NCBI Conserved Domain Search

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

398-475

9.57e-08

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 50.31 E-value: 9.57e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117  398 PQSVTNITVKNRNETALILEWNKVNNNNNYSYTLSYNSQNTSINGSEEGVAVT-----YTVPDLTAGTEYTFTLYTVFKG 472
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTpsstsYTLTGLKPGTEYEFRVRAVNGA 80


                   ...
gi 1764596117  473 VES 475
Cdd:smart00060  81 GEG 83

fn3

Fibronectin type III domain;

400-469

1.72e-06

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 46.64 E-value: 1.72e-06

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1764596117 400 SVTNITVKNRNETALILEWNKVNNNNNY--SYTLSY---NSQNTSINGSEEGVAVTYTVPDLTAGTEYTFTLYTV 469
Cdd:pfam00041   2 APSNLTVTDVTSTSLTVSWTPPPDGNGPitGYEVEYrpkNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAV 76

FN3

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

398-485

1.75e-05

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

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 44.02 E-value: 1.75e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 398 PQSVTNITVKNRNETALILEWNKVNNNNNY--SYTLSY---NSQNTSINGSEEGVAVTYTVPDLTAGTEYTFTLYTVFKG 472
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPitGYVVEYrekGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|...
gi 1764596117 473 VESRAYHITSVTV 485
Cdd:cd00063    81 GESPPSESVTVTT 93

Name

Accession

Description

Interval

E-value

PTPc

smart00194

Protein tyrosine phosphatase, catalytic domain;

638-897

2.14e-121

Protein tyrosine phosphatase, catalytic domain;

Pssm-ID: 214550 [Multi-domain] Cd Length: 259 Bit Score: 369.30 E-value: 2.14e-121

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117  638 GFSEEYEDLSTVG-TDQSCTVATLPENKSKNRFTNVLPYDISRVKLAAQTGSDLDYINANYIHGYgKKNKQYIAAQGPLP 716
Cdd:smart00194   1 GLEEEFEKLDRLKpDDESCTVAAFPENRDKNRYKDVLPYDHTRVKLKPPPGEGSDYINASYIDGP-NGPKAYIATQGPLP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117  717 STVSDFWRMVWEQKSSAIVMLTNCTEGGRIKCEHYWPVD-DMPCLYGNLRVSVQSEQKESCWTRREFVVRNESTSEERGV 795
Cdd:smart00194  80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEeGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTV 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117  796 THFHFTAWPDHGVPKGTEELIQFRWIVRQHIETFpfSGPTVVHCSAGVGRTGTLIALDLLLQQMDKEEVVSIADCVRCMR 875
Cdd:smart00194 160 THYHYTNWPDHGVPESPESILDLIRAVRKSQSTS--TGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKELR 237

                          250       260
                   ....*....|....*....|..
gi 1764596117  876 LSRPLMVQTQSQYVFLHQCIMD 897
Cdd:smart00194 238 SQRPGMVQTEEQYIFLYRAILE 259

R-PTPc-H

cd14619

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

667-899

4.36e-121

Pssm-ID: 350467 [Multi-domain] Cd Length: 233 Bit Score: 367.29 E-value: 4.36e-121

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 667 NRFTNVLPYDISRVKLAA-QTGSDLDYINANYIHGYGKkNKQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEGGR 745
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKPiHEEPGSDYINANYMPGYWS-SQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 746 IKCEHYWPVDDMPCLYGNLRVSVQSEQKESCWTRREFVVRNESTSEERGVTHFHFTAWPDHGVPKGTEELIQFRWIVRQH 825
Cdd:cd14619    80 VKCEHYWPLDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQW 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1764596117 826 IETFPFSGPTVVHCSAGVGRTGTLIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLHQCIMDSL 899
Cdd:cd14619   160 LDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233

Y_phosphatase

pfam00102

Protein-tyrosine phosphatase;

663-897

4.82e-110

Protein-tyrosine phosphatase;

Pssm-ID: 459674 [Multi-domain] Cd Length: 234 Bit Score: 338.45 E-value: 4.82e-110

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 663 NKSKNRFTNVLPYDISRVKLAAQTGSDlDYINANYIHGYGKKNKqYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTE 742
Cdd:pfam00102   1 NLEKNRYKDVLPYDHTRVKLTGDPGPS-DYINASYIDGYKKPKK-YIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 743 GGRIKCEHYWP-VDDMPCLYGNLRVSVQSEQK-ESCWTRREFVVRNESTSEERGVTHFHFTAWPDHGVPKGTEELIQFRW 820
Cdd:pfam00102  79 KGREKCAQYWPeEEGESLEYGDFTVTLKKEKEdEKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1764596117 821 IVRQHiETFPFSGPTVVHCSAGVGRTGTLIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLHQCIMD 897
Cdd:pfam00102 159 KVRKS-SLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAILE 234

R3-PTPc

cd14548

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

668-893

2.15e-108

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: 333.94 E-value: 2.15e-108

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 668 RFTNVLPYDISRVKLAAQT---GSDldYINANYIHGYGKKnKQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEGG 744
Cdd:cd14548     1 RYTNILPYDHSRVKLIPINeeeGSD--YINANYIPGYNSP-REFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 745 RIKCEHYWPVDDMPCLYGNLRVSVQSEQKESCWTRREFVVRNEstSEERGVTHFHFTAWPDHGVPKGTEELIQFRWIVRQ 824
Cdd:cd14548    78 RVKCDHYWPFDQDPVYYGDITVTMLSESVLPDWTIREFKLERG--DEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRD 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1764596117 825 HIEtfPFSGPTVVHCSAGVGRTGTLIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLHQ 893
Cdd:cd14548   156 YIK--QEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222

R-PTPc-J

cd14615

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

667-897

4.42e-106

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: 327.93 E-value: 4.42e-106

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 667 NRFTNVLPYDISRVKLAAQTGSDLDYINANYIHGYGKKnKQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEGGRI 746
Cdd:cd14615     1 NRYNNVLPYDISRVKLSVQSHSTDDYINANYMPGYNSK-KEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 747 KCEHYWPvDDMPCLYGNLRVSVQSEQKESCWTRREFVVRNESTSEERGVTHFHFTAWPDHGVPKGTEELIQFRWIVRQHI 826
Cdd:cd14615    80 KCEEYWP-SKQKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREYM 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1764596117 827 ETFPFSGPTVVHCSAGVGRTGTLIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLHQCIMD 897
Cdd:cd14615   159 KQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229

PTPc

cd00047

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

692-893

3.14e-95

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: 298.43 E-value: 3.14e-95

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 692 YINANYIHGYGKKNKqYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEGGRIKCEHYWP-VDDMPCLYGNLRVSVQS 770
Cdd:cd00047     1 YINASYIDGYRGPKE-YIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPeEGGKPLEYGDITVTLVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 771 EQKESCWTRREFVVRNESTSEERGVTHFHFTAWPDHGVPKGTEELIQFRWIVRQHIEtfPFSGPTVVHCSAGVGRTGTLI 850
Cdd:cd00047    80 EEELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEAR--KPNGPIVVHCSAGVGRTGTFI 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1764596117 851 ALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLHQ 893
Cdd:cd00047   158 AIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200

R-PTPc-V

cd14618

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

667-896

2.67e-94

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: 297.24 E-value: 2.67e-94

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 667 NRFTNVLPYDISRVKLAaQTGSD--LDYINANYIHGYGKKnKQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEGG 744
Cdd:cd14618     1 NRYPHVLPYDHSRVRLS-QLGGEphSDYINANFIPGYTSP-QEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 745 RIKCEHYWPVDDMPCLYGNLRVSVQSEQKESCWTRREFVVRNESTSEERGVTHFHFTAWPDHGVPKGTEELIQFRWIVRQ 824
Cdd:cd14618    79 RVLCDHYWPSESTPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVRE 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1764596117 825 HIETFPFSGPTVVHCSAGVGRTGTLIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLHQCIM 896
Cdd:cd14618   159 HVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCIL 230

R-PTPc-LAR-1

cd14553

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

663-898

9.84e-90

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

Pssm-ID: 350401 [Multi-domain] Cd Length: 238 Bit Score: 285.06 E-value: 9.84e-90

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 663 NKSKNRFTNVLPYDISRVKLAAQTG-SDLDYINANYIHGYGKKNkQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCT 741
Cdd:cd14553     3 NKPKNRYANVIAYDHSRVILQPIEGvPGSDYINANYCDGYRKQN-AYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 742 EGGRIKCEHYWPVDDmPCLYGNLRVSVQSEQKESCWTRREFVVRNESTSEERGVTHFHFTAWPDHGVPKGTEELIQFRWI 821
Cdd:cd14553    82 ERSRVKCDQYWPTRG-TETYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRR 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1764596117 822 VRQHieTFPFSGPTVVHCSAGVGRTGTLIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLHQCIMDS 898
Cdd:cd14553   161 VKAC--NPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDALLEA 235

R-PTPc-B

cd14617

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

667-893

1.66e-89

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: 284.12 E-value: 1.66e-89

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 667 NRFTNVLPYDISRVKLAAQTGSDL-DYINANYIHGYGKKnKQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEGGR 745
Cdd:cd14617     1 NRYNNILPYDSTRVKLSNVDDDPCsDYINASYIPGNNFR-REYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 746 IKCEHYWPVDDMPCLYGNLRVSVQSEQKESCWTRREFVVRNESTSE-ERGVTHFHFTAWPDHGVPKGTEELIQFRWIVRQ 824
Cdd:cd14617    80 VKCDHYWPADQDSLYYGDLIVQMLSESVLPEWTIREFKICSEEQLDaPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVRD 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1764596117 825 HIETFPFSGPTVVHCSAGVGRTGTLIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLHQ 893
Cdd:cd14617   160 YINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228

R-PTPc-O

cd14614

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

652-895

2.39e-88

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: 281.78 E-value: 2.39e-88

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 652 DQSCTVATLPENKSKNRFTNVLPYDISRVKLAAQTGSD-LDYINANYIHGYGKKnKQYIAAQGPLPSTVSDFWRMVWEQK 730
Cdd:cd14614     1 DIPHFAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEgSDYINANYIPGYNSP-QEYIATQGPLPETRNDFWKMVLQQK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 731 SSAIVMLTNCTEGGRIKCEHYWPVDDMPCLYGNLRVSVQSEQKESCWTRREFvvRNESTSEERGVTHFHFTAWPDHGVP- 809
Cdd:cd14614    80 SQIIVMLTQCNEKRRVKCDHYWPFTEEPVAYGDITVEMLSEEEQPDWAIREF--RVSYADEVQDVMHFNYTAWPDHGVPt 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 810 -KGTEELIQFRWIVRQHIETFPfsGPTVVHCSAGVGRTGTLIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQY 888
Cdd:cd14614   158 aNAAESILQFVQMVRQQAVKSK--GPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQY 235


                  ....*..
gi 1764596117 889 VFLHQCI 895
Cdd:cd14614   236 IFIHQCV 242

PTPc-N9

cd14543

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

635-892

1.51e-86

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: 278.09 E-value: 1.51e-86

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 635 QNRGFSEEYEDL---STVGTDQSctvATLPENKSKNRFTNVLPYDISRVKLAAQTGSDL-DYINANYIHGYGKKNKqYIA 710
Cdd:cd14543     1 QKRGIYEEYEDIrrePPAGTFLC---SLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERtDYINANFMDGYKQKNA-YIA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 711 AQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEGGRIKCEHYWPVDDMPCL-YGNLRVSVQSEQKESCWTRREFVVRNEST 789
Cdd:cd14543    77 TQGPLPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLrYGDLTVTNLSVENKEHYKKTTLEIHNTET 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 790 SEERGVTHFHFTAWPDHGVPKGTEELIQFRWIVRQHIET-----------FPFSGPTVVHCSAGVGRTGTLIALDLLLQQ 858
Cdd:cd14543   157 DESRQVTHFQFTSWPDFGVPSSAAALLDFLGEVRQQQALavkamgdrwkgHPPGPPIVVHCSAGIGRTGTFCTLDICLSQ 236

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1764596117 859 MDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLH 892
Cdd:cd14543   237 LEDVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCY 270

R5-PTPc-1

cd14549

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

692-892

5.01e-80

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: 258.05 E-value: 5.01e-80

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 692 YINANYIHGYgKKNKQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEGGRIKCEHYWPVDDMPClYGNLRVSVQSE 771
Cdd:cd14549     1 YINANYVDGY-NKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTET-YGNIQVTLLST 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 772 QKESCWTRREFVVRNE------STSEERGVTHFHFTAWPDHGVPKGTEELIQFrwiVRQHIETFP-FSGPTVVHCSAGVG 844
Cdd:cd14549    79 EVLATYTVRTFSLKNLklkkvkGRSSERVVYQYHYTQWPDHGVPDYTLPVLSF---VRKSSAANPpGAGPIVVHCSAGVG 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1764596117 845 RTGTLIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLH 892
Cdd:cd14549   156 RTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203

R-PTPc-G-1

cd17667

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

639-900

2.44e-77

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: 253.42 E-value: 2.44e-77

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 639 FSEEYEDLSTVGTDQSCTV--ATLPENKSKNRFTNVLPYDISRVKLAAQTGSDL---DYINANYIHGYGKKnKQYIAAQG 713
Cdd:cd17667     1 FSEDFEEVQRCTADMNITAehSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSkhsDYINANYVDGYNKA-KAYIATQG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 714 PLPSTVSDFWRMVWEQKSSAIVMLTNCTEGGRIKCEHYWPVDDMPcLYGNLRVSVQSEQKESCWTRREFVVRN------- 786
Cdd:cd17667    80 PLKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENSE-EYGNIIVTLKSTKIHACYTVRRFSIRNtkvkkgq 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 787 ----ESTSEERGVTHFHFTAWPDHGVPKGTEELIQFrwIVRQHIETFPFSGPTVVHCSAGVGRTGTLIALDLLLQQMDKE 862
Cdd:cd17667   159 kgnpKGRQNERTVIQYHYTQWPDMGVPEYALPVLTF--VRRSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDK 236

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1764596117 863 EVVSIADCVRCMRLSRPLMVQTQSQYVFLHQCIMDSLL 900
Cdd:cd17667   237 STVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAIL 274

PTPc-KIM

cd14547

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

667-893

5.60e-77

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: 250.39 E-value: 5.60e-77

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 667 NRFTNVLPYDISRVKL-AAQTGSDLDYINANYIHGYGKKNKQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEGgR 745
Cdd:cd14547     1 NRYKTILPNEHSRVCLpSVDDDPLSSYINANYIRGYDGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA-K 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 746 IKCEHYWPvDDMPCLYGNLRVSVQSEQKESCWTRREFVVRNEStsEERGVTHFHFTAWPDHGVPKGTEELIQFRWIVRQH 825
Cdd:cd14547    80 EKCAQYWP-EEENETYGDFEVTVQSVKETDGYTVRKLTLKYGG--EKRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEEA 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1764596117 826 IETFPFSGPTVVHCSAGVGRTGTLIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLHQ 893
Cdd:cd14547   157 RQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224

R-PTPc-F-1

cd14626

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

627-898

2.88e-75

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

Pssm-ID: 350474 [Multi-domain] Cd Length: 276 Bit Score: 248.03 E-value: 2.88e-75

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 627 HFSSMSCDQNRGFSEEYEDLSTvGTDQSCTVATLPENKSKNRFTNVLPYDISRVKLAAQTG-SDLDYINANYIHGYGKKN 705
Cdd:cd14626     6 NIERLKANDGLKFSQEYESIDP-GQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGvPGSDYINANYIDGYRKQN 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 706 KqYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEGGRIKCEHYWPVDDMPClYGNLRVSVQSEQKESCWTRREFVVR 785
Cdd:cd14626    85 A-YIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPIRGTET-YGMIQVTLLDTVELATYSVRTFALY 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 786 NESTSEERGVTHFHFTAWPDHGVPKGTEELIQFrwIVRQHIETFPFSGPTVVHCSAGVGRTGTLIALDLLLQQMDKEEVV 865
Cdd:cd14626   163 KNGSSEKREVRQFQFMAWPDHGVPEYPTPILAF--LRRVKACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTV 240

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1764596117 866 SIADCVRCMRLSRPLMVQTQSQYVFLHQCIMDS 898
Cdd:cd14626   241 DIYGHVTCMRSQRNYMVQTEDQYIFIHEALLEA 273

PTPc-N13

cd14597

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

662-896

3.35e-74

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: 243.58 E-value: 3.35e-74

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 662 ENKSKNRFTNVLPYDISRVKLaaqtGSDLDYINANYIH-GYGKKNKQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNC 740
Cdd:cd14597     2 ENRKKNRYKNILPYDTTRVPL----GDEGGYINASFIKmPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 741 TEGGRIKCEHYWP-VDDMPCLYGN-LRVSVQSEQKESCWTRREFVVRNESTSEERGVTHFHFTAWPDHGVPKGTEELIQF 818
Cdd:cd14597    78 VEGGKIKCQRYWPeILGKTTMVDNrLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLLTF 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1764596117 819 RWIVRqHIETfpfSGPTVVHCSAGVGRTGTLIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLHQCIM 896
Cdd:cd14597   158 ISYMR-HIHK---SGPIITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVIL 231

PTPc-N3

cd14600

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

656-896

5.72e-74

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: 244.37 E-value: 5.72e-74

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 656 TVATLPENKSKNRFTNVLPYDISRVKLaaqTGSDlDYINANY----IHGYGKKNKqYIAAQGPLPSTVSDFWRMVWEQKS 731
Cdd:cd14600    33 TCAKLPQNMDKNRYKDVLPYDATRVVL---QGNE-DYINASYvnmeIPSANIVNK-YIATQGPLPHTCAQFWQVVWEQKL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 732 SAIVMLTNCTEGGRIKCEHYWPvdDMP--CLYGNLRVSVQSEQKESCWTRREFVVRNESTSEERGVTHFHFTAWPDHGVP 809
Cdd:cd14600   108 SLIVMLTTLTERGRTKCHQYWP--DPPdvMEYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVP 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 810 KGTEELIQFRWIVRQ-HIEtfpfSGPTVVHCSAGVGRTGTLIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQY 888
Cdd:cd14600   186 DDSSDFLEFVNYVRSkRVE----NEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQY 261


                  ....*...
gi 1764596117 889 VFLHQCIM 896
Cdd:cd14600   262 KFVCEAIL 269

PTPc-N3_4

cd14541

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

691-895

6.36e-73

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: 239.15 E-value: 6.36e-73

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 691 DYINANY----IHGYGKKNKqYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEGGRIKCEHYWPVDDMPCLYGNLRV 766
Cdd:cd14541     1 DYINANYvnmeIPGSGIVNR-YIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETMQFGNLQI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 767 SVQSEQKESCWTRREFVVRNESTSEERGVTHFHFTAWPDHGVPKGTEELIQFRWIVRQHIETfpFSGPTVVHCSAGVGRT 846
Cdd:cd14541    80 TCVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVG--MVEPTVVHCSAGIGRT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1764596117 847 GTLIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLHQCI 895
Cdd:cd14541   158 GVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAI 206

R-PTP-LAR-2

cd14554

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

658-893

1.12e-72

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

Pssm-ID: 350402 [Multi-domain] Cd Length: 238 Bit Score: 239.35 E-value: 1.12e-72

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 658 ATLPENKSKNRFTNVLPYDISRVKLAAQTGSD-LDYINANYIHGYgKKNKQYIAAQGPLPSTVSDFWRMVWEQKSSAIVM 736
Cdd:cd14554     1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEgSDYINASFIDGY-RQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 737 LTNCTEGGRIKCEHYWPVDdMPCLYGNLRVSVQSEQKESCWTRREFVVRNESTSEERGVTHFHFTAWPDHGVPKGTEELI 816
Cdd:cd14554    80 LTKLREMGREKCHQYWPAE-RSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFI 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1764596117 817 QFRWIVRQHIETFPFSGPTVVHCSAGVGRTGTLIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLHQ 893
Cdd:cd14554   159 DFIGQVHKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYR 235

R-PTPc-A-1

cd14621

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

612-900

1.94e-72

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

Pssm-ID: 350469 [Multi-domain] Cd Length: 296 Bit Score: 241.08 E-value: 1.94e-72

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 612 SSNKYKPIHLKKFPMHFSSMSCDQNRGFSEEYEDLSTVGTDQSCTVATLPENKSKNRFTNVLPYDISRVKLAAQTG-SDL 690
Cdd:cd14621     1 TNRKYPPLPVDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGvPDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 691 DYINANYIHGYGKKNKqYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEGGRIKCEHYWPvdDMPC-LYGNLRVSVQ 769
Cdd:cd14621    81 DYINASFINGYQEKNK-FIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWP--DQGCwTYGNIRVSVE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 770 SEQKESCWTRREFVVRN----ESTSEERGVTHFHFTAWPDHGVPKGTEELIQFRWIVRQHIETFpfSGPTVVHCSAGVGR 845
Cdd:cd14621   158 DVTVLVDYTVRKFCIQQvgdvTNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCNPQY--AGAIVVHCSAGVGR 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1764596117 846 TGTLIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLHQCIMDSLL 900
Cdd:cd14621   236 TGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYL 290

PTPc-N20_13

cd14538

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

692-899

4.60e-72

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: 236.50 E-value: 4.60e-72

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 692 YINANYIH-GYGKKNKQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEGGRIKCEHYWP--VDDMPCLYGNLRVSV 768
Cdd:cd14538     1 YINASHIRiPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPdsLNKPLICGGRLEVSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 769 QSEQKESCWTRREFVVRNESTSEERGVTHFHFTAWPDHGVPKGTEELIQFRWIVRqHIETfpfSGPTVVHCSAGVGRTGT 848
Cdd:cd14538    81 EKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMR-RIHN---SGPIVVHCSAGIGRTGV 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1764596117 849 LIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLHQCIMDSL 899
Cdd:cd14538   157 LITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207

R-PTPc-M-1

cd14633

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

627-900

9.04e-71

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: 235.71 E-value: 9.04e-71

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 627 HFSSMSCDQNRGFSEEYEDLSTvGTDQSCTVATLPENKSKNRFTNVLPYDISRVKLAAQTG-SDLDYINANYIHGYGKKN 705
Cdd:cd14633     5 HITQMKCAEGYGFKEEYESFFE-GQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGeTSSDYINGNYIDGYHRPN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 706 kQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEGGRIKCEHYWPVDDMpcLYGNLRVSVQSEQKESCWTRREFVVR 785
Cdd:cd14633    84 -HYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTE--IYKDIKVTLIETELLAEYVIRTFAVE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 786 NESTSEERGVTHFHFTAWPDHGVPKGTEELIQFrwIVRQHIETFPFSGPTVVHCSAGVGRTGTLIALDLLLQQMDKEEVV 865
Cdd:cd14633   161 KRGVHEIREIRQFHFTGWPDHGVPYHATGLLGF--VRQVKSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREGVV 238

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1764596117 866 SIADCVRCMRLSRPLMVQTQSQYVFLHQCIMDSLL 900
Cdd:cd14633   239 DIYNCVRELRSRRVNMVQTEEQYVFIHDAILEACL 273

PTP_fungal

cd18533

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

692-893

1.07e-69

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: 230.21 E-value: 1.07e-69

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 692 YINANYIHGYGKKNKQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEGGRIKCEHYWPVDDMPCLYGNLRVSVQSE 771
Cdd:cd18533     1 YINASYITLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEYGDLTVELVSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 772 QK--ESCWTRREFVVRNEsTSEERGVTHFHFTAWPDHGVPKGTEELIQFRWIVRQHIETFPFSGPTVVHCSAGVGRTGTL 849
Cdd:cd18533    81 EEndDGGFIVREFELSKE-DGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSASLDPPIIVHCSAGVGRTGTF 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1764596117 850 IALDLLLQQMDKEEVVS---------IADCVRCMRLSRPLMVQTQSQYVFLHQ 893
Cdd:cd18533   160 IALDSLLDELKRGLSDSqdledsedpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212

R-PTPc-D-1

cd14624

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

616-899

1.49e-68

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: 230.00 E-value: 1.49e-68

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 616 YKPIHLKKFPMHFSSMSCDQNRGFSEEYEDLSTvGTDQSCTVATLPENKSKNRFTNVLPYDISRVKLAAQTG-SDLDYIN 694
Cdd:cd14624     1 HPPIPILELADHIERLKANDNLKFSQEYESIDP-GQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGiPGSDYIN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 695 ANYIHGYGKKNKqYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEGGRIKCEHYWPVDDMPClYGNLRVSVQSEQKE 774
Cdd:cd14624    80 ANYIDGYRKQNA-YIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRGTET-YGLIQVTLLDTVEL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 775 SCWTRREFVVRNESTSEERGVTHFHFTAWPDHGVPKGTEELIQFrwIVRQHIETFPFSGPTVVHCSAGVGRTGTLIALDL 854
Cdd:cd14624   158 ATYCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAF--LRRVKTCNPPDAGPMVVHCSAGVGRTGCFIVIDA 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1764596117 855 LLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLHQCIMDSL 899
Cdd:cd14624   236 MLERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAV 280

R-PTPc-T-1

cd14630

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

662-900

2.13e-68

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: 227.60 E-value: 2.13e-68

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 662 ENKSKNRFTNVLPYDISRVKLAAQTGS-DLDYINANYIHGYgKKNKQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNC 740
Cdd:cd14630     2 ENRNKNRYGNIISYDHSRVRLQLLDGDpHSDYINANYIDGY-HRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 741 TEGGRIKCEHYWPvDDMPcLYGNLRVSVQSEQKESCWTRREFVVRNESTSEERGVTHFHFTAWPDHGVPKGTEELIQFrw 820
Cdd:cd14630    81 VEVGRVKCVRYWP-DDTE-VYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGF-- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 821 iVRQ-HIETFPFSGPTVVHCSAGVGRTGTLIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLHQCIMDSL 899
Cdd:cd14630   157 -VRQvKFLNPPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAILEAC 235


                  .
gi 1764596117 900 L 900
Cdd:cd14630   236 L 236

R-PTPc-S-1

cd14625

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

616-899

8.96e-68

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: 227.67 E-value: 8.96e-68

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 616 YKPIHLKKFPMHFSSMSCDQNRGFSEEYEDLSTvGTDQSCTVATLPENKSKNRFTNVLPYDISRVKLAAQTG-SDLDYIN 694
Cdd:cd14625     1 HPPIPISELAEHTERLKANDNLKLSQEYESIDP-GQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGiMGSDYIN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 695 ANYIHGYGKKNKqYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEGGRIKCEHYWPVDDMPClYGNLRVSVQSEQKE 774
Cdd:cd14625    80 ANYIDGYRKQNA-YIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWPSRGTET-YGMIQVTLLDTIEL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 775 SCWTRREFVVRNESTSEERGVTHFHFTAWPDHGVPKGTEELIQFrwIVRQHIETFPFSGPTVVHCSAGVGRTGTLIALDL 854
Cdd:cd14625   158 ATFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAF--LRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDA 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1764596117 855 LLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLHQCIMDSL 899
Cdd:cd14625   236 MLERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAV 280

R-PTPc-Q

cd14616

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

667-893

1.51e-67

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: 224.79 E-value: 1.51e-67

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 667 NRFTNVLPYDISRVKLAAQTGS-DLDYINANYIHGYGKKNkQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEGGR 745
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAGVpGSDYINASYISGYLCPN-EFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 746 IKCEHYWPVDDMP-CLYGNLRVSVQSEQKESCWTRREFVVrnESTSEERGVTHFHFTAWPDHGVPKGTEELIQFRWIVRQ 824
Cdd:cd14616    80 IRCHQYWPEDNKPvTVFGDIVITKLMEDVQIDWTIRDLKI--ERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVRA 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1764596117 825 HIETfpFSGPTVVHCSAGVGRTGTLIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLHQ 893
Cdd:cd14616   158 SRAH--DNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224

R-PTPc-C-1

cd14557

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

692-893

1.03e-66

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: 221.62 E-value: 1.03e-66

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 692 YINANYIHGYgKKNKQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEGGRIKCEHYWP-VDDMPCLYGNLRVSVQS 770
Cdd:cd14557     1 YINASYIDGF-KEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPsMEEGSRAFGDVVVKINE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 771 EQKESCWTRREFVVRNE-STSEERGVTHFHFTAWPDHGVPKGTEELIQfrwiVRQHIETFP--FSGPTVVHCSAGVGRTG 847
Cdd:cd14557    80 EKICPDYIIRKLNINNKkEKGSGREVTHIQFTSWPDHGVPEDPHLLLK----LRRRVNAFNnfFSGPIVVHCSAGVGRTG 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1764596117 848 TLIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLHQ 893
Cdd:cd14557   156 TYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201

PTPc-N11_6

cd14544

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

663-895

1.72e-65

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: 220.41 E-value: 1.72e-65

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 663 NKSKNRFTNVLPYDISRVKL----AAQTGSDldYINANYIH------GYGKKNKQYIAAQGPLPSTVSDFWRMVWEQKSS 732
Cdd:cd14544     1 NKGKNRYKNILPFDHTRVILkdrdPNVPGSD--YINANYIRnenegpTTDENAKTYIATQGCLENTVSDFWSMVWQENSR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 733 AIVMLTNCTEGGRIKCEHYWPVDDMPCLYGNLRVSVQSEQKESCWTRREFVV-RNESTSEERGVTHFHFTAWPDHGVPKG 811
Cdd:cd14544    79 VIVMTTKEVERGKNKCVRYWPDEGMQKQYGPYRVQNVSEHDTTDYTLRELQVsKLDQGDPIREIWHYQYLSWPDHGVPSD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 812 TEELIQFRWIVRQHIETFPFSGPTVVHCSAGVGRTGTLIALDLLLQQMDKEEV---VSIADCVRCMRLSRPLMVQTQSQY 888
Cdd:cd14544   159 PGGVLNFLEDVNQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGLdcdIDIQKTIQMVRSQRSGMVQTEAQY 238


                  ....*..
gi 1764596117 889 VFLHQCI 895
Cdd:cd14544   239 KFIYVAV 245

R-PTPc-typeIIb-1

cd14555

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

692-900

1.08e-64

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: 216.32 E-value: 1.08e-64

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 692 YINANYIHGYGKKNkQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEGGRIKCEHYWPVDDMpcLYGNLRVSVQSE 771
Cdd:cd14555     1 YINANYIDGYHRPN-HYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTE--VYGDIKVTLVET 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 772 QKESCWTRREFVVRNESTSEERGVTHFHFTAWPDHGVPKGTEELIQFrwIVRQHIETFPFSGPTVVHCSAGVGRTGTLIA 851
Cdd:cd14555    78 EPLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGF--IRRVKASNPPSAGPIVVHCSAGAGRTGCYIV 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1764596117 852 LDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLHQCIMDSLL 900
Cdd:cd14555   156 IDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAILEACL 204

PTPc-N1_2

cd14545

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

666-890

1.11e-64

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

Pssm-ID: 350393 [Multi-domain] Cd Length: 231 Bit Score: 217.26 E-value: 1.11e-64

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 666 KNRFTNVLPYDISRVKLAAQTGsDLDYINANYIHgYGKKNKQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEGGR 745
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKLKQG-DNDYINASLVE-VEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 746 IKCEHYWP---VDDMPCLYGNLRVSVQSEQKESCWTRREFVVRNESTSEERGVTHFHFTAWPDHGVPKGTEELIQFRWIV 822
Cdd:cd14545    79 IKCAQYWPqgeGNAMIFEDTGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQKV 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 823 RQHIETFPFSGPTVVHCSAGVGRTGTLIALDLLLQQMDKEEV--VSIADCVRCMRLSRPLMVQTQSQYVF 890
Cdd:cd14545   159 RESGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPssVDVKKVLLEMRKYRMGLIQTPDQLRF 228

PTPc-N1

cd14608

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

643-897

1.64e-64

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: 218.74 E-value: 1.64e-64

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 643 YEDLSTVGTDQSCTVATLPENKSKNRFTNVLPYDISRVKLAAQtgsDLDYINANYIHgYGKKNKQYIAAQGPLPSTVSDF 722
Cdd:cd14608     5 YQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQE---DNDYINASLIK-MEEAQRSYILTQGPLPNTCGHF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 723 WRMVWEQKSSAIVMLTNCTEGGRIKCEHYWPV-DDMPCLY--GNLRVSVQSEQKESCWTRREFVVRNESTSEERGVTHFH 799
Cdd:cd14608    81 WEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQkEEKEMIFedTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 800 FTAWPDHGVPKGTEELIQFRWIVRQHIETFPFSGPTVVHCSAGVGRTGTLIALDLLLQQMDKEE---VVSIADCVRCMRL 876
Cdd:cd14608   161 YTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKdpsSVDIKKVLLEMRK 240

                         250       260
                  ....*....|....*....|.
gi 1764596117 877 SRPLMVQTQSQYVFLHQCIMD 897
Cdd:cd14608   241 FRMGLIQTADQLRFSYLAVIE 261

PTPc-N7

cd14612

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

660-892

5.07e-64

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

Pssm-ID: 350460 [Multi-domain] Cd Length: 247 Bit Score: 216.24 E-value: 5.07e-64

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 660 LPENKSKNRFTNVLPYDISRVKL--AAQTGSDLDYINANYIHGYGKKNKQYIAAQGPLPSTVSDFWRMVWEQKSSAIVML 737
Cdd:cd14612    12 IPGHASKDRYKTILPNPQSRVCLrrAGSQEEEGSYINANYIRGYDGKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMI 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 738 TNCTEGGRiKCEHYWPVDDMPclYGNLRVSVQSEQKESCWTRREFVVRNEStsEERGVTHFHFTAWPDHGVPKGTEELIQ 817
Cdd:cd14612    92 TKLKEKKE-KCVHYWPEKEGT--YGRFEIRVQDMKECDGYTIRDLTIQLEE--ESRSVKHYWFSSWPDHQTPESAGPLLR 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1764596117 818 FRWIVRQHIETFPFSGPTVVHCSAGVGRTGTLIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLH 892
Cdd:cd14612   167 LVAEVEESRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLH 241

R-PTPc-E-1

cd14620

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

669-897

9.17e-64

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: 214.80 E-value: 9.17e-64

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 669 FTNVLPYDISRVKLAAQTGSDL-DYINANYIHGYGKKNKqYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEGGRIK 747
Cdd:cd14620     1 YPNILPYDHSRVILSQLDGIPCsDYINASYIDGYKEKNK-FIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 748 CEHYWPvdDMPC-LYGNLRVSVQSEQKESCWTRREFVVRNESTSE---ERGVTHFHFTAWPDHGVPKGTEELIQFRWIVR 823
Cdd:cd14620    80 CYQYWP--DQGCwTYGNIRVAVEDCVVLVDYTIRKFCIQPQLPDGckaPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVK 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1764596117 824 QHIETfpFSGPTVVHCSAGVGRTGTLIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLHQCIMD 897
Cdd:cd14620   158 SVNPV--HAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALLE 229

R-PTP-S-2

cd14627

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

658-899

2.29e-62

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

Pssm-ID: 350475 [Multi-domain] Cd Length: 290 Bit Score: 213.06 E-value: 2.29e-62

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 658 ATLPENKSKNRFTNVLPYDISRVKLAAQTGSD-LDYINANYIHGYgKKNKQYIAAQGPLPSTVSDFWRMVWEQKSSAIVM 736
Cdd:cd14627    48 ANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEgSDYINASFIDGY-RQQKAYIATQGPLAETTEDFWRMLWENNSTIVVM 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 737 LTNCTEGGRIKCEHYWPVDdMPCLYGNLRVSVQSEQKESCWTRREFVVRNESTSEERGVTHFHFTAWPDHGVPKGTEELI 816
Cdd:cd14627   127 LTKLREMGREKCHQYWPAE-RSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFI 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 817 QFRWIVRQHIETFPFSGPTVVHCSAGVGRTGTLIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLHQCIM 896
Cdd:cd14627   206 DFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAAL 285


                  ...
gi 1764596117 897 DSL 899
Cdd:cd14627   286 EYL 288

R-PTP-D-2

cd14628

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

638-899

4.56e-62

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

Pssm-ID: 350476 [Multi-domain] Cd Length: 292 Bit Score: 212.28 E-value: 4.56e-62

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 638 GFSEEYEDLSTVGTDQSCTV-ATLPENKSKNRFTNVLPYDISRVKLAAQTGSD-LDYINANYIHGYgKKNKQYIAAQGPL 715
Cdd:cd14628    26 GMELEFKRLASSKAHTSRFIsANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEgSDYINASFIDGY-RQQKAYIATQGPL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 716 PSTVSDFWRMVWEQKSSAIVMLTNCTEGGRIKCEHYWPVDdMPCLYGNLRVSVQSEQKESCWTRREFVVRNESTSEERGV 795
Cdd:cd14628   105 AETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAE-RSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTV 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 796 THFHFTAWPDHGVPKGTEELIQFRWIVRQHIETFPFSGPTVVHCSAGVGRTGTLIALDLLLQQMDKEEVVSIADCVRCMR 875
Cdd:cd14628   184 RQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLR 263

                         250       260
                  ....*....|....*....|....
gi 1764596117 876 LSRPLMVQTQSQYVFLHQCIMDSL 899
Cdd:cd14628   264 TQRPAMVQTEDQYQFCYRAALEYL 287

R-PTPc-A-E-1

cd14551

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

692-893

7.33e-62

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: 208.23 E-value: 7.33e-62

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 692 YINANYIHGYGKKNKqYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEGGRIKCEHYWPvdDMPC-LYGNLRVSVQS 770
Cdd:cd14551     1 YINASYIDGYQEKNK-FIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWP--DQGCwTYGNLRVRVED 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 771 EQKESCWTRREFVVR--NESTSEE--RGVTHFHFTAWPDHGVPKGTEELIQFRWIVRQHIEtfPFSGPTVVHCSAGVGRT 846
Cdd:cd14551    78 TVVLVDYTTRKFCIQkvNRGIGEKrvRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSANP--PRAGPIVVHCSAGVGRT 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1764596117 847 GTLIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLHQ 893
Cdd:cd14551   156 GTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202

R-PTPc-K-1

cd14631

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

691-900

1.06e-61

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: 208.72 E-value: 1.06e-61

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 691 DYINANYIHGYgKKNKQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEGGRIKCEHYWPVDDMpcLYGNLRVSVQS 770
Cdd:cd14631    14 DYINANYIDGY-QRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTE--VYGDFKVTCVE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 771 EQKESCWTRREFVVRNESTSEERGVTHFHFTAWPDHGVPKGTEELIQFrwIVRQHIETFPFSGPTVVHCSAGVGRTGTLI 850
Cdd:cd14631    91 MEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSF--IRRVKLSNPPSAGPIVVHCSAGAGRTGCYI 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1764596117 851 ALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLHQCIMDSLL 900
Cdd:cd14631   169 VIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACL 218

R-PTPc-U-1

cd14632

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

692-900

2.41e-61

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: 207.21 E-value: 2.41e-61

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 692 YINANYIHGYGKKNkQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEGGRIKCEHYWPvdDMPCLYGNLRVSVQSE 771
Cdd:cd14632     1 YINANYIDGYHRSN-HFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWP--DDSDTYGDIKITLLKT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 772 QKESCWTRREFVVRNESTSEERGVTHFHFTAWPDHGVPKGTEELIQFrwIVRQHIETFPFSGPTVVHCSAGVGRTGTLIA 851
Cdd:cd14632    78 ETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAF--IRRVKASTPPDAGPVVVHCSAGAGRTGCYIV 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1764596117 852 LDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLHQCIMDSLL 900
Cdd:cd14632   156 LDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAILEACL 204

PTPc-N18

cd14603

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

652-895

2.53e-61

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

Pssm-ID: 350451 [Multi-domain] Cd Length: 266 Bit Score: 209.30 E-value: 2.53e-61

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 652 DQSCT--VATLPENKSKNRFTNVLPYDISRVKLA-AQTGSDLDYINANYIHGYgKKNKQYIAAQGPLPSTVSDFWRMVWE 728
Cdd:cd14603    17 DYVCStvAGGRKENVKKNRYKDILPYDQTRVILSlLQEEGHSDYINANFIKGV-DGSRAYIATQGPLSHTVLDFWRMIWQ 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 729 QKSSAIVMLTNCTEGGRIKCEHYWPVDDMPCLYGNLRVSVQSEQkescWTRREFVVRNESTS---EERGVTHFHFTAWPD 805
Cdd:cd14603    96 YGVKVILMACREIEMGKKKCERYWAQEQEPLQTGPFTITLVKEK----RLNEEVILRTLKVTfqkESRSVSHFQYMAWPD 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 806 HGVPKGTEELIQFRWIVRQHIETFPFsgPTVVHCSAGVGRTGTLIALD----LLLQQMDKEEvVSIADCVRCMRLSRPLM 881
Cdd:cd14603   172 HGIPDSPDCMLAMIELARRLQGSGPE--PLCVHCSAGCGRTGVICTVDyvrqLLLTQRIPPD-FSIFDVVLEMRKQRPAA 248

                         250
                  ....*....|....
gi 1764596117 882 VQTQSQYVFLHQCI 895
Cdd:cd14603   249 VQTEEQYEFLYHTV 262

R-PTP-F-2

cd14629

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

658-899

6.86e-61

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

Pssm-ID: 350477 [Multi-domain] Cd Length: 291 Bit Score: 209.20 E-value: 6.86e-61

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 658 ATLPENKSKNRFTNVLPYDISRVKLAAQTGSD-LDYINANYIHGYgKKNKQYIAAQGPLPSTVSDFWRMVWEQKSSAIVM 736
Cdd:cd14629    48 ANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEgSDYINASFIDGY-RQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVM 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 737 LTNCTEGGRIKCEHYWPVDdMPCLYGNLRVSVQSEQKESCWTRREFVVRNESTSEERGVTHFHFTAWPDHGVPKGTEELI 816
Cdd:cd14629   127 LTKLREMGREKCHQYWPAE-RSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFI 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 817 QFRWIVRQHIETFPFSGPTVVHCSAGVGRTGTLIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLHQCIM 896
Cdd:cd14629   206 DFIGQVHKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAAL 285


                  ...
gi 1764596117 897 DSL 899
Cdd:cd14629   286 EYL 288

PTPc-N22_18_12

cd14542

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

692-893

4.97e-60

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: 203.42 E-value: 4.97e-60

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 692 YINANYIHGyGKKNKQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEGGRIKCEHYWPVD-DMPCLYGNLRVSVQS 770
Cdd:cd14542     1 YINANFIKG-VSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEgEEQLQFGPFKISLEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 771 EQkescWTRREFVVRN---ESTSEERGVTHFHFTAWPDHGVPKGTEELIQFRWIVRQHIETFPFsgPTVVHCSAGVGRTG 847
Cdd:cd14542    80 EK----RVGPDFLIRTlkvTFQKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDV--PICVHCSAGCGRTG 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1764596117 848 TLIALD----LLLQQMDKEEvVSIADCVRCMRLSRPLMVQTQSQYVFLHQ 893
Cdd:cd14542   154 TICAIDyvwnLLKTGKIPEE-FSLFDLVREMRKQRPAMVQTKEQYELVYR 202

R-PTPc-Z-1

cd17668

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

692-896

6.08e-60

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: 203.29 E-value: 6.08e-60

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 692 YINANYIHGYGKKnKQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEGGRIKCEHYWPVDDMPcLYGNLRVSVQSE 771
Cdd:cd17668     1 YINANYVDGYNKP-KAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSE-EYGNFLVTQKSV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 772 QKESCWTRREFVVRN--------ESTSEERGVTHFHFTAWPDHGVPKGTEELIQFrwiVRQHIET-FPFSGPTVVHCSAG 842
Cdd:cd17668    79 QVLAYYTVRNFTLRNtkikkgsqKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTF---VRKASYAkRHAVGPVVVHCSAG 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1764596117 843 VGRTGTLIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLHQCIM 896
Cdd:cd17668   156 VGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209

R-PTP-N2

cd14610

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

634-890

7.87e-60

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: 205.68 E-value: 7.87e-60

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 634 DQNRgFSEEYEDLSTVGTD-QSCTVATLPENKSKNRFTNVLPYDISRVKLAAQTGSDL-DYINANYIHGYGKKNKQYIAA 711
Cdd:cd14610    15 NKNR-LEKEWEALCAYQAEpNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHsDYINASPIMDHDPRNPAYIAT 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 712 QGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEGGRIKCEHYWPvDDMPCLYGNLRVSVQSEQkesCWTR----REFVVRNE 787
Cdd:cd14610    94 QGPLPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWP-DEGSNLYHIYEVNLVSEH---IWCEdflvRSFYLKNL 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 788 STSEERGVTHFHFTAWPDHGVPKGTEELIQFRWIVRQHIETfpFSGPTVVHCSAGVGRTGTLIALDLLLQQMDK-EEVVS 866
Cdd:cd14610   170 QTNETRTVTQFHFLSWNDQGVPASTRSLLDFRRKVNKCYRG--RSCPIIVHCSDGAGRSGTYILIDMVLNKMAKgAKEID 247

                         250       260
                  ....*....|....*....|....
gi 1764596117 867 IADCVRCMRLSRPLMVQTQSQYVF 890
Cdd:cd14610   248 IAATLEHLRDQRPGMVQTKEQFEF 271

PTPc-N6

cd14606

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

661-895

6.94e-59

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: 202.42 E-value: 6.94e-59

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 661 PENKSKNRFTNVLPYDISRVKLAAQ----TGSDldYINANYIH----GYGKKNKQYIAAQGPLPSTVSDFWRMVWEQKSS 732
Cdd:cd14606    16 PENKSKNRYKNILPFDHSRVILQGRdsniPGSD--YINANYVKnqllGPDENAKTYIASQGCLEATVNDFWQMAWQENSR 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 733 AIVMLTNCTEGGRIKCEHYWPVDDMPCLYGNLRVSVQSEQKESCWTRREFVVRNESTSEE-RGVTHFHFTAWPDHGVPKG 811
Cdd:cd14606    94 VIVMTTREVEKGRNKCVPYWPEVGMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGELiREIWHYQYLSWPDHGVPSE 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 812 TEELIQFRWIVRQHIETFPFSGPTVVHCSAGVGRTGTLIALDLLLQQMDKEEV---VSIADCVRCMRLSRPLMVQTQSQY 888
Cdd:cd14606   174 PGGVLSFLDQINQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKGLdcdIDIQKTIQMVRAQRSGMVQTEAQY 253


                  ....*..
gi 1764596117 889 VFLHQCI 895
Cdd:cd14606   254 KFIYVAI 260

PTPc-N20

cd14596

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

692-899

7.63e-59

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: 200.36 E-value: 7.63e-59

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 692 YINANYIH-GYGKKNKQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEGGRIKCEHYWPVD-DMPCLYGNLRVSVQ 769
Cdd:cd14596     1 YINASYITmPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETlQEPMELENYQLRLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 770 SEQKESCWTRREFVVRNESTSEERGVTHFHFTAWPDHGVPKGTEELIQF-RWIVRQHIEtfpfsGPTVVHCSAGVGRTGT 848
Cdd:cd14596    81 NYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFiCYMRKVHNT-----GPIVVHCSAGIGRAGV 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1764596117 849 LIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLHQCIMDSL 899
Cdd:cd14596   156 LICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVL 206

PTPc-N4

cd14601

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

691-896

2.63e-58

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: 199.02 E-value: 2.63e-58

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 691 DYINANYIH----GYGKKNkQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEGGRIKCEHYWPVDDMPCLYGNLRV 766
Cdd:cd14601     1 DYINANYINmeipSSSIIN-RYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSSSYGGFQV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 767 SVQSEQKESCWTRREFVVRNESTSEERGVTHFHFTAWPDHGVPKGTEELIQFRWIVRQHIETFPfsGPTVVHCSAGVGRT 846
Cdd:cd14601    80 TCHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKD--EPVVVHCSAGIGRT 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1764596117 847 GTLIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLHQCIM 896
Cdd:cd14601   158 GVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAIL 207

PTPc-N5

cd14613

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

666-892

5.98e-58

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

Pssm-ID: 350461 [Multi-domain] Cd Length: 258 Bit Score: 199.70 E-value: 5.98e-58

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 666 KNRFTNVLPYDISRVKLAAQTGSDL--DYINANYIHGYGKKNKQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEG 743
Cdd:cd14613    28 KNRYKTILPNPHSRVCLTSPDQDDPlsSYINANYIRGYGGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 744 GRiKCEHYWPVDDMpcLYGNLRVSVQSEQKESCWTRREFVVRneSTSEERGVTHFHFTAWPDHGVPKGTEELIQFRWIV- 822
Cdd:cd14613   108 NE-KCTEYWPEEQV--TYEGIEITVKQVIHADDYRLRLITLK--SGGEERGLKHYWYTSWPDQKTPDNAPPLLQLVQEVe 182

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1764596117 823 --RQHIEtfPFSGPTVVHCSAGVGRTGTLIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLH 892
Cdd:cd14613   183 eaRQQAE--PNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVH 252

PTPc-N12

cd14604

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

662-895

3.51e-57

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: 199.00 E-value: 3.51e-57

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 662 ENKSKNRFTNVLPYDISRVKLAAQTGS-DLDYINANYIHG-YGKKnkQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTN 739
Cdd:cd14604    56 ENVKKNRYKDILPFDHSRVKLTLKTSSqDSDYINANFIKGvYGPK--AYIATQGPLANTVIDFWRMIWEYNVAIIVMACR 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 740 CTEGGRIKCEHYWPV-DDMPCLYGNLRVSVQSEQkescwTRREFVVRN---ESTSEERGVTHFHFTAWPDHGVPKGTEEL 815
Cdd:cd14604   134 EFEMGRKKCERYWPLyGEEPMTFGPFRISCEAEQ-----ARTDYFIRTlllEFQNETRRLYQFHYVNWPDHDVPSSFDSI 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 816 IQFRWIVRQHIETFPFsgPTVVHCSAGVGRTGTLIALDL---LLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLH 892
Cdd:cd14604   209 LDMISLMRKYQEHEDV--PICIHCSAGCGRTGAICAIDYtwnLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVH 286


                  ...
gi 1764596117 893 QCI 895
Cdd:cd14604   287 RAI 289

PTPc-N2

cd14607

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

643-895

7.71e-57

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: 196.34 E-value: 7.71e-57

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 643 YEDLSTVGTDQSCTVATLPENKSKNRFTNVLPYDISRVKLaaqTGSDLDYINANYIHgYGKKNKQYIAAQGPLPSTVSDF 722
Cdd:cd14607     4 YLEIRNESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKL---QNTENDYINASLVV-IEEAQRSYILTQGPLPNTCCHF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 723 WRMVWEQKSSAIVMLTNCTEGGRIKCEHYWPVDDMPCLY---GNLRVSVQSEQKESCWTRREFVVRNESTSEERGVTHFH 799
Cdd:cd14607    80 WLMVWQQKTKAVVMLNRIVEKDSVKCAQYWPTDEEEVLSfkeTGFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFH 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 800 FTAWPDHGVPKGTEELIQFRWIVRQHIETFPFSGPTVVHCSAGVGRTGTLIALDLLLQQMDKEE--VVSIADCVRCMRLS 877
Cdd:cd14607   160 YTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRKY 239

                         250
                  ....*....|....*...
gi 1764596117 878 RPLMVQTQSQYVFLHQCI 895
Cdd:cd14607   240 RMGLIQTPDQLRFSYMAV 257

R-PTP-C-2

cd14558

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

692-892

1.15e-56

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: 194.15 E-value: 1.15e-56

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 692 YINANYIHGYgKKNKQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEGGRIKCEHYWPVDDMPclYGNLRVSVQSE 771
Cdd:cd14558     1 YINASFIDGY-WGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKT--YGDIEVELKDT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 772 QKESCWTRREFVVRNESTSEERGVTHFHFTAWPDHGVPKGTEELIQFRWIVRQHIETFP----FSGPTVVHCSAGVGRTG 847
Cdd:cd14558    78 EKSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKQKLPYKNskhgRSVPIVVHCSDGSSRTG 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1764596117 848 TLIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLH 892
Cdd:cd14558   158 IFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202

R-PTPc-R

cd14611

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

665-893

1.64e-56

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: 194.37 E-value: 1.64e-56

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 665 SKNRFTNVLPYDISRVKLAAQTGSDL--DYINANYIHGYGKKNKQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTE 742
Cdd:cd14611     1 TKNRYKTILPNPHSRVCLKPKNSNDSlsTYINANYIRGYGGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 743 GGRiKCEHYWPvdDMPCLYGNLRVSVQSEQKESCWTRREFVVRNESTSeeRGVTHFHFTAWPDHGVPKGTEELIQFRWIV 822
Cdd:cd14611    81 KNE-KCVLYWP--EKRGIYGKVEVLVNSVKECDNYTIRNLTLKQGSQS--RSVKHYWYTSWPDHKTPDSAQPLLQLMLDV 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1764596117 823 RQHIETFPFSGPTVVHCSAGVGRTGTLIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLHQ 893
Cdd:cd14611   156 EEDRLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVHH 226

PTPc-N22

cd14602

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

666-897

2.22e-56

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: 194.29 E-value: 2.22e-56

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 666 KNRFTNVLPYDISRVKLAAQTG-SDLDYINANYIHG-YGKKnkQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEG 743
Cdd:cd14602     1 KNRYKDILPYDHSRVELSLITSdEDSDYINANFIKGvYGPR--AYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 744 GRIKCEHYWP-VDDMPCLYGNLRVSVQSEQKESCWTRRefVVRNESTSEERGVTHFHFTAWPDHGVPKGTEELIQFRWIV 822
Cdd:cd14602    79 GKKKCERYWAePGEMQLEFGPFSVTCEAEKRKSDYIIR--TLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 823 R--QHIEtfpfSGPTVVHCSAGVGRTGTLIALD---LLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLHQCIMD 897
Cdd:cd14602   157 RcyQEDD----SVPICIHCSAGCGRTGVICAIDytwMLLKDGIIPENFSVFSLIQEMRTQRPSLVQTKEQYELVYNAVIE 232

R-PTPc-A-2

cd14623

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

668-897

2.54e-56

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: 194.11 E-value: 2.54e-56

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 668 RFTNVLPYDISRVKLAAQTGSD-LDYINANYIHGYgKKNKQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEGGRI 746
Cdd:cd14623     1 RVLQIIPYEFNRVIIPVKRGEEnTDYVNASFIDGY-RQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 747 KCEHYWPVDDMpCLYGNLRVSVQSEQKESCWTRREFVVRNESTSEERGVTHFHFTAWPDHGVPKGTEELIQFRWIVRQHI 826
Cdd:cd14623    80 KCAQYWPSDGS-VSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQ 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1764596117 827 ETfpfSG--PTVVHCSAGVGRTGTLIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLHQCIMD 897
Cdd:cd14623   159 QQ---SGnhPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228

PTPc-N21_14

cd14540

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

692-893

5.00e-56

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: 192.67 E-value: 5.00e-56

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 692 YINANYIH-GYGKKNKQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEGGRIKCEHYWPVDDMPCL---YGNLRVS 767
Cdd:cd14540     1 YINASHITaTVGGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEHDaltFGEYKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 768 VQSEQKESCWTRREFVVRNESTSEERGVTHFHFTAWPDHGVPKGT-------EELIQFRWIVRQHIETFPFSGPTVVHCS 840
Cdd:cd14540    81 TKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVsgfldflEEINSVRRHTNQDVAGHNRNPPTLVHCS 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1764596117 841 AGVGRTGTLIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLHQ 893
Cdd:cd14540   161 AGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYN 213

R-PTP-N

cd14609

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

639-890

5.60e-56

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

Pssm-ID: 350457 [Multi-domain] Cd Length: 281 Bit Score: 194.87 E-value: 5.60e-56

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 639 FSEEYEDLSTVGTD-QSCTVATLPENKSKNRFTNVLPYDISRVKLAAQTG-SDLDYINANYIHGYGKKNKQYIAAQGPLP 716
Cdd:cd14609    17 LAKEWQALCAYQAEpNTCSTAQGEANVKKNRNPDFVPYDHARIKLKAESNpSRSDYINASPIIEHDPRMPAYIATQGPLS 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 717 STVSDFWRMVWEQKSSAIVMLTNCTEGGRIKCEHYWPvDDMPCLYGNLRVSVQSEQkesCWTR----REFVVRNESTSEE 792
Cdd:cd14609    97 HTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWP-DEGSSLYHIYEVNLVSEH---IWCEdflvRSFYLKNVQTQET 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 793 RGVTHFHFTAWPDHGVPKGTEELIQFRWIVRQHIETfpFSGPTVVHCSAGVGRTGTLIALDLLLQQMDKE-EVVSIADCV 871
Cdd:cd14609   173 RTLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCYRG--RSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGvKEIDIAATL 250

                         250
                  ....*....|....*....
gi 1764596117 872 RCMRLSRPLMVQTQSQYVF 890
Cdd:cd14609   251 EHVRDQRPGMVRTKDQFEF 269

PTPc-N14

cd14599

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

642-899

5.87e-56

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: 195.22 E-value: 5.87e-56

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 642 EYEDLSTVGTDQSCTVATLPENKSKNRFTNVLPYDISRVKLAAQTGSDLDYINANYIH-GYGKKNKQYIAAQGPLPSTVS 720
Cdd:cd14599    17 EYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVPTKENNTGYINASHIKvTVGGEEWHYIATQGPLPHTCH 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 721 DFWRMVWEQKSSAIVMLTNCTEGGRIKCEHYWP---VDDMPCLYGNLRVSVQSEQKESCWTRREFVVRNESTSEERGVTH 797
Cdd:cd14599    97 DFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPklgSKHSSATYGKFKVTTKFRTDSGCYATTGLKVKHLLSGQERTVWH 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 798 FHFTAWPDHGVPKGTE------ELIQfrwIVRQHIETFPFSG-----PTVVHCSAGVGRTGTLIALDLLLQQMDKEEVVS 866
Cdd:cd14599   177 LQYTDWPDHGCPEEVQgflsylEEIQ---SVRRHTNSMLDSTkncnpPIVVHCSAGVGRTGVVILTELMIGCLEHNEKVE 253

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1764596117 867 IADCVRCMRLSRPLMVQTQSQYVFLHQCIMDSL 899
Cdd:cd14599   254 VPVMLRHLREQRMFMIQTIAQYKFVYQVLIQFL 286

R-PTPc-A-E-2

cd14552

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

692-895

1.10e-54

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: 188.25 E-value: 1.10e-54

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 692 YINANYIHGYGKKNkQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEGGRIKCEHYWPVDDMpCLYGNLRVSVQSE 771
Cdd:cd14552     1 YINASFIDGYRQKD-AYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPEDGS-VSSGDITVELKDQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 772 QKESCWTRREFVVRNESTSEERGVTHFHFTAWPDHGVP---KGTEELIQFRWIVRQHIEtfpfSGPTVVHCSAGVGRTGT 848
Cdd:cd14552    79 TDYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPdngKGMIDLIAAVQKQQQQSG----NHPITVHCSAGAGRTGT 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1764596117 849 LIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLHQCI 895
Cdd:cd14552   155 FCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201

PTPc-N11

cd14605

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

662-895

2.43e-54

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: 189.46 E-value: 2.43e-54

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 662 ENKSKNRFTNVLPYDISRVKL----AAQTGSDldYINANYI-------HGYGKKNKQYIAAQGPLPSTVSDFWRMVWEQK 730
Cdd:cd14605     1 ENKNKNRYKNILPFDHTRVVLhdgdPNEPVSD--YINANIImpefetkCNNSKPKKSYIATQGCLQNTVNDFWRMVFQEN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 731 SSAIVMLTNCTEGGRIKCEHYWPVDDMPCLYGNLRVSVQSEQKESCWTRREF-VVRNESTSEERGVTHFHFTAWPDHGVP 809
Cdd:cd14605    79 SRVIVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYILRELkLSKVGQGNTERTVWQYHFRTWPDHGVP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 810 KGTEELIQFRWIVRQHIETFPFSGPTVVHCSAGVGRTGTLIALDLLLQQMDKEEV---VSIADCVRCMRLSRPLMVQTQS 886
Cdd:cd14605   159 SDPGGVLDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVdcdIDVPKTIQMVRSQRSGMVQTEA 238


                  ....*....
gi 1764596117 887 QYVFLHQCI 895
Cdd:cd14605   239 QYRFIYMAV 247

R-PTP-N-N2

cd14546

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

692-895

1.29e-51

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

Pssm-ID: 350394 [Multi-domain] Cd Length: 208 Bit Score: 179.95 E-value: 1.29e-51

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 692 YINANYIHGYGKKNKQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEGGRIKCEHYWPvDDMPCLYGNLRVSVQSE 771
Cdd:cd14546     1 YINASTIYDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWP-EEGSEVYHIYEVHLVSE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 772 QkesCWTR----REFVVRNESTSEERGVTHFHFTAWPDHGVPKGTEELIQFRWIVRQHIETfpFSGPTVVHCSAGVGRTG 847
Cdd:cd14546    80 H---IWCDdylvRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSYRG--RSCPIVVHCSDGAGRTG 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1764596117 848 TLIALDLLLQQMDK-EEVVSIADCVRCMRLSRPLMVQTQSQYVFLHQCI 895
Cdd:cd14546   155 TYILIDMVLNRMAKgAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAV 203

R-PTPc-E-2

cd14622

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

691-897

1.25e-50

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: 177.12 E-value: 1.25e-50

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 691 DYINANYIHGYGKKNkQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEGGRIKCEHYWPVDDmPCLYGNLRVSVQS 770
Cdd:cd14622     1 DYINASFIDGYRQKD-YFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEG-SVTHGEITIEIKN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 771 EQKESCWTRREFVVRNESTSEERGVTHFHFTAWPDHGVP---KGTEELIQFrwIVRQHIETfpFSGPTVVHCSAGVGRTG 847
Cdd:cd14622    79 DTLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPaegKGMIDLIAA--VQKQQQQT--GNHPIVVHCSAGAGRTG 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1764596117 848 TLIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLHQCIMD 897
Cdd:cd14622   155 TFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQD 204

COG5599

Protein tyrosine phosphatase [Signal transduction mechanisms];

613-891

1.37e-48

Protein tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 444335 [Multi-domain] Cd Length: 282 Bit Score: 174.12 E-value: 1.37e-48

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 613 SNKYKPIHLKKFPMHFSSMscdqnrgFSEEYEDLSTVGTDQscTVATLPENKSKNRFTNVLPYDISRVklaaqtGSDLDY 692
Cdd:COG5599     1 VSPKNPIAIKSEEEKINSR-------LSTLTNELAPSHNDP--QYLQNINGSPLNRFRDIQPYKETAL------RANLGY 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 693 INANYIHGYGkkNKQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEGG--RIKCEHYWPVDDMpclYGNLRVSVQS 770
Cdd:COG5599    66 LNANYIQVIG--NHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISkpKVKMPVYFRQDGE---YGKYEVSSEL 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 771 EQKESCWTR---REFVVRNESTSEE-RGVTHFHFTAWPDHGVPkGTEELIQFRWIVRQHIETFPFS-GPTVVHCSAGVGR 845
Cdd:COG5599   141 TESIQLRDGieaRTYVLTIKGTGQKkIEIPVLHVKNWPDHGAI-SAEALKNLADLIDKKEKIKDPDkLLPVVHCRAGVGR 219

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1764596117 846 TGTLIALdLLLQQMDKEEV---VSIADCVRCMRLSR-PLMVQTQSQYVFL 891
Cdd:COG5599   220 TGTLIAC-LALSKSINALVqitLSVEEIVIDMRTSRnGGMVQTSEQLDVL 268

PTP-N23

cd14539

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

692-893

1.47e-47

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

Pssm-ID: 350387 [Multi-domain] Cd Length: 205 Bit Score: 168.33 E-value: 1.47e-47

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 692 YINANYIHGYGKKNKQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEGGRIKCEHYWPVD-DMPCLYGNLRVSVQS 770
Cdd:cd14539     1 YINASLIEDLTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTErGQALVYGAITVSLQS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 771 EQKESCWTRREFVVRNESTSEERGVTHFHFTAWPDHGVPKGTEELIQFRWIVRQH-IETFPFSGPTVVHCSAGVGRTGTL 849
Cdd:cd14539    81 VRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHyLQQRSLQTPIVVHCSSGVGRTGAF 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1764596117 850 IALDLLLQQMDKE-EVVSIADCVRCMRLSRPLMVQTQSQYVFLHQ 893
Cdd:cd14539   161 CLLYAAVQEIEAGnGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205

PTPc_plant_PTP1

cd17658

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

692-890

2.09e-46

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: 164.94 E-value: 2.09e-46

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 692 YINANYIHGYGKKN-KQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEGGR-IKCEHYWPVDD-MPCLYGNLRVSV 768
Cdd:cd17658     1 YINASLVETPASESlPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStAKCADYFPAEEnESREFGRISVTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 769 QSEQ-KESCWTRREFVVR-NESTSEERGVTHFHFTAWPDHGVPKGTEELiqfRWIVRQHIETFPFSGPTVVHCSAGVGRT 846
Cdd:cd17658    81 KKLKhSQHSITLRVLEVQyIESEEPPLSVLHIQYPEWPDHGVPKDTRSV---RELLKRLYGIPPSAGPIVVHCSAGIGRT 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1764596117 847 GTLIALDLLLQQMDKEEV--VSIADCVRCMRLSRPLMVQTQSQYVF 890
Cdd:cd17658   158 GAYCTIHNTIRRILEGDMsaVDLSKTVRKFRSQRIGMVQTQDQYIF 203

PHA02746

protein tyrosine phosphatase; Provisional

661-900

2.35e-45

protein tyrosine phosphatase; Provisional

Pssm-ID: 165113 [Multi-domain] Cd Length: 323 Bit Score: 166.36 E-value: 2.35e-45

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 661 PENKSKNRFTNVLPYDISRVKLAAQTG--------------------SDLDYINANYIHGYGKKNKqYIAAQGPLPSTVS 720
Cdd:PHA02746   49 KENLKKNRFHDIPCWDHSRVVINAHESlkmfdvgdsdgkkievtsedNAENYIHANFVDGFKEANK-FICAQGPKEDTSE 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 721 DFWRMVWEQKSSAIVMLTNcTEGGRIKCEHYWPV-DDMPCLYGNLRVSVQSEQKESCWTRREFVVRNESTSEERGVTHFH 799
Cdd:PHA02746  128 DFFKLISEHESQVIVSLTD-IDDDDEKCFELWTKeEDSELAFGRFVAKILDIIEELSFTKTRLMITDKISDTSREIHHFW 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 800 FTAWPDHGVPKGTEELIQFRWIVRQH-------IETFPFS-GPTVVHCSAGVGRTGTLIALDLLLQQMDKEEVVSIADCV 871
Cdd:PHA02746  207 FPDWPDNGIPTGMAEFLELINKVNEEqaelikqADNDPQTlGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEVCLGEIV 286

                         250       260
                  ....*....|....*....|....*....
gi 1764596117 872 RCMRLSRPLMVQTQSQYVFLHQCIMDSLL 900
Cdd:PHA02746  287 LKIRKQRHSSVFLPEQYAFCYKALKYAII 315

PHA02738

hypothetical protein; Provisional

663-895

3.00e-44

hypothetical protein; Provisional

Pssm-ID: 222923 [Multi-domain] Cd Length: 320 Bit Score: 162.79 E-value: 3.00e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 663 NKSKNRFTNVLPYDISRVKLAAQTGSDlDYINANYIHGYGKKnKQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTE 742
Cdd:PHA02738   49 NRKLNRYLDAVCFDHSRVILPAERNRG-DYINANYVDGFEYK-KKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKE 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 743 GGRIKCEHYWP-VDDMPCLYGNLRVSVQSEQKESCWTRREFVVrNESTSEERGVTHFHFTAWPDHGVPKGTEELIQFRWI 821
Cdd:PHA02738  127 NGREKCFPYWSdVEQGSIRFGKFKITTTQVETHPHYVKSTLLL-TDGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLE 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 822 VRQ-----HIETFPFSG------PTVVHCSAGVGRTGTLIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVF 890
Cdd:PHA02738  206 VRQcqkelAQESLQIGHnrlqppPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYFF 285


                  ....*
gi 1764596117 891 LHQCI 895
Cdd:PHA02738  286 CYRAV 290

R-PTPc-typeIIb-2

cd14556

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

692-893

1.38e-43

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: 156.80 E-value: 1.38e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 692 YINANYIHGYgKKNKQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLtNCTEGGRIKCEHYWPVDDMPClYGNLRVSVQSE 771
Cdd:cd14556     1 YINAALLDSY-KQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVML-NQLDPKDQSCPQYWPDEGSGT-YGPIQVEFVST 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 772 QKESCWTRREFVVRNESTSEE--RGVTHFHFTAWPDHG-VPKGTEELIQFRWIVRQHIETFPfSGPTVVHCSAGVGRTGT 848
Cdd:cd14556    78 TIDEDVISRIFRLQNTTRPQEgyRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQEQSG-EGPIVVHCLNGVGRSGV 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1764596117 849 LIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLHQ 893
Cdd:cd14556   157 FCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201

PTPc-N21

cd14598

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

692-899

2.10e-42

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: 154.36 E-value: 2.10e-42

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 692 YINANYIH-GYGKKNKQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEGGRIKCEHYWP---VDDMPCLYGNLRVS 767
Cdd:cd14598     1 YINASHIKvTVGGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlgSRHNTVTYGRFKIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 768 VQSEQKESCWTRREFVVRNESTSEERGVTHFHFTAWPDHGVP---KGTEELIQFRWIVRQH----IETFPFSGPTVVHCS 840
Cdd:cd14598    81 TRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPedlKGFLSYLEEIQSVRRHtnstIDPKSPNPPVLVHCS 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1764596117 841 AGVGRTGTLIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLHQCIMDSL 899
Cdd:cd14598   161 AGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFL 219

PTPc_motif

smart00404

Protein tyrosine phosphatase, catalytic domain motif;

795-897

1.68e-41

Protein tyrosine phosphatase, catalytic domain motif;

Pssm-ID: 214649 [Multi-domain] Cd Length: 105 Bit Score: 147.12 E-value: 1.68e-41

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117  795 VTHFHFTAWPDHGVPKGTEELIQFRWIVRQHIETFPFSGPTVVHCSAGVGRTGTLIALDLLLQQMDKE-EVVSIADCVRC 873
Cdd:smart00404   2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVKE 81

                           90       100
                   ....*....|....*....|....
gi 1764596117  874 MRLSRPLMVQTQSQYVFLHQCIMD 897
Cdd:smart00404  82 LRSQRPGMVQTEEQYLFLYRALLE 105

PTPc_DSPc

smart00012

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

795-897

1.68e-41

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: 147.12 E-value: 1.68e-41

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117  795 VTHFHFTAWPDHGVPKGTEELIQFRWIVRQHIETFPFSGPTVVHCSAGVGRTGTLIALDLLLQQMDKE-EVVSIADCVRC 873
Cdd:smart00012   2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEaGEVDIFDTVKE 81

                           90       100
                   ....*....|....*....|....
gi 1764596117  874 MRLSRPLMVQTQSQYVFLHQCIMD 897
Cdd:smart00012  82 LRSQRPGMVQTEEQYLFLYRALLE 105

PHA02747

protein tyrosine phosphatase; Provisional

661-909

2.38e-40

protein tyrosine phosphatase; Provisional

Pssm-ID: 165114 [Multi-domain] Cd Length: 312 Bit Score: 151.31 E-value: 2.38e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 661 PENKSKNRFTNVLPYDISRVKLAAQTGSDLDYINANYIHGYgKKNKQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNc 740
Cdd:PHA02747   49 PENQPKNRYWDIPCWDHNRVILDSGGGSTSDYIHANWIDGF-EDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTP- 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 741 TEG--GRIKCEHYW-PVDDMPCLYGNLRVSVQSEQKESCWTRREFVVRNESTSEERGVTHFHFTAWPDHGVPKGTEELIQ 817
Cdd:PHA02747  127 TKGtnGEEKCYQYWcLNEDGNIDMEDFRIETLKTSVRAKYILTLIEITDKILKDSRKISHFQCSEWFEDETPSDHPDFIK 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 818 FRWIV----RQHIETFPFS----GPTVVHCSAGVGRTGTLIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYV 889
Cdd:PHA02747  207 FIKIIdinrKKSGKLFNPKdallCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYL 286

                         250       260
                  ....*....|....*....|..
gi 1764596117 890 FLHQC--IMDSLLPKEDSIPEP 909
Cdd:PHA02747  287 FIQPGyeVLHYFLSKIKAIDKI 308

PHA02742

protein tyrosine phosphatase; Provisional

641-890

7.61e-37

protein tyrosine phosphatase; Provisional

Pssm-ID: 165109 [Multi-domain] Cd Length: 303 Bit Score: 140.91 E-value: 7.61e-37

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 641 EEYEDLSTVGTDQSCTVATLPENKSKNRFTNVLPYDISRVKLAAQTGSDlDYINANYIHGYGKKnKQYIAAQGPLPSTVS 720
Cdd:PHA02742   30 EEHEHIMQEIVAFSCNESLELKNMKKCRYPDAPCFDRNRVILKIEDGGD-DFINASYVDGHNAK-GRFICTQAPLEETAL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 721 DFWRMVWEQKSSAIVMLTNCTEGGRIKCEHYW-PVDDMPCLYGNLRVSVQSEQKESCWTRREFVVRNESTSEERGVTHFH 799
Cdd:PHA02742  108 DFWQAIFQDQVRVIVMITKIMEDGKEACYPYWmPHERGKATHGEFKIKTKKIKSFRNYAVTNLCLTDTNTGASLDIKHFA 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 800 FTAWPDHGVPKGTEELIQFRWIVR--QHIETFPFSG-------PTVVHCSAGVGRTGTLIALDLLLQQMDKEEVVSIADC 870
Cdd:PHA02742  188 YEDWPHGGLPRDPNKFLDFVLAVReaDLKADVDIKGenivkepPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSI 267

                         250       260
                  ....*....|....*....|
gi 1764596117 871 VRCMRLSRPLMVQTQSQYVF 890
Cdd:PHA02742  268 VRDLRKQRHNCLSLPQQYIF 287

R5-PTP-2

cd14550

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

692-893

1.33e-36

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: 136.68 E-value: 1.33e-36

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 692 YINANYIHGYgKKNKQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEGGriKCEHYWPVDDMPCLYGNLRVSVQSE 771
Cdd:cd14550     1 YINASYLQGY-RRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNE--DEPIYWPTKEKPLECETFKVTLSGE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 772 qKESCW------TRREFVVrnESTSEER--GVTHFHFTAWPDHGVPKGTE-ELIQfrwIVRQHIETfpFSGPTVVHCSAG 842
Cdd:cd14550    78 -DHSCLsneirlIVRDFIL--ESTQDDYvlEVRQFQCPSWPNPCSPIHTVfELIN---TVQEWAQQ--RDGPIVVHDRYG 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1764596117 843 VGRTGTLIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLHQ 893
Cdd:cd14550   150 GVQAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200

R-PTPc-T-2

cd14634

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

692-897

4.45e-28

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: 112.42 E-value: 4.45e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 692 YINANYIHGYgKKNKQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLtNCTEGGRIkCEHYWPvDDMPCLYGNLRVSVQSE 771
Cdd:cd14634     1 YINAALMDSH-KQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVML-NEMDAAQL-CMQYWP-EKTSCCYGPIQVEFVSA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 772 QKESCWTRREFVVRNESTSEE--RGVTHFHFTAWPDH-GVPKGTEELIQF-RWIVRQHIETFPFSGPTVVHCSAGVGRTG 847
Cdd:cd14634    77 DIDEDIISRIFRICNMARPQDgyRIVQHLQYIGWPAYrDTPPSKRSILKVvRRLEKWQEQYDGREGRTVVHCLNGGGRSG 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1764596117 848 TLIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLHQCIMD 897
Cdd:cd14634   157 TFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVALE 206

R-PTP-Z-2

cd17669

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

692-896

1.40e-27

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: 111.24 E-value: 1.40e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 692 YINANYIHGYGKKNkQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEGGRIKCEhYWPVDDMPCLYGNLRVSVQSE 771
Cdd:cd17669     1 YINASYIMGYYQSN-EFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPNKDEPINCETFKVTLIAE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 772 QKESCWTRREFVVRN---ESTSEER--GVTHFHFTAWPDHGVP-KGTEELIQfrwIVRQhiETFPFSGPTVVHCSAGVGR 845
Cdd:cd17669    79 EHKCLSNEEKLIIQDfilEATQDDYvlEVRHFQCPKWPNPDSPiSKTFELIS---IIKE--EAANRDGPMIVHDEHGGVT 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1764596117 846 TGTLIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLHQCIM 896
Cdd:cd17669   154 AGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204

R-PTP-G-2

cd17670

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

692-896

8.22e-27

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

Pssm-ID: 350508 [Multi-domain] Cd Length: 205 Bit Score: 109.00 E-value: 8.22e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 692 YINANYIHGYGKKNkQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNctEGGRIKCEH-YWPVDDMPCLYGNLRVSVQS 770
Cdd:cd17670     1 YINASYIMGYYRSN-EFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD--NQGLAEDEFvYWPSREESMNCEAFTVTLIS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 771 EQKESCWTRREFVVRN---ESTSEER--GVTHFHFTAWPDHGVP-KGTEELIQfrwIVRQhiETFPFSGPTVVHCSAGVG 844
Cdd:cd17670    78 KDRLCLSNEEQIIIHDfilEATQDDYvlEVRHFQCPKWPNPDAPiSSTFELIN---VIKE--EALTRDGPTIVHDEFGAV 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1764596117 845 RTGTLIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLHQCIM 896
Cdd:cd17670   153 SAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204

R-PTPc-K-2

cd14636

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

692-892

8.69e-24

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: 100.10 E-value: 8.69e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 692 YINANYIHGYgKKNKQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLT--NCTEGgrikCEHYWPVDDMpCLYGNLRVSVQ 769
Cdd:cd14636     1 YINAALMDSY-RQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNevDLAQG----CPQYWPEEGM-LRYGPIQVECM 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 770 SEQKESCWTRREFVVRNESTSEE--RGVTHFHFTAWPDH-GVPKGTEELIQFRWIVRQ-HIETFPFSGPTVVHCSAGVGR 845
Cdd:cd14636    75 SCSMDCDVISRIFRICNLTRPQEgyLMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKwQEECDEGEGRTIIHCLNGGGR 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1764596117 846 TGTLIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLH 892
Cdd:cd14636   155 SGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCY 201

R-PTPc-M-2

cd14635

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

692-897

1.31e-23

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: 99.76 E-value: 1.31e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 692 YINANYIHGYgKKNKQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEGGRikCEHYWPVDDMPcLYGNLRVSVQSE 771
Cdd:cd14635     1 YINAALMDSY-KQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPAQL--CPQYWPENGVH-RHGPIQVEFVSA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 772 QKESCWTRREFVVRNESTSEE--RGVTHFHFTAWPDH-GVPKGTEELIQF-RWIVRQHIETFPFSGPTVVHCSAGVGRTG 847
Cdd:cd14635    77 DLEEDIISRIFRIYNAARPQDgyRMVQQFQFLGWPMYrDTPVSKRSFLKLiRQVDKWQEEYNGGEGRTVVHCLNGGGRSG 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1764596117 848 TLIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLHQCIMD 897
Cdd:cd14635   157 TFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVALE 206

R-PTPc-U-2

cd14637

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

692-897

5.99e-22

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: 94.98 E-value: 5.99e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 692 YINANYIHGYgKKNKQYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEGGRI-KCEHYWPvDDMPCLYGNLRVSVQS 770
Cdd:cd14637     1 YINAALTDSY-TRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWP-EPGLQQYGPMEVEFVS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 771 EQKESCWTRREFVVRNESTSEERG--VTHFHFTAW-PDHGVPKGTEELIQFRWIVRQHIETfPFSGPTVVHCSAGVGRTG 847
Cdd:cd14637    79 GSADEDIVTRLFRVQNITRLQEGHlmVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQRE-SGEGRTVVHCLNGGGRSG 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1764596117 848 TLIALDLLLQQMDKEEVVSIADCVRCMRLSRPLMVQTQSQYVFLHQCIMD 897
Cdd:cd14637   158 TYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIALE 207

PTP_YopH-like

cd14559

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

667-891

6.81e-20

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

Pssm-ID: 350407 [Multi-domain] Cd Length: 227 Bit Score: 89.38 E-value: 6.81e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 667 NRFTNVLpydiSRVKLAAQTGsdldyINANYIHgYGKKNKqYIAAQGPLPSTVSDFWRMVWEQKSSAIVMLTNCTEggrI 746
Cdd:cd14559     1 NRFTNIQ----TRVSTPVGKN-----LNANRVQ-IGNKNV-AIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKD---I 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 747 KCEHYWPVDDMPCLYGnlRVSVQSEQKESCWTRREFVVRNES-TSEERGVTH----FHFTAWPDHGvPKGTEELIQFRWI 821
Cdd:cd14559    67 QRKGLPPYFRQSGTYG--SVTVKSKKTGKDELVDGLKADMYNlKITDGNKTItipvVHVTNWPDHT-AISSEGLKELADL 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 822 VRQHIETF--------------PFSGPTVVHCSAGVGRTGTLIAldlLLQQMDKEEVVSIADCVRCMRLSR-PLMVQTQS 886
Cdd:cd14559   144 VNKSAEEKrnfykskgssaindKNKLLPVIHCRAGVGRTGQLAA---AMELNKSPNNLSVEDIVSDMRTSRnGKMVQKDE 220


                  ....*
gi 1764596117 887 QYVFL 891
Cdd:cd14559   221 QLDTL 225

CDC14

COG2453

Protein-tyrosine phosphatase [Signal transduction mechanisms];

785-893

4.79e-14

Protein-tyrosine phosphatase [Signal transduction mechanisms];

Pssm-ID: 441989 [Multi-domain] Cd Length: 140 Bit Score: 70.00 E-value: 4.79e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 785 RNESTSEERGVTHFHFtAWPDHGVPkgTEELIQ--FRWIVRQHIEtfpfSGPTVVHCSAGVGRTGTLIALDLLLQQMDKE 862
Cdd:COG2453    38 LLLGLLEEAGLEYLHL-PIPDFGAP--DDEQLQeaVDFIDEALRE----GKKVLVHCRGGIGRTGTVAAAYLVLLGLSAE 110

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1764596117 863 EVVSIAdcvrcmRLSRPLMVQTQSQYVFLHQ 893
Cdd:COG2453   111 EALARV------RAARPGAVETPAQRAFLER 135

PHA02740

protein tyrosine phosphatase; Provisional

641-907

1.31e-12

protein tyrosine phosphatase; Provisional

Pssm-ID: 165107 [Multi-domain] Cd Length: 298 Bit Score: 69.61 E-value: 1.31e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 641 EEYEDLSTVGTDQSCTVATLPENKSKNRfTNVLP---YDISRVKLAaqtgSDLDYINANYIHGYGKKNKqYIAAQGPLPS 717
Cdd:PHA02740   29 KEYRAIVPEHEDEANKACAQAENKAKDE-NLALHitrLLHRRIKLF----NDEKVLDARFVDGYDFEQK-FICIINLCED 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 718 TVSDFWRMVWEQKSSAIVMLTNCTEGgriKC-EHYWPVDDMPCL-YGNLRVsvqseQKESCWTRREFV----VRNESTSE 791
Cdd:PHA02740  103 ACDKFLQALSDNKVQIIVLISRHADK---KCfNQFWSLKEGCVItSDKFQI-----ETLEIIIKPHFNltllSLTDKFGQ 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 792 ERGVTHFHFTAWPDHGVPKGTEELIQFRWIV-------RQHiETFPFSGPTVVHCSAGVGRTGTLIALDLLLQQMDKEEV 864
Cdd:PHA02740  175 AQKISHFQYTAWPADGFSHDPDAFIDFFCNIddlcadlEKH-KADGKIAPIIIDCIDGISSSAVFCVFDICATEFDKTGM 253

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1764596117 865 VSIADCVRCMRLSRPLMVQTQSQYVFLHQCIMDSLLPKEDSIP 907
Cdd:PHA02740  254 LSIANALKKVRQKKYGCMNCLDDYVFCYHLIAAYLKEKFDILK 296

FN3

COG3401

Fibronectin type 3 domain [General function prediction only];

17-530

1.96e-11

Fibronectin type 3 domain [General function prediction only];

Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 67.72 E-value: 1.96e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117  17 VWGTSTSMPIPVSTSIATTKTTGLPTPPSLTNVDTVSVTNRTETTLTLE----WNKVNNNSNYIYTLSYNSQNKSINGSM 92
Cdd:COG3401    32 SGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAavavAAAPPTATGLTTLTGSGSVGGATNTGL 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117  93 ESPVVTYRVINLTAGTEYNFILYTVFGEALSTGYNFTEVTTPQSVTNITVKNRNETALILEWNKVNNNSNYSYTLSYNSQ 172
Cdd:COG3401   112 TSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTT 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 173 NTSING-SEEGSAVTYTVLDLTAGTEYVFilytvfkglqSMGHSFTTVTT-PQSVTNITVKNRNETALILEWNKVNNNNN 250
Cdd:COG3401   192 LVDGGGdIEPGTTYYYRVAATDTGGESAP----------SNEVSVTTPTTpPSAPTGLTATADTPGSVTLSWDPVTESDA 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 251 YSYTLsYNSQNTSINGSE--EGSAVTYTVLDLTAGTEYIFILYTV-FKGLQSMGHSFTTVTT----PQSVTNITVKNRNE 323
Cdd:COG3401   262 TGYRV-YRSNSGDGPFTKvaTVTTTSYTDTGLTNGTTYYYRVTAVdAAGNESAPSNVVSVTTdltpPAAPSGLTATAVGS 340

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 324 TALILEWNKANNNNNYSYTL--SYNSQSTSINGSEEGSAVTYTVLDLTAGTEYVFILHTVFKGLQSMGHSFTTVTTPQSV 401
Cdd:COG3401   341 SSITLSWTASSDADVTGYNVyrSTSGGGTYTKIAETVTTTSYTDTGLTPGTTYYYKVTAVDAAGNESAPSEEVSATTASA 420

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 402 TNITVKNRNETALILEWNKVNNNNNYSYTLSYNSQNTSINGSEEGVAVTYTVPDLTAGTEYTFTLYTVFKGV-ESRAYHI 480
Cdd:COG3401   421 ASGESLTASVDAVPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTtGSLVGGS 500

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1764596117 481 TSVTVPNSVT---GLHCQYSSGGYGLTLVWDPPNGGRTFVQVNMSSKSFSHIG 530
Cdd:COG3401   501 GASSVTNSVSvigASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLITDLVSL 553

PTP_PTPDC1

cd14506

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

792-892

4.37e-10

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: 60.44 E-value: 4.37e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 792 ERGVTHFHFtAWPDHGVPKgTEELIQFRWIVRQHIETfpfSGPTVVHCSAGVGRTGTLIALDLLLQQMdkeevVSIADCV 871
Cdd:cd14506    74 RAGIYFYNF-GWKDYGVPS-LTTILDIVKVMAFALQE---GGKVAVHCHAGLGRTGVLIACYLVYALR-----MSADQAI 143

                          90       100
                  ....*....|....*....|.
gi 1764596117 872 RCMRLSRPLMVQTQSQYVFLH 892
Cdd:cd14506   144 RLVRSKRPNSIQTRGQVLCVR 164

PTP_DSP_cys

cd14494

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

833-893

8.82e-10

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

Pssm-ID: 350344 [Multi-domain] Cd Length: 113 Bit Score: 56.97 E-value: 8.82e-10

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1764596117 833 GPTVVHCSAGVGRTGTLIALDLLLQQMdkeevVSIADCVRCMRLSRP-LMVQTQSQYVFLHQ 893
Cdd:cd14494    57 EPVLVHCKAGVGRTGTLVACYLVLLGG-----MSAEEAVRIVRLIRPgGIPQTIEQLDFLIK 113

FN3

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

398-475

9.57e-08

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 50.31 E-value: 9.57e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117  398 PQSVTNITVKNRNETALILEWNKVNNNNNYSYTLSYNSQNTSINGSEEGVAVT-----YTVPDLTAGTEYTFTLYTVFKG 472
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTpsstsYTLTGLKPGTEYEFRVRAVNGA 80


                   ...
gi 1764596117  473 VES 475
Cdd:smart00060  81 GEG 83

CDKN3-like

cd14505

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

791-893

2.85e-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: 51.11 E-value: 2.85e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 791 EERGVTHFHFtAWPDHGVPkgtEELIQFRWIVRQHIETFPFSGPTVVHCSAGVGRTGTLIA--LDLLLQQMDKEEVVSIa 868
Cdd:cd14505    69 QQAGITWHHL-PIPDGGVP---SDIAQWQELLEELLSALENGKKVLIHCKGGLGRTGLIAAclLLELGDTLDPEQAIAA- 143

                          90       100
                  ....*....|....*....|....*
gi 1764596117 869 dcvrcMRLSRPLMVQTQSQYVFLHQ 893
Cdd:cd14505   144 -----VRALRPGAIQTPKQENFLHQ 163

fn3

Fibronectin type III domain;

400-469

1.72e-06

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 46.64 E-value: 1.72e-06

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1764596117 400 SVTNITVKNRNETALILEWNKVNNNNNY--SYTLSY---NSQNTSINGSEEGVAVTYTVPDLTAGTEYTFTLYTV 469
Cdd:pfam00041   2 APSNLTVTDVTSTSLTVSWTPPPDGNGPitGYEVEYrpkNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAV 76

FN3

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

134-205

3.14e-06

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 46.07 E-value: 3.14e-06

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1764596117  134 PQSVTNITVKNRNETALILEWNKVNNNSNYSYTLSYNSQNTSINGSEE-----GSAVTYTVLDLTAGTEYVFILYTV 205
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKevnvtPSSTSYTLTGLKPGTEYEFRVRAV 77

DUSP23

cd14504

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

784-893

4.75e-06

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: 47.27 E-value: 4.75e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 784 VRNESTSEERGVTHFHFTAwPDHGVPkgTEELI-QFRWIVRQHIEtfpFSGPTVVHCSAGVGRTGTLIALDLLLQQMDke 862
Cdd:cd14504    39 PPPEHSDTCPGLRYHHIPI-EDYTPP--TLEQIdEFLDIVEEANA---KNEAVLVHCLAGKGRTGTMLACYLVKTGKI-- 110

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1764596117 863 evvSIADCVRCMRLSRPLMVQTQSQYVFLHQ 893
Cdd:cd14504   111 ---SAVDAINEIRRIRPGSIETSEQEKFVIQ 138

CDC14_C

cd14499

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

783-894

5.96e-06

C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division control protein 14 (CDC14) family is highly conserved in all eukaryotes, although the roles of its members seem to have diverged during evolution. Yeast Cdc14, the best characterized member of this family, is a dual-specificity phosphatase that plays key roles in cell cycle control. It preferentially dephosphorylates cyclin-dependent kinase (CDK) targets, which makes it the main antagonist of CDK in the cell. Cdc14 functions at the end of mitosis and it triggers the events that completely eliminates the activity of CDK and other mitotic kinases. It is also involved in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint, and in chromosome segregation. Cdc14 phosphatases also function in DNA replication, DNA damage checkpoint, and DNA repair. Vertebrates may contain more than one Cdc14 homolog; humans have three (CDC14A, CDC14B, and CDC14C). CDC14 family proteins contain a highly conserved N-terminal pseudophosphatase domain that contributes to substrate specificity and a C-terminal catalytic dual-specificity phosphatase domain with the PTP signature motif.

Pssm-ID: 350349 [Multi-domain] Cd Length: 174 Bit Score: 47.45 E-value: 5.96e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 783 VVR------NESTSEERGVTHF--HFtawPDHGVPkgTEELIQ-FRWIVRQHietfpfSGPTVVHCSAGVGRTGTLIALD 853
Cdd:cd14499    62 VVRlnkklyDAKRFTDAGIRHYdlYF---PDGSTP--SDDIVKkFLDICENE------KGAIAVHCKAGLGRTGTLIACY 130

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1764596117 854 LllqqMDK-----EEVvsIAdcvrCMRLSRPLMVQTQSQYvFLHQC 894
Cdd:cd14499   131 L----MKHygftaREA--IA----WLRICRPGSVIGPQQQ-FLEEK 165

fn3

Fibronectin type III domain;

136-205

7.02e-06

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 45.10 E-value: 7.02e-06

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1764596117 136 SVTNITVKNRNETALILEWNKVNNNSNY--SYTLSY---NSQNTSINGSEEGSAVTYTVLDLTAGTEYVFILYTV 205
Cdd:pfam00041   2 APSNLTVTDVTSTSLTVSWTPPPDGNGPitGYEVEYrpkNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAV 76

FN3

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

398-485

1.75e-05

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 44.02 E-value: 1.75e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 398 PQSVTNITVKNRNETALILEWNKVNNNNNY--SYTLSY---NSQNTSINGSEEGVAVTYTVPDLTAGTEYTFTLYTVFKG 472
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPitGYVVEYrekGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                          90
                  ....*....|...
gi 1764596117 473 VESRAYHITSVTV 485
Cdd:cd00063    81 GESPPSESVTVTT 93

FN3

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

222-293

1.92e-05

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 43.76 E-value: 1.92e-05

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1764596117  222 PQSVTNITVKNRNETALILEWNKVNNNNNYSYTLSYNSQNTSINGSEE-----GSAVTYTVLDLTAGTEYIFILYTV 293
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKevnvtPSSTSYTLTGLKPGTEYEFRVRAV 77

fn3

Fibronectin type III domain;

52-117

2.41e-05

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 43.56 E-value: 2.41e-05

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1764596117  52 VSVTNRTETTLTLEWNKVNNNSNYI--YTLSY---NSQNKSINGSMESPVVTYRVINLTAGTEYNFILYTV 117
Cdd:pfam00041   6 LTVTDVTSTSLTVSWTPPPDGNGPItgYEVEYrpkNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAV 76

FN3

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

41-117

2.81e-05

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 43.37 E-value: 2.81e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117   41 PTPPSltnvdTVSVTNRTETTLTLEWNKVNNNSNYIYTLSYNSQNKSINGSMESPVVT-----YRVINLTAGTEYNFILY 115
Cdd:smart00060   1 PSPPS-----NLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVNVTpsstsYTLTGLKPGTEYEFRVR 75


                   ..
gi 1764596117  116 TV 117
Cdd:smart00060  76 AV 77

fn3

Fibronectin type III domain;

312-381

2.93e-05

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 43.17 E-value: 2.93e-05

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1764596117 312 SVTNITVKNRNETALILEWNKANNNNNY--SYTLSY---NSQSTSINGSEEGSAVTYTVLDLTAGTEYVFILHTV 381
Cdd:pfam00041   2 APSNLTVTDVTSTSLTVSWTPPPDGNGPitGYEVEYrpkNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAV 76

fn3

Fibronectin type III domain;

224-293

3.46e-05

Fibronectin type III domain;

Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 43.17 E-value: 3.46e-05

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1764596117 224 SVTNITVKNRNETALILEWNKVNNNNNY--SYTLSY---NSQNTSINGSEEGSAVTYTVLDLTAGTEYIFILYTV 293
Cdd:pfam00041   2 APSNLTVTDVTSTSLTVSWTPPPDGNGPitGYEVEYrpkNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAV 76

FN3

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

310-376

6.46e-05

Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 42.22 E-value: 6.46e-05

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1764596117  310 PQSVTNITVKNRNETALILEWNKANNNNNYSYTLSYNSQSTSINGSEE-----GSAVTYTVLDLTAGTEYVF 376
Cdd:smart00060   1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKevnvtPSSTSYTLTGLKPGTEYEF 72

PTP-IVa

cd14500

protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), ...

791-865

1.73e-04

protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), also known as protein-tyrosine phosphatases of regenerating liver (PRLs) constitute a family of small, prenylated phosphatases that are the most oncogenic of all PTPs. They stimulate progression from G1 into S phase during mitosis and enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. They associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation. Vertebrates contain three members: PRL-1, PRL-2, and PRL-3.

Pssm-ID: 350350 [Multi-domain] Cd Length: 156 Bit Score: 42.98 E-value: 1.73e-04

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1764596117 791 EERGVtHFHFTAWPDHGVPkgTEELIQfRW--IVRQHIETFPFSGPTV-VHCSAGVGRTGTLIALDLLLQQMDKEEVV 865
Cdd:cd14500    55 EKAGI-KVHDWPFDDGSPP--PDDVVD-DWldLLKTRFKEEGKPGACIaVHCVAGLGRAPVLVAIALIELGMKPEDAV 128

FN3

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

134-211

2.22e-04

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 40.94 E-value: 2.22e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 134 PQSVTNITVKNRNETALILEWNKV--NNNSNYSYTLSY---NSQNTSINGSEEGSAVTYTVLDLTAGTEYVFILYTVFKG 208
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPedDGGPITGYVVEYrekGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80


                  ...
gi 1764596117 209 LQS 211
Cdd:cd00063    81 GES 83

FN3

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

41-133

2.80e-04

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 40.94 E-value: 2.80e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117  41 PTPPSltnvdTVSVTNRTETTLTLEWNKVNNNSNYI--YTLSYNSQNKSINGSMESPVVT---YRVINLTAGTEYNFILY 115
Cdd:cd00063     1 PSPPT-----NLRVTDVTSTSVTLSWTPPEDDGGPItgYVVEYREKGSGDWKEVEVTPGSetsYTLTGLKPGTEYEFRVR 75

                          90
                  ....*....|....*...
gi 1764596117 116 TVFGEALSTGYNFTEVTT 133
Cdd:cd00063    76 AVNGGGESPPSESVTVTT 93

FN3

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

222-299

5.50e-04

Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 39.79 E-value: 5.50e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1764596117 222 PQSVTNITVKNRNETALILEWNKVNNNNNY--SYTLSY---NSQNTSINGSEEGSAVTYTVLDLTAGTEYIFILYTVFKG 296
Cdd:cd00063     1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPitGYVVEYrekGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80


                  ...
gi 1764596117 297 LQS 299
Cdd:cd00063    81 GES 83

Oca4

COG2365

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

833-865

1.50e-03

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

Pssm-ID: 441932 [Multi-domain] Cd Length: 248 Bit Score: 41.48 E-value: 1.50e-03

                          10        20        30
                  ....*....|....*....|....*....|...
gi 1764596117 833 GPTVVHCSAGVGRTGTLIALDLLLQQMDKEEVV 865
Cdd:COG2365   134 GPVLFHCTAGKDRTGVAAALLLLALGVPRETIM 166

FN3