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Conserved domains on  [gi|2064663964|ref|XP_002404238|]
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LOW QUALITY PROTEIN: tyrosine-protein phosphatase non-receptor type 14 [Ixodes scapularis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 833-1054 2.42e-129

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: 391.43  E-value: 2.42e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  833 YINASHVSASVGDSQRFYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTDTEDDqGHEKCYQYWPQANGEEAALSFGEYRV 912
Cdd:cd14540      1 YINASHITATVGGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEG-GREKCFRYWPTLGGEHDALTFGEYKV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  913 VRKSAVSSAVAVTTCLVLSRTQgvSCTHRNVWHLRYTDWPDHGTPGDVQGFLGFMEEVDSVRRLALNDQRLRTRNAPTVV 992
Cdd:cd14540     80 STKFSVSSGCYTTTGLRVKHTL--SGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSVRRHTNQDVAGHNRNPPTLV 157

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2064663964  993 HCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLAQYKFVHQVLIRYL 1054
Cdd:cd14540    158 HCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
FERM_F1_PTPN14_like cd17099
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 18-102 2.95e-46

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein phosphatase non-receptors PTPN14, PTPN21, and similar proteins; This family includes tyrosine-protein phosphatase non-receptors PTPN14 and PTPN21, both of which are protein-tyrosine phosphatase (PTP). They belong to the FERM family of PTPs characterized by a conserved N-terminal FERM domain and a C-terminal PTP catalytic domain with an intervening sequence containing an acidic region and a putative SH3 domain-binding sequence. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). PTPN14 plays a role in the nucleus during cell proliferation. PTPN21 interacts with a Tec tyrosine kinase family member, the epithelial and endothelial tyrosine kinase (Etk, also known as Bmx), modulates Stat3 activation, and plays a role in the regulation of cell growth and differentiation.


:

Pssm-ID: 340619  Cd Length: 85  Bit Score: 160.09  E-value: 2.95e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964   18 KSLCVIAVKLLENSTVECIVSSRTVGKECLQNVCQRLQILQPEYFGLRYPSKDGVLRWVDLDRPLKKQLDKYARECCLYL 97
Cdd:cd17099      1 KNSFVVRIQLLDNTVLECTLSPESTGQDCLEYVAQRLELREIEYFGLRYVNKKGQLRWVDLEKPLKKQLDKHAHEPLLYF 80


                   ....*
gi 2064663964   98 GVMFY 102
Cdd:cd17099     81 GVMFY 85
FERM_C_PTPN14_PTPN21 cd13188
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 14 and 21 (PTPN14 and ...
 216-309 9.88e-40

FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 14 and 21 (PTPN14 and 21); This CD contains PTP members: pez/PTPN14 and PTPN21. A number of mutations in Pez have been shown to be associated with breast and colorectal cancer. The PTPN protein family belong to larger family of PTPs. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. The members are composed of a N-terminal FERM domain and a C-terminal PTP catalytic domain. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. Like most other ERM members they have a phosphoinositide-binding site in their FERM domain. The FERM C domain is the third structural domain within the FERM domain. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs) , the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


:

Pssm-ID: 270009  Cd Length: 91  Bit Score: 141.66  E-value: 9.88e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  216 YGEELFDVKDAAGNETVLGVSVEGVTARYNRGGTaneTASYRWSEIVDLIHHKKSFKIEGRENGRSAQFQLEDVPTAKYI 295
Cdd:cd13188      1 YGEESFPAKDEQGNEVLIGASLEGIFVKHDNGRP---PVFFRWEDIKNVINHKRTFSIECQNSEETVQFQFEDAETAKYV 77

                           90
                   ....*....|....
gi 2064663964  296 WKMCVQQHKFFMSM 309
Cdd:cd13188     78 WKLCVLQHKFYRQN 91
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 22-221 1.71e-39

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


:

Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 145.52  E-value: 1.71e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964    22 VIAVKLLENSTVECIVSSRTVGKECLQNVCQRLQILQPEYFGLRYPSKDGVLR-WVDLDRPLKKQLDKYArECCLYLGVM 100
Cdd:smart00295    1 VLKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLRhWLDPAKTLLDQDVKSE-PLTLYFRVK 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964   101 FYVFNVDRLHNDVTRY-YYFSHLKSDVIEGKLACTRDEAIQLASYSLQAEFGDHRPE-HHTSDYLKNFVLLPKSVAgGEE 178
Cdd:smart00295   80 FYPPDPNQLKEDPTRLnLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEElHDLRGELSLKRFLPKQLL-DSR 158

                           170       180       190       200
                    ....*....|....*....|....*....|....*....|...
gi 2064663964   179 NQEALLEQIIQAHRSLQGIHHSLAELYYIIAVQGLEGYGEELF 221
Cdd:smart00295  159 KLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
PRK10263 super family cl35903
DNA translocase FtsK; Provisional
 546-721 1.48e-05

DNA translocase FtsK; Provisional


The actual alignment was detected with superfamily member PRK10263:

Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 49.31  E-value: 1.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  546 VDGVAHGRPLLAPPLHTYStpeltsqglsyemnPAQLFANLNYQHKPPPPYPYSQRPTASTPDLTRNHSHLLQVSTSPDL 625
Cdd:PRK10263   363 VPGPQTGEPVIAPAPEGYP--------------QQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQP 428

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  626 VSRRHLTPNPTQGSEPSlaQYQWVNGRAVEDVKPVLPTYVPVGESwNAQVSGVVQPQRIQVFVSSSPVPATEQTavKPSN 705
Cdd:PRK10263   429 AQQPYYAPAPEQPVAGN--AWQAEEQQSTFAPQSTYQTEQTYQQP-AAQEPLYQQPQPVEQQPVVEPEPVVEET--KPAR 503

                          170       180
                   ....*....|....*....|.
gi 2064663964  706 PP-----PLPERQTSEEESSA 721
Cdd:PRK10263   504 PPlyyfeEVEEKRAREREQLA 524
 
Name Accession Description Interval E-value
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 833-1054 2.42e-129

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: 391.43  E-value: 2.42e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  833 YINASHVSASVGDSQRFYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTDTEDDqGHEKCYQYWPQANGEEAALSFGEYRV 912
Cdd:cd14540      1 YINASHITATVGGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEG-GREKCFRYWPTLGGEHDALTFGEYKV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  913 VRKSAVSSAVAVTTCLVLSRTQgvSCTHRNVWHLRYTDWPDHGTPGDVQGFLGFMEEVDSVRRLALNDQRLRTRNAPTVV 992
Cdd:cd14540     80 STKFSVSSGCYTTTGLRVKHTL--SGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSVRRHTNQDVAGHNRNPPTLV 157

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2064663964  993 HCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLAQYKFVHQVLIRYL 1054
Cdd:cd14540    158 HCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
783-1052 2.93e-85

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 276.08  E-value: 2.93e-85
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964   783 EFENIAKRKP-NADFSTALLLENIPRNRFSDVLPYEENRVRLTPSADNRTGYINASHVSasVGDSQRFYIAAQGPMQTTA 861
Cdd:smart00194    5 EFEKLDRLKPdDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYID--GPNGPKAYIATQGPLPSTV 82

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964   862 KSFWQMVWENHVGVVVMLTDtEDDQGHEKCYQYWPQANGEEaaLSFGEYRVVRKSAVSSAVAVTTCLVLSRTQGVscTHR 941
Cdd:smart00194   83 EDFWRMVWEQKVTVIVMLTE-LVEKGREKCAQYWPDEEGEP--LTYGDITVTLKSVEKVDDYTIRTLEVTNTGCS--ETR 157

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964   942 NVWHLRYTDWPDHGTPGDVQGFLGFMEEVDSVRRlalndqrlrTRNAPTVVHCTAGVGRSGVVILCDILLFCLDHNVPVD 1021
Cdd:smart00194  158 TVTHYHYTNWPDHGVPESPESILDLIRAVRKSQS---------TSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVD 228

                           250       260       270
                    ....*....|....*....|....*....|.
gi 2064663964  1022 LPRVLTLVRMQRMLSVQTLAQYKFVHQVLIR 1052
Cdd:smart00194  229 IFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
804-1051 4.15e-82

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 266.42  E-value: 4.15e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  804 NIPRNRFSDVLPYEENRVRLTPSADNrTGYINASHVSASVGdsQRFYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTdTE 883
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGP-SDYINASYIDGYKK--PKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLT-EL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  884 DDQGHEKCYQYWPQANGEEaaLSFGEYRV--VRKSAVSSAVAVTTcLVLSRTQgvSCTHRNVWHLRYTDWPDHGTPGDVQ 961
Cdd:pfam00102   77 EEKGREKCAQYWPEEEGES--LEYGDFTVtlKKEKEDEKDYTVRT-LEVSNGG--SEETRTVKHFHYTGWPDHGVPESPN 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  962 GFLGFMEEVdsvrrlalNDQRLRTRNAPTVVHCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLA 1041
Cdd:pfam00102  152 SLLDLLRKV--------RKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLE 223

                          250
                   ....*....|
gi 2064663964 1042 QYKFVHQVLI 1051
Cdd:pfam00102  224 QYIFLYDAIL 233
FERM_F1_PTPN14_like cd17099
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 18-102 2.95e-46

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein phosphatase non-receptors PTPN14, PTPN21, and similar proteins; This family includes tyrosine-protein phosphatase non-receptors PTPN14 and PTPN21, both of which are protein-tyrosine phosphatase (PTP). They belong to the FERM family of PTPs characterized by a conserved N-terminal FERM domain and a C-terminal PTP catalytic domain with an intervening sequence containing an acidic region and a putative SH3 domain-binding sequence. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). PTPN14 plays a role in the nucleus during cell proliferation. PTPN21 interacts with a Tec tyrosine kinase family member, the epithelial and endothelial tyrosine kinase (Etk, also known as Bmx), modulates Stat3 activation, and plays a role in the regulation of cell growth and differentiation.


Pssm-ID: 340619  Cd Length: 85  Bit Score: 160.09  E-value: 2.95e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964   18 KSLCVIAVKLLENSTVECIVSSRTVGKECLQNVCQRLQILQPEYFGLRYPSKDGVLRWVDLDRPLKKQLDKYARECCLYL 97
Cdd:cd17099      1 KNSFVVRIQLLDNTVLECTLSPESTGQDCLEYVAQRLELREIEYFGLRYVNKKGQLRWVDLEKPLKKQLDKHAHEPLLYF 80


                   ....*
gi 2064663964   98 GVMFY 102
Cdd:cd17099     81 GVMFY 85
PHA02738 PHA02738
hypothetical protein; Provisional
 783-1054 2.13e-45

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 166.64  E-value: 2.13e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  783 EFENIAKRKPNADFSTALllENIPRNRFSDVLPYEENRVRLtPSADNRTGYINASHVSASvgDSQRFYIAAQGPMQTTAK 862
Cdd:PHA02738    30 EHQKVISEKVDGTFNAEK--KNRKLNRYLDAVCFDHSRVIL-PAERNRGDYINANYVDGF--EYKKKFICGQAPTRQTCY 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  863 SFWQMVWENHVGVVVMLTDTEDDqGHEKCYQYWpqANGEEAALSFGEYRVVRKSAVSSAVAVTTCLVLsrTQGVSCThRN 942
Cdd:PHA02738   105 DFYRMLWMEHVQIIVMLCKKKEN-GREKCFPYW--SDVEQGSIRFGKFKITTTQVETHPHYVKSTLLL--TDGTSAT-QT 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  943 VWHLRYTDWPDHGTPGDVQGFLGFMEEVDSVRR------LALNDQRLRTrnAPTVVHCTAGVGRSGVVILCDILLFCLDH 1016
Cdd:PHA02738   179 VTHFNFTAWPDHDVPKNTSEFLNFVLEVRQCQKelaqesLQIGHNRLQP--PPIVVHCNAGLGRTPCYCVVDISISRFDA 256

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 2064663964 1017 NVPVDLPRVLTLVRMQRMLSVQTLAQYKFVHQVLIRYL 1054
Cdd:PHA02738   257 CATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAVKRYV 294
FERM_C_PTPN14_PTPN21 cd13188
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 14 and 21 (PTPN14 and ...
 216-309 9.88e-40

FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 14 and 21 (PTPN14 and 21); This CD contains PTP members: pez/PTPN14 and PTPN21. A number of mutations in Pez have been shown to be associated with breast and colorectal cancer. The PTPN protein family belong to larger family of PTPs. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. The members are composed of a N-terminal FERM domain and a C-terminal PTP catalytic domain. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. Like most other ERM members they have a phosphoinositide-binding site in their FERM domain. The FERM C domain is the third structural domain within the FERM domain. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs) , the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270009  Cd Length: 91  Bit Score: 141.66  E-value: 9.88e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  216 YGEELFDVKDAAGNETVLGVSVEGVTARYNRGGTaneTASYRWSEIVDLIHHKKSFKIEGRENGRSAQFQLEDVPTAKYI 295
Cdd:cd13188      1 YGEESFPAKDEQGNEVLIGASLEGIFVKHDNGRP---PVFFRWEDIKNVINHKRTFSIECQNSEETVQFQFEDAETAKYV 77

                           90
                   ....*....|....
gi 2064663964  296 WKMCVQQHKFFMSM 309
Cdd:cd13188     78 WKLCVLQHKFYRQN 91
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 22-221 1.71e-39

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 145.52  E-value: 1.71e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964    22 VIAVKLLENSTVECIVSSRTVGKECLQNVCQRLQILQPEYFGLRYPSKDGVLR-WVDLDRPLKKQLDKYArECCLYLGVM 100
Cdd:smart00295    1 VLKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLRhWLDPAKTLLDQDVKSE-PLTLYFRVK 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964   101 FYVFNVDRLHNDVTRY-YYFSHLKSDVIEGKLACTRDEAIQLASYSLQAEFGDHRPE-HHTSDYLKNFVLLPKSVAgGEE 178
Cdd:smart00295   80 FYPPDPNQLKEDPTRLnLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEElHDLRGELSLKRFLPKQLL-DSR 158

                           170       180       190       200
                    ....*....|....*....|....*....|....*....|...
gi 2064663964   179 NQEALLEQIIQAHRSLQGIHHSLAELYYIIAVQGLEGYGEELF 221
Cdd:smart00295  159 KLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
802-1054 2.65e-31

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 124.43  E-value: 2.65e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  802 LENIPRNRFSDVLPYEENRVRltpsADNrtGYINASHVSasVGDSQRfYIAAQGPMQTTAKSFWQMVWENHVGVVVMLT- 880
Cdd:COG5599     40 INGSPLNRFRDIQPYKETALR----ANL--GYLNANYIQ--VIGNHR-YIATQYPLEEQLEDFFQMLFDNNTPVLVVLAs 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  881 DTEDDQGHEKCYQYWPQaNGEEAALSFgEYRVVRKSAVSSAVAVTTCLVlsRTQGVSCTHRNVWHLRYTDWPDHGTPGDV 960
Cdd:COG5599    111 DDEISKPKVKMPVYFRQ-DGEYGKYEV-SSELTESIQLRDGIEARTYVL--TIKGTGQKKIEIPVLHVKNWPDHGAISAE 186

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  961 QgflgFMEEVDSVRRLAlndQRLRTRNAPTVVHCTAGVGRSGVVILCDILLFCL--DHNVPVDLPRVLTLVRMQR---Ml 1035
Cdd:COG5599    187 A----LKNLADLIDKKE---KIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSInaLVQITLSVEEIVIDMRTSRnggM- 258

                          250
                   ....*....|....*....
gi 2064663964 1036 sVQTLAQYkfvhQVLIRYL 1054
Cdd:COG5599    259 -VQTSEQL----DVLVKLA 272
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 105-221 3.54e-31

FERM central domain; This domain is the central structural domain of the FERM domain.


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 118.53  E-value: 3.54e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  105 NVDRLHNDVTRYYYFSHLKSDVIEGKLACTRDEAIQLASYSLQAEFGDHRPEHHTSDYLKNFVLLPKSVAgGEENQEALL 184
Cdd:pfam00373    2 LELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYLSLESFLPKQLL-RKMKSKELE 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2064663964  185 EQIIQAHRSLQGIHHSLAELYYIIAVQGLEGYGEELF 221
Cdd:pfam00373   81 KRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 114-213 2.55e-26

FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C/N, alpha-, and C-lobe/A-lobe, B-lobe, C-lobe/F1, F2, F3). The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases, the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the pleckstrin homology (PH) and phosphotyrosine binding (PTB) domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 271216  Cd Length: 99  Bit Score: 103.87  E-value: 2.55e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  114 TRYYYFSHLKSDVIEGKLACTRDEAIQLASYSLQAEFGDHRPEHHTSDYLKNFVLLPKSVAGGeENQEALLEQIIQAHRS 193
Cdd:cd14473      1 TRYLLYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKPKYLSLKRFLPKQLLKQ-RKPEEWEKRIVELHKK 79

                           90       100
                   ....*....|....*....|
gi 2064663964  194 LQGIHHSLAELYYIIAVQGL 213
Cdd:cd14473     80 LRGLSPAEAKLKYLKIARKL 99
FERM_N pfam09379
FERM N-terminal domain; This domain is the N-terminal ubiquitin-like structural domain of the ...
 25-87 4.62e-16

FERM N-terminal domain; This domain is the N-terminal ubiquitin-like structural domain of the FERM domain.


Pssm-ID: 430570  Cd Length: 63  Bit Score: 73.39  E-value: 4.62e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2064663964   25 VKLLENSTVECIVSSRTVGKECLQNVCQRLQILQPEYFGLRYPSKDGVLRWVDLDRPLKKQLD 87
Cdd:pfam09379    1 VRLLDGTVLEFDVQPKATGQVLLDQVCNHLNLKEKDYFGLQFLDDNGEHRWLDLSKRLSKQAP 63
FERM_C pfam09380
FERM C-terminal PH-like domain;
225-310 6.71e-16

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 73.83  E-value: 6.71e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  225 DAAGNETVLGVSVEGVTARYNRGGTANetaSYRWSEIVDLIHHKKSFKIEGREN--GRSAQFQLEDVPTAKYIWKMCVQQ 302
Cdd:pfam09380    1 DKEGTDLWLGVSAKGILVYEDNNKILN---LFPWREIRKISFKRKKFLIKLRDKssEETLGFYTESSRACKYLWKLCVEQ 77


                   ....*...
gi 2064663964  303 HKFFMSMQ 310
Cdd:pfam09380   78 HTFFRLRR 85
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 546-721 1.48e-05

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 49.31  E-value: 1.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  546 VDGVAHGRPLLAPPLHTYStpeltsqglsyemnPAQLFANLNYQHKPPPPYPYSQRPTASTPDLTRNHSHLLQVSTSPDL 625
Cdd:PRK10263   363 VPGPQTGEPVIAPAPEGYP--------------QQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQP 428

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  626 VSRRHLTPNPTQGSEPSlaQYQWVNGRAVEDVKPVLPTYVPVGESwNAQVSGVVQPQRIQVFVSSSPVPATEQTavKPSN 705
Cdd:PRK10263   429 AQQPYYAPAPEQPVAGN--AWQAEEQQSTFAPQSTYQTEQTYQQP-AAQEPLYQQPQPVEQQPVVEPEPVVEET--KPAR 503

                          170       180
                   ....*....|....*....|.
gi 2064663964  706 PP-----PLPERQTSEEESSA 721
Cdd:PRK10263   504 PPlyyfeEVEEKRAREREQLA 524
 
Name Accession Description Interval E-value
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 833-1054 2.42e-129

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: 391.43  E-value: 2.42e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  833 YINASHVSASVGDSQRFYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTDTEDDqGHEKCYQYWPQANGEEAALSFGEYRV 912
Cdd:cd14540      1 YINASHITATVGGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEG-GREKCFRYWPTLGGEHDALTFGEYKV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  913 VRKSAVSSAVAVTTCLVLSRTQgvSCTHRNVWHLRYTDWPDHGTPGDVQGFLGFMEEVDSVRRLALNDQRLRTRNAPTVV 992
Cdd:cd14540     80 STKFSVSSGCYTTTGLRVKHTL--SGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSVRRHTNQDVAGHNRNPPTLV 157

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2064663964  993 HCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLAQYKFVHQVLIRYL 1054
Cdd:cd14540    158 HCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQYL 219
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 770-1055 1.31e-105

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: 331.58  E-value: 1.31e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  770 VLESRLEDGQVFLEFENIAKRKPNADFSTALLLENIPRNRFSDVLPYEENRVRLTPSADNRTGYINASHVSASVGDSQRF 849
Cdd:cd14599      4 TLERKLEEGMVFTEYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVPTKENNTGYINASHIKVTVGGEEWH 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  850 YIAAQGPMQTTAKSFWQMVWENHVGVVVMLTdTEDDQGHEKCYQYWPQANGEEAALSFGEYRVVRKSAVSSAVAVTTCLV 929
Cdd:cd14599     84 YIATQGPLPHTCHDFWQMVWEQGVNVIAMVT-AEEEGGRSKSHRYWPKLGSKHSSATYGKFKVTTKFRTDSGCYATTGLK 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  930 LSRTqgVSCTHRNVWHLRYTDWPDHGTPGDVQGFLGFMEEVDSVRRLALND-QRLRTRNAPTVVHCTAGVGRSGVVILCD 1008
Cdd:cd14599    163 VKHL--LSGQERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRRHTNSMlDSTKNCNPPIVVHCSAGVGRTGVVILTE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 2064663964 1009 ILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLAQYKFVHQVLIRYLR 1055
Cdd:cd14599    241 LMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFLK 287
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
783-1052 2.93e-85

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 276.08  E-value: 2.93e-85
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964   783 EFENIAKRKP-NADFSTALLLENIPRNRFSDVLPYEENRVRLTPSADNRTGYINASHVSasVGDSQRFYIAAQGPMQTTA 861
Cdd:smart00194    5 EFEKLDRLKPdDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYID--GPNGPKAYIATQGPLPSTV 82

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964   862 KSFWQMVWENHVGVVVMLTDtEDDQGHEKCYQYWPQANGEEaaLSFGEYRVVRKSAVSSAVAVTTCLVLSRTQGVscTHR 941
Cdd:smart00194   83 EDFWRMVWEQKVTVIVMLTE-LVEKGREKCAQYWPDEEGEP--LTYGDITVTLKSVEKVDDYTIRTLEVTNTGCS--ETR 157

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964   942 NVWHLRYTDWPDHGTPGDVQGFLGFMEEVDSVRRlalndqrlrTRNAPTVVHCTAGVGRSGVVILCDILLFCLDHNVPVD 1021
Cdd:smart00194  158 TVTHYHYTNWPDHGVPESPESILDLIRAVRKSQS---------TSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVD 228

                           250       260       270
                    ....*....|....*....|....*....|.
gi 2064663964  1022 LPRVLTLVRMQRMLSVQTLAQYKFVHQVLIR 1052
Cdd:smart00194  229 IFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
804-1051 4.15e-82

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 266.42  E-value: 4.15e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  804 NIPRNRFSDVLPYEENRVRLTPSADNrTGYINASHVSASVGdsQRFYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTdTE 883
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKLTGDPGP-SDYINASYIDGYKK--PKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLT-EL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  884 DDQGHEKCYQYWPQANGEEaaLSFGEYRV--VRKSAVSSAVAVTTcLVLSRTQgvSCTHRNVWHLRYTDWPDHGTPGDVQ 961
Cdd:pfam00102   77 EEKGREKCAQYWPEEEGES--LEYGDFTVtlKKEKEDEKDYTVRT-LEVSNGG--SEETRTVKHFHYTGWPDHGVPESPN 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  962 GFLGFMEEVdsvrrlalNDQRLRTRNAPTVVHCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLA 1041
Cdd:pfam00102  152 SLLDLLRKV--------RKSSLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLE 223

                          250
                   ....*....|
gi 2064663964 1042 QYKFVHQVLI 1051
Cdd:pfam00102  224 QYIFLYDAIL 233
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 833-1055 4.81e-78

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: 254.90  E-value: 4.81e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  833 YINASHVSASVGDSQRFYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTdTEDDQGHEKCYQYWPQANGEEAALSFGEYRV 912
Cdd:cd14598      1 YINASHIKVTVGGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVT-AEEEGGREKSFRYWPRLGSRHNTVTYGRFKI 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  913 VRKSAVSSAVAVTTCLVLSRTqgVSCTHRNVWHLRYTDWPDHGTPGDVQGFLGFMEEVDSVRRLALNDQRLRTRNAPTVV 992
Cdd:cd14598     80 TTRFRTDSGCYATTGLKIKHL--LTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNSTIDPKSPNPPVLV 157

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2064663964  993 HCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLAQYKFVHQVLIRYLR 1055
Cdd:cd14598    158 HCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 833-1048 6.71e-66

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: 220.62  E-value: 6.71e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  833 YINASHVSasVGDSQRFYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTDtEDDQGHEKCYQYWPQANGEEaaLSFGEYRV 912
Cdd:cd00047      1 YINASYID--GYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTN-LVEKGREKCERYWPEEGGKP--LEYGDITV 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  913 VRKSAVSSAVAVTTCLVLSRTQgvSCTHRNVWHLRYTDWPDHGTPGDVQGFLGFMEEVDsvrrlalndQRLRTRNAPTVV 992
Cdd:cd00047     76 TLVSEEELSDYTIRTLELSPKG--CSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVR---------KEARKPNGPIVV 144

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2064663964  993 HCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLAQYKFVHQ 1048
Cdd:cd00047    145 HCSAGVGRTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 771-1052 7.78e-61

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: 208.94  E-value: 7.78e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  771 LESRLEDGQVFLEFENIAKRKPNADFSTALLLENIPRNRFSDVLPYEENRVRLTPSADnrtgYINASHVS---ASVGDSQ 847
Cdd:cd14600      7 LKKGLESGTVLIQFEQLYRKKPGLAITCAKLPQNMDKNRYKDVLPYDATRVVLQGNED----YINASYVNmeiPSANIVN 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  848 RfYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTdTEDDQGHEKCYQYWPQAngeEAALSFGEYRVVRKSAVSSAVAVTTC 927
Cdd:cd14600     83 K-YIATQGPLPHTCAQFWQVVWEQKLSLIVMLT-TLTERGRTKCHQYWPDP---PDVMEYGGFRVQCHSEDCTIAYVFRE 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  928 LVLSRTQgvSCTHRNVWHLRYTDWPDHGTPGDVQGFLGFmeeVDSVRRLalndqrlRTRNAPTVVHCTAGVGRSGVVILC 1007
Cdd:cd14600    158 MLLTNTQ--TGEERTVTHLQYVAWPDHGVPDDSSDFLEF---VNYVRSK-------RVENEPVLVHCSAGIGRTGVLVTM 225

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 2064663964 1008 DILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLAQYKFVHQVLIR 1052
Cdd:cd14600    226 ETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAILR 270
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 833-1048 2.51e-55

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: 190.92  E-value: 2.51e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  833 YINASHVSASvGDSQRFYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTDtEDDQGHEKCYQYWPQangEEAALSFGEYRV 912
Cdd:cd18533      1 YINASYITLP-GTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTP-LVENGREKCDQYWPS---GEYEGEYGDLTV 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  913 --VRKSAVSSAVAVTTCLVLSRTQGVScthRNVWHLRYTDWPDHGTPGDVQGFLGFMEEVDSVRRLALNDqrlrtrnAPT 990
Cdd:cd18533     76 elVSEEENDDGGFIVREFELSKEDGKV---KKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSASLD-------PPI 145

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2064663964  991 VVHCTAGVGRSGVVILCDILLFCLDHNVPVDLPR------VLTLV---RMQRMLSVQTLAQYKFVHQ 1048
Cdd:cd18533    146 IVHCSAGVGRTGTFIALDSLLDELKRGLSDSQDLedsedpVYEIVnqlRKQRMSMVQTLRQYIFLYD 212
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 779-1047 3.51e-55

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: 192.96  E-value: 3.51e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  779 QVFLEFENIAKRKPNADFSTALLLENIPRNRFSDVLPYEENRVRLT-PSADNRTGYINASHVSasvGDSQR-FYIAAQGP 856
Cdd:cd14543      4 GIYEEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPkRNGDERTDYINANFMD---GYKQKnAYIATQGP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  857 MQTTAKSFWQMVWENHVGVVVMLTDTeDDQGHEKCYQYWPqaNGEEAALSFGEYRVVRKSAVSSAVAVTTCLVLSRTQGV 936
Cdd:cd14543     81 LPKTYSDFWRMVWEQKVLVIVMTTRV-VERGRVKCGQYWP--LEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETD 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  937 SctHRNVWHLRYTDWPDHGTPGDVQGFLGFMEEVDSVRRLALNDQ----RLRTRNAPTVVHCTAGVGRSGVVILCDILLF 1012
Cdd:cd14543    158 E--SRQVTHFQFTSWPDFGVPSSAAALLDFLGEVRQQQALAVKAMgdrwKGHPPGPPIVVHCSAGIGRTGTFCTLDICLS 235

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 2064663964 1013 CLDHNVPVDLPRVLTLVRMQRMLSVQTLAQYKFVH 1047
Cdd:cd14543    236 QLEDVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 804-1056 9.04e-54

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: 188.06  E-value: 9.04e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  804 NIPRNRFSDVLPYEENRVRLTPSADNRTG--YINASHV-----SASVGDSQRFYIAAQGPMQTTAKSFWQMVWENHVGVV 876
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILKDRDPNVPGsdYINANYIrneneGPTTDENAKTYIATQGCLENTVSDFWSMVWQENSRVI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  877 VMLTdTEDDQGHEKCYQYWPQANGEEAalsFGEYRVVRKSAVSSAVAVTTCLVLSRTqGVSCTHRNVWHLRYTDWPDHGT 956
Cdd:cd14544     81 VMTT-KEVERGKNKCVRYWPDEGMQKQ---YGPYRVQNVSEHDTTDYTLRELQVSKL-DQGDPIREIWHYQYLSWPDHGV 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  957 PGDVQGFLGFMEEVDSvRRLALNDQrlrtrnAPTVVHCTAGVGRSGVVILCDILLFCLDHN---VPVDLPRVLTLVRMQR 1033
Cdd:cd14544    156 PSDPGGVLNFLEDVNQ-RQESLPHA------GPIVVHCSAGIGRTGTFIVIDMLLDQIKRKgldCDIDIQKTIQMVRSQR 228

                          250       260
                   ....*....|....*....|...
gi 2064663964 1034 MLSVQTLAQYKFVHQVLIRYLRN 1056
Cdd:cd14544    229 SGMVQTEAQYKFIYVAVAQYIET 251
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 833-1054 7.80e-52

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: 181.03  E-value: 7.80e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  833 YINASHVSASVGDSQRFYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTdTEDDQGHEKCYQYWPQANGEEAALSfGEYRV 912
Cdd:cd14538      1 YINASHIRIPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVT-QDVEGGKVKCHRYWPDSLNKPLICG-GRLEV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  913 VRKSAVSSAVAVTTCLVLSRTQgvSCTHRNVWHLRYTDWPDHGTPGDVQGFLGFMeevdsvrRLAlndqRLRTRNAPTVV 992
Cdd:cd14538     79 SLEKYQSLQDFVIRRISLRDKE--TGEVHHITHLNFTTWPDHGTPQSADPLLRFI-------RYM----RRIHNSGPIVV 145

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2064663964  993 HCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLAQYKFVHQVLIRYL 1054
Cdd:cd14538    146 HCSAGIGRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 809-1048 5.80e-49

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: 173.31  E-value: 5.80e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  809 RFSDVLPYEENRVRLTPSADNRTG-YINASHVSASvgDSQRFYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTDTEDdQG 887
Cdd:cd14548      1 RYTNILPYDHSRVKLIPINEEEGSdYINANYIPGY--NSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCME-KG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  888 HEKCYQYWPQangEEAALSFGEYRVVRKSAVSSAVAVTTCLVLSRTQgvscTHRNVWHLRYTDWPDHGTPGDVQGFLGFm 967
Cdd:cd14548     78 RVKCDHYWPF---DQDPVYYGDITVTMLSESVLPDWTIREFKLERGD----EVRSVRQFHFTAWPDHGVPEAPDSLLRF- 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  968 eeVDSVRrlalndQRLRTRNAPTVVHCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLAQYKFVH 1047
Cdd:cd14548    150 --VRLVR------DYIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLH 221


                   .
gi 2064663964 1048 Q 1048
Cdd:cd14548    222 Q 222
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 803-1054 1.60e-48

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: 173.28  E-value: 1.60e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  803 ENIPRNRFSDVLPYEENRVRLTPSADNRTG--YINAS------HVSASVGDSQRFYIAAQGPMQTTAKSFWQMVWENHVG 874
Cdd:cd14605      1 ENKNKNRYKNILPFDHTRVVLHDGDPNEPVsdYINANiimpefETKCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  875 VVVMlTDTEDDQGHEKCYQYWPqangEEAALSfgEYRVVRKSAVSSAVA---VTTCLVLSRTqGVSCTHRNVWHLRYTDW 951
Cdd:cd14605     81 VIVM-TTKEVERGKSKCVKYWP----DEYALK--EYGVMRVRNVKESAAhdyILRELKLSKV-GQGNTERTVWQYHFRTW 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  952 PDHGTPGDVQGFLGFMEEVDsvrrlalNDQRLRTRNAPTVVHCTAGVGRSGVVILCDILLFCLDH---NVPVDLPRVLTL 1028
Cdd:cd14605    153 PDHGVPSDPGGVLDFLEEVH-------HKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREkgvDCDIDVPKTIQM 225

                          250       260
                   ....*....|....*....|....*.
gi 2064663964 1029 VRMQRMLSVQTLAQYKFVHQVLIRYL 1054
Cdd:cd14605    226 VRSQRSGMVQTEAQYRFIYMAVQHYI 251
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 803-1054 1.31e-47

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: 171.22  E-value: 1.31e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  803 ENIPRNRFSDVLPYEENRVRLTPSADNRTG--YINASHVSASV---GDSQRFYIAAQGPMQTTAKSFWQMVWENHVGVVV 877
Cdd:cd14606     17 ENKSKNRYKNILPFDHSRVILQGRDSNIPGsdYINANYVKNQLlgpDENAKTYIASQGCLEATVNDFWQMAWQENSRVIV 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  878 MlTDTEDDQGHEKCYQYWPQANGEEAalsFGEYRVV---RKSAVSSAVAVTTCLVLSRTQGVscthRNVWHLRYTDWPDH 954
Cdd:cd14606     97 M-TTREVEKGRNKCVPYWPEVGMQRA---YGPYSVTncgEHDTTEYKLRTLQVSPLDNGELI----REIWHYQYLSWPDH 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  955 GTPGDVQGFLGFMEEVDSVrrlalndQRLRTRNAPTVVHCTAGVGRSGVVILCDILLFCLDH---NVPVDLPRVLTLVRM 1031
Cdd:cd14606    169 GVPSEPGGVLSFLDQINQR-------QESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTkglDCDIDIQKTIQMVRA 241

                          250       260
                   ....*....|....*....|...
gi 2064663964 1032 QRMLSVQTLAQYKFVHQVLIRYL 1054
Cdd:cd14606    242 QRSGMVQTEAQYKFIYVAIAQFI 264
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 808-1048 3.58e-47

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: 168.34  E-value: 3.58e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  808 NRFSDVLPYEENRVRLTP-SADNRTGYINASHVSASVGDSQRfYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTDTEddQ 886
Cdd:cd14547      1 NRYKTILPNEHSRVCLPSvDDDPLSSYINANYIRGYDGEEKA-YIATQGPLPNTVADFWRMVWQEKTPIIVMITNLT--E 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  887 GHEKCYQYWPQANGEEaalsFGEYRVvrksAVSSavaVTTC-------LVLSRTQGVscthRNVWHLRYTDWPDHGTPGD 959
Cdd:cd14547     78 AKEKCAQYWPEEENET----YGDFEV----TVQS---VKETdgytvrkLTLKYGGEK----RYLKHYWYTSWPDHKTPEA 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  960 VQGFLGFMEEVDSVRRLAlndqrlrTRNAPTVVHCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQT 1039
Cdd:cd14547    143 AQPLLSLVQEVEEARQTE-------PHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQT 215


                   ....*....
gi 2064663964 1040 LAQYKFVHQ 1048
Cdd:cd14547    216 AEQYEFVHR 224
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 804-1051 3.62e-47

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: 168.73  E-value: 3.62e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  804 NIPRNRFSDVLPYEENRVRLTPsADNRTG--YINASHVSASvgDSQRFYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTD 881
Cdd:cd14553      3 NKPKNRYANVIAYDHSRVILQP-IEGVPGsdYINANYCDGY--RKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  882 TEDdQGHEKCYQYWPQANGEeaalSFGEYRVVRKSAVSSAVAVTTCLVLSRTqGVScTHRNVWHLRYTDWPDHGTPGDVQ 961
Cdd:cd14553     80 LEE-RSRVKCDQYWPTRGTE----TYGLIQVTLLDTVELATYTVRTFALHKN-GSS-EKREVRQFQFTAWPDHGVPEHPT 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  962 GFLGFMeevdsvrrlalndQRLRTRN----APTVVHCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSV 1037
Cdd:cd14553    153 PFLAFL-------------RRVKACNppdaGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMV 219

                          250
                   ....*....|....
gi 2064663964 1038 QTLAQYKFVHQVLI 1051
Cdd:cd14553    220 QTEDQYIFIHDALL 233
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 803-1048 4.59e-47

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: 169.62  E-value: 4.59e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  803 ENIPRNRFSDVLPYEENRVRLTPSADN-RTGYINASHVSASvgDSQRFYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTd 881
Cdd:cd14603     29 ENVKKNRYKDILPYDQTRVILSLLQEEgHSDYINANFIKGV--DGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMAC- 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  882 TEDDQGHEKCYQYWPQangEEAALSFGEYRV--VRKSAVSSAVAVTTCLVlsRTQGVScthRNVWHLRYTDWPDHGTPGD 959
Cdd:cd14603    106 REIEMGKKKCERYWAQ---EQEPLQTGPFTItlVKEKRLNEEVILRTLKV--TFQKES---RSVSHFQYMAWPDHGIPDS 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  960 VQGFLGFMEEvdsVRRLALNDQrlrtrnAPTVVHCTAGVGRSGVVILCD-ILLFCLDHNVPVD---LPRVLTLvRMQRML 1035
Cdd:cd14603    178 PDCMLAMIEL---ARRLQGSGP------EPLCVHCSAGCGRTGVICTVDyVRQLLLTQRIPPDfsiFDVVLEM-RKQRPA 247

                          250
                   ....*....|...
gi 2064663964 1036 SVQTLAQYKFVHQ 1048
Cdd:cd14603    248 AVQTEEQYEFLYH 260
FERM_F1_PTPN14_like cd17099
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 18-102 2.95e-46

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein phosphatase non-receptors PTPN14, PTPN21, and similar proteins; This family includes tyrosine-protein phosphatase non-receptors PTPN14 and PTPN21, both of which are protein-tyrosine phosphatase (PTP). They belong to the FERM family of PTPs characterized by a conserved N-terminal FERM domain and a C-terminal PTP catalytic domain with an intervening sequence containing an acidic region and a putative SH3 domain-binding sequence. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). PTPN14 plays a role in the nucleus during cell proliferation. PTPN21 interacts with a Tec tyrosine kinase family member, the epithelial and endothelial tyrosine kinase (Etk, also known as Bmx), modulates Stat3 activation, and plays a role in the regulation of cell growth and differentiation.


Pssm-ID: 340619  Cd Length: 85  Bit Score: 160.09  E-value: 2.95e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964   18 KSLCVIAVKLLENSTVECIVSSRTVGKECLQNVCQRLQILQPEYFGLRYPSKDGVLRWVDLDRPLKKQLDKYARECCLYL 97
Cdd:cd17099      1 KNSFVVRIQLLDNTVLECTLSPESTGQDCLEYVAQRLELREIEYFGLRYVNKKGQLRWVDLEKPLKKQLDKHAHEPLLYF 80


                   ....*
gi 2064663964   98 GVMFY 102
Cdd:cd17099     81 GVMFY 85
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 803-1054 3.20e-46

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: 165.77  E-value: 3.20e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  803 ENIPRNRFSDVLPYEENRVRLtpsaDNRTGYINASHVSASVGDSQRFYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTDt 882
Cdd:cd14597      2 ENRKKNRYKNILPYDTTRVPL----GDEGGYINASFIKMPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQ- 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  883 EDDQGHEKCYQYWPQANGEEAALSFG-EYRVVRKSAVSSAVAVTTCLVLSRTQGVscthRNVWHLRYTDWPDHGTPGDVQ 961
Cdd:cd14597     77 EVEGGKIKCQRYWPEILGKTTMVDNRlQLTLVRMQQLKNFVIRVLELEDIQTREV----RHITHLNFTAWPDHDTPSQPE 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  962 GFLGFMEEVDSVRRLalndqrlrtrnAPTVVHCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLA 1041
Cdd:cd14597    153 QLLTFISYMRHIHKS-----------GPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTED 221

                          250
                   ....*....|...
gi 2064663964 1042 QYKFVHQVLIRYL 1054
Cdd:cd14597    222 QYIFCYQVILYVL 234
PHA02738 PHA02738
hypothetical protein; Provisional
 783-1054 2.13e-45

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 166.64  E-value: 2.13e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  783 EFENIAKRKPNADFSTALllENIPRNRFSDVLPYEENRVRLtPSADNRTGYINASHVSASvgDSQRFYIAAQGPMQTTAK 862
Cdd:PHA02738    30 EHQKVISEKVDGTFNAEK--KNRKLNRYLDAVCFDHSRVIL-PAERNRGDYINANYVDGF--EYKKKFICGQAPTRQTCY 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  863 SFWQMVWENHVGVVVMLTDTEDDqGHEKCYQYWpqANGEEAALSFGEYRVVRKSAVSSAVAVTTCLVLsrTQGVSCThRN 942
Cdd:PHA02738   105 DFYRMLWMEHVQIIVMLCKKKEN-GREKCFPYW--SDVEQGSIRFGKFKITTTQVETHPHYVKSTLLL--TDGTSAT-QT 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  943 VWHLRYTDWPDHGTPGDVQGFLGFMEEVDSVRR------LALNDQRLRTrnAPTVVHCTAGVGRSGVVILCDILLFCLDH 1016
Cdd:PHA02738   179 VTHFNFTAWPDHDVPKNTSEFLNFVLEVRQCQKelaqesLQIGHNRLQP--PPIVVHCNAGLGRTPCYCVVDISISRFDA 256

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 2064663964 1017 NVPVDLPRVLTLVRMQRMLSVQTLAQYKFVHQVLIRYL 1054
Cdd:PHA02738   257 CATVSIPSIVSSIRNQRYYSLFIPFQYFFCYRAVKRYV 294
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 833-1052 2.72e-44

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: 159.42  E-value: 2.72e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  833 YINASHVSASVGDS---QRfYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTdTEDDQGHEKCYQYWPQANGEEaalSFGE 909
Cdd:cd14541      2 YINANYVNMEIPGSgivNR-YIAAQGPLPNTCADFWQMVWEQKSTLIVMLT-TLVERGRVKCHQYWPDLGETM---QFGN 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  910 YRVVRKSAVSSAVAVTTCLVLSRTQgvSCTHRNVWHLRYTDWPDHGTPGDVQGFLGFmeeVDSVRRLALndqrlrTRNAP 989
Cdd:cd14541     77 LQITCVSEEVTPSFAFREFILTNTN--TGEERHITQMQYLAWPDHGVPDDSSDFLDF---VKRVRQNRV------GMVEP 145

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2064663964  990 TVVHCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLAQYKFVHQVLIR 1052
Cdd:cd14541    146 TVVHCSAGIGRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAILR 208
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 808-1048 7.73e-44

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: 158.83  E-value: 7.73e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  808 NRFSDVLPYEENRVRLTPSADNRTGYINASHVSASvgDSQRFYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTDTeDDQG 887
Cdd:cd14615      1 NRYNNVLPYDISRVKLSVQSHSTDDYINANYMPGY--NSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKC-VEQG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  888 HEKCYQYWPqangEEAALSFGEYRVVRKSAVSSAVAVTTCLVLSRTQgvSCTHRNVWHLRYTDWPDHGTPGDVQGFLGFm 967
Cdd:cd14615     78 RTKCEEYWP----SKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQ--TNESRTVRHFHFTSWPDHGVPETTDLLINF- 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  968 eevdsvRRLALNDQRLRTRNAPTVVHCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLAQYKFVH 1047
Cdd:cd14615    151 ------RHLVREYMKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLN 224


                   .
gi 2064663964 1048 Q 1048
Cdd:cd14615    225 Q 225
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 807-1045 1.03e-43

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: 158.71  E-value: 1.03e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  807 RNRFSDVLPYEENRVRLTpSADNRTGYINASHVSASvgDSQRFYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTDTEdDQ 886
Cdd:cd14545      1 LNRYRDRDPYDHDRSRVK-LKQGDNDYINASLVEVE--EAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLM-EK 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  887 GHEKCYQYWPQANGEEAALSFGEYRVVRKSA-VSSAVAVTTCLVLSRTQGVScthRNVWHLRYTDWPDHGTPGDVQGFLG 965
Cdd:cd14545     77 GQIKCAQYWPQGEGNAMIFEDTGLKVTLLSEeDKSYYTVRTLELENLKTQET---REVLHFHYTTWPDFGVPESPAAFLN 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  966 FMEEvdsVRRLALndqrLRTRNAPTVVHCTAGVGRSGVVILCDILLFCLDHNVP--VDLPRVLTLVRMQRMLSVQTLAQY 1043
Cdd:cd14545    154 FLQK---VRESGS----LSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQL 226


                   ..
gi 2064663964 1044 KF 1045
Cdd:cd14545    227 RF 228
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 778-1054 1.07e-43

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 161.32  E-value: 1.07e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  778 GQVFLEFENIAKRKPNADFSTALLLENIPRNRFSDVLPYEENRVRLTPSADNRTGYINASHVSASVGDSQrfYIAAQGPM 857
Cdd:PHA02747    25 GIIRDEHHQIILKPFDGLIANFEKPENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGFEDDKK--FIATQGPF 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  858 QTTAKSFWQMVWENHVGVVVMLTDTEDDQGHEKCYQYWpqANGEEAALSFGEYRVvrkSAVSSAVAVTTCLVLSR-TQGV 936
Cdd:PHA02747   103 AETCADFWKAVWQEHCSIIVMLTPTKGTNGEEKCYQYW--CLNEDGNIDMEDFRI---ETLKTSVRAKYILTLIEiTDKI 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  937 SCTHRNVWHLRYTDWPDHGTPGDVQGFLGFMEEVDSVRRLALN-----DQRLrtrnAPTVVHCTAGVGRSGVVILCDILL 1011
Cdd:PHA02747   178 LKDSRKISHFQCSEWFEDETPSDHPDFIKFIKIIDINRKKSGKlfnpkDALL----CPIVVHCSDGVGKTGIFCAVDICL 253

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 2064663964 1012 FCLDHNVPVDLPRVLTLVRMQRMLSVQTLAQYKFV---HQVLIRYL 1054
Cdd:PHA02747   254 NQLVKRKAICLAKTAEKIREQRHAGIMNFDDYLFIqpgYEVLHYFL 299
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 780-1045 1.20e-43

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: 159.36  E-value: 1.20e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  780 VFLEFENiakRKPNADFSTALLLENIPRNRFSDVLPYEENRVRLTpSADNrtGYINASHVSasVGDSQRFYIAAQGPMQT 859
Cdd:cd14607      3 LYLEIRN---ESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQ-NTEN--DYINASLVV--IEEAQRSYILTQGPLPN 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  860 TAKSFWQMVWENHVGVVVMLTDTEdDQGHEKCYQYWPQAngEEAALSFGEYRVVRKSAVSSAVAVTTCLVLSRTQGVSCT 939
Cdd:cd14607     75 TCCHFWLMVWQQKTKAVVMLNRIV-EKDSVKCAQYWPTD--EEEVLSFKETGFSVKLLSEDVKSYYTVHLLQLENINSGE 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  940 HRNVWHLRYTDWPDHGTPGDVQGFLGFMEEVDSVRRLALNdqrlrtrNAPTVVHCTAGVGRSGVVILCDILLFCLDHNVP 1019
Cdd:cd14607    152 TRTISHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPE-------HGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDP 224

                          250       260
                   ....*....|....*....|....*...
gi 2064663964 1020 --VDLPRVLTLVRMQRMLSVQTLAQYKF 1045
Cdd:cd14607    225 dsVDIKQVLLDMRKYRMGLIQTPDQLRF 252
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 808-1054 1.45e-43

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: 158.13  E-value: 1.45e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  808 NRFSDVLPYEENRVRLTP-SADNRTGYINASHVSASvgDSQRFYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTDTEDDq 886
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKPiHEEPGSDYINANYMPGY--WSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEA- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  887 GHEKCYQYWPQangEEAALSFGEYRVVRKSA-VSSAVAVTTCLVLSRTQGVScthRNVWHLRYTDWPDHGTPGDVQGFLG 965
Cdd:cd14619     78 GRVKCEHYWPL---DYTPCTYGHLRVTVVSEeVMENWTVREFLLKQVEEQKT---LSVRHFHFTAWPDHGVPSSTDTLLA 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  966 FmeevdsvRRLALNDQRLRTRNAPTVVHCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLAQYKF 1045
Cdd:cd14619    152 F-------RRLLRQWLDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVF 224


                   ....*....
gi 2064663964 1046 VHQVLIRYL 1054
Cdd:cd14619    225 LHQCILDFL 233
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 833-1055 2.77e-43

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: 156.45  E-value: 2.77e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  833 YINASHVSASVGDSQRFYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTdTEDDQGHEKCYQYWPQANGEEAALSFGEYRV 912
Cdd:cd14596      1 YINASYITMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMT-REVERGKVKCHRYWPETLQEPMELENYQLRL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  913 VRKSAVSSavavTTCLVLSRTQGVSCTHRNVWHLRYTDWPDHGTPGDVQGFLGFMEEVDSVRRLalndqrlrtrnAPTVV 992
Cdd:cd14596     80 ENYQALQY----FIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNT-----------GPIVV 144

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2064663964  993 HCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLAQYKFVHQVLIRYLR 1055
Cdd:cd14596    145 HCSAGIGRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 808-1048 1.95e-42

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: 154.69  E-value: 1.95e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  808 NRFSDVLPYEENRVRLTPSADNR-TGYINASHVSASvgDSQRFYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTDTEDdQ 886
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNVDDDPcSDYINASYIPGN--NFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVE-K 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  887 GHEKCYQYWPQangEEAALSFGEYRVVRKS-AVSSAVAVTTCLVLSRTQgVSCtHRNVWHLRYTDWPDHGTPGDVQGFLG 965
Cdd:cd14617     78 GRVKCDHYWPA---DQDSLYYGDLIVQMLSeSVLPEWTIREFKICSEEQ-LDA-PRLVRHFHYTVWPDHGVPETTQSLIQ 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  966 FmeeVDSVRrlalnDQRLRTRNA-PTVVHCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLAQYK 1044
Cdd:cd14617    153 F---VRTVR-----DYINRTPGSgPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYV 224


                   ....
gi 2064663964 1045 FVHQ 1048
Cdd:cd14617    225 YLHQ 228
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 833-1051 2.22e-42

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: 153.98  E-value: 2.22e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  833 YINASHVSASvgDSQRFYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTDTEDdQGHEKCYQYWPQANGEEaalsFGEYRV 912
Cdd:cd17668      1 YINANYVDGY--NKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVE-KGRRKCDQYWPADGSEE----YGNFLV 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  913 VRKSAVSSAVAVTTCLVLSRT------QGVSCTHRNVWHLRYTDWPDHGTPGDVQGFLGFMEEVDSVRRLALNdqrlrtr 986
Cdd:cd17668     74 TQKSVQVLAYYTVRNFTLRNTkikkgsQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHAVG------- 146

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2064663964  987 naPTVVHCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLAQYKFVHQVLI 1051
Cdd:cd17668    147 --PVVVHCSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 804-1048 2.93e-42

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: 154.60  E-value: 2.93e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  804 NIPRNRFSDVLPYEENRVRLTP--SADNrTGYINASHVSASvgDSQRFYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTD 881
Cdd:cd14554      6 NKFKNRLVNILPYESTRVCLQPirGVEG-SDYINASFIDGY--RQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTK 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  882 TEdDQGHEKCYQYWPQANGEE---------AALSFGEYrVVRKSAVSSAvavttclvlsRTQGVscthRNVWHLRYTDWP 952
Cdd:cd14554     83 LR-EMGREKCHQYWPAERSARyqyfvvdpmAEYNMPQY-ILREFKVTDA----------RDGQS----RTVRQFQFTDWP 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  953 DHGTPGDVQGFLGFMEEVDsvrrlalNDQRLRTRNAPTVVHCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQ 1032
Cdd:cd14554    147 EQGVPKSGEGFIDFIGQVH-------KTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQ 219

                          250
                   ....*....|....*.
gi 2064663964 1033 RMLSVQTLAQYKFVHQ 1048
Cdd:cd14554    220 RPAMVQTEDQYQFCYR 235
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 833-1047 1.21e-41

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: 151.73  E-value: 1.21e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  833 YINASHVSASvgDSQRFYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTDTEdDQGHEKCYQYWPQANGEEaalsFGEYRV 912
Cdd:cd14549      1 YINANYVDGY--NKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLV-ERGRRKCDQYWPKEGTET----YGNIQV 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  913 VRKSAVSSAVAVTTCLVLSRTQGVSCTH----RNVWHLRYTDWPDHGTPGDVQGFLGFmeevdsVRRLALNDqrlRTRNA 988
Cdd:cd14549     74 TLLSTEVLATYTVRTFSLKNLKLKKVKGrsseRVVYQYHYTQWPDHGVPDYTLPVLSF------VRKSSAAN---PPGAG 144

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2064663964  989 PTVVHCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLAQYKFVH 1047
Cdd:cd14549    145 PIVVHCSAGVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 782-1054 1.35e-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: 154.51  E-value: 1.35e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  782 LEFENIAKRKPNAD-FSTALLLENIPRNRFSDVLPYEENRVRLTP-SADNRTGYINASHVSASvgDSQRFYIAAQGPMQT 859
Cdd:cd14627     30 LEFKRLANSKAHTSrFISANLPCNKFKNRLVNIMPYETTRVCLQPiRGVEGSDYINASFIDGY--RQQKAYIATQGPLAE 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  860 TAKSFWQMVWENHVGVVVMLTDTEDdQGHEKCYQYWPqanGEEAALSfgEYRVVRKSAvSSAVAVTTCLVLSRTQGVSCT 939
Cdd:cd14627    108 TTEDFWRMLWENNSTIVVMLTKLRE-MGREKCHQYWP---AERSARY--QYFVVDPMA-EYNMPQYILREFKVTDARDGQ 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  940 HRNVWHLRYTDWPDHGTPGDVQGFLGFMEEVDSVRRLALNDqrlrtrnAPTVVHCTAGVGRSGVVILCDILLFCLDHNVP 1019
Cdd:cd14627    181 SRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQD-------GPISVHCSAGVGRTGVFITLSIVLERMRYEGV 253

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 2064663964 1020 VDLPRVLTLVRMQRMLSVQTLAQYKFVHQVLIRYL 1054
Cdd:cd14627    254 VDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYL 288
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 808-1048 7.16e-41

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: 150.06  E-value: 7.16e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  808 NRFSDVLPYEENRVRLTPSADNR-TGYINASHVSASVGDSQrfYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTDTEDdQ 886
Cdd:cd14616      1 NRFPNIKPYNNNRVKLIADAGVPgSDYINASYISGYLCPNE--FIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFE-K 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  887 GHEKCYQYWPQANGEEAAlsFGEYrVVRKSAVSSAVAVTTCLVLSRTQGVSCTHRnvwHLRYTDWPDHGTPGDVQGFLGF 966
Cdd:cd14616     78 GRIRCHQYWPEDNKPVTV--FGDI-VITKLMEDVQIDWTIRDLKIERHGDYMMVR---QCNFTSWPEHGVPESSAPLIHF 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  967 MEEVDSVRRlalndqrlrTRNAPTVVHCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLAQYKFV 1046
Cdd:cd14616    152 VKLVRASRA---------HDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFL 222


                   ..
gi 2064663964 1047 HQ 1048
Cdd:cd14616    223 HQ 224
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 810-1051 7.92e-41

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: 150.09  E-value: 7.92e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  810 FSDVLPYEENRVRLTPSADNR-TGYINASHVSASVGDSQrfYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTDTEDDQgH 888
Cdd:cd14620      1 YPNILPYDHSRVILSQLDGIPcSDYINASYIDGYKEKNK--FIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERK-E 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  889 EKCYQYWPqangEEAALSFGEYRV-VRKSAVSSAVAVTTCLVLSRTQGVSCTHRNVWHLRYTDWPDHGTPGDVQGFLGFM 967
Cdd:cd14620     78 EKCYQYWP----DQGCWTYGNIRVaVEDCVVLVDYTIRKFCIQPQLPDGCKAPRLVTQLHFTSWPDFGVPFTPIGMLKFL 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  968 EEVDSVRRlalndqrlrTRNAPTVVHCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLAQYKFVH 1047
Cdd:cd14620    154 KKVKSVNP---------VHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIY 224


                   ....
gi 2064663964 1048 QVLI 1051
Cdd:cd14620    225 QALL 228
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 804-1053 8.28e-41

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: 150.76  E-value: 8.28e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  804 NIP----RNRFSDVLPYEENRV--RLTPSADNRTGYINASHVSASVGdSQRFYIAAQGPMQTTAKSFWQMVWENHVGVVV 877
Cdd:cd14612     11 DIPghasKDRYKTILPNPQSRVclRRAGSQEEEGSYINANYIRGYDG-KEKAYIATQGPMLNTVSDFWEMVWQEECPIIV 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  878 MLTDTEddQGHEKCYQYWPQANGeeaalSFGEYRVvRKSAVSSAVAVTTCLVLSRTQGVScthRNVWHLRYTDWPDHGTP 957
Cdd:cd14612     90 MITKLK--EKKEKCVHYWPEKEG-----TYGRFEI-RVQDMKECDGYTIRDLTIQLEEES---RSVKHYWFSSWPDHQTP 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  958 GDVQGFLGFMEEVDSVRRLAlndqrlrTRNAPTVVHCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSV 1037
Cdd:cd14612    159 ESAGPLLRLVAEVEESRQTA-------ASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMI 231

                          250
                   ....*....|....*.
gi 2064663964 1038 QTLAQYKFVHQVLIRY 1053
Cdd:cd14612    232 QTSEQYQFLHHTLALY 247
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 768-1051 8.97e-41

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: 151.73  E-value: 8.97e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  768 DSVLESRLEDGQVF-LEFENIakrKPNADFS--TALLLENIPRNRFSDVLPYEENRVRLTPsADNRTG--YINASHVSAS 842
Cdd:cd14626      5 DNIERLKANDGLKFsQEYESI---DPGQQFTweNSNLEVNKPKNRYANVIAYDHSRVILTS-VDGVPGsdYINANYIDGY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  843 vgDSQRFYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTDTEDdQGHEKCYQYWPqANGEEaalSFGEYRVVRKSAVSSAV 922
Cdd:cd14626     81 --RKQNAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEE-KSRVKCDQYWP-IRGTE---TYGMIQVTLLDTVELAT 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  923 AVTTCLVLSRTQgvSCTHRNVWHLRYTDWPDHGTPGDVQGFLGFMEEVDSVRRLalndqrlrtRNAPTVVHCTAGVGRSG 1002
Cdd:cd14626    154 YSVRTFALYKNG--SSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPP---------DAGPMVVHCSAGVGRTG 222

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 2064663964 1003 VVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLAQYKFVHQVLI 1051
Cdd:cd14626    223 CFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALL 271
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 783-1051 1.07e-40

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: 151.34  E-value: 1.07e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  783 EFENIakRKPNADFSTALLLENIP----RNRFSDVLPYEENRVRLTPSA---DNRTGYINASHVSASvgDSQRFYIAAQG 855
Cdd:cd17667      4 DFEEV--QRCTADMNITAEHSNHPdnkhKNRYINILAYDHSRVKLRPLPgkdSKHSDYINANYVDGY--NKAKAYIATQG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  856 PMQTTAKSFWQMVWENHVGVVVMLTDTEDdQGHEKCYQYWPQANGEEaalsFGEYRVVRKSAvssavAVTTCLVLSRTQG 935
Cdd:cd17667     80 PLKSTFEDFWRMIWEQNTGIIVMITNLVE-KGRRKCDQYWPTENSEE----YGNIIVTLKST-----KIHACYTVRRFSI 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  936 VSC--------------THRNVWHLRYTDWPDHGTPGDVQGFLGFMEEVDSVRRLALndqrlrtrnAPTVVHCTAGVGRS 1001
Cdd:cd17667    150 RNTkvkkgqkgnpkgrqNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARTPEM---------GPVLVHCSAGVGRT 220

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 2064663964 1002 GVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLAQYKFVHQVLI 1051
Cdd:cd17667    221 GTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALL 270
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 808-1051 1.38e-40

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: 149.71  E-value: 1.38e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  808 NRFSDVLPYEENRVRLTP-SADNRTGYINASHVSASvgDSQRFYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTDTEDDq 886
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQlGGEPHSDYINANFIPGY--TSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMEN- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  887 GHEKCYQYWPqanGEEAALSFGEYRVVRKSAVSSAVAVTTCLVLSrtQGVSCTHRNVWHLRYTDWPDHGTPGDVQGFLGF 966
Cdd:cd14618     78 GRVLCDHYWP---SESTPVSYGHITVHLLAQSSEDEWTRREFKLW--HEDLRKERRVKHLHYTAWPDHGIPESTSSLMAF 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  967 MEevdsvrrLALNDQRLRTRNAPTVVHCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLAQYKFV 1046
Cdd:cd14618    153 RE-------LVREHVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFL 225


                   ....*
gi 2064663964 1047 HQVLI 1051
Cdd:cd14618    226 HSCIL 230
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 782-1054 1.42e-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: 151.81  E-value: 1.42e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  782 LEFENIAKRKPNAD-FSTALLLENIPRNRFSDVLPYEENRVRLTP-SADNRTGYINASHVSASvgDSQRFYIAAQGPMQT 859
Cdd:cd14628     29 LEFKRLASSKAHTSrFISANLPCNKFKNRLVNIMPYESTRVCLQPiRGVEGSDYINASFIDGY--RQQKAYIATQGPLAE 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  860 TAKSFWQMVWENHVGVVVMLTDTEDdQGHEKCYQYWPqanGEEAALSfgEYRVVRKSAvSSAVAVTTCLVLSRTQGVSCT 939
Cdd:cd14628    107 TTEDFWRMLWEHNSTIVVMLTKLRE-MGREKCHQYWP---AERSARY--QYFVVDPMA-EYNMPQYILREFKVTDARDGQ 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  940 HRNVWHLRYTDWPDHGTPGDVQGFLGFMEEVDSVRRLALNDqrlrtrnAPTVVHCTAGVGRSGVVILCDILLFCLDHNVP 1019
Cdd:cd14628    180 SRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQD-------GPISVHCSAGVGRTGVFITLSIVLERMRYEGV 252

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 2064663964 1020 VDLPRVLTLVRMQRMLSVQTLAQYKFVHQVLIRYL 1054
Cdd:cd14628    253 VDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYL 287
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 790-1051 1.91e-40

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: 150.95  E-value: 1.91e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  790 RKPNADF--STALLLENIPRNRFSDVLPYEENRVRLTPSADNrtgYINASHVSasVGDSQRFYIAAQGPMQTTAKSFWQM 867
Cdd:cd14608      9 RHEASDFpcRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDND---YINASLIK--MEEAQRSYILTQGPLPNTCGHFWEM 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  868 VWENHVGVVVMLTDTEdDQGHEKCYQYWPQANGEEAALSFGEYRVVRKSAVSSAVAVTTCLVLSR--TQGVscthRNVWH 945
Cdd:cd14608     84 VWEQKSRGVVMLNRVM-EKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENltTQET----REILH 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  946 LRYTDWPDHGTPGDVQGFLGFMEEVDSvrrlalnDQRLRTRNAPTVVHCTAGVGRSGVVILCDILLFCLDHN---VPVDL 1022
Cdd:cd14608    159 FHYTTWPDFGVPESPASFLNFLFKVRE-------SGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRkdpSSVDI 231

                          250       260
                   ....*....|....*....|....*....
gi 2064663964 1023 PRVLTLVRMQRMLSVQTLAQYKFVHQVLI 1051
Cdd:cd14608    232 KKVLLEMRKFRMGLIQTADQLRFSYLAVI 260
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 833-1052 6.77e-40

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: 147.01  E-value: 6.77e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  833 YINASHVSASVGDSQ--RFYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTdTEDDQGHEKCYQYWPQANGEEaalSFGEY 910
Cdd:cd14601      2 YINANYINMEIPSSSiiNRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLT-TQVERGRVKCHQYWPEPSGSS---SYGGF 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  911 RVVRKSAVSSAVAVTTCLVLSRTQgvSCTHRNVWHLRYTDWPDHGTPGDVQGFLGFMEEVDSVRRlalndqrlrTRNAPT 990
Cdd:cd14601     78 QVTCHSEEGNPAYVFREMTLTNLE--KNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRA---------GKDEPV 146

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2064663964  991 VVHCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLAQYKFVHQVLIR 1052
Cdd:cd14601    147 VVHCSAGIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILK 208
FERM_C_PTPN14_PTPN21 cd13188
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 14 and 21 (PTPN14 and ...
 216-309 9.88e-40

FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 14 and 21 (PTPN14 and 21); This CD contains PTP members: pez/PTPN14 and PTPN21. A number of mutations in Pez have been shown to be associated with breast and colorectal cancer. The PTPN protein family belong to larger family of PTPs. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. The members are composed of a N-terminal FERM domain and a C-terminal PTP catalytic domain. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. Like most other ERM members they have a phosphoinositide-binding site in their FERM domain. The FERM C domain is the third structural domain within the FERM domain. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs) , the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270009  Cd Length: 91  Bit Score: 141.66  E-value: 9.88e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  216 YGEELFDVKDAAGNETVLGVSVEGVTARYNRGGTaneTASYRWSEIVDLIHHKKSFKIEGRENGRSAQFQLEDVPTAKYI 295
Cdd:cd13188      1 YGEESFPAKDEQGNEVLIGASLEGIFVKHDNGRP---PVFFRWEDIKNVINHKRTFSIECQNSEETVQFQFEDAETAKYV 77

                           90
                   ....*....|....
gi 2064663964  296 WKMCVQQHKFFMSM 309
Cdd:cd13188     78 WKLCVLQHKFYRQN 91
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
 22-221 1.71e-39

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 145.52  E-value: 1.71e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964    22 VIAVKLLENSTVECIVSSRTVGKECLQNVCQRLQILQPEYFGLRYPSKDGVLR-WVDLDRPLKKQLDKYArECCLYLGVM 100
Cdd:smart00295    1 VLKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLRhWLDPAKTLLDQDVKSE-PLTLYFRVK 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964   101 FYVFNVDRLHNDVTRY-YYFSHLKSDVIEGKLACTRDEAIQLASYSLQAEFGDHRPE-HHTSDYLKNFVLLPKSVAgGEE 178
Cdd:smart00295   80 FYPPDPNQLKEDPTRLnLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEElHDLRGELSLKRFLPKQLL-DSR 158

                           170       180       190       200
                    ....*....|....*....|....*....|....*....|...
gi 2064663964   179 NQEALLEQIIQAHRSLQGIHHSLAELYYIIAVQGLEGYGEELF 221
Cdd:smart00295  159 KLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 807-1053 5.56e-39

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: 145.78  E-value: 5.56e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  807 RNRFSDVLPYEENRVRLTPSA--DNRTGYINASHVSAsVGDSQRFYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTDTEd 884
Cdd:cd14613     28 KNRYKTILPNPHSRVCLTSPDqdDPLSSYINANYIRG-YGGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIE- 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  885 dQGHEKCYQYWPqangEEAALSFGEYRVVRKSAVSSAVAVTTCLVLSRTQgvsctHRNVWHLRYTDWPDHGTPGDVQGFL 964
Cdd:cd14613    106 -EMNEKCTEYWP----EEQVTYEGIEITVKQVIHADDYRLRLITLKSGGE-----ERGLKHYWYTSWPDQKTPDNAPPLL 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  965 GFMEEVDSVRrlalndQRLRTRNAPTVVHCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLAQYK 1044
Cdd:cd14613    176 QLVQEVEEAR------QQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQ 249


                   ....*....
gi 2064663964 1045 FVHQVLIRY 1053
Cdd:cd14613    250 FVHHVLSLY 258
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 807-1048 1.42e-38

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: 143.52  E-value: 1.42e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  807 RNRFSDVLPYEENRVRLTP--SADNRTGYINASHVSASVGdSQRFYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTDTED 884
Cdd:cd14611      2 KNRYKTILPNPHSRVCLKPknSNDSLSTYINANYIRGYGG-KEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  885 DqgHEKCYQYWPQANGeeaalSFGEYRVVrksaVSSAVAVTTCLV--LSRTQGVSCthRNVWHLRYTDWPDHGTPGDVQG 962
Cdd:cd14611     81 K--NEKCVLYWPEKRG-----IYGKVEVL----VNSVKECDNYTIrnLTLKQGSQS--RSVKHYWYTSWPDHKTPDSAQP 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  963 FLGFMEEVDSVRRLALNdqrlrtrNAPTVVHCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLAQ 1042
Cdd:cd14611    148 LLQLMLDVEEDRLASPG-------RGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQ 220


                   ....*.
gi 2064663964 1043 YKFVHQ 1048
Cdd:cd14611    221 YEFVHH 226
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 759-1051 1.77e-38

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: 145.26  E-value: 1.77e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  759 PPSPRDQRPDSVLESRLEDGQVF-LEFENIakrKPNADFS--TALLLENIPRNRFSDVLPYEENRVRLT-----PSADnr 830
Cdd:cd14624      2 PPIPILELADHIERLKANDNLKFsQEYESI---DPGQQFTweHSNLEVNKPKNRYANVIAYDHSRVLLSaiegiPGSD-- 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  831 tgYINASHVSASvgDSQRFYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTDTEDdQGHEKCYQYWPQANGEEAALsfgey 910
Cdd:cd14624     77 --YINANYIDGY--RKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEE-RSRVKCDQYWPSRGTETYGL----- 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  911 rvVRKSAVSSAVAVTTCL-VLSRTQGVSCTHRNVWHLRYTDWPDHGTPGDVQGFLGFMeevdsvrrlalndQRLRTRN-- 987
Cdd:cd14624    147 --IQVTLLDTVELATYCVrTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFL-------------RRVKTCNpp 211

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2064663964  988 --APTVVHCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLAQYKFVHQVLI 1051
Cdd:cd14624    212 daGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALL 277
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 833-1048 1.77e-38

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: 142.66  E-value: 1.77e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  833 YINASHVSASvgDSQRFYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTDTEDdQGHEKCYQYWPQAngEEAALSFGEYRV 912
Cdd:cd14557      1 YINASYIDGF--KEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEE-GNRNKCAQYWPSM--EEGSRAFGDVVV 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  913 -VRKSAVSSAVAVTTCLVLSRTQGVSctHRNVWHLRYTDWPDHGTPGDVQGFLGFMEEVDSVRRLAlndqrlrtrNAPTV 991
Cdd:cd14557     76 kINEEKICPDYIIRKLNINNKKEKGS--GREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFF---------SGPIV 144

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2064663964  992 VHCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLAQYKFVHQ 1048
Cdd:cd14557    145 VHCSAGVGRTGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 759-1051 1.81e-38

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: 145.24  E-value: 1.81e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  759 PPSPRDQRPDSVLESRLEDG-QVFLEFENIakrKPNADFS--TALLLENIPRNRFSDVLPYEENRVRLTP-SADNRTGYI 834
Cdd:cd14625      2 PPIPISELAEHTERLKANDNlKLSQEYESI---DPGQQFTweHSNLEVNKPKNRYANVIAYDHSRVILQPiEGIMGSDYI 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  835 NASHVSASvgDSQRFYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTDTEDdQGHEKCYQYWPQANGEEaalsfgeYRVVR 914
Cdd:cd14625     79 NANYIDGY--RKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEE-KSRIKCDQYWPSRGTET-------YGMIQ 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  915 KSAVSSAVAVTTCL-VLSRTQGVSCTHRNVWHLRYTDWPDHGTPGDVQGFLGFMeevdsvrrlalndQRLRTRN----AP 989
Cdd:cd14625    149 VTLLDTIELATFCVrTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFL-------------RRVKTCNppdaGP 215

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2064663964  990 TVVHCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLAQYKFVHQVLI 1051
Cdd:cd14625    216 IVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALL 277
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 797-1053 4.63e-38

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 145.56  E-value: 4.63e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  797 STALLLENIPRNRFSDVLPYEENRVRLTP--------------------SADNRTGYINASHVSASVGDSQrfYIAAQGP 856
Cdd:PHA02746    44 NHFLKKENLKKNRFHDIPCWDHSRVVINAheslkmfdvgdsdgkkievtSEDNAENYIHANFVDGFKEANK--FICAQGP 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  857 MQTTAKSFWQMVWENHVGVVVMLTDTEDDqgHEKCYQYWPQANGEEaaLSFGEYrVVRKSAVSSAVAVTTCLVLSrTQGV 936
Cdd:PHA02746   122 KEDTSEDFFKLISEHESQVIVSLTDIDDD--DEKCFELWTKEEDSE--LAFGRF-VAKILDIIEELSFTKTRLMI-TDKI 195

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  937 SCTHRNVWHLRYTDWPDHGTPGDVQGFLGFMEEVDSVR-RLALNDQRLRTRNAPTVVHCTAGVGRSGVVILCDILLFCLD 1015
Cdd:PHA02746   196 SDTSREIHHFWFPDWPDNGIPTGMAEFLELINKVNEEQaELIKQADNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLE 275

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 2064663964 1016 HNVPVDLPRVLTLVRMQRMLSVQTLAQYKFVHQVLiRY 1053
Cdd:PHA02746   276 KEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKAL-KY 312
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 807-1051 5.91e-38

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: 142.29  E-value: 5.91e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  807 RNRFSDVLPYEENRVRLT-PSADNRTGYINASHVSASVGdsQRFYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTdTEDD 885
Cdd:cd14602      1 KNRYKDILPYDHSRVELSlITSDEDSDYINANFIKGVYG--PRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMAC-MEFE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  886 QGHEKCYQYWpqANGEEAALSFGEYRVV-----RKSAVSSAVAVTTCLVLSRTqgvscthrnVWHLRYTDWPDHGTPGDV 960
Cdd:cd14602     78 MGKKKCERYW--AEPGEMQLEFGPFSVTceaekRKSDYIIRTLKVKFNSETRT---------IYQFHYKNWPDHDVPSSI 146

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  961 QGFLGFMEEvdsVRRLALNDqrlrtrNAPTVVHCTAGVGRSGVVILCDILLFCL-DHNVPVDLpRVLTLV---RMQRMLS 1036
Cdd:cd14602    147 DPILELIWD---VRCYQEDD------SVPICIHCSAGCGRTGVICAIDYTWMLLkDGIIPENF-SVFSLIqemRTQRPSL 216

                          250
                   ....*....|....*
gi 2064663964 1037 VQTLAQYKFVHQVLI 1051
Cdd:cd14602    217 VQTKEQYELVYNAVI 231
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 782-1054 2.34e-37

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: 142.17  E-value: 2.34e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  782 LEFENIAKRKPNAD-FSTALLLENIPRNRFSDVLPYEENRVRLTP-SADNRTGYINASHVSASvgDSQRFYIAAQGPMQT 859
Cdd:cd14629     30 LEFKLLANSKAHTSrFISANLPCNKFKNRLVNIMPYELTRVCLQPiRGVEGSDYINASFIDGY--RQQKAYIATQGPLAE 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  860 TAKSFWQMVWENHVGVVVMLTDTEDdQGHEKCYQYWPqanGEEAALSfgEYRVVRKSAvSSAVAVTTCLVLSRTQGVSCT 939
Cdd:cd14629    108 TTEDFWRMLWEHNSTIVVMLTKLRE-MGREKCHQYWP---AERSARY--QYFVVDPMA-EYNMPQYILREFKVTDARDGQ 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  940 HRNVWHLRYTDWPDHGTPGDVQGFLGFMEEVDSVRRLALNDqrlrtrnAPTVVHCTAGVGRSGVVILCDILLFCLDHNVP 1019
Cdd:cd14629    181 SRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVHKTKEQFGQD-------GPITVHCSAGVGRTGVFITLSIVLERMRYEGV 253

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 2064663964 1020 VDLPRVLTLVRMQRMLSVQTLAQYKFVHQVLIRYL 1054
Cdd:cd14629    254 VDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEYL 288
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 759-1053 3.79e-37

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: 142.08  E-value: 3.79e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  759 PPSPRDQRPDSVLESRLEDGQVFLEFENIAKRKP-NADFSTALLLENIPRNRFSDVLPYEENRVRLTP-SADNRTGYINA 836
Cdd:cd14621      6 PPLPVDKLEEEINRRMADDNKLFREEFNALPACPiQATCEAASKEENKEKNRYVNILPYDHSRVHLTPvEGVPDSDYINA 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  837 SHVSAsVGDSQRFyIAAQGPMQTTAKSFWQMVWENHVGVVVMLTDTEDDQgHEKCYQYWPqangEEAALSFGEYRVVRKS 916
Cdd:cd14621     86 SFING-YQEKNKF-IAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERK-ECKCAQYWP----DQGCWTYGNIRVSVED 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  917 AVSSAVAVTTCLVLSRTQGVSCT--HRNVWHLRYTDWPDHGTPGDVQGFLGFMEEVDsvrrlALNDQRLrtrnAPTVVHC 994
Cdd:cd14621    159 VTVLVDYTVRKFCIQQVGDVTNKkpQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVK-----NCNPQYA----GAIVVHC 229

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2064663964  995 TAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLAQYKFVHQVLIRY 1053
Cdd:cd14621    230 SAGVGRTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEH 288
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 803-1051 9.56e-37

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: 138.62  E-value: 9.56e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  803 ENIPRNRFSDVLPYEENRVRLTP-SADNRTGYINASHVSASvgDSQRFYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTD 881
Cdd:cd14630      2 ENRNKNRYGNIISYDHSRVRLQLlDGDPHSDYINANYIDGY--HRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTN 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  882 TEDdQGHEKCYQYWPqangeEAALSFGEYRVVRKSAVSSAVAVTTCLVLSRTQgvSCTHRNVWHLRYTDWPDHGTPGDVQ 961
Cdd:cd14630     80 LVE-VGRVKCVRYWP-----DDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKG--YHEIREIRQFHFTSWPDHGVPCYAT 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  962 GFLGFMEEVdsvrrlalndQRLRTRNA-PTVVHCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTL 1040
Cdd:cd14630    152 GLLGFVRQV----------KFLNPPDAgPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTE 221

                          250
                   ....*....|.
gi 2064663964 1041 AQYKFVHQVLI 1051
Cdd:cd14630    222 EQYVFVHDAIL 232
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 798-1048 1.40e-36

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: 138.48  E-value: 1.40e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  798 TALLLENIPRNRFSDVLPYEENRVRLTpSADNRTG--YINASHVSASvgDSQRFYIAAQGPMQTTAKSFWQMVWENHVGV 875
Cdd:cd14614      6 AADLPVNRCKNRYTNILPYDFSRVKLV-SMHEEEGsdYINANYIPGY--NSPQEYIATQGPLPETRNDFWKMVLQQKSQI 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  876 VVMLTDTeDDQGHEKCYQYWPQAngeEAALSFGEYRVVRKSAVSSAVAVTTCLVLSRTQGVSCthrnVWHLRYTDWPDHG 955
Cdd:cd14614     83 IVMLTQC-NEKRRVKCDHYWPFT---EEPVAYGDITVEMLSEEEQPDWAIREFRVSYADEVQD----VMHFNYTAWPDHG 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  956 TPgDVQGFLGFMEEVDSVRrlalndQRLRTRNAPTVVHCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRML 1035
Cdd:cd14614    155 VP-TANAAESILQFVQMVR------QQAVKSKGPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMS 227

                          250
                   ....*....|...
gi 2064663964 1036 SVQTLAQYKFVHQ 1048
Cdd:cd14614    228 MVQTEEQYIFIHQ 240
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 803-1050 7.55e-36

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: 138.14  E-value: 7.55e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  803 ENIPRNRFSDVLPYEENRVRLT---PSADnrTGYINASHVSASVGdsQRFYIAAQGPMQTTAKSFWQMVWENHVGVVVML 879
Cdd:cd14604     56 ENVKKNRYKDILPFDHSRVKLTlktSSQD--SDYINANFIKGVYG--PKAYIATQGPLANTVIDFWRMIWEYNVAIIVMA 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  880 TdTEDDQGHEKCYQYWPqaNGEEAALSFGEYRVvrksAVSSAVAVTTCLVLSRTQGVSCTHRNVWHLRYTDWPDHGTPgd 959
Cdd:cd14604    132 C-REFEMGRKKCERYWP--LYGEEPMTFGPFRI----SCEAEQARTDYFIRTLLLEFQNETRRLYQFHYVNWPDHDVP-- 202

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  960 vQGFLGFMEEVDSVRRLALNDqrlrtrNAPTVVHCTAGVGRSGVVILCDILLFCLDHN-VPVDLpRVLTLV---RMQRML 1035
Cdd:cd14604    203 -SSFDSILDMISLMRKYQEHE------DVPICIHCSAGCGRTGAICAIDYTWNLLKAGkIPEEF-NVFNLIqemRTQRHS 274

                          250
                   ....*....|....*
gi 2064663964 1036 SVQTLAQYKFVHQVL 1050
Cdd:cd14604    275 AVQTKEQYELVHRAI 289
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 833-1050 1.07e-35

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: 134.70  E-value: 1.07e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  833 YINASHVSasvGDSQR-FYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTDTEdDQGHEKCYQYWPqangEEAALSFGEYR 911
Cdd:cd14552      1 YINASFID---GYRQKdAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIK-ERSQNKCAQYWP----EDGSVSSGDIT 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  912 V-VRKSAVSSAVAVTTCLVlsrTQGVSCTHRNVWHLRYTDWPDHGTPGDVQGFLGFMEEVDSvrrlalndQRLRTRNAPT 990
Cdd:cd14552     73 VeLKDQTDYEDYTLRDFLV---TKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQK--------QQQQSGNHPI 141

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  991 VVHCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLAQYKFVHQVL 1050
Cdd:cd14552    142 TVHCSAGAGRTGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 833-1048 1.16e-35

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: 134.27  E-value: 1.16e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  833 YINASHVSASvgDSQRFYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTDTEDdQGHEKCYQYWPqangEEAALSFGEYRV 912
Cdd:cd14551      1 YINASYIDGY--QEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKE-RKEKKCSQYWP----DQGCWTYGNLRV 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  913 -VRKSAVSSAVAVTTCLVLSRTQGVSCTH-RNVWHLRYTDWPDHGTPGDVQGFLGFMEEVdsvrrLALNDQRLRtrnaPT 990
Cdd:cd14551     74 rVEDTVVLVDYTTRKFCIQKVNRGIGEKRvRLVTQFHFTSWPDFGVPFTPIGMLKFLKKV-----KSANPPRAG----PI 144

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2064663964  991 VVHCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLAQYKFVHQ 1048
Cdd:cd14551    145 VVHCSAGVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 791-1045 1.34e-35

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: 137.11  E-value: 1.34e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  791 KPNADFsTALLLENIPRNRFSDVLPYEENRVRLT-PSADNRTGYINASHVSASvgDSQR-FYIAAQGPMQTTAKSFWQMV 868
Cdd:cd14610     32 EPNATN-VAQREENVQKNRSLAVLPYDHSRIILKaENSHSHSDYINASPIMDH--DPRNpAYIATQGPLPATVADFWQMV 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  869 WENHVGVVVMLTDTEDDqGHEKCYQYWPQangEEAALsfgeYRVVRKSAVSSAVAVTTCLV----LSRTQgvSCTHRNVW 944
Cdd:cd14610    109 WESGCVVIVMLTPLAEN-GVKQCYHYWPD---EGSNL----YHIYEVNLVSEHIWCEDFLVrsfyLKNLQ--TNETRTVT 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  945 HLRYTDWPDHGTPGDVQGFLGFMEEVDSVrrlalndqrLRTRNAPTVVHCTAGVGRSGVVILCDILLFCLDHNVP-VDLP 1023
Cdd:cd14610    179 QFHFLSWNDQGVPASTRSLLDFRRKVNKC---------YRGRSCPIIVHCSDGAGRSGTYILIDMVLNKMAKGAKeIDIA 249

                          250       260
                   ....*....|....*....|..
gi 2064663964 1024 RVLTLVRMQRMLSVQTLAQYKF 1045
Cdd:cd14610    250 ATLEHLRDQRPGMVQTKEQFEF 271
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 799-1055 1.65e-35

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 137.44  E-value: 1.65e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  799 ALLLENIPRNRFSDVLPYEENRVRLtPSADNRTGYINASHVSASvgDSQRFYIAAQGPMQTTAKSFWQMVWENHVGVVVM 878
Cdd:PHA02742    47 SLELKNMKKCRYPDAPCFDRNRVIL-KIEDGGDDFINASYVDGH--NAKGRFICTQAPLEETALDFWQAIFQDQVRVIVM 123

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  879 LTDTEDDqGHEKCYQYWpqANGEEAALSFGEYRVVRKSAVS-SAVAVTTCLVLSRTQGVSCthrNVWHLRYTDWPDHGTP 957
Cdd:PHA02742   124 ITKIMED-GKEACYPYW--MPHERGKATHGEFKIKTKKIKSfRNYAVTNLCLTDTNTGASL---DIKHFAYEDWPHGGLP 197

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  958 GDVQGFLGFmeeVDSVRRLAL-----NDQRLRTRNAPTVVHCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQ 1032
Cdd:PHA02742   198 RDPNKFLDF---VLAVREADLkadvdIKGENIVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQ 274

                          250       260
                   ....*....|....*....|...
gi 2064663964 1033 RMLSVQTLAQYKFVHQVLIRYLR 1055
Cdd:PHA02742   275 RHNCLSLPQQYIFCYFIVLIFAK 297
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 809-1050 7.75e-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: 132.86  E-value: 7.75e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  809 RFSDVLPYEENRVRL-TPSADNRTGYINASHVSASvgDSQRFYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTDTEdDQG 887
Cdd:cd14623      1 RVLQIIPYEFNRVIIpVKRGEENTDYVNASFIDGY--RQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELE-ERG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  888 HEKCYQYWPQangeEAALSFGEYRV-VRKSAVSSAVAVTTCLVLSRTQGVScthRNVWHLRYTDWPDHGTPGDVQGFLGF 966
Cdd:cd14623     78 QEKCAQYWPS----DGSVSYGDITIeLKKEEECESYTVRDLLVTNTRENKS---RQIRQFHFHGWPEVGIPSDGKGMINI 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  967 MEevdsvrrlALNDQRLRTRNAPTVVHCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLAQYKFV 1046
Cdd:cd14623    151 IA--------AVQKQQQQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFC 222


                   ....
gi 2064663964 1047 HQVL 1050
Cdd:cd14623    223 YKVV 226
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 791-1045 7.92e-35

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: 134.78  E-value: 7.92e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  791 KPNAdFSTALLLENIPRNRFSDVLPYEENRVRLTPSAD-NRTGYINASHVsasVGDSQRF--YIAAQGPMQTTAKSFWQM 867
Cdd:cd14609     30 EPNT-CSTAQGEANVKKNRNPDFVPYDHARIKLKAESNpSRSDYINASPI---IEHDPRMpaYIATQGPLSHTIADFWQM 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  868 VWENHVGVVVMLTDTEDDqGHEKCYQYWPQangEEAALsfgeYRVVRKSAVSSAVAVTTCLVLS------RTQGVscthR 941
Cdd:cd14609    106 VWENGCTVIVMLTPLVED-GVKQCDRYWPD---EGSSL----YHIYEVNLVSEHIWCEDFLVRSfylknvQTQET----R 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  942 NVWHLRYTDWPDHGTPGDVQGFLGFMEEVDSVrrlalndqrLRTRNAPTVVHCTAGVGRSGVVILCDILLFCLDHNVP-V 1020
Cdd:cd14609    174 TLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKC---------YRGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGVKeI 244

                          250       260
                   ....*....|....*....|....*
gi 2064663964 1021 DLPRVLTLVRMQRMLSVQTLAQYKF 1045
Cdd:cd14609    245 DIAATLEHVRDQRPGMVRTKDQFEF 269
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 833-1048 2.87e-34

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: 130.58  E-value: 2.87e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  833 YINASHVSASVGDSQRFyIAAQGPMQTTAKSFWQMVWENHVGVVVMLTdTEDDQGHEKCYQYWPQANGeeAALSFGEYRV 912
Cdd:cd14539      1 YINASLIEDLTPYCPRF-IATQAPLPGTAADFWLMVYEQQVSVIVMLV-SEQENEKQKVHRYWPTERG--QALVYGAITV 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  913 VRKSAVSSAVAVTTCLVLS-RTQGVScthRNVWHLRYTDWPDHGTPGDVQGFLGFMEEVDSVRrlalndQRLRTRNAPTV 991
Cdd:cd14539     77 SLQSVRTTPTHVERIISIQhKDTRLS---RSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHY------LQQRSLQTPIV 147

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2064663964  992 VHCTAGVGRSGVvilcdillFCL----------DHNVPvDLPRVLTLVRMQRMLSVQTLAQYKFVHQ 1048
Cdd:cd14539    148 VHCSSGVGRTGA--------FCLlyaavqeieaGNGIP-DLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 833-1050 6.92e-34

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: 129.35  E-value: 6.92e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  833 YINASHVSasvGDSQR-FYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTDTEDDQgHEKCYQYWPQangeEAALSFGEYR 911
Cdd:cd14622      2 YINASFID---GYRQKdYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQERE-QEKCVQYWPS----EGSVTHGEIT 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  912 V-VRKSAVSSAVAVTTCLVLSRTQGVScthRNVWHLRYTDWPDHGTPGDVQGFLGFMEevdsvrrlALNDQRLRTRNAPT 990
Cdd:cd14622     74 IeIKNDTLLETISIRDFLVTYNQEKQT---RLVRQFHFHGWPEIGIPAEGKGMIDLIA--------AVQKQQQQTGNHPI 142

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  991 VVHCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLAQYKFVHQVL 1050
Cdd:cd14622    143 VVHCSAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 793-1051 2.59e-33

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: 130.16  E-value: 2.59e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  793 NADFSTALLLENIPRNRFSDVLPYEENRVRLTP-SADNRTGYINASHVSASvgDSQRFYIAAQGPMQTTAKSFWQMVWEN 871
Cdd:cd14633     29 SAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPiEGETSSDYINGNYIDGY--HRPNHYIATQGPMQETIYDFWRMVWHE 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  872 HVGVVVMLTDTEdDQGHEKCYQYWPqangEEAALSFGEYRVVRKSAVSSAVAVTTCLVLSRtqGVScTHRNVWHLRYTDW 951
Cdd:cd14633    107 NTASIIMVTNLV-EVGRVKCCKYWP----DDTEIYKDIKVTLIETELLAEYVIRTFAVEKR--GVH-EIREIRQFHFTGW 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  952 PDHGTPGDVQGFLGFMEEVDSvrrlalndqRLRTRNAPTVVHCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRM 1031
Cdd:cd14633    179 PDHGVPYHATGLLGFVRQVKS---------KSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVVDIYNCVRELRS 249

                          250       260
                   ....*....|....*....|
gi 2064663964 1032 QRMLSVQTLAQYKFVHQVLI 1051
Cdd:cd14633    250 RRVNMVQTEEQYVFIHDAIL 269
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 833-1048 2.62e-33

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: 127.54  E-value: 2.62e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  833 YINASHVSASVGDsqRFYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTDtEDDQGHEKCYQYWPQANGEEaaLSFGEYRV 912
Cdd:cd14542      1 YINANFIKGVSGS--KAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACR-EFEMGKKKCERYWPEEGEEQ--LQFGPFKI 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  913 --VRKSAVSSAVAVTTcLVLSRTQgvscTHRNVWHLRYTDWPDHGTPGDVQGFLgfmEEVDSVRRLALNDQrlrtrnAPT 990
Cdd:cd14542     76 slEKEKRVGPDFLIRT-LKVTFQK----ESRTVYQFHYTAWPDHGVPSSVDPIL---DLVRLVRDYQGSED------VPI 141

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2064663964  991 VVHCTAGVGRSGVviLCDI-----LLfcLDHNVPVDLpRVLTLV---RMQRMLSVQTLAQYKFVHQ 1048
Cdd:cd14542    142 CVHCSAGCGRTGT--ICAIdyvwnLL--KTGKIPEEF-SLFDLVremRKQRPAMVQTKEQYELVYR 202
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 833-1051 6.20e-33

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: 126.57  E-value: 6.20e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  833 YINASHVSASvgDSQRFYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTDTEDdQGHEKCYQYWPqangeEAALSFGEYRV 912
Cdd:cd14555      1 YINANYIDGY--HRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVE-VGRVKCSRYWP-----DDTEVYGDIKV 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  913 VRKSAVSSAVAVTTCLVLSRtQGVScTHRNVWHLRYTDWPDHGTPGDVQGFLGFmeevdsVRRLALNDQrlrTRNAPTVV 992
Cdd:cd14555     73 TLVETEPLAEYVVRTFALER-RGYH-EIREVRQFHFTGWPDHGVPYHATGLLGF------IRRVKASNP---PSAGPIVV 141

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2064663964  993 HCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLAQYKFVHQVLI 1051
Cdd:cd14555    142 HCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAIL 200
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 820-1051 1.18e-32

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: 126.29  E-value: 1.18e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  820 RVRLTPSADNRTG-YINASHVSASVGDSQrfYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTDTEDdQGHEKCYQYWPqa 898
Cdd:cd14631      1 RVILQPVEDDPSSdYINANYIDGYQRPSH--YIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVE-VGRVKCYKYWP-- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  899 ngEEAALsFGEYRVVRKSAVSSAVAVTTCLVLSRtQGVScTHRNVWHLRYTDWPDHGTPGDVQGFLGFmeevdsVRRLAL 978
Cdd:cd14631     76 --DDTEV-YGDFKVTCVEMEPLAEYVVRTFTLER-RGYN-EIREVKQFHFTGWPDHGVPYHATGLLSF------IRRVKL 144

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2064663964  979 NDQrlrTRNAPTVVHCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLAQYKFVHQVLI 1051
Cdd:cd14631    145 SNP---PSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAIL 214
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 833-1045 7.61e-32

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: 123.73  E-value: 7.61e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  833 YINASHVSASVGDSQRFYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTDTEDDQGHEKCYQYWPQANGEEAalSFGEYRV 912
Cdd:cd17658      1 YINASLVETPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTAKCADYFPAEENESR--EFGRISV 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  913 VRKSAVSSAVAVTTCLVLSRTQGVSCTHRNVWHLRYTDWPDHGTPGDVQgflgfmeevdSVRRLALNDQRLRTRNAPTVV 992
Cdd:cd17658     79 TNKKLKHSQHSITLRVLEVQYIESEEPPLSVLHIQYPEWPDHGVPKDTR----------SVRELLKRLYGIPPSAGPIVV 148

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2064663964  993 HCTAGVGRSGVvilcdillFCLDHNV----------PVDLPRVLTLVRMQRMLSVQTLAQYKF 1045
Cdd:cd17658    149 HCSAGIGRTGA--------YCTIHNTirrilegdmsAVDLSKTVRKFRSQRIGMVQTQDQYIF 203
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
802-1054 2.65e-31

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 124.43  E-value: 2.65e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  802 LENIPRNRFSDVLPYEENRVRltpsADNrtGYINASHVSasVGDSQRfYIAAQGPMQTTAKSFWQMVWENHVGVVVMLT- 880
Cdd:COG5599     40 INGSPLNRFRDIQPYKETALR----ANL--GYLNANYIQ--VIGNHR-YIATQYPLEEQLEDFFQMLFDNNTPVLVVLAs 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  881 DTEDDQGHEKCYQYWPQaNGEEAALSFgEYRVVRKSAVSSAVAVTTCLVlsRTQGVSCTHRNVWHLRYTDWPDHGTPGDV 960
Cdd:COG5599    111 DDEISKPKVKMPVYFRQ-DGEYGKYEV-SSELTESIQLRDGIEARTYVL--TIKGTGQKKIEIPVLHVKNWPDHGAISAE 186

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  961 QgflgFMEEVDSVRRLAlndQRLRTRNAPTVVHCTAGVGRSGVVILCDILLFCL--DHNVPVDLPRVLTLVRMQR---Ml 1035
Cdd:COG5599    187 A----LKNLADLIDKKE---KIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSInaLVQITLSVEEIVIDMRTSRnggM- 258

                          250
                   ....*....|....*....
gi 2064663964 1036 sVQTLAQYkfvhQVLIRYL 1054
Cdd:COG5599    259 -VQTSEQL----DVLVKLA 272
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
 105-221 3.54e-31

FERM central domain; This domain is the central structural domain of the FERM domain.


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 118.53  E-value: 3.54e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  105 NVDRLHNDVTRYYYFSHLKSDVIEGKLACTRDEAIQLASYSLQAEFGDHRPEHHTSDYLKNFVLLPKSVAgGEENQEALL 184
Cdd:pfam00373    2 LELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYLSLESFLPKQLL-RKMKSKELE 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2064663964  185 EQIIQAHRSLQGIHHSLAELYYIIAVQGLEGYGEELF 221
Cdd:pfam00373   81 KRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 833-1051 9.97e-31

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: 120.54  E-value: 9.97e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  833 YINASHVSASvgDSQRFYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTDTEdDQGHEKCYQYWPqangeEAALSFGEYRV 912
Cdd:cd14632      1 YINANYIDGY--HRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLV-EVGRVKCSKYWP-----DDSDTYGDIKI 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  913 VRKSAVSSAVAVTTCLVLSRtQGVSCTHRnVWHLRYTDWPDHGTPGDVQGFLGFMEEVDSVRRLalndqrlrtRNAPTVV 992
Cdd:cd14632     73 TLLKTETLAEYSVRTFALER-RGYSARHE-VKQFHFTSWPEHGVPYHATGLLAFIRRVKASTPP---------DAGPVVV 141

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2064663964  993 HCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLAQYKFVHQVLI 1051
Cdd:cd14632    142 HCSAGAGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAIL 200
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 833-1046 1.42e-30

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: 119.86  E-value: 1.42e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  833 YINASHVSASvGDSQRFYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTDTEDDqGHEKCYQYWPqangEEAALSFGEYRV 912
Cdd:cd14546      1 YINASTIYDH-DPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQEN-GVKQCARYWP----EEGSEVYHIYEV 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  913 vrkSAVSSAVAVTTCLVLS------RTQGVscthRNVWHLRYTDWPDHGTPGDVQGFLGFMEEVdsvrrlalnDQRLRTR 986
Cdd:cd14546     75 ---HLVSEHIWCDDYLVRSfylknlQTSET----RTVTQFHFLSWPDEGIPASAKPLLEFRRKV---------NKSYRGR 138

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2064663964  987 NAPTVVHCTAGVGRSGVVILCDILLFCLDHNV-PVDLPRVLTLVRMQRMLSVQTLAQYKFV 1046
Cdd:cd14546    139 SCPIVVHCSDGAGRTGTYILIDMVLNRMAKGAkEIDIAATLEHLRDQRPGMVKTKDQFEFV 199
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 833-1045 1.95e-30

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: 119.42  E-value: 1.95e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  833 YINASHVSASVGdsQRFYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTD-TEDDQghEKCYQYWPqangeEAALSFGEYR 911
Cdd:cd14558      1 YINASFIDGYWG--PKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTElKEGDQ--EQCAQYWG-----DEKKTYGDIE 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  912 VVRKSAVSSAVAVTTCLVLSRTQGVSCthRNVWHLRYTDWPDHGTPGDVQGFLGFMEevdSVRRLALNDQRLRTRNAPTV 991
Cdd:cd14558     72 VELKDTEKSPTYTVRVFEITHLKRKDS--RTVYQYQYHKWKGEELPEKPKDLVDMIK---SIKQKLPYKNSKHGRSVPIV 146

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2064663964  992 VHCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLAQYKF 1045
Cdd:cd14558    147 VHCSDGSSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQF 200
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 833-1048 6.76e-28

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: 112.12  E-value: 6.76e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  833 YINASHVSASvgDSQRFYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTDTedDQGHEKCYQYWPqangEEAALSFGEYRV 912
Cdd:cd14556      1 YINAALLDSY--KQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQL--DPKDQSCPQYWP----DEGSGTYGPIQV 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  913 VRKSAVSSAVAVTTCLVLSRTQGVSCTHRNVWHLRYTDWPDHG-TPGDVQGFLGFMEEVDSVRRlalndqrlRTRNAPTV 991
Cdd:cd14556     73 EFVSTTIDEDVISRIFRLQNTTRPQEGYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQE--------QSGEGPIV 144

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2064663964  992 VHCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLAQYKFVHQ 1048
Cdd:cd14556    145 VHCLNGVGRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
943-1051 3.23e-27

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 106.67  E-value: 3.23e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964   943 VWHLRYTDWPDHGTPGDVQGFLGFMEEVDSVrrlalndQRLRTRNAPTVVHCTAGVGRSGVVILCDILL-FCLDHNVPVD 1021
Cdd:smart00404    2 VKHYHYTGWPDHGVPESPDSILELLRAVKKN-------LNQSESSGPVVVHCSAGVGRTGTFVAIDILLqQLEAEAGEVD 74

                            90       100       110
                    ....*....|....*....|....*....|
gi 2064663964  1022 LPRVLTLVRMQRMLSVQTLAQYKFVHQVLI 1051
Cdd:smart00404   75 IFDTVKELRSQRPGMVQTEEQYLFLYRALL 104
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 943-1051 3.23e-27

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: 106.67  E-value: 3.23e-27
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964   943 VWHLRYTDWPDHGTPGDVQGFLGFMEEVDSVrrlalndQRLRTRNAPTVVHCTAGVGRSGVVILCDILL-FCLDHNVPVD 1021
Cdd:smart00012    2 VKHYHYTGWPDHGVPESPDSILELLRAVKKN-------LNQSESSGPVVVHCSAGVGRTGTFVAIDILLqQLEAEAGEVD 74

                            90       100       110
                    ....*....|....*....|....*....|
gi 2064663964  1022 LPRVLTLVRMQRMLSVQTLAQYKFVHQVLI 1051
Cdd:smart00012   75 IFDTVKELRSQRPGMVQTEEQYLFLYRALL 104
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
 114-213 2.55e-26

FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C/N, alpha-, and C-lobe/A-lobe, B-lobe, C-lobe/F1, F2, F3). The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases, the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the pleckstrin homology (PH) and phosphotyrosine binding (PTB) domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 271216  Cd Length: 99  Bit Score: 103.87  E-value: 2.55e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  114 TRYYYFSHLKSDVIEGKLACTRDEAIQLASYSLQAEFGDHRPEHHTSDYLKNFVLLPKSVAGGeENQEALLEQIIQAHRS 193
Cdd:cd14473      1 TRYLLYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKPKYLSLKRFLPKQLLKQ-RKPEEWEKRIVELHKK 79

                           90       100
                   ....*....|....*....|
gi 2064663964  194 LQGIHHSLAELYYIIAVQGL 213
Cdd:cd14473     80 LRGLSPAEAKLKYLKIARKL 99
FERM_F1_PTPN21 cd17192
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 18-103 5.01e-23

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein phosphatase non-receptor type 21 (PTPN21) and similar proteins; PTPN21, also termed protein-tyrosine phosphatase D1 (PTPD1), is a cytosolic non-receptor protein-tyrosine phosphatase (PTP) that belongs to the FERM family of PTPs characterized by a conserved N-terminal FERM domain and a C-terminal PTP catalytic domain with an intervening sequence containing an acidic region and a putative SH3 domain-binding sequence. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). PTPN21 interacts with a Tec tyrosine kinase family member, the epithelial and endothelial tyrosine kinase (Etk, also known as Bmx), modulates Stat3 activation, and plays a role in the regulation of cell growth and differentiation. It also associates with and activates Src tyrosine kinase, and directs epidermal growth factor (EGF)/Src signaling to the nucleus through activating ERK1/2- and Elk1-dependent gene transcription. PTPD1-Src complex interacts a protein kinase A-anchoring protein AKAP121 to forms a PTPD1-Src-AKAP121 complex, which is required for efficient maintenance of mitochondrial membrane potential and ATP oxidative synthesis. As a novel component of the endocytic pathway, PTPN21 supports EGF receptor stability and mitogenic signaling in bladder cancer cells. Moreover, PTPD1 regulates focal adhesion kinase (FAK) autophosphorylation and cell migration through modulating Src-FAK signaling at adhesion sites.


Pssm-ID: 340712  Cd Length: 87  Bit Score: 93.93  E-value: 5.01e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964   18 KSLCVIAVKLLENSTVECIVSSRTVGKECLQNVCQRLQILQPEYFGLRYPSKDGVLRWVDLDRPLKKQLDKYARECCLYL 97
Cdd:cd17192      1 KSCLVARIQLLNNEFVEFTLSVESTGQECLEAVAQRLELREITYFSLWYYNKQNQQRWVDLEKPLKKQLDKYALEPTVYF 80


                   ....*.
gi 2064663964   98 GVMFYV 103
Cdd:cd17192     81 GVVFYV 86
FERM_F1_PTPN14 cd17191
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 18-103 6.19e-22

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein phosphatase non-receptor type 14 (PTPN14) and similar proteins; PTPN14, also termed protein-tyrosine phosphatase pez, or PTPD2, or PTP36, is a widely expressed non-transmembrane cytosolic protein tyrosine phosphatase (PTP). It belongs to the FERM family of PTPs characterized by a conserved N-terminal FERM domain and a C-terminal PTP catalytic domain with an intervening sequence containing an acidic region and a putative SH3 domain-binding sequence. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). PTPN14 plays a role in the nucleus during cell proliferation. It forms a complex with Kibra and LATS1 proteins and negatively regulates the key Hippo pathway protein Yes-associated protein (YAP) oncogenic function by controlling its localization. It specifically regulates p130 Crk-associated substrate (p130Cas) phosphorylation at tyrosine residue 128 (Y128) in colorectal cancer (CRC) cells. Moreover, PTPN14 may be a critical enzyme in regulating endothelial cell function. It plays a crucial role in organogenesis by inducing transforming growth factor beta (TGFbeta) and epithelial-mesenchymal transition (EMT). It also acts as a modifier of angiogenesis and hereditary haemorrhagic telangiectasia. It regulates the lymphatic function and choanal development through the interaction with the vascular endothelial growth factor receptor 3 (VEGFR3), a receptor tyrosine kinase essential for lymphangiogenesis. Furthermore, PTPN14 functions as a regulator of cell motility through its action on cell-cell adhesion. Beta-Catenin, a central component of adherens junctions, has been identified as a PTPN14 substrate. PTPN14 works as a novel sperm-motility biomarker and a potential mitochondrial protein.


Pssm-ID: 340711  Cd Length: 87  Bit Score: 90.87  E-value: 6.19e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964   18 KSLCVIAVKLLENSTVECIVSSRTVGKECLQNVCQRLQILQPEYFGLRYPSKDGVLRWVDLDRPLKKQLDKYARECCLYL 97
Cdd:cd17191      1 KNCFVTRIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFLSKSQQARWVELEKPLKKQLDKFANEPLLFF 80


                   ....*.
gi 2064663964   98 GVMFYV 103
Cdd:cd17191     81 GVMFYV 86
FERM_F0_F1 cd01765
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain and F1 sub-domain, found ...
 22-101 1.93e-20

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain and F1 sub-domain, found in FERM (Four.1/Ezrin/Radixin/Moesin) family proteins; FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain is present at the N-terminus of a large and diverse group of proteins that mediate linkage of the cytoskeleton to the plasma membrane. FERM-containing proteins are ubiquitous components of the cytocortex and are involved in cell transport, cell structure and signaling functions. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N), which is structurally similar to ubiquitin.


Pssm-ID: 340464  Cd Length: 80  Bit Score: 86.49  E-value: 1.93e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964   22 VIAVKLLENSTVECIVSSRTVGKECLQNVCQRLQILQPEYFGLRYPSKDGVLRWVDLDRPLKKQLDKyARECCLYLGVMF 101
Cdd:cd01765      2 SCRVRLLDGTELTLEVSKKATGQELFDKVCEKLNLLEKDYFGLFYEDNDGQKHWLDLDKKISKQLKR-SGPYQFYFRVKF 80
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 838-1049 5.27e-19

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: 86.61  E-value: 5.27e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  838 HVSASVGDSQR---FYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTDTEDDQgheKCYQYWPqangEEAALSFGEYRVVR 914
Cdd:cd14634      1 YINAALMDSHKqpaAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEMDAAQ---LCMQYWP----EKTSCCYGPIQVEF 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  915 KSAVSSAVAVTTCLVLSRTQGVSCTHRNVWHLRYTDWPDH-GTPGDVQGFLGFmeevdsVRRLALNDQRLRTRNAPTVVH 993
Cdd:cd14634     74 VSADIDEDIISRIFRICNMARPQDGYRIVQHLQYIGWPAYrDTPPSKRSILKV------VRRLEKWQEQYDGREGRTVVH 147

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2064663964  994 CTAGVGRSGVVI-LCDILLFCLDHNVpVDLPRVLTLVRMQRMLSVQTLAQYKFVHQV 1049
Cdd:cd14634    148 CLNGGGRSGTFCaICSVCEMIQQQNI-IDVFHTVKTLRNNKSNMVETLEQYKFVYEV 203
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 833-1048 5.47e-19

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: 86.22  E-value: 5.47e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  833 YINASHVSASvgDSQRFYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTDTEDDqghEKCYQYWPqanGEEAALSFGEYRv 912
Cdd:cd14550      1 YINASYLQGY--RRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELN---EDEPIYWP---TKEKPLECETFK- 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  913 VRKSAVSSAVAVTTCLVLSRTQGVSCTHRN----VWHLRYTDWPDHGTPgdvqgFLGFMEEVDSVRRLAlndqrlRTRNA 988
Cdd:cd14550     72 VTLSGEDHSCLSNEIRLIVRDFILESTQDDyvleVRQFQCPSWPNPCSP-----IHTVFELINTVQEWA------QQRDG 140

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2064663964  989 PTVVH-----CTAGvgrsgvvilcdilLFC--------LDHNVPVDLPRVLTLVRMQRMLSVQTLAQYKFVHQ 1048
Cdd:cd14550    141 PIVVHdryggVQAA-------------TFCalttlhqqLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 816-1055 3.47e-17

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 83.48  E-value: 3.47e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  816 YEENRVRLTpsadNRTGYINASHVSASvgDSQRFYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTDTEDdqghEKCY-QY 894
Cdd:PHA02740    65 LLHRRIKLF----NDEKVLDARFVDGY--DFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHAD----KKCFnQF 134

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  895 WpqANGEEAALSFGEYRVVRKSAVSSAVAVTTCLVLSRTQGvscTHRNVWHLRYTDWPDHGTPGDVQGFLGFMEEVDSVr 974
Cdd:PHA02740   135 W--SLKEGCVITSDKFQIETLEIIIKPHFNLTLLSLTDKFG---QAQKISHFQYTAWPADGFSHDPDAFIDFFCNIDDL- 208

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  975 RLALNDQRLRTRNAPTVVHCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLAQYKFVHQVLIRYL 1054
Cdd:PHA02740   209 CADLEKHKADGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAYL 288


                   .
gi 2064663964 1055 R 1055
Cdd:PHA02740   289 K 289
FERM_N pfam09379
FERM N-terminal domain; This domain is the N-terminal ubiquitin-like structural domain of the ...
 25-87 4.62e-16

FERM N-terminal domain; This domain is the N-terminal ubiquitin-like structural domain of the FERM domain.


Pssm-ID: 430570  Cd Length: 63  Bit Score: 73.39  E-value: 4.62e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2064663964   25 VKLLENSTVECIVSSRTVGKECLQNVCQRLQILQPEYFGLRYPSKDGVLRWVDLDRPLKKQLD 87
Cdd:pfam09379    1 VRLLDGTVLEFDVQPKATGQVLLDQVCNHLNLKEKDYFGLQFLDDNGEHRWLDLSKRLSKQAP 63
FERM_C pfam09380
FERM C-terminal PH-like domain;
225-310 6.71e-16

FERM C-terminal PH-like domain;


Pssm-ID: 462779 [Multi-domain]  Cd Length: 85  Bit Score: 73.83  E-value: 6.71e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  225 DAAGNETVLGVSVEGVTARYNRGGTANetaSYRWSEIVDLIHHKKSFKIEGREN--GRSAQFQLEDVPTAKYIWKMCVQQ 302
Cdd:pfam09380    1 DKEGTDLWLGVSAKGILVYEDNNKILN---LFPWREIRKISFKRKKFLIKLRDKssEETLGFYTESSRACKYLWKLCVEQ 77


                   ....*...
gi 2064663964  303 HKFFMSMQ 310
Cdd:pfam09380   78 HTFFRLRR 85
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 838-1049 1.02e-15

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: 76.99  E-value: 1.02e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  838 HVSASVGDSQR---FYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTDTEDDQGhekCYQYWPqangEEAALSFGEYRVvr 914
Cdd:cd14636      1 YINAALMDSYRqpaAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVDLAQG---CPQYWP----EEGMLRYGPIQV-- 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  915 kSAVSSAVavtTCLVLSRTQGVSCTHRN------VWHLRYTDWPDH-GTPGDVQGFLGFMEEVDSVRrlalndQRLRTRN 987
Cdd:cd14636     72 -ECMSCSM---DCDVISRIFRICNLTRPqegylmVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQ------EECDEGE 141

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2064663964  988 APTVVHCTAGVGRSGVviLCDILLFC--LDHNVPVDLPRVLTLVRMQRMLSVQTLAQYKFVHQV 1049
Cdd:cd14636    142 GRTIIHCLNGGGRSGM--FCAISIVCemIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDV 203
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 833-1051 2.92e-15

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: 75.88  E-value: 2.92e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  833 YINASHVSASVGDSQrfYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTDTEDDQgheKCYQYWPqangEEAALSFGEYRV 912
Cdd:cd14635      1 YINAALMDSYKQPSA--FIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQ---LCPQYWP----ENGVHRHGPIQV 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  913 VRKSAVSSAVAVTTCLVLSRTQGVSCTHRNVWHLRYTDWPDH-GTPGDVQGFLGFMEEVDSVRrlalndQRLRTRNAPTV 991
Cdd:cd14635     72 EFVSADLEEDIISRIFRIYNAARPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQ------EEYNGGEGRTV 145

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  992 VHCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLAQYKFVHQVLI 1051
Cdd:cd14635    146 VHCLNGGGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVAL 205
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 833-1051 7.71e-15

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: 74.56  E-value: 7.71e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  833 YINAShVSASVGDSQRFYIAAQgPMQTTAKSFWQMVWENHVGVVVMLTDTEDDQGHEKCYQYWPQANGEEAALSFGEYrv 912
Cdd:cd14637      1 YINAA-LTDSYTRSAAFIVTLH-PLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAWPCLQYWPEPGLQQYGPMEVEF-- 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  913 vrksaVSSAVAVTTCLVLSRTQGVSCT---HRNVWHLRYTDW-PDHGTPGDVQGFLGFMEEVDSVRRlalndqrlRTRNA 988
Cdd:cd14637     77 -----VSGSADEDIVTRLFRVQNITRLqegHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQR--------ESGEG 143

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2064663964  989 PTVVHCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLAQYKFVHQVLI 1051
Cdd:cd14637    144 RTVVHCLNGGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIAL 206
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 833-1051 1.03e-12

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: 68.17  E-value: 1.03e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  833 YINASHVSASVGDSQrfYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTdteDDQG-HEKCYQYWPQangEEAALSFGEYR 911
Cdd:cd17670      1 YINASYIMGYYRSNE--FIITQHPLPHTTKDFWRMIWDHNAQIIVMLP---DNQGlAEDEFVYWPS---REESMNCEAFT 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  912 VV-----RKSAVSSAVAVTTCLVLSRTQGVSCTHrnVWHLRYTDWPDHGTPgdvqgFLGFMEEVDSVRRLALndqrlrTR 986
Cdd:cd17670     73 VTliskdRLCLSNEEQIIIHDFILEATQDDYVLE--VRHFQCPKWPNPDAP-----ISSTFELINVIKEEAL------TR 139

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2064663964  987 NAPTVVHCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLAQYKFVHQVLI 1051
Cdd:cd17670    140 DGPTIVHDEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
FERM_F1_FARP1_like cd17098
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, RhoGEF and ...
 23-102 6.85e-12

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, RhoGEF and pleckstrin domain-containing protein 1 (FARP1) and similar proteins; This family includes the F1 sub-domain of FERM, RhoGEF and pleckstrin domain-containing proteins FARP1, FARP2, and FERM domain-containing protein 7 (FRMD7). FARP1, also termed chondrocyte-derived ezrin-like protein (CDEP), or pleckstrin homology (PH) domain-containing family C member 2 (PLEKHC2), is a neuronal activator of the RhoA GTPase. It promotes outgrowth of developing motor neuron dendrites. It also regulates excitatory synapse formation and morphology, as well as activates the GTPase Rac1 to promote F-actin assembly. FARP2, also termed FERM domain including RhoGEF (FIR), or Pleckstrin homology (PH) domain-containing family C member 3, is a Dbl-family guanine nucleotide exchange factor (GEF) that activates Rac1 or Cdc42 in response to upstream signals, suggesting roles in regulating processes such as neuronal axon guidance and bone homeostasis. It is also a key molecule involved in the response of neuronal growth cones to class-3 semaphorins. FRMD7 plays an important role in neuronal development and is involved in the regulation of F-actin, neurofilament, and microtubule dynamics. All family members contain a FERM domain that is made up of three sub-domains, F1, F2, and F3. This family corresponds to F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340618  Cd Length: 85  Bit Score: 62.23  E-value: 6.85e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964   23 IAVKLLENSTVECIVSSRTVGKECLQNVCQRLQILQPEYFGLRYPSKDGVLRWVDLDRPLKKQLdKYARECCLYLGVMFY 102
Cdd:cd17098      3 VKVQMLDDTVHIFQVQQKALGEVLFDQVCKHLNLLESDYFGLEFTDPEGNKCWLDPEKPILRQV-KRPKDVVFKFVVKFY 81
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 833-1051 2.41e-10

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: 61.16  E-value: 2.41e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  833 YINASHVSASVGDSQrfYIAAQGPMQTTAKSFWQMVWENHVGVVVMLTDTEDDQGHEkcYQYWPQANGEEAALSFGEYRV 912
Cdd:cd17669      1 YINASYIMGYYQSNE--FIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDE--FVYWPNKDEPINCETFKVTLI 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  913 VRKSAVSSAVA--VTTCLVLSRTQGVSCTHrnVWHLRYTDWPDHGTPgdvqgFLGFMEEVDSVRRLALNdqrlrtRNAPT 990
Cdd:cd17669     77 AEEHKCLSNEEklIIQDFILEATQDDYVLE--VRHFQCPKWPNPDSP-----ISKTFELISIIKEEAAN------RDGPM 143

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2064663964  991 VVHCTAGVGRSGVVILCDILLFCLDHNVPVDLPRVLTLVRMQRMLSVQTLAQYKFVHQVLI 1051
Cdd:cd17669    144 IVHDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
FERM_C_PTPN4_PTPN3_like cd13189
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 3 and 4 (PTPN4 and ...
 216-306 3.19e-10

FERM domain C-lobe of Protein tyrosine phosphatase non-receptor proteins 3 and 4 (PTPN4 and PTPN3); PTPN4 (also called PTPMEG, protein tyrosine phosphatase, megakaryocyte) is a cytoplasmic protein-tyrosine phosphatase (PTP) thought to play a role in cerebellar function. PTPMEG-knockout mice have impaired memory formation and cerebellar long-term depression. PTPN3/PTPH1 is a membrane-associated PTP that is implicated in regulating tyrosine phosphorylation of growth factor receptors, p97 VCP (valosin-containing protein, or Cdc48 in Saccharomyces cerevisiae), and HBV (Hepatitis B Virus) gene expression; it is mutated in a subset of colon cancers. PTPMEG and PTPN3/PTPH1 contains a N-terminal FERM domain, a middle PDZ domain, and a C-terminal phosphatase domain. PTP1/Tyrosine-protein phosphatase 1 from nematodes and a FERM_C repeat 1 from Tetraodon nigroviridis are also included in this cd. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs) , the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270010  Cd Length: 95  Bit Score: 57.71  E-value: 3.19e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  216 YGEELFDVKDAAGNETVLGVSVEGVTArYNRGGTANEtasYRWSEIVDLIHHKKSFKIEGR-ENGRSAQ----FQLEDVP 290
Cdd:cd13189      2 YGVELHSARDSNNLELQIGVSSAGILV-FQNGIRINT---FPWSKIVKISFKRKQFFIQLRrEPNESRDtilgFNMLSYR 77

                           90
                   ....*....|....*.
gi 2064663964  291 TAKYIWKMCVQQHKFF 306
Cdd:cd13189     78 ACKNLWKSCVEHHTFF 93
FERM_F1_MYLIP cd17104
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in E3 ...
 20-87 3.84e-10

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in E3 ubiquitin-protein ligase MYLIP and similar proteins; MYLIP, also termed inducible degrader of the LDL-receptor (Idol), or myosin regulatory light chain interacting protein (MIR), is an E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of myosin regulatory light chain (MRLC), LDLR, VLDLR and LRP8. Its activity depends on E2 ubiquitin-conjugating enzymes of the UBE2D family, including UBE2D1, UBE2D2, UBE2D3, and UBE2D4. MYLIP stimulates clathrin-independent endocytosis and acts as a sterol-dependent inhibitor of cellular cholesterol uptake by binding directly to the cytoplasmic tail of the LDLR and promoting its ubiquitination via the UBE2D1/E1 complex. The ubiquitinated LDLR then enters the multivesicular body (MVB) protein-sorting pathway and is shuttled to the lysosome for degradation. Moreover, MYLIP has been identified as a novel ERM-like protein that affects cytoskeleton interactions regulating cell motility, such as neurite outgrowth. The ERM proteins includes ezrin, radixin, and moesin, which are cytoskeletal effector proteins linking actin to membrane-bound proteins at the cell surface. MYLIP contains a FERM-domain and a C-terminal C3HC4-type RING-HC finger. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340624  Cd Length: 81  Bit Score: 57.28  E-value: 3.84e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2064663964   20 LCViaVKLLENSTVECIVSSRTVGKECLQNVCQRLQILQPEYFGLRYPSKDGVLRWVDLDRPLKKQLD 87
Cdd:cd17104      2 LCL--VSQPDSVVIEVEVDPKANGQECLDKVCQKLGIIEKDYFGLQYTGPKGERLWLNLRNRISRQLP 67
FERM_F1_EPB41L4A cd17107
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte band ...
 26-103 1.50e-09

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte band 4.1-like protein 4A (EPB41L4A) and similar proteins; EPB41L4A, also termed protein NBL4, is a member of the band 4.1/Nbl4 (novel band 4.1-like protein 4) group of the FERM protein superfamily. It contains a FERM domain that is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). EPB41L4A is an important component of the beta-catenin/Tcf pathway. It may be related to determination of cell polarity or proliferation.


Pssm-ID: 340627  Cd Length: 91  Bit Score: 55.81  E-value: 1.50e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2064663964   26 KLLENSTVECIVSSRtvGKECLQNVCQRLQILQPEYFGLRYPSKDGVLRWVDLDRPLKKQLDKYARECCLYLGVMFYV 103
Cdd:cd17107     14 ELILTIQQDGIKSSK--GSVVLDVVFQHLNLLETDYFGLRYIDRQHQTHWLDPAKTLSEQLKLIGPPYTLYFGVKFYA 89
FERM_C_4_1_family cd13184
FERM domain C-lobe of Protein 4.1 family; The protein 4.1 family includes four well-defined ...
 216-306 1.52e-09

FERM domain C-lobe of Protein 4.1 family; The protein 4.1 family includes four well-defined members: erythroid protein 4.1 (4.1R), the best known and characterized member, 4.1G (general), 4.1N (neuronal), and 4.1 B (brain). The less well understood 4.1O/FRMD3 is not a true member of this family and is not included in this hierarchy. Besides three highly conserved domains, FERM, SAB (spectrin and actin binding domain) and CTD (C-terminal domain), the proteins from this family contain several unique domains: U1, U2 and U3. FERM domains like other members of the FERM domain superfamily have a cloverleaf architecture with three distinct lobes: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The brain is a particularly rich source of protein 4.1 isoforms. The various 4.1R, 4.1G, 4.1N, and 4.1B mRNAs are all expressed in distinct patterns within the brain. It is likely that 4.1 proteins play important functional roles in the brain including motor coordination and spatial learning, postmitotic differentiation, and synaptic architecture and function. In addition they are found in nonerythroid, nonneuronal cells where they may play a general structural role in nuclear architecture and/or may interact with splicing factors. The FERM C domain is the third structural domain within the FERM domain. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs) , the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270005  Cd Length: 94  Bit Score: 55.79  E-value: 1.52e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  216 YGEELFDVKDAAGNETVLGVSVEGV-----TARYNRggtanetasYRWSEIVDLIHHKKSFKIEGR-----ENGRSAQFQ 285
Cdd:cd13184      1 YGVDLHPAKDSEGVDIMLGVCSSGLlvyrdRLRINR---------FAWPKVLKISYKRNNFYIKIRpgefeQYETTIGFK 71

                           90       100
                   ....*....|....*....|.
gi 2064663964  286 LEDVPTAKYIWKMCVQQHKFF 306
Cdd:cd13184     72 LPNHRAAKRLWKVCVEHHTFF 92
FERM_F1_FRMD3 cd17102
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 25-102 1.66e-09

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM domain-containing protein 3 (FRMD3) and similar proteins; FRMD3, also termed band 4.1-like protein 4O, or ovary type protein 4.1 (4.1O), belongs to the 4.1 protein superfamily, which share the highly conserved membrane-association FERM domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). FRMD3 is involved in maintaining cell shape and integrity. It also functions as a tumour suppressor in non-small cell lung carcinoma (NSCLC). Some single nucleotide polymorphisms (SNPs) located in FRMD3 have been associated with diabetic kidney disease (DKD) in different ethnicities.


Pssm-ID: 340622  Cd Length: 82  Bit Score: 55.33  E-value: 1.66e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2064663964   25 VKLLENSTV-ECIVSSRTVGKECLQNVCQRLQILQPEYFGLRYPSKDGVLRWVDLDRPLKKQLdKYARECCLYLGVMFY 102
Cdd:cd17102      5 IRLLDDSEViCCEFKKDTKGQFLLDYVCNYLNLLEKDYFGLRYVDTEKQRHWLDPNKSIYKQL-KGVPPYVLCFRVKFY 82
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 834-1044 5.72e-09

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


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 57.79  E-value: 5.72e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  834 INASHVSasVGDSQRFyIAAQGPMQTTAKSFWQMVWENHVGVVVMLTdTEDDQGHEKCYQYWPQANgeeaalSFGEYRVV 913
Cdd:cd14559     18 LNANRVQ--IGNKNVA-IACQYPKNEQLEDHLKMLADNRTPCLVVLA-SNKDIQRKGLPPYFRQSG------TYGSVTVK 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  914 RKSAVSSAVAVTTCL---VLSRTQGVSCTHRNVWHLryTDWPDHGTPG--DVQGFLGFMEEVDSVRRLALNDQRLRTRNA 988
Cdd:cd14559     88 SKKTGKDELVDGLKAdmyNLKITDGNKTITIPVVHV--TNWPDHTAISseGLKELADLVNKSAEEKRNFYKSKGSSAIND 165

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2064663964  989 PT----VVHCTAGVGRSGVVILCDILlfcLDHNVPVDLPRVLTLVRMQR---MlsVQTLAQYK 1044
Cdd:cd14559    166 KNkllpVIHCRAGVGRTGQLAAAMEL---NKSPNNLSVEDIVSDMRTSRngkM--VQKDEQLD 223
FERM_F1_PTPN3_like cd17100
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 25-103 2.09e-08

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein phosphatase non-receptor type 3 (PTPN3) and similar proteins; This family includes two tyrosine-protein phosphatase non-receptors, PTPN3 and PTPN4, both of which belong to the non-transmembrane FERM-containing protein-tyrosine phosphatase (PTP) subfamily characterized by a conserved N-terminal FERM domain, a PDZ domain, and a C-terminal PTP catalytic domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340620  Cd Length: 86  Bit Score: 52.31  E-value: 2.09e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964   25 VKLLENSTVECIVSSRTVGKECLQNVCQRLQILQPEYFGLRYPSKDG---VLRWVDLDRPLKKQLdKYARECCLYLGVMF 101
Cdd:cd17100      6 VHFLDDTEQTFEVEKRDKGQVLLDKVFNHLELVEKDYFGLQFSDDSPatdSMRWLDPLKPIRKQI-KGGPPYYLNFRVKF 84


                   ..
gi 2064663964  102 YV 103
Cdd:cd17100     85 YV 86
FERM_F1_EPB41L5 cd17205
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 19-102 3.02e-08

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte membrane protein band 4.1-like 5 (EPB41L5); EPB41L5 is a mesenchymal-specific protein that is an integral component of the ARF6-based pathway. It is normally induced during epithelial-mesenchymal transition (EMT) by an EMT-related transcriptional factor, ZEB1, which drives ARF6-based invasion, metastasis and drug resistance. EPB41L5 also binds to paxillin to enhance integrin/paxillin association, and thus promotes focal adhesion dynamics. Moreover, EPB41L5 acts as a substrate for the E3 ubiquitin ligase Mind bomb 1 (Mib1), which is essential for activation of Notch signaling. EPB41L5 is a member of the band 4.1/Nbl4 (novel band 4.1-like protein 4) group of the FERM protein superfamily. It contains a FERM domain that is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340725  Cd Length: 86  Bit Score: 51.96  E-value: 3.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964   19 SLCVIAVKLLENSTVECIVSSRTVGKECLQNVCQRLQILQPEYFGLRYPSKDGVLRWVDLDRPLKKQLdKYARECCLYLG 98
Cdd:cd17205      1 SIITCRVSLLDGTDVSVDLPKKAKGQELFEQIMYHLDLIEKDYFGLRFMDSAQVAHWLDVTKSIKKQV-KIGPPYCLHLR 79


                   ....
gi 2064663964   99 VMFY 102
Cdd:cd17205     80 VKFY 83
FERM_C-lobe cd00836
FERM domain C-lobe; The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N ...
 217-307 4.84e-08

FERM domain C-lobe; The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 275389  Cd Length: 93  Bit Score: 51.61  E-value: 4.84e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  217 GEELFDVKDAA--GNETVLGVSVEGVTarYNRGGTANETASYRWSEIVDlIHHK--KSFKIE--GRENGRSAQFQLEDvP 290
Cdd:cd00836      1 GVEFFPVKDKSkkGSPIILGVNPEGIS--VYDELTGQPLVLFPWPNIKK-ISFSgaKKFTIVvaDEDKQSKLLFQTPS-R 76

                           90
                   ....*....|....*..
gi 2064663964  291 TAKYIWKMCVQQHKFFM 307
Cdd:cd00836     77 QAKEIWKLIVGYHRFLL 93
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 951-1047 1.14e-07

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: 53.51  E-value: 1.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  951 WPDHGTPGdvqgflgfMEEV-DSVRRLALNdQRLRTRNAptvVHCTAGVGRSGVVILCdILLFCldHNVPVDLprVLTLV 1029
Cdd:cd14506     84 WKDYGVPS--------LTTIlDIVKVMAFA-LQEGGKVA---VHCHAGLGRTGVLIAC-YLVYA--LRMSADQ--AIRLV 146

                           90
                   ....*....|....*...
gi 2064663964 1030 RMQRMLSVQTLAQYKFVH 1047
Cdd:cd14506    147 RSKRPNSIQTRGQVLCVR 164
FERM_F1_EPB41L1 cd17201
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 25-86 1.15e-07

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte membrane protein band 4.1-like protein 1 (EPB41L1) and similar proteins; EPB41L1, also termed neuronal protein 4.1 (4.1N), belongs to the skeletal protein 4.1 family that is involved in cellular processes such as cell adhesion, migration and signaling. It is a cytoskeleton-associated protein that may serve as a tumor suppressor in solid tumors. It suppresses hypoxia-induced epithelial-mesenchymal transition in epithelial ovarian cancer (EOC) cells. The down-regulation of EPB41L1 expression is a critical step for non-small cell lung cancer (NSCLC) development. Moreover, EPB41L1 functions as a linker protein between inositol 1,4,5-trisphosphate receptor type1 (IP3R1) and actin filaments in neurons. EPB41L1 contains a FERM domain, a spectrin and actin binding (SAB) domain, and a C-terminal domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340721  Cd Length: 84  Bit Score: 50.27  E-value: 1.15e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2064663964   25 VKLLENSTVECIVSSRTVGKECLQNVCQRLQILQPEYFGLRYPSKDGVLRWVDLDRPLKKQL 86
Cdd:cd17201      6 VTLLDGSEYECEVEKHARGQVLFDTVCEHLNLLEKDYFGLTFCDTESQKNWLDPSKEIKKQI 67
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 952-1048 1.19e-07

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


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 52.27  E-value: 1.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  952 PDHGTPGDVQGFLGFMEEVdsvrRLALNDQRlrtrnaPTVVHCTAGVGRSGVVILCdiLLfcLDHNVPVDLPRVLTLVRM 1031
Cdd:cd14505     81 PDGGVPSDIAQWQELLEEL----LSALENGK------KVLIHCKGGLGRTGLIAAC--LL--LELGDTLDPEQAIAAVRA 146

                           90
                   ....*....|....*..
gi 2064663964 1032 QRMLSVQTLAQYKFVHQ 1048
Cdd:cd14505    147 LRPGAIQTPKQENFLHQ 163
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
938-1048 2.76e-07

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 50.74  E-value: 2.76e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  938 CTHRNVWHLRYtDWPDHGTPGDVQgflgFMEEVDSVRRLalndqrlRTRNAPTVVHCTAGVGRSGVVILCdillFCLDHN 1017
Cdd:COG2453     43 LEEAGLEYLHL-PIPDFGAPDDEQ----LQEAVDFIDEA-------LREGKKVLVHCRGGIGRTGTVAAA----YLVLLG 106

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2064663964 1018 VPVDlpRVLTLVRMQRMLSVQTLAQYKFVHQ 1048
Cdd:COG2453    107 LSAE--EALARVRAARPGAVETPAQRAFLER 135
FERM_F1_EPB41L3 cd17203
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 25-86 2.80e-07

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte membrane protein band 4.1-like protein 3 (EPB41L3) and similar proteins; EPB41L3, also termed 4.1B, or differentially expressed in adenocarcinoma of the lung protein 1 (DAL-1), belongs to the skeletal protein 4.1 family that is involved in cellular processes such as cell adhesion, migration and signaling. EPB41L3 is a tumor suppressor that has been implicated in a variety of meningiomas and carcinomas. EPB41L3 contains a FERM domain, a spectrin and actin binding (SAB) domain, and a C-terminal domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340723  Cd Length: 84  Bit Score: 49.17  E-value: 2.80e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2064663964   25 VKLLENSTVECIVSSRTVGKECLQNVCQRLQILQPEYFGLRYPSKDGVLRWVDLDRPLKKQL 86
Cdd:cd17203      6 VTLLDGSEYTCEVEKRSKGQVLFDKVCEHLNLLEKDYFGLTYRDSENQKNWLDPAKEIKKQI 67
FERM_F1_FARP1 cd17189
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, ARH/RhoGEF ...
 23-86 5.34e-07

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, ARH/RhoGEF and pleckstrin domain-containing protein 1 (FARP1); FARP1, also termed chondrocyte-derived ezrin-like protein (CDEP), or pleckstrin homology (PH) domain-containing family C member 2 (PLEKHC2), is a neuronal activator of the RhoA GTPase. It promotes outgrowth of developing motor neuron dendrites. It also regulates excitatory synapse formation and morphology, as well as activates the GTPase Rac1 to promote F-actin assembly. As a novel downstream signaling partner of Rif, FARP1 is involved in the regulation of semaphorin signaling in neurons. FARP1 contains a FERM domain, a Dbl-homology (DH) domain and two pleckstrin homology (PH) domains. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340709  Cd Length: 85  Bit Score: 48.26  E-value: 5.34e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2064663964   23 IAVKLLENSTVECIVSSRTVGKECLQNVCQRLQILQPEYFGLRYPSKDGVLRWVDLDRPLKKQL 86
Cdd:cd17189      3 IKVQMLDDTQEVFEVPQRAPGKVLLDAVCSHLNLVEGDYFGLEFQDHRKVMVWLDLLKPIVKQI 66
FERM_F1_ERM_like cd17097
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the ERM family ...
 31-102 1.01e-06

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the ERM family proteins; The ezrin-radixin-moesin (ERM) family includes a group of closely related cytoskeletal proteins that play an essential role in microvilli formation, T-cell activation, and tumor metastasis through providing a regulated linkage between F-actin and membrane-associated proteins. These proteins may also function in signaling cascades that regulate the assembly of actin stress fibers. The ERM proteins consist of an N-terminal FERM domain, a coiled-coil (CC) domain and a C-terminal tail segment (C-tail) containing a well-defined actin-binding motif. They exist in two states, a dormant state in which the FERM domain binds to its own C-terminal tail and thereby precludes binding of some partner proteins, and an activated state, in which the FERM domain binds to one of many membrane binding proteins and the C-terminal tail binds to F-actin. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). Merlin, which is highly related to the members of the ezrin, radixin, and moesin (ERM) protein family that are directly attached to and functionally linked with NHE1, is included in this family.


Pssm-ID: 340617  Cd Length: 83  Bit Score: 47.66  E-value: 1.01e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2064663964   31 STVECIVSSRTVGKECLQNVCQRLQILQPEYFGLRYPSKDGVLRWVDLDRPLKKQLDKYARECCLYLGVMFY 102
Cdd:cd17097     10 AELEFSIKPKAKGRELFDLVCRTIGLRETWYFGLQYENKKGRVAWLKPDKKVLTQDVSKNNTLKFFFLVKFY 81
FERM_F1_EPB41L5_like cd17108
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 25-102 1.46e-06

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte membrane protein band 4.1-like 5 (EPB41L5) and similar proteins; This family includes FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte membrane protein band 4.1-like proteins, EPB41L5 and EPB41L4B. EPB41L5 is a mesenchymal-specific protein that is an integral component of the ARF6-based pathway. EPB41L4B is a positive regulator of keratinocyte adhesion and motility, suggesting a role in wound healing. It also promotes cancer metastasis in melanoma, prostate cancer and breast cancer. Both EPB41L5 and EPB41L4B contain a FERM domain that is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340628  Cd Length: 81  Bit Score: 46.96  E-value: 1.46e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2064663964   25 VKLLENSTVECIVSSRTVGKECLQNVCQRLQILQPEYFGLRYPSKDGVLRWVDLDRPLKKQLdKYARECCLYLGVMFY 102
Cdd:cd17108      5 VILLDGTDLSIELPKKAKGQELYEQVFYHLDLIEKDYFGLQFMDAAQVQHWLDPTKKIKKQV-KIGPPYTLRFRVKFY 81
FERM_F1_EPB41L cd17106
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 25-86 3.72e-06

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte membrane protein band 4.1-like proteins; The family includes erythrocyte membrane protein band 4.1-like proteins EPB41L1/4.1N, EPB41L2/4.1G, and EPB41L3/4.1B. They belong to the skeletal protein 4.1 family that is involved in cellular processes such as cell adhesion, migration and signaling. EPB41L1 is a cytoskeleton-associated protein that may serve as a tumor suppressor in solid tumors. EPB41L2 is involved in cellular processes such as cell adhesion, migration and signaling. EPB41L3 also acts as a tumor suppressor implicated in a variety of meningiomas and carcinomas. Members in this family contain a FERM domain, a spectrin and actin binding (SAB) domain, and a C-terminal domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340626  Cd Length: 84  Bit Score: 45.89  E-value: 3.72e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2064663964   25 VKLLENSTVECIVSSRTVGKECLQNVCQRLQILQPEYFGLRYPSKDGVLRWVDLDRPLKKQL 86
Cdd:cd17106      6 VLLLDGTEYTCEVEKRAKGQVLFDKVCEHLNLLEKDYFGLTYRDAQDQKNWLDPAKEIKKQI 67
FERM_C_ERM cd13194
FERM domain C-lobe/F3 of the ERM family; The ERM family includes ezrin, radixin, moesin and ...
 216-307 4.54e-06

FERM domain C-lobe/F3 of the ERM family; The ERM family includes ezrin, radixin, moesin and merlin. They are composed of a N-terminal FERM (ERM) domain (also called N-ERMAD (N-terminal ERM association domain)), a coiled coil region (CRR), and a C-terminal domain CERMAD (C-terminal ERM association domain) which has an F-actin-binding site (ABD). Two actin-binding sites have been identified in the middle and N-terminal domains. Merlin is structurally similar to the ERM proteins, but instead of an actin-binding domain (ABD), it contains a C-terminal domain (CTD), just like the proteins from the 4.1 family. Activated ezrin, radixin and moesin are thought to be involved in the linking of actin filaments to CD43, CD44, ICAM1-3 cell adhesion molecules, various membrane channels and receptors, such as the Na+/H+ exchanger-3 (NHE3), cystic fibrosis transmembrane conductance regulator (CFTR), and the beta2-adrenergic receptor. The ERM proteins exist in two states, a dormant state in which the FERM domain binds to its own C-terminal tail and thereby precludes binding of some partner proteins, and an activated state, in which the FERM domain binds to one of many membrane binding proteins and the C-terminal tail binds to F-actin. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain of ERM is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270015  Cd Length: 97  Bit Score: 46.11  E-value: 4.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  216 YGEELFDVKDAAGNETVLGVSVEGVTArYNRGGTANETASYRWSEIVDLIHHKKSFKIegRENGRSAQ---FQLEDVPTA 292
Cdd:cd13194      2 YGVNYFEIKNKKGTDLWLGVDALGLNI-YEPDNKLTPKIGFPWSEIRNISFNDKKFVI--KPIDKKAPdfvFYSPRLRIN 78

                           90
                   ....*....|....*
gi 2064663964  293 KYIWKMCVQQHKFFM 307
Cdd:cd13194     79 KRILDLCMGNHELYM 93
FERM_F1_FRMD4A cd17199
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 25-103 4.82e-06

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM domain-containing protein 4A (FRMD4A); FRMD4A is a cytohesin adaptor involved in cell structure, transport and signaling. It promotes the growth of cancer cells in tongue, head and neck squamous cell carcinomas. It also regulates tau secretion by activating cytohesin-Arf6 signaling through connecting cytohesin family Arf6-specific guanine-nucleotide exchange factors (GEFs) and Par-3 at primordial adherens junctions during epithelial polarization. As a genetic risk factor for late-onset Alzheimer's disease (AD), FRMD4A may play a role in amyloidogenic and tau-related pathways in AD. FRMD4A contains a FERM domain that is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340719  Cd Length: 89  Bit Score: 45.73  E-value: 4.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964   25 VKLLENSTVECIVSSRTVGKECLQNVCQRLQILQPEYFGLRYPSKDGVLRWVDLDRP-LKKQLDKYARECCLYLGVMFYV 103
Cdd:cd17199      7 VHLLDDRKLELLVQPKLLAKELLDLVASHFNLKEKEYFGIAFTDETGHLNWLQLDRRvLEHDFPKKSGPVVLYFCVRFYI 86
FERM_F1_FRMD4B cd17200
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 25-103 7.74e-06

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM domain-containing protein 4B (FRMD4B); FRMD4B, also termed GRP1-binding protein GRSP1, interacts with the coil-coil domain of ARF exchange factor GRP1 to form the Grsp1-Grp1 complex that co-localizes with cortical actin rich regions in response to stimulation of CHO-T cells with insulin or epidermal growth factor (EGF). FRMD4B contains a FERM protein interaction domain as well as two coiled coil domains and may therefore function as a scaffolding protein. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340720  Cd Length: 89  Bit Score: 45.26  E-value: 7.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964   25 VKLLENSTVECIVSSRTVGKECLQNVCQRLQILQPEYFGLRYPSKDGVLRWVDLD-RPLKKQLDKYARECCLYLGVMFYV 103
Cdd:cd17200      7 VHLLDDRKLELLVQPKLLSRELLDLVASHFNLKEKEYFGITFIDDTGQSNWLQLDhRVLDHDLPKKSGPVTLYFAVRFYI 86
FERM_F1_FRMD7 cd17188
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 25-102 8.87e-06

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM domain-containing protein 7 (FRMD7); FRMD7 plays an important role in neuronal development and is involved in the regulation of F-actin, neurofilament, and microtubule dynamics. It interacts with the Rho GTPase regulator, RhoGDIalpha, and activates the Rho subfamily member Rac1, which regulates reorganization of actin filaments and controls neuronal outgrowth. Mutations in the FRMD7 gene are responsible for the X-linked idiopathic congenital nystagmus (ICN), a disease which affects ocular motor control. FRMD7 contains a FERM domain, and a pleckstrin homology (PH) domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340708  Cd Length: 86  Bit Score: 44.80  E-value: 8.87e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2064663964   25 VKLLENSTVECIVSSRTVGKECLQNVCQRLQILQPEYFGLRYPSKDGVLRWVDLDRPLKKQLdKYARECCLYLGVMFY 102
Cdd:cd17188      6 VQFLDDSQKVFVVDQKSTGKDLFNMSCSHLNLVEKEYFGLEFRNHAGNNVWLELLKPITKQI-KNPKELIFKFTVKFF 82
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 956-1048 1.13e-05

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


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 46.12  E-value: 1.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  956 TPGDVQGFLGFMEEVdsvrrlalndqrlRTRNAPTVVHCTAGVGRSGVVILCdiLLFCLDHNVPVDlprVLTLVRMQRML 1035
Cdd:cd14504     64 TLEQIDEFLDIVEEA-------------NAKNEAVLVHCLAGKGRTGTMLAC--YLVKTGKISAVD---AINEIRRIRPG 125

                           90
                   ....*....|...
gi 2064663964 1036 SVQTLAQYKFVHQ 1048
Cdd:cd14504    126 SIETSEQEKFVIQ 138
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 546-721 1.48e-05

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 49.31  E-value: 1.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  546 VDGVAHGRPLLAPPLHTYStpeltsqglsyemnPAQLFANLNYQHKPPPPYPYSQRPTASTPDLTRNHSHLLQVSTSPDL 625
Cdd:PRK10263   363 VPGPQTGEPVIAPAPEGYP--------------QQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQP 428

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  626 VSRRHLTPNPTQGSEPSlaQYQWVNGRAVEDVKPVLPTYVPVGESwNAQVSGVVQPQRIQVFVSSSPVPATEQTavKPSN 705
Cdd:PRK10263   429 AQQPYYAPAPEQPVAGN--AWQAEEQQSTFAPQSTYQTEQTYQQP-AAQEPLYQQPQPVEQQPVVEPEPVVEET--KPAR 503

                          170       180
                   ....*....|....*....|.
gi 2064663964  706 PP-----PLPERQTSEEESSA 721
Cdd:PRK10263   504 PPlyyfeEVEEKRAREREQLA 524
FERM_F1_EPB41 cd17105
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 25-86 1.50e-05

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte membrane protein band 4.1 (EPB41) and similar proteins; EPB41, also termed protein 4.1 (P4.1), or 4.1R, or Band 4.1, or EPB4.1, belongs to the skeletal protein 4.1 family that is involved in cellular processes such as cell adhesion, migration and signaling. EPB41 is a widely expressed cytoskeletal phosphoprotein that stabilizes the spectrin-actin cytoskeleton and anchors the cytoskeleton to the cell membrane. EPB41 contains a FERM domain, a spectrin and actin binding (SAB) domain, and a C-terminal domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340625  Cd Length: 83  Bit Score: 44.42  E-value: 1.50e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2064663964   25 VKLLENSTVECIVSSRTVGKECLQNVCQRLQILQPEYFGLRYPSKDGVLRWVDLDRPLKKQL 86
Cdd:cd17105      5 VSLLDDTVYECEVEKHAKGQDLFKKVCEHLNLLEEDYFGLAIWDSPTSKTWLDPAKEIKKQV 66
FERM_F1_EPB41L2 cd17202
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
 25-86 1.97e-05

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte membrane protein band 4.1-like protein 2 (EPB41L2) and similar proteins; EPB41L2, also termed generally expressed protein 4.1 (4.1G), belongs to the skeletal protein 4.1 family that is involved in cellular processes such as cell adhesion, migration and signaling. EPB41L2 contains a FERM domain, a spectrin and actin binding (SAB) domain, and a C-terminal domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340722  Cd Length: 84  Bit Score: 43.81  E-value: 1.97e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2064663964   25 VKLLENSTVECIVSSRTVGKECLQNVCQRLQILQPEYFGLRYPSKDGVLRWVDLDRPLKKQL 86
Cdd:cd17202      6 VTLLDGTEYSCDLEKRAKGQVLFDKVCEHLNLLEKDYFGLLYQVSANQKNWLDSTKEIKRQI 67
FERM_F1_PTPN13_like cd17101
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 23-103 4.71e-05

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein phosphatase non-receptor type 13 (PTPN13) and similar proteins; This family includes tyrosine-protein phosphatase non-receptor type 13 (PTPN13), FERM and PDZ domain-containing protein 2 (FRMPD2), and FERM domain-containing proteins FRMD1 and FRMD6. All family members contain a FERM domain that is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340621  Cd Length: 97  Bit Score: 43.32  E-value: 4.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964   23 IAVKLLENSTVECIVSSRTVGKECLQNVCQRLQILQPEYFGLRYpSKDGVLRWVDLDrplkKQLDKYAREC--------- 93
Cdd:cd17101      4 VNVVLLNGQRLQVAVDVKTTVQDLFDQVCDHLGLQETELFGLAV-LKDGEYFFLDPD----TKLSKYAPKGwkseakkgl 78

                           90
                   ....*....|....*..
gi 2064663964   94 -------CLYLGVMFYV 103
Cdd:cd17101     79 kggkpvfTLYFRVKFYV 95
FERM_C_PTPH13 cd13187
FERM domain C-lobe of Protein tyrosine phosphatase non-receptor 13 (PTPH13); There are many ...
 220-309 4.80e-05

FERM domain C-lobe of Protein tyrosine phosphatase non-receptor 13 (PTPH13); There are many functions of PTPN13 (also called PTPL1, PTP-BAS, hPTP1E, FAP1, or PTPL1). Mice lacking PTPN13 activity have abnormal regulation of signal transducer and activator of transcription signaling in their T cells, mild impairment of motor nerve repair, and a significant reduction in the growth of retinal glia cultures. It also plays a role in adipocyte differentiation. PTPN13 contains a kinase non-catalytic C-lobe domain (KIND), a FERM domain with two potential phosphatidylinositol 4,5-biphosphate [PtdIns(4,5)P2]-binding motifs, 5 PDZ domains, and a carboxy-terminal catalytic domain. There is an nteraction between the FERM domain of PTPL1 and PtdIns(4,5)P2 which is thought to regulate the membrane localization of PTPN13. PDZ are protein/protein interaction domains so there is the potential for numerous partners that can actively participate in the regulation of its phosphatase activity or can permit direct or indirect recruitment of tyrosine phosphorylated PTPL1 substrates. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270008  Cd Length: 103  Bit Score: 43.47  E-value: 4.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  220 LFDVKDAAGNETVLGVSVEGVTARYNRGGTANETASYRWSEIVDLIHHKKSFKIEGR-ENGRSAQFQLEDVPTAKYIWKM 298
Cdd:cd13187      7 VYREKKSSTLSLWLGICSRGIIIYEEKNGARTPVLRFPWRETQKISFDKKKFTIESRgGSGIKHTFYTDSYKKSQYLLQL 86

                           90
                   ....*....|.
gi 2064663964  299 CVQQHKFFMSM 309
Cdd:cd13187     87 CSAQHKFHIQM 97
FERM_C_FRMD4A_FRMD4B cd13191
FERM domain C-lobe of FERM domain-containing protein 4A and 4B (FRMD4A and 4B); FRMD4A is part ...
 221-313 8.00e-05

FERM domain C-lobe of FERM domain-containing protein 4A and 4B (FRMD4A and 4B); FRMD4A is part of the Par-3/FRMD4A/cytohesin-1 complex that activates Arf6, a central player in actin cytoskeleton dynamics and membrane trafficking, during junctional remodeling and epithelial polarization. The Par-3/Par-6/aPKC/Cdc42 complex regulates the conversion of primordial adherens junctions (AJs) into belt-like AJs and the formation of linear actin cables. When primordial AJs are formed, Par-3 recruits scaffolding protein FRMD4A which connects Par-3 and the Arf6 guanine-nucleotide exchange factor (GEF), cytohesin-1. FRMD4B (also called GRP1-binding protein, GRSP1) is a novel member of GRP1 signaling complexes that are recruited to plasma membrane ruffles in response to insulin receptor signaling. The GRSP1/FRMD4B protein contains a FERM protein domain as well as two coiled coil domains and may function as a scaffolding protein. GRP1 and GRSP1 interact through the coiled coil domains in the two proteins. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs) , the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270012  Cd Length: 113  Bit Score: 43.10  E-value: 8.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  221 FDVKDAAGNETVLGVSVEGVtARYNRGGTANETASYRWSEIVDLIHHKKSFKIEGRENGRSAQ-----FQLEDVPT---- 291
Cdd:cd13191      5 YEVKDKNGIPWWLGVSYKGI-GQYDLQDKVKPRKFFQWKQLENLYFRDRKFSIEVRDPRRNSHrsrrtFQSSSVSVhvwy 83

                           90       100
                   ....*....|....*....|....*...
gi 2064663964  292 ------AKYIWKMCVQQHKFFMSMQETR 313
Cdd:cd13191     84 gqtpalCKTIWSMAIAQHQFYLDRKQSK 111
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 968-1048 1.47e-04

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: 42.34  E-value: 1.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  968 EEVDSVRRLAlndQRLRTRNAPTVVHCTAGVGRSGVVILCDILlfCLDHNVPVDLPRVLTLVRMQRMlsVQTLAQYKFVH 1047
Cdd:cd14494     40 AMVDRFLEVL---DQAEKPGEPVLVHCKAGVGRTGTLVACYLV--LLGGMSAEEAVRIVRLIRPGGI--PQTIEQLDFLI 112


                   .
gi 2064663964 1048 Q 1048
Cdd:cd14494    113 K 113
FERM_F1_EPB41L4B cd17204
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte band ...
 25-102 1.49e-04

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte band 4.1-like protein 4B (EPB41L4B); EPB41L4B, also termed FERM-containing protein CG1, or expressed in high metastatic cells (Ehm2), or Lulu2, is a member of the band 4.1/Nbl4 (novel band 4.1-like protein 4) group of the FERM protein superfamily. It contains a FERM domain that is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). EPB41L4B is a positive regulator of keratinocyte adhesion and motility, suggesting a role in wound healing. It also promotes cancer metastasis in melanoma, prostate cancer and breast cancer.


Pssm-ID: 340724  Cd Length: 84  Bit Score: 41.34  E-value: 1.49e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2064663964   25 VKLLENSTVECIVSSRTVGKECLQNVCQRLQILQPEYFGLRYPSKDGVLRWVDLDRPLKKQLdKYARECCLYLGVMFY 102
Cdd:cd17204      5 VLLLDGTDVSVELPKHAKGQDLFDQIVYHLDLVETDYFGLQFMDAAQVAHWLDHTKPIKKQI-KIGPPYTLHFRIKYY 81
FERM_F1_FARP2 cd17190
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, ARH/RhoGEF ...
 23-102 3.05e-04

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, ARH/RhoGEF and pleckstrin domain-containing protein 2 (FARP2) and similar proteins; FARP2, also termed FERM domain including RhoGEF (FIR), or Pleckstrin homology (PH) domain-containing family C member 3, is a Dbl-family guanine nucleotide exchange factor (GEF) that activates Rac1 or Cdc42 in response to upstream signals, suggesting roles in regulating processes such as neuronal axon guidance and bone homeostasis. It is also a key molecule involved in the response of neuronal growth cones to class-3 semaphorins. FARP2 contains a FERM domain, a Dbl-homology (DH) domain and two pleckstrin homology (PH) domains. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340710  Cd Length: 85  Bit Score: 40.55  E-value: 3.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964   23 IAVKLLENSTVECIVSSRTVGKECLQNVCQRLQILQPEYFGLRYPSKDGVLRWVDLDRPLKKQLDKyARECCLYLGVMFY 102
Cdd:cd17190      3 LRVKLLDNTTEPLEIEPKADGQALLSQVFKRLNLVESDYFGLEFQNSQSNWIWLEPMKLIVKQVRR-PKNTKLRLAVKFF 81
FERM_C_MYLIP_IDOL cd13195
FERM domain C-lobe of E3 ubiquitin ligase myosin regulatory light chain-interacting protein ...
 216-306 3.25e-04

FERM domain C-lobe of E3 ubiquitin ligase myosin regulatory light chain-interacting protein (MYLIP; also called inducible degrader of the LDL receptor, IDOL); MYLIP/IDOL is a regulator of the LDL receptor (LDLR) pathway via the nuclear receptor liver X receptor (LXR). In response to cellular cholesterol loading, the activation of LXR leads to the induction of MYLIP expression. MYLIP stimulates ubiquitination of the LDLR on its cytoplasmic tail, directing its degradation. The LXR-MYLIP-LDLR pathway provides a complementary pathway to sterol regulatory element-binding proteins for the feedback inhibition of cholesterol uptake. MYLIP has an N-terminal FERM domain and in some cases a C-terminal RING domain. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270016  Cd Length: 111  Bit Score: 41.08  E-value: 3.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  216 YGEELFDVKDAAGNETVLGVSVEGVTArYNRGGTANETASYrwSEIVDLIHHKKSFKIEGRENGRSAQ---FQLEDVPTA 292
Cdd:cd13195      1 YGVEFFEVRNIEGQKLLIGVGPHGITI-CNDDFEVIERIPY--TAIQMATSSGRVFTLTYLSDDGSVKvleFKLPSTRAA 77

                           90
                   ....*....|....
gi 2064663964  293 KYIWKMCVQQHKFF 306
Cdd:cd13195     78 SGLYRAITEKHAFY 91
PHA03247 PHA03247
large tegument protein UL36; Provisional
 590-762 4.98e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 4.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  590 HKPPPPyPYSQRPTASTPD----LTRNHSHLLQVSTSPDLVSRRHLTPNPTQGSEPSLAQYQWVNGRAVEDVKPVL---- 661
Cdd:PHA03247  2622 HAPDPP-PPSPSPAANEPDphppPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTslad 2700

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  662 -----PTYVPVGESWnaqVSGVVQPQRIQVFVSSSPV-------PATEQTAVKPSNPPPLPERQTSEEESSATRPVGPmm 729
Cdd:PHA03247  2701 pppppPTPEPAPHAL---VSATPLPPGPAAARQASPAlpaapapPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAP-- 2775

                          170       180       190
                   ....*....|....*....|....*....|...
gi 2064663964  730 lAAMNGLTLTLSRPDSLSMQSTDAPVPECPPSP 762
Cdd:PHA03247  2776 -AAGPPRRLTRPAVASLSESRESLPSPWDPADP 2807
FERM_C_NBL4_NBL5 cd13186
FERM domain C-lobe of Novel band 4.1-like protein 4 and 5 (NBL4 and 5); NBL4 (also called ...
 217-306 5.25e-04

FERM domain C-lobe of Novel band 4.1-like protein 4 and 5 (NBL4 and 5); NBL4 (also called Erythrocyte protein band 4.1-like 4; Epb4 1l4) plays a role the beta-catenin/Tcf signaling pathway and is thought to be involved in establishing the cell polarity or proliferation. NBL4 may be also involved in adhesion, in cell motility and/or in cell-to-cell communication. No role for NBL5 has been proposed to date. Both NBL4 and NBL5 contain a N-terminal FERM domain which has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe is a member of the PH superfamily. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs) , the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270007  Cd Length: 92  Bit Score: 39.96  E-value: 5.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  217 GEELFDVKDAAGNETVLGVSVEGVTARYNRggtaNETASYRWSEIVDLIHHKKSFKIEGRENGRSAQ-----FQLEDVPT 291
Cdd:cd13186      1 GVDLHPVKGEDGNEYFLGLTPTGILVFENK----TKIGLFFWPRITKLDFKGKKLKLVVKEKDDQEQehtfvFRLPNKKA 76

                           90
                   ....*....|....*
gi 2064663964  292 AKYIWKMCVQQHKFF 306
Cdd:cd13186     77 CKHLWKCAVEHHAFF 91
FERM_F1_FRMD4 cd17103
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
 25-106 1.10e-03

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM domain-containing proteins FRMD4A, FRMD4B, and similar proteins; This family includes FERM domain-containing proteins FRMD4A and FRMD4B, both of which contain a FERM domain that is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). FRMD4A is a cytohesin adaptor involved in cell structure, transport and signaling. It promotes the growth of cancer cells in tongue, head and neck squamous cell carcinomas. FRMD4B, also termed GRP1-binding protein GRSP1, interacts with the coil-coil domain of ARF exchange factor GRP1 to form the Grsp1-Grp1 complex that co-localizes with cortical actin rich regions in response to stimulation of CHO-T cells with insulin or epidermal growth factor (EGF).


Pssm-ID: 340623  Cd Length: 91  Bit Score: 39.19  E-value: 1.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964   25 VKLLENSTVECIVSSRTVGKECLQNVCQRLQILQPEYFGLRYPSKDGVLRWVDLDR-------PLKKQLDKYAreccLYL 97
Cdd:cd17103      7 VVLLDDRRLEILVQPKLLAGDLLDLVASHFNLKEKEYFGLAYEDETGHYNWLQLDKrvldhefPKKWSSGPLV----LHF 82


                   ....*....
gi 2064663964   98 GVMFYVFNV 106
Cdd:cd17103     83 AVKFYVESI 91
FERM_F1_PTPN4 cd17194
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
 22-88 1.52e-03

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein phosphatase non-receptor type 4 (PTPN4); PTPN4, also termed protein-tyrosine phosphatase MEG1 (MEG) or PTPase-MEG1, belongs to the non-transmembrane FERM-containing protein-tyrosine phosphatase (PTP) subfamily characterized by a conserved N-terminal FERM domain, a PDZ domain, and a C-terminal PTP catalytic domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). PTPN4 protects cells against apoptosis. It associates with the mitogen-activated protein kinase p38gamma (also known as MAPK12) to form a PTPN4-p38gamma complex that promotes cellular signaling, preventing cell death induction. It also inhibits tyrosine phosphorylation and subsequent cytoplasm translocation of TRIF-related adaptor molecule (TRAM, also known as TICAM2), resulting in the disturbance of TRAM-TRIF interaction. Moreover, PTPN4 negatively regulates cell proliferation and motility through dephosphorylation of CrkI.


Pssm-ID: 340714  Cd Length: 84  Bit Score: 38.74  E-value: 1.52e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2064663964   22 VIAVKLLENSTVECIVSSRTVGKECLQNVCQRLQILQPEYFGLRYP--SKDGVlRWVDLDRPLKKQLDK 88
Cdd:cd17194      3 VCNILLLDNTVQAFKVNKHDQGQVLLDLVFKHLDLTERDYFGLQLAddSTDNP-RWLDPNKPIRKQLKR 70
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 592-771 1.69e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.47  E-value: 1.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  592 PPPPYPYSQRPTASTPDLTRNHSHLLQVSTSPDLVSRRHLTPNPTQGSEPSLAQYQWVNGRAVEDVKP-------VLPTY 664
Cdd:PHA03307   189 PPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPlprpapiTLPTR 268

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  665 VPVGESWNAQvsgvvqpqriqvfvSSSPVPATEQTAVKPSNPPPLPERQTSEEESSATRPVGPMMLAAMNGLTLTLSRPD 744
Cdd:PHA03307   269 IWEASGWNGP--------------SSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSE 334

                          170       180
                   ....*....|....*....|....*..
gi 2064663964  745 SlSMQSTDAPVPECPPSPRDQRPDSVL 771
Cdd:PHA03307   335 S-SRGAAVSPGPSPSRSPSPSRPPPPA 360
FERM_C_FARP1-like cd13193
FERM domain C-lobe of FERM, RhoGEF and pleckstrin domain-containing protein 1 and related ...
 213-310 2.76e-03

FERM domain C-lobe of FERM, RhoGEF and pleckstrin domain-containing protein 1 and related proteins; Members here include FARP1 (also called Chondrocyte-derived ezrin-like protein; PH domain-containing family C member 2), FARP2 (also called FIR/FERM domain including RhoGEF; FGD1-related Cdc42-GEF/FRG), and FRMD7(FERM domain containing 7). FARP1 and FARP2 are members of the Dbl family guanine nucleotide exchange factors (GEFs) which are upstream positive regulators of Rho GTPases. FARP1 has increased expression in differentiated chondrocytes. FARP2 is thought to regulate neurite remodeling by mediating the signaling pathways from membrane proteins to Rac. It is found in brain, lung, and testis, as well as embryonic hippocampal and cortical neurons. These members are composed of a N-terminal FERM domain, a proline-rich (PR) domain, Dbl-homology (DH), and two C-terminal PH domains. Other members in this family do not contain the DH domains such as the Human FERM domain containing protein 7 and Caenorhabditis elegans CFRM3, both of which have unknown functions. They contain an N-terminal FERM domain, a PH domain, followed by a FA (FERM adjacent) domain. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270014  Cd Length: 122  Bit Score: 38.86  E-value: 2.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064663964  213 LEGYGEELFDVKDAAGNETVLGVSVEGVTARynRGGTANETASyrWSEIVDLIHHKKSFKI----EGRENGRSA-QFQLE 287
Cdd:cd13193      6 CELYGIRLHPAKDREGVKLNLAVAHMGILVF--QGFTKINTFS--WAKIRKLSFKRKRFLIklhpEAYGSYKDTvEFSFE 81

                           90       100
                   ....*....|....*....|...
gi 2064663964  288 DVPTAKYIWKMCVQQHKFFMSMQ 310
Cdd:cd13193     82 SRNECKSFWKKCIEHHAFFRCSE 104
 
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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