGPLPNT 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1204 VVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCLY---GDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTI 1280
Cdd:cd14608     77 CGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIfedTNLKLTLISEDIKSYYTVRQLELENLTTQETREI 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1281 TQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKN-RAGLPVVHCSAGVGRTGTLIALDYLLQRIEKE---AVVDVYGIVH 1356
Cdd:cd14608    157 LHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSpEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRkdpSSVDIKKVLL 236

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1822521637 1357 NMRMSRTCMVQTENQYIFLHQCILD----VTGDKSIDE 1390
Cdd:cd14608    237 EMRKFRMGLIQTADQLRFSYLAVIEgakfIMGDSSVQD 274

R-PTPc-E-2

cd14622

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

1177-1381

5.82e-53

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

Pssm-ID: 350470 [Multi-domain] Cd Length: 205 Bit Score: 184.44 E-value: 5.82e-53

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1177 DYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDmSSCLYGDIVVNIVSE 1256
Cdd:cd14622      1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSE-GSVTHGEITIEIKND 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1257 ETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKNRAGLPVVHCSAGVGRTGTLIAL 1336
Cdd:cd14622     80 TLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTGNHPIVVHCSAGAGRTGTFIAL 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1822521637 1337 DYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1381
Cdd:cd14622    160 SNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQD 204

PTPc-N4

cd14601

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

1177-1382

6.30e-53

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

Pssm-ID: 350449 [Multi-domain] Cd Length: 212 Bit Score: 184.76 E-value: 6.30e-53

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1177 DYINASYM----PGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCLYGDIVVN 1252
Cdd:cd14601      1 DYINANYInmeiPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSSSYGGFQVT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1253 IVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRdylnKNRAGLP---VVHCSAGVGR 1329
Cdd:cd14601     81 CHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVR----NKRAGKDepvVVHCSAGIGR 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1822521637 1330 TGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILDV 1382
Cdd:cd14601    157 TGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKV 209

R-PTP-N-N2

cd14546

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

1178-1379

1.11e-52

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

Pssm-ID: 350394 [Multi-domain] Cd Length: 208 Bit Score: 183.80 E-value: 1.11e-52

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1178 YINASYMpgYHLD---KAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSClYGDIVVNIV 1254
Cdd:cd14546      1 YINASTI--YDHDprnPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEV-YHIYEVHLV 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1255 SEET-SPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMmrdyLNKNRAGLP---VVHCSAGVGRT 1330
Cdd:cd14546     78 SEHIwCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRK----VNKSYRGRScpiVVHCSDGAGRT 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1331 GTLIALDYLLQRIEKEAV-VDVYGIVHNMRMSRTCMVQTENQYIFLHQCI 1379
Cdd:cd14546    154 GTYILIDMVLNRMAKGAKeIDIAATLEHLRDQRPGMVKTKDQFEFVLTAV 203

PTPc-N21_14

cd14540

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

1178-1382

3.77e-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: 179.96 E-value: 3.77e-51

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1178 YINASYMPGYHLDKA--FIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSC---LYGDIVVN 1252
Cdd:cd14540      1 YINASHITATVGGKQrfYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEHdalTFGEYKVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1253 IVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQF--------QRMMRDYLNKNRAGLPVVHCS 1324
Cdd:cd14540     81 TKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFleeinsvrRHTNQDVAGHNRNPPTLVHCS 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521637 1325 AGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILDV 1382
Cdd:cd14540    161 AGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQY 218

PTP-N23

cd14539

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

1178-1377

1.29e-50

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

Pssm-ID: 350387 [Multi-domain] Cd Length: 205 Bit Score: 177.96 E-value: 1.29e-50

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1178 YINASYMPGY-HLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMSSCL-YGDIVVNIVS 1255
Cdd:cd14539      1 YINASLIEDLtPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALvYGAITVSLQS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1256 EETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKNRA-GLP-VVHCSAGVGRTGTL 1333
Cdd:cd14539     81 VRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQRSlQTPiVVHCSSGVGRTGAF 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1822521637 1334 IALDYLLQRIEKE-AVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1377
Cdd:cd14539    161 CLLYAAVQEIEAGnGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205

PTPc-N5

cd14613

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

1140-1376

4.71e-50

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

Pssm-ID: 350461 [Multi-domain] Cd Length: 258 Bit Score: 178.13 E-value: 4.71e-50

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1140 KEAFQVPDNKV------------KNRYTNIFPYDVARVKL-DRQPNSSSSDYINASYMPGY-HLDKAFIAAQGPLPNTVV 1205
Cdd:cd14613      5 AEFFEIPMNFVdpkeydipglvrKNRYKTILPNPHSRVCLtSPDQDDPLSSYINANYIRGYgGEEKVYIATQGPTVNTVG 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1206 DFWRMVWEQKTKVIVMLTNCVEQNRvKCERYWPMDmsSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGcpEPRTITQFHF 1285
Cdd:cd14613     85 DFWRMVWQERSPIIVMITNIEEMNE-KCTEYWPEE--QVTYEGIEITVKQVIHADDYRLRLITLKSGG--EERGLKHYWY 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1286 TSWPDHGVPKTTDKLLQFQRMMRDYLNKNRA--GLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRT 1363
Cdd:cd14613    160 TSWPDQKTPDNAPPLLQLVQEVEEARQQAEPncGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRG 239

                          250
                   ....*....|...
gi 1822521637 1364 CMVQTENQYIFLH 1376
Cdd:cd14613    240 GMIQTCEQYQFVH 252

R-PTPc-typeIIb-2

cd14556

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

1178-1377

9.85e-45

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

Pssm-ID: 350404 [Multi-domain] Cd Length: 201 Bit Score: 160.65 E-value: 9.85e-45

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1178 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLtNCVEQNRVKCERYWPMDMSSClYGDIVVNIVSEE 1257
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVML-NQLDPKDQSCPQYWPDEGSGT-YGPIQVEFVSTT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1258 TSPEWTTRKFNVKKTGCPEP--RTITQFHFTSWPDHG-VPKTTDKLLQFQRMMRDYLNKNRAGLPVVHCSAGVGRTGTLI 1334
Cdd:cd14556     79 IDEDVISRIFRLQNTTRPQEgyRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQEQSGEGPIVVHCLNGVGRSGVFC 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1822521637 1335 ALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1377
Cdd:cd14556    159 AISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201

COG5599

Protein tyrosine phosphatase [Signal transduction mechanisms];

1136-1375

3.79e-43

Protein tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 444335 [Multi-domain] Cd Length: 282 Bit Score: 159.10 E-value: 3.79e-43

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1136 TNQSKEAFQVPDNKVKNRYTNIFPYDVARVkldrqpnSSSSDYINASY--MPGYHLdkaFIAAQGPLPNTVVDFWRMVWE 1213
Cdd:COG5599     30 SHNDPQYLQNINGSPLNRFRDIQPYKETAL-------RANLGYLNANYiqVIGNHR---YIATQYPLEEQLEDFFQMLFD 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1214 QKTKVIVMLTNCVE--QNRVKCERYWPMDMSsclYGDIVVNIVSEET---SPEWTTRKFNVKKTGC-PEPRTITQFHFTS 1287
Cdd:COG5599    100 NNTPVLVVLASDDEisKPKVKMPVYFRQDGE---YGKYEVSSELTESiqlRDGIEARTYVLTIKGTgQKKIEIPVLHVKN 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1288 WPDHGVPkTTDKLLQFQRMMRDYLNKNRA--GLPVVHCSAGVGRTGTLIALDYLLQRI--EKEAVVDVYGIVHNMRMSRT 1363
Cdd:COG5599    177 WPDHGAI-SAEALKNLADLIDKKEKIKDPdkLLPVVHCRAGVGRTGTLIACLALSKSInaLVQITLSVEEIVIDMRTSRN 255

                          250
                   ....*....|...
gi 1822521637 1364 C-MVQTENQYIFL 1375
Cdd:COG5599    256 GgMVQTSEQLDVL 268

PTPc_plant_PTP1

cd17658

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

1178-1374

1.72e-42

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

Pssm-ID: 350496 [Multi-domain] Cd Length: 206 Bit Score: 154.54 E-value: 1.72e-42

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1178 YINASYM--PGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNR-VKCERYWPM-DMSSCLYGDIVVNI 1253
Cdd:cd17658      1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStAKCADYFPAeENESREFGRISVTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1254 VSEETSPE-WTTRKFNVKKTGCPE-PRTITQFHFTSWPDHGVPKTTDKLLQFQRmmRDYLNKNRAGLPVVHCSAGVGRTG 1331
Cdd:cd17658     81 KKLKHSQHsITLRVLEVQYIESEEpPLSVLHIQYPEWPDHGVPKDTRSVRELLK--RLYGIPPSAGPIVVHCSAGIGRTG 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1822521637 1332 TLIALDYLLQRIEKEAV--VDVYGIVHNMRMSRTCMVQTENQYIF 1374
Cdd:cd17658    159 AYCTIHNTIRRILEGDMsaVDLSKTVRKFRSQRIGMVQTQDQYIF 203

PTPc-N14

cd14599

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

1145-1380

1.74e-42

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

Pssm-ID: 350447 [Multi-domain] Cd Length: 287 Bit Score: 157.47 E-value: 1.74e-42

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1145 VPDNKVKNRYTNIFPYDVARVKLdrQPN-SSSSDYINASYMP------GYHldkaFIAAQGPLPNTVVDFWRMVWEQKTK 1217
Cdd:cd14599     35 LPENAERNRIREVVPYEENRVEL--VPTkENNTGYINASHIKvtvggeEWH----YIATQGPLPHTCHDFWQMVWEQGVN 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1218 VIVMLTNCVEQNRVKCERYWP---MDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVP 1294
Cdd:cd14599    109 VIAMVTAEEEGGRSKSHRYWPklgSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWHLQYTDWPDHGCP 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1295 KTTDKLLQFQ---RMMRDYLN------KNRAGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCM 1365
Cdd:cd14599    189 EEVQGFLSYLeeiQSVRRHTNsmldstKNCNPPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRHLREQRMFM 268

                          250
                   ....*....|....*
gi 1822521637 1366 VQTENQYIFLHQCIL 1380
Cdd:cd14599    269 IQTIAQYKFVYQVLI 283

PHA02738

hypothetical protein; Provisional

1148-1404

7.69e-42

hypothetical protein; Provisional

Pssm-ID: 222923 [Multi-domain] Cd Length: 320 Bit Score: 156.62 E-value: 7.69e-42

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1148 NKVKNRYTNIFPYDVARVKLDRQPNSSssDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVE 1227
Cdd:PHA02738    49 NRKLNRYLDAVCFDHSRVILPAERNRG--DYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKE 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1228 QNRVKCERYWP-MDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKtGCPEPRTITQFHFTSWPDHGVPKTTDKLLQF--- 1303
Cdd:PHA02738   127 NGREKCFPYWSdVEQGSIRFGKFKITTTQVETHPHYVKSTLLLTD-GTSATQTVTHFNFTAWPDHDVPKNTSEFLNFvle 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1304 ----QRMM---RDYLNKNRAGLP--VVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIF 1374
Cdd:PHA02738   206 vrqcQKELaqeSLQIGHNRLQPPpiVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFF 285

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1822521637 1375 LHQCI---LDVTGDKSIDEPIYENQADLIYENV 1404
Cdd:PHA02738   286 CYRAVkryVNLTVNKVSKKLIPNVQTVSFNKNL 318

PHA02747

protein tyrosine phosphatase; Provisional

1127-1411

4.55e-41

protein tyrosine phosphatase; Provisional

Pssm-ID: 165114 [Multi-domain] Cd Length: 312 Bit Score: 154.39 E-value: 4.55e-41

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1127 EYQGLANVGTNQSKEAFQVPDNKVKNRYTNIFPYDVARVKLDRQpNSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVD 1206
Cdd:PHA02747    30 EHHQIILKPFDGLIANFEKPENQPKNRYWDIPCWDHNRVILDSG-GGSTSDYIHANWIDGFEDDKKFIATQGPFAETCAD 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1207 FWRMVWEQKTKVIVMLTNCVEQN-RVKCERYW-PMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFH 1284
Cdd:PHA02747   109 FWKAVWQEHCSIIVMLTPTKGTNgEEKCYQYWcLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKISHFQ 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1285 FTSWPDHGVPKTTDKLLQF--------QRMMRDYLNKNRAGLP-VVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIV 1355
Cdd:PHA02747   189 CSEWFEDETPSDHPDFIKFikiidinrKKSGKLFNPKDALLCPiVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTA 268

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1822521637 1356 HNMRMSRTCMVQTENQYIFLhqcildvtgdksidEPIYENQADLIYENVDAIKVAN 1411
Cdd:PHA02747   269 EKIREQRHAGIMNFDDYLFI--------------QPGYEVLHYFLSKIKAIDKIKF 310

PTPc_motif

smart00404

Protein tyrosine phosphatase, catalytic domain motif;

1279-1381

3.24e-40

Protein tyrosine phosphatase, catalytic domain motif;

Pssm-ID: 214649 [Multi-domain] Cd Length: 105 Bit Score: 144.04 E-value: 3.24e-40

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  1279 TITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKNRAGLP-VVHCSAGVGRTGTLIALDYLLQRIEKEA-VVDVYGIVH 1356
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPvVVHCSAGVGRTGTFVAIDILLQQLEAEAgEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 1822521637  1357 NMRMSRTCMVQTENQYIFLHQCILD 1381
Cdd:smart00404   81 ELRSQRPGMVQTEEQYLFLYRALLE 105

PTPc_DSPc

smart00012

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

1279-1381

3.24e-40

Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine phosphatases. Homologues detected by this profile and not by those of "PTPc" or "DSPc" are predicted to be protein phosphatases with a similar fold to DSPs and PTPs, yet with unpredicted specificities.

Pssm-ID: 214469 [Multi-domain] Cd Length: 105 Bit Score: 144.04 E-value: 3.24e-40

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  1279 TITQFHFTSWPDHGVPKTTDKLLQFQRMMRDYLNKNRAGLP-VVHCSAGVGRTGTLIALDYLLQRIEKEA-VVDVYGIVH 1356
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPvVVHCSAGVGRTGTFVAIDILLQQLEAEAgEVDIFDTVK 80

                            90       100
                    ....*....|....*....|....*
gi 1822521637  1357 NMRMSRTCMVQTENQYIFLHQCILD 1381
Cdd:smart00012   81 ELRSQRPGMVQTEEQYLFLYRALLE 105

PHA02742

protein tyrosine phosphatase; Provisional

1148-1380

8.38e-38

protein tyrosine phosphatase; Provisional

Pssm-ID: 165109 [Multi-domain] Cd Length: 303 Bit Score: 144.37 E-value: 8.38e-38

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1148 NKVKNRYTNIFPYDVARVKLDRQpnSSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVE 1227
Cdd:PHA02742    52 NMKKCRYPDAPCFDRNRVILKIE--DGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIME 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1228 QNRVKCERYW-PMDMSSCLYGDIVVNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQFQRM 1306
Cdd:PHA02742   130 DGKEACYPYWmPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFVLA 209

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1307 MR--------DYLNKNRAGLP--VVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLH 1376
Cdd:PHA02742   210 VReadlkadvDIKGENIVKEPpiLVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCY 289


                   ....
gi 1822521637 1377 QCIL 1380
Cdd:PHA02742   290 FIVL 293

R-PTPc-T-2

cd14634

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

1178-1381

1.92e-36

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

Pssm-ID: 350482 [Multi-domain] Cd Length: 206 Bit Score: 137.07 E-value: 1.92e-36

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1178 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTncvEQNRVK-CERYWPmDMSSCLYGDIVVNIVSE 1256
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLN---EMDAAQlCMQYWP-EKTSCCYGPIQVEFVSA 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1257 ETSPEWTTRKFNVKKTGCPEP--RTITQFHFTSWPDH-GVPKTTDKLLQFQRMMRDYLNK--NRAGLPVVHCSAGVGRTG 1331
Cdd:cd14634     77 DIDEDIISRIFRICNMARPQDgyRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQydGREGRTVVHCLNGGGRSG 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1332 TLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1381
Cdd:cd14634    157 TFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206

PTPc-N21

cd14598

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

1178-1380

5.55e-35

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

Pssm-ID: 350446 [Multi-domain] Cd Length: 220 Bit Score: 133.56 E-value: 5.55e-35

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1178 YINASYMP----GYHLDkaFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRVKCERYWPMDMS---SCLYGDIV 1250
Cdd:cd14598      1 YINASHIKvtvgGKEWD--YIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSrhnTVTYGRFK 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1251 VNIVSEETSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTDKLLQF-------QRMMRDYLNKNRAGLPV-VH 1322
Cdd:cd14598     79 ITTRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYleeiqsvRRHTNSTIDPKSPNPPVlVH 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521637 1323 CSAGVGRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCIL 1380
Cdd:cd14598    159 CSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLI 216

PHA02746

protein tyrosine phosphatase; Provisional

1146-1379

2.65e-34

protein tyrosine phosphatase; Provisional

Pssm-ID: 165113 [Multi-domain] Cd Length: 323 Bit Score: 134.77 E-value: 2.65e-34

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1146 PDNKVKNRYTNIFPYDVARVKL------------DRQPN-------SSSSDYINASYMPGYHLDKAFIAAQGPLPNTVVD 1206
Cdd:PHA02746    49 KENLKKNRFHDIPCWDHSRVVInaheslkmfdvgDSDGKkievtseDNAENYIHANFVDGFKEANKFICAQGPKEDTSED 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1207 FWRMVWEQKTKVIVMLTNcVEQNRVKCERYWPMDMSSCL-YGDIVVNI--VSEETSpeWTTRKFNVKKTGCPEPRTITQF 1283
Cdd:PHA02746   129 FFKLISEHESQVIVSLTD-IDDDDEKCFELWTKEEDSELaFGRFVAKIldIIEELS--FTKTRLMITDKISDTSREIHHF 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1284 HFTSWPDHGVPKTTDKLLQF--------QRMMRDYLNKNRAGLP-VVHCSAGVGRTGTLIALDYLLQRIEKEAVVDVYGI 1354
Cdd:PHA02746   206 WFPDWPDNGIPTGMAEFLELinkvneeqAELIKQADNDPQTLGPiVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEI 285

                          250       260
                   ....*....|....*....|....*
gi 1822521637 1355 VHNMRMSRTCMVQTENQYIFLHQCI 1379
Cdd:PHA02746   286 VLKIRKQRHSSVFLPEQYAFCYKAL 310

R-PTPc-U-2

cd14637

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

1178-1381

2.48e-28

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

Pssm-ID: 350485 [Multi-domain] Cd Length: 207 Bit Score: 113.85 E-value: 2.48e-28

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1178 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQNRV-KCERYWPmDMSSCLYGDIVVNIVSE 1256
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWP-EPGLQQYGPMEVEFVSG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1257 ETSPEWTTRKFNVKKTG--CPEPRTITQFHFTSW-PDHGVPKTTDKLLQFQRMMRDYLNKNRAGLPVVHCSAGVGRTGTL 1333
Cdd:cd14637     80 SADEDIVTRLFRVQNITrlQEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQRESGEGRTVVHCLNGGGRSGTY 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1822521637 1334 IALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1381
Cdd:cd14637    160 CASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207

R-PTPc-M-2

cd14635

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

1178-1381

6.76e-28

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

Pssm-ID: 350483 [Multi-domain] Cd Length: 206 Bit Score: 112.47 E-value: 6.76e-28

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1178 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLtNCVEQNRVkCERYWPmDMSSCLYGDIVVNIVSEE 1257
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVML-NDVDPAQL-CPQYWP-ENGVHRHGPIQVEFVSAD 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1258 TSPEWTTRKFNVKKTGCPEP--RTITQFHFTSWPDH-GVPKTTDKLLQFQRMMRDYLNKNRA--GLPVVHCSAGVGRTGT 1332
Cdd:cd14635     78 LEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEYNGgeGRTVVHCLNGGGRSGT 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1822521637 1333 LIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1381
Cdd:cd14635    158 FCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206

R5-PTP-2

cd14550

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

1178-1377

9.48e-28

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

Pssm-ID: 350398 [Multi-domain] Cd Length: 200 Bit Score: 112.03 E-value: 9.48e-28

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1178 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCveQNRVKCERYWPMDMSSCLYGDIVVNIVSEE 1257
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDN--ELNEDEPIYWPTKEKPLECETFKVTLSGED 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1258 TSPEW-----TTRKFNVKKTGCPEPRTITQFHFTSWPDHGVP-KTTDKLLQ-FQRmmrdyLNKNRAGLPVVHCSAGVGRT 1330
Cdd:cd14550     79 HSCLSneirlIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPiHTVFELINtVQE-----WAQQRDGPIVVHDRYGGVQA 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1822521637 1331 GTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQ 1377
Cdd:cd14550    154 ATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200

R-PTPc-K-2

cd14636

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

1178-1381

2.58e-26

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

Pssm-ID: 350484 [Multi-domain] Cd Length: 206 Bit Score: 108.19 E-value: 2.58e-26

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1178 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTncvEQNRVK-CERYWPmDMSSCLYGDIVVNIVSE 1256
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLN---EVDLAQgCPQYWP-EEGMLRYGPIQVECMSC 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1257 ETSPEWTTRKFNVKKTGCPEP--RTITQFHFTSWPDH-GVPKTTDKLLQFQRMMRDYLNK--NRAGLPVVHCSAGVGRTG 1331
Cdd:cd14636     77 SMDCDVISRIFRICNLTRPQEgyLMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEEcdEGEGRTIIHCLNGGGRSG 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1332 TLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCILD 1381
Cdd:cd14636    157 MFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206

R-PTP-Z-2

cd17669

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

1178-1380

8.46e-24

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

Pssm-ID: 350507 [Multi-domain] Cd Length: 204 Bit Score: 100.84 E-value: 8.46e-24

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1178 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNcvEQNRVKCE-RYWPMDMSSCLYGDIVVNIVSE 1256
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPD--GQNMAEDEfVYWPNKDEPINCETFKVTLIAE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1257 E-----TSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPktTDKLLQFQRMMRDYlNKNRAGLPVVHCSAGVGRTG 1331
Cdd:cd17669     79 EhkclsNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSP--ISKTFELISIIKEE-AANRDGPMIVHDEHGGVTAG 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1822521637 1332 TLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCIL 1380
Cdd:cd17669    156 TFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204

R-PTP-G-2

cd17670

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

1178-1380

1.25e-23

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

Pssm-ID: 350508 [Multi-domain] Cd Length: 205 Bit Score: 100.14 E-value: 1.25e-23

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1178 YINASYMPGYHLDKAFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNcvEQNRVKCER-YWPMDMSSCLYGDIVVNIVSE 1256
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD--NQGLAEDEFvYWPSREESMNCEAFTVTLISK 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1257 E-----TSPEWTTRKFNVKKTGCPEPRTITQFHFTSWPDHGVPKTTD----KLLQFQRMMRDylnknraGLPVVHCSAGV 1327
Cdd:cd17670     79 DrlclsNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTfeliNVIKEEALTRD-------GPTIVHDEFGA 151

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1822521637 1328 GRTGTLIALDYLLQRIEKEAVVDVYGIVHNMRMSRTCMVQTENQYIFLHQCIL 1380
Cdd:cd17670    152 VSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204

PTP_YopH-like

cd14559

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

1152-1372

9.64e-20

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

Pssm-ID: 350407 [Multi-domain] Cd Length: 227 Bit Score: 89.77 E-value: 9.64e-20

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1152 NRYTNIfpydVARVKLDRQPNssssdyINASYMP--GYHLdkaFIAAQGPLPNTVVDFWRMVWEQKTKVIVMLTNCVEQN 1229
Cdd:cd14559      1 NRFTNI----QTRVSTPVGKN------LNANRVQigNKNV---AIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQ 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1230 RVKCERYWPMdmsSCLYGDIVVNivSEETSPEWTTRKFNVK----KTGCPEPR-TITQFHFTSWPDHG------------ 1292
Cdd:cd14559     68 RKGLPPYFRQ---SGTYGSVTVK--SKKTGKDELVDGLKADmynlKITDGNKTiTIPVVHVTNWPDHTaisseglkelad 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1293 -VPKTTDKLLQF--QRMMRDYLNKNRaGLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVDvygIVHNMRMSRTC-MVQT 1368
Cdd:cd14559    143 lVNKSAEEKRNFykSKGSSAINDKNK-LLPVIHCRAGVGRTGQLAAAMELNKSPNNLSVED---IVSDMRTSRNGkMVQK 218


                   ....
gi 1822521637 1369 ENQY 1372
Cdd:cd14559    219 DEQL 222

FN3

Fibronectin type 3 domain [General function prediction only];

200-744

1.94e-16

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 84.67 E-value: 1.94e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  200 SVTPEDTLSTPVEVTNTTNPSPVTGLSVVNGTTESLRIKWT-RPTDTRASDYTYRVTVTNVTGGVSWTESTSKDKTTFTA 278
Cdd:COG3401     30 GGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGgRAGTTSGVAAVAVAAAPPTATGLTTLTGSGSVGGATNT 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  279 TGLQPGDQYQLSVQSVTPEDTVSSPLEVTNTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRATNYTYIVTVTNVTGGVSS 358
Cdd:COG3401    110 GLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTS 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  359 TTVTSRGETTFKATGLQpgdqYLLSVQSVTPEDTWSTPVEVT-NTTNPSPVTGLTVVNGTTHSLRIEWTPPTDTRATNYT 437
Cdd:COG3401    190 TTLVDGGGDIEPGTTYY----YRVAATDTGGESAPSNEVSVTtPTTPPSAPTGLTATADTPGSVTLSWDPVTESDATGYR 265

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  438 YKVTVTnvaGGVSSTTITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEV----TSTTNPSPVTGLSVVNGTTQS 513
Cdd:COG3401    266 VYRSNS---GDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNESAPSNVvsvtTDLTPPAAPSGLTATAVGSSS 342

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  514 LTIEWTSPNDTTASNyiYNVTVTNVTGGVSWTESTSKGETTFTATGLQPGDQYQLSVQSVT---PEDTLSTPEQVTNTTN 590
Cdd:COG3401    343 ITLSWTASSDADVTG--YNVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDaagNESAPSEEVSATTASA 420

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  591 PSPVTGLSVVNGTTQSLGIEWT-------SPTDTRASNYTYIVTVTNVTGGGRSTTVTSKGETAFTATGLQPGDQYQLSV 663
Cdd:COG3401    421 ASGESLTASVDAVPLTDVAGATaaasaasNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGS 500

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  664 QSVTPEGTLSTPVEVTSTTNPSPVTGLSVVNGT--------TQSLTIEWTRPTDTRASNYTYNVTVTNVTGGVSWTQSTS 735
Cdd:COG3401    501 GASSVTNSVSVIGASAAAAVGGAPDGTPNVTGAspvtvgasTGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITTLGGS 580


                   ....*....
gi 1822521637  736 KDETTFTAT 744
Cdd:COG3401    581 LLTTTSTNT 589

FN3

Fibronectin type 3 domain [General function prediction only];

357-950

2.84e-16

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 84.28 E-value: 2.84e-16

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  357 SSTTVTSRGETTFKATGLQPGDQYLLSVQSVTPEDTWSTPVEVTNTTNPSPVTGLTVVNGTTHSLRIEWTPPTDTRATNY 436
Cdd:COG3401      1 TGSSYLTSLDAGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  437 TYKVTVTNVAGGVSSTTITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTI 516
Cdd:COG3401     81 AVAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  517 EWTSPNDTTASNYIYNVTVTNVTGGVSWTESTSKGETTftatgLQPGDQYQLSVQSVTPEDTLSTPEQV---TNTTNPSP 593
Cdd:COG3401    161 SSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGD-----IEPGTTYYYRVAATDTGGESAPSNEVsvtTPTTPPSA 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  594 VTGLSVVNGTTQSLGIEWTSPTDTRASNYT-YIVTvtnvTGGGRSTTVTSKGETAFTATGLQPGDQYQLSVQSVTPEGTL 672
Cdd:COG3401    236 PTGLTATADTPGSVTLSWDPVTESDATGYRvYRSN----SGDGPFTKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNE 311

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  673 STPVEV----TSTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYtyNVTVTNVTGGVSWTQSTSKDETTFTATRLQP 748
Cdd:COG3401    312 SAPSNVvsvtTDLTPPAAPSGLTATAVGSSSITLSWTASSDADVTGY--NVYRSTSGGGTYTKIAETVTTTSYTDTGLTP 389

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  749 GDQYLLSVQSVTPEDTLSTPAQVTSTTNPSPVTGLSVVNSTTqSLRIEWTTPNNIRASNYTYNVTVTNVTDGASSTTITS 828
Cdd:COG3401    390 GTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVD-AVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAV 468

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  829 KGETTFTVTGLQPGDQYRlSVRSVTPEDTWSTPAQVTSTSNPSPVSGLTVVNRTTVSIEVTWAAPTDARAPEYTYRITLA 908
Cdd:COG3401    469 PFTTTSSTVTATTTDTTT-ANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLI 547

                          570       580       590       600
                   ....*....|....*....|....*....|....*....|..
gi 1822521637  909 NVTRRGRGAIDTGPGVTTFTVTNLVPGVEYELRLQSVTPAGT 950
Cdd:COG3401    548 TDLVSLTTSASSSVSGAGLGSGNLYLITTLGGSLLTTTSTNT 589

FN3

Fibronectin type 3 domain [General function prediction only];

59-651

7.32e-14

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 76.19 E-value: 7.32e-14

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637   59 TRASNYTYNVTVTNVAGGVSSITTTGKNETTFTATGLQPGDQYLLSVRSVTPEDTLSTPVEVTSTTNPSPVIGLSVVNGT 138
Cdd:COG3401     12 GIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAAAPPTA 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  139 TQSLWIEWTSPTDTRATNYTYIVTVTNVTGGVSWTKSTNKDKTTFTATGLQPGDQYQLSVRSVTPEDTLSTPVEVTNTTN 218
Cdd:COG3401     92 TGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVS 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  219 PSPVTGLSVVNGTTESLRI--KWTRPTDTRASDYTYRVTVTNVTGGVSWTESTSKdkttftatglqpgdqyqlsvqsvtp 296
Cdd:COG3401    172 PDTSATAAVATTSLTVTSTtlVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSV------------------------- 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  297 edtvsspleVTNTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRATNytYIVTVTNVTGGvSSTTVTSRGETTFKATGLQP 376
Cdd:COG3401    227 ---------TTPTTPPSAPTGLTATADTPGSVTLSWDPVTESDATG--YRVYRSNSGDG-PFTKVATVTTTSYTDTGLTN 294

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  377 GDQYLLSVQSVTPEDTWSTPVEV----TNTTNPSPVTGLTVVNGTTHSLRIEWTPPTDTRATNytYKVTVTNVAGGVSST 452
Cdd:COG3401    295 GTTYYYRVTAVDAAGNESAPSNVvsvtTDLTPPAAPSGLTATAVGSSSITLSWTASSDADVTG--YNVYRSTSGGGTYTK 372

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  453 TITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPVTGLS-------VVNGTTQSLTIEWTSPNDTT 525
Cdd:COG3401    373 IAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESltasvdaVPLTDVAGATAAASAASNPG 452

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  526 ASNYIYNVTVTNVTGGVSWTESTSKGETT---------FTATGLQPGDQYQLSVQSVTPEDTLSTPEQVTNTTNPSPVTG 596
Cdd:COG3401    453 VSAAVLADGGDTGNAVPFTTTSSTVTATTtdtttanlsVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTG 532

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521637  597 LSVVNGT--TQSLGIEWTSPTDTRASNYTYIVTVTNVTGGGRSTTVTSKGETAFTAT 651
Cdd:COG3401    533 ASPVTVGasTGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITTLGGSLLTTTSTNT 589

FN3

Fibronectin type 3 domain [General function prediction only];

34-558

2.46e-13

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 74.65 E-value: 2.46e-13

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637   34 SPVTGLSVVSRTTDSLRIEWTSPNDTRASNYTYNVTVTNVAGGVSSITTTGKNETTFTATGLQPGDQYLLSVRSVTPEDT 113
Cdd:COG3401     82 VAVAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTAS 161

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  114 LSTPVEVTSTTNPSPVIGLSVVNGTTQSLWIEWTSPTDTRATNYTYIVTVTNVTGgvswtkstnkdkttftatglqpgdq 193
Cdd:COG3401    162 SVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGG------------------------- 216

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  194 yqlsvrsvtpEDTLSTPVEVT-NTTNPSPVTGLSVVNGTTESLRIKWTRPTDTRASDYT-YRVTvtnvTGGVSWTESTSK 271
Cdd:COG3401    217 ----------ESAPSNEVSVTtPTTPPSAPTGLTATADTPGSVTLSWDPVTESDATGYRvYRSN----SGDGPFTKVATV 282

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  272 DKTTFTATGLQPGDQYQLSVQSVTPEDTVSSPLEV----TNTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRATNytYIV 347
Cdd:COG3401    283 TTTSYTDTGLTNGTTYYYRVTAVDAAGNESAPSNVvsvtTDLTPPAAPSGLTATAVGSSSITLSWTASSDADVTG--YNV 360

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  348 TVTNVTGGVSSTTVTSRGETTFKATGLQPGDQYLLSVQSVT---PEDTWSTPVEVTNTTNPSPVTGLTVVNGTTHSLRIE 424
Cdd:COG3401    361 YRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDaagNESAPSEEVSATTASAASGESLTASVDAVPLTDVAG 440

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  425 WT-------PPTDTRATNYTYKVTVTNVAGGVSSTTITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTN 497
Cdd:COG3401    441 ATaaasaasNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAV 520

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1822521637  498 PSPVTGLSVVNGT--------TQSLTIEWTSPNDTTASNYIYNVTVTNVTGGVSWTESTSKGETTFTAT 558
Cdd:COG3401    521 GGAPDGTPNVTGAspvtvgasTGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITTLGGSLLTTTSTNT 589

FN3

Fibronectin type 3 domain [General function prediction only];

27-368

1.78e-10

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 65.41 E-value: 1.78e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637   27 SQNVTDPSPVTGLSVVSRTTDSLRIEWTSPNDTRASNYTYNVTvTNVAGGVSSITTTgkNETTFTATGLQPGDQYLLSVR 106
Cdd:COG3401    227 TTPTTPPSAPTGLTATADTPGSVTLSWDPVTESDATGYRVYRS-NSGDGPFTKVATV--TTTSYTDTGLTNGTTYYYRVT 303

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  107 SVTPEDTLSTPVEV----TSTTNPSPVIGLSVVNGTTQSLWIEWTSPTDTRATNytYIVTVTNVTGGVSWTKSTNKDKTT 182
Cdd:COG3401    304 AVDAAGNESAPSNVvsvtTDLTPPAAPSGLTATAVGSSSITLSWTASSDADVTG--YNVYRSTSGGGTYTKIAETVTTTS 381

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  183 FTATGLQPGDQYQLSVRSVTPEDTLSTPVEVTNTTNPSPVTGLSVVNGTTEslrikWTRPTDTRASDYTYRVTVTNVTGG 262
Cdd:COG3401    382 YTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVDA-----VPLTDVAGATAAASAASNPGVSAA 456

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  263 VSWTESTSKDKTTFTATGLQPGDQYQLSVQSVTPEDTVSSPLEVTNTTNPSPVTGLSVVNGTTQSLTiewtrPTDTRATN 342
Cdd:COG3401    457 VLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGA-----PDGTPNVT 531

                          330       340
                   ....*....|....*....|....*.
gi 1822521637  343 YTYIVTVTNVTGGVSSTTVTSRGETT 368
Cdd:COG3401    532 GASPVTVGASTGDVLITDLVSLTTSA 557

FhaB

Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ...

29-896

1.13e-09

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

Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 63.25 E-value: 1.13e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637   29 NVTDPSPVTGLSVVSRTTDSLRIEWTSPNDTRASNYTYNVTVTNVAGGVSSITTTGKNETTFTATGLQPGDQYLLSVRSV 108
Cdd:COG3210    820 TITINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATAASITVGSGGVATSTGTANAGTLTNL 899

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  109 TPEDTLSTPVEVTSTTNPSPVIGLSVVNGTTQSLWIEWTSPTDTRATNYTYIVTVTNVTGGVSWTKSTNKDKTTFTATGL 188
Cdd:COG3210    900 GTTTNAASGNGAVLATVTATGTGGGGLTGGNAAAGGTGAGNGTTALSGTQGNAGLSAASASDGAGDTGASSAAGSSAVGT 979

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  189 QPGDQYQLSVRSVTPEDTLSTPVEVTNTTNPSPVT-GLSVVNGTTESLRIKWTRPTDTRASDYTYRVTVTNVTGGVSWTE 267
Cdd:COG3210    980 SANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAiVAGGNGVTGTTGTASATGTGTAATAGGQNGVGVNASGISGGNAA 1059

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  268 STSKDKTTFTATGLQPGDQYQLSVQSVTPEDTVSSPLEVTNTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRATNYTYIV 347
Cdd:COG3210   1060 ALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGATGTSGGTTTSTGGVTASKVGGTTTVGATGTSTASTEA 1139

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  348 TVTNVTGGVSSTTVTSRGETTFKATGLQPGDQYLLSVQSVTPEDTWSTPVEVTNTTNPSPVTGLTVVNGTTHSLRIEWTP 427
Cdd:COG3210   1140 AGAGTLTGLVAVSAVAGGASSASAGDTTAVAAATTTTTGSAINGGADSAATEGTAGTDLKGGDSTGGSTTTIGTTNVTTT 1219

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  428 PTDTRATNYTYKVTVTNVAGGVSSTTITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPVTGLSVV 507
Cdd:COG3210   1220 TTLTASDTGNTTATGGSSAGQTGSFVAAGSASGTGDATTGATAGAVSNGATSTVAGNAGATATGSTVDIGSTSATSAGGS 1299

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  508 NGTTQSLTIEWTSPNDTTASNYIYNVTVTNVTGGVSWTESTSKGETTFTATGLQPGDQYQLSVQSVTPEDTLSTPEQVTN 587
Cdd:COG3210   1300 LDTTGNTAGANGATVGTGIGGTTATGTAVAAVNSGGVNAGGGTINTTAANTGLNGGNGATDSAAGAGSGGAAGSLAATAG 1379

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  588 TTNPSPVTGLSVVNGTTQSLGIEWTSPTDTRASNYTYIVTVTNVTGGGRSTTVTSKGETAFTATGLQPGDQYQLSVQSVT 667
Cdd:COG3210   1380 AGTVLTGAGNNTGAEGTNAGRDGGVTTSGTGVGNNGGVSGTTVAGTTGSSATTGTGGTGNTTGTSVAGAGGGNADASAIN 1459

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  668 PEGTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYNVTVTNVTGGVSWTQSTSKDETTFTATRLQ 747
Cdd:COG3210   1460 TGNASSLGAGGSTAGNAVGGAVIGGTTTGGNGAGVAGATASNGGTSTGAGGTAGGTTAEVAKASLEGGEGTYGGSSVAEA 1539

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  748 PGDQYLLSVQSVTPEDTLSTPAQVTSTTNPSPVTGLSVVNSTTQSLRIEWTTPNNIRASNYTYNVTVTNVTDGASSTTIT 827
Cdd:COG3210   1540 GTGGGILGAVSGAGSEGGAAGGVTGSVGVGGTDGAGGDTGGADDTGAQAPTAGNTATLTLSLAEGTNAEYGGTTNVTSGT 1619

                          810       820       830       840       850       860
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1822521637  828 SKGETTFTVTGLQPGDQYRLSVRSVTPEDTWSTPAQVTSTSNPSPVSGLTVVNRTTVSIEVTWAAPTDA 896
Cdd:COG3210   1620 AGNAGATGANSNTVVTTNGGEGVLALVAGGNTTNGTTLSGAVNGAGNGWAVDLTDATLAGLGGATTAAA 1688

COG4733

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

275-784

1.19e-09

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

Pssm-ID: 443767 [Multi-domain] Cd Length: 978 Bit Score: 63.04 E-value: 1.19e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  275 TFTATGLQPGDQYQLSVQSVTPEDTVSSPLEVTNTTNPSpvtgLSVVNGTT--QSLTIEWTRPTDtrATNYTYIVTVtnv 352
Cdd:COG4733    503 TYTITAVQHAPEKYAAIDAGAFDDVPPQWPPVNVTTSES----LSVVAQGTavTTLTVSWDAPAG--AVAYEVEWRR--- 573

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  353 tGGVSSTTVTSRGETTFKATGLQPGDqYLLSVQSVTPEDT---WSTPVEVT---NTTNPSPVTGLTVVNGTTHsLRIEWT 426
Cdd:COG4733    574 -DDGNWVSVPRTSGTSFEVPGIYAGD-YEVRVRAINALGVssaWAASSETTvtgKTAPPPAPTGLTATGGLGG-ITLSWS 650

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  427 PPTDTRATnyTYKVTVTNVAGGVSSTTITNKGET-AFTATGLQPGDQYQLSVQSVtpeDTL--STPVEVTSTTNPSPVTG 503
Cdd:COG4733    651 FPVDADTL--RTEIRYSTTGDWASATVAQALYPGnTYTLAGLKAGQTYYYRARAV---DRSgnVSAWWVSGQASADAAGI 725

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  504 LSVVNGttQSLTIEWTSPNDTTASNyiynvtvtnvtggvswteSTSKGETTFTATGLQPGDQYQLSVQSVTPEDTLSTPE 583
Cdd:COG4733    726 LDAITG--QILETELGQELDAIIQN------------------ATVAEVVAATVTDVTAQIDTAVLFAGVATAAAIGAEA 785

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  584 QVTNTTNpSPVTGLSVVNGTTQSLGIEWTSPTDTRASNYTYIVTVTNVTGGGRSTTVTSKGETAFTATGLQPGDQYQLSV 663
Cdd:COG4733    786 RVAATVA-ESATAAAATGTAADAAGDASGGVTAGTSGTTGAGDTAASTTRVAAAVVLAGVVVYGDAIIESGNTGDIVATG 864

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  664 QSVTPEGTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEwtrptdTRASNYTYNVTVTNVTGGVSWTQSTSKdETTFTA 743
Cdd:COG4733    865 DIASAAAGAVATTVSGTTAADVSAVADSTAASLTAIVIAA------TTIIDAIGDGTTREPAGDIGASGGAQG-FAVTIV 937

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 1822521637  744 TRLQPGDQYLLSVQSVTPEDTLSTPAQVTSTTNPSPVTGLS 784
Cdd:COG4733    938 GSFDGAGAVATVDAGQSVVDGVGTAVEAANGTETAAGGGSQ 978

PHA02740

protein tyrosine phosphatase; Provisional

1126-1379

2.06e-09

protein tyrosine phosphatase; Provisional

Pssm-ID: 165107 [Multi-domain] Cd Length: 298 Bit Score: 60.37 E-value: 2.06e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1126 EEYQGLANVGTNQSKEAFQVPDNKVK--NRYTNIFPYDVARVKLdrqpnSSSSDYINASYMPGYHLDKAFIAAQGPLPNT 1203
Cdd:PHA02740    29 KEYRAIVPEHEDEANKACAQAENKAKdeNLALHITRLLHRRIKL-----FNDEKVLDARFVDGYDFEQKFICIINLCEDA 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1204 VVDFWRMVWEQKTKVIVMLTNCVEQNRVkcERYWPMDmSSCLygdIVVNIVSEETSPEWTTRKFNVK------KTGcpEP 1277
Cdd:PHA02740   104 CDKFLQALSDNKVQIIVLISRHADKKCF--NQFWSLK-EGCV---ITSDKFQIETLEIIIKPHFNLTllsltdKFG--QA 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1278 RTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDY---LNKNRA----GLPVVHCSAGVGRTGTLIALDYLLQRIEKEAVVD 1350
Cdd:PHA02740   176 QKISHFQYTAWPADGFSHDPDAFIDFFCNIDDLcadLEKHKAdgkiAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLS 255

                          250       260
                   ....*....|....*....|....*....
gi 1822521637 1351 VYGIVHNMRMSRTCMVQTENQYIFLHQCI 1379
Cdd:PHA02740   256 IANALKKVRQKKYGCMNCLDDYVFCYHLI 284

FN3

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

498-574

3.91e-09

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 54.93 E-value: 3.91e-09

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521637   498 PSPVTGLSVVNGTTQSLTIEWTSPNDTTASNYIYNVTVTNVTGGVSWTE-STSKGETTFTATGLQPGDQYQLSVQSVT 574
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEvNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

fn3

Fibronectin type III domain;

220-295

4.43e-09

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 54.73 E-value: 4.43e-09

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521637  220 SPVTGLSVVNGTTESLRIKWTRPTDTRASDYTYRVTVTNVTGGVSWTEST-SKDKTTFTATGLQPGDQYQLSVQSVT 295
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITvPGTTTSVTLTGLKPGTEYEVRVQAVN 77

FN3

Fibronectin type 3 domain [General function prediction only];

30-501

6.32e-09

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 60.40 E-value: 6.32e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637   30 VTDPSPVTGLSVVSRTTDSLRIEWTSPNDTRASNYTYNVTVTNVAGGVSSITTTGKNETTFTATGLQPGDQYLLSVRSVT 109
Cdd:COG3401    149 GVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTT 228

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  110 PEDTLSTPVEVTSTTNPSPVIGLSvvngttqslwieWTSPTDTRATNytYIVTVTNVTGGvSWTKSTNKDKTTFTATGLQ 189
Cdd:COG3401    229 PTTPPSAPTGLTATADTPGSVTLS------------WDPVTESDATG--YRVYRSNSGDG-PFTKVATVTTTSYTDTGLT 293

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  190 PGDQYQLSVRSVTPEDTLSTPVEV----TNTTNPSPVTGLSVVNGTTESLRIKWTRPTDTRASdyTYRVTVTNVTGGVSW 265
Cdd:COG3401    294 NGTTYYYRVTAVDAAGNESAPSNVvsvtTDLTPPAAPSGLTATAVGSSSITLSWTASSDADVT--GYNVYRSTSGGGTYT 371

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  266 TESTSKDKTTFTATGLQPGDQYQLSVQSVTPEDTVSSPLEVTNTTNPSPVTGLSVVNGTTqsltiEWTRPTDTRATNYTY 345
Cdd:COG3401    372 KIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASAASGESLTASVD-----AVPLTDVAGATAAAS 446

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  346 IVTVTNVTGGVSSTTVTSRGETTFKATGLQPGDQYLLSVQSVTPEDTWSTPVEVTNTTNPSPVTGLTVVNGTTHSLRIEW 425
Cdd:COG3401    447 AASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDG 526

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1822521637  426 TPPTDTRATNYTYKVTVTNVAGGVSSTTITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPV 501
Cdd:COG3401    527 TPNVTGASPVTVGASTGDVLITDLVSLTTSASSSVSGAGLGSGNLYLITTLGGSLLTTTSTNTNDVAGVHGGTLLV 602

FN3

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

219-295

1.42e-08

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 53.00 E-value: 1.42e-08

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521637   219 PSPVTGLSVVNGTTESLRIKWTRPTDTRASDYTYRVTVTNVTGGVSWTE-STSKDKTTFTATGLQPGDQYQLSVQSVT 295
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEvNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

RhsA

COG3209

Uncharacterized conserved protein RhaS, contains 28 RHS repeats [General function prediction ...

54-811

3.15e-08

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

Pssm-ID: 442442 [Multi-domain] Cd Length: 1103 Bit Score: 58.61 E-value: 3.15e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637   54 TSPNDTRASNYTYNVTVTNVAGGVSSITTTGKNETTFTATGLQPGDQYLLSVRSVTPEDTLSTPVEVTSTTNPSPVIGLS 133
Cdd:COG3209      8 GGTTGASSTLLAATNAGGGTAVTNAGSTVLLAKGGLSTAAAAGGAATLTARSASTTDVVGTLTGAGGTSAGGVTALGDAS 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  134 VVNGTTQSLWIEWTSPTDTRATNYTYIVTVTNVTGGVSWTKSTNKDKTTFTATGLQPGDQYQLSVRSVTPEDTLSTPVEV 213
Cdd:COG3209     88 AAGGGYVGGAAAGGGATLTGLAAATASAGRLVSTGAGAGGTVTAATGGTLGATAGSATTGSTDGGRGGVAVTGLAGGGAS 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  214 TNTTNPSPVTGLSVVNGTTESLRIKWTRPTDTRASDYTYRVTVTNVTGGVSWTESTSKDKTTFTATGLQPGDQYQLSVQS 293
Cdd:COG3209    168 AYGLTLGGAAAGPATGVGTGAVTLATGLAGSALLALGSGAILGGLAGAYSGSATTATGTALGTPASVAATVTGSATGAAG 247

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  294 VTPEDTVSSPLEVTNTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRATNYTYIVTVTNVTGGVSSTTVTSRGETTFKATG 373
Cdd:COG3209    248 AGAAVATAATTLGGTTGAGTGASGAGLDASTGTGGAGGSNAAATAGGLGGAGLGSGGAGGGGTAGGTTTAAGTTGTAAVS 327

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  374 LQPGDQYLLSVQSVTPEDTWSTPVEVTNTTNPSPVTGLTVVNGTTHSLRIEWTPPTDTRATNYTYKVTVTNVAGGVSSTT 453
Cdd:COG3209    328 GAADAGTTTTTGTGTGGTTTTVGGGGSLTLGGYGAAGGLTTSVGAGGGGSTSGSTTTVGGGGTATGSGGGSSTTGVGAGT 407

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  454 ITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTSPNDTTASNYIYNV 533
Cdd:COG3209    408 TTTSTTGGDGGPATAAGALTAGGTATGTGTGGGGTTAGTDATTTTGGAGASGTLTTTGGAATGATTGGGTEAGTGGGTLT 487

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  534 TVTNVTGGVSWTESTSKGETTFTATGLQPGDQYQLSVQSVTPEDTLSTPEQVTNTTNPSPVTGLSVVNGTTQSLGIEWTS 613
Cdd:COG3209    488 SGSAGATTLGTDTTLDDTLGGTTTTTAGARGLVVTTGTTLTLGTTTTATLSATDATGTGDTTTTGTVGTGTSTGTGGTGT 567

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  614 PTDTRASNYTYIVTVTNVTGGGRSTTVTSKGETAFTATGLQPGDQYQLSVQSVTPEGTLSTPVEVTSTTNPSPVTGLSVV 693
Cdd:COG3209    568 VTTTGDGTGGASTTTGTTGGTATTTTVTTTTTTSTAGTTTTTTSGYTRAGLTLTLGTGTASGLERATASTGSTTGGTTGT 647

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  694 NGTTQSLTIEWTRPTDTRASNYTYNVTVTNVTGGVswTQSTSKDETTFTATRLQPGDQYLLSVQSVTPEDTLSTPAQVTS 773
Cdd:COG3209    648 GVTTTGTTTTRATGTTGTGTGVTAGLTTLATGGTT--VGGGTGTTSTATTGATTGGTETGTTVTTLAGGTTTRLGTTTTG 725

                          730       740       750
                   ....*....|....*....|....*....|....*...
gi 1822521637  774 TTNPSPVTGLSVVNSTTQSLRIEWTTPNNIRASNYTYN 811
Cdd:COG3209    726 GGGGTTTDGTGTGGTTGTLTTTSTTTTTTAGALTYTYD 763

fn3

Fibronectin type III domain;

871-949

3.68e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 52.03 E-value: 3.68e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  871 SPVSGLTVVNRTTVSIEVTWAAPTDARAPEYTYRITLANVTRRGRGA-IDTGPGVTTFTVTNLVPGVEYELRLQSVTPAG 949
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNeITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80

FN3

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

405-481

4.24e-08

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 51.85 E-value: 4.24e-08

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521637   405 PSPVTGLTVVNGTTHSLRIEWTPPTDTRATNYTYKVTVTNVAGGVSSTTITNKG-ETAFTATGLQPGDQYQLSVQSVT 481
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPsSTSYTLTGLKPGTEYEFRVRAVN 78

FN3

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

870-958

4.65e-08

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 52.11 E-value: 4.65e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  870 PSPVSGLTVVNRTTVSIEVTWAAPTDARAPEYTYRITLANVTRRGRGAIDTGPG-VTTFTVTNLVPGVEYELRLQSVTPA 948
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEVEVTPGsETSYTLTGLKPGTEYEFRVRAVNGG 80

                           90
                   ....*....|..
gi 1822521637  949 GT--RSSPETVR 958
Cdd:cd00063     81 GEspPSESVTVT 92

FN3

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

126-202

4.82e-08

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 51.85 E-value: 4.82e-08

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521637   126 PSPVIGLSVVNGTTQSLWIEWTSPTDTRATNYTYIVTVTNVTGGVSWTK-STNKDKTTFTATGLQPGDQYQLSVRSVT 202
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEvNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

FN3

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

870-949

5.80e-08

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 51.46 E-value: 5.80e-08

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637   870 PSPVSGLTVVNRTTVSIEVTWAAPTDARAPEYTYRITLANVTRRGRGA-IDTGPGVTTFTVTNLVPGVEYELRLQSVTPA 948
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKeVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80


                    .
gi 1822521637   949 G 949
Cdd:smart00060   81 G 81

fn3

Fibronectin type III domain;

778-853

6.82e-08

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 51.26 E-value: 6.82e-08

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521637  778 SPVTGLSVVNSTTQSLRIEWTTPNNIRASNYTYNVTVTNVTDGASSTTIT-SKGETTFTVTGLQPGDQYRLSVRSVT 853
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITvPGTTTSVTLTGLKPGTEYEVRVQAVN 77

FN3

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

33-124

7.72e-08

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 51.34 E-value: 7.72e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637   33 PSPVTGLSVVSRTTDSLRIEWTSPNDTRASNYTYNVTVTNV-AGGVSSITTTGKNETTFTATGLQPGDQYLLSVRSVTpE 111
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKgSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVN-G 79

                           90
                   ....*....|...
gi 1822521637  112 DTLSTPVEVTSTT 124
Cdd:cd00063     80 GGESPPSESVTVT 92

CDC14

COG2453

Protein-tyrosine phosphatase [Signal transduction mechanisms];

1276-1377

9.32e-08

Protein-tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 441989 [Multi-domain] Cd Length: 140 Bit Score: 52.67 E-value: 9.32e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1276 EPRTITQFHFTsWPDHGVPKTTdkllQFQRMMRDYLNKNRAGLPV-VHCSAGVGRTGTLIALdYLLQR-IE-KEAVVDVy 1352
Cdd:COG2453     44 EEAGLEYLHLP-IPDFGAPDDE----QLQEAVDFIDEALREGKKVlVHCRGGIGRTGTVAAA-YLVLLgLSaEEALARV- 116

                           90       100
                   ....*....|....*....|....*
gi 1822521637 1353 givhnmRMSRTCMVQTENQYIFLHQ 1377
Cdd:COG2453    117 ------RAARPGAVETPAQRAFLER 135

PTP_DSP_cys

cd14494

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

1300-1377

9.61e-08

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

Pssm-ID: 350344 [Multi-domain] Cd Length: 113 Bit Score: 51.58 E-value: 9.61e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1300 LLQFQRMMRDYLNKNRAGLPV-VHCSAGVGRTGTLIALDYLLQRIEkeavvDVYGIVHNMRMSRT-CMVQTENQYIFLHQ 1377
Cdd:cd14494     39 LAMVDRFLEVLDQAEKPGEPVlVHCKAGVGRTGTLVACYLVLLGGM-----SAEEAVRIVRLIRPgGIPQTIEQLDFLIK 113

FN3

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

777-853

1.03e-07

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 50.69 E-value: 1.03e-07

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521637   777 PSPVTGLSVVNSTTQSLRIEWTTPNNIRASNYTYNVTVTNVTDGASSTTITSKG-ETTFTVTGLQPGDQYRLSVRSVT 853
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPsSTSYTLTGLKPGTEYEFRVRAVN 78

CDKN3-like

cd14505

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

1280-1377

1.04e-07

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

Pssm-ID: 350355 [Multi-domain] Cd Length: 163 Bit Score: 53.04 E-value: 1.04e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1280 ITQFHFtSWPDHGVPkttDKLLQFQRMMRDYLNKNRAGLPVV-HCSAGVGRTGTLIA--LDYLLQRIEKEAVVDvygIVh 1356
Cdd:cd14505     73 ITWHHL-PIPDGGVP---SDIAQWQELLEELLSALENGKKVLiHCKGGLGRTGLIAAclLLELGDTLDPEQAIA---AV- 144

                           90       100
                   ....*....|....*....|.
gi 1822521637 1357 nmRMSRTCMVQTENQYIFLHQ 1377
Cdd:cd14505    145 --RALRPGAIQTPKQENFLHQ 163

fn3

Fibronectin type III domain;

406-481

1.27e-07

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 50.49 E-value: 1.27e-07

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521637  406 SPVTGLTVVNGTTHSLRIEWTPPTDTRATNYTYKVTVTNVAGGVSSTTITNKG-ETAFTATGLQPGDQYQLSVQSVT 481
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITVPGtTTSVTLTGLKPGTEYEVRVQAVN 77

FN3

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

405-496

1.37e-07

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 50.57 E-value: 1.37e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  405 PSPVTGLTVVNGTTHSLRIEWTPPTDTRATNYTYKVTVTNVAGGVSST-TITNKGETAFTATGLQPGDQYQLSVQSVTpE 483
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEvEVTPGSETSYTLTGLKPGTEYEFRVRAVN-G 79

                           90
                   ....*....|...
gi 1822521637  484 DTLSTPVEVTSTT 496
Cdd:cd00063     80 GGESPPSESVTVT 92

FN3

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

684-760

1.45e-07

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 50.31 E-value: 1.45e-07

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521637   684 PSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYNVTVTNVTGGVSWTQ-STSKDETTFTATRLQPGDQYLLSVQSVT 760
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEvNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

FN3

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

777-866

1.77e-07

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 50.57 E-value: 1.77e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  777 PSPVTGLSVVNSTTQSLRIEWTTPNNIRASNYTYNVTVTNVTDGASST-TITSKGETTFTVTGLQPGDQYRLSVRSVTpE 855
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEvEVTPGSETSYTLTGLKPGTEYEFRVRAVN-G 79

                           90
                   ....*....|.
gi 1822521637  856 DTWSTPAQVTS 866
Cdd:cd00063     80 GGESPPSESVT 90

FN3

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

312-403

1.99e-07

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 50.19 E-value: 1.99e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  312 PSPVTGLSVVNGTTQSLTIEWTRPTDTRATNYTYIVTVTNVTGGVSST-TVTSRGETTFKATGLQPGDQYLLSVQSVTpE 390
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEvEVTPGSETSYTLTGLKPGTEYEFRVRAVN-G 79

                           90
                   ....*....|...
gi 1822521637  391 DTWSTPVEVTNTT 403
Cdd:cd00063     80 GGESPPSESVTVT 92

PTP_PTEN-like

cd14497

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

1276-1360

2.39e-07

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

Pssm-ID: 350347 [Multi-domain] Cd Length: 160 Bit Score: 51.81 E-value: 2.39e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1276 EPRTITQFHFT----SWPDHGVPkTTDKLLQFQRMMRDYLNKNRAGLPVVHCSAGVGRTGTLIA--LDYLLQRI-EKEAV 1348
Cdd:cd14497     52 EYDDDSKFEGRvlhyGFPDHHPP-PLGLLLEIVDDIDSWLSEDPNNVAVVHCKAGKGRTGTVICayLLYYGQYStADEAL 130

                           90
                   ....*....|..
gi 1822521637 1349 VDVYgivhNMRM 1360
Cdd:cd14497    131 EYFA----KKRF 138

FN3

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

219-310

3.12e-07

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 49.80 E-value: 3.12e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  219 PSPVTGLSVVNGTTESLRIKWTRPTDTRASDYTYRVTVTNVTGGVSWT-ESTSKDKTTFTATGLQPGDQYQLSVQSVTpE 297
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEvEVTPGSETSYTLTGLKPGTEYEFRVRAVN-G 79

                           90
                   ....*....|...
gi 1822521637  298 DTVSSPLEVTNTT 310
Cdd:cd00063     80 GGESPPSESVTVT 92

FN3

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

33-109

3.47e-07

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 49.15 E-value: 3.47e-07

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521637    33 PSPVTGLSVVSRTTDSLRIEWTSPNDTRASNYTYNVTVTNVAGGVSSIT-TTGKNETTFTATGLQPGDQYLLSVRSVT 109
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEvNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

FN3

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

591-679

4.88e-07

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 49.03 E-value: 4.88e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  591 PSPVTGLSVVNGTTQSLGIEWTSPTDTRASNYTYIVTVTNVTGGGRST-TVTSKGETAFTATGLQPGDQYQLSVQSVTP- 668
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEvEVTPGSETSYTLTGLKPGTEYEFRVRAVNGg 80

                           90
                   ....*....|..
gi 1822521637  669 -EGTLSTPVEVT 679
Cdd:cd00063     81 gESPPSESVTVT 92

COG4625

Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ...

347-837

5.30e-07

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

Pssm-ID: 443664 [Multi-domain] Cd Length: 900 Bit Score: 54.40 E-value: 5.30e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  347 VTVTNVTGGVSSTTVTSRGETTFKATGLQPGDQYLLSVQSVTPEDTwSTPVEVTNTTNPSPVTGLTVVNGTTHSLRIEWT 426
Cdd:COG4625      1 GGGGGGGGGGGGGGGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGG-GGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  427 PPTDTRATNYTYKVTVTNVAGGVSSTTITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPVTGLSV 506
Cdd:COG4625     80 GGGGGGGGGGTGGVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGG 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  507 VNGTTQSLTIEWTSPNDTTASNYIYNVTVTNVTGGVSWTESTSKGETTFTATGLQPGDQYQLSVQSVTPEDTLSTpeqVT 586
Cdd:COG4625    160 AGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGGGGG---GG 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  587 NTTNPSPVTGLSVVNGTTQSLGIEWTSPTDTRASNYTYIVTVTNVTGGGRSTTVTSKGETAFTATGLQPGDQYQLSVQSV 666
Cdd:COG4625    237 GGGGGGGGGGGAGGGGGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGGGGGGGGGGGGGGGGGGGGGGGG 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  667 TPEGTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYNVTVTNVTGGVSWTQSTSKDETTFTATRL 746
Cdd:COG4625    317 GGGGGGGGGGGGGGGGGAGGGGGSGGAGAGGGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGA 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  747 QPGDQYLLSVQSVTPEDTLSTPAQVTSTTNPSPVTGLSVVNSTTQSLRIEWTTPNNIRASNYTYNVTVTNVTDGASSTTI 826
Cdd:COG4625    397 GGGGGGGGAGGTGGGGAGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGSGAGTL 476

                          490
                   ....*....|.
gi 1822521637  827 TSKGETTFTVT 837
Cdd:COG4625    477 TLTGNNTYTGT 487

fn3

Fibronectin type III domain;

499-574

5.46e-07

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 48.57 E-value: 5.46e-07

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521637  499 SPVTGLSVVNGTTQSLTIEWTSPNDTTASNYIYNVTVTNVTGGVSWTEST-SKGETTFTATGLQPGDQYQLSVQSVT 574
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITvPGTTTSVTLTGLKPGTEYEVRVQAVN 77

FN3

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

312-388

6.81e-07

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 48.38 E-value: 6.81e-07

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521637   312 PSPVTGLSVVNGTTQSLTIEWTRPTDTRATNYTYIVTVTNVTGGVSSTTV-TSRGETTFKATGLQPGDQYLLSVQSVT 388
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVnVTPSSTSYTLTGLKPGTEYEFRVRAVN 78

FN3

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

591-670

6.94e-07

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 48.38 E-value: 6.94e-07

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637   591 PSPVTGLSVVNGTTQSLGIEWTSPTDTRASNYTYIVTVTNVTGGGRSTTVTSKG-ETAFTATGLQPGDQYQLSVQSVTPE 669
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTPsSTSYTLTGLKPGTEYEFRVRAVNGA 80


                    .
gi 1822521637   670 G 670
Cdd:smart00060   81 G 81

fn3

Fibronectin type III domain;

34-109

1.51e-06

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 47.41 E-value: 1.51e-06

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521637   34 SPVTGLSVVSRTTDSLRIEWTSPNDTRASNYTYNVTVTNVAGGVSSIT-TTGKNETTFTATGLQPGDQYLLSVRSVT 109
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEiTVPGTTTSVTLTGLKPGTEYEVRVQAVN 77

fn3

Fibronectin type III domain;

685-760

1.54e-06

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 47.41 E-value: 1.54e-06

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521637  685 SPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYNVTVTNVTGGVSW-TQSTSKDETTFTATRLQPGDQYLLSVQSVT 760
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWnEITVPGTTTSVTLTGLKPGTEYEVRVQAVN 77

RhsA

COG3209

Uncharacterized conserved protein RhaS, contains 28 RHS repeats [General function prediction ...

27-718

2.07e-06

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

Pssm-ID: 442442 [Multi-domain] Cd Length: 1103 Bit Score: 52.45 E-value: 2.07e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637   27 SQNVTDPSPVTGLSVVSRTTDSLRIEWTSPNDTRASNYTYNVTVTNVAGGVSSITTTGKNETTFTATGLQPGDQYLLSVR 106
Cdd:COG3209     77 AGGVTALGDASAAGGGYVGGAAAGGGATLTGLAAATASAGRLVSTGAGAGGTVTAATGGTLGATAGSATTGSTDGGRGGV 156

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  107 SVTPEDTLSTPVEVTSTTNPSPVIGLSVVNGTTqSLWIEWTSPTDTRATNYTYIVTVTNVTGGVSWTKSTNKDKTTFTAT 186
Cdd:COG3209    157 AVTGLAGGGASAYGLTLGGAAAGPATGVGTGAV-TLATGLAGSALLALGSGAILGGLAGAYSGSATTATGTALGTPASVA 235

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  187 GLQPGDQYQLSVRSVTPEDTLSTPVEVTNTTNPSPVTGLSVVNGTTESLRIKWTRPTDTRASDYTYRVTVTNVTGGVSWT 266
Cdd:COG3209    236 ATVTGSATGAAGAGAAVATAATTLGGTTGAGTGASGAGLDASTGTGGAGGSNAAATAGGLGGAGLGSGGAGGGGTAGGTT 315

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  267 ESTSKDKTTFTATGLQPGDQYQLSVQSVTPEDTVSSPLEVTNTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRATNYTYI 346
Cdd:COG3209    316 TAAGTTGTAAVSGAADAGTTTTTGTGTGGTTTTVGGGGSLTLGGYGAAGGLTTSVGAGGGGSTSGSTTTVGGGGTATGSG 395

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  347 VTVTNVTGGVSSTTVTSRGETTFKATGLQPGDQYLLSVQSVTPEDTWSTPVEVTNTTNPSPVTGLTVVNGTTHSLRIEWT 426
Cdd:COG3209    396 GGSSTTGVGAGTTTTSTTGGDGGPATAAGALTAGGTATGTGTGGGGTTAGTDATTTTGGAGASGTLTTTGGAATGATTGG 475

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  427 PPTDTRATNYTYKVTVTNVAGGVSSTTITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPVTGLSV 506
Cdd:COG3209    476 GTEAGTGGGTLTSGSAGATTLGTDTTLDDTLGGTTTTTAGARGLVVTTGTTLTLGTTTTATLSATDATGTGDTTTTGTVG 555

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  507 VNGTTQSLTIEWTSPNDTTASNYIYNVTVTNVTGGVSWTESTSKGETTFTATGLQPGDQYQLSVQSVTPEDTLSTPEQVT 586
Cdd:COG3209    556 TGTSTGTGGTGTVTTTGDGTGGASTTTGTTGGTATTTTVTTTTTTSTAGTTTTTTSGYTRAGLTLTLGTGTASGLERATA 635

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  587 NTTNPSPVTGLSVVNGTTQSLGIEWTSPTDTRASNYTYIVTVTNVTGGGRSTTVTSKGETAFTATGLQPGDQYQLSVQSV 666
Cdd:COG3209    636 STGSTTGGTTGTGVTTTGTTTTRATGTTGTGTGVTAGLTTLATGGTTVGGGTGTTSTATTGATTGGTETGTTVTTLAGGT 715

                          650       660       670       680       690
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1822521637  667 TPEGTLSTPVEVTSTTNPSPVTGLSVVNGTTQSltieWTRPTDTRASNYTYN 718
Cdd:COG3209    716 TTRLGTTTTGGGGGTTTDGTGTGGTTGTLTTTS----TTTTTTAGALTYTYD 763

AidA

COG3468

Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular ...

409-838

2.23e-06

Autotransporter adhesin AidA [Cell wall/membrane/envelope biogenesis, Intracellular trafficking, secretion, and vesicular transport];

Pssm-ID: 442691 [Multi-domain] Cd Length: 846 Bit Score: 52.26 E-value: 2.23e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  409 TGLTVVNGTTHSLRIEWTPPTDTRATNYTYKVTVTNVAGGVSSTTITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLST 488
Cdd:COG3468      8 GATGLGGGGTGGGGGLGGTGGGNAGLGIGNGGGGGAASGSGAGGVAGNGGGGGGGAGGGGGGAGSGGGLAGAGSGGTGGN 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  489 PVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTSPNDTTASNYIYNVTVTNVTGGVSWTESTSKGETTFTATGLQPGDQYQL 568
Cdd:COG3468     88 STGGGGGNSGTGGTGGGGGGGGSGNGGGGGGGGGGGGTGGGGGGGTGSAGGGGGGGGGGTGVGGTGAAAAGGGTGSGGGG 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  569 SVQSVTPEDTLSTPEQVTNTTNPSPVTGLSVVNGTTQSLGIEWTSpTDTRASNYTYIVTVTNVTGGGRSTTVTSKGETAF 648
Cdd:COG3468    168 SGGGGGAGGGGGGGAGGSGGAGSTGSGAGGGGGGSGGGGGAAGTG-GGGGGGGGAGGATGGAGSGGNTGGGVGGGGGSAG 246

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  649 TATGLQPGDQYQLSVQSVTPEGTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYNVTVTNVTGGV 728
Cdd:COG3468    247 GTGGGGLTGGGAAGTGGGGGGTGTGSGGGGGGGANGGGSGGGGGASGTGGGGTASTGGGGGGGGGNGGGGGGGSNAGGGS 326

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  729 SWTQSTSKDETTFTATrlqpGDQYLLSVQSVTPEDTLSTPAQVTSTTNPSPVTGLSVVNSTTQSlriewTTPNNIRASNY 808
Cdd:COG3468    327 GGGGGGGGGGGGGGTT----LNGAGSAGGGTGAALAGTGGSGSGGGGGGGSGGGGGAGGGGANT-----GSDGVGTGLTT 397

                          410       420       430
                   ....*....|....*....|....*....|
gi 1822521637  809 TYNVTVTNVTDGASSTTITSKGETTFTVTG 838
Cdd:COG3468    398 GGTGNNGGGGVGGGGGGGLTLTGGTLTVNG 427

FhaB

Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ...

120-838

2.37e-06

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

Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 52.46 E-value: 2.37e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  120 VTSTTNPSPVIGLSVVNGTTQSLWIEWTSPTDTRATNYTYIVTVTNVTGGVSWTKSTNKDKTTFTATGLQPGDQYQLSVR 199
Cdd:COG3210      4 GLAGTTGNKTIGVDIAVTTTAATLGSNTAGTSGLNILGSGGVGTAGGIASNAGTTASTSGGSGTAGGVGNTSASTGGIGA 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  200 SVTPEDTLSTPVEVTNTTNPSPVTGLSVVNGTTESLRIKWTRPTDTRASDYTYRVTVTNVTGGVSWTESTSKDKTTFTAT 279
Cdd:COG3210     84 AAANTAGTLETGLTSNIGGGSVNGSNSTGNGTLTTTAASATTGNNTGGTTTSSTNTVTTLGGTTTGNTVLSTSGAGNNTN 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  280 GLQPGDQYQLSVQSVTPEDTVSSPLEVTNTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRATNYTYIVTVTNVTGGVSST 359
Cdd:COG3210    164 TNNSSSGTNIGNSIPTTGGSLNVVAANPTGVTGVGGALINATAGVLANAGGGTAGGVASANSTLTGGVVAAGTGAGVIST 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  360 TVTSRGETTFKATGLQPGDQYLLSVQSVTPEDTWSTPVEVTNTTNPSPVTGLTVVNGTTHSLRIEWTPPTDTRATNYTYK 439
Cdd:COG3210    244 GGTDISSLSVAAGAGTGGAGGTGNAGNTTIGTTVTGTNATGSNTAGASSGDTTTNGTSSVTGAGGTGVLGGGTAAGITTT 323

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  440 VTVTNVAGGVSSTTITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWT 519
Cdd:COG3210    324 NTVGGNGDGNNTTANSGAGLVSGGTGGNNGTTGTGAGSGLTGTGNGGGLTTAGAGTVASTVGTATASTGNASSTTVLGSG 403

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  520 SPNDTTASNYIYNVTVTNVTGGVSWTESTskgeTTFTATGLQPGDQYQLSVQSVTPEDTLSTPEQVTNTTNPSPVTGLSV 599
Cdd:COG3210    404 SLATGNTGTTIAGNGGSANAGGFTTTGGV----LGITGNGTVTGGTIGGLTGSGTTNGAGLSGNTDVSGTGTVTNSAGNT 479

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  600 VNGTTQSLGIEWTSPTDTRASNYTYIVTVTNVTGGGRSTTVTSKGeTAFTATGLQPGDQYQLSVQSVTPEGTLSTPVEVT 679
Cdd:COG3210    480 TSATTLAGGGIGTVTTNATISNNAGGDANGIATGLTGITAGGGGG-GNATSGGTGGDGTTLSGSGLTTTVSGGASGTTAA 558

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  680 STTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYNVTVTNVTGGVSWTQSTSKDETTFTATRLQPGDQYLLSVQSV 759
Cdd:COG3210    559 SGSNTANTLGVLAATGGTSNATTAGNSTSATGGTGTNSGGTVLSIGTGSAGATGTITLGAGTSGAGANATGGGAGLTGSA 638

                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1822521637  760 TPEDTLSTPAQVTSTTNPSPVTGLSVVNSTTQSLRIEWTTPNNIRASNYTYNVTVTNVTDGASSTTITSKGETTFTVTG 838
Cdd:COG3210    639 VGAALSGTGSGTTGTASANGSNTTGVNTAGGTGGGTTGTVTSGATGGTTGTTLNAATGGTLNNAGNTLTISTGSITVTG 717

FN3

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

126-217

2.94e-06

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 47.11 E-value: 2.94e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  126 PSPVIGLSVVNGTTQSLWIEWTSPTDTRATNYTYIVTVTNVTGGvSWTK--STNKDKTTFTATGLQPGDQYQLSVRSVTp 203
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSG-DWKEveVTPGSETSYTLTGLKPGTEYEFRVRAVN- 78

                           90
                   ....*....|....
gi 1822521637  204 EDTLSTPVEVTNTT 217
Cdd:cd00063     79 GGGESPPSESVTVT 92

fn3

Fibronectin type III domain;

313-388

3.02e-06

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 46.64 E-value: 3.02e-06

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521637  313 SPVTGLSVVNGTTQSLTIEWTRPTDTRATNYTYIVTVTNVTGGVSSTTVT-SRGETTFKATGLQPGDQYLLSVQSVT 388
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITvPGTTTSVTLTGLKPGTEYEVRVQAVN 77

PRK15375

type III secretion system effector GTPase-activating protein SptP;

1201-1335

5.16e-06

type III secretion system effector GTPase-activating protein SptP;

Pssm-ID: 185273 [Multi-domain] Cd Length: 535 Bit Score: 50.96 E-value: 5.16e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1201 PNTVVDFWRMVWEQKTKVIVMLTNcveQNRVKCERYWPMDMSSCLYGDIVVNIVSEETSPEW-TTRKFNVKKTGCPEPRT 1279
Cdd:PRK15375   346 PDALEAHMKMLLEKECSCLVVLTS---EDQMQAKQLPPYFRGSYTFGEVHTNSQKVSSASQGeAIDQYNMQLSCGEKRYT 422

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1822521637 1280 ITQFHFTSWPDHGVPKTTDKLLQFQRMMRdylNKNRAG----------LPVVHCSAGVGRTGTLIA 1335
Cdd:PRK15375   423 IPVLHVKNWPDHQPLPSTDQLEYLADRVK---NSNQNGapgrsssdkhLPMIHCLGGVGRTGTMAA 485

fn3

Fibronectin type III domain;

592-667

5.54e-06

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 45.87 E-value: 5.54e-06

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521637  592 SPVTGLSVVNGTTQSLGIEWTSPTDTRASNYTYIVTVTNVTGGGRSTTVT-SKGETAFTATGLQPGDQYQLSVQSVT 667
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWNEITvPGTTTSVTLTGLKPGTEYEVRVQAVN 77

COG4733

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

71-671

5.96e-06

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

Pssm-ID: 443767 [Multi-domain] Cd Length: 978 Bit Score: 51.10 E-value: 5.96e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637   71 TNVAGGVSSITttGKNETTFTATGLQPGDQYLlsvRSVTPEDTlstPVEVTSTTNPSPVIGLSVVNGTTQSLWIEWTSPT 150
Cdd:COG4733    412 RRIGGRVSSVD--GRVVTLDRPVTMEAGDRYL---RVRLPDGT---SVARTVQSVAGRTLTVSTAYSETPEAGAVWAFGP 483

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  151 DTRATNYTYIVTVTNVTGGvswtkstnkdktTFTATGLQPGDQYQLSVRSVTPEDTLSTPVEVTNTTNPSpvtgLSVVNG 230
Cdd:COG4733    484 DELETQLFRVVSIEENEDG------------TYTITAVQHAPEKYAAIDAGAFDDVPPQWPPVNVTTSES----LSVVAQ 547

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  231 TTE--SLRIKWTRPTDT------------------------------RASDYTYRVTVTNVTGGVS-WTESTSkdkttFT 277
Cdd:COG4733    548 GTAvtTLTVSWDAPAGAvayevewrrddgnwvsvprtsgtsfevpgiYAGDYEVRVRAINALGVSSaWAASSE-----TT 622

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  278 ATGLqpgdqyqlsvqsvtpedtvssplevtnTTNPSPVTGLSVVNGTTQsLTIEWTRPTDTRATnYTYIVTVTNVTGGVS 357
Cdd:COG4733    623 VTGK---------------------------TAPPPAPTGLTATGGLGG-ITLSWSFPVDADTL-RTEIRYSTTGDWASA 673

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  358 STTVTSRGETTFKATGLQPGDQYLLSVQSVtpeDTWSTPVEVTNTTNPSPVTGLTVVNGTTHSLRIEWTPPTDTRATNYT 437
Cdd:COG4733    674 TVAQALYPGNTYTLAGLKAGQTYYYRARAV---DRSGNVSAWWVSGQASADAAGILDAITGQILETELGQELDAIIQNAT 750

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  438 YKVTVTNVAGGVSSTTITNKGETAFTATglqpgdqyqlSVQSVTPEDTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIE 517
Cdd:COG4733    751 VAEVVAATVTDVTAQIDTAVLFAGVATA----------AAIGAEARVAATVAESATAAAATGTAADAAGDASGGVTAGTS 820

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  518 WTSPNDTTASNYIYNVTVTNVTGGVSWTESTSKGETTFtatglQPGDQYQLSVQSVTPEDTLSTPEQVTNTTNPSPVTGL 597
Cdd:COG4733    821 GTTGAGDTAASTTRVAAAVVLAGVVVYGDAIIESGNTG-----DIVATGDIASAAAGAVATTVSGTTAADVSAVADSTAA 895

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1822521637  598 SVVNGTTQSLGIEWTSPTDTRASNYTYIVTVTNVTG--GGRSTTVTSKGETAFTATGLQPGDQYQLSVQSVTPEGT 671
Cdd:COG4733    896 SLTAIVIAATTIIDAIGDGTTREPAGDIGASGGAQGfaVTIVGSFDGAGAVATVDAGQSVVDGVGTAVEAANGTET 971

FN3

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

498-574

6.00e-06

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 45.95 E-value: 6.00e-06

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822521637  498 PSPVTGLSVVNGTTQSLTIEWTSPNDTTASNYIYNVTVTNVTGGVSWT-ESTSKGETTFTATGLQPGDQYQLSVQSVT 574
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSGDWKEvEVTPGSETSYTLTGLKPGTEYEFRVRAVN 78

PTP_PTPDC1

cd14506

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

1283-1376

8.03e-06

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

Pssm-ID: 350356 [Multi-domain] Cd Length: 206 Bit Score: 48.50 E-value: 8.03e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1283 FHFTSWPDHGVPkTTDKLLQFQRMMRDYLNKnrAGLPVVHCSAGVGRTGTLIA--LDYLLQRIEKEAVVDVygivhnmRM 1360
Cdd:cd14506     79 FYNFGWKDYGVP-SLTTILDIVKVMAFALQE--GGKVAVHCHAGLGRTGVLIAcyLVYALRMSADQAIRLV-------RS 148

                           90
                   ....*....|....*.
gi 1822521637 1361 SRTCMVQTENQYIFLH 1376
Cdd:cd14506    149 KRPNSIQTRGQVLCVR 164

FN3

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

684-775

8.04e-06

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 45.57 E-value: 8.04e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  684 PSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYNVTVTNVTGGvSWTQ--STSKDETTFTATRLQPGDQYLLSVQSVTp 761
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITGYVVEYREKGSG-DWKEveVTPGSETSYTLTGLKPGTEYEFRVRAVN- 78

                           90
                   ....*....|....
gi 1822521637  762 EDTLSTPAQVTSTT 775
Cdd:cd00063     79 GGGESPPSESVTVT 92

FN3

Fibronectin type 3 domain [General function prediction only];

646-1041

8.21e-06

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 50.39 E-value: 8.21e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  646 TAFTATGLQPGDQYQLSVQSVTPEGTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTR-ASNYTYNVTVTNV 724
Cdd:COG3401      4 SYLTSLDAGIAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTgGRAGTTSGVAAVA 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  725 TGGVSWTQSTSKDETTFTATRLQPGDQYLLSVQSVTPEDTLSTPAQVTSTTNPSPVTGLSVVNSTTQSLRIEWTTPNNIR 804
Cdd:COG3401     84 VAAAPPTATGLTTLTGSGSVGGATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSV 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  805 ASNYTYNVTVTNVTDGASSTTITSKGETTFTVTG-LQPGDQYRLSVRSVTPEDTWSTPAQV---TSTSNPSPVSGLTVVN 880
Cdd:COG3401    164 AGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGdIEPGTTYYYRVAATDTGGESAPSNEVsvtTPTTPPSAPTGLTATA 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  881 RTTVSIEVTWAAPTDARAPEYT-YRITLANVTRRGRGAIDTgpgvTTFTVTNLVPGVEYELRLQSVTPAGTRSSP----E 955
Cdd:COG3401    244 DTPGSVTLSWDPVTESDATGYRvYRSNSGDGPFTKVATVTT----TSYTDTGLTNGTTYYYRVTAVDAAGNESAPsnvvS 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  956 TVRNATIPAAISDFRCSGSTGYMVEAKWSQPNGQFSMFKALTYDGEQLISNLSLGK--EERSLTVDNLQPGRTYTLRV-- 1031
Cdd:COG3401    320 VTTDLTPPAAPSGLTATAVGSSSITLSWTASSDADVTGYNVYRSTSGGGTYTKIAEtvTTTSYTDTGLTPGTTYYYKVta 399

                          410
                   ....*....|
gi 1822521637 1032 VTESGNTSSQ 1041
Cdd:COG3401    400 VDAAGNESAP 409

PTP_VSP_TPTE

cd14510

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

1289-1376

8.82e-06

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

Pssm-ID: 350360 [Multi-domain] Cd Length: 177 Bit Score: 47.74 E-value: 8.82e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1289 PDHGVPkTTDKLLQFQRMMRDYLNKNRAGLPVVHCSAGVGRTGTLIA---LDYLLQRIEKEAvVDVYGivhNMRMSRTCM 1365
Cdd:cd14510     82 DDHNVP-TLDEMLSFTAEVREWMAADPKNVVAIHCKGGKGRTGTMVCawlIYSGQFESAKEA-LEYFG---ERRTDKSVS 156

                           90
                   ....*....|....*.
gi 1822521637 1366 -----VQTENQYIFLH 1376
Cdd:cd14510    157 skfqgVETPSQSRYVG 172

fn3

Fibronectin type III domain;

127-202

2.16e-05

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 44.33 E-value: 2.16e-05

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521637  127 SPVIGLSVVNGTTQSLWIEWTSPTDTRATNYTYIVTVTNVTGGVSW-TKSTNKDKTTFTATGLQPGDQYQLSVRSVT 202
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNGPITGYEVEYRPKNSGEPWnEITVPGTTTSVTLTGLKPGTEYEVRVQAVN 77

FhaB

Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ...

321-968

3.03e-05

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

Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 48.99 E-value: 3.03e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  321 VNGTTQSLTIEWTRPTDTRATNYTYIVTVTNVTGGVSSTTVTSRGETTFKATGLQPGDQYLLSVQSVTPEDTWSTPVEVT 400
Cdd:COG3210    814 VTGSGGTITINTATTGLTGTGDTTSGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATAASITVGSGGVATSTGTANA 893

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  401 NTTNPSPVTGLTVVNGTTHSLriewTPPTDTRATNYTYKVTVTNVAGGVSSTTITNKGETAFTATGLQPGDQYQLSVQSV 480
Cdd:COG3210    894 GTLTNLGTTTNAASGNGAVLA----TVTATGTGGGGLTGGNAAAGGTGAGNGTTALSGTQGNAGLSAASASDGAGDTGAS 969

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  481 TPEDTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTSPNDTTASNYIYNVTVTNVTGGVSWTESTSKGETTFTATGL 560
Cdd:COG3210    970 SAAGSSAVGTSANSAGSTGGVIAATGILVAGNSGTTASTTGGSGAIVAGGNGVTGTTGTASATGTGTAATAGGQNGVGVN 1049

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  561 QPGDQYQLSVQSVTPEDTLSTPEQVTNTTNPSPVTGLSVVNGTTQSLGIEWTSPTDTRASNYTYIVTVTNVTGGGRSTTV 640
Cdd:COG3210   1050 ASGISGGNAAALTASGTAGTTGGTAASNGGGGTAQASGAGTTHTLGGITNGGATGTSGGTTTSTGGVTASKVGGTTTVGA 1129

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  641 TSKGETAFTATGLQPGDQYQLSVQSVTPEGTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYNVT 720
Cdd:COG3210   1130 TGTSTASTEAAGAGTLTGLVAVSAVAGGASSASAGDTTAVAAATTTTTGSAINGGADSAATEGTAGTDLKGGDSTGGSTT 1209

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  721 VTNVTGGVSWTQSTSKDETTFTATRLQPGDQYLLSVQSVTPEDTLSTPAQVTSTTNPSPVTGLSVVNSTTQSLRIEWTTP 800
Cdd:COG3210   1210 TIGTTNVTTTTTLTASDTGNTTATGGSSAGQTGSFVAAGSASGTGDATTGATAGAVSNGATSTVAGNAGATATGSTVDIG 1289

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  801 NNIRASNYTYNVTVTNVTDGASSTTITSKGETTFTVTGLQPGDqyRLSVRSVTPEDTWSTPAQVTSTSNPSPVSGLTVVN 880
Cdd:COG3210   1290 STSATSAGGSLDTTGNTAGANGATVGTGIGGTTATGTAVAAVN--SGGVNAGGGTINTTAANTGLNGGNGATDSAAGAGS 1367

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  881 RTTVSIEVTWAAPTDARAPEYTYRITLANVTRRGRGAIDTGPGVTTFTVTNLVPGVEYELRLQSVTPAGTRSSPETVRNA 960
Cdd:COG3210   1368 GGAAGSLAATAGAGTVLTGAGNNTGAEGTNAGRDGGVTTSGTGVGNNGGVSGTTVAGTTGSSATTGTGGTGNTTGTSVAG 1447


                   ....*...
gi 1822521637  961 TIPAAISD 968
Cdd:COG3210   1448 AGGGNADA 1455

FN3

Fibronectin type 3 domain [General function prediction only];

29-280

5.23e-05

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 47.69 E-value: 5.23e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637   29 NVTDPSPVTGLSVVSRTTDSLRIEWTSPNDTRASNYtyNVTVTNVAGGVSSITTTGKNETTFTATGLQPGDQYLLSVRSV 108
Cdd:COG3401    323 DLTPPAAPSGLTATAVGSSSITLSWTASSDADVTGY--NVYRSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAV 400

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  109 T---PEDTLSTPVEVTSTTNPSPVIGLSVVNGTTQSLWIEWTSPT----DTRATNYTYIVTVTNVTGGVSWTKSTNKDKT 181
Cdd:COG3401    401 DaagNESAPSEEVSATTASAASGESLTASVDAVPLTDVAGATAAAsaasNPGVSAAVLADGGDTGNAVPFTTTSSTVTAT 480

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  182 T---------FTATGLQPGDQYQLSVRSVTPEDTLSTPVEVTNTTNPSPVTGLSVVNGTTESLRIKWTRPTDTRASDYTY 252
Cdd:COG3401    481 TtdtttanlsVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTTSASSS 560

                          250       260
                   ....*....|....*....|....*...
gi 1822521637  253 RVTVTNVTGGVSWTESTSKDKTTFTATG 280
Cdd:COG3401    561 VSGAGLGSGNLYLITTLGGSLLTTTSTN 588

COG4733

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

824-1039

7.68e-05

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

Pssm-ID: 443767 [Multi-domain] Cd Length: 978 Bit Score: 47.25 E-value: 7.68e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  824 TTITSKGETTFTVTGLQPGDQYRLSVRSVTPEDTWSTPAQVTSTSNPSpvsgLTVVNRTTV--SIEVTWAAPTDARAPEY 901
Cdd:COG4733    494 VSIEENEDGTYTITAVQHAPEKYAAIDAGAFDDVPPQWPPVNVTTSES----LSVVAQGTAvtTLTVSWDAPAGAVAYEV 569

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  902 TYRITLANVTRRGRgaidtgPGVTTFTVTNLVPGvEYELRLQSVTPAGTRSSPETVRNATI------PAAISDFRCSGST 975
Cdd:COG4733    570 EWRRDDGNWVSVPR------TSGTSFEVPGIYAG-DYEVRVRAINALGVSSAWAASSETTVtgktapPPAPTGLTATGGL 642

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  976 GyMVEAKWSQPNG----QFSMFKALTYDGEQLISNLSLGKeERSLTVDNLQPGRTYTLRV--VTESGNTS 1039
Cdd:COG4733    643 G-GITLSWSFPVDadtlRTEIRYSTTGDWASATVAQALYP-GNTYTLAGLKAGQTYYYRAraVDRSGNVS 710

COG4625

Uncharacterized conserved protein, contains a C-terminal beta-barrel porin domain [Function ...

131-651

1.09e-04

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

Pssm-ID: 443664 [Multi-domain] Cd Length: 900 Bit Score: 46.70 E-value: 1.09e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  131 GLSVVNGTTQSLWIEWTSPTDTRATNYTYIVTVTNVTGGVSWTKSTNKDKTTFTATGLQPGDQYQLSVRSVTPEDTLSTP 210
Cdd:COG4625      2 GGGGGGGGGGGGGGGTGGGGAGGGGGAGGGAGGGGAGGGGGGGGGGGGAGGGGGGGGTGGGGGGGGGGGGGGAGGGGGGG 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  211 VEVTNTTNPSPVTGLSVVNGTTESLRIKWTRPTDTRASDYTYRVTVTNVTGGVSWTESTSKDKTTFTATGLQPGDQYQLS 290
Cdd:COG4625     82 GGGGGGGGTGGVGGGGGGGGGGGGGGGGGGGGGGGGSAGGGGGGAGGAGGGGGGGAGGGGGGGGGGGAGGGGGGGAGGAG 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  291 VQSVTPEDTVSSPLEVTNTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRATNYTYIVTVTNVTGGVSSTTVTSRGETTFK 370
Cdd:COG4625    162 GGGGGGGGGGGGGGGGGGGGGGGGGGGGGGGNGGGGGGGGGGGGGGGGGGGGAGGGGGGGGGGGGGGGGGGGGGGGGGGG 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  371 ATGLQPGDQYLLSVQSVTPEDTWSTPVEVTNTTNPSPVTGLTVVNGTTHSLRIeWTPPTDTRATNYTYKVTVTNVAGGVS 450
Cdd:COG4625    242 GGGGGGAGGGGGGGGGNGGGGGAGGGGGGGGGGSGGGGGGGGGGGSGGGGGGG-GGGGGGGGGGGGGGGGGGGGGGGGGG 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  451 STTITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTSPNDTTASNYI 530
Cdd:COG4625    321 GGGGGGGGGGGGGAGGGGGSGGAGAGGGGAGGGGAGGGGGGGTGGGGGGGGGGGGGSGGGGAGGGGGSGGGGGGGAGGGG 400

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  531 YNVTVTNVTGGVSWTESTSKGETTFTATGLQPGDQYQLSVQSVTPEDTLSTPEQVTNTTNPSPVTGLSVVNGTtqslgie 610
Cdd:COG4625    401 GGGGAGGTGGGGAGGGGGAAGGGGGGTGAGGGGGGGGTGAGGGGATGGGGGGGGGAGGSGGGAGAGGGSGSGA------- 473

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 1822521637  611 wtsPTDTRASNYTYIVTVTNVTGGGRSTTVTSKGETAFTAT 651
Cdd:COG4625    474 ---GTLTLTGNNTYTGTTTVNGGGNYTQSAGSTLAVEVDAA 511

DUSP23

cd14504

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

1282-1335

1.34e-04

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

Pssm-ID: 350354 [Multi-domain] Cd Length: 142 Bit Score: 43.42 E-value: 1.34e-04

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1822521637 1282 QFHFTSWPDHGVPkTTDKLLQFQRMMRDYLNKNRAGLpvVHCSAGVGRTGTLIA 1335
Cdd:cd14504     51 RYHHIPIEDYTPP-TLEQIDEFLDIVEEANAKNEAVL--VHCLAGKGRTGTMLA 101

CDC14_C

cd14499

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

1321-1342

3.12e-04

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

Pssm-ID: 350349 [Multi-domain] Cd Length: 174 Bit Score: 43.21 E-value: 3.12e-04

                           10        20
                   ....*....|....*....|..
gi 1822521637 1321 VHCSAGVGRTGTLIALdYLLQR 1342
Cdd:cd14499    114 VHCKAGLGRTGTLIAC-YLMKH 134

Chi1

Chitinase [Carbohydrate transport and metabolism];

392-598

5.92e-04

Chitinase [Carbohydrate transport and metabolism];

Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 44.36 E-value: 5.92e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  392 TWSTPVEVTNTTNPSPVTGLTVVNGTTHSLRIEWTPPTDTRATNYTYKVTVTNVAGGVSSTTITNKGETAFTATGLQPGD 471
Cdd:COG3469      1 SSSVSTAASPTAGGASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  472 QYQLSV-------QSVTPEDTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTSPNDTTASNYIYNVTVTNVTGGVSW 544
Cdd:COG3469     81 TATAAAaaatstsATLVATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTETAT 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1822521637  545 TESTSKGETTFTATGLQPGDQYQlSVQSVTPEDTLSTPEQVTNTTNPSPVTGLS 598
Cdd:COG3469    161 GGTTTTSTTTTTTSASTTPSATT-TATATTASGATTPSATTTATTTGPPTPGLP 213

Herpes_BLLF1

pfam05109

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...

270-748

9.68e-04

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

Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 43.75 E-value: 9.68e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  270 SKDKTTFTATGLQPGDQYQLSVQSVTPEDtvssplevTNTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTR---------- 339
Cdd:pfam05109  312 SQDMPTNTTDITYVGDNATYSVPMVTSED--------ANSPNVTVTAFWAWPNNTETDFKCKWTLTSGTPsgcenisgaf 383

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  340 ATNYTYIVTVTNVtGGVSSTTVTSRGETTFKATGLQpgdqyllSVQSVTPEDTWSTP-VEVTNTTNPSPVTGLTvvnGTT 418
Cdd:pfam05109  384 ASNRTFDITVSGL-GTAPKTLIITRTATNATTTTHK-------VIFSKAPESTTTSPtLNTTGFAAPNTTTGLP---SST 452

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  419 HsLRIEWTPPTDTRATNYTYKVTVTNVAGGVS-STTITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPveVTSTTN 497
Cdd:pfam05109  453 H-VPTNLTAPASTGPTVSTADVTSPTPAGTTSgASPVTPSPSPRDNGTESKAPDMTSPTSAVTTPTPNATSP--TPAVTT 529

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  498 PSPVTGLSVVNGTTQSLTIEWTSPNDTTASNYIYNVTVTNVTGGVSWTESTSKGET-TFTATGLQPGDQY-QLSVQSVTP 575
Cdd:pfam05109  530 PTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPTPNATIPTLGKTSPTSAVTTpTPNATSPTVGETSpQANTTNHTL 609

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  576 EDTLSTPEQVT---NTTNPSPVTGLSVVNGTTQSLGIEWTSPTDT-------RASNYTYIVTVTNVTGGGRSTTVTSKGE 645
Cdd:pfam05109  610 GGTSSTPVVTSppkNATSAVTTGQHNITSSSTSSMSLRPSSISETlspstsdNSTSHMPLLTSAHPTGGENITQVTPAST 689

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  646 TAFTATGLQPGDQYQLSVQSVTP--EGTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYT------- 716
Cdd:pfam05109  690 STHHVSTSSPAPRPGTTSQASGPgnSSTSTKPGEVNVTKGTPPKNATSPQAPSGQKTAVPTVTSTGGKANSTTggkhttg 769

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 1822521637  717 ----YNVTVTNVTGGVSWTQSTSKDETTF----TATRLQP 748
Cdd:pfam05109  770 hgarTSTEPTTDYGGDSTTPRTRYNATTYlppsTSSKLRP 809

FhaB

Large exoprotein involved in heme utilization or adhesion [Intracellular trafficking, ...

27-933

1.05e-03

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

Pssm-ID: 442443 [Multi-domain] Cd Length: 1698 Bit Score: 43.60 E-value: 1.05e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637   27 SQNVTDPSPVTGLSVVSRTTDSLRIEWTSPNDTRASNYTYNVTVTNVAGGVSSITTTGKNETTFTATGLQPGDQYLLSVR 106
Cdd:COG3210    278 TGTNATGSNTAGASSGDTTTNGTSSVTGAGGTGVLGGGTAAGITTTNTVGGNGDGNNTTANSGAGLVSGGTGGNNGTTGT 357

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  107 SVTPEDTLSTPVEVTSTTNPSPVIGLSVVNGTTQSLWIEWTSPTDTRATNYTYIVTVTNVTGGVSWTKSTNKDKTTFTAT 186
Cdd:COG3210    358 GAGSGLTGTGNGGGLTTAGAGTVASTVGTATASTGNASSTTVLGSGSLATGNTGTTIAGNGGSANAGGFTTTGGVLGITG 437

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  187 GLQPGDQYQLSVRSVTPEDTLSTPVEVTNTTNPSPVTGLSVVNGTTESLRIKWTRPTDTRASDYTYRVTVTNVTGGVSWT 266
Cdd:COG3210    438 NGTVTGGTIGGLTGSGTTNGAGLSGNTDVSGTGTVTNSAGNTTSATTLAGGGIGTVTTNATISNNAGGDANGIATGLTGI 517

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  267 ESTSKDKTTFTATGLQPGDQYQLSVQSVTPEDTVSSPLEVTNTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRATNYTYI 346
Cdd:COG3210    518 TAGGGGGGNATSGGTGGDGTTLSGSGLTTTVSGGASGTTAASGSNTANTLGVLAATGGTSNATTAGNSTSATGGTGTNSG 597

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  347 VTVTNVTGGVSSTTVTSRGETTFKATGLQPGDQYLLSVQSVTPEDTWSTPVEVTNTTNPSPVTGLTVVNGTTHSLRIEWT 426
Cdd:COG3210    598 GTVLSIGTGSAGATGTITLGAGTSGAGANATGGGAGLTGSAVGAALSGTGSGTTGTASANGSNTTGVNTAGGTGGGTTGT 677

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  427 PPTDTRATNYTYKVTVTNVAGGVSSTTITNKGETAFTATG----LQPGDQYQLSVQSVTPEDTLSTPVEVTST-----TN 497
Cdd:COG3210    678 VTSGATGGTTGTTLNAATGGTLNNAGNTLTISTGSITVTGqigaLANANGDTVTFGNLGTGATLTLNAGVTITsgnagTL 757

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  498 PSPVTGLSVVNGTTQSLTIE--------WTSPNDTTASNYIYNVTVTNVTGGVSWTESTSKGETTFTATGLQPGDQYQLS 569
Cdd:COG3210    758 SIGLTANTTASGTTLTLANAngntsagaTLDNAGAEISIDITADGTITAAGTTAINVTGSGGTITINTATTGLTGTGDTT 837

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  570 VQSVTPEDTLSTPEQVTNTTNPSPVTGLSVVNGTTQSLGIEWTSPTDTRASNYTYIVTVTNVTGGGRSTTVTSKGETAFT 649
Cdd:COG3210    838 SGAGGSNTTDTTTGTTSDGASGGGTAGANSGSLAATAASITVGSGGVATSTGTANAGTLTNLGTTTNAASGNGAVLATVT 917

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  650 ATGLQPGDQYQLSVQSVTPEGTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYNVTVTNVTGGVS 729
Cdd:COG3210    918 ATGTGGGGLTGGNAAAGGTGAGNGTTALSGTQGNAGLSAASASDGAGDTGASSAAGSSAVGTSANSAGSTGGVIAATGIL 997

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  730 WTQSTSKDETTFTATRLQPGDQYLLSVQSVTPEDTLSTPAQVTSTTNPSPVTGLSVVNSTTQSLRIEWTTPNNIRASNYT 809
Cdd:COG3210    998 VAGNSGTTASTTGGSGAIVAGGNGVTGTTGTASATGTGTAATAGGQNGVGVNASGISGGNAAALTASGTAGTTGGTAASN 1077

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  810 YNVTVTNVTDGASSTTITSKGETTFTVTGLQPGDQYRLSVRSVTPEDTWSTPAQVTSTSNPSPVSGLTVVNRTTVSIEVT 889
Cdd:COG3210   1078 GGGGTAQASGAGTTHTLGGITNGGATGTSGGTTTSTGGVTASKVGGTTTVGATGTSTASTEAAGAGTLTGLVAVSAVAGG 1157

                          890       900       910       920
                   ....*....|....*....|....*....|....*....|....
gi 1822521637  890 WAAPTDARAPEYTYRITLANVTRRGRGAIDTGPGVTTFTVTNLV 933
Cdd:COG3210   1158 ASSASAGDTTAVAAATTTTTGSAINGGADSAATEGTAGTDLKGG 1201

MJ0795

COG1361

S-layer protein MJ0795, predicted component of type IV pili-like system [General function ...

467-828

1.31e-03

S-layer protein MJ0795, predicted component of type IV pili-like system [General function prediction only];

Pssm-ID: 440972 [Multi-domain] Cd Length: 409 Bit Score: 42.76 E-value: 1.31e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  467 LQPGDQYQLSVQ----------SVTPEDTLSTPVEVTSTTNPspvTGLSVVNGTTQSLTIEWTSPNDTTASNYIYNVTVT 536
Cdd:COG1361     36 VAPGEEVTLTVTitndgtltarNVTVELEGDYPFEVKSGEQS---VGGSLPPGQSVTVTFTVTVPEDAEPGTYPIPVTVS 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  537 nvtggVSWTESTSKGETTFTATgLQPGDQYQLSVQSVTPEDTLstpeqVTNTTNPSPVTGLSVVNGTTQSLGIEWTSPTD 616
Cdd:COG1361    113 -----YSYGYTDRTETETYTVT-VKVEGEPRFEVVSVTSPDSL-----TPGDTGTLTLTIKNTGTGTAKNVTVTLTSPSG 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  617 TRASNYTYIVTVTNVTGGgRSTTVTSKGETAFTATGLQPGDQ----YQLSVQSVTPEGTLSTPVEVT-------STTNPS 685
Cdd:COG1361    182 DLTDLEPGPRPATNVVVV-LSSPVSPVGSNSVALGTLEPGESatftFKVDVSEDAEPGPYPLPLTVTyrdedgdTYSDTV 260

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  686 PVtGLSVVNgtTQSLTIEWTRPTDTRASNYTYNVTVTN--------VTGGVSWTQSTSKDETTFTATRLQPGDqyllsvq 757
Cdd:COG1361    261 TI-GVYVAP--KADFEVENVESTITAGETVTITITVTNtgnetaknVVARLSADDPLSSLDDEAFIGDLAPGE------- 330

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1822521637  758 svtpedtlSTPAQVTSTTNPSPVTGlsvvnSTTQSLRIEWTTPNNIRASNYTYNVTVTNVTDGASSTTITS 828
Cdd:COG1361    331 --------SATVTFTVSASSDATPG-----TYPITVTIRYDDDDGNTQLSDTITVPVEVTEPSSGGLLTVL 388

Chi1

Chitinase [Carbohydrate transport and metabolism];

424-647

1.49e-03

Chitinase [Carbohydrate transport and metabolism];

Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 42.82 E-value: 1.49e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  424 EWTPPTDTRATNYTYKVTVTNVAGGVSSTTITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPVTG 503
Cdd:COG3469      4 VSTAASPTAGGASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTATAT 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  504 LSVVNGTTQSLTIEWTSPNDTTASNYIYNVTVTNVTGGVSWTESTSKGETTftatglqpgdqyqlSVQSVTPEDTLSTPE 583
Cdd:COG3469     84 AAAAAATSTSATLVATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTT--------------TSGASATSSAGSTTT 149

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1822521637  584 QVTNTTNPSPVTGLSVVNGTTQSLGIEWTSPTDTRASNYtyivTVTNVTGGGRSTTVTSKGETA 647
Cdd:COG3469    150 TTTVSGTETATGGTTTTSTTTTTTSASTTPSATTTATAT----TASGATTPSATTTATTTGPPT 209

PTP_PTEN

cd14509

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

1289-1359

1.54e-03

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

Pssm-ID: 350359 [Multi-domain] Cd Length: 158 Bit Score: 40.65 E-value: 1.54e-03

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521637 1289 PDHGVPkTTDKLLQFQRMMRDYLNKNRAGLPVVHCSAGVGRTGTLIALdYLLQRIE----KEAvVDVYGI--VHNMR 1359
Cdd:cd14509     68 DDHNPP-PLELIKPFCEDVDEWLKEDEKNVAAVHCKAGKGRTGVMICC-YLLYLGKfpsaKEA-LDFYGAkrTKNKK 141

DSP_DUSP16

cd14646

dual specificity phosphatase domain of dual specificity protein phosphatase 16; Dual ...

1274-1344

1.55e-03

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

Pssm-ID: 350494 [Multi-domain] Cd Length: 145 Bit Score: 40.39 E-value: 1.55e-03

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1822521637 1274 CPEPRTITQFHFTSWPDHGvpKTTDKLLQFQRMMRDYLNKNRA--GLPVVHCSAGVGRTGTlIALDYLLQRIE 1344
Cdd:cd14646     39 CPKPDFIPESHFLRVPVND--SFCEKILPWLDKSVDFIEKAKAsnGRVLVHCLAGISRSAT-IAIAYIMKRMD 108

fn3

Fibronectin type III domain;

965-1041

1.82e-03

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 38.94 E-value: 1.82e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  965 AISDFRCSGSTGYMVEAKWSQP---NGQFSMFKaLTY---DGEQLISNLSLGKEERSLTVDNLQPGRTYTLRVVTESGNT 1038
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPpdgNGPITGYE-VEYrpkNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ...
gi 1822521637 1039 SSQ 1041
Cdd:pfam00041   81 EGP 83

Chi1

Chitinase [Carbohydrate transport and metabolism];

299-518

1.94e-03

Chitinase [Carbohydrate transport and metabolism];

Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 42.43 E-value: 1.94e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  299 TVSSPLEVTNTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRATNYTYIVTVTNVTGGVSSTTVTSRGETTfkATGLQPGD 378
Cdd:COG3469      1 SSSVSTAASPTAGGASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTA--ATSSTTST 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  379 QYLLSV---QSVTPEDTWSTPVEVTNTTNPSPVTGLTVVNGTTHSLRIEWTPPTDTRATNYTYKVTVTNVAGGVSSTTIT 455
Cdd:COG3469     79 TATATAaaaAATSTSATLVATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTTTTVSGTET 158

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1822521637  456 NKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEW 518
Cdd:COG3469    159 ATGGTTTTSTTTTTTSASTTPSATTTATATTASGATTPSATTTATTTGPPTPGLPKHVLVGYW 221

DSPc

smart00195

Dual specificity phosphatase, catalytic domain;

1296-1377

2.36e-03

Dual specificity phosphatase, catalytic domain;

Pssm-ID: 214551 [Multi-domain] Cd Length: 138 Bit Score: 39.96 E-value: 2.36e-03

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  1296 TTDKLLQFQRMMRDYLN--KNRAGLPVVHCSAGVGRTGTLIALdYLLQRiEKEAVVDVYGIVhnmRMSRTCMVQTENqyi 1373
Cdd:smart00195   56 TETKISPYFPEAVEFIEdaESKGGKVLVHCQAGVSRSATLIIA-YLMKT-RNMSLNDAYDFV---KDRRPIISPNFG--- 127


                    ....
gi 1822521637  1374 FLHQ 1377
Cdd:smart00195  128 FLRQ 131

COG4935

Regulatory P domain of the subtilisin-like proprotein convertases and other proteases ...

272-827

3.29e-03

Regulatory P domain of the subtilisin-like proprotein convertases and other proteases [Posttranslational modification, protein turnover, chaperones];

Pssm-ID: 443962 [Multi-domain] Cd Length: 641 Bit Score: 41.73 E-value: 3.29e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  272 DKTTFTATGLQPGDQYQLSVQSVTPEDTVSSPLEVTNTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRATNYTYIVTVTN 351
Cdd:COG4935     10 TGLAAAVLAAAAGTGSAATAEGGAASTATSAAVAGASAAAAAATAVGAGASSLAASAAAAAAAASGAAAGAVDAAPAAAT 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  352 VTGGVSSTTVTSRGETTFKATGLQPGDQYLLSVQSVTPEDTWSTPVEVTNTTNPSPVTGLTVVNGTTHSLRIEWTPPTDT 431
Cdd:COG4935     90 VVGAALGVVAVAGAGLAATASGAAAGAVAAAANGNTGAGPGSGGTGGGSGGAGAAAAAAALSAAGAAVGVAAVAGAAGGG 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  432 RATNYTYKVTVTNVAGGVS-STTITNKGETAFTATGLQPGDQYQLSVQSVTPEDTLSTPVEVTSTTNPSPVTGLSVVNGT 510
Cdd:COG4935    170 GGVGVAAAVGVVLGAGLVAdGGNGGGGAVAGGAAGGGGGGGGGGGLGGAAGGGGAGLAAAGGGGGGAAAAAAAGVGGLGA 249

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  511 TQSLTIEWTSPNDTTASNYIYNVTVTNVTGGVSWTESTSKGETTFTATGLQPGDQYQLSVQSVTPEDTLSTPEQVTNTTN 590
Cdd:COG4935    250 AATAAAADGGGGGGAGAAGAGGSAGAAAGGAGAGVVGAAAGGGDAALGGAVGAAGTGNAAAAAAASAGSGGGGGSAAAAG 329

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  591 PSPVTGLSVVNGTTQSLGIEWTSPTDTRASNYTYIVTVTNVTGGGRSTTVTskgetAFTATGLQPGDQYQLSVQSVTPEG 670
Cdd:COG4935    330 AAAAAAAAAAGAAAGVSGAASVVAGASGGGAGTAAAAGGGAAAAAAGGAAA-----AGAAAGAAAGAAAGAAAAGGVASA 404

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  671 TLSTPVEVTSTTNPSPVTGLSVVNGTTQSLTIEWTRPTDTRASNYTYNVTVTNVTGGVSWTQSTSKDETTFTATRLQPGD 750
Cdd:COG4935    405 AGAVGAGTAAGASATAAVSTGAASGSSTTSSTGTTATATGLGGGADAGSTSTGTGSAAGAAGGTTTATSGLASSTTAAAA 484

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822521637  751 QYLLSVQSVTPEDTLSTPAQVTSTTNPSPVTGLSVVNSTTQSLRIEWTTPNNIRASNYTYNVTVTNVTDGASSTTIT 827
Cdd:COG4935    485 AAAAGLATTAAVAAGAAGAAAAAATAASVGGATGAAGTTNSTATFSNTTDVAIPDNGPAGVTSTITVSGGGAVEDVT 561

DSPc

pfam00782

Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...

1296-1377

3.32e-03

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

Pssm-ID: 395632 [Multi-domain] Cd Length: 127 Bit Score: 39.17 E-value: 3.32e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1296 TTDKLLQFQRMMRDYLN--KNRAGLPVVHCSAGVGRTGTLIALdYLLQRiEKEAVVDVYGIVhnmRMSRTCMVQTENqyi 1373
Cdd:pfam00782   47 HETNISKYLEEAVEFIDdaRQKGGKVLVHCQAGISRSATLIIA-YLMKT-RNLSLNEAYSFV---KERRPGISPNFG--- 118


                   ....
gi 1822521637 1374 FLHQ 1377
Cdd:pfam00782  119 FKRQ 122

TpbA-like

cd14529

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

1277-1361

3.68e-03

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

Pssm-ID: 350378 [Multi-domain] Cd Length: 158 Bit Score: 39.66 E-value: 3.68e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1277 PRTITQFHFTSWPDHGVPKTTDKLLQFQRMMRDylnKNRAGlPVV-HCSAGVGRTGTLIALdYLlqriekeavvDVYG-- 1353
Cdd:cd14529     53 AAKIDGVKYVNLPLSATRPTESDVQSFLLIMDL---KLAPG-PVLiHCKHGKDRTGLVSAL-YR----------IVYGgs 117

                           90
                   ....*....|.
gi 1822521637 1354 ---IVHNMRMS 1361
Cdd:cd14529    118 keeANEDYRLS 128

DSP_MKP

cd14512

dual specificity phosphatase domain of mitogen-activated protein kinase phosphatase; ...

1272-1342

4.64e-03

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

Pssm-ID: 350362 [Multi-domain] Cd Length: 136 Bit Score: 39.00 E-value: 4.64e-03

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1822521637 1272 TGCPEPRTITQFHFTSWP--DHgvpkTTDKLLQFQRMMRDYLN--KNRAGLPVVHCSAGVGRTGTlIALDYLLQR 1342
Cdd:cd14512     35 NTCPNPDFIGLFHYKRIPvnDS----FCQNISPWFDEAIEFIEeaKASNGGVLVHCLAGISRSAT-IAIAYLMKR 104

DUF4959

pfam16323

Domain of unknown function (DUF4959); This family consists of uncharacterized proteins around ...

213-307

5.26e-03

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

Pssm-ID: 465093 [Multi-domain] Cd Length: 106 Bit Score: 38.00 E-value: 5.26e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  213 VTNTTNPSPVTGLSVVNGTTESLrIKWTRPTDtraSDYTYRVTVTNVTGGVSWTESTSKDKTTFTATGLQPGDQYQLSVQ 292
Cdd:pfam16323   13 GTDGTAPGPVTNVKVKNIPGGAT-ISYTLPDD---PDLLYVKAVYTIRNGKEREVKASYYTDSLTVEGFGDTGEYEVKLY 88

                           90
                   ....*....|....*
gi 1822521637  293 SVTPEDTVSSPLEVT 307
Cdd:pfam16323   89 AVSRSENESEPVEVK 103

DSP_DUSP11

cd17665

dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar ...

1289-1334

5.52e-03

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

Pssm-ID: 350503 Cd Length: 169 Bit Score: 39.18 E-value: 5.52e-03

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1822521637 1289 PDHGVPKTtDKLLQFQRMMRDYLNKNRA--GLPVVHCSAGVGRTGTLI 1334
Cdd:cd17665     85 PGHQVPDD-KTIQSFKDAVKDFLEKNKDndKLIGVHCTHGLNRTGYLI 131

DSP_MKP_classIII

cd14568

dual specificity phosphatase domain of class III mitogen-activated protein kinase phosphatase; ...

1268-1359

6.35e-03

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

Pssm-ID: 350416 [Multi-domain] Cd Length: 140 Bit Score: 38.55 E-value: 6.35e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637 1268 NVKKTgCPEPRTITQFHFTSWPDHGVPKttDKLLQFQRMMRDYLNKNRA--GLPVVHCSAGVGRTGTlIALDYLLQRIeK 1345
Cdd:cd14568     32 NVSNT-CPKPDFIPDSHFLRIPVNDSYC--EKLLPWLDKAVEFIEKARAsnKRVLVHCLAGISRSAT-IAIAYIMKHM-R 106

                           90
                   ....*....|....
gi 1822521637 1346 EAVVDVYGIVHNMR 1359
Cdd:cd14568    107 MSLDDAYRFVKEKR 120

REJ

pfam02010

REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor ...

506-810

8.39e-03

REJ domain; The REJ (Receptor for Egg Jelly) domain is found in PKD1, and the sperm receptor for egg jelly Swiss:Q26627. The function of this domain is unknown. The domain is 600 amino acids long so is probably composed of multiple structural domains. There are six completely conserved cysteine residues that may form disulphide bridges. This region contains tandem PKD-like domains.

Pssm-ID: 366875 [Multi-domain] Cd Length: 448 Bit Score: 40.18 E-value: 8.39e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  506 VVNGTTQSLTIEWTSPNDTTASNYIYNVTVTNVTGGVSWTESTS-KGETTFTATGLQPGDQYQLSV-------------Q 571
Cdd:pfam02010  114 VDPGSSSGLTYLWSCRRSSSGDNPLLNNDPVCFSDQNEGTLLQStSSSLTIPASTLQANVTYTFKLtvskgsrnsasttQ 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  572 SVT------PEDTLSTPEQVTNTTNPSPVTGLSVVNGTT-----QSLGIEWTSPTdtrasNYTYIVTVTNVTgggrSTTV 640
Cdd:pfam02010  194 TILvvdgnpPIIILSCISNCNRKNNPVDRLVLLASTCLNcssdlSDVTYRWLSLG-----SENTSLVLDQLN----SQTS 264

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  641 TSKGETAFT--ATGLQPGDQYQLSVQSVTPEGTLSTPVEVTSTTNPSPVTGLSVVNGT-----TQSLTIEWTRPTDTRAS 713
Cdd:pfam02010  265 TGRSGPYLVikAGVLQSGVSYRFTLIVTVYPGLVSGLASISFITNAPPTGGTCSVTPTegtalETKFTVTCQGWTDDDLP 344

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822521637  714 NYTYNVTVTNVTGGVSWTQSTSKDETTFTATRLQPGD---QYLLSVQsVTPEDTLSTPAQVTSTTNPSPVT----GLSVV 786
Cdd:pfam02010  345 LTYQFGDISFREASEEWFLLYEGSSQISISTFLPPGLpanDYQVTVV-VVVYDSLGAATSVSLTITVTPPSssdeLLYFL 423

                          330       340
                   ....*....|....*....|....
gi 1822521637  787 NSTTQSLRIEWTTPNNIRASNYTY 810
Cdd:pfam02010  424 LGTTSDLSALLQSGDPQQAAQLIL 447

Chi1