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Conserved domains on  [gi|1838351042|ref|XP_033929193|]
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receptor-type tyrosine-protein phosphatase kappa-like [Melopsittacus undulatus]

Protein Classification

fibronectin type III domain-containing protein( domain architecture ID 12877517)

fibronectin type III (FN3) domain-containing protein may be involved in specific interactions with other molecules through its FN3 domain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
865-1094 2.35e-110

Protein-tyrosine phosphatase;


:

Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 347.31  E-value: 2.35e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  865 NQSKNRYKNIIPYDHCRVVLQPSDTGNDYINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQN 944
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  945 KTKCEQYWP---EQEQIYGDFTVTL-NNTRTTTGLITRIFSLHKAGCGFPRVVEQFHYLLWPDHGVPRNSAQLLCLVDVV 1020
Cdd:pfam00102   81 REKCAQYWPeeeGESLEYGDFTVTLkKEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLRKV 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1838351042 1021 NKRALEAPAGPVVVHCSAGIGRTGTFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYEVVLE 1094
Cdd:pfam00102  161 RKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1127-1388 2.47e-57

Protein tyrosine phosphatase, catalytic domain;


:

Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 199.04  E-value: 2.47e-57
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  1127 LEKEFKALQKFseLFQLLPCREAEKPTNQPKNRKPGILPADSCRPILMSSLNADGspGYINAVFVNTYTEEDRLIITQMP 1206
Cdd:smart00194    2 LEEEFEKLDRL--KPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGS--DYINASYIDGPNGPKAYIATQGP 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  1207 FPNTVVDFWALVWDYTCTAVVVLNQLQELD-ETYAEFWPMQGEAA--YGRFHVQFISEEPGAGFTAWTLALTNKQQPKkp 1283
Cdd:smart00194   78 LPSTVEDFWRMVWEQKVTVIVMLTELVEKGrEKCAQYWPDEEGEPltYGDITVTLKSVEKVDDYTIRTLEVTNTGCSE-- 155

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  1284 PLEVRFWQLKDWPmKQHLPPHPATIISLLGNVEtHHRQSRDGHILITCWDGASRSGIFCAAGFLCEQIQSEGLVDVSQAV 1363
Cdd:smart00194  156 TRTVTHYHYTNWP-DHGVPESPESILDLIRAVR-KSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIV 233

                           250       260
                    ....*....|....*....|....*
gi 1838351042  1364 RMLKRRRRQLIKDVEQYGLCYELAL 1388
Cdd:smart00194  234 KELRSQRPGMVQTEEQYIFLYRAIL 258
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 513-591 2.40e-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.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 38.63  E-value: 2.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  513 PDKPEQLWLDPSTGS---LSWEPLPSCKGEIIGYQLNITARSaQDRALLELERLRLSGSVTAHPLPahgPGTSYVVTVRG 589
Cdd:cd00063      1 PSPPTNLRVTDVTSTsvtLSWTPPEDDGGPITGYVVEYREKG-SGDWKEVEVTPGSETSYTLTGLK---PGTEYEFRVRA 76


                   ..
gi 1838351042  590 LT 591
Cdd:cd00063     77 VN 78
 
Name Accession Description Interval E-value
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
865-1094 2.35e-110

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 347.31  E-value: 2.35e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  865 NQSKNRYKNIIPYDHCRVVLQPSDTGNDYINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQN 944
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  945 KTKCEQYWP---EQEQIYGDFTVTL-NNTRTTTGLITRIFSLHKAGCGFPRVVEQFHYLLWPDHGVPRNSAQLLCLVDVV 1020
Cdd:pfam00102   81 REKCAQYWPeeeGESLEYGDFTVTLkKEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLRKV 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1838351042 1021 NKRALEAPAGPVVVHCSAGIGRTGTFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYEVVLE 1094
Cdd:pfam00102  161 RKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
841-1094 5.67e-107

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 339.25  E-value: 5.67e-107
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042   841 GRLGEYQQLSS--SLMHPCNAGKELCNQSKNRYKNIIPYDHCRVVLQPSDT-GNDYINASYVDSYRSPRFFIAAQGPLPG 917
Cdd:smart00194    1 GLEEEFEKLDRlkPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGeGSDYINASYIDGPNGPKAYIATQGPLPS 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042   918 TVLDFWQMVWQEKTSVIVMLTGLVEQNKTKCEQYWPE---QEQIYGDFTVTLNNTRTTTGLITRIFSLHKAGCGFPRVVE 994
Cdd:smart00194   81 TVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDeegEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVT 160

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042   995 QFHYLLWPDHGVPRNSAQLLCLVDVVNKRAlEAPAGPVVVHCSAGIGRTGTFIALDFLLKMGKAEGKVDVFHCVQRLREQ 1074
Cdd:smart00194  161 HYHYTNWPDHGVPESPESILDLIRAVRKSQ-STSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQ 239

                           250       260
                    ....*....|....*....|
gi 1838351042  1075 RISMVQTKEQYTFLYEVVLE 1094
Cdd:smart00194  240 RPGMVQTEEQYIFLYRAILE 259
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 893-1090 3.19e-91

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: 293.42  E-value: 3.19e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  893 YINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQNKTKCEQYWPE---QEQIYGDFTVTLNNT 969
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEeggKPLEYGDITVTLVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  970 RTTTGLITRIFSLHKAGCGFPRVVEQFHYLLWPDHGVPRNSAQLLCLVDVVNKRAlEAPAGPVVVHCSAGIGRTGTFIAL 1049
Cdd:cd00047     81 EELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEA-RKPNGPIVVHCSAGVGRTGTFIAI 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1838351042 1050 DFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYE 1090
Cdd:cd00047    160 DILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1127-1388 2.47e-57

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 199.04  E-value: 2.47e-57
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  1127 LEKEFKALQKFseLFQLLPCREAEKPTNQPKNRKPGILPADSCRPILMSSLNADGspGYINAVFVNTYTEEDRLIITQMP 1206
Cdd:smart00194    2 LEEEFEKLDRL--KPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGS--DYINASYIDGPNGPKAYIATQGP 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  1207 FPNTVVDFWALVWDYTCTAVVVLNQLQELD-ETYAEFWPMQGEAA--YGRFHVQFISEEPGAGFTAWTLALTNKQQPKkp 1283
Cdd:smart00194   78 LPSTVEDFWRMVWEQKVTVIVMLTELVEKGrEKCAQYWPDEEGEPltYGDITVTLKSVEKVDDYTIRTLEVTNTGCSE-- 155

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  1284 PLEVRFWQLKDWPmKQHLPPHPATIISLLGNVEtHHRQSRDGHILITCWDGASRSGIFCAAGFLCEQIQSEGLVDVSQAV 1363
Cdd:smart00194  156 TRTVTHYHYTNWP-DHGVPESPESILDLIRAVR-KSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIV 233

                           250       260
                    ....*....|....*....|....*
gi 1838351042  1364 RMLKRRRRQLIKDVEQYGLCYELAL 1388
Cdd:smart00194  234 KELRSQRPGMVQTEEQYIFLYRAIL 258
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 1185-1385 1.62e-55

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: 191.85  E-value: 1.62e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1185 YINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQELDETYAEFWPMQGEAAYGRFHVQFISEEPG 1264
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQSCPQYWPDEGSGTYGPIQVEFVSTTID 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1265 AGFTAWTLALTNKQQPKKPPLEVRFWQLKDWPMKQHLPPHPATIISLLGNVETHHRQSRDGHILITCWDGASRSGIFCAA 1344
Cdd:cd14556     81 EDVISRIFRLQNTTRPQEGYRMVQQFQFLGWPRDRDTPPSKRALLKLLSEVEKWQEQSGEGPIVVHCLNGVGRSGVFCAI 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1838351042 1345 GFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQYGLCYE 1385
Cdd:cd14556    161 SSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1154-1388 6.96e-53

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 185.52  E-value: 6.96e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1154 NQPKNRKPGILPADSCRPILMSSlnaDGSPGYINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQ 1233
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGD---PGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1234 ELD-ETYAEFWP--MQGEAAYGRFHVQFISEEP-GAGFTAWTLALTNKQQpkKPPLEVRFWQLKDWPmKQHLPPHPATII 1309
Cdd:pfam00102   78 EKGrEKCAQYWPeeEGESLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGS--EETRTVKHFHYTGWP-DHGVPESPNSLL 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1838351042 1310 SLLGNVETHHRQSRDGHILITCWDGASRSGIFCAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQYGLCYELAL 1388
Cdd:pfam00102  155 DLLRKVRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
862-1088 7.38e-51

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 181.44  E-value: 7.38e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  862 ELCNQSK-NRYKNIIPYDHcrVVLQPSDTgndYINASYVDSYRsPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGL 940
Cdd:COG5599     38 QNINGSPlNRFRDIQPYKE--TALRANLG---YLNANYIQVIG-NHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASD 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  941 VE--QNKTKCEQYWPEQEQiYGDFTVTLNNTRTT---TGLITRIFSLHKAGCGFP-RVVEQFHYLLWPDHGvPRNSAQLL 1014
Cdd:COG5599    112 DEisKPKVKMPVYFRQDGE-YGKYEVSSELTESIqlrDGIEARTYVLTIKGTGQKkIEIPVLHVKNWPDHG-AISAEALK 189

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1838351042 1015 CLVDVVNKRA--LEAPAGPVVVHCSAGIGRTGTFIALDFLLKMGKAEG--KVDVFHCVQRLREQR-ISMVQTKEQYTFL 1088
Cdd:COG5599    190 NLADLIDKKEkiKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRnGGMVQTSEQLDVL 268
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 857-1094 1.05e-48

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 175.96  E-value: 1.05e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  857 CNAGKELCNQSKNRYKNIIPYDHCRVVLQPSDTGNDYINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVM 936
Cdd:PHA02742    44 CNESLELKNMKKCRYPDAPCFDRNRVILKIEDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVM 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  937 LTGLVEQNKTKCEQYWPEQEQ---IYGDFTVTLNNTRTTTGLITRIFSLHKAGCGFPRVVEQFHYLLWPDHGVPRNSAQL 1013
Cdd:PHA02742   124 ITKIMEDGKEACYPYWMPHERgkaTHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKF 203

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1014 LCLV----------DVVNKRALEAPAGPVVVHCSAGIGRTGTFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKE 1083
Cdd:PHA02742   204 LDFVlavreadlkaDVDIKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQ 283

                          250
                   ....*....|.
gi 1838351042 1084 QYTFLYEVVLE 1094
Cdd:PHA02742   284 QYIFCYFIVLI 294
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 1151-1390 7.93e-24

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 104.34  E-value: 7.93e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1151 KPTNQPKNRKPGILPADSCRPILMS--SLNA----------------DGSPGYINAVFVNTYTEEDRLIITQMPFPNTVV 1212
Cdd:PHA02746    48 KKENLKKNRFHDIPCWDHSRVVINAheSLKMfdvgdsdgkkievtseDNAENYIHANFVDGFKEANKFICAQGPKEDTSE 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1213 DFWALVWDYTCTAVVVLNQLQELDETYAEFW--PMQGEAAYGRFHVQFISEEPGAGFTAWTLALTNKQQPKKPPLEvRFW 1290
Cdd:PHA02746   128 DFFKLISEHESQVIVSLTDIDDDDEKCFELWtkEEDSELAFGRFVAKILDIIEELSFTKTRLMITDKISDTSREIH-HFW 206

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1291 qLKDWPmKQHLPPHPATIISLLGNVETHHRQ---------SRDGHILITCWDGASRSGIFCAAGFLCEQIQSEGLVDVSQ 1361
Cdd:PHA02746   207 -FPDWP-DNGIPTGMAEFLELINKVNEEQAElikqadndpQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGE 284

                          250       260
                   ....*....|....*....|....*....
gi 1838351042 1362 AVRMLKRRRRQLIKDVEQYGLCYeLALSY 1390
Cdd:PHA02746   285 IVLKIRKQRHSSVFLPEQYAFCY-KALKY 312
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 513-591 2.40e-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.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 38.63  E-value: 2.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  513 PDKPEQLWLDPSTGS---LSWEPLPSCKGEIIGYQLNITARSaQDRALLELERLRLSGSVTAHPLPahgPGTSYVVTVRG 589
Cdd:cd00063      1 PSPPTNLRVTDVTSTsvtLSWTPPEDDGGPITGYVVEYREKG-SGDWKEVEVTPGSETSYTLTGLK---PGTEYEFRVRA 76


                   ..
gi 1838351042  590 LT 591
Cdd:cd00063     77 VN 78
 
Name Accession Description Interval E-value
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
865-1094 2.35e-110

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 347.31  E-value: 2.35e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  865 NQSKNRYKNIIPYDHCRVVLQPSDTGNDYINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQN 944
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  945 KTKCEQYWP---EQEQIYGDFTVTL-NNTRTTTGLITRIFSLHKAGCGFPRVVEQFHYLLWPDHGVPRNSAQLLCLVDVV 1020
Cdd:pfam00102   81 REKCAQYWPeeeGESLEYGDFTVTLkKEKEDEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLRKV 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1838351042 1021 NKRALEAPAGPVVVHCSAGIGRTGTFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYEVVLE 1094
Cdd:pfam00102  161 RKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
841-1094 5.67e-107

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 339.25  E-value: 5.67e-107
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042   841 GRLGEYQQLSS--SLMHPCNAGKELCNQSKNRYKNIIPYDHCRVVLQPSDT-GNDYINASYVDSYRSPRFFIAAQGPLPG 917
Cdd:smart00194    1 GLEEEFEKLDRlkPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGeGSDYINASYIDGPNGPKAYIATQGPLPS 80

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042   918 TVLDFWQMVWQEKTSVIVMLTGLVEQNKTKCEQYWPE---QEQIYGDFTVTLNNTRTTTGLITRIFSLHKAGCGFPRVVE 994
Cdd:smart00194   81 TVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDeegEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVT 160

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042   995 QFHYLLWPDHGVPRNSAQLLCLVDVVNKRAlEAPAGPVVVHCSAGIGRTGTFIALDFLLKMGKAEGKVDVFHCVQRLREQ 1074
Cdd:smart00194  161 HYHYTNWPDHGVPESPESILDLIRAVRKSQ-STSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELRSQ 239

                           250       260
                    ....*....|....*....|
gi 1838351042  1075 RISMVQTKEQYTFLYEVVLE 1094
Cdd:smart00194  240 RPGMVQTEEQYIFLYRAILE 259
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 893-1090 3.19e-91

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: 293.42  E-value: 3.19e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  893 YINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQNKTKCEQYWPE---QEQIYGDFTVTLNNT 969
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEeggKPLEYGDITVTLVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  970 RTTTGLITRIFSLHKAGCGFPRVVEQFHYLLWPDHGVPRNSAQLLCLVDVVNKRAlEAPAGPVVVHCSAGIGRTGTFIAL 1049
Cdd:cd00047     81 EELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEA-RKPNGPIVVHCSAGVGRTGTFIAI 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1838351042 1050 DFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYE 1090
Cdd:cd00047    160 DILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 864-1098 1.70e-90

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


Pssm-ID: 350401 [Multi-domain]  Cd Length: 238  Bit Score: 292.76  E-value: 1.70e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  864 CNQSKNRYKNIIPYDHCRVVLQPSD--TGNDYINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLV 941
Cdd:cd14553      2 VNKPKNRYANVIAYDHSRVILQPIEgvPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  942 EQNKTKCEQYWP-EQEQIYGDFTVTLNNTRTTTGLITRIFSLHKAGCGFPRVVEQFHYLLWPDHGVPRNSAQLLCLVDVV 1020
Cdd:cd14553     82 ERSRVKCDQYWPtRGTETYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRV 161

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1838351042 1021 nkRALEAP-AGPVVVHCSAGIGRTGTFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYEVVLEGLLC 1098
Cdd:cd14553    162 --KACNPPdAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLEAVTC 238
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 870-1090 2.04e-81

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: 266.53  E-value: 2.04e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  870 RYKNIIPYDHCRVVLQP--SDTGNDYINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQNKTK 947
Cdd:cd14548      1 RYTNILPYDHSRVKLIPinEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  948 CEQYWP--EQEQIYGDFTVTLNNTRTTTGLITRIFSL-HKAGCgfpRVVEQFHYLLWPDHGVPRNSAQLLCLVDVVNKRa 1024
Cdd:cd14548     81 CDHYWPfdQDPVYYGDITVTMLSESVLPDWTIREFKLeRGDEV---RSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDY- 156

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1838351042 1025 LEAPAGPVVVHCSAGIGRTGTFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYE 1090
Cdd:cd14548    157 IKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 865-1098 2.36e-80

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: 264.19  E-value: 2.36e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  865 NQSKNRYKNIIPYDHCRVVLQ--PSDTGNDYINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVE 942
Cdd:cd14630      3 NRNKNRYGNIISYDHSRVRLQllDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  943 QNKTKCEQYWPEQEQIYGDFTVTLNNTRTTTGLITRIFSLHKAGCGFPRVVEQFHYLLWPDHGVPRNSAQLLCLVDVVnk 1022
Cdd:cd14630     83 VGRVKCVRYWPDDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVRQV-- 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1838351042 1023 RALEAP-AGPVVVHCSAGIGRTGTFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYEVVLEGLLC 1098
Cdd:cd14630    161 KFLNPPdAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILEACLC 237
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 839-1097 5.34e-78

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: 259.20  E-value: 5.34e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  839 GAGRLGEYQQLSSSLMHPCNAGKELCNQSKNRYKNIIPYDHCRVVLQP--SDTGNDYINASYVDSYRSPRFFIAAQGPLP 916
Cdd:cd14633     14 GYGFKEEYESFFEGQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPieGETSSDYINGNYIDGYHRPNHYIATQGPMQ 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  917 GTVLDFWQMVWQEKTSVIVMLTGLVEQNKTKCEQYWPEQEQIYGDFTVTLNNTRTTTGLITRIFSLHKAGCGFPRVVEQF 996
Cdd:cd14633     94 ETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEIYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQF 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  997 HYLLWPDHGVPRNSAQLLCLVDVVNKRAlEAPAGPVVVHCSAGIGRTGTFIALDFLLKMGKAEGKVDVFHCVQRLREQRI 1076
Cdd:cd14633    174 HFTGWPDHGVPYHATGLLGFVRQVKSKS-PPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRV 252

                          250       260
                   ....*....|....*....|.
gi 1838351042 1077 SMVQTKEQYTFLYEVVLEGLL 1097
Cdd:cd14633    253 NMVQTEEQYVFIHDAILEACL 273
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 869-1094 1.56e-77

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: 255.90  E-value: 1.56e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  869 NRYKNIIPYDHCRVVLQ-PSDTGNDYINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQNKTK 947
Cdd:cd14615      1 NRYNNVLPYDISRVKLSvQSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRTK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  948 CEQYWP-EQEQIYGDFTVTLNNTRTTTGLITRIFSLHKAGCGFPRVVEQFHYLLWPDHGVPRNSAQLLCLVDVVNKRALE 1026
Cdd:cd14615     81 CEEYWPsKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREYMKQ 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1838351042 1027 APA-GPVVVHCSAGIGRTGTFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYEVVLE 1094
Cdd:cd14615    161 NPPnSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 893-1090 1.63e-77

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: 254.58  E-value: 1.63e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  893 YINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQNKTKCEQYWP-EQEQIYGDFTVTLNNTRT 971
Cdd:cd14549      1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPkEGTETYGNIQVTLLSTEV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  972 TTGLITRIFSL------HKAGCGFPRVVEQFHYLLWPDHGVPRNSAQLLCLVDVVNkRALEAPAGPVVVHCSAGIGRTGT 1045
Cdd:cd14549     81 LATYTVRTFSLknlklkKVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSS-AANPPGAGPIVVHCSAGVGRTGT 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1838351042 1046 FIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYE 1090
Cdd:cd14549    160 YIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIHD 204
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 865-1098 1.31e-74

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: 249.57  E-value: 1.31e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  865 NQSKNRYKNIIPYDHCRVVLQPSD--TGNDYINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVE 942
Cdd:cd14626     41 NKPKNRYANVIAYDHSRVILTSVDgvPGSDYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEE 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  943 QNKTKCEQYWPEQ-EQIYGDFTVTLNNTRTTTGLITRIFSLHKAGCGFPRVVEQFHYLLWPDHGVPRNSAQLLCLVDVVn 1021
Cdd:cd14626    121 KSRVKCDQYWPIRgTETYGMIQVTLLDTVELATYSVRTFALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRV- 199

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1838351042 1022 KRALEAPAGPVVVHCSAGIGRTGTFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYEVVLEGLLC 1098
Cdd:cd14626    200 KACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEAATC 276
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 893-1090 1.73e-74

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: 246.39  E-value: 1.73e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  893 YINASYVD-SYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQNKTKCEQYWPEQ--EQIYGDFTVTLNNT 969
Cdd:cd18533      1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGeyEGEYGDLTVELVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  970 RTTT--GLITRIFSLHKAGCGfPRVVEQFHYLLWPDHGVPRNSAQLLCLVDVVN-KRALEAPAGPVVVHCSAGIGRTGTF 1046
Cdd:cd18533     81 EENDdgGFIVREFELSKEDGK-VKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKReLNDSASLDPPIIVHCSAGVGRTGTF 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1838351042 1047 IALDFLLKM--------GKAEGKVD-VFHCVQRLREQRISMVQTKEQYTFLYE 1090
Cdd:cd18533    160 IALDSLLDElkrglsdsQDLEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 865-1092 7.59e-74

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: 246.22  E-value: 7.59e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  865 NQSKNRYKNIIPYDHCRVVLQ---PSDTGNDYINASYVDSYRSPRF-------FIAAQGPLPGTVLDFWQMVWQEKTSVI 934
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILKdrdPNVPGSDYINANYIRNENEGPTtdenaktYIATQGCLENTVSDFWSMVWQENSRVI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  935 VMLTGLVEQNKTKCEQYWPE---QEQiYGDFTVTLNNTRTTTGLITRIFSLHKAGCGFP-RVVEQFHYLLWPDHGVPRNS 1010
Cdd:cd14544     81 VMTTKEVERGKNKCVRYWPDegmQKQ-YGPYRVQNVSEHDTTDYTLRELQVSKLDQGDPiREIWHYQYLSWPDHGVPSDP 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1011 AQLLCLVDVVNKRALEAP-AGPVVVHCSAGIGRTGTFIALDFLLKMGKAEG---KVDVFHCVQRLREQRISMVQTKEQYT 1086
Cdd:cd14544    160 GGVLNFLEDVNQRQESLPhAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRSGMVQTEAQYK 239


                   ....*.
gi 1838351042 1087 FLYEVV 1092
Cdd:cd14544    240 FIYVAV 245
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 893-1097 7.99e-74

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: 244.44  E-value: 7.99e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  893 YINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQNKTKCEQYWPEQEQIYGDFTVTLNNTRTT 972
Cdd:cd14555      1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTEVYGDIKVTLVETEPL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  973 TGLITRIFSLHKAGCGFPRVVEQFHYLLWPDHGVPRNSAQLLCLVDVVnkRALEAP-AGPVVVHCSAGIGRTGTFIALDF 1051
Cdd:cd14555     81 AEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRV--KASNPPsAGPIVVHCSAGAGRTGCYIVIDI 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1838351042 1052 LLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYEVVLEGLL 1097
Cdd:cd14555    159 MLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILEACL 204
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 869-1089 1.65e-73

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: 244.23  E-value: 1.65e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  869 NRYKNIIPYDHCRVVLQPSDTG--NDYINASYVDSYR-SPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEqNK 945
Cdd:cd14547      1 NRYKTILPNEHSRVCLPSVDDDplSSYINANYIRGYDgEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTE-AK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  946 TKCEQYWP-EQEQIYGDFTVTLNNTRTTTGLITRIFSLHKagCGFPRVVEQFHYLLWPDHGVPRNSAQLLCLV-DVVNKR 1023
Cdd:cd14547     80 EKCAQYWPeEENETYGDFEVTVQSVKETDGYTVRKLTLKY--GGEKRYLKHYWYTSWPDHKTPEAAQPLLSLVqEVEEAR 157

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1838351042 1024 ALEAPAGPVVVHCSAGIGRTGTFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLY 1089
Cdd:cd14547    158 QTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVH 223
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 871-1094 1.16e-72

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: 242.15  E-value: 1.16e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  871 YKNIIPYDHCRVVLQPSD--TGNDYINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQNKTKC 948
Cdd:cd14620      1 YPNILPYDHSRVILSQLDgiPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  949 EQYWPEQE-QIYGDFTVTLNNTRTTTGLITRIF---SLHKAGCGFPRVVEQFHYLLWPDHGVPRNSAQLLCLVDVVnKRA 1024
Cdd:cd14620     81 YQYWPDQGcWTYGNIRVAVEDCVVLVDYTIRKFciqPQLPDGCKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKV-KSV 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1025 LEAPAGPVVVHCSAGIGRTGTFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYEVVLE 1094
Cdd:cd14620    160 NPVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 893-1098 2.51e-72

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: 239.95  E-value: 2.51e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  893 YINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQNKTKCEQYWPEQEQIYGDFTVTLNNTRTT 972
Cdd:cd14632      1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSDTYGDIKITLLKTETL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  973 TGLITRIFSLHKAGCGFPRVVEQFHYLLWPDHGVPRNSAQLLCLVDVVnKRALEAPAGPVVVHCSAGIGRTGTFIALDFL 1052
Cdd:cd14632     81 AEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRV-KASTPPDAGPVVVHCSAGAGRTGCYIVLDVM 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1838351042 1053 LKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYEVVLEGLLC 1098
Cdd:cd14632    160 LDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACLC 205
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 858-1089 2.93e-72

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: 242.66  E-value: 2.93e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  858 NAGKELCNQSKNRYKNIIPYDHCRVVLQP--SDTGNDYINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIV 935
Cdd:cd14543     22 LCSLAPANQEKNRYGDVLCLDQSRVKLPKrnGDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIV 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  936 MLTGLVEQNKTKCEQYWPEQE---QIYGDFTVTLNNTRTTTGLITRIFSLHKAGCGFPRVVEQFHYLLWPDHGVPRNSAQ 1012
Cdd:cd14543    102 MTTRVVERGRVKCGQYWPLEEgssLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESRQVTHFQFTSWPDFGVPSSAAA 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1013 LL-CLVDVVNKRAL-----------EAPAGPVVVHCSAGIGRTGTFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQ 1080
Cdd:cd14543    182 LLdFLGEVRQQQALavkamgdrwkgHPPGPPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVRRMRTQRAFSIQ 261


                   ....*....
gi 1838351042 1081 TKEQYTFLY 1089
Cdd:cd14543    262 TPDQYYFCY 270
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 881-1097 4.43e-72

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: 239.92  E-value: 4.43e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  881 RVVLQP--SDTGNDYINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQNKTKCEQYWPEQEQI 958
Cdd:cd14631      1 RVILQPveDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTEV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  959 YGDFTVTLNNTRTTTGLITRIFSLHKAGCGFPRVVEQFHYLLWPDHGVPRNSAQLLCLVDVVnKRALEAPAGPVVVHCSA 1038
Cdd:cd14631     81 YGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRV-KLSNPPSAGPIVVHCSA 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1838351042 1039 GIGRTGTFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYEVVLEGLL 1097
Cdd:cd14631    160 GAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 218
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 869-1096 1.63e-71

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: 239.02  E-value: 1.63e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  869 NRYKNIIPYDHCRVVLQP--SDTGNDYINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQNKT 946
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKPihEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  947 KCEQYWPEQEQ--IYGDFTVTLNNTRTTTGLITRIFSLHKAGCGFPRVVEQFHYLLWPDHGVPRNSAQLLCLVDVVNKRA 1024
Cdd:cd14619     81 KCEHYWPLDYTpcTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQWL 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1838351042 1025 -LEAPAGPVVVHCSAGIGRTGTFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYEVVLEGL 1096
Cdd:cd14619    161 dQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 808-1098 1.15e-70

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


Pssm-ID: 350473 [Multi-domain]  Cd Length: 282  Bit Score: 238.45  E-value: 1.15e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  808 IPVEALLEALKRFKRAEIEAEQTEDESVNThGAGRLGEYQQLSsslmhpcnagkelCNQSKNRYKNIIPYDHCRVVLQPS 887
Cdd:cd14625      4 IPISELAEHTERLKANDNLKLSQEYESIDP-GQQFTWEHSNLE-------------VNKPKNRYANVIAYDHSRVILQPI 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  888 D--TGNDYINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQNKTKCEQYWPEQ-EQIYGDFTV 964
Cdd:cd14625     70 EgiMGSDYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRgTETYGMIQV 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  965 TLNNTRTTTGLITRIFSLHKAGCGFPRVVEQFHYLLWPDHGVPRNSAQLLCLVDVVnKRALEAPAGPVVVHCSAGIGRTG 1044
Cdd:cd14625    150 TLLDTIELATFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRV-KTCNPPDAGPIVVHCSAGVGRTG 228

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1838351042 1045 TFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYEVVLEGLLC 1098
Cdd:cd14625    229 CFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAVAC 282
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 865-1097 1.99e-69

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: 234.54  E-value: 1.99e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  865 NQSKNRYKNIIPYDHCRVVLQP----SDTGNDYINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGL 940
Cdd:cd17667     27 NKHKNRYINILAYDHSRVKLRPlpgkDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNL 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  941 VEQNKTKCEQYWP-EQEQIYGDFTVTLNNTRTTTGLITRIFS-----LHKAGCGFP------RVVEQFHYLLWPDHGVPR 1008
Cdd:cd17667    107 VEKGRRKCDQYWPtENSEEYGNIIVTLKSTKIHACYTVRRFSirntkVKKGQKGNPkgrqneRTVIQYHYTQWPDMGVPE 186

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1009 NSAQLLCLVDvvNKRALEAP-AGPVVVHCSAGIGRTGTFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTF 1087
Cdd:cd17667    187 YALPVLTFVR--RSSAARTPeMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIF 264

                          250
                   ....*....|
gi 1838351042 1088 LYEVVLEGLL 1097
Cdd:cd17667    265 IHDALLEAIL 274
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 865-1094 2.30e-69

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: 234.00  E-value: 2.30e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  865 NQSKNRYKNIIPYDHCRVVLQPSDT---GNDYINASYVDSY-----RSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVM 936
Cdd:cd14606     18 NKSKNRYKNILPFDHSRVILQGRDSnipGSDYINANYVKNQllgpdENAKTYIASQGCLEATVNDFWQMAWQENSRVIVM 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  937 LTGLVEQNKTKCEQYWPE--QEQIYGDFTVTLNNTRTTTGLITRIFSLHKAGCG-FPRVVEQFHYLLWPDHGVPRNSAQL 1013
Cdd:cd14606     98 TTREVEKGRNKCVPYWPEvgMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGeLIREIWHYQYLSWPDHGVPSEPGGV 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1014 LCLVDVVNKRALEAP-AGPVVVHCSAGIGRTGTFIALDFLLKMGKAEG---KVDVFHCVQRLREQRISMVQTKEQYTFLY 1089
Cdd:cd14606    178 LSFLDQINQRQESLPhAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGldcDIDIQKTIQMVRAQRSGMVQTEAQYKFIY 257


                   ....*
gi 1838351042 1090 EVVLE 1094
Cdd:cd14606    258 VAIAQ 262
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 864-1093 2.33e-68

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: 230.10  E-value: 2.33e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  864 CNQSKNRYKNIIPYDHCRVVLQP--SDTGNDYINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLV 941
Cdd:cd14554      5 CNKFKNRLVNILPYESTRVCLQPirGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKLR 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  942 EQNKTKCEQYWP-EQEQIYGDFTVTLNNTRTTTGLITRIFSLHKAGCGFPRVVEQFHYLLWPDHGVPRNSAQLLCLVDVV 1020
Cdd:cd14554     85 EMGREKCHQYWPaERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQV 164

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1838351042 1021 NK-RALEAPAGPVVVHCSAGIGRTGTFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYEVVL 1093
Cdd:cd14554    165 HKtKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRAAL 238
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 865-1093 2.42e-66

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: 224.38  E-value: 2.42e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  865 NQSKNRYKNIIPYDHCRVVLQP--SDTGNDYINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVE 942
Cdd:cd14614     12 NRCKNRYTNILPYDFSRVKLVSmhEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNE 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  943 QNKTKCEQYWP--EQEQIYGDFTVTLNNTRTTTGLITRIFSLHKAGCgfPRVVEQFHYLLWPDHGVPR-NSAQ-LLCLVD 1018
Cdd:cd14614     92 KRRVKCDHYWPftEEPVAYGDITVEMLSEEEQPDWAIREFRVSYADE--VQDVMHFNYTAWPDHGVPTaNAAEsILQFVQ 169

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1838351042 1019 VVNKRALEAPaGPVVVHCSAGIGRTGTFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYEVVL 1093
Cdd:cd14614    170 MVRQQAVKSK-GPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIHQCVQ 243
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 857-1101 3.36e-65

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: 223.36  E-value: 3.36e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  857 CNAGKELCNQSKNRYKNIIPYDHCRVVLQPSD--TGNDYINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVI 934
Cdd:cd14621     44 CEAASKEENKEKNRYVNILPYDHSRVHLTPVEgvPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATI 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  935 VMLTGLVEQNKTKCEQYWPEQE-QIYGDFTVTLNNTRTTTGLITRIFSLHKAG----CGFPRVVEQFHYLLWPDHGVPRN 1009
Cdd:cd14621    124 VMVTNLKERKECKCAQYWPDQGcWTYGNIRVSVEDVTVLVDYTVRKFCIQQVGdvtnKKPQRLITQFHFTSWPDFGVPFT 203

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1010 SAQLLCLVDVVnKRALEAPAGPVVVHCSAGIGRTGTFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLY 1089
Cdd:cd14621    204 PIGMLKFLKKV-KNCNPQYAGAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIY 282

                          250
                   ....*....|..
gi 1838351042 1090 EVVLEGLLCGST 1101
Cdd:cd14621    283 QALLEHYLYGDT 294
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 865-1100 3.81e-65

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: 222.68  E-value: 3.81e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  865 NQSKNRYKNIIPYDHCRVVLQPSD--TGNDYINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVE 942
Cdd:cd14624     47 NKPKNRYANVIAYDHSRVLLSAIEgiPGSDYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEE 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  943 QNKTKCEQYWPEQ-EQIYGDFTVTLNNTRTTTGLITRIFSLHKAGCGFPRVVEQFHYLLWPDHGVPRNSAQLLCLVDVVn 1021
Cdd:cd14624    127 RSRVKCDQYWPSRgTETYGLIQVTLLDTVELATYCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRV- 205

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1838351042 1022 KRALEAPAGPVVVHCSAGIGRTGTFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYEVVLEGLLCGS 1100
Cdd:cd14624    206 KTCNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAVTCGN 284
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 893-1090 9.36e-65

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: 218.24  E-value: 9.36e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  893 YINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQNKTKCEQYWPEQ-EQIYGDFTVTLNNTRT 971
Cdd:cd14551      1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQgCWTYGNLRVRVEDTVV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  972 TTGLITRIFSLHK----AGCGFPRVVEQFHYLLWPDHGVPRNSAQLLCLVDVVnKRALEAPAGPVVVHCSAGIGRTGTFI 1047
Cdd:cd14551     81 LVDYTTRKFCIQKvnrgIGEKRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKV-KSANPPRAGPIVVHCSAGVGRTGTFI 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1838351042 1048 ALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYE 1090
Cdd:cd14551    160 VIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 869-1090 1.46e-64

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: 218.63  E-value: 1.46e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  869 NRYKNIIPYDHCRVVLQ--PSDTGNDYINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQNKT 946
Cdd:cd14617      1 NRYNNILPYDSTRVKLSnvDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  947 KCEQYWP-EQEQI-YGDFTVTLNNTRTTTGLITRIFSLhkagCG-----FPRVVEQFHYLLWPDHGVPRNSAQLLCLVDV 1019
Cdd:cd14617     81 KCDHYWPaDQDSLyYGDLIVQMLSESVLPEWTIREFKI----CSeeqldAPRLVRHFHYTVWPDHGVPETTQSLIQFVRT 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1838351042 1020 VNKRALEAP-AGPVVVHCSAGIGRTGTFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYE 1090
Cdd:cd14617    157 VRDYINRTPgSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 893-1090 6.04e-64

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: 215.85  E-value: 6.04e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  893 YINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQNKTKCEQYWP---EQEQIYGDFTVTLNNT 969
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPsmeEGSRAFGDVVVKINEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  970 RTTTGLITRIFSL-HKAGCGFPRVVEQFHYLLWPDHGVPRNSAQLLCLVDVVNKRAlEAPAGPVVVHCSAGIGRTGTFIA 1048
Cdd:cd14557     81 KICPDYIIRKLNInNKKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFN-NFFSGPIVVHCSAGVGRTGTYIG 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1838351042 1049 LDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYE 1090
Cdd:cd14557    160 IDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 865-1092 8.07e-64

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: 217.58  E-value: 8.07e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  865 NQSKNRYKNIIPYDHCRVVLQ---PSDTGNDYINASYV--------DSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSV 933
Cdd:cd14605      2 NKNKNRYKNILPFDHTRVVLHdgdPNEPVSDYINANIImpefetkcNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  934 IVMLTGLVEQNKTKCEQYWPEQEQI--YGDFTVtlNNTRTTTG--LITRIFSLHKAGCG-FPRVVEQFHYLLWPDHGVPR 1008
Cdd:cd14605     82 IVMTTKEVERGKSKCVKYWPDEYALkeYGVMRV--RNVKESAAhdYILRELKLSKVGQGnTERTVWQYHFRTWPDHGVPS 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1009 NSAQLLCLVDVVN-KRALEAPAGPVVVHCSAGIGRTGTFIALDFLLKMGKAEG---KVDVFHCVQRLREQRISMVQTKEQ 1084
Cdd:cd14605    160 DPGGVLDFLEEVHhKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGvdcDIDVPKTIQMVRSQRSGMVQTEAQ 239


                   ....*...
gi 1838351042 1085 YTFLYEVV 1092
Cdd:cd14605    240 YRFIYMAV 247
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 893-1092 8.70e-64

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: 215.60  E-value: 8.70e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  893 YINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQNKTKCEQYWPEQEQI-YGDFTVTLNNTRT 971
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGSVsSGDITVELKDQTD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  972 TTGLITRIFSLHKAGCGFPRVVEQFHYLLWPDHGVPRNSAQLLCLVDVVNKRALEAPAGPVVVHCSAGIGRTGTFIALDF 1051
Cdd:cd14552     81 YEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQSGNHPITVHCSAGAGRTGTFCALST 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1838351042 1052 LLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYEVV 1092
Cdd:cd14552    161 VLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 893-1096 1.28e-63

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: 215.32  E-value: 1.28e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  893 YINASYV--DSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQNKTKCEQYWPEQEQ----IYGDFTVTL 966
Cdd:cd14538      1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNkpliCGGRLEVSL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  967 NNTRTTTGLITRIFSLHKAGCGFPRVVEQFHYLLWPDHGVPRNSAQLLCLVDVVNKRALEapaGPVVVHCSAGIGRTGTF 1046
Cdd:cd14538     81 EKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIHNS---GPIVVHCSAGIGRTGVL 157

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1047 IALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYEVVLEGL 1096
Cdd:cd14538    158 ITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 893-1090 1.30e-63

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: 214.95  E-value: 1.30e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  893 YINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQNKTKCEQYWPEQEQIYGDFTVTLNNTRTT 972
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKTYGDIEVELKDTEKS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  973 TGLITRIFSLHKAGCGFPRVVEQFHYLLWPDHGVPRNSAQLLCLVDVVNKRALEAPAG-----PVVVHCSAGIGRTGTFI 1047
Cdd:cd14558     81 PTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNSKhgrsvPIVVHCSDGSSRTGIFC 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1838351042 1048 ALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYE 1090
Cdd:cd14558    161 ALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 868-1089 1.47e-63

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


Pssm-ID: 350393 [Multi-domain]  Cd Length: 231  Bit Score: 216.10  E-value: 1.47e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  868 KNRYKNIIPYDHCRVVLQPSDTGNDYINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQNKTK 947
Cdd:cd14545      1 LNRYRDRDPYDHDRSRVKLKQGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQIK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  948 CEQYWPeQEQIYG------DFTVTLNNTRTTTGLITRIFSLHKAGCGFPRVVEQFHYLLWPDHGVPRNSAQLL-CLVDVV 1020
Cdd:cd14545     81 CAQYWP-QGEGNAmifedtGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLnFLQKVR 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1838351042 1021 NKRALEAPAGPVVVHCSAGIGRTGTFIALDFLLKMGKAEG--KVDVFHCVQRLREQRISMVQTKEQYTFLY 1089
Cdd:cd14545    160 ESGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNpsSVDVKKVLLEMRKYRMGLIQTPDQLRFSY 230
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 805-1096 1.60e-63

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: 218.06  E-value: 1.60e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  805 NTQIPVEALLEALKRFkrAEIEAEQtedesvntHGAGRLGEYQQLSSSLMHPCN--AGKELCNQSKNRYKNIIPYDHCRV 882
Cdd:cd14627      1 NTEVPARNLYSYIQKL--AQVEVGE--------HVTGMELEFKRLANSKAHTSRfiSANLPCNKFKNRLVNIMPYETTRV 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  883 VLQP--SDTGNDYINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQNKTKCEQYWP-EQEQIY 959
Cdd:cd14627     71 CLQPirGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPaERSARY 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  960 GDFTVTLNNTRTTTGLITRIFSLHKAGCGFPRVVEQFHYLLWPDHGVPRNSAQLLCLVDVVNKRALE-APAGPVVVHCSA 1038
Cdd:cd14627    151 QYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQfGQDGPISVHCSA 230

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1838351042 1039 GIGRTGTFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYEVVLEGL 1096
Cdd:cd14627    231 GVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYL 288
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 867-1089 6.45e-63

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: 214.70  E-value: 6.45e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  867 SKNRYKNIIPYDHCRVVLQ---PSDTGNDYINASYVDSYR-SPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVE 942
Cdd:cd14612     17 SKDRYKTILPNPQSRVCLRragSQEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKE 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  943 QnKTKCEQYWPEQEQIYGDFTVTLNNTRTTTGLITRIFSLHKAGCGfpRVVEQFHYLLWPDHGVPRNSAQLLCLVDVVNK 1022
Cdd:cd14612     97 K-KEKCVHYWPEKEGTYGRFEIRVQDMKECDGYTIRDLTIQLEEES--RSVKHYWFSSWPDHQTPESAGPLLRLVAEVEE 173

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1838351042 1023 RALEAPA-GPVVVHCSAGIGRTGTFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLY 1089
Cdd:cd14612    174 SRQTAASpGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLH 241
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 806-1096 2.28e-62

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: 214.98  E-value: 2.28e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  806 TQIPVEALLEALKRFKRAEIEAEQTedesvnthgaGRLGEYQQLSSSLMHPCN--AGKELCNQSKNRYKNIIPYDHCRVV 883
Cdd:cd14628      1 TEVPARNLYAYIQKLTQIETGENVT----------GMELEFKRLASSKAHTSRfiSANLPCNKFKNRLVNIMPYESTRVC 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  884 LQP--SDTGNDYINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQNKTKCEQYWP-EQEQIYG 960
Cdd:cd14628     71 LQPirGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPaERSARYQ 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  961 DFTVTLNNTRTTTGLITRIFSLHKAGCGFPRVVEQFHYLLWPDHGVPRNSAQLLCLVDVVNKRALE-APAGPVVVHCSAG 1039
Cdd:cd14628    151 YFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQfGQDGPISVHCSAG 230

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1838351042 1040 IGRTGTFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYEVVLEGL 1096
Cdd:cd14628    231 VGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYL 287
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 893-1093 5.70e-62

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


Pssm-ID: 350506 [Multi-domain]  Cd Length: 209  Bit Score: 210.61  E-value: 5.70e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  893 YINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQNKTKCEQYWP-EQEQIYGDFTVTLNNTRT 971
Cdd:cd17668      1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPaDGSEEYGNFLVTQKSVQV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  972 TTGLITRIFSLH--------KAGCGFPRVVEQFHYLLWPDHGVPRNSAQLLCLVDVVNKrALEAPAGPVVVHCSAGIGRT 1043
Cdd:cd17668     81 LAYYTVRNFTLRntkikkgsQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASY-AKRHAVGPVVVHCSAGVGRT 159

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1044 GTFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYEVVL 1093
Cdd:cd17668    160 GTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 892-1093 6.02e-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: 6.02e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  892 DYINASYVDsYRSPRF-----FIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQNKTKCEQYWPE--QEQIYGDFTV 964
Cdd:cd14541      1 DYINANYVN-MEIPGSgivnrYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDlgETMQFGNLQI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  965 TLNNTRTTTGLITRIFSLHKAGCGFPRVVEQFHYLLWPDHGVPRNSAQLLCLVDVVnKRALEAPAGPVVVHCSAGIGRTG 1044
Cdd:cd14541     80 TCVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRV-RQNRVGMVEPTVVHCSAGIGRTG 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1838351042 1045 TFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYEVVL 1093
Cdd:cd14541    159 VLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAIL 207
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 865-1093 6.03e-62

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: 213.17  E-value: 6.03e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  865 NQSKNRYKNIIPYDHCRVVLQPSDtgnDYINASYVD----SYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGL 940
Cdd:cd14600     40 NMDKNRYKDVLPYDATRVVLQGNE---DYINASYVNmeipSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTL 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  941 VEQNKTKCEQYWPEQEQI--YGDFTVTLNNTRTTTGLITRIFSLHKAGCGFPRVVEQFHYLLWPDHGVPRNSAQLLCLVD 1018
Cdd:cd14600    117 TERGRTKCHQYWPDPPDVmeYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVPDDSSDFLEFVN 196

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1838351042 1019 VVNKRALEAPagPVVVHCSAGIGRTGTFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYEVVL 1093
Cdd:cd14600    197 YVRSKRVENE--PVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAIL 269
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 869-1093 9.30e-62

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: 210.95  E-value: 9.30e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  869 NRYKNIIPYDHCRVVLQ--PSDTGNDYINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQNKT 946
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSqlGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  947 KCEQYWPEQEQ--IYGDFTVTLNNTRTTTGLITRIFSLHKAGCGFPRVVEQFHYLLWPDHGVPRNSAQLLCLVDVVNKRA 1024
Cdd:cd14618     81 LCDHYWPSESTpvSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVREHV 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1025 LEAP-AGPVVVHCSAGIGRTGTFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYEVVL 1093
Cdd:cd14618    161 QATKgKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 892-1092 1.48e-61

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: 209.09  E-value: 1.48e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  892 DYINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQNKTKCEQYWPEQEQI-YGDFTVTLNNTR 970
Cdd:cd14622      1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVtHGEITIEIKNDT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  971 TTTGLITRIFSLHKAGCGFPRVVEQFHYLLWPDHGVPRNSAQLLCLVDVVNKRALEAPAGPVVVHCSAGIGRTGTFIALD 1050
Cdd:cd14622     81 LLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTGNHPIVVHCSAGAGRTGTFIALS 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1838351042 1051 FLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYEVV 1092
Cdd:cd14622    161 NILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 858-1094 2.09e-61

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: 211.22  E-value: 2.09e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  858 NAGKELCNQSKNRYKNIIPYDHCRVVLQP--SDTGNDYINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIV 935
Cdd:cd14603     23 VAGGRKENVKKNRYKDILPYDQTRVILSLlqEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVIL 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  936 MLTGLVEQNKTKCEQYWPEQEQI--YGDFTVT-LNNTRTTTGLITRIFSLHKagCGFPRVVEQFHYLLWPDHGVPRNSAQ 1012
Cdd:cd14603    103 MACREIEMGKKKCERYWAQEQEPlqTGPFTITlVKEKRLNEEVILRTLKVTF--QKESRSVSHFQYMAWPDHGIPDSPDC 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1013 LLCLVDVVNKRALEAPAgPVVVHCSAGIGRTGTFIALDF---LLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLY 1089
Cdd:cd14603    181 MLAMIELARRLQGSGPE-PLCVHCSAGCGRTGVICTVDYvrqLLLTQRIPPDFSIFDVVLEMRKQRPAAVQTEEQYEFLY 259


                   ....*
gi 1838351042 1090 EVVLE 1094
Cdd:cd14603    260 HTVAQ 264
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 815-1092 2.50e-60

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: 209.40  E-value: 2.50e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  815 EALKRFKRaEIEAEQTEDESVNTHGAGRLGEYQQLSSSL----MHPCNAGKELCNQSKNRYKNIIPYDHCRV--VLQPSD 888
Cdd:cd14604      4 EILKKFIE-RVQAMKSTDHNGEDNFASDFMRLRRLSTKYrtekIYPTATGEKEENVKKNRYKDILPFDHSRVklTLKTSS 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  889 TGNDYINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQNKTKCEQYWP---EQEQIYGDFTVT 965
Cdd:cd14604     83 QDSDYINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPlygEEPMTFGPFRIS 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  966 LNNTRTTTGLITRIFSLHkagcgF---PRVVEQFHYLLWPDHGVPRNSAQLLCLVDVVNKRAlEAPAGPVVVHCSAGIGR 1042
Cdd:cd14604    163 CEAEQARTDYFIRTLLLE-----FqneTRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQ-EHEDVPICIHCSAGCGR 236

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1838351042 1043 TGTFIALDF---LLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYEVV 1092
Cdd:cd14604    237 TGAICAIDYtwnLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 289
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 865-1093 2.93e-60

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: 206.60  E-value: 2.93e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  865 NQSKNRYKNIIPYDHCRVVLQPSdtgNDYINASYVdsyRSP-----RFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTG 939
Cdd:cd14597      3 NRKKNRYKNILPYDTTRVPLGDE---GGYINASFI---KMPvgdeeFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQ 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  940 LVEQNKTKCEQYWPEQ----EQIYGDFTVTLNNTRTTTGLITRIFSLHKAGCGFPRVVEQFHYLLWPDHGVPRNSAQLLC 1015
Cdd:cd14597     77 EVEGGKIKCQRYWPEIlgktTMVDNRLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLLT 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1838351042 1016 LVDVVnkRALEApAGPVVVHCSAGIGRTGTFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYEVVL 1093
Cdd:cd14597    157 FISYM--RHIHK-SGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVIL 231
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 869-1090 9.77e-60

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: 204.76  E-value: 9.77e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  869 NRYKNIIPYDHCRVVL--QPSDTGNDYINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQNKT 946
Cdd:cd14616      1 NRFPNIKPYNNNRVKLiaDAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  947 KCEQYWPEQEQ---IYGDFTVTLNNTRTTTGLITRIFSLHKAGCGFprVVEQFHYLLWPDHGVPRNSAQLLCLVDVVN-K 1022
Cdd:cd14616     81 RCHQYWPEDNKpvtVFGDIVITKLMEDVQIDWTIRDLKIERHGDYM--MVRQCNFTSWPEHGVPESSAPLIHFVKLVRaS 158

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1838351042 1023 RALEAPagPVVVHCSAGIGRTGTFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYE 1090
Cdd:cd14616    159 RAHDNT--PMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 845-1096 1.81e-59

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


Pssm-ID: 350477 [Multi-domain]  Cd Length: 291  Bit Score: 206.50  E-value: 1.81e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  845 EYQQLSSSLMHPCN--AGKELCNQSKNRYKNIIPYDHCRVVLQP--SDTGNDYINASYVDSYRSPRFFIAAQGPLPGTVL 920
Cdd:cd14629     31 EFKLLANSKAHTSRfiSANLPCNKFKNRLVNIMPYELTRVCLQPirGVEGSDYINASFIDGYRQQKAYIATQGPLAETTE 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  921 DFWQMVWQEKTSVIVMLTGLVEQNKTKCEQYWP-EQEQIYGDFTVTLNNTRTTTGLITRIFSLHKAGCGFPRVVEQFHYL 999
Cdd:cd14629    111 DFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPaERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFT 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1000 LWPDHGVPRNSAQLLCLVDVVNKRALE-APAGPVVVHCSAGIGRTGTFIALDFLLKMGKAEGKVDVFHCVQRLREQRISM 1078
Cdd:cd14629    191 DWPEQGVPKTGEGFIDFIGQVHKTKEQfGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAM 270

                          250
                   ....*....|....*...
gi 1838351042 1079 VQTKEQYTFLYEVVLEGL 1096
Cdd:cd14629    271 VQTEDQYQLCYRAALEYL 288
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 868-1094 2.41e-59

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: 203.92  E-value: 2.41e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  868 KNRYKNIIPYDHCRVVLQ--PSDTGNDYINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQNK 945
Cdd:cd14602      1 KNRYKDILPYDHSRVELSliTSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  946 TKCEQYWPE--QEQI-YGDFTVTLNNTRTTTGLITRIFslhKAGCG-FPRVVEQFHYLLWPDHGVPRNSAQLLCLV-DVV 1020
Cdd:cd14602     81 KKCERYWAEpgEMQLeFGPFSVTCEAEKRKSDYIIRTL---KVKFNsETRTIYQFHYKNWPDHDVPSSIDPILELIwDVR 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1838351042 1021 NKRALEAPagPVVVHCSAGIGRTGTFIALDF---LLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYEVVLE 1094
Cdd:cd14602    158 CYQEDDSV--PICIHCSAGCGRTGVICAIDYtwmLLKDGIIPENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIE 232
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 867-1089 3.77e-59

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: 203.23  E-value: 3.77e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  867 SKNRYKNIIPYDHCRVVLQP---SDTGNDYINASYVDSYRS-PRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVE 942
Cdd:cd14611      1 TKNRYKTILPNPHSRVCLKPknsNDSLSTYINANYIRGYGGkEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  943 QNKtKCEQYWPEQEQIYGDFTVTLNNTRTTTGLITRIFSLhKAGcGFPRVVEQFHYLLWPDHGVPRNSAQLLCLVDVVNK 1022
Cdd:cd14611     81 KNE-KCVLYWPEKRGIYGKVEVLVNSVKECDNYTIRNLTL-KQG-SQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDVEE 157

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1838351042 1023 RALEAPA-GPVVVHCSAGIGRTGTFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLY 1089
Cdd:cd14611    158 DRLASPGrGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 845-1094 4.02e-58

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


Pssm-ID: 350458 [Multi-domain]  Cd Length: 283  Bit Score: 202.59  E-value: 4.02e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  845 EYQQLSSSLMHP--CNAGKELCNQSKNRYKNIIPYDHCRVVL--QPSDTGNDYINASYVDSY--RSPRFfIAAQGPLPGT 918
Cdd:cd14610     22 EWEALCAYQAEPnaTNVAQREENVQKNRSLAVLPYDHSRIILkaENSHSHSDYINASPIMDHdpRNPAY-IATQGPLPAT 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  919 VLDFWQMVWQEKTSVIVMLTGLVEQNKTKCEQYWP-EQEQIYGDFTVTLNNTRT-TTGLITRIFSLHKAGCGFPRVVEQF 996
Cdd:cd14610    101 VADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPdEGSNLYHIYEVNLVSEHIwCEDFLVRSFYLKNLQTNETRTVTQF 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  997 HYLLWPDHGVPRNSAQLLCLVDVVNKrALEAPAGPVVVHCSAGIGRTGTFIALDFLL-KMGKAEGKVDVFHCVQRLREQR 1075
Cdd:cd14610    181 HFLSWNDQGVPASTRSLLDFRRKVNK-CYRGRSCPIIVHCSDGAGRSGTYILIDMVLnKMAKGAKEIDIAATLEHLRDQR 259

                          250
                   ....*....|....*....
gi 1838351042 1076 ISMVQTKEQYTFLYEVVLE 1094
Cdd:cd14610    260 PGMVQTKEQFEFALTAVAE 278
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 868-1092 5.35e-58

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: 201.24  E-value: 5.35e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  868 KNRYKNIIPYDHCRVVLQPSDTGN---DYINASYVDSY-RSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQ 943
Cdd:cd14613     28 KNRYKTILPNPHSRVCLTSPDQDDplsSYINANYIRGYgGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  944 NKtKCEQYWPEQEQIYGDFTVTLNNTRTTTGLITRIFSLhKAGcGFPRVVEQFHYLLWPDHGVPRNSAQLLCLVDVVNKR 1023
Cdd:cd14613    108 NE-KCTEYWPEEQVTYEGIEITVKQVIHADDYRLRLITL-KSG-GEERGLKHYWYTSWPDQKTPDNAPPLLQLVQEVEEA 184

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1838351042 1024 ALEAPA--GPVVVHCSAGIGRTGTFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYEVV 1092
Cdd:cd14613    185 RQQAEPncGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVHHVL 255
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 842-1092 9.86e-58

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: 200.19  E-value: 9.86e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  842 RLGEYQQLSSSLMHPCNAGKElcNQSKNRYKNIIPYDHCRVVLQpsDTGNDYINASYVDSYRSPRFFIAAQGPLPGTVLD 921
Cdd:cd14607      3 LYLEIRNESHDYPHRVAKYPE--NRNRNRYRDVSPYDHSRVKLQ--NTENDYINASLVVIEEAQRSYILTQGPLPNTCCH 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  922 FWQMVWQEKTSVIVMLTGLVEQNKTKCEQYWPEQEQ---IYGD--FTVTLNNTRTTTGLITRIFSLHKAGCGFPRVVEQF 996
Cdd:cd14607     79 FWLMVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEevlSFKEtgFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHF 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  997 HYLLWPDHGVPRNSAQLL-CLVDVVNKRALEAPAGPVVVHCSAGIGRTGTFIALDF-LLKMGKAEG-KVDVFHCVQRLRE 1073
Cdd:cd14607    159 HYTTWPDFGVPESPASFLnFLFKVRESGSLSPEHGPAVVHCSAGIGRSGTFSLVDTcLVLMEKKDPdSVDIKQVLLDMRK 238

                          250
                   ....*....|....*....
gi 1838351042 1074 QRISMVQTKEQYTFLYEVV 1092
Cdd:cd14607    239 YRMGLIQTPDQLRFSYMAV 257
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1127-1388 2.47e-57

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 199.04  E-value: 2.47e-57
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  1127 LEKEFKALQKFseLFQLLPCREAEKPTNQPKNRKPGILPADSCRPILMSSLNADGspGYINAVFVNTYTEEDRLIITQMP 1206
Cdd:smart00194    2 LEEEFEKLDRL--KPDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGS--DYINASYIDGPNGPKAYIATQGP 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  1207 FPNTVVDFWALVWDYTCTAVVVLNQLQELD-ETYAEFWPMQGEAA--YGRFHVQFISEEPGAGFTAWTLALTNKQQPKkp 1283
Cdd:smart00194   78 LPSTVEDFWRMVWEQKVTVIVMLTELVEKGrEKCAQYWPDEEGEPltYGDITVTLKSVEKVDDYTIRTLEVTNTGCSE-- 155

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  1284 PLEVRFWQLKDWPmKQHLPPHPATIISLLGNVEtHHRQSRDGHILITCWDGASRSGIFCAAGFLCEQIQSEGLVDVSQAV 1363
Cdd:smart00194  156 TRTVTHYHYTNWP-DHGVPESPESILDLIRAVR-KSQSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIV 233

                           250       260
                    ....*....|....*....|....*
gi 1838351042  1364 RMLKRRRRQLIKDVEQYGLCYELAL 1388
Cdd:smart00194  234 KELRSQRPGMVQTEEQYIFLYRAIL 258
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 870-1094 6.09e-57

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: 196.80  E-value: 6.09e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  870 RYKNIIPYDHCRVVL--QPSDTGNDYINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQNKTK 947
Cdd:cd14623      1 RVLQIIPYEFNRVIIpvKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  948 CEQYWPEQEQI-YGDFTVTLNNTRTTTGLITRIFSLHKAGCGFPRVVEQFHYLLWPDHGVPRNSAQLLCLVDVVNKRALE 1026
Cdd:cd14623     81 CAQYWPSDGSVsYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQQ 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1838351042 1027 APAGPVVVHCSAGIGRTGTFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYEVVLE 1094
Cdd:cd14623    161 SGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 845-1095 2.63e-56

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: 197.17  E-value: 2.63e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  845 EYQQLSSSLmhPCNAGKELCNQSKNRYKNIIPYDHCRVVLQPSDtgNDYINASYVDSYRSPRFFIAAQGPLPGTVLDFWQ 924
Cdd:cd14608      7 DIRHEASDF--PCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQED--NDYINASLIKMEEAQRSYILTQGPLPNTCGHFWE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  925 MVWQEKTSVIVMLTGLVEQNKTKCEQYWP---EQEQIYGD--FTVTLNNTRTTTGLITRIFSLHKAGCGFPRVVEQFHYL 999
Cdd:cd14608     83 MVWEQKSRGVVMLNRVMEKGSLKCAQYWPqkeEKEMIFEDtnLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYT 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1000 LWPDHGVPRNSAQLL-CLVDVVNKRALEAPAGPVVVHCSAGIGRTGTFIALD---FLLKMGKAEGKVDVFHCVQRLREQR 1075
Cdd:cd14608    163 TWPDFGVPESPASFLnFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADtclLLMDKRKDPSSVDIKKVLLEMRKFR 242

                          250       260
                   ....*....|....*....|
gi 1838351042 1076 ISMVQTKEQYTFLYEVVLEG 1095
Cdd:cd14608    243 MGLIQTADQLRFSYLAVIEG 262
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 845-1094 2.89e-56

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: 197.18  E-value: 2.89e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  845 EYQQLSSSLMHP--CNAGKELCNQSKNRYKNIIPYDHCRVVLQ----PSDTgnDYINASYVDSYrSPRF--FIAAQGPLP 916
Cdd:cd14609     20 EWQALCAYQAEPntCSTAQGEANVKKNRNPDFVPYDHARIKLKaesnPSRS--DYINASPIIEH-DPRMpaYIATQGPLS 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  917 GTVLDFWQMVWQEKTSVIVMLTGLVEQNKTKCEQYWP-EQEQIYGDFTVTLNNTRT-TTGLITRIFSLHKAGCGFPRVVE 994
Cdd:cd14609     97 HTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPdEGSSLYHIYEVNLVSEHIwCEDFLVRSFYLKNVQTQETRTLT 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  995 QFHYLLWPDHGVPRNSAQLLCLVDVVNKrALEAPAGPVVVHCSAGIGRTGTFIALDFLL-KMGKAEGKVDVFHCVQRLRE 1073
Cdd:cd14609    177 QFHFLSWPAEGIPSSTRPLLDFRRKVNK-CYRGRSCPIIVHCSDGAGRTGTYILIDMVLnRMAKGVKEIDIAATLEHVRD 255

                          250       260
                   ....*....|....*....|.
gi 1838351042 1074 QRISMVQTKEQYTFLYEVVLE 1094
Cdd:cd14609    256 QRPGMVRTKDQFEFALTAVAE 276
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 1185-1385 1.62e-55

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: 191.85  E-value: 1.62e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1185 YINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQELDETYAEFWPMQGEAAYGRFHVQFISEEPG 1264
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQSCPQYWPDEGSGTYGPIQVEFVSTTID 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1265 AGFTAWTLALTNKQQPKKPPLEVRFWQLKDWPMKQHLPPHPATIISLLGNVETHHRQSRDGHILITCWDGASRSGIFCAA 1344
Cdd:cd14556     81 EDVISRIFRLQNTTRPQEGYRMVQQFQFLGWPRDRDTPPSKRALLKLLSEVEKWQEQSGEGPIVVHCLNGVGRSGVFCAI 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1838351042 1345 GFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQYGLCYE 1385
Cdd:cd14556    161 SSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 893-1089 1.79e-55

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: 191.48  E-value: 1.79e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  893 YINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQNKTKCEQYWPEQEQ---IYGDFTVTL-NN 968
Cdd:cd14542      1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEeqlQFGPFKISLeKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  969 TRTTTGLITRIFslhKAGCGF-PRVVEQFHYLLWPDHGVPRNSAQLLCLVDVVnKRALEAPAGPVVVHCSAGIGRTGTFI 1047
Cdd:cd14542     81 KRVGPDFLIRTL---KVTFQKeSRTVYQFHYTAWPDHGVPSSVDPILDLVRLV-RDYQGSEDVPICVHCSAGCGRTGTIC 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1838351042 1048 ALDF---LLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLY 1089
Cdd:cd14542    157 AIDYvwnLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVY 201
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 893-1096 6.63e-55

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: 190.34  E-value: 6.63e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  893 YINASYVdsyRSP-----RFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQNKTKCEQYWPEQEQI---YGDFTV 964
Cdd:cd14596      1 YINASYI---TMPvgeeeLFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEpmeLENYQL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  965 TLNNTRTTTGLITRIFSLHKAGCGFPRVVEQFHYLLWPDHGVPRNSAQLLCLVDVVNKRALEapaGPVVVHCSAGIGRTG 1044
Cdd:cd14596     78 RLENYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNT---GPIVVHCSAGIGRAG 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1838351042 1045 TFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYEVVLEGL 1096
Cdd:cd14596    155 VLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVL 206
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1154-1388 6.96e-53

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 185.52  E-value: 6.96e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1154 NQPKNRKPGILPADSCRPILMSSlnaDGSPGYINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQ 1233
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGD---PGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1234 ELD-ETYAEFWP--MQGEAAYGRFHVQFISEEP-GAGFTAWTLALTNKQQpkKPPLEVRFWQLKDWPmKQHLPPHPATII 1309
Cdd:pfam00102   78 EKGrEKCAQYWPeeEGESLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGS--EETRTVKHFHYTGWP-DHGVPESPNSLL 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1838351042 1310 SLLGNVETHHRQSRDGHILITCWDGASRSGIFCAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQYGLCYELAL 1388
Cdd:pfam00102  155 DLLRKVRKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 893-1090 6.56e-52

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: 181.45  E-value: 6.56e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  893 YINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQNKTkCEQYWPEQEQ-IYGDFTVTLNNTRT 971
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQLDPKDQS-CPQYWPDEGSgTYGPIQVEFVSTTI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  972 TTGLITRIFSL-------HKAgcgfpRVVEQFHYLLWPDHG-VPRNSAQLLCLVDVVNKRALEAPAGPVVVHCSAGIGRT 1043
Cdd:cd14556     80 DEDVISRIFRLqnttrpqEGY-----RMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQEQSGEGPIVVHCLNGVGRS 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1838351042 1044 GTFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYE 1090
Cdd:cd14556    155 GVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 893-1094 1.13e-51

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: 181.10  E-value: 1.13e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  893 YINASYV--DSYRSPrFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQNKTKCEQYWPEQ-EQIYGDFTVTLNNT 969
Cdd:cd14546      1 YINASTIydHDPRNP-AYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEgSEVYHIYEVHLVSE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  970 RT-TTGLITRIFSLHKAGCGFPRVVEQFHYLLWPDHGVPRNSAQLLCLVDVVNKrALEAPAGPVVVHCSAGIGRTGTFIA 1048
Cdd:cd14546     80 HIwCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNK-SYRGRSCPIVVHCSDGAGRTGTYIL 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1838351042 1049 LDFLL-KMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYEVVLE 1094
Cdd:cd14546    159 IDMVLnRMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAE 205
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 893-1096 1.71e-51

catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21) and type 14 (PTPN14) belong to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Both PTPN21 and PTPN14 contain an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350388 [Multi-domain]  Cd Length: 219  Bit Score: 180.73  E-value: 1.71e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  893 YINASYVDSY--RSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQNKTKCEQYWP-----EQEQIYGDFTVT 965
Cdd:cd14540      1 YINASHITATvgGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPtlggeHDALTFGEYKVS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  966 LNNTRTTTGLITRIFSLHKAGCGFPRVVEQFHYLLWPDHGVPRNSAQLLCLVDVVN---KRALEAPAG-----PVVVHCS 1037
Cdd:cd14540     81 TKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINsvrRHTNQDVAGhnrnpPTLVHCS 160

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1838351042 1038 AGIGRTGTFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYEVVLEGL 1096
Cdd:cd14540    161 AGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
862-1088 7.38e-51

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 181.44  E-value: 7.38e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  862 ELCNQSK-NRYKNIIPYDHcrVVLQPSDTgndYINASYVDSYRsPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGL 940
Cdd:COG5599     38 QNINGSPlNRFRDIQPYKE--TALRANLG---YLNANYIQVIG-NHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASD 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  941 VE--QNKTKCEQYWPEQEQiYGDFTVTLNNTRTT---TGLITRIFSLHKAGCGFP-RVVEQFHYLLWPDHGvPRNSAQLL 1014
Cdd:COG5599    112 DEisKPKVKMPVYFRQDGE-YGKYEVSSELTESIqlrDGIEARTYVLTIKGTGQKkIEIPVLHVKNWPDHG-AISAEALK 189

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1838351042 1015 CLVDVVNKRA--LEAPAGPVVVHCSAGIGRTGTFIALDFLLKMGKAEG--KVDVFHCVQRLREQR-ISMVQTKEQYTFL 1088
Cdd:COG5599    190 NLADLIDKKEkiKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRnGGMVQTSEQLDVL 268
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 893-1090 5.44e-50

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: 176.12  E-value: 5.44e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  893 YINASYV--DSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQNKT-KCEQYWP---EQEQIYGDFTVTL 966
Cdd:cd17658      1 YINASLVetPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPaeeNESREFGRISVTN 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  967 NNTRTT-TGLITRIFSL-HKAGCGFPRVVEQFHYLLWPDHGVPRNSAQLLCLVdvvnKRALEAP--AGPVVVHCSAGIGR 1042
Cdd:cd17658     81 KKLKHSqHSITLRVLEVqYIESEEPPLSVLHIQYPEWPDHGVPKDTRSVRELL----KRLYGIPpsAGPIVVHCSAGIGR 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1838351042 1043 TGTFIALDFLLK---MGKAEGkVDVFHCVQRLREQRISMVQTKEQYTFLYE 1090
Cdd:cd17658    157 TGAYCTIHNTIRrilEGDMSA-VDLSKTVRKFRSQRIGMVQTQDQYIFCYA 206
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 892-1094 7.66e-49

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


Pssm-ID: 350449 [Multi-domain]  Cd Length: 212  Bit Score: 173.21  E-value: 7.66e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  892 DYINASYVD----SYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQNKTKCEQYWPE--QEQIYGDFTVT 965
Cdd:cd14601      1 DYINANYINmeipSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEpsGSSSYGGFQVT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  966 LNNTRTTTGLITRIFSLHKAGCGFPRVVEQFHYLLWPDHGVPRNSAQLLCLVDVVNKRALEAPAgPVVVHCSAGIGRTGT 1045
Cdd:cd14601     81 CHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDE-PVVVHCSAGIGRTGV 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1838351042 1046 FIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYEVVLE 1094
Cdd:cd14601    160 LITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 208
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 857-1094 1.05e-48

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 175.96  E-value: 1.05e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  857 CNAGKELCNQSKNRYKNIIPYDHCRVVLQPSDTGNDYINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVM 936
Cdd:PHA02742    44 CNESLELKNMKKCRYPDAPCFDRNRVILKIEDGGDDFINASYVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVM 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  937 LTGLVEQNKTKCEQYWPEQEQ---IYGDFTVTLNNTRTTTGLITRIFSLHKAGCGFPRVVEQFHYLLWPDHGVPRNSAQL 1013
Cdd:PHA02742   124 ITKIMEDGKEACYPYWMPHERgkaTHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKF 203

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1014 LCLV----------DVVNKRALEAPAGPVVVHCSAGIGRTGTFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKE 1083
Cdd:PHA02742   204 LDFVlavreadlkaDVDIKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQ 283

                          250
                   ....*....|.
gi 1838351042 1084 QYTFLYEVVLE 1094
Cdd:PHA02742   284 QYIFCYFIVLI 294
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 893-1090 1.62e-47

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: 169.10  E-value: 1.62e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  893 YINASYVDSYR--SPRFfIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQNKTKCEQYWPE---QEQIYGDFTVTLN 967
Cdd:cd14539      1 YINASLIEDLTpyCPRF-IATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTergQALVYGAITVSLQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  968 NTRTTTGLITRIFSLHKAGCGFPRVVEQFHYLLWPDHGVPRNSAQLLCLVDVVN-----KRALEApagPVVVHCSAGIGR 1042
Cdd:cd14539     80 SVRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHshylqQRSLQT---PIVVHCSSGVGR 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1838351042 1043 TGTFIAL-DFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYE 1090
Cdd:cd14539    157 TGAFCLLyAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 1185-1385 7.72e-46

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: 164.00  E-value: 7.72e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1185 YINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQELD-ETYAEFWPMQGEAA--YGRFHVQFISE 1261
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGrEKCERYWPEEGGKPleYGDITVTLVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1262 EPGAGFTAWTLALTNKQQPKkpPLEVRFWQLKDWPmKQHLPPHPATIISLLGNVETHHRQSrDGHILITCWDGASRSGIF 1341
Cdd:cd00047     81 EELSDYTIRTLELSPKGCSE--SREVTHLHYTGWP-DHGVPSSPEDLLALVRRVRKEARKP-NGPIVVHCSAGVGRTGTF 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1838351042 1342 CAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQYGLCYE 1385
Cdd:cd00047    157 IAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 865-1096 4.59e-45

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: 164.79  E-value: 4.59e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  865 NQSKNRYKNIIPYDHCRVVLQPSDTGND-YINASYVDSYRSPR--FFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLV 941
Cdd:cd14599     38 NAERNRIREVVPYEENRVELVPTKENNTgYINASHIKVTVGGEewHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEE 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  942 EQNKTKCEQYWPE-----QEQIYGDFTVTlNNTRT------TTGL-ITRIFSlhkagcGFPRVVEQFHYLLWPDHGVPRN 1009
Cdd:cd14599    118 EGGRSKSHRYWPKlgskhSSATYGKFKVT-TKFRTdsgcyaTTGLkVKHLLS------GQERTVWHLQYTDWPDHGCPEE 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1010 SAQLLCLVDVVN------KRALEAPAG---PVVVHCSAGIGRTGTFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQ 1080
Cdd:cd14599    191 VQGFLSYLEEIQsvrrhtNSMLDSTKNcnpPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVEVPVMLRHLREQRMFMIQ 270

                          250
                   ....*....|....*.
gi 1838351042 1081 TKEQYTFLYEVVLEGL 1096
Cdd:cd14599    271 TIAQYKFVYQVLIQFL 286
PHA02738 PHA02738
hypothetical protein; Provisional
 862-1092 1.96e-43

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 161.25  E-value: 1.96e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  862 ELCNQSKNRYKNIIPYDHCRVVLQPSDTGNDYINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLV 941
Cdd:PHA02738    46 EKKNRKLNRYLDAVCFDHSRVILPAERNRGDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKK 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  942 EQNKTKCEQYWPEQEQ---IYGDFTVTLNNTRTTTGLITRIFSLHKaGCGFPRVVEQFHYLLWPDHGVPRNSAQLLCLVD 1018
Cdd:PHA02738   126 ENGREKCFPYWSDVEQgsiRFGKFKITTTQVETHPHYVKSTLLLTD-GTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVL 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1019 VVNK--------------RALEAPagPVVVHCSAGIGRTGTFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQ 1084
Cdd:PHA02738   205 EVRQcqkelaqeslqighNRLQPP--PIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQ 282


                   ....*...
gi 1838351042 1085 YTFLYEVV 1092
Cdd:PHA02738   283 YFFCYRAV 290
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 865-1093 1.21e-42

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 158.63  E-value: 1.21e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  865 NQSKNRYKNIIPYDHCRVVLQP-SDTGNDYINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQ 943
Cdd:PHA02747    51 NQPKNRYWDIPCWDHNRVILDSgGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPTKGT 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  944 N-KTKCEQYWPEQEQ---IYGDFTV-TLNNTRTTTGLITRIFSLHKAgCGFPRVVEQFHYLLWPDHGVPRNSA---QLLC 1015
Cdd:PHA02747   131 NgEEKCYQYWCLNEDgniDMEDFRIeTLKTSVRAKYILTLIEITDKI-LKDSRKISHFQCSEWFEDETPSDHPdfiKFIK 209

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1016 LVDVVNKRAL------EAPAGPVVVHCSAGIGRTGTFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFL- 1088
Cdd:PHA02747   210 IIDINRKKSGklfnpkDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYLFIq 289


                   ....*..
gi 1838351042 1089 --YEVVL 1093
Cdd:PHA02747   290 pgYEVLH 296
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 865-1097 1.32e-41

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 155.96  E-value: 1.32e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  865 NQSKNRYKNIIPYDHCRVVLQ--------------PS-------DTGNDYINASYVDSYRSPRFFIAAQGPLPGTVLDFW 923
Cdd:PHA02746    51 NLKKNRFHDIPCWDHSRVVINaheslkmfdvgdsdGKkievtseDNAENYIHANFVDGFKEANKFICAQGPKEDTSEDFF 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  924 QMVWQEKTSVIVMLTGlVEQNKTKCEQYW--PE-QEQIYGDFTVTLNNTRTTTGLITRIFSLHKAGCGFPRVVEQFHYLL 1000
Cdd:PHA02746   131 KLISEHESQVIVSLTD-IDDDDEKCFELWtkEEdSELAFGRFVAKILDIIEELSFTKTRLMITDKISDTSREIHHFWFPD 209

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1001 WPDHGVPRNSAQLLCLVDVVNKRALE---------APAGPVVVHCSAGIGRTGTFIALDFLLKMGKAEGKVDVFHCVQRL 1071
Cdd:PHA02746   210 WPDNGIPTGMAEFLELINKVNEEQAElikqadndpQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIVLKI 289

                          250       260
                   ....*....|....*....|....*.
gi 1838351042 1072 REQRISMVQTKEQYTFLYEVVLEGLL 1097
Cdd:PHA02746   290 RKQRHSSVFLPEQYAFCYKALKYAII 315
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 1149-1388 2.98e-41

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: 152.29  E-value: 2.98e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1149 AEKPTNQPKNRKPGILPADSCRPILMSSLNADGSpGYINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVV 1228
Cdd:cd14554      1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEGS-DYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVM 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1229 LNQLQELD-ETYAEFWPMQGEAAYGRFHVQFISEEPGAGFTAWTLALTNKQQPKKPplEVRFWQLKDWPmKQHLPPHPAT 1307
Cdd:cd14554     80 LTKLREMGrEKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSR--TVRQFQFTDWP-EQGVPKSGEG 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1308 IISLLGNV-ETHHRQSRDGHILITCWDGASRSGIFCAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQYGLCYEL 1386
Cdd:cd14554    157 FIDFIGQVhKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236


                   ..
gi 1838351042 1387 AL 1388
Cdd:cd14554    237 AL 238
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 1100-1393 4.26e-41

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: 153.74  E-value: 4.26e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1100 STGVPVESITSHVRCLQEAEASRHNNVLEKEFKAL---QKFSELFQllpcrEAEKPTNQPKNRKPGILPADSCRPILMSS 1176
Cdd:cd14627      1 NTEVPARNLYSYIQKLAQVEVGEHVTGMELEFKRLansKAHTSRFI-----SANLPCNKFKNRLVNIMPYETTRVCLQPI 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1177 LNADGSpGYINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQELD-ETYAEFWPMQGEAAYGRFH 1255
Cdd:cd14627     76 RGVEGS-DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGrEKCHQYWPAERSARYQYFV 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1256 VQFISEEPGAGFTAWTLALTNKQQPKKPplEVRFWQLKDWPmKQHLPPHPATIISLLGNV-ETHHRQSRDGHILITCWDG 1334
Cdd:cd14627    155 VDPMAEYNMPQYILREFKVTDARDGQSR--TVRQFQFTDWP-EQGVPKSGEGFIDFIGQVhKTKEQFGQDGPISVHCSAG 231

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1838351042 1335 ASRSGIFCAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQYGLCYELALSYLNS 1393
Cdd:cd14627    232 VGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYLGS 290
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 1185-1388 7.43e-41

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: 149.79  E-value: 7.43e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1185 YINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNqlqELDETY--AEFWPMQGEAAYGRFHVQFISEE 1262
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLN---EMDAAQlcMQYWPEKTSCCYGPIQVEFVSAD 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1263 PGAGFTAWTLALTNKQQPKKPPLEVRFWQLKDWPMKQHLPPHPATIISLLGNVETHHRQ--SRDGHILITCWDGASRSGI 1340
Cdd:cd14634     78 IDEDIISRIFRICNMARPQDGYRIVQHLQYIGWPAYRDTPPSKRSILKVVRRLEKWQEQydGREGRTVVHCLNGGGRSGT 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1838351042 1341 FCAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQYGLCYELAL 1388
Cdd:cd14634    158 FCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVAL 205
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 1185-1388 1.18e-40

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: 149.29  E-value: 1.18e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1185 YINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQELDETYA--EFWPMQGEAAYGRFHVQFISEE 1262
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAWPclQYWPEPGLQQYGPMEVEFVSGS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1263 PGAGFTAWTLALTNKQQPKKPPLEVRFWQLKDWPMKQHLPPHPATIISLLGNVETHHRQSRDGHILITCWDGASRSGIFC 1342
Cdd:cd14637     81 ADEDIVTRLFRVQNITRLQEGHLMVRHFQFLRWSAYRDTPDSKKAFLHLLASVEKWQRESGEGRTVVHCLNGGGRSGTYC 160

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1838351042 1343 AAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQYGLCYELAL 1388
Cdd:cd14637    161 ASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIAL 206
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 1101-1395 2.91e-40

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: 151.42  E-value: 2.91e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1101 TGVPVESITSHVRCLQEAEASRHNNVLEKEFKALQkfSELFQLLPCREAEKPTNQPKNRKPGILPADSCRPILMSSLNAD 1180
Cdd:cd14628      1 TEVPARNLYAYIQKLTQIETGENVTGMELEFKRLA--SSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGVE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1181 GSpGYINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQELD-ETYAEFWPMQGEAAYGRFHVQFI 1259
Cdd:cd14628     79 GS-DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGrEKCHQYWPAERSARYQYFVVDPM 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1260 SEEPGAGFTAWTLALTNKQQPKKPplEVRFWQLKDWPmKQHLPPHPATIISLLGNV-ETHHRQSRDGHILITCWDGASRS 1338
Cdd:cd14628    158 AEYNMPQYILREFKVTDARDGQSR--TVRQFQFTDWP-EQGVPKSGEGFIDFIGQVhKTKEQFGQDGPISVHCSAGVGRT 234

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1838351042 1339 GIFCAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQYGLCYELALSYLNSFE 1395
Cdd:cd14628    235 GVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYLGSFD 291
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 893-1094 4.39e-40

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: 147.86  E-value: 4.39e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  893 YINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTglvEQNKTK-CEQYWPEQEQ-IYGDFTVTLNNTR 970
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLN---EMDAAQlCMQYWPEKTScCYGPIQVEFVSAD 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  971 TTTGLITRIF---SLHKAGCGFpRVVEQFHYLLWPDH-GVPRNSAQLLCLVDVVNK--RALEAPAGPVVVHCSAGIGRTG 1044
Cdd:cd14634     78 IDEDIISRIFricNMARPQDGY-RIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKwqEQYDGREGRTVVHCLNGGGRSG 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1045 TFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYEVVLE 1094
Cdd:cd14634    157 TFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 1185-1388 1.57e-38

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: 143.24  E-value: 1.57e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1185 YINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLqELDETYAEFWPMQGEAAYGRFHVQFISEEPG 1264
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEV-DLAQGCPQYWPEEGMLRYGPIQVECMSCSMD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1265 AGFTAWTLALTNKQQPKKPPLEVRFWQLKDWPMKQHLPPHPATIISLLGNVETHHRQSR--DGHILITCWDGASRSGIFC 1342
Cdd:cd14636     80 CDVISRIFRICNLTRPQEGYLMVQQFQYLGWASHREVPGSKRSFLKLILQVEKWQEECDegEGRTIIHCLNGGGRSGMFC 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1838351042 1343 AAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQYGLCYELAL 1388
Cdd:cd14636    160 AISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVAL 205
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 1185-1385 1.75e-38

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: 142.79  E-value: 1.75e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1185 YINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQELD-ETYAEFWPMQGEAAYGRFHVQFISEEP 1263
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSqNKCAQYWPEDGSVSSGDITVELKDQTD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1264 GAGFTAWTLALTNKQQPKKPplEVRFWQLKDWPmKQHLPPHPATIISLLGNVETHHRQSRDGHILITCWDGASRSGIFCA 1343
Cdd:cd14552     81 YEDYTLRDFLVTKGKGGSTR--TVRQFHFHGWP-EVGIPDNGKGMIDLIAAVQKQQQQSGNHPITVHCSAGAGRTGTFCA 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1838351042 1344 AGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQYGLCYE 1385
Cdd:cd14552    158 LSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYK 199
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 1101-1394 1.98e-38

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: 146.02  E-value: 1.98e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1101 TGVPVESITSHVRCLQEAEASRHNNVLEKEFKALQkfSELFQLLPCREAEKPTNQPKNRKPGILPADSCRPILMSSLNAD 1180
Cdd:cd14629      2 TEVPARNLYAHIQKLTQVPPGESVTAMELEFKLLA--NSKAHTSRFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGVE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1181 GSpGYINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQELD-ETYAEFWPMQGEAAYGRFHVQFI 1259
Cdd:cd14629     80 GS-DYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGrEKCHQYWPAERSARYQYFVVDPM 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1260 SEEPGAGFTAWTLALTNKQQPKKPplEVRFWQLKDWPmKQHLPPHPATIISLLGNV-ETHHRQSRDGHILITCWDGASRS 1338
Cdd:cd14629    159 AEYNMPQYILREFKVTDARDGQSR--TIRQFQFTDWP-EQGVPKTGEGFIDFIGQVhKTKEQFGQDGPITVHCSAGVGRT 235

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1838351042 1339 GIFCAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQYGLCYELALSYLNSF 1394
Cdd:cd14629    236 GVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEYLGSF 291
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 893-1094 6.61e-38

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: 141.32  E-value: 6.61e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  893 YINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTglvEQNKTK-CEQYWPEQEQI-YGDFTVTLNNTR 970
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLN---EVDLAQgCPQYWPEEGMLrYGPIQVECMSCS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  971 TTTGLITRIFSLhkagCGFPR------VVEQFHYLLWPDH-GVPRNSAQLLCLVDVVNKRALEAPAGP--VVVHCSAGIG 1041
Cdd:cd14636     78 MDCDVISRIFRI----CNLTRpqegylMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEECDEGEgrTIIHCLNGGG 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1838351042 1042 RTGTFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYEVVLE 1094
Cdd:cd14636    154 RSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVALE 206
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 1185-1390 6.28e-37

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: 138.60  E-value: 6.28e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1185 YINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQELD-ETYAEFWPMQGEAAYGRFHVQFISEEP 1263
Cdd:cd14622      2 YINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREqEKCVQYWPSEGSVTHGEITIEIKNDTL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1264 GAGFTAWTLALTNKQQpkKPPLEVRFWQLKDWPmKQHLPPHPATIISLLGNVETHHRQSRDGHILITCWDGASRSGIFCA 1343
Cdd:cd14622     82 LETISIRDFLVTYNQE--KQTRLVRQFHFHGWP-EIGIPAEGKGMIDLIAAVQKQQQQTGNHPIVVHCSAGAGRTGTFIA 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1838351042 1344 AGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQYGLCYELALSY 1390
Cdd:cd14622    159 LSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQDF 205
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 893-1096 4.19e-36

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: 136.64  E-value: 4.19e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  893 YINASYVD-SYRSPRF-FIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQNKTKCEQYWP-----EQEQIYGDFTVT 965
Cdd:cd14598      1 YINASHIKvTVGGKEWdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlgsrHNTVTYGRFKIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  966 LNnTRT------TTGL-ITRIFSlhkagcGFPRVVEQFHYLLWPDHGVPRNSAQLLCLVDVVN--KRAL------EAPAG 1030
Cdd:cd14598     81 TR-FRTdsgcyaTTGLkIKHLLT------GQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQsvRRHTnstidpKSPNP 153

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1838351042 1031 PVVVHCSAGIGRTGTFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYEVVLEGL 1096
Cdd:cd14598    154 PVLVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFL 219
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 1185-1388 1.00e-35

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: 135.20  E-value: 1.00e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1185 YINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQELdETYAEFWPMQGEAAYGRFHVQFISEEPG 1264
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPA-QLCPQYWPENGVHRHGPIQVEFVSADLE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1265 AGFTAWTLALTNKQQPKKPPLEVRFWQLKDWPMKQHLPPHPATIISLLGNVETHHRQ--SRDGHILITCWDGASRSGIFC 1342
Cdd:cd14635     80 EDIISRIFRIYNAARPQDGYRMVQQFQFLGWPMYRDTPVSKRSFLKLIRQVDKWQEEynGGEGRTVVHCLNGGGRSGTFC 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1838351042 1343 AAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQYGLCYELAL 1388
Cdd:cd14635    160 AISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVAL 205
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 1163-1386 1.25e-35

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: 135.56  E-value: 1.25e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1163 ILPADSCR---PILMSSLNADgspgYINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQEL-DET 1238
Cdd:cd14623      5 IIPYEFNRviiPVKRGEENTD----YVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERgQEK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1239 YAEFWPMQGEAAYGRFHVQFISEEPGAGFTAWTLALTNKQQPKKPplEVRFWQLKDWPmKQHLPPHPATIISLLGNVETH 1318
Cdd:cd14623     81 CAQYWPSDGSVSYGDITIELKKEEECESYTVRDLLVTNTRENKSR--QIRQFHFHGWP-EVGIPSDGKGMINIIAAVQKQ 157

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1838351042 1319 HRQSRDGHILITCWDGASRSGIFCAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQYGLCYEL 1386
Cdd:cd14623    158 QQQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKV 225
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 893-1094 2.04e-35

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: 134.27  E-value: 2.04e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  893 YINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQNKT-KCEQYWPEQ-EQIYGDFTVTLNNTR 970
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPEPgLQQYGPMEVEFVSGS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  971 TTTGLITRIFSLHKagcgFPR------VVEQFHYLLW-PDHGVPRNSAQLLCLVDVVNKRALEAPAGPVVVHCSAGIGRT 1043
Cdd:cd14637     81 ADEDIVTRLFRVQN----ITRlqeghlMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQRESGEGRTVVHCLNGGGRS 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1838351042 1044 GTFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYEVVLE 1094
Cdd:cd14637    157 GTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 893-1094 2.73e-35

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: 134.04  E-value: 2.73e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  893 YINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLveQNKTKCEQYWPEQE-QIYGDFTVTLNNTRT 971
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDV--DPAQLCPQYWPENGvHRHGPIQVEFVSADL 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  972 TTGLITRIFSLHKAGC---GFpRVVEQFHYLLWPDH-GVPRNSAQLLCLVDVVNK--RALEAPAGPVVVHCSAGIGRTGT 1045
Cdd:cd14635     79 EEDIISRIFRIYNAARpqdGY-RMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKwqEEYNGGEGRTVVHCLNGGGRSGT 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1838351042 1046 FIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYEVVLE 1094
Cdd:cd14635    158 FCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 893-1090 3.58e-35

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: 133.22  E-value: 3.58e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  893 YINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLveQNKTKCEQYWPEQEQI--YGDFTVTLNNTR 970
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDN--ELNEDEPIYWPTKEKPleCETFKVTLSGED 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  971 T-----TTGLITRIFSLHKAGCGFPRVVEQFHYLLWPDHGVPRNSAqlLCLVDVVNKRALEApAGPVVVHCSAGIGRTGT 1045
Cdd:cd14550     79 HsclsnEIRLIVRDFILESTQDDYVLEVRQFQCPSWPNPCSPIHTV--FELINTVQEWAQQR-DGPIVVHDRYGGVQAAT 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1838351042 1046 FIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYE 1090
Cdd:cd14550    156 FCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 995-1094 3.16e-34

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: 127.09  E-value: 3.16e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042   995 QFHYLLWPDHGVPRNSAQLLCLVDVVNK-RALEAPAGPVVVHCSAGIGRTGTFIALDFLL-KMGKAEGKVDVFHCVQRLR 1072
Cdd:smart00012    4 HYHYTGWPDHGVPESPDSILELLRAVKKnLNQSESSGPVVVHCSAGVGRTGTFVAIDILLqQLEAEAGEVDIFDTVKELR 83

                            90       100
                    ....*....|....*....|..
gi 1838351042  1073 EQRISMVQTKEQYTFLYEVVLE 1094
Cdd:smart00012   84 SQRPGMVQTEEQYLFLYRALLE 105
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
995-1094 3.16e-34

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 127.09  E-value: 3.16e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042   995 QFHYLLWPDHGVPRNSAQLLCLVDVVNK-RALEAPAGPVVVHCSAGIGRTGTFIALDFLL-KMGKAEGKVDVFHCVQRLR 1072
Cdd:smart00404    4 HYHYTGWPDHGVPESPDSILELLRAVKKnLNQSESSGPVVVHCSAGVGRTGTFVAIDILLqQLEAEAGEVDIFDTVKELR 83

                            90       100
                    ....*....|....*....|..
gi 1838351042  1073 EQRISMVQTKEQYTFLYEVVLE 1094
Cdd:smart00404   84 SQRPGMVQTEEQYLFLYRALLE 105
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 1185-1385 3.58e-34

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: 130.59  E-value: 3.58e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1185 YINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQELDETY-AEFWPmQGEAAYGRFHVQFISEEP 1263
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQcAQYWG-DEKKTYGDIEVELKDTEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1264 GAGFTAWTLALTNKQqpKKPPLEVRFWQLKDWPMKQhLPPHPATIISLLGNV-----ETHHRQSRDGHILITCWDGASRS 1338
Cdd:cd14558     80 SPTYTVRVFEITHLK--RKDSRTVYQYQYHKWKGEE-LPEKPKDLVDMIKSIkqklpYKNSKHGRSVPIVVHCSDGSSRT 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1838351042 1339 GIFCAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQYGLCYE 1385
Cdd:cd14558    157 GIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 1152-1393 4.86e-32

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: 125.59  E-value: 4.86e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1152 PTNQPKNRKPGILPADSCRPILMsslNADGSPG--YINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVL 1229
Cdd:cd14553      1 EVNKPKNRYANVIAYDHSRVILQ---PIEGVPGsdYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMM 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1230 NQLQELDETYAE-FWPMQGEAAYGRFHVQFISEEPGAGFTAWTLALTNKQQPKKppLEVRFWQLKDWPmKQHLPPHPATI 1308
Cdd:cd14553     78 TKLEERSRVKCDqYWPTRGTETYGLIQVTLLDTVELATYTVRTFALHKNGSSEK--REVRQFQFTAWP-DHGVPEHPTPF 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1309 ISLLGNVETHHrqSRD-GHILITCWDGASRSGIFCAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQYGLCYELA 1387
Cdd:cd14553    155 LAFLRRVKACN--PPDaGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDAL 232


                   ....*.
gi 1838351042 1388 LSYLNS 1393
Cdd:cd14553    233 LEAVTC 238
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 1158-1380 1.94e-31

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: 123.28  E-value: 1.94e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1158 NRKPGILPADSCRpILMSSLNADGSPGYINAVFVNTYT-EEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQELD 1236
Cdd:cd14547      1 NRYKTILPNEHSR-VCLPSVDDDPLSSYINANYIRGYDgEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEAK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1237 ETYAEFWPMQGEAAYGRFHVQFISEEPGAGFTAWTLALTNKQQPKKppleVRFWQLKDWPmKQHLPPHPATIISLLGNVE 1316
Cdd:cd14547     80 EKCAQYWPEEENETYGDFEVTVQSVKETDGYTVRKLTLKYGGEKRY----LKHYWYTSWP-DHKTPEAAQPLLSLVQEVE 154

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1838351042 1317 THHRQSRD-GHILITCWDGASRSGIFCAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQY 1380
Cdd:cd14547    155 EARQTEPHrGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQY 219
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 1154-1388 2.69e-30

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: 121.68  E-value: 2.69e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1154 NQPKNRKPGILPADSCRPILMSslnADGSPG--YINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQ 1231
Cdd:cd14626     41 NKPKNRYANVIAYDHSRVILTS---VDGVPGsdYINANYIDGYRKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTR 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1232 LQELDETYA-EFWPMQGEAAYGRFHVQFISEEPGAGFTAWTLALTNKQQPKKPplEVRFWQLKDWPmKQHLPPHPATIIS 1310
Cdd:cd14626    118 LEEKSRVKCdQYWPIRGTETYGMIQVTLLDTVELATYSVRTFALYKNGSSEKR--EVRQFQFMAWP-DHGVPEYPTPILA 194

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1838351042 1311 LLGNVETHHRQSRdGHILITCWDGASRSGIFCAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQYGLCYELAL 1388
Cdd:cd14626    195 FLRRVKACNPPDA-GPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALL 271
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 1151-1384 5.71e-30

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: 120.55  E-value: 5.71e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1151 KPTNQPKNRKPGILPADSCRpILMSSLNADGSPGYINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLN 1230
Cdd:cd14543     26 APANQEKNRYGDVLCLDQSR-VKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYSDFWRMVWEQKVLVIVMTT 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1231 QLQELDETY-AEFWPMQGEAA--YGRFHVQFISEEPGAGFTAWTLALTNKQQpkkppLEVR---FWQLKDWPmKQHLPPH 1304
Cdd:cd14543    105 RVVERGRVKcGQYWPLEEGSSlrYGDLTVTNLSVENKEHYKKTTLEIHNTET-----DESRqvtHFQFTSWP-DFGVPSS 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1305 PATIISLLGNVETHHRQS-------RDGH-----ILITCWDGASRSGIFCAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQ 1372
Cdd:cd14543    179 AAALLDFLGEVRQQQALAvkamgdrWKGHppgppIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNVMQTVRRMRTQRAF 258

                          250
                   ....*....|..
gi 1838351042 1373 LIKDVEQYGLCY 1384
Cdd:cd14543    259 SIQTPDQYYFCY 270
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 1148-1388 2.74e-29

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: 118.01  E-value: 2.74e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1148 EAEKPTNQPKNRKPGILPADSCRPILMSSLNADGSPGYINAVFVNTYT-EEDRLIITQMPFPNTVVDFWALVWDYTCTAV 1226
Cdd:cd14612      9 ELDIPGHASKDRYKTILPNPQSRVCLRRAGSQEEEGSYINANYIRGYDgKEKAYIATQGPMLNTVSDFWEMVWQEECPII 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1227 VVLNQLQELDETYAEFWPmQGEAAYGRFHVQFISEEPGAGFTAWTLALTNKQQPKkpplEVRFWQLKDWPMKQhLPPHPA 1306
Cdd:cd14612     89 VMITKLKEKKEKCVHYWP-EKEGTYGRFEIRVQDMKECDGYTIRDLTIQLEEESR----SVKHYWFSSWPDHQ-TPESAG 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1307 TIISLLGNVEtHHRQS--RDGHILITCWDGASRSGIFCAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQYGLCY 1384
Cdd:cd14612    163 PLLRLVAEVE-ESRQTaaSPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLH 241


                   ....*
gi 1838351042 1385 E-LAL 1388
Cdd:cd14612    242 HtLAL 246
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 1185-1385 1.12e-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: 114.73  E-value: 1.12e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1185 YINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQElDETYAEFWPMQGEA-AYGRFHVQFISEEp 1263
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNEL-NEDEPIYWPTKEKPlECETFKVTLSGED- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1264 gagftawTLALTNKQQPKKPP-----------LEVRFWQLKDWPmkqHLPPHPATIISLLGNVETHHrQSRDGHILITCW 1332
Cdd:cd14550     79 -------HSCLSNEIRLIVRDfilestqddyvLEVRQFQCPSWP---NPCSPIHTVFELINTVQEWA-QQRDGPIVVHDR 147

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1838351042 1333 DGASRSGIFCAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQYGLCYE 1385
Cdd:cd14550    148 YGGVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 1185-1389 1.91e-28

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: 114.01  E-value: 1.91e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1185 YINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQELDETYAEFWPMQGEAAYGR-FHVQFISEEp 1263
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFVYWPSREESMNCEaFTVTLISKD- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1264 gagftawTLALTNKQQ-----------PKKPPLEVRFWQLKDWPMkqhlPPHPATIISLLGNVETHHRQSRDGHILITCW 1332
Cdd:cd17670     80 -------RLCLSNEEQiiihdfileatQDDYVLEVRHFQCPKWPN----PDAPISSTFELINVIKEEALTRDGPTIVHDE 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1838351042 1333 DGASRSGIFCAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQYGLCYELALS 1389
Cdd:cd17670    149 FGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAMLS 205
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 1103-1388 4.47e-28

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: 115.58  E-value: 4.47e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1103 VPVESITSHVRCLQEAEASRhnnvLEKEFKAL---QKFSelfqllpCREAEKPTNQPKNRKPGILPADSCRPILMSSLNA 1179
Cdd:cd14625      4 IPISELAEHTERLKANDNLK----LSQEYESIdpgQQFT-------WEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGI 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1180 DGSpGYINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQELDETYA-EFWPMQGEAAYGRFHVQF 1258
Cdd:cd14625     73 MGS-DYINANYIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCdQYWPSRGTETYGMIQVTL 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1259 ISEEPGAGFTAWTLALTNKQQPKKPplEVRFWQLKDWPmKQHLPPHPATIISLLGNVETHHRQSRdGHILITCWDGASRS 1338
Cdd:cd14625    152 LDTIELATFCVRTFSLHKNGSSEKR--EVRQFQFTAWP-DHGVPEYPTPFLAFLRRVKTCNPPDA-GPIVVHCSAGVGRT 227

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1339 GIFCAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQYGLCYELAL 1388
Cdd:cd14625    228 GCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALL 277
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 1157-1384 1.04e-26

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: 110.01  E-value: 1.04e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1157 KNRKPGILPADSCRPILMSSLNADGSPGYINAVFVNTYT-EEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQEL 1235
Cdd:cd14611      2 KNRYKTILPNPHSRVCLKPKNSNDSLSTYINANYIRGYGgKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1236 DETYAEFWPmQGEAAYGRFHVQFISEEPGAGFTAWTLALTNKQQPKKppleVRFWQLKDWPmkQHLPPHPAT-IISLLGN 1314
Cdd:cd14611     82 NEKCVLYWP-EKRGIYGKVEVLVNSVKECDNYTIRNLTLKQGSQSRS----VKHYWYTSWP--DHKTPDSAQpLLQLMLD 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1838351042 1315 VETHHRQSRD-GHILITCWDGASRSGIFCAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQYGLCY 1384
Cdd:cd14611    155 VEEDRLASPGrGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 1154-1380 1.32e-26

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: 111.36  E-value: 1.32e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1154 NQPKNRKPGILPADSCRpILMSSLnaDGSPG--YINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQ 1231
Cdd:cd14624     47 NKPKNRYANVIAYDHSR-VLLSAI--EGIPGsdYINANYIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTK 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1232 LQELDETYA-EFWPMQGEAAYGRFHVQFISEEPGAGFTAWTLALTNKQQPKKPplEVRFWQLKDWPmKQHLPPHPATIIS 1310
Cdd:cd14624    124 LEERSRVKCdQYWPSRGTETYGLIQVTLLDTVELATYCVRTFALYKNGSSEKR--EVRQFQFTAWP-DHGVPEHPTPFLA 200

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1311 LLGNVETHHRQSRdGHILITCWDGASRSGIFCAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQY 1380
Cdd:cd14624    201 FLRRVKTCNPPDA-GPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQY 269
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 1147-1380 1.90e-26

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: 109.95  E-value: 1.90e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1147 REAEKPTNQPKNRKPGILPADSCRPILMSSLNADGSPGYINAVFVNTYTEEDRLII-TQMPFPNTVVDFWALVWDYTCTA 1225
Cdd:cd14613     18 KEYDIPGLVRKNRYKTILPNPHSRVCLTSPDQDDPLSSYINANYIRGYGGEEKVYIaTQGPTVNTVGDFWRMVWQERSPI 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1226 VVVLNQLQELDETYAEFWPmQGEAAYGRFHVQFISEEPGAGFTAWTLALTNKQQPKKppleVRFWQLKDWPmKQHLPPHP 1305
Cdd:cd14613     98 IVMITNIEEMNEKCTEYWP-EEQVTYEGIEITVKQVIHADDYRLRLITLKSGGEERG----LKHYWYTSWP-DQKTPDNA 171

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1838351042 1306 ATIISLLGNVETHHRQSR--DGHILITCWDGASRSGIFCAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQY 1380
Cdd:cd14613    172 PPLLQLVQEVEEARQQAEpnCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQY 248
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 1158-1380 2.17e-26

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: 108.88  E-value: 2.17e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1158 NRKPGILPADSCRpILMSSLNADGSPGYINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQELDE 1237
Cdd:cd14618      1 NRYPHVLPYDHSR-VRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGR 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1238 TYAE-FWPMQGE-AAYGRFHVQFISEEPGAGFTAWTLALTNKQQPKKPplEVRFWQLKDWPmKQHLPPHPATIISLLGNV 1315
Cdd:cd14618     80 VLCDhYWPSESTpVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKER--RVKHLHYTAWP-DHGIPESTSSLMAFRELV 156

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1838351042 1316 ETHHRQSRD-GHILITCWDGASRSGIFCAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQY 1380
Cdd:cd14618    157 REHVQATKGkGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQY 222
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 1159-1380 9.90e-26

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: 107.05  E-value: 9.90e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1159 RKPGILPADSCRPILMSSLNADGSpGYINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQELDET 1238
Cdd:cd14548      1 RYTNILPYDHSRVKLIPINEEEGS-DYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1239 YAE-FWPM-QGEAAYGRFHVQFISEEPGAGFTAWTLALTNKQQPKKppleVRFWQLKDWPmkQH-LPPHPATIISLLGNV 1315
Cdd:cd14548     80 KCDhYWPFdQDPVYYGDITVTMLSESVLPDWTIREFKLERGDEVRS----VRQFHFTAWP--DHgVPEAPDSLLRFVRLV 153

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1838351042 1316 ethhRQSRD---GHILITCWDGASRSGIFCAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQY 1380
Cdd:cd14548    154 ----RDYIKqekGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQY 217
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 1185-1388 1.13e-25

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: 106.23  E-value: 1.13e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1185 YINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQELDETYAEFWPMQGEAAYGR-FHVQFISEEp 1263
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFVYWPNKDEPINCEtFKVTLIAEE- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1264 gagftawTLALTNKQQ-----------PKKPPLEVRFWQLKDWPMkqhlPPHPATIISLLGNVETHHRQSRDGHILITCW 1332
Cdd:cd17669     80 -------HKCLSNEEKliiqdfileatQDDYVLEVRHFQCPKWPN----PDSPISKTFELISIIKEEAANRDGPMIVHDE 148

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1838351042 1333 DGASRSGIFCAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQYGLCYELAL 1388
Cdd:cd17669    149 HGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 893-1093 1.58e-25

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: 105.92  E-value: 1.58e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  893 YINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVML---TGLVEQNKTkceqYWPEQEQIYG--DFTVTLN 967
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLpdnQGLAEDEFV----YWPSREESMNceAFTVTLI 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  968 NT-----RTTTGLITRIFSLHKAGCGFPRVVEQFHYLLWPDHGVPRNSAqlLCLVDVVNKRALEAPaGPVVVHCSAGIGR 1042
Cdd:cd17670     77 SKdrlclSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISST--FELINVIKEEALTRD-GPTIVHDEFGAVS 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1838351042 1043 TGTFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYEVVL 1093
Cdd:cd17670    154 AGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 1158-1380 2.26e-25

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: 106.05  E-value: 2.26e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1158 NRKPGILPADSCRpILMSSLNADGSpGYINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQELDE 1237
Cdd:cd14615      1 NRYNNVLPYDISR-VKLSVQSHSTD-DYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGR 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1238 TYA-EFWPMQGEAAYGRFHVQFISEEPgagFTAWTL---ALTNKQQPKKPPleVRFWQLKDWPmKQHLPPHPATIISLLG 1313
Cdd:cd14615     79 TKCeEYWPSKQKKDYGDITVTMTSEIV---LPEWTIrdfTVKNAQTNESRT--VRHFHFTSWP-DHGVPETTDLLINFRH 152

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1838351042 1314 NVETHHRQS-RDGHILITCWDGASRSGIFCAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQY 1380
Cdd:cd14615    153 LVREYMKQNpPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQY 220
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 1154-1384 2.73e-25

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: 106.39  E-value: 2.73e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1154 NQPKNRKPGILPADSCRPILMSSLNADGSPGYINAVFVNTYTEEDRL-------IITQMPFPNTVVDFWALVWDYTCTAV 1226
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILKDRDPNVPGSDYINANYIRNENEGPTTdenaktyIATQGCLENTVSDFWSMVWQENSRVI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1227 VVL-NQLQELDETYAEFWPMQGEA-AYGRFHVQFISEEPGAGFTAWTLALTNKQQPkKPPLEVRFWQLKDWPmkQH-LPP 1303
Cdd:cd14544     81 VMTtKEVERGKNKCVRYWPDEGMQkQYGPYRVQNVSEHDTTDYTLRELQVSKLDQG-DPIREIWHYQYLSWP--DHgVPS 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1304 HPATIISLLGNVetHHRQS---RDGHILITCWDGASRSGIFCAAGFLCEQIQSEGL---VDVSQAVRMLKRRRRQLIKDV 1377
Cdd:cd14544    158 DPGGVLNFLEDV--NQRQEslpHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQRSGMVQTE 235


                   ....*..
gi 1838351042 1378 EQYGLCY 1384
Cdd:cd14544    236 AQYKFIY 242
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 1137-1390 1.32e-24

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: 105.88  E-value: 1.32e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1137 FSELFQLLP-------CREAEKPTNQPKNRKPGILPADSCRpILMSSLNADGSPGYINAVFVNTYTEEDRLIITQMPFPN 1209
Cdd:cd14621     28 FREEFNALPacpiqatCEAASKEENKEKNRYVNILPYDHSR-VHLTPVEGVPDSDYINASFINGYQEKNKFIAAQGPKEE 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1210 TVVDFWALVWDYTCTAVVVLNQLQELDETY-AEFWPMQGEAAYGRFHVqfiSEEPGAGFTAWTLALTNKQQ-----PKKP 1283
Cdd:cd14621    107 TVNDFWRMIWEQNTATIVMVTNLKERKECKcAQYWPDQGCWTYGNIRV---SVEDVTVLVDYTVRKFCIQQvgdvtNKKP 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1284 PLEVRFWQLKDWPmKQHLPPHPATIISLLGNVETHHRQSRdGHILITCWDGASRSGIFCAAGFLCEQIQSEGLVDVSQAV 1363
Cdd:cd14621    184 QRLITQFHFTSWP-DFGVPFTPIGMLKFLKKVKNCNPQYA-GAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKVDVYGFV 261

                          250       260
                   ....*....|....*....|....*..
gi 1838351042 1364 RMLKRRRRQLIKDVEQYGLCYELALSY 1390
Cdd:cd14621    262 SRIRAQRCQMVQTDMQYVFIYQALLEH 288
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 1185-1380 2.26e-24

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: 102.44  E-value: 2.26e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1185 YINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQELDETY-AEFWPMQGEaAYGRFHVQFISEEP 1263
Cdd:cd14632      1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKcSKYWPDDSD-TYGDIKITLLKTET 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1264 GAGFTAWTLALTNKQQPKKPplEVRFWQLKDWPmKQHLPPHPATIISLLGNVETHHRQSRdGHILITCWDGASRSGIFCA 1343
Cdd:cd14632     80 LAEYSVRTFALERRGYSARH--EVKQFHFTSWP-EHGVPYHATGLLAFIRRVKASTPPDA-GPVVVHCSAGAGRTGCYIV 155

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1838351042 1344 AGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQY 1380
Cdd:cd14632    156 LDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQY 192
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 1144-1395 2.29e-24

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: 104.72  E-value: 2.29e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1144 LPCREAEKPTNQPKNRKPGILPADSCRPILMSSLNadgspGYINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTC 1223
Cdd:cd14608     15 FPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDN-----DYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKS 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1224 TAVVVLNQLQELDETY-AEFWPMQGEAAY----GRFHVQFISEEPGAGFTAWTLALTN--KQQPKkpplEVRFWQLKDWP 1296
Cdd:cd14608     90 RGVVMLNRVMEKGSLKcAQYWPQKEEKEMifedTNLKLTLISEDIKSYYTVRQLELENltTQETR----EILHFHYTTWP 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1297 mKQHLPPHPATIISLLGNV-ETHHRQSRDGHILITCWDGASRSGIFCAAG---FLCEQIQSEGLVDVSQAVRMLKRRRRQ 1372
Cdd:cd14608    166 -DFGVPESPASFLNFLFKVrESGSLSPEHGPVVVHCSAGIGRSGTFCLADtclLLMDKRKDPSSVDIKKVLLEMRKFRMG 244

                          250       260
                   ....*....|....*....|...
gi 1838351042 1373 LIKDVEQyglcyeLALSYLNSFE 1395
Cdd:cd14608    245 LIQTADQ------LRFSYLAVIE 261
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 1144-1380 3.83e-24

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: 103.04  E-value: 3.83e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1144 LPCREAEKPTNQPKNRKPGILPADSCRPILMSsLNADGSPGYINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTC 1223
Cdd:cd14614      2 IPHFAADLPVNRCKNRYTNILPYDFSRVKLVS-MHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1224 TAVVVLNQLQELDETYAE-FWPMQGE-AAYGRFHVQFISEE--PGAGFTAWTLALTNKQQpkkpplEVRFWQLKDWPmkQ 1299
Cdd:cd14614     81 QIIVMLTQCNEKRRVKCDhYWPFTEEpVAYGDITVEMLSEEeqPDWAIREFRVSYADEVQ------DVMHFNYTAWP--D 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1300 HLPPHPATIISLLGNVETHHRQS--RDGHILITCWDGASRSGIFCAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDV 1377
Cdd:cd14614    153 HGVPTANAAESILQFVQMVRQQAvkSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTE 232


                   ...
gi 1838351042 1378 EQY 1380
Cdd:cd14614    233 EQY 235
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 1122-1389 6.15e-24

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: 103.60  E-value: 6.15e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1122 RHNNVLEKEFKALQKFselfQLLP--CREAEKPTNQPKNRKPGILPADSCRpILMSSLNADGSPGYINAVFVNTYTEED- 1198
Cdd:cd14610     14 KNKNRLEKEWEALCAY----QAEPnaTNVAQREENVQKNRSLAVLPYDHSR-IILKAENSHSHSDYINASPIMDHDPRNp 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1199 RLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQE--LDETYaEFWPMQGEAAYGRFHVQFISEEPGA-GFTAWTLALT 1275
Cdd:cd14610     89 AYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAEngVKQCY-HYWPDEGSNLYHIYEVNLVSEHIWCeDFLVRSFYLK 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1276 NKQQPKKPplEVRFWQLKDWpMKQHLPPHPATIISLLGNVETHHRqSRDGHILITCWDGASRSGIFCAAGFLCEQI-QSE 1354
Cdd:cd14610    168 NLQTNETR--TVTQFHFLSW-NDQGVPASTRSLLDFRRKVNKCYR-GRSCPIIVHCSDGAGRSGTYILIDMVLNKMaKGA 243

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1838351042 1355 GLVDVSQAVRMLKRRRRQLIKDVEQyglcYELALS 1389
Cdd:cd14610    244 KEIDIAATLEHLRDQRPGMVQTKEQ----FEFALT 274
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 1151-1390 7.93e-24

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 104.34  E-value: 7.93e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1151 KPTNQPKNRKPGILPADSCRPILMS--SLNA----------------DGSPGYINAVFVNTYTEEDRLIITQMPFPNTVV 1212
Cdd:PHA02746    48 KKENLKKNRFHDIPCWDHSRVVINAheSLKMfdvgdsdgkkievtseDNAENYIHANFVDGFKEANKFICAQGPKEDTSE 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1213 DFWALVWDYTCTAVVVLNQLQELDETYAEFW--PMQGEAAYGRFHVQFISEEPGAGFTAWTLALTNKQQPKKPPLEvRFW 1290
Cdd:PHA02746   128 DFFKLISEHESQVIVSLTDIDDDDEKCFELWtkEEDSELAFGRFVAKILDIIEELSFTKTRLMITDKISDTSREIH-HFW 206

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1291 qLKDWPmKQHLPPHPATIISLLGNVETHHRQ---------SRDGHILITCWDGASRSGIFCAAGFLCEQIQSEGLVDVSQ 1361
Cdd:PHA02746   207 -FPDWP-DNGIPTGMAEFLELINKVNEEQAElikqadndpQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGE 284

                          250       260
                   ....*....|....*....|....*....
gi 1838351042 1362 AVRMLKRRRRQLIKDVEQYGLCYeLALSY 1390
Cdd:PHA02746   285 IVLKIRKQRHSSVFLPEQYAFCY-KALKY 312
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 1185-1380 1.17e-23

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: 100.38  E-value: 1.17e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1185 YINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQELDETY-AEFWPMQGEaAYGRFHVQFISEEP 1263
Cdd:cd14555      1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKcSRYWPDDTE-VYGDIKVTLVETEP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1264 GAGFTAWTLALTNKQQPKKPplEVRFWQLKDWPmKQHLPPHPATIISLLGNVETHHRQSRdGHILITCWDGASRSGIFCA 1343
Cdd:cd14555     80 LAEYVVRTFALERRGYHEIR--EVRQFHFTGWP-DHGVPYHATGLLGFIRRVKASNPPSA-GPIVVHCSAGAGRTGCYIV 155

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1838351042 1344 AGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQY 1380
Cdd:cd14555    156 IDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQY 192
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 1154-1388 1.20e-23

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: 101.26  E-value: 1.20e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1154 NQPKNRKPGILPADSCRpILMSSLNADGSPGYINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQ 1233
Cdd:cd14630      3 NRNKNRYGNIISYDHSR-VRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1234 ELDETY-AEFWPMQGEAaYGRFHVQFISEEPGAGFTAWTLALTNKQQPKKPplEVRFWQLKDWPmkQHLPPHPATiiSLL 1312
Cdd:cd14630     82 EVGRVKcVRYWPDDTEV-YGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIR--EIRQFHFTSWP--DHGVPCYAT--GLL 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1313 GNVethhRQSR------DGHILITCWDGASRSGIFCAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQYGLCYEL 1386
Cdd:cd14630    155 GFV----RQVKflnppdAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDA 230


                   ..
gi 1838351042 1387 AL 1388
Cdd:cd14630    231 IL 232
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 1161-1388 1.60e-23

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: 100.79  E-value: 1.60e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1161 PGILPADSCRPILMsslNADGSPG--YINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQELDET 1238
Cdd:cd14620      2 PNILPYDHSRVILS---QLDGIPCsdYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1239 YA-EFWPMQGEAAYGRFHVQFISEEPGAGFTAWTLALTNK-QQPKKPPLEVRFWQLKDWPmKQHLPPHPATIISLLGNVE 1316
Cdd:cd14620     79 KCyQYWPDQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQPQlPDGCKAPRLVTQLHFTSWP-DFGVPFTPIGMLKFLKKVK 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1838351042 1317 THHrQSRDGHILITCWDGASRSGIFCAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQYGLCYELAL 1388
Cdd:cd14620    158 SVN-PVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALL 228
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 893-1093 1.82e-23

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: 99.68  E-value: 1.82e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  893 YINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLveQNKTKCE-QYWPEQEQ--IYGDFTVTLNNT 969
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDG--QNMAEDEfVYWPNKDEpiNCETFKVTLIAE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  970 -----RTTTGLITRIFSLHKAGCGFPRVVEQFHYLLWPDHGVPrnSAQLLCLVDVVNKRALEAPaGPVVVHCSAGIGRTG 1044
Cdd:cd17669     79 ehkclSNEEKLIIQDFILEATQDDYVLEVRHFQCPKWPNPDSP--ISKTFELISIIKEEAANRD-GPMIVHDEHGGVTAG 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1838351042 1045 TFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKEQYTFLYEVVL 1093
Cdd:cd17669    156 TFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 1105-1384 2.95e-23

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: 101.93  E-value: 2.95e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1105 VESITSHVRCLQEAEASRHN--NVLEKEFKALQKFSELF---QLLPCREAEKPTNQPKNRKPGILPADSCRPIL---MSS 1176
Cdd:cd14604      3 VEILKKFIERVQAMKSTDHNgeDNFASDFMRLRRLSTKYrteKIYPTATGEKEENVKKNRYKDILPFDHSRVKLtlkTSS 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1177 LNADgspgYINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQELDETYAE-FWPMQGEAA--YGR 1253
Cdd:cd14604     83 QDSD----YINANFIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCErYWPLYGEEPmtFGP 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1254 FHVQFISEEPGAGFTAWTLALTNKQQPKkpplevRFWQLK--DWPmKQHLPPHPATIISLLGnVETHHRQSRDGHILITC 1331
Cdd:cd14604    159 FRISCEAEQARTDYFIRTLLLEFQNETR------RLYQFHyvNWP-DHDVPSSFDSILDMIS-LMRKYQEHEDVPICIHC 230

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1838351042 1332 WDGASRSGIFCA---------AGFLCEQIqseglvDVSQAVRMLKRRRRQLIKDVEQYGLCY 1384
Cdd:cd14604    231 SAGCGRTGAICAidytwnllkAGKIPEEF------NVFNLIQEMRTQRHSAVQTKEQYELVH 286
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 1185-1380 4.91e-23

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: 98.58  E-value: 4.91e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1185 YINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQELDETY-AEFWPMQGEAAYGRFHVQFISEEP 1263
Cdd:cd14549      1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKcDQYWPKEGTETYGNIQVTLLSTEV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1264 GAGFTAWTLALTN--KQQPKKPPLEVRFWQL--KDWPmkQH-LPPHPATIISLLGNVETHHRQSRdGHILITCWDGASRS 1338
Cdd:cd14549     81 LATYTVRTFSLKNlkLKKVKGRSSERVVYQYhyTQWP--DHgVPDYTLPVLSFVRKSSAANPPGA-GPIVVHCSAGVGRT 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1838351042 1339 GIFCAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQY 1380
Cdd:cd14549    158 GTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQY 199
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 1172-1380 5.47e-23

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: 98.94  E-value: 5.47e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1172 ILMSSLNADGSPGYINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQELDETYA-EFWPMQGEaA 1250
Cdd:cd14631      2 VILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCyKYWPDDTE-V 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1251 YGRFHVQFISEEPGAGFTAWTLALtnKQQPKKPPLEVRFWQLKDWPmKQHLPPHPATIISLLGNVETHHRQSRdGHILIT 1330
Cdd:cd14631     81 YGDFKVTCVEMEPLAEYVVRTFTL--ERRGYNEIREVKQFHFTGWP-DHGVPYHATGLLSFIRRVKLSNPPSA-GPIVVH 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1331 CWDGASRSGIFCAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQY 1380
Cdd:cd14631    157 CSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQY 206
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 1185-1385 5.64e-23

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: 98.45  E-value: 5.64e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1185 YINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQELDETY-AEFWPMQGEAAYGRFHVQFISEEP 1263
Cdd:cd14551      1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKcSQYWPDQGCWTYGNLRVRVEDTVV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1264 GAGFTAWTLAL--TNKQQPKKPPLEVRFWQLKDWPmKQHLPPHPATIISLLGNVETHHRQsRDGHILITCWDGASRSGIF 1341
Cdd:cd14551     81 LVDYTTRKFCIqkVNRGIGEKRVRLVTQFHFTSWP-DFGVPFTPIGMLKFLKKVKSANPP-RAGPIVVHCSAGVGRTGTF 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1838351042 1342 CAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQYGLCYE 1385
Cdd:cd14551    159 IVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 1158-1391 1.22e-22

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: 98.42  E-value: 1.22e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1158 NRKPGILPADSCRpILMSSLNADGSPGYINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQELDE 1237
Cdd:cd14619      1 NRFRNVLPYDWSR-VPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGR 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1238 TYAE-FWPMQGE-AAYGRFHVQFISEEPGAGFTAWTLALTNKQQPKKppLEVRFWQLKDWPmKQHLPPHPATIISLLGNV 1315
Cdd:cd14619     80 VKCEhYWPLDYTpCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKT--LSVRHFHFTAWP-DHGVPSSTDTLLAFRRLL 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1838351042 1316 ETHHRQSRD-GHILITCWDGASRSGIFCAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQYGLCYELALSYL 1391
Cdd:cd14619    157 RQWLDQTMSgGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 1142-1388 2.27e-22

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: 98.58  E-value: 2.27e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1142 QLLPCREAEKPTNQPKNRKPGILPADSCRpILMSSLNADGSPGYINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDY 1221
Cdd:cd14633     28 QSAPWDSAKKDENRMKNRYGNIIAYDHSR-VRLQPIEGETSSDYINGNYIDGYHRPNHYIATQGPMQETIYDFWRMVWHE 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1222 TCTAVVVLNQLQELDETY-AEFWPMQGEaAYGRFHVQFISEEPGAGFTAWTLALtnKQQPKKPPLEVRFWQLKDWPmkQH 1300
Cdd:cd14633    107 NTASIIMVTNLVEVGRVKcCKYWPDDTE-IYKDIKVTLIETELLAEYVIRTFAV--EKRGVHEIREIRQFHFTGWP--DH 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1301 LPPHPATiiSLLGNVETHHRQS--RDGHILITCWDGASRSGIFCAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVE 1378
Cdd:cd14633    182 GVPYHAT--GLLGFVRQVKSKSppNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRSRRVNMVQTEE 259

                          250
                   ....*....|
gi 1838351042 1379 QYGLCYELAL 1388
Cdd:cd14633    260 QYVFIHDAIL 269
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 1185-1382 2.90e-22

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: 96.05  E-value: 2.90e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1185 YINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQELDETY-AEFWPM--QGEAAYGRFHVQFISE 1261
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKcAQYWPSmeEGSRAFGDVVVKINEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1262 EPGAGFTAWTLALTNKQQpKKPPLEVRFWQLKDWPmKQHLPPHPATIISLLGNVEThHRQSRDGHILITCWDGASRSGIF 1341
Cdd:cd14557     81 KICPDYIIRKLNINNKKE-KGSGREVTHIQFTSWP-DHGVPEDPHLLLKLRRRVNA-FNNFFSGPIVVHCSAGVGRTGTY 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1838351042 1342 CAAGFLCEQIQSEGLVDVSQAVRMLkRRRRQLIKDVE-QYGL 1382
Cdd:cd14557    158 IGIDAMLEGLEAEGRVDVYGYVVKL-RRQRCLMVQVEaQYIL 198
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 1157-1384 5.73e-22

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: 96.31  E-value: 5.73e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1157 KNRKPGILPADSCRPILMSSlnaDGSPGYINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQELD 1236
Cdd:cd14545      1 LNRYRDRDPYDHDRSRVKLK---QGDNDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1237 ETY-AEFWPMQGEAAYGR----FHVQFISEEPGAGFTAWTLALTNKQQPkkPPLEVRFWQLKDWPmKQHLPPHPATIISL 1311
Cdd:cd14545     78 QIKcAQYWPQGEGNAMIFedtgLKVTLLSEEDKSYYTVRTLELENLKTQ--ETREVLHFHYTTWP-DFGVPESPAAFLNF 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1838351042 1312 LGNVETHHRQSRD-GHILITCWDGASRSGIFCAAGFLCEQIQSEGL--VDVSQAVRMLKRRRRQLIKDVEQYGLCY 1384
Cdd:cd14545    155 LQKVRESGSLSSDvGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRFSY 230
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 1185-1385 8.35e-22

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: 95.14  E-value: 8.35e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1185 YINAVFVNTYTE-EDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQELDE-TYAEFWPMQ-GEA-AYGRFHVQFIS 1260
Cdd:cd14539      1 YINASLIEDLTPyCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKqKVHRYWPTErGQAlVYGAITVSLQS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1261 EEPGAGFTAWTLALTNKQQPKKPplEVRFWQLKDWPmkQH-LPPHPATIISLLGNVETHHRQSRDGH--ILITCWDGASR 1337
Cdd:cd14539     81 VRTTPTHVERIISIQHKDTRLSR--SVVHLQFTTWP--ELgLPDSPNPLLRFIEEVHSHYLQQRSLQtpIVVHCSSGVGR 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1838351042 1338 SGIFC---AAgfLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQYGLCYE 1385
Cdd:cd14539    157 TGAFCllyAA--VQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 1122-1389 2.10e-21

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: 95.87  E-value: 2.10e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1122 RHNNVLEKEFKALQKFselfQLLP--CREAEKPTNQPKNRKPGILPADSCRPILMSSLNADGSPgYINAvfvNTYTEED- 1198
Cdd:cd14609     12 RNRDRLAKEWQALCAY----QAEPntCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNPSRSD-YINA---SPIIEHDp 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1199 RL---IITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQELDETYAE-FWPMQGEAAYGRFHVQFISEEPGA-GFTAWTLA 1273
Cdd:cd14609     84 RMpayIATQGPLSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDrYWPDEGSSLYHIYEVNLVSEHIWCeDFLVRSFY 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1274 LTNKQQPKKPPLEVrfWQLKDWPmKQHLPPHPATIISLLGNVETHHRqSRDGHILITCWDGASRSGIFCAAGFLCEQIqS 1353
Cdd:cd14609    164 LKNVQTQETRTLTQ--FHFLSWP-AEGIPSSTRPLLDFRRKVNKCYR-GRSCPIIVHCSDGAGRTGTYILIDMVLNRM-A 238

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1838351042 1354 EGL--VDVSQAVRMLKRRRRQLIKDVEQyglcYELALS 1389
Cdd:cd14609    239 KGVkeIDIAATLEHVRDQRPGMVRTKDQ----FEFALT 272
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 1129-1384 4.15e-21

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: 94.89  E-value: 4.15e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1129 KEFKALQKFSELFQ---LLPCREAEKPTNQPKNRKPGILPADSCRPILmSSLNADGSPGYINAVFVNTYTEEDRLIITQM 1205
Cdd:cd14603      2 GEFSEIRACSAAFKadyVCSTVAGGRKENVKKNRYKDILPYDQTRVIL-SLLQEEGHSDYINANFIKGVDGSRAYIATQG 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1206 PFPNTVVDFWALVWDYTCTAVVVLNQLQELDETYAE-FWPMQGE-AAYGRFHVQFISEE-PGAGFTAWTLALTNKQQPKK 1282
Cdd:cd14603     81 PLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCErYWAQEQEpLQTGPFTITLVKEKrLNEEVILRTLKVTFQKESRS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1283 ppleVRFWQLKDWPmKQHLPPHPATIISLLGNVETHHRQSRDGhILITCWDGASRSGIFCAAGF-----LCEQIQSEglV 1357
Cdd:cd14603    161 ----VSHFQYMAWP-DHGIPDSPDCMLAMIELARRLQGSGPEP-LCVHCSAGCGRTGVICTVDYvrqllLTQRIPPD--F 232

                          250       260
                   ....*....|....*....|....*..
gi 1838351042 1358 DVSQAVRMLKRRRRQLIKDVEQYGLCY 1384
Cdd:cd14603    233 SIFDVVLEMRKQRPAAVQTEEQYEFLY 259
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 1148-1393 7.05e-21

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: 94.18  E-value: 7.05e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1148 EAEKPTNQPKNRKPGILPADSCRPILMSSLNADGSPGYINAVFVNTYTEED-----RLIITQMPFPNTVVDFWALVWDYT 1222
Cdd:cd14606     12 EGQRPENKSKNRYKNILPFDHSRVILQGRDSNIPGSDYINANYVKNQLLGPdenakTYIASQGCLEATVNDFWQMAWQEN 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1223 CTAVVVLNQLQELDETY-AEFWP-MQGEAAYGRFHVQFISEEPGAGFTAWTLALTNKQQPKKPPlEVRFWQLKDWPmKQH 1300
Cdd:cd14606     92 SRVIVMTTREVEKGRNKcVPYWPeVGMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGELIR-EIWHYQYLSWP-DHG 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1301 LPPHPATIISLLGNVETHHRQSRD-GHILITCWDGASRSGIFCAAGFLCEQIQSEGL---VDVSQAVRMLKRRRRQLIKD 1376
Cdd:cd14606    170 VPSEPGGVLSFLDQINQRQESLPHaGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRSGMVQT 249

                          250
                   ....*....|....*..
gi 1838351042 1377 VEQYGLCYELALSYLNS 1393
Cdd:cd14606    250 EAQYKFIYVAIAQFIET 266
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 1158-1385 1.60e-20

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: 91.90  E-value: 1.60e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1158 NRKPGILPADSCRpILMSSLNADGSPGYINAVFV--NTYTEEdrLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQEL 1235
Cdd:cd14617      1 NRYNNILPYDSTR-VKLSNVDDDPCSDYINASYIpgNNFRRE--YIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEK 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1236 DETYAE-FWPMQGEA-AYGRFHVQFISEEPGAGFTAWTLALTNKQQPKKPPLeVRFWQLKDWPmKQHLPPHPATIISLLG 1313
Cdd:cd14617     78 GRVKCDhYWPADQDSlYYGDLIVQMLSESVLPEWTIREFKICSEEQLDAPRL-VRHFHYTVWP-DHGVPETTQSLIQFVR 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1838351042 1314 NVETH-HRQSRDGHILITCWDGASRSGIFCAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQYGLCYE 1385
Cdd:cd14617    156 TVRDYiNRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 1158-1380 2.90e-20

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: 91.12  E-value: 2.90e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1158 NRKPGILPADSCRPILMSSLNADGSpGYINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQELDE 1237
Cdd:cd14616      1 NRFPNIKPYNNNRVKLIADAGVPGS-DYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGR 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1238 TYA-EFWPMQGE--AAYGRFHVQFISEEPGAGFTAWTLaltnKQQPKKPPLEVRFWQLKDWPmKQHLPPHPATIISLLGN 1314
Cdd:cd14616     80 IRChQYWPEDNKpvTVFGDIVITKLMEDVQIDWTIRDL----KIERHGDYMMVRQCNFTSWP-EHGVPESSAPLIHFVKL 154

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1838351042 1315 VEThHRQSRDGHILITCWDGASRSGIFCAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQY 1380
Cdd:cd14616    155 VRA-SRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQY 219
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 1185-1385 2.99e-20

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: 90.77  E-value: 2.99e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1185 YINAVFVN-TYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQELD-ETYAEFWPM-QGEAAYGRFHVQFISE 1261
Cdd:cd18533      1 YINASYITlPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGrEKCDQYWPSgEYEGEYGDLTVELVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1262 E--PGAGFTAWTLALTNKQQPKKpplEVRFWQLKDWP-MKqhlppHPATIISLLGNVETHHRQSRDGH----ILITCWDG 1334
Cdd:cd18533     81 EenDDGGFIVREFELSKEDGKVK---KVYHIQYKSWPdFG-----VPDSPEDLLTLIKLKRELNDSASldppIIVHCSAG 152

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1335 ASRSGIFCAAGFLCEQIQSEGLVD---------VSQAVRMLKRRRRQLIKDVEQYGLCYE 1385
Cdd:cd18533    153 VGRTGTFIALDSLLDELKRGLSDSqdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 1144-1384 3.16e-20

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: 91.95  E-value: 3.16e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1144 LPCREAEKPTNQPKNRKPGILPADSCRPILMSSLNadgspGYINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTC 1223
Cdd:cd14607     14 YPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTEN-----DYINASLVVIEEAQRSYILTQGPLPNTCCHFWLMVWQQKT 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1224 TAVVVLNQLQELD-ETYAEFWPMQGEAAYG----RFHVQFISEEPGAGFTAWTLALTNKQQPKKPplEVRFWQLKDWPmK 1298
Cdd:cd14607     89 KAVVMLNRIVEKDsVKCAQYWPTDEEEVLSfketGFSVKLLSEDVKSYYTVHLLQLENINSGETR--TISHFHYTTWP-D 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1299 QHLPPHPATIISLLGNV-ETHHRQSRDGHILITCWDGASRSGIFCAAG--FLCEQIQSEGLVDVSQAVRMLKRRRRQLIK 1375
Cdd:cd14607    166 FGVPESPASFLNFLFKVrESGSLSPEHGPAVVHCSAGIGRSGTFSLVDtcLVLMEKKDPDSVDIKQVLLDMRKYRMGLIQ 245


                   ....*....
gi 1838351042 1376 DVEQYGLCY 1384
Cdd:cd14607    246 TPDQLRFSY 254
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1150-1391 7.13e-20

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 92.37  E-value: 7.13e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1150 EKPTNQPKNRKPGILPADSCRPILMSSlnADGSPGYINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVL 1229
Cdd:PHA02747    47 EKPENQPKNRYWDIPCWDHNRVILDSG--GGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVML 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1230 NQLQEL--DETYAEFWPMQ--GEAAYGRFHVQFISEEPGAGFTAWTLALTNKQQpkKPPLEVRFWQLKDWPMKQHLPPHP 1305
Cdd:PHA02747   125 TPTKGTngEEKCYQYWCLNedGNIDMEDFRIETLKTSVRAKYILTLIEITDKIL--KDSRKISHFQCSEWFEDETPSDHP 202

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1306 -----ATIISLLGNVETHHRQSRDG---HILITCWDGASRSGIFCAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDV 1377
Cdd:PHA02747   203 dfikfIKIIDINRKKSGKLFNPKDAllcPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNF 282

                          250
                   ....*....|....*..
gi 1838351042 1378 EQYGL---CYELALSYL 1391
Cdd:PHA02747   283 DDYLFiqpGYEVLHYFL 299
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 1154-1393 9.00e-20

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: 90.46  E-value: 9.00e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1154 NQPKNRKPGILPADSCRPILmsslnADGSPG-----YINAVFVNTYTE--------EDRLIITQMPFPNTVVDFWALVWD 1220
Cdd:cd14605      2 NKNKNRYKNILPFDHTRVVL-----HDGDPNepvsdYINANIIMPEFEtkcnnskpKKSYIATQGCLQNTVNDFWRMVFQ 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1221 YTCTAVVVLNQLQELDETY-AEFWPMQGE-AAYGRFHVQFISEEPGAGFTAWTLALTNKQQPKkppLEVRFWQ--LKDWP 1296
Cdd:cd14605     77 ENSRVIVMTTKEVERGKSKcVKYWPDEYAlKEYGVMRVRNVKESAAHDYILRELKLSKVGQGN---TERTVWQyhFRTWP 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1297 mKQHLPPHPATIISLLGnvETHHRQ---SRDGHILITCWDGASRSGIFCAAGFLCEQIQSEGL---VDVSQAVRMLKRRR 1370
Cdd:cd14605    154 -DHGVPSDPGGVLDFLE--EVHHKQesiMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQR 230

                          250       260
                   ....*....|....*....|...
gi 1838351042 1371 RQLIKDVEQYGLCYELALSYLNS 1393
Cdd:cd14605    231 SGMVQTEAQYRFIYMAVQHYIET 253
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 1114-1390 2.52e-19

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 90.45  E-value: 2.52e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1114 CLQEAEASRHNNVLEKEFKALQKFSELFQllpCREAEKPTNQPKNRKPGILPADSCRPILMSSlnaDGSPGYINAVFVNT 1193
Cdd:PHA02742    15 CEQLIEESNLAEILKEEHEHIMQEIVAFS---CNESLELKNMKKCRYPDAPCFDRNRVILKIE---DGGDDFINASYVDG 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1194 YTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQELD-ETYAEFW--PMQGEAAYGRFHVQFISEEPGAGFTAW 1270
Cdd:PHA02742    89 HNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDGkEACYPYWmpHERGKATHGEFKIKTKKIKSFRNYAVT 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1271 TLALTNKQQPKKppLEVRFWQLKDWPmKQHLPPHPATIISLLgnVETHHRQS------------RDGHILITCWDGASRS 1338
Cdd:PHA02742   169 NLCLTDTNTGAS--LDIKHFAYEDWP-HGGLPRDPNKFLDFV--LAVREADLkadvdikgenivKEPPILVHCSAGLDRA 243

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1838351042 1339 GIFCAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQYGLCYELALSY 1390
Cdd:PHA02742   244 GAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIFCYFIVLIF 295
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 1185-1380 1.16e-18

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: 86.19  E-value: 1.16e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1185 YINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQELDETYA-EFWPMQGEAAYGRFHVQFISEEP 1263
Cdd:cd17668      1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCdQYWPADGSEEYGNFLVTQKSVQV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1264 GAGFTAWTLALTN------KQQPKKPPLEVRFWQLKDWPmKQHLPPHPATIISLLgNVETHHRQSRDGHILITCWDGASR 1337
Cdd:cd17668     81 LAYYTVRNFTLRNtkikkgSQKGRPSGRVVTQYHYTQWP-DMGVPEYTLPVLTFV-RKASYAKRHAVGPVVVHCSAGVGR 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1838351042 1338 SGIFCAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQY 1380
Cdd:cd17668    159 TGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQY 201
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 1185-1389 9.86e-18

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: 83.26  E-value: 9.86e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1185 YINAVFVntYTEEDR---LIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQELDETY-AEFWPMQGEAAYGRFHVQFIS 1260
Cdd:cd14546      1 YINASTI--YDHDPRnpaYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQcARYWPEEGSEVYHIYEVHLVS 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1261 EEP-GAGFTAWTLALTNKQQPKKPplEVRFWQLKDWPmKQHLPPHPATIISLLGNVETHHRqSRDGHILITCWDGASRSG 1339
Cdd:cd14546     79 EHIwCDDYLVRSFYLKNLQTSETR--TVTQFHFLSWP-DEGIPASAKPLLEFRRKVNKSYR-GRSCPIVVHCSDGAGRTG 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1838351042 1340 IFCAAGFLCEQIqSEGL--VDVSQAVRMLKRRRRQLIKDVEQyglcYELALS 1389
Cdd:cd14546    155 TYILIDMVLNRM-AKGAkeIDIAATLEHLRDQRPGMVKTKDQ----FEFVLT 201
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 1154-1391 2.53e-17

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: 82.96  E-value: 2.53e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1154 NQPKNRKPGILPADSCRpilmSSLNADGspGYINAVFVNTYT--EEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQ 1231
Cdd:cd14597      3 NRKKNRYKNILPYDTTR----VPLGDEG--GYINASFIKMPVgdEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQ 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1232 LQELDETYAE-FWPmqgeAAYGRfhVQFISEEpgagftaWTLALTNKQQPKKppLEVRFWQLKDWPMKQ-----HL---- 1301
Cdd:cd14597     77 EVEGGKIKCQrYWP----EILGK--TTMVDNR-------LQLTLVRMQQLKN--FVIRVLELEDIQTREvrhitHLnfta 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1302 ------PPHPATIISLLGNVETHHRQsrdGHILITCWDGASRSGIFCAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIK 1375
Cdd:cd14597    142 wpdhdtPSQPEQLLTFISYMRHIHKS---GPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQ 218

                          250
                   ....*....|....*.
gi 1838351042 1376 DVEQYGLCYELALSYL 1391
Cdd:cd14597    219 TEDQYIFCYQVILYVL 234
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 1134-1388 3.02e-17

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: 83.75  E-value: 3.02e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1134 LQKFSELFQLLP-----CreAEKPTNQPKNRKPGILPADSCRPILmsslnaDGSPGYINAVFVNTYTEE----DRLIITQ 1204
Cdd:cd14600     17 LIQFEQLYRKKPglaitC--AKLPQNMDKNRYKDVLPYDATRVVL------QGNEDYINASYVNMEIPSanivNKYIATQ 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1205 MPFPNTVVDFWALVWDYTCTAVVVLNQLQELDETYA-EFWPMQGEAA-YGRFHVQFISEEPGAGFTAWTLALTNKQQPKK 1282
Cdd:cd14600     89 GPLPHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKChQYWPDPPDVMeYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEE 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1283 PPleVRFWQLKDWPmKQHLPPHPATIISLLGNVethhRQSRDGH--ILITCWDGASRSGIFCA---AGFLCEQIQSEGLV 1357
Cdd:cd14600    169 RT--VTHLQYVAWP-DHGVPDDSSDFLEFVNYV----RSKRVENepVLVHCSAGIGRTGVLVTmetAMCLTERNQPVYPL 241

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1838351042 1358 DVsqaVRMLKRRRRQLIKDVEQYGLCYELAL 1388
Cdd:cd14600    242 DI---VRKMRDQRAMMVQTSSQYKFVCEAIL 269
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 1185-1384 7.43e-17

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: 80.54  E-value: 7.43e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1185 YINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQELDETYAE-FWPMQGEAA--YGRFHVQFISE 1261
Cdd:cd14542      1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCErYWPEEGEEQlqFGPFKISLEKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1262 EP-GAGFTAWTLALTNKQQPKkpplevRFWQL--KDWPmKQHLPPHPATIISLLGNVEThHRQSRDGHILITCWDGASRS 1338
Cdd:cd14542     81 KRvGPDFLIRTLKVTFQKESR------TVYQFhyTAWP-DHGVPSSVDPILDLVRLVRD-YQGSEDVPICVHCSAGCGRT 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1838351042 1339 GIFCAAGFLCEQIQSEGLVD---VSQAVRMLKRRRRQLIKDVEQYGLCY 1384
Cdd:cd14542    153 GTICAIDYVWNLLKTGKIPEefsLFDLVREMRKQRPAMVQTKEQYELVY 201
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 1157-1384 8.23e-17

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: 81.42  E-value: 8.23e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1157 KNRKPGILPADSCRpILMSSLNADGSPGYINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQELD 1236
Cdd:cd14602      1 KNRYKDILPYDHSR-VELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1237 ETYAE-FWPMQGEAA--YGRFHVQFISEEPGAGFTAWTLaltnKQQPKKPPLEVRFWQLKDWPmKQHLPPHPATIISLLG 1313
Cdd:cd14602     80 KKKCErYWAEPGEMQleFGPFSVTCEAEKRKSDYIIRTL----KVKFNSETRTIYQFHYKNWP-DHDVPSSIDPILELIW 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1838351042 1314 NVETHHRQSrDGHILITCWDGASRSGIFCAAGFLCEQIQsEGLV----DVSQAVRMLKRRRRQLIKDVEQYGLCY 1384
Cdd:cd14602    155 DVRCYQEDD-SVPICIHCSAGCGRTGVICAIDYTWMLLK-DGIIpenfSVFSLIQEMRTQRPSLVQTKEQYELVY 227
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 1152-1380 2.48e-16

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: 80.85  E-value: 2.48e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1152 PTNQPKNRKPGILPADSCRPILMSSLNADGS-PGYINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLN 1230
Cdd:cd17667     25 PDNKHKNRYINILAYDHSRVKLRPLPGKDSKhSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMIT 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1231 QLQELDETYA-EFWPMQGEAAYGRFHVQFISEEPGAGFTAWTLALTN-------KQQPKKPPLE--VRFWQLKDWPmKQH 1300
Cdd:cd17667    105 NLVEKGRRKCdQYWPTENSEEYGNIIVTLKSTKIHACYTVRRFSIRNtkvkkgqKGNPKGRQNErtVIQYHYTQWP-DMG 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1301 LPPHPATIISLLGNvETHHRQSRDGHILITCWDGASRSGIFCAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQY 1380
Cdd:cd17667    184 VPEYALPVLTFVRR-SSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQY 262
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1286-1389 2.92e-16

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 75.86  E-value: 2.92e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  1286 EVRFWQLKDWPmKQHLPPHPATIISLLGNVETHHRQSRDGH-ILITCWDGASRSGIFCAAGFLCEQIQSEGL-VDVSQAV 1363
Cdd:smart00404    1 TVKHYHYTGWP-DHGVPESPDSILELLRAVKKNLNQSESSGpVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTV 79

                            90       100
                    ....*....|....*....|....*.
gi 1838351042  1364 RMLKRRRRQLIKDVEQYGLCYELALS 1389
Cdd:smart00404   80 KELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1286-1389 2.92e-16

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: 75.86  E-value: 2.92e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  1286 EVRFWQLKDWPmKQHLPPHPATIISLLGNVETHHRQSRDGH-ILITCWDGASRSGIFCAAGFLCEQIQSEGL-VDVSQAV 1363
Cdd:smart00012    1 TVKHYHYTGWP-DHGVPESPDSILELLRAVKKNLNQSESSGpVVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTV 79

                            90       100
                    ....*....|....*....|....*.
gi 1838351042  1364 RMLKRRRRQLIKDVEQYGLCYELALS 1389
Cdd:smart00012   80 KELRSQRPGMVQTEEQYLFLYRALLE 105
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 1185-1391 4.98e-16

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: 78.18  E-value: 4.98e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1185 YINAVFVNTYTEEDRL--IITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQELDETYAE-FWP---MQGEAAYGRFHVQF 1258
Cdd:cd14538      1 YINASHIRIPVGGDTYhyIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHrYWPdslNKPLICGGRLEVSL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1259 ISEEPGAGFTAWTLALTNKQQPKKPPleVRFWQLKDWpmkqhlPPH--PATIISLLGNVETHHRQSRDGHILITCWDGAS 1336
Cdd:cd14538     81 EKYQSLQDFVIRRISLRDKETGEVHH--ITHLNFTTW------PDHgtPQSADPLLRFIRYMRRIHNSGPIVVHCSAGIG 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1838351042 1337 RSGIFCAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQYGLCYELALSYL 1391
Cdd:cd14538    153 RTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1185-1391 1.06e-15

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: 77.88  E-value: 1.06e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1185 YINAVFVnTYTEEDR---LIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQELDETYAE-FWP-MQGEAA---YGRFHV 1256
Cdd:cd14540      1 YINASHI-TATVGGKqrfYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFrYWPtLGGEHDaltFGEYKV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1257 QFISEEPGAGFTAWTLALTNKQQpkkpPLEVRFWQLK--DWPmKQHLPPHPATIISLL---GNVETHHRQSRDGH----- 1326
Cdd:cd14540     80 STKFSVSSGCYTTTGLRVKHTLS----GQSRTVWHLQytDWP-DHGCPEDVSGFLDFLeeiNSVRRHTNQDVAGHnrnpp 154

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1838351042 1327 ILITCWDGASRSGIFCAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQYGLCYELALSYL 1391
Cdd:cd14540    155 TLVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 1126-1391 2.83e-15

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: 78.12  E-value: 2.83e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1126 VLEKEFKALQKFSElFQLLPCREAEK-------PTNQPKNRKPGILPADSCRPILMSslNADGSPGYINA--VFVNTYTE 1196
Cdd:cd14599      4 TLERKLEEGMVFTE-YEQIPKKKADGvfttatlPENAERNRIREVVPYEENRVELVP--TKENNTGYINAshIKVTVGGE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1197 EDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQELDETYA-EFWPMQG----EAAYGRFHV--QFISEepgAGFTA 1269
Cdd:cd14599     81 EWHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKShRYWPKLGskhsSATYGKFKVttKFRTD---SGCYA 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1270 wTLALTNKQQPKKPPLEVRFWQLKDWPmKQHLPPHPATIISLLGNVETHHR---------QSRDGHILITCWDGASRSGI 1340
Cdd:cd14599    158 -TTGLKVKHLLSGQERTVWHLQYTDWP-DHGCPEEVQGFLSYLEEIQSVRRhtnsmldstKNCNPPIVVHCSAGVGRTGV 235

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1838351042 1341 FCAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQYGLCYELALSYL 1391
Cdd:cd14599    236 VILTELMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFL 286
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 860-1092 1.04e-14

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 76.54  E-value: 1.04e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  860 GKELCNQSKNRYKN------IIPYDHCRVVLQPSDTgndYINASYVDSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSV 933
Cdd:PHA02740    42 ANKACAQAENKAKDenlalhITRLLHRRIKLFNDEK---VLDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQI 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  934 IVMLTGLVEQNKTKceQYWPEQEQ---IYGDFTVTLNNTRTTTGLITRIFSLHKAGcGFPRVVEQFHYLLWPDHGV---P 1007
Cdd:PHA02740   119 IVLISRHADKKCFN--QFWSLKEGcviTSDKFQIETLEIIIKPHFNLTLLSLTDKF-GQAQKISHFQYTAWPADGFshdP 195

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1008 RNSAQLLCLVDV----VNKRALEAPAGPVVVHCSAGIGRTGTFIALDFLLKMGKAEGKVDVFHCVQRLREQRISMVQTKE 1083
Cdd:PHA02740   196 DAFIDFFCNIDDlcadLEKHKADGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLD 275


                   ....*....
gi 1838351042 1084 QYTFLYEVV 1092
Cdd:PHA02740   276 DYVFCYHLI 284
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1185-1380 2.11e-14

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: 73.90  E-value: 2.11e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1185 YINAVFVNTYTEE----DRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQELDETYA-EFWPMQGEAA-YGRFHVQF 1258
Cdd:cd14541      2 YINANYVNMEIPGsgivNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKChQYWPDLGETMqFGNLQITC 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1259 ISEEPGAGFTAWTLALTNKQQPKKPplEVRFWQLKDWPmkQH-LPPHPATIISLLGNVethhRQSRDGH---ILITCWDG 1334
Cdd:cd14541     82 VSEEVTPSFAFREFILTNTNTGEER--HITQMQYLAWP--DHgVPDDSSDFLDFVKRV----RQNRVGMvepTVVHCSAG 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1838351042 1335 ASRSGIFCA---AGFLCEQIQSeglVDVSQAVRMLKRRRRQLIKDVEQY 1380
Cdd:cd14541    154 IGRTGVLITmetAMCLIEANEP---VYPLDIVRTMRDQRAMLIQTPSQY 199
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 1185-1385 2.37e-14

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: 73.27  E-value: 2.37e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1185 YINAVFVNTYTEED--RLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQELDET--YAEFWPMQGEAA--YGRFHVQf 1258
Cdd:cd17658      1 YINASLVETPASESlpKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTakCADYFPAEENESreFGRISVT- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1259 iseEPGAGFTAWTLALTNKQ-QPKK---PPLEVRFWQLKDWPmkQHLPPH-PATIISLLGNVetHHRQSRDGHILITCWD 1333
Cdd:cd17658     80 ---NKKLKHSQHSITLRVLEvQYIEseePPLSVLHIQYPEWP--DHGVPKdTRSVRELLKRL--YGIPPSAGPIVVHCSA 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1838351042 1334 GASRSGIFCAAGFLCEQIQSEGL--VDVSQAVRMLKRRRRQLIKDVEQYGLCYE 1385
Cdd:cd17658    153 GIGRTGAYCTIHNTIRRILEGDMsaVDLSKTVRKFRSQRIGMVQTQDQYIFCYA 206
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 1139-1391 3.21e-14

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 75.00  E-value: 3.21e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1139 ELFQLLPCRE--AEKPTNQPKNRKPGILPADSCRPILMSSLNADGSPGYINAVFVNTYTEEDRLIITQMPFPNTVVDFWA 1216
Cdd:PHA02740    30 EYRAIVPEHEdeANKACAQAENKAKDENLALHITRLLHRRIKLFNDEKVLDARFVDGYDFEQKFICIINLCEDACDKFLQ 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1217 LVWDYTCTAVVVLNQLQElDETYAEFWPMQGEA--AYGRFHVQFISEEPGAGFTAWTLALTNKQ-QPKKppleVRFWQLK 1293
Cdd:PHA02740   110 ALSDNKVQIIVLISRHAD-KKCFNQFWSLKEGCviTSDKFQIETLEIIIKPHFNLTLLSLTDKFgQAQK----ISHFQYT 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1294 DWPmKQHLPPHPATIISLLGNVETHH----RQSRDGH---ILITCWDGASRSGIFCAAGFLCEQIQSEGLVDVSQAVRML 1366
Cdd:PHA02740   185 AWP-ADGFSHDPDAFIDFFCNIDDLCadleKHKADGKiapIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKV 263

                          250       260
                   ....*....|....*....|....*
gi 1838351042 1367 KRRRRQLIKDVEQYGLCYELALSYL 1391
Cdd:PHA02740   264 RQKKYGCMNCLDDYVFCYHLIAAYL 288
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 1185-1388 4.70e-14

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: 72.67  E-value: 4.70e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1185 YINAVFVN----TYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVL-NQLQELDETYAEFWP-MQGEAAYGRFHVQF 1258
Cdd:cd14601      2 YINANYINmeipSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLtTQVERGRVKCHQYWPePSGSSSYGGFQVTC 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1259 ISEEPGAGFTAWTLALTNKQQPKKPPLEVrfWQLKDWPmKQHLPPHPATIISLLGNVEThHRQSRDGHILITCWDGASRS 1338
Cdd:cd14601     82 HSEEGNPAYVFREMTLTNLEKNESRPLTQ--IQYIAWP-DHGVPDDSSDFLDFVCLVRN-KRAGKDEPVVVHCSAGIGRT 157

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1838351042 1339 GIFC---AAGFLCEQIQSEGLVDVsqaVRMLKRRRRQLIKDVEQYGLCYELAL 1388
Cdd:cd14601    158 GVLItmeTAMCLIECNQPVYPLDI---VRTMRDQRAMMIQTPSQYRFVCEAIL 207
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 894-1090 1.39e-13

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: 71.66  E-value: 1.39e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  894 INASYVdSYRSPRFFIAAQGPLPGTVLDFWQMVWQEKTSVIVMLTGLVEQNKTKCEQYWPEQEQiYGDFTVTLNNTRT-- 971
Cdd:cd14559     18 LNANRV-QIGNKNVAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYFRQSGT-YGSVTVKSKKTGKde 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  972 -TTGLITRIFSLHKAGCGFPRVVEQFHYLLWPDHGVPRNSA--QLLCLVDVVNK-----------RALEAPAGPV-VVHC 1036
Cdd:cd14559     96 lVDGLKADMYNLKITDGNKTITIPVVHVTNWPDHTAISSEGlkELADLVNKSAEekrnfykskgsSAINDKNKLLpVIHC 175

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1838351042 1037 SAGIGRTGTFIAldfLLKMGKAEGKVDVFHCVQRLREQRIS-MVQTKEQYTFLYE 1090
Cdd:cd14559    176 RAGVGRTGQLAA---AMELNKSPNNLSVEDIVSDMRTSRNGkMVQKDEQLDTLKE 227
PHA02738 PHA02738
hypothetical protein; Provisional
 1148-1393 2.66e-13

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 72.65  E-value: 2.66e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1148 EAEKpTNQPKNRKPGILPADSCRPILMSSLNAdGSpgYINAVFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVV 1227
Cdd:PHA02738    44 NAEK-KNRKLNRYLDAVCFDHSRVILPAERNR-GD--YINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIV 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1228 VLNQLQE-LDETYAEFWP--MQGEAAYGRFHVQFISEEPGAGFTAWTLALTNKQQPKKpplEVRFWQLKDWPmKQHLPPH 1304
Cdd:PHA02738   120 MLCKKKEnGREKCFPYWSdvEQGSIRFGKFKITTTQVETHPHYVKSTLLLTDGTSATQ---TVTHFNFTAWP-DHDVPKN 195

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1305 PATIISLLGNV-----ETHHRQSRDGH-------ILITCWDGASRSGIFCAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQ 1372
Cdd:PHA02738   196 TSEFLNFVLEVrqcqkELAQESLQIGHnrlqpppIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYY 275

                          250       260
                   ....*....|....*....|.
gi 1838351042 1373 LIKDVEQYGLCYELALSYLNS 1393
Cdd:PHA02738   276 SLFIPFQYFFCYRAVKRYVNL 296
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 1185-1391 9.72e-13

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: 68.62  E-value: 9.72e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1185 YINAVFVNTYT--EEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQELDETYAE-FWPMQGEAAY--GRFHVQFI 1259
Cdd:cd14596      1 YINASYITMPVgeEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHrYWPETLQEPMelENYQLRLE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1260 SEEPGAGFTAWTLALTNKQQPKKPplEVRFWQLKDWPmkQHLPPHPATiiSLLGNVETHHRQSRDGHILITCWDGASRSG 1339
Cdd:cd14596     81 NYQALQYFIIRIIKLVEKETGENR--LIKHLQFTTWP--DHGTPQSSD--QLVKFICYMRKVHNTGPIVVHCSAGIGRAG 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1838351042 1340 IFCAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQYGLCYELALSYL 1391
Cdd:cd14596    155 VLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVL 206
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 1185-1391 3.42e-12

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: 67.31  E-value: 3.42e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1185 YINA--VFVNTYTEEDRLIITQMPFPNTVVDFWALVWDYTCTAVVVLNQLQELD-ETYAEFWPMQGE----AAYGRFHV- 1256
Cdd:cd14598      1 YINAshIKVTVGGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGrEKSFRYWPRLGSrhntVTYGRFKIt 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1257 -QFISEepgAGFTAwTLALTNKQQPKKPPLEVRFWQLKDWPMKQHlPPHPATIISLLGNVETHHR--------QSRDGHI 1327
Cdd:cd14598     81 tRFRTD---SGCYA-TTGLKIKHLLTGQERTVWHLQYTDWPEHGC-PEDLKGFLSYLEEIQSVRRhtnstidpKSPNPPV 155

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1838351042 1328 LITCWDGASRSGIFCAAGFLCEQIQSEGLVDVSQAVRMLKRRRRQLIKDVEQYGLCYELALSYL 1391
Cdd:cd14598    156 LVHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFL 219
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 985-1088 3.14e-11

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: 62.68  E-value: 3.14e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  985 AGCGFPRVVEQFHYLLwpDHG----------------------------VPRNSA----QLLCLVDVVNKRalEAPAGPV 1032
Cdd:cd14504     10 AGMAFPRLPEHYAYLN--ENGirhvvtlteepppehsdtcpglryhhipIEDYTPptleQIDEFLDIVEEA--NAKNEAV 85

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1838351042 1033 VVHCSAGIGRTGTFIALdFLLKMGKAEGkVDVfhcVQRLREQRISMVQTKEQYTFL 1088
Cdd:cd14504     86 LVHCLAGKGRTGTMLAC-YLVKTGKISA-VDA---INEIRRIRPGSIETSEQEKFV 136
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
995-1090 1.68e-10

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 60.37  E-value: 1.68e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  995 QFHYLLWPDHGVPRNsAQLLCLVDVVnKRALEAPaGPVVVHCSAGIGRTGTFIALdFLLKMGkaegkVDVFHCVQRLREQ 1074
Cdd:COG2453     49 EYLHLPIPDFGAPDD-EQLQEAVDFI-DEALREG-KKVLVHCRGGIGRTGTVAAA-YLVLLG-----LSAEEALARVRAA 119

                           90
                   ....*....|....*.
gi 1838351042 1075 RISMVQTKEQYTFLYE 1090
Cdd:COG2453    120 RPGAVETPAQRAFLER 135
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1023-1090 4.01e-10

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: 58.52  E-value: 4.01e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1838351042 1023 RALEAPAGPVVVHCSAGIGRTGTFIALDFLLKMGKaegkvDVFHCVQRLREQR-ISMVQTKEQYTFLYE 1090
Cdd:cd14494     50 DQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLGGM-----SAEEAVRIVRLIRpGGIPQTIEQLDFLIK 113
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 995-1090 2.24e-08

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


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 54.96  E-value: 2.24e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  995 QFHYLLWPDHGVPRNSAQLLCLVDVVnKRALEAPAGpVVVHCSAGIGRTGTfIALDFLLKMGkaeGKVDVFHCVQRLREQ 1074
Cdd:cd14505     74 TWHHLPIPDGGVPSDIAQWQELLEEL-LSALENGKK-VLIHCKGGLGRTGL-IAACLLLELG---DTLDPEQAIAAVRAL 147

                           90
                   ....*....|....*.
gi 1838351042 1075 RISMVQTKEQYTFLYE 1090
Cdd:cd14505    148 RPGAIQTPKQENFLHQ 163
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 996-1090 8.04e-08

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: 54.28  E-value: 8.04e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  996 FHYLLWPDHGVPrNSAQLLCLVDVVNKRALEApaGPVVVHCSAGIGRTGTFIA--LDFLLKMGKAEgkvdvfhCVQRLRE 1073
Cdd:cd14506     79 FYNFGWKDYGVP-SLTTILDIVKVMAFALQEG--GKVAVHCHAGLGRTGVLIAcyLVYALRMSADQ-------AIRLVRS 148

                           90
                   ....*....|....*..
gi 1838351042 1074 QRISMVQTKEQYTFLYE 1090
Cdd:cd14506    149 KRPNSIQTRGQVLCVRE 165
CDC14_C cd14499
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ...
 995-1049 7.33e-05

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: 44.75  E-value: 7.33e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1838351042  995 QFHYLLWPDHGVPRNsaqllclvDVVNK--RALEAPAGPVVVHCSAGIGRTGTFIAL 1049
Cdd:cd14499     81 RHYDLYFPDGSTPSD--------DIVKKflDICENEKGAIAVHCKAGLGRTGTLIAC 129
PTP-IVa1 cd18537
protein tyrosine phosphatase type IVA 1; Protein tyrosine phosphatase type IVA 1 (PTP-IVa1), ...
 994-1083 7.55e-04

protein tyrosine phosphatase type IVA 1; Protein tyrosine phosphatase type IVA 1 (PTP-IVa1), also known as protein-tyrosine phosphatase of regenerating liver 1 (PRL-1), stimulates progression from G1 into S phase during mitosis and enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. It may play a role in the development and maintenance of differentiating epithelial tissues. PRL-1 promotes cell growth and migration by activating both the ERK1/2 and RhoA pathways. It is a member of the PTP-IVa/PRL family of small, prenylated phosphatases that are the most oncogenic of all PTPs. PRLs associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation.


Pssm-ID: 350513 [Multi-domain]  Cd Length: 167  Bit Score: 41.98  E-value: 7.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  994 EQFHYLLWP-DHGVPRNSAQLLCLVDVVNKRALEAPAGPVVVHCSAGIGRTGTFIALDFLlkmgkaEGKVDVFHCVQRLR 1072
Cdd:cd18537     61 EGIQVLDWPfDDGAPPSNQIVDDWLNLLKVKFREEPGCCIAVHCVAGLGRAPVLVALALI------ECGMKYEDAVQFIR 134

                           90
                   ....*....|.
gi 1838351042 1073 EQRISMVQTKE 1083
Cdd:cd18537    135 QKRRGAFNSKQ 145
PTP-IVa3 cd18535
protein tyrosine phosphatase type IVA 3; Protein tyrosine phosphatase type IVA 3 (PTP-IVa3), ...
 1001-1088 9.83e-04

protein tyrosine phosphatase type IVA 3; Protein tyrosine phosphatase type IVA 3 (PTP-IVa3), also known as protein-tyrosine phosphatase of regenerating liver 3 (PRL-3), stimulates progression from G1 into S phase during mitosis and enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. It exerts its oncogenic functions through activation of PI3K/Akt, which is a key regulator of the rapamycin-sensitive mTOR complex 1. PRL-3 is a member of the PTP-IVa/PRL family of small, prenylated phosphatases that are the most oncogenic of all PTPs. PRLs associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation.


Pssm-ID: 350511 [Multi-domain]  Cd Length: 154  Bit Score: 41.16  E-value: 9.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042 1001 WP-DHGVPRNSAQLLCLVDVVNKRALEAPAGPVVVHCSAGIGRTGTFIALDFLLKMGKAEgkvdvfHCVQRLREQRISMV 1079
Cdd:cd18535     64 WPfDDGAPPPGKVVEDWLSLLKTKFCEDPGCCVAVHCVAGLGRAPVLVALALIESGMKYE------DAIQFIRQKRRGAI 137


                   ....*....
gi 1838351042 1080 QTKeQYTFL 1088
Cdd:cd18535    138 NSK-QLTYL 145
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 1001-1060 1.62e-03

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: 40.64  E-value: 1.62e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1838351042 1001 WPDHGVPrnSAQLLC-LVDVVNKRALEAPAGPVVVHCSAGIGRTGTFIALdFLLKMGKAEG 1060
Cdd:cd14497     68 FPDHHPP--PLGLLLeIVDDIDSWLSEDPNNVAVVHCKAGKGRTGTVICA-YLLYYGQYST 125
Y_phosphatase3 pfam13350
Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 ...
 1023-1049 1.86e-03

Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 families.


Pssm-ID: 463853 [Multi-domain]  Cd Length: 243  Bit Score: 41.46  E-value: 1.86e-03
                           10        20
                   ....*....|....*....|....*..
gi 1838351042 1023 RALEAPAGPVVVHCSAGIGRTGTFIAL 1049
Cdd:pfam13350  123 EALADNDGPVLFHCTAGKDRTGVAAAL 149
Oca4 COG2365
Protein tyrosine/serine phosphatase Oca4 [Signal transduction mechanisms];
1025-1056 2.28e-03

Protein tyrosine/serine phosphatase Oca4 [Signal transduction mechanisms];


Pssm-ID: 441932 [Multi-domain]  Cd Length: 248  Bit Score: 41.48  E-value: 2.28e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1838351042 1025 LEAPAGPVVVHCSAGIGRTGTFIALdFLLKMG 1056
Cdd:COG2365    129 ADAENGPVLFHCTAGKDRTGVAAAL-LLLALG 159
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 513-591 2.40e-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.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 38.63  E-value: 2.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838351042  513 PDKPEQLWLDPSTGS---LSWEPLPSCKGEIIGYQLNITARSaQDRALLELERLRLSGSVTAHPLPahgPGTSYVVTVRG 589
Cdd:cd00063      1 PSPPTNLRVTDVTSTsvtLSWTPPEDDGGPITGYVVEYREKG-SGDWKEVEVTPGSETSYTLTGLK---PGTEYEFRVRA 76


                   ..
gi 1838351042  590 LT 591
Cdd:cd00063     77 VN 78
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 1023-1049 2.47e-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: 40.05  E-value: 2.47e-03
                           10        20
                   ....*....|....*....|....*..
gi 1838351042 1023 RALEAPaGPVVVHCSAGIGRTGTFIAL 1049
Cdd:cd14529     84 DLKLAP-GPVLIHCKHGKDRTGLVSAL 109
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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