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Conserved domains on  [gi|514686563|ref|XP_004990859|]
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plasminogen [Salpingoeca rosetta]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
4459-4719 5.44e-94

Protein tyrosine phosphatase, catalytic domain;


:

Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 306.12  E-value: 5.44e-94
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563   4459 GAIEEFQTIPK-TSATGSFTHSQRE--RQKNRYLDILAYDQTRVRLGD-DGSGSDYINANYVTFPstPTPFRFIASQGPK 4534
Cdd:smart00194    1 GLEEEFEKLDRlKPDDESCTVAAFPenRDKNRYKDVLPYDHTRVKLKPpPGEGSDYINASYIDGP--NGPKAYIATQGPL 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563   4535 PNTVNEHWQMLWEQRVHVIVMLAQVVEGGRQKCAQYWPPGAGQTMTTPLLEVTHVSSTPDDpydpEIITTKLKVRHRING 4614
Cdd:smart00194   79 PSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVD----DYTIRTLEVTNTGCS 154

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563   4615 QVREITHVQYVGWPDHGVPESPDKFLDLVDRVqrLRSQLPEDAPyILVHCSAGIGRSGVLIVVLVMLDRLRKKKLPNARE 4694
Cdd:smart00194  155 ETRTVTHYHYTNWPDHGVPESPESILDLIRAV--RKSQSTSTGP-IVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFE 231

                           250       260
                    ....*....|....*....|....*
gi 514686563   4695 IVKALREQRMGLVQVAAQYRFCFTA 4719
Cdd:smart00194  232 IVKELRSQRPGMVQTEEQYIFLYRA 256
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 359-432 1.13e-29

Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like receptors. Can occur in up to 38 copies (in apolipoprotein(a)). Plasminogen-like kringles possess affinity for free lysine and lysine- containing peptides.


:

Pssm-ID: 214527  Cd Length: 83  Bit Score: 114.79  E-value: 1.13e-29
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 514686563    359 YDANNMGYRGPIATTRNGRTCQRWDSQSPHPHSFTPLLFPDADLRENYCRNPDG-ERTAWCFTTDPSRQWELCDV 432
Cdd:smart00130    4 YAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGdSEGPWCYTTDPNVRWEYCDI 78
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 4350-4414 5.31e-23

CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


:

Pssm-ID: 460154 [Multi-domain]  Cd Length: 65  Bit Score: 95.16  E-value: 5.31e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 514686563  4350 VGMRVLVKGYGPGTLLYYGKHATKPGYRCGVALDDPIGRNNGTVGGFWYFDCDDNHGILCDPRKV 4414
Cdd:pfam01302    1 VGDRVEVPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
TNFRSF super family cl22855
Tumor necrosis factor receptor superfamily (TNFRSF); Members of TNFR superfamily (TNFRSF) ...
 934-1057 5.17e-10

Tumor necrosis factor receptor superfamily (TNFRSF); Members of TNFR superfamily (TNFRSF) interactions with TNF superfamily (TNFSF) ligands (TNFL) control key cellular processes such as differentiation, proliferation, apoptosis, and cell growth. Dysregulation of these pathways has been shown to result in a wide range of pathological conditions, including autoimmune diseases, inflammation, cancer, and viral infection. There are 29 very diverse family members of TNFRSF reported in humans: 22 are type I transmembrane receptors (single pass with the N terminus on extracellular side of the cell membrane) and have a clear signal peptide; the remaining 7 members are either type III transmembrane receptors (single pass with the N terminus on extracellular side of the membrane but no signal sequence; TNFR13B, TNFR13C, TNFR17, and XEDAR), or attached to the membrane via a glycosylphosphatidylinositol (GPI) linker (TNFR10C), or secreted as soluble receptors (TNFR11B and TNFR6B). All TNFRs contain relatively short cysteine-rich domains (CRDs) in the ectodomain, and are involved in interaction with the TNF homology domain (THD) of their ligands. TNFRs often have multiple CRDs (between one and six), with the most frequent configurations of three or four copies; most CRDs possess three disulfide bridges, but could have between one and four. Localized or genome-wide duplication and evolution of the TNFRSF members appear to have paralleled the emergence of the adaptive immune system; teleosts (i.e. ray-finned, bony fish), which possess an immune system with B and T cells, possess primary and secondary lymphoid organs, and are capable of adaptive responses to pathogens also display several characteristics that are different from the mammalian immune system, making teleost TNFSF orthologs and paralogs of interest to better understand immune system evolution and the immunological pathways elicited to pathogens.


The actual alignment was detected with superfamily member cd13416:

Pssm-ID: 473981 [Multi-domain]  Cd Length: 159  Bit Score: 61.16  E-value: 5.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563  934 RRC-QNYTTCELGSTFQTVGPTPTTDRKCDACTVCPSTHRQIAECTLLLNAECEE---------------CSSCPSGTYM 997
Cdd:cd13416    26 RPCgDNQTVCEPCLDGVTFSDVVSHTEPCQPCTRCPGLMSMRAPCTATHDTVCECaygyyldedsgtcepCTVCPPGQGV 105

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514686563  998 DQACTDDHDTICAPcdtCATGKY--EAAACDPlhntqCEPCDVCSPSQYQLRACRATLNTVC 1057
Cdd:cd13416   106 VQSCGPNQDTVCEA---CPEGTYsdEDSSTDP-----CLPCTVCEDGEVELRECTPVSDTVC 159
TNFRSF super family cl22855
Tumor necrosis factor receptor superfamily (TNFRSF); Members of TNFR superfamily (TNFRSF) ...
 3682-3816 5.98e-06

Tumor necrosis factor receptor superfamily (TNFRSF); Members of TNFR superfamily (TNFRSF) interactions with TNF superfamily (TNFSF) ligands (TNFL) control key cellular processes such as differentiation, proliferation, apoptosis, and cell growth. Dysregulation of these pathways has been shown to result in a wide range of pathological conditions, including autoimmune diseases, inflammation, cancer, and viral infection. There are 29 very diverse family members of TNFRSF reported in humans: 22 are type I transmembrane receptors (single pass with the N terminus on extracellular side of the cell membrane) and have a clear signal peptide; the remaining 7 members are either type III transmembrane receptors (single pass with the N terminus on extracellular side of the membrane but no signal sequence; TNFR13B, TNFR13C, TNFR17, and XEDAR), or attached to the membrane via a glycosylphosphatidylinositol (GPI) linker (TNFR10C), or secreted as soluble receptors (TNFR11B and TNFR6B). All TNFRs contain relatively short cysteine-rich domains (CRDs) in the ectodomain, and are involved in interaction with the TNF homology domain (THD) of their ligands. TNFRs often have multiple CRDs (between one and six), with the most frequent configurations of three or four copies; most CRDs possess three disulfide bridges, but could have between one and four. Localized or genome-wide duplication and evolution of the TNFRSF members appear to have paralleled the emergence of the adaptive immune system; teleosts (i.e. ray-finned, bony fish), which possess an immune system with B and T cells, possess primary and secondary lymphoid organs, and are capable of adaptive responses to pathogens also display several characteristics that are different from the mammalian immune system, making teleost TNFSF orthologs and paralogs of interest to better understand immune system evolution and the immunological pathways elicited to pathogens.


The actual alignment was detected with superfamily member cd10583:

Pssm-ID: 473981 [Multi-domain]  Cd Length: 159  Bit Score: 49.36  E-value: 5.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 3682 VCSPCNAGEYQLLPCLPRSDRECEPCnpctPGNTTLVAECTLERdtiCTEC-ASCRSDQWISSPCTVSSDTVCSnitqCd 3760
Cdd:cd10583    14 TCDKCPAGTYVSKHCTETSLRECSPC----PNGTFTRHENGIEQ---CHRCrKPCPAPMIEKTPCTALTDRECT----C- 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 514686563 3761 fpreyrdVPATLTSNAVCKNVSTCAPGQFISAQATPTNDVTCAnvslPCSGETYEA 3816
Cdd:cd10583    82 -------PPGTFLSNDTCVPHSVCPVGWGVRKKGTETEDVRCK----PCPRGTFSD 126
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 45-189 6.44e-04

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


:

Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 43.98  E-value: 6.44e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563     45 VVVLVEGSFYVAEGEFAAFTQAALDVsTALLTASPTGTHLtSVIEFST-----FPCSAESqctpfvsDAEELADRIDSID 119
Cdd:smart00327    2 VVFLLDGSGSMGGNRFELAKEFVLKL-VEQLDIGPDGDRV-GLVTFSDdarvlFPLNDSR-------SKDALLEALASLS 72

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 514686563    120 -QSFGLVRTAGAIQYALDN---RFQVPDPDRRSVLLAIAKSAPLNPSEPVRQA---LQDAGVDAFFVLLDPDNSTVQ 189
Cdd:smart00327   73 yKLGGGTNLGAALQYALENlfsKSAGSRRGAPKVVILITDGESNDGPKDLLKAakeLKRSGVKVFVVGVGNDVDEEE 149
TNFRSF super family cl22855
Tumor necrosis factor receptor superfamily (TNFRSF); Members of TNFR superfamily (TNFRSF) ...
 516-669 7.36e-04

Tumor necrosis factor receptor superfamily (TNFRSF); Members of TNFR superfamily (TNFRSF) interactions with TNF superfamily (TNFSF) ligands (TNFL) control key cellular processes such as differentiation, proliferation, apoptosis, and cell growth. Dysregulation of these pathways has been shown to result in a wide range of pathological conditions, including autoimmune diseases, inflammation, cancer, and viral infection. There are 29 very diverse family members of TNFRSF reported in humans: 22 are type I transmembrane receptors (single pass with the N terminus on extracellular side of the cell membrane) and have a clear signal peptide; the remaining 7 members are either type III transmembrane receptors (single pass with the N terminus on extracellular side of the membrane but no signal sequence; TNFR13B, TNFR13C, TNFR17, and XEDAR), or attached to the membrane via a glycosylphosphatidylinositol (GPI) linker (TNFR10C), or secreted as soluble receptors (TNFR11B and TNFR6B). All TNFRs contain relatively short cysteine-rich domains (CRDs) in the ectodomain, and are involved in interaction with the TNF homology domain (THD) of their ligands. TNFRs often have multiple CRDs (between one and six), with the most frequent configurations of three or four copies; most CRDs possess three disulfide bridges, but could have between one and four. Localized or genome-wide duplication and evolution of the TNFRSF members appear to have paralleled the emergence of the adaptive immune system; teleosts (i.e. ray-finned, bony fish), which possess an immune system with B and T cells, possess primary and secondary lymphoid organs, and are capable of adaptive responses to pathogens also display several characteristics that are different from the mammalian immune system, making teleost TNFSF orthologs and paralogs of interest to better understand immune system evolution and the immunological pathways elicited to pathogens.


The actual alignment was detected with superfamily member cd10577:

Pssm-ID: 473981 [Multi-domain]  Cd Length: 163  Bit Score: 43.23  E-value: 7.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563  516 MCASVnpCYPHQYEASPPTVTSDRVCVAISNCTTSQFQTAAPtatsnrECRSIRPPCMLGsEYLVAEPTTTTDRICedvk 595
Cdd:cd10577    14 MCCSK--CPPGQHVKHSCTKTSDTVCAPCEESTYTQLWNWVP------ECLSCSSPCSSD-QVETQACTRQQNRIC---- 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514686563  596 NCTESQFqVVAPTATSDRVCAKLRECRDDQYIAVPATPTSNRICLRLAECTedqyelVEPTETSNRVCAPCTPC 669
Cdd:cd10577    81 SCKPGWY-CVLKLQEGCRQCRPLKKCGPGFGVARPGTASSDVECKPCAPGT------FSDTTSSTDTCRPHRIC 147
TNFRSF super family cl22855
Tumor necrosis factor receptor superfamily (TNFRSF); Members of TNFR superfamily (TNFRSF) ...
 666-789 3.21e-03

Tumor necrosis factor receptor superfamily (TNFRSF); Members of TNFR superfamily (TNFRSF) interactions with TNF superfamily (TNFSF) ligands (TNFL) control key cellular processes such as differentiation, proliferation, apoptosis, and cell growth. Dysregulation of these pathways has been shown to result in a wide range of pathological conditions, including autoimmune diseases, inflammation, cancer, and viral infection. There are 29 very diverse family members of TNFRSF reported in humans: 22 are type I transmembrane receptors (single pass with the N terminus on extracellular side of the cell membrane) and have a clear signal peptide; the remaining 7 members are either type III transmembrane receptors (single pass with the N terminus on extracellular side of the membrane but no signal sequence; TNFR13B, TNFR13C, TNFR17, and XEDAR), or attached to the membrane via a glycosylphosphatidylinositol (GPI) linker (TNFR10C), or secreted as soluble receptors (TNFR11B and TNFR6B). All TNFRs contain relatively short cysteine-rich domains (CRDs) in the ectodomain, and are involved in interaction with the TNF homology domain (THD) of their ligands. TNFRs often have multiple CRDs (between one and six), with the most frequent configurations of three or four copies; most CRDs possess three disulfide bridges, but could have between one and four. Localized or genome-wide duplication and evolution of the TNFRSF members appear to have paralleled the emergence of the adaptive immune system; teleosts (i.e. ray-finned, bony fish), which possess an immune system with B and T cells, possess primary and secondary lymphoid organs, and are capable of adaptive responses to pathogens also display several characteristics that are different from the mammalian immune system, making teleost TNFSF orthologs and paralogs of interest to better understand immune system evolution and the immunological pathways elicited to pathogens.


The actual alignment was detected with superfamily member cd10575:

Pssm-ID: 473981 [Multi-domain]  Cd Length: 163  Bit Score: 41.62  E-value: 3.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563  666 CTPCPVGVaFEERACTNVSNTVCSVC-------------------RTCGEGTFESSPCNTT-NRVCdpisECTATQY--- 722
Cdd:cd10575    16 CDQCPPGT-FVAKHCTRDRPTVCGPCpdlhytqfwnylekcrycnVFCTERQVEKRQCNAThNRVC----ECKPGYYmeh 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 514686563  723 EFdpptattdrvCRNLTQCLPFiEYESQPPTPTSNRECAltSCDPGTFEVVPptiTSARECDPVKQC 789
Cdd:cd10575    91 GF----------CLRHSSCPPG-EGVIKLGTPYSDTQCE--PCPPGFFSASS---SSTEPCQPHTNC 141
 
Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
4459-4719 5.44e-94

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 306.12  E-value: 5.44e-94
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563   4459 GAIEEFQTIPK-TSATGSFTHSQRE--RQKNRYLDILAYDQTRVRLGD-DGSGSDYINANYVTFPstPTPFRFIASQGPK 4534
Cdd:smart00194    1 GLEEEFEKLDRlKPDDESCTVAAFPenRDKNRYKDVLPYDHTRVKLKPpPGEGSDYINASYIDGP--NGPKAYIATQGPL 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563   4535 PNTVNEHWQMLWEQRVHVIVMLAQVVEGGRQKCAQYWPPGAGQTMTTPLLEVTHVSSTPDDpydpEIITTKLKVRHRING 4614
Cdd:smart00194   79 PSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVD----DYTIRTLEVTNTGCS 154

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563   4615 QVREITHVQYVGWPDHGVPESPDKFLDLVDRVqrLRSQLPEDAPyILVHCSAGIGRSGVLIVVLVMLDRLRKKKLPNARE 4694
Cdd:smart00194  155 ETRTVTHYHYTNWPDHGVPESPESILDLIRAV--RKSQSTSTGP-IVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFE 231

                           250       260
                    ....*....|....*....|....*
gi 514686563   4695 IVKALREQRMGLVQVAAQYRFCFTA 4719
Cdd:smart00194  232 IVKELRSQRPGMVQTEEQYIFLYRA 256
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
4483-4721 2.61e-92

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 300.31  E-value: 2.61e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563  4483 RQKNRYLDILAYDQTRVRLGDDGSGSDYINANYVtfPSTPTPFRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEG 4562
Cdd:pfam00102    2 LEKNRYKDVLPYDHTRVKLTGDPGPSDYINASYI--DGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563  4563 GRQKCAQYWPPGAGQTMTTPLLEVTHVSSTPDdpyDPEIITTKLKVRHRINGQVREITHVQYVGWPDHGVPESPDKFLDL 4642
Cdd:pfam00102   80 GREKCAQYWPEEEGESLEYGDFTVTLKKEKED---EKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDL 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 514686563  4643 VDRVqRLRSQLPEDAPyILVHCSAGIGRSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRFCFTACL 4721
Cdd:pfam00102  157 LRKV-RKSSLDGRSGP-IVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 4510-4717 3.17e-78

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: 258.37  E-value: 3.17e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4510 YINANYVTFPSTPTpfRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGGRQKCAQYWPPGAGQTMTTPLLEVTHV 4589
Cdd:cd00047     1 YINASYIDGYRGPK--EYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGDITVTLV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4590 SSTPddpyDPEIITTKLKVRHRINGQVREITHVQYVGWPDHGVPESPDKFLDLVDRVQRLRSQlpEDAPyILVHCSAGIG 4669
Cdd:cd00047    79 SEEE----LSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARK--PNGP-IVVHCSAGVG 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 514686563 4670 RSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRFCF 4717
Cdd:cd00047   152 RTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIY 199
PHA02738 PHA02738
hypothetical protein; Provisional
 4462-4728 7.90e-41

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 155.47  E-value: 7.90e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4462 EEFQTIPKTSATGSFTHSQRERQKNRYLDILAYDQTRVRLGDDGSGSDYINANYVT-FPSTPtpfRFIASQGPKPNTVNE 4540
Cdd:PHA02738   29 REHQKVISEKVDGTFNAEKKNRKLNRYLDAVCFDHSRVILPAERNRGDYINANYVDgFEYKK---KFICGQAPTRQTCYD 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4541 HWQMLWEQRVHVIVMLAQVVEGGRQKCAQYWPPGAGQTMTTPLLEVTHVSSTPddpyDPEIITTKLKVRHRiNGQVREIT 4620
Cdd:PHA02738  106 FYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSIRFGKFKITTTQVET----HPHYVKSTLLLTDG-TSATQTVT 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4621 HVQYVGWPDHGVPESPDKFLDLVDRVQRLRSQLPEDA----------PYILVHCSAGIGRSGVLIVVLVMLDRLRKKKLP 4690
Cdd:PHA02738  181 HFNFTAWPDHDVPKNTSEFLNFVLEVRQCQKELAQESlqighnrlqpPPIVVHCNAGLGRTPCYCVVDISISRFDACATV 260

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 514686563 4691 NAREIVKALREQRMGLVQVAAQYRFCFTACLAKLDSID 4728
Cdd:PHA02738  261 SIPSIVSSIRNQRYYSLFIPFQYFFCYRAVKRYVNLTV 298
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
4485-4713 6.70e-35

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 137.14  E-value: 6.70e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4485 KNRYLDILAYDQTRVRlGDDGsgsdYINANYVtfpSTPTPFRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGG- 4563
Cdd:COG5599    45 LNRFRDIQPYKETALR-ANLG----YLNANYI---QVIGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISk 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4564 -RQKCAQYWPPgAGQTmttpLLEVTHVSSTPDDPYDPEIITTKLKVRHRINGQ-VREITHVQYVGWPDHGVPeSPDKFLD 4641
Cdd:COG5599   117 pKVKMPVYFRQ-DGEY----GKYEVSSELTESIQLRDGIEARTYVLTIKGTGQkKIEIPVLHVKNWPDHGAI-SAEALKN 190

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 514686563 4642 LVDRVQRLRSQLPEDAPYILVHCSAGIGRSGVLIVVLVMLDRLRKKKLP--NAREIVKALREQR-MGLVQVAAQY 4713
Cdd:COG5599   191 LADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVQItlSVEEIVIDMRTSRnGGMVQTSEQL 265
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 359-432 1.13e-29

Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like receptors. Can occur in up to 38 copies (in apolipoprotein(a)). Plasminogen-like kringles possess affinity for free lysine and lysine- containing peptides.


Pssm-ID: 214527  Cd Length: 83  Bit Score: 114.79  E-value: 1.13e-29
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 514686563    359 YDANNMGYRGPIATTRNGRTCQRWDSQSPHPHSFTPLLFPDADLRENYCRNPDG-ERTAWCFTTDPSRQWELCDV 432
Cdd:smart00130    4 YAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGdSEGPWCYTTDPNVRWEYCDI 78
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 359-432 3.74e-28

Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, prothrombin, and apolipoprotein A. Structure is disulfide-rich, nearly all-beta.


Pssm-ID: 395005  Cd Length: 79  Bit Score: 110.09  E-value: 3.74e-28
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 514686563   359 YDANNMGYRGPIATTRNGRTCQRWDSQSPHPHSF-TPLLFPDADLRENYCRNPDGERTAWCFTTDPSRQWELCDV 432
Cdd:pfam00051    2 YHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDI 76
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 359-432 4.55e-28

Kringle domain; Kringle domains are believed to play a role in binding mediators, such as peptides, other proteins, membranes, or phospholipids. They are autonomous structural domains, found in a varying number of copies, in blood clotting and fibrinolytic proteins, some serine proteases and plasma proteins. Plasminogen-like kringles possess affinity for free lysine and lysine-containing peptides.


Pssm-ID: 238056  Cd Length: 83  Bit Score: 110.16  E-value: 4.55e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 514686563  359 YDANNMGYRGPIATTRNGRTCQRWDSQSPHPHSFTPLLFPDADLRENYCRNPDGE-RTAWCFTTDPSRQWELCDV 432
Cdd:cd00108     5 YWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDpEGPWCYTTDPNVRWEYCDI 79
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 4350-4414 5.31e-23

CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 460154 [Multi-domain]  Cd Length: 65  Bit Score: 95.16  E-value: 5.31e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 514686563  4350 VGMRVLVKGYGPGTLLYYGKHATKPGYRCGVALDDPIGRNNGTVGGFWYFDCDDNHGILCDPRKV 4414
Cdd:pfam01302    1 VGDRVEVPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 4350-4415 5.35e-15

Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and transportation of vesicles and organelles along the cytoskeletal network; A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 214997 [Multi-domain]  Cd Length: 68  Bit Score: 72.23  E-value: 5.35e-15
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 514686563   4350 VGMRVLVKGYG-PGTLLYYGKHATKPGYRCGVALDDP-IGRNNGTVGGFWYFDCDDNHGILCDPRKVR 4415
Cdd:smart01052    1 VGDRVEVGGGGrRGTVRYVGPTPFAPGVWVGVELDEPlRGKNDGSVKGVRYFECPPKHGIFVRPSKVE 68
TNFRSF16 cd13416
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ...
 934-1057 5.17e-10

Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 neurotrophin receptor (p75NTR) or CD271; TNFRSF16 (also known as nerve growth factor receptor (NGFR) or p75 neurotrophin receptor (p75NTR or p75(NTR)), CD271, Gp80-LNGFR) is a common receptor for both neurotrophins and proneurotrophins, and plays a diverse role in many tissues, including the nervous system. It has been shown to be expressed in various types of stem cells and has been used to prospectively isolate stem cells with different degrees of potency. p75NTR owes its signaling to the recruitment of intracellular binding proteins, leading to the activation of different signaling pathways. It binds nerve growth factor (NGF) and the complex can initiate a signaling cascade which has been associated with both neuronal apoptosis and neuronal survival of discrete populations of neurons, depending on the presence or absence of intracellular signaling molecules downstream of p75NTR (e.g. NF-kB, JNK, or p75NTR intracellular death domain). p75NTR can also bind NGF in concert with the neurotrophic tyrosine kinase receptor type 1 (TrkA) protein where it is thought to modulate the formation of the high-affinity neurotrophin binding complex. On melanoma cell, p75NTR is an immunosuppressive factor, induced by interferon (IFN)-gamma, and mediates down-regulation of melanoma antigens. It can interact with the aggregated form of amyloid beta (Abeta) peptides, and plays an important role in etiopathogenesis of Alzheimer's disease by influencing protein tau hyper-phosphorylation. p75(NTR) is involved in the formation and progression of retina diseases; its expression is induced in retinal pigment epithelium (RPE) cells and its knockdown rescues RPE cell proliferation activity and inhibits RPE apoptosis induced by hypoxia. It can therefore be a potential therapeutic target for RPE hypoxia or oxidative stress diseases.


Pssm-ID: 276921 [Multi-domain]  Cd Length: 159  Bit Score: 61.16  E-value: 5.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563  934 RRC-QNYTTCELGSTFQTVGPTPTTDRKCDACTVCPSTHRQIAECTLLLNAECEE---------------CSSCPSGTYM 997
Cdd:cd13416    26 RPCgDNQTVCEPCLDGVTFSDVVSHTEPCQPCTRCPGLMSMRAPCTATHDTVCECaygyyldedsgtcepCTVCPPGQGV 105

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514686563  998 DQACTDDHDTICAPcdtCATGKY--EAAACDPlhntqCEPCDVCSPSQYQLRACRATLNTVC 1057
Cdd:cd13416   106 VQSCGPNQDTVCEA---CPEGTYsdEDSSTDP-----CLPCTVCEDGEVELRECTPVSDTVC 159
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 4350-4411 9.51e-07

Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 227569 [Multi-domain]  Cd Length: 669  Bit Score: 55.46  E-value: 9.51e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514686563 4350 VGMRVLVKGYgPGTLLYYGKHATKPGYRCGVALDDPIGRNNGTVGGFWYFDCDDNHGILCDP 4411
Cdd:COG5244     6 VNDRVLLGDK-FGTVRFIGKTKFKDGIWIGLELDDPVGKNDGSVNGVRYFHCKKRHGIFIRP 66
TNFRSF21 cd10583
Tumor necrosis factor receptor superfamily member 21 (TNFRSF21), also known as death receptor ...
 3682-3816 5.98e-06

Tumor necrosis factor receptor superfamily member 21 (TNFRSF21), also known as death receptor (DR6); TNFRSF21 (also known as death receptor 6 (DR6), CD358, BM-018) is highly expressed in differentiating neurons as well as in the adult brain, and is upregulated in injured neurons. DR6 negatively regulates neurondendrocyte, axondendrocyte, and oligodendrocyte survival, hinders axondendrocyte and oligodendrocyte regeneration and its inhibition has a neuro-protective effect in nerve injury. It activates nuclear factor kappa-B (NFkB) and mitogen-activated protein kinase 8 (MAPK8, also called c-Jun N-terminal kinase 1), and induces cell apoptosis by associating with TNFRSF1A-associated via death domain (TRADD), which is known to mediate signal transduction of tumor necrosis factor receptors. TNFRSF21 plays a role in T-helper cell activation, and may be involved in inflammation and immune regulation. Its possible ligand is alpha-amyloid precursor protein (APP), hence probably involved in the development of Alzheimer's disease; when released, APP binds in an autocrine/paracrine manner to activate a caspase-dependent self-destruction program that removes unnecessary or connectionless axons. Increasing beta-catenin levels in brain endothelium upregulates TNFRSF21 and TNFRSF19, indicating that these death receptors are downstream target genes of Wnt/beta-catenin signaling, which has been shown to be required for blood-brain barrier development. DR6 is up-regulated in numerous solid tumors as well as in tumor vascular cells, including ovarian cancer and may be a clinically useful diagnostic and predictive serum biomarker for some adult sarcoma subtypes.


Pssm-ID: 276909 [Multi-domain]  Cd Length: 159  Bit Score: 49.36  E-value: 5.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 3682 VCSPCNAGEYQLLPCLPRSDRECEPCnpctPGNTTLVAECTLERdtiCTEC-ASCRSDQWISSPCTVSSDTVCSnitqCd 3760
Cdd:cd10583    14 TCDKCPAGTYVSKHCTETSLRECSPC----PNGTFTRHENGIEQ---CHRCrKPCPAPMIEKTPCTALTDRECT----C- 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 514686563 3761 fpreyrdVPATLTSNAVCKNVSTCAPGQFISAQATPTNDVTCAnvslPCSGETYEA 3816
Cdd:cd10583    82 -------PPGTFLSNDTCVPHSVCPVGWGVRKKGTETEDVRCK----PCPRGTFSD 126
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 45-189 6.44e-04

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 43.98  E-value: 6.44e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563     45 VVVLVEGSFYVAEGEFAAFTQAALDVsTALLTASPTGTHLtSVIEFST-----FPCSAESqctpfvsDAEELADRIDSID 119
Cdd:smart00327    2 VVFLLDGSGSMGGNRFELAKEFVLKL-VEQLDIGPDGDRV-GLVTFSDdarvlFPLNDSR-------SKDALLEALASLS 72

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 514686563    120 -QSFGLVRTAGAIQYALDN---RFQVPDPDRRSVLLAIAKSAPLNPSEPVRQA---LQDAGVDAFFVLLDPDNSTVQ 189
Cdd:smart00327   73 yKLGGGTNLGAALQYALENlfsKSAGSRRGAPKVVILITDGESNDGPKDLLKAakeLKRSGVKVFVVGVGNDVDEEE 149
TNFRSF1B cd10577
Tumor necrosis factor receptor superfamily member 1B (TNFRSF1B), also known as TNFR2; TNFRSF1B ...
 516-669 7.36e-04

Tumor necrosis factor receptor superfamily member 1B (TNFRSF1B), also known as TNFR2; TNFRSF1B (also known as TNFR2, type 2 TNFR, TNFBR, TNFR80, TNF-R75, TNF-R-II, p75, CD120b) binds TNF-alpha, but lacks the death domain (DD) that is associated with the cytoplasmic domain of TNFRSF1A (TNFR1). It is inducible and expressed exclusively by oligodendrocytes, astrocytes, T cells, thymocytes, myocytes, endothelial cells, and in human mesenchymal stem cells. TNFRSF1B protects oligodendrocyte progenitor cells (OLGs) against oxidative stress, and induces the up-regulation of cell survival genes. While pro-inflammatory and pathogen-clearing activities of TNF are mediated mainly through activation of TNFRSF1A, a strong activator of NF-kappaB, TNFRSF1B is more responsible for suppression of inflammation. Although the affinities of both receptors for soluble TNF are similar, TNFRSF1B is sometimes more abundantly expressed and thought to associate with TNF, thereby increasing its concentration near TNFRSF1A receptors, and making TNF available to activate TNFRSF1A (a ligand-passing mechanism).


Pssm-ID: 276903 [Multi-domain]  Cd Length: 163  Bit Score: 43.23  E-value: 7.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563  516 MCASVnpCYPHQYEASPPTVTSDRVCVAISNCTTSQFQTAAPtatsnrECRSIRPPCMLGsEYLVAEPTTTTDRICedvk 595
Cdd:cd10577    14 MCCSK--CPPGQHVKHSCTKTSDTVCAPCEESTYTQLWNWVP------ECLSCSSPCSSD-QVETQACTRQQNRIC---- 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514686563  596 NCTESQFqVVAPTATSDRVCAKLRECRDDQYIAVPATPTSNRICLRLAECTedqyelVEPTETSNRVCAPCTPC 669
Cdd:cd10577    81 SCKPGWY-CVLKLQEGCRQCRPLKKCGPGFGVARPGTASSDVECKPCAPGT------FSDTTSSTDTCRPHRIC 147
TNFRSF6B cd10575
Tumor necrosis factor receptor superfamily member 6B (TNFRSF6B), also known as decoy receptor ...
 666-789 3.21e-03

Tumor necrosis factor receptor superfamily member 6B (TNFRSF6B), also known as decoy receptor 3 (DcR3); The subfamily TNFRSF6B is also known as decoy receptor 3 (DcR3), M68, or TR6. This protein is a soluble receptor without death domain and cytoplasmic domain, and secreted by cells. It acts as a decoy receptor that competes with death receptors for ligand binding. It is a pleiotropic immunomodulator and biomarker for inflammatory diseases, autoimmune diseases, and cancer. Over-expression of this gene has been noted in several cancers, including pancreatic carcinoma, and gastrointestinal tract tumors. It can neutralize the biological effects of three tumor necrosis factor superfamily (TNFSF) members: TNFSF6 (Fas ligand/FasL/CD95L) and TNFSF14 (LIGHT) which are both involved in apoptosis and inflammation, and TNFSF15 (TNF-like molecule 1A/TL1A), which is a T cell co-stimulator and involved in gut inflammation. DcR3 is a novel inflammatory marker; higher DcR3 levels strongly correlate with inflammation and independently predict cardiovascular and all-cause mortality in chronic kidney disease (CKD) patients on hemodialysis. Increased synovial inflammatory cells infiltration in rheumatoid arthritis and ankylosing spondylitis is also associated with the elevated DcR3 expression. In cartilaginous fish, mRNA expression of DcR3 in the thymus and leydig, which are the representative lymphoid tissues of elasmobranchs, suggests that DcR3 may act as a modulator in the immune system. Interestingly, in banded dogfish (Triakis scyllia), DcR3 mRNA is strongly expressed in the gill, compared with human expression in the normal lung; both are respiratory organs, suggesting potential relevance of DcR3 to respiratory function.


Pssm-ID: 276901 [Multi-domain]  Cd Length: 163  Bit Score: 41.62  E-value: 3.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563  666 CTPCPVGVaFEERACTNVSNTVCSVC-------------------RTCGEGTFESSPCNTT-NRVCdpisECTATQY--- 722
Cdd:cd10575    16 CDQCPPGT-FVAKHCTRDRPTVCGPCpdlhytqfwnylekcrycnVFCTERQVEKRQCNAThNRVC----ECKPGYYmeh 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 514686563  723 EFdpptattdrvCRNLTQCLPFiEYESQPPTPTSNRECAltSCDPGTFEVVPptiTSARECDPVKQC 789
Cdd:cd10575    91 GF----------CLRHSSCPPG-EGVIKLGTPYSDTQCE--PCPPGFFSASS---SSTEPCQPHTNC 141
TNFR_c6 pfam00020
TNFR/NGFR cysteine-rich region;
991-1033 4.46e-03

TNFR/NGFR cysteine-rich region;


Pssm-ID: 459633 [Multi-domain]  Cd Length: 39  Bit Score: 37.68  E-value: 4.46e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 514686563   991 CPSGTYMDQactdDHDTICAPCDTCATGKYEAAACDPLHNTQC 1033
Cdd:pfam00020    1 CPPGTYTDN----WNGLKCLPCTVCPPGQVVVRPCTPTSDTVC 39
 
Name Accession Description Interval E-value
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
4459-4719 5.44e-94

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 306.12  E-value: 5.44e-94
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563   4459 GAIEEFQTIPK-TSATGSFTHSQRE--RQKNRYLDILAYDQTRVRLGD-DGSGSDYINANYVTFPstPTPFRFIASQGPK 4534
Cdd:smart00194    1 GLEEEFEKLDRlKPDDESCTVAAFPenRDKNRYKDVLPYDHTRVKLKPpPGEGSDYINASYIDGP--NGPKAYIATQGPL 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563   4535 PNTVNEHWQMLWEQRVHVIVMLAQVVEGGRQKCAQYWPPGAGQTMTTPLLEVTHVSSTPDDpydpEIITTKLKVRHRING 4614
Cdd:smart00194   79 PSTVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEGEPLTYGDITVTLKSVEKVD----DYTIRTLEVTNTGCS 154

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563   4615 QVREITHVQYVGWPDHGVPESPDKFLDLVDRVqrLRSQLPEDAPyILVHCSAGIGRSGVLIVVLVMLDRLRKKKLPNARE 4694
Cdd:smart00194  155 ETRTVTHYHYTNWPDHGVPESPESILDLIRAV--RKSQSTSTGP-IVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFE 231

                           250       260
                    ....*....|....*....|....*
gi 514686563   4695 IVKALREQRMGLVQVAAQYRFCFTA 4719
Cdd:smart00194  232 IVKELRSQRPGMVQTEEQYIFLYRA 256
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
4483-4721 2.61e-92

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 300.31  E-value: 2.61e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563  4483 RQKNRYLDILAYDQTRVRLGDDGSGSDYINANYVtfPSTPTPFRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEG 4562
Cdd:pfam00102    2 LEKNRYKDVLPYDHTRVKLTGDPGPSDYINASYI--DGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEK 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563  4563 GRQKCAQYWPPGAGQTMTTPLLEVTHVSSTPDdpyDPEIITTKLKVRHRINGQVREITHVQYVGWPDHGVPESPDKFLDL 4642
Cdd:pfam00102   80 GREKCAQYWPEEEGESLEYGDFTVTLKKEKED---EKDYTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDL 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 514686563  4643 VDRVqRLRSQLPEDAPyILVHCSAGIGRSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRFCFTACL 4721
Cdd:pfam00102  157 LRKV-RKSSLDGRSGP-IVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 4510-4717 3.17e-78

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: 258.37  E-value: 3.17e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4510 YINANYVTFPSTPTpfRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGGRQKCAQYWPPGAGQTMTTPLLEVTHV 4589
Cdd:cd00047     1 YINASYIDGYRGPK--EYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGDITVTLV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4590 SSTPddpyDPEIITTKLKVRHRINGQVREITHVQYVGWPDHGVPESPDKFLDLVDRVQRLRSQlpEDAPyILVHCSAGIG 4669
Cdd:cd00047    79 SEEE----LSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKEARK--PNGP-IVVHCSAGVG 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 514686563 4670 RSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRFCF 4717
Cdd:cd00047   152 RTGTFIAIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIY 199
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 4456-4718 2.46e-67

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: 229.94  E-value: 2.46e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4456 GMKGAIEEFQTIPKTSATGSFTHSQR--ERQKNRYLDILAYDQTRVRLGDDGSG--SDYINANYVTFPSTPTPFrfIASQ 4531
Cdd:cd14543     1 QKRGIYEEYEDIRREPPAGTFLCSLApaNQEKNRYGDVLCLDQSRVKLPKRNGDerTDYINANFMDGYKQKNAY--IATQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4532 GPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGGRQKCAQYWPPGAGQTMTTPLLEVTHVSSTPDDPYdpeiITTKLKVRHR 4611
Cdd:cd14543    79 GPLPKTYSDFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHY----KKTTLEIHNT 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4612 INGQVREITHVQYVGWPDHGVP---ESPDKFLDLVDRVQRL--RSQLPEDA-----PYILVHCSAGIGRSGVLIVVLVML 4681
Cdd:cd14543   155 ETDESRQVTHFQFTSWPDFGVPssaAALLDFLGEVRQQQALavKAMGDRWKghppgPPIVVHCSAGIGRTGTFCTLDICL 234

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 514686563 4682 DRLRKKKLPNAREIVKALREQRMGLVQVAAQYRFCFT 4718
Cdd:cd14543   235 SQLEDVGTLNVMQTVRRMRTQRAFSIQTPDQYYFCYK 271
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 4510-4716 4.35e-65

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: 221.35  E-value: 4.35e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4510 YINANYVTFPSTPtPFRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGGRQKCAQYWPPGAGQTMTTPlLEVTHV 4589
Cdd:cd18533     1 YINASYITLPGTS-SKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEYGD-LTVELV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4590 SSTPDDpyDPEIITTKLKVRHRiNGQVREITHVQYVGWPDHGVPESPDKFLDLVDRVQRLRSQLPEDAPyILVHCSAGIG 4669
Cdd:cd18533    79 SEEEND--DGGFIVREFELSKE-DGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSASLDPP-IIVHCSAGVG 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 514686563 4670 RSGVLIV---VLVMLDRLRKKKLPNAR------EIVKALREQRMGLVQVAAQYRFC 4716
Cdd:cd18533   155 RTGTFIAldsLLDELKRGLSDSQDLEDsedpvyEIVNQLRKQRMSMVQTLRQYIFL 210
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 4510-4724 9.87e-65

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


Pssm-ID: 350386 [Multi-domain]  Cd Length: 207  Bit Score: 219.94  E-value: 9.87e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4510 YINANYVTFPSTPTPFRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGGRQKCAQYWPPGAGQTMTT-PLLEVTH 4588
Cdd:cd14538     1 YINASHIRIPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKPLICgGRLEVSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4589 VSSTPDDPYDPEIITtklkVRHRINGQVREITHVQYVGWPDHGVPESPDKFLDLVDRVQRLRSQLPedapyILVHCSAGI 4668
Cdd:cd14538    81 EKYQSLQDFVIRRIS----LRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIRYMRRIHNSGP-----IVVHCSAGI 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 514686563 4669 GRSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRFCFTACLAKL 4724
Cdd:cd14538   152 GRTGVLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 4510-4717 1.53e-63

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: 216.94  E-value: 1.53e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4510 YINANYVTFPSTPTPFRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGGRQKCAQYWPPGAGQTMTTPL--LEVT 4587
Cdd:cd14540     1 YINASHITATVGGKQRFYIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEHDALTFgeYKVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4588 HVSSTPDDPYdpeiITTKLKVRHRINGQVREITHVQYVGWPDHGVPESPDKFLDLVDRVQRLRSQLPEDA------PYIL 4661
Cdd:cd14540    81 TKFSVSSGCY----TTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSVRRHTNQDVaghnrnPPTL 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 514686563 4662 VHCSAGIGRSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRFCF 4717
Cdd:cd14540   157 VHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVY 212
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 4487-4715 9.09e-63

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: 214.91  E-value: 9.09e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4487 RYLDILAYDQTRVRLG--DDGSGSDYINANYVtfPSTPTPFRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGGR 4564
Cdd:cd14548     1 RYTNILPYDHSRVKLIpiNEEEGSDYINANYI--PGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4565 QKCAQYWPpgagqTMTTPL----LEVTHVSstpDDPYdPEIITTKLKVRHRinGQVREITHVQYVGWPDHGVPESPDKfl 4640
Cdd:cd14548    79 VKCDHYWP-----FDQDPVyygdITVTMLS---ESVL-PDWTIREFKLERG--DEVRSVRQFHFTAWPDHGVPEAPDS-- 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 514686563 4641 dLVDRVQRLRSQLPEDAPYILVHCSAGIGRSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRF 4715
Cdd:cd14548   146 -LLRFVRLVRDYIKQEKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIF 219
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 4480-4721 1.11e-62

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: 215.08  E-value: 1.11e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4480 QRERQKNRYLDILAYDQTRVRLGDDGsgsDYINANYVTFPSTPTPFRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQV 4559
Cdd:cd14597     1 KENRKKNRYKNILPYDTTRVPLGDEG---GYINASFIKMPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4560 VEGGRQKCAQYWPPGAGQT-MTTPLLEVTHVSSTPDDPYdpeiITTKLKVRHRINGQVREITHVQYVGWPDHGVPESPDK 4638
Cdd:cd14597    78 VEGGKIKCQRYWPEILGKTtMVDNRLQLTLVRMQQLKNF----VIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQ 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4639 FLDLVDRVQRLRSQLPedapyILVHCSAGIGRSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRFCFT 4718
Cdd:cd14597   154 LLTFISYMRHIHKSGP-----IITHCSAGIGRSGTLICIDVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQ 228


                  ...
gi 514686563 4719 ACL 4721
Cdd:cd14597   229 VIL 231
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 4509-4715 4.09e-62

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


Pssm-ID: 350389 [Multi-domain]  Cd Length: 212  Bit Score: 212.57  E-value: 4.09e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4509 DYINANYVTF--PSTPTPFRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGGRQKCAQYWPPGaGQTMTTPLLEV 4586
Cdd:cd14541     1 DYINANYVNMeiPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDL-GETMQFGNLQI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4587 THVSSTPDDPYdpeiITTKLKVRHRINGQVREITHVQYVGWPDHGVPESPDKFLDLVDRVQRLRSQLPEdaPyILVHCSA 4666
Cdd:cd14541    80 TCVSEEVTPSF----AFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQNRVGMVE--P-TVVHCSA 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 514686563 4667 GIGRSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRF 4715
Cdd:cd14541   153 GIGRTGVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRF 201
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 4485-4717 4.14e-62

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


Pssm-ID: 350393 [Multi-domain]  Cd Length: 231  Bit Score: 213.41  E-value: 4.14e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4485 KNRYLDILAYDQTRVRLGDDGSGSDYINANYVTFPSTPTpfRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGGR 4564
Cdd:cd14545     1 LNRYRDRDPYDHDRSRVKLKQGDNDYINASLVEVEEAKR--SYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4565 QKCAQYWPPGAGQTMTTPL--LEVTHVSSTPDDPYdpeiITTKLKVRHRINGQVREITHVQYVGWPDHGVPESPDKFLDL 4642
Cdd:cd14545    79 IKCAQYWPQGEGNAMIFEDtgLKVTLLSEEDKSYY----TVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNF 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 514686563 4643 VDRVQRLRSQLPEDAPYIlVHCSAGIGRSGVLIVV---LVMLDRLRKKKLpNAREIVKALREQRMGLVQVAAQYRFCF 4717
Cdd:cd14545   155 LQKVRESGSLSSDVGPPV-VHCSAGIGRSGTFCLVdtcLVLIEKGNPSSV-DVKKVLLEMRKYRMGLIQTPDQLRFSY 230
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 4483-4719 2.52e-60

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: 209.24  E-value: 2.52e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4483 RQKNRYLDILAYDQTRVRLGD---DGSGSDYINANYVTFP-STPTPFR----FIASQGPKPNTVNEHWQMLWEQRVHVIV 4554
Cdd:cd14544     2 KGKNRYKNILPFDHTRVILKDrdpNVPGSDYINANYIRNEnEGPTTDEnaktYIATQGCLENTVSDFWSMVWQENSRVIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4555 MLAQVVEGGRQKCAQYWpPGAGQTMTTPLLEVTHVSSTPDDPYD-PEIITTKLKVRHRIngqvREITHVQYVGWPDHGVP 4633
Cdd:cd14544    82 MTTKEVERGKNKCVRYW-PDEGMQKQYGPYRVQNVSEHDTTDYTlRELQVSKLDQGDPI----REIWHYQYLSWPDHGVP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4634 ESPDKFLDLVDRVQRLRSQLPEDAPyILVHCSAGIGRSGVLIVVLVMLDRLRKKKLPNAREI---VKALREQRMGLVQVA 4710
Cdd:cd14544   157 SDPGGVLNFLEDVNQRQESLPHAGP-IVVHCSAGIGRTGTFIVIDMLLDQIKRKGLDCDIDIqktIQMVRSQRSGMVQTE 235


                  ....*....
gi 514686563 4711 AQYRFCFTA 4719
Cdd:cd14544   236 AQYKFIYVA 244
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 4477-4726 2.42e-58

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: 203.96  E-value: 2.42e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4477 THSQRERQ------KNRYLDILAYDQTRVRL-GDDGS--GSDYINANYVT---FPSTPTPFRFIASQGPKPNTVNEHWQM 4544
Cdd:cd14606     7 LHQRLEGQrpenksKNRYKNILPFDHSRVILqGRDSNipGSDYINANYVKnqlLGPDENAKTYIASQGCLEATVNDFWQM 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4545 LWEQRVHVIVMLAQVVEGGRQKCAQYWPPGAGQTMTTPLLeVTHVSstpddpydpEIITTKLKVRH------RINGQVRE 4618
Cdd:cd14606    87 AWQENSRVIVMTTREVEKGRNKCVPYWPEVGMQRAYGPYS-VTNCG---------EHDTTEYKLRTlqvsplDNGELIRE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4619 ITHVQYVGWPDHGVPESPDKFLDLVDRVQRLRSQLPEDAPyILVHCSAGIGRSGVLIVVLVMLDRLRKKKLPNAREIVKA 4698
Cdd:cd14606   157 IWHYQYLSWPDHGVPSEPGGVLSFLDQINQRQESLPHAGP-IIVHCSAGIGRTGTIIVIDMLMENISTKGLDCDIDIQKT 235

                         250       260       270
                  ....*....|....*....|....*....|.
gi 514686563 4699 L---REQRMGLVQVAAQYRFCFTACLAKLDS 4726
Cdd:cd14606   236 IqmvRAQRSGMVQTEAQYKFIYVAIAQFIET 266
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 4483-4721 4.88e-58

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: 201.98  E-value: 4.88e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4483 RQKNRYLDILAYDQTRVRL----GDDGSgsDYINANYVTfpstptPFR----FIASQGPKPNTVNEHWQMLWEQRVHVIV 4554
Cdd:cd14554     7 KFKNRLVNILPYESTRVCLqpirGVEGS--DYINASFID------GYRqrgaYIATQGPLAETTEDFWRMLWEHNSTIIV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4555 MLAQVVEGGRQKCAQYWPPGAGQTMTTPLLEvthvsstPDDPYD-PEIITTKLKVRHRINGQVREITHVQYVGWPDHGVP 4633
Cdd:cd14554    79 MLTKLREMGREKCHQYWPAERSARYQYFVVD-------PMAEYNmPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVP 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4634 ESPDKFLDLVDRVQRLRSQLPEDAPyILVHCSAGIGRSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQY 4713
Cdd:cd14554   152 KSGEGFIDFIGQVHKTKEQFGQEGP-ITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQY 230


                  ....*...
gi 514686563 4714 RFCFTACL 4721
Cdd:cd14554   231 QFCYRAAL 238
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 4485-4721 4.36e-56

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: 197.77  E-value: 4.36e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4485 KNRYLDILAYDQTRVRLGDDgsgSDYINANYVTF--PSTPTPFRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEG 4562
Cdd:cd14600    43 KNRYKDVLPYDATRVVLQGN---EDYINASYVNMeiPSANIVNKYIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTER 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4563 GRQKCAQYWpPGAGQTMTTPLLEVTHVSSTPDDPY-DPEIITTKLKvrhriNGQVREITHVQYVGWPDHGVPESPDKFLD 4641
Cdd:cd14600   120 GRTKCHQYW-PDPPDVMEYGGFRVQCHSEDCTIAYvFREMLLTNTQ-----TGEERTVTHLQYVAWPDHGVPDDSSDFLE 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4642 LVDRVQRLRSqlpEDAPyILVHCSAGIGRSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRFCFTACL 4721
Cdd:cd14600   194 FVNYVRSKRV---ENEP-VLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKMRDQRAMMVQTSSQYKFVCEAIL 269
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 4483-4721 5.59e-56

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: 196.08  E-value: 5.59e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4483 RQKNRYLDILAYDQTRVRLGD-DG-SGSDYINANYVTfpstptPFR----FIASQGPKPNTVNEHWQMLWEQRVHVIVML 4556
Cdd:cd14553     4 KPKNRYANVIAYDHSRVILQPiEGvPGSDYINANYCD------GYRkqnaYIATQGPLPETFGDFWRMVWEQRSATIVMM 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4557 AQVVEGGRQKCAQYWPPGAGQT---MTTPLLEVTHVSstpddpydpeIITTKLKVRHRIN-GQVREITHVQYVGWPDHGV 4632
Cdd:cd14553    78 TKLEERSRVKCDQYWPTRGTETyglIQVTLLDTVELA----------TYTVRTFALHKNGsSEKREVRQFQFTAWPDHGV 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4633 PESPDKFLDLVDRVqrlRSQLPEDAPYILVHCSAGIGRSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQ 4712
Cdd:cd14553   148 PEHPTPFLAFLRRV---KACNPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQ 224


                  ....*....
gi 514686563 4713 YRFCFTACL 4721
Cdd:cd14553   225 YIFIHDALL 233
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 4462-4719 8.83e-56

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: 196.58  E-value: 8.83e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4462 EEFQTIPKTSAT----GSFTH----SQRERQKNRYLDILAYDQTRVRLG--DDGSGSDYINANYVTFPSTPTpfRFIASQ 4531
Cdd:cd14603     2 GEFSEIRACSAAfkadYVCSTvaggRKENVKKNRYKDILPYDQTRVILSllQEEGHSDYINANFIKGVDGSR--AYIATQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4532 GPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGGRQKCAQYWpPGAGQTMTTPLLEVTHVSstpDDPYDPEIITTKLKVRHR 4611
Cdd:cd14603    80 GPLSHTVLDFWRMIWQYGVKVILMACREIEMGKKKCERYW-AQEQEPLQTGPFTITLVK---EKRLNEEVILRTLKVTFQ 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4612 inGQVREITHVQYVGWPDHGVPESPDKFLDLVDRVQRLRSqlpEDAPYILVHCSAGIGRSGVLIVVLVMLDRLRKKKLP- 4690
Cdd:cd14603   156 --KESRSVSHFQYMAWPDHGIPDSPDCMLAMIELARRLQG---SGPEPLCVHCSAGCGRTGVICTVDYVRQLLLTQRIPp 230

                         250       260       270
                  ....*....|....*....|....*....|.
gi 514686563 4691 --NAREIVKALREQRMGLVQVAAQYRFCFTA 4719
Cdd:cd14603   231 dfSIFDVVLEMRKQRPAAVQTEEQYEFLYHT 261
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 4486-4715 6.29e-55

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: 192.61  E-value: 6.29e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4486 NRYLDILAYDQTRVRLG--DDGSGSDYINANYVTFPSTPTPfRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGg 4563
Cdd:cd14547     1 NRYKTILPNEHSRVCLPsvDDDPLSSYINANYIRGYDGEEK-AYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4564 RQKCAQYWPPGAGQTMTTplLEVTHVSSTPDDPYdpeiITTKLKVRHriNGQVREITHVQYVGWPDHGVPESPDKFLDLV 4643
Cdd:cd14547    79 KEKCAQYWPEEENETYGD--FEVTVQSVKETDGY----TVRKLTLKY--GGEKRYLKHYWYTSWPDHKTPEAAQPLLSLV 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514686563 4644 DRVQRLRSQLPEDAPyILVHCSAGIGRSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRF 4715
Cdd:cd14547   151 QEVEEARQTEPHRGP-IVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEF 221
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 4486-4715 1.39e-54

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: 191.95  E-value: 1.39e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4486 NRYLDILAYDQTRVRLGDDGSG-SDYINANYVtfPSTPTPFRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGGR 4564
Cdd:cd14615     1 NRYNNVLPYDISRVKLSVQSHStDDYINANYM--PGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4565 QKCAQYWPpgAGQTMTTPLLEVTHVSSTPddpyDPEIITTKLKVRHRINGQVREITHVQYVGWPDHGVPESPDKFLDLVD 4644
Cdd:cd14615    79 TKCEEYWP--SKQKKDYGDITVTMTSEIV----LPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRH 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 514686563 4645 RVQRLRSQLPEDAPyILVHCSAGIGRSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRF 4715
Cdd:cd14615   153 LVREYMKQNPPNSP-ILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVF 222
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 4450-4717 3.30e-54

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: 192.90  E-value: 3.30e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4450 QRFLDEGMkgAIEEFQTIPKTSATGSFTHSQ--RERQKNRYLDILAYDQTRVRL---GDDGSGsdYINANYVTFPSTPTP 4524
Cdd:cd14599     6 ERKLEEGM--VFTEYEQIPKKKADGVFTTATlpENAERNRIREVVPYEENRVELvptKENNTG--YINASHIKVTVGGEE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4525 FRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGGRQKCAQYWPPGAGQ--TMTTPLLEVTHVSSTPDDPYdpeiI 4602
Cdd:cd14599    82 WHYIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPKLGSKhsSATYGKFKVTTKFRTDSGCY----A 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4603 TTKLKVRHRINGQVREITHVQYVGWPDHGVPESPDKFLDLVDRVQRLR----SQLPEDA---PYILVHCSAGIGRSGVLI 4675
Cdd:cd14599   158 TTGLKVKHLLSGQERTVWHLQYTDWPDHGCPEEVQGFLSYLEEIQSVRrhtnSMLDSTKncnPPIVVHCSAGVGRTGVVI 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 514686563 4676 VVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRFCF 4717
Cdd:cd14599   238 LTELMIGCLEHNEKVEVPVMLRHLREQRMFMIQTIAQYKFVY 279
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 4510-4716 1.29e-53

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: 187.94  E-value: 1.29e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4510 YINANYVtfPSTPTPFRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGGRQKCAQYWPpgAGQTMTTPLLEVTHV 4589
Cdd:cd14549     1 YINANYV--DGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWP--KEGTETYGNIQVTLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4590 SSTPDDPYDPEIIT---TKLKVRHRINGQvREITHVQYVGWPDHGVPESPDKFLDLVDRVQRLRsqlPEDAPYILVHCSA 4666
Cdd:cd14549    77 STEVLATYTVRTFSlknLKLKKVKGRSSE-RVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAAN---PPGAGPIVVHCSA 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 514686563 4667 GIGRSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRFC 4716
Cdd:cd14549   153 GVGRTGTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFI 202
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 4486-4715 4.46e-53

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


Pssm-ID: 350467 [Multi-domain]  Cd Length: 233  Bit Score: 187.79  E-value: 4.46e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4486 NRYLDILAYDQTRVRLG--DDGSGSDYINANYVtfPSTPTPFRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGG 4563
Cdd:cd14619     1 NRFRNVLPYDWSRVPLKpiHEEPGSDYINANYM--PGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4564 RQKCAQYWPPGAgQTMTTPLLEVTHVSstpdDPYDPEIITTKLKVRHRINGQVREITHVQYVGWPDHGVPESPDKFLDLV 4643
Cdd:cd14619    79 RVKCEHYWPLDY-TPCTYGHLRVTVVS----EEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFR 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514686563 4644 DRVQRLRSQLPEDAPYIlVHCSAGIGRSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRF 4715
Cdd:cd14619   154 RLLRQWLDQTMSGGPTV-VHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVF 224
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 4510-4724 1.13e-51

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: 182.64  E-value: 1.13e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4510 YINANYVTFPSTPTPFRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGGRQKCAQYWPPGAGQTMttpllEVTHV 4589
Cdd:cd14596     1 YINASYITMPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPM-----ELENY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4590 SSTPDDPYDPEIITTK-LKVRHRINGQVREITHVQYVGWPDHGVPESPDKFLDLVDRVQRLRSQLPedapyILVHCSAGI 4668
Cdd:cd14596    76 QLRLENYQALQYFIIRiIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFICYMRKVHNTGP-----IVVHCSAGI 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 514686563 4669 GRSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRFCFTACLAKL 4724
Cdd:cd14596   151 GRAGVLICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVL 206
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 4486-4721 6.44e-51

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: 181.29  E-value: 6.44e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4486 NRYLDILAYDQTRVRLGDDGSG--SDYINANYVtfPSTPTPFRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGG 4563
Cdd:cd14618     1 NRYPHVLPYDHSRVRLSQLGGEphSDYINANFI--PGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4564 RQKCAQYWP----PGAGQTMTTPLLevthvSSTPDDpydpEIITTKLKVRHRINGQVREITHVQYVGWPDHGVPESPDKF 4639
Cdd:cd14618    79 RVLCDHYWPsestPVSYGHITVHLL-----AQSSED----EWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSL 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4640 LDLVDRVQRlRSQLPEDAPYILVHCSAGIGRSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRFcFTA 4719
Cdd:cd14618   150 MAFRELVRE-HVQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIF-LHS 227


                  ..
gi 514686563 4720 CL 4721
Cdd:cd14618   228 CI 229
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 4480-4721 1.06e-50

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: 182.53  E-value: 1.06e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4480 QRERQKNRYLDILAYDQTRVRLGDDGSgsDYINANYVTFPSTPTpfRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQV 4559
Cdd:cd14608    23 PKNKNRNRYRDVSPFDHSRIKLHQEDN--DYINASLIKMEEAQR--SYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4560 VEGGRQKCAQYWPPGAGQTMT--TPLLEVTHVSSTPDDPYdpeiITTKLKVRHRINGQVREITHVQYVGWPDHGVPESPD 4637
Cdd:cd14608    99 MEKGSLKCAQYWPQKEEKEMIfeDTNLKLTLISEDIKSYY----TVRQLELENLTTQETREILHFHYTTWPDFGVPESPA 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4638 KFLDLVDRVQRLRSQLPEDAPyILVHCSAGIGRSGVLIVVLVMLDRLRKKKLPNAREIVKAL---REQRMGLVQVAAQYR 4714
Cdd:cd14608   175 SFLNFLFKVRESGSLSPEHGP-VVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLlemRKFRMGLIQTADQLR 253


                  ....*..
gi 514686563 4715 FCFTACL 4721
Cdd:cd14608   254 FSYLAVI 260
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 4483-4719 5.52e-50

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: 179.78  E-value: 5.52e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4483 RQKNRYLDILAYDQTRVRLgdDGSGSDYINANYVTFPSTPTpfRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEG 4562
Cdd:cd14607    25 RNRNRYRDVSPYDHSRVKL--QNTENDYINASLVVIEEAQR--SYILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEK 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4563 GRQKCAQYWPPGAGQTMT--TPLLEVTHVSSTPDDPYdpeiiTTKLKVRHRIN-GQVREITHVQYVGWPDHGVPESPDKF 4639
Cdd:cd14607   101 DSVKCAQYWPTDEEEVLSfkETGFSVKLLSEDVKSYY-----TVHLLQLENINsGETRTISHFHYTTWPDFGVPESPASF 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4640 LDLVDRVQRLRSQLPEDAPYIlVHCSAGIGRSGVLIVV---LVMLDRlRKKKLPNAREIVKALREQRMGLVQVAAQYRFC 4716
Cdd:cd14607   176 LNFLFKVRESGSLSPEHGPAV-VHCSAGIGRSGTFSLVdtcLVLMEK-KDPDSVDIKQVLLDMRKYRMGLIQTPDQLRFS 253


                  ...
gi 514686563 4717 FTA 4719
Cdd:cd14607   254 YMA 256
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 4443-4721 1.02e-49

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: 179.46  E-value: 1.02e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4443 SNIRDEQQRF-LDEGMKGAiEEFQTI-PKTSATGSFTHSQRERQKNRYLDILAYDQTRVRLG--DDGSGSDYINANYVTF 4518
Cdd:cd14626     1 SDLADNIERLkANDGLKFS-QEYESIdPGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTsvDGVPGSDYINANYIDG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4519 PSTPTPFrfIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGGRQKCAQYWPpgAGQTMTTPLLEVTHVSSTPDDPYD 4598
Cdd:cd14626    80 YRKQNAY--IATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWP--IRGTETYGMIQVTLLDTVELATYS 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4599 PEIITtklkVRHRINGQVREITHVQYVGWPDHGVPESPDKFLDLVDRVQRLRsqlPEDAPYILVHCSAGIGRSGVLIVVL 4678
Cdd:cd14626   156 VRTFA----LYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVKACN---PPDAGPMVVHCSAGVGRTGCFIVID 228

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 514686563 4679 VMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRFCFTACL 4721
Cdd:cd14626   229 AMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEALL 271
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 4462-4721 1.05e-49

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: 179.46  E-value: 1.05e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4462 EEFQTIPKTSATGSFT--HSQR--ERQKNRYLDILAYDQTRVRL----GDDGSGSDYINANYVTFPSTPTPFrfIASQGP 4533
Cdd:cd17667     3 EDFEEVQRCTADMNITaeHSNHpdNKHKNRYINILAYDHSRVKLrplpGKDSKHSDYINANYVDGYNKAKAY--IATQGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4534 KPNTVNEHWQMLWEQRVHVIVMLAQVVEGGRQKCAQYWPPGA----GQTMTTplLEVTHVSSTpddpYDPEIIT---TKL 4606
Cdd:cd17667    81 LKSTFEDFWRMIWEQNTGIIVMITNLVEKGRRKCDQYWPTENseeyGNIIVT--LKSTKIHAC----YTVRRFSirnTKV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4607 KVRHRIN--GQVREITHVQ--YVGWPDHGVPESPDKFLDLVDRVQrlRSQLPEDAPyILVHCSAGIGRSGVLIVVLVMLD 4682
Cdd:cd17667   155 KKGQKGNpkGRQNERTVIQyhYTQWPDMGVPEYALPVLTFVRRSS--AARTPEMGP-VLVHCSAGVGRTGTYIVIDSMLQ 231

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 514686563 4683 RLRKKKLPNAREIVKALREQRMGLVQVAAQYRFCFTACL 4721
Cdd:cd17667   232 QIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALL 270
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 4455-4728 2.68e-49

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: 179.16  E-value: 2.68e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4455 EGMKGAIEEFQTIPKTSA-TGSFTHSQR--ERQKNRYLDILAYDQTRVRLGD--DGSGSDYINANYVTFPSTPTPFrfIA 4529
Cdd:cd14628    22 ENVTGMELEFKRLASSKAhTSRFISANLpcNKFKNRLVNIMPYESTRVCLQPirGVEGSDYINASFIDGYRQQKAY--IA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4530 SQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGGRQKCAQYWPPGAGQTMTTPLLEvthvsstPDDPYD-PEIITTKLKV 4608
Cdd:cd14628   100 TQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVD-------PMAEYNmPQYILREFKV 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4609 RHRINGQVREITHVQYVGWPDHGVPESPDKFLDLVDRVQRLRSQLPEDAPyILVHCSAGIGRSGVLIVVLVMLDRLRKKK 4688
Cdd:cd14628   173 TDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGP-ISVHCSAGVGRTGVFITLSIVLERMRYEG 251

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 514686563 4689 LPNAREIVKALREQRMGLVQVAAQYRFCFTACLAKLDSID 4728
Cdd:cd14628   252 VVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYLGSFD 291
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 4455-4726 3.78e-49

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: 178.39  E-value: 3.78e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4455 EGMKGAIEEFQTIPKTSA-TGSFTHSQR--ERQKNRYLDILAYDQTRVRLGD--DGSGSDYINANYVTFPSTPTPFrfIA 4529
Cdd:cd14627    23 EHVTGMELEFKRLANSKAhTSRFISANLpcNKFKNRLVNIMPYETTRVCLQPirGVEGSDYINASFIDGYRQQKAY--IA 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4530 SQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGGRQKCAQYWPPGAGQTMTTPLLEvthvsstPDDPYD-PEIITTKLKV 4608
Cdd:cd14627   101 TQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVD-------PMAEYNmPQYILREFKV 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4609 RHRINGQVREITHVQYVGWPDHGVPESPDKFLDLVDRVQRLRSQLPEDAPyILVHCSAGIGRSGVLIVVLVMLDRLRKKK 4688
Cdd:cd14627   174 TDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGP-ISVHCSAGVGRTGVFITLSIVLERMRYEG 252

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 514686563 4689 LPNAREIVKALREQRMGLVQVAAQYRFCFTACLAKLDS 4726
Cdd:cd14627   253 VVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYLGS 290
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 4483-4719 1.24e-48

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


Pssm-ID: 350453 [Multi-domain]  Cd Length: 253  Bit Score: 175.59  E-value: 1.24e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4483 RQKNRYLDILAYDQTRVRLGD---DGSGSDYINANYV-------TFPSTPTPfRFIASQGPKPNTVNEHWQMLWEQRVHV 4552
Cdd:cd14605     3 KNKNRYKNILPFDHTRVVLHDgdpNEPVSDYINANIImpefetkCNNSKPKK-SYIATQGCLQNTVNDFWRMVFQENSRV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4553 IVMLAQVVEGGRQKCAQYWPPGAGqTMTTPLLEVTHVSSTPDDPYdpeiITTKLKVRHRINGQV-REITHVQYVGWPDHG 4631
Cdd:cd14605    82 IVMTTKEVERGKSKCVKYWPDEYA-LKEYGVMRVRNVKESAAHDY----ILRELKLSKVGQGNTeRTVWQYHFRTWPDHG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4632 VPESPDKFLDLVDRVQRLRSQLPEDAPyILVHCSAGIGRSGVLIVVLVMLDRLRKKKLP---NAREIVKALREQRMGLVQ 4708
Cdd:cd14605   157 VPSDPGGVLDFLEEVHHKQESIMDAGP-VVVHCSAGIGRTGTFIVIDILIDIIREKGVDcdiDVPKTIQMVRSQRSGMVQ 235

                         250
                  ....*....|.
gi 514686563 4709 VAAQYRFCFTA 4719
Cdd:cd14605   236 TEAQYRFIYMA 246
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 4485-4726 6.28e-48

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: 174.91  E-value: 6.28e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4485 KNRYLDILAYDQTRVRLGD--DGSGSDYINANYVTFPSTPTPFrfIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEG 4562
Cdd:cd14629    56 KNRLVNIMPYELTRVCLQPirGVEGSDYINASFIDGYRQQKAY--IATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREM 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4563 GRQKCAQYWPPGAGQTMTTPLLEvthvsstPDDPYD-PEIITTKLKVRHRINGQVREITHVQYVGWPDHGVPESPDKFLD 4641
Cdd:cd14629   134 GREKCHQYWPAERSARYQYFVVD-------PMAEYNmPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFID 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4642 LVDRVQRLRSQLPEDAPyILVHCSAGIGRSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRFCFTACL 4721
Cdd:cd14629   207 FIGQVHKTKEQFGQDGP-ITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAAL 285


                  ....*
gi 514686563 4722 AKLDS 4726
Cdd:cd14629   286 EYLGS 290
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 4462-4721 9.27e-47

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: 171.43  E-value: 9.27e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4462 EEFQTI-PKTSATGSFTHSQRERQKNRYLDILAYDQTRVRLG--DDGSGSDYINANYVTFPSTPTPFrfIASQGPKPNTV 4538
Cdd:cd14625    26 QEYESIdPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQpiEGIMGSDYINANYIDGYRKQNAY--IATQGPLPETF 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4539 NEHWQMLWEQRVHVIVMLAQVVEGGRQKCAQYWpPGAGqTMTTPLLEVTHVsstpdDPYDPEIITTKLKVRHRiNG--QV 4616
Cdd:cd14625   104 GDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYW-PSRG-TETYGMIQVTLL-----DTIELATFCVRTFSLHK-NGssEK 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4617 REITHVQYVGWPDHGVPESPDKFLDLVDRVQRLRsqlPEDAPYILVHCSAGIGRSGVLIVVLVMLDRLRKKKLPNAREIV 4696
Cdd:cd14625   176 REVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCN---PPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHV 252

                         250       260
                  ....*....|....*....|....*
gi 514686563 4697 KALREQRMGLVQVAAQYRFCFTACL 4721
Cdd:cd14625   253 TLMRSQRNYMVQTEDQYSFIHDALL 277
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 4509-4721 1.68e-46

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: 167.81  E-value: 1.68e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4509 DYINANYVTF--PSTPTPFRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGGRQKCAQYWPPGAGQTmTTPLLEV 4586
Cdd:cd14601     1 DYINANYINMeiPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSS-SYGGFQV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4587 THVSSTPDDPYdpeiITTKLKVRHRINGQVREITHVQYVGWPDHGVPESPDKFLDLVDRVQRLRSQLPEDapyILVHCSA 4666
Cdd:cd14601    80 TCHSEEGNPAY----VFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGKDEP---VVVHCSA 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 514686563 4667 GIGRSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRFCFTACL 4721
Cdd:cd14601   153 GIGRTGVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAIL 207
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 4483-4715 2.43e-46

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: 168.91  E-value: 2.43e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4483 RQKNRYLDILAYDQTRVRL--GDDGSGSDYINANYVtfPSTPTPFRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVV 4560
Cdd:cd14614    13 RCKNRYTNILPYDFSRVKLvsMHEEEGSDYINANYI--PGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCN 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4561 EGGRQKCAQYWP----PGAGQTMTTPLLEVTHvsstpddpyDPEIITTKLKVRHriNGQVREITHVQYVGWPDHGVP--- 4633
Cdd:cd14614    91 EKRRVKCDHYWPfteePVAYGDITVEMLSEEE---------QPDWAIREFRVSY--ADEVQDVMHFNYTAWPDHGVPtan 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4634 --ESPDKFLDLVdRVQRLRSQLPedapyILVHCSAGIGRSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAA 4711
Cdd:cd14614   160 aaESILQFVQMV-RQQAVKSKGP-----MIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEE 233


                  ....
gi 514686563 4712 QYRF 4715
Cdd:cd14614   234 QYIF 237
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 4510-4713 2.64e-46

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: 166.93  E-value: 2.64e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4510 YINANYVTfpSTPTPFRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGGRQKCAQYWPPGAGQTMTtpLLEVThV 4589
Cdd:cd14557     1 YINASYID--GFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRA--FGDVV-V 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4590 SSTPDDPYdPEIITTKLKVRH-RINGQVREITHVQYVGWPDHGVPESPDKFLDLVDRVQRLRSQLpeDAPyILVHCSAGI 4668
Cdd:cd14557    76 KINEEKIC-PDYIIRKLNINNkKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNFF--SGP-IVVHCSAGV 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 514686563 4669 GRSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQY 4713
Cdd:cd14557   152 GRTGTYIGIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQY 196
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 4510-4717 6.47e-46

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: 166.69  E-value: 6.47e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4510 YINANYVTFPSTPTPFRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGGRQKCAQYWPPGAGQ--TMTTPLLEVT 4587
Cdd:cd14598     1 YINASHIKVTVGGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRLGSRhnTVTYGRFKIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4588 HVSSTPDDPYdpeiITTKLKVRHRINGQVREITHVQYVGWPDHGVPESPDKFLDLVDRVQRLRSQLPEDA------PYIL 4661
Cdd:cd14598    81 TRFRTDSGCY----ATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTNSTIdpkspnPPVL 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 514686563 4662 VHCSAGIGRSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRFCF 4717
Cdd:cd14598   157 VHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVY 212
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 4486-4715 1.84e-45

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: 165.48  E-value: 1.84e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4486 NRYLDILAYDQTRVRLG--DDGSGSDYINANYVtfPSTPTPFRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGG 4563
Cdd:cd14617     1 NRYNNILPYDSTRVKLSnvDDDPCSDYINASYI--PGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4564 RQKCAQYWPpgagqTMTTPLLEVTHVSSTPDDPYDPEIITTKLKV--RHRINGQvREITHVQYVGWPDHGVPESPDKFLD 4641
Cdd:cd14617    79 RVKCDHYWP-----ADQDSLYYGDLIVQMLSESVLPEWTIREFKIcsEEQLDAP-RLVRHFHYTVWPDHGVPETTQSLIQ 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514686563 4642 LVDRVQRLRSQLPEDAPYIlVHCSAGIGRSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRF 4715
Cdd:cd14617   153 FVRTVRDYINRTPGSGPTV-VHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVY 225
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 4462-4721 1.93e-45

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: 167.60  E-value: 1.93e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4462 EEFQTI-PKTSATGSFTHSQRERQKNRYLDILAYDQTRVRLG--DDGSGSDYINANYVTFPSTPTPFrfIASQGPKPNTV 4538
Cdd:cd14624    26 QEYESIdPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSaiEGIPGSDYINANYIDGYRKQNAY--IATQGALPETF 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4539 NEHWQMLWEQRVHVIVMLAQVVEGGRQKCAQYWPPGAgqTMTTPLLEVTHVSSTPDDPYdpeiITTKLKVRHRINGQVRE 4618
Cdd:cd14624   104 GDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPSRG--TETYGLIQVTLLDTVELATY----CVRTFALYKNGSSEKRE 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4619 ITHVQYVGWPDHGVPESPDKFLDLVDRVQRLRsqlPEDAPYILVHCSAGIGRSGVLIVVLVMLDRLRKKKLPNAREIVKA 4698
Cdd:cd14624   178 VRQFQFTAWPDHGVPEHPTPFLAFLRRVKTCN---PPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTVDIYGHVTL 254

                         250       260
                  ....*....|....*....|...
gi 514686563 4699 LREQRMGLVQVAAQYRFCFTACL 4721
Cdd:cd14624   255 MRAQRNYMVQTEDQYIFIHDALL 277
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 4483-4721 4.73e-45

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: 164.81  E-value: 4.73e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4483 RQKNRYLDILAYDQTRVRLG--DDGSGSDYINANYVTfpSTPTPFRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVV 4560
Cdd:cd14630     4 RNKNRYGNIISYDHSRVRLQllDGDPHSDYINANYID--GYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4561 EGGRQKCAQYWPpgaGQTMTTPLLEVTHVSSTPDDPYDPEIITTKLKVRHringQVREITHVQYVGWPDHGVPESPDKFL 4640
Cdd:cd14630    82 EVGRVKCVRYWP---DDTEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYH----EIREIRQFHFTSWPDHGVPCYATGLL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4641 DLVDRVQRLRsqlPEDAPYILVHCSAGIGRSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRFCFTAC 4720
Cdd:cd14630   155 GFVRQVKFLN---PPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAI 231


                  .
gi 514686563 4721 L 4721
Cdd:cd14630   232 L 232
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 4486-4715 6.53e-45

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: 163.92  E-value: 6.53e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4486 NRYLDILAYDQTRVRLGDDGS--GSDYINANYVTfpSTPTPFRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGG 4563
Cdd:cd14616     1 NRFPNIKPYNNNRVKLIADAGvpGSDYINASYIS--GYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4564 RQKCAQYWP----PGA--GQTMTTPLLEVTHVSSTPDDpydpeiittkLKV-RHrinGQVREITHVQYVGWPDHGVPESP 4636
Cdd:cd14616    79 RIRCHQYWPednkPVTvfGDIVITKLMEDVQIDWTIRD----------LKIeRH---GDYMMVRQCNFTSWPEHGVPESS 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 514686563 4637 DKFLDLVDRVqrlRSQLPEDAPYILVHCSAGIGRSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRF 4715
Cdd:cd14616   146 APLIHFVKLV---RASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIF 221
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 4456-4721 9.76e-45

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: 165.22  E-value: 9.76e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4456 GMKGAIEEF---QTIPKTSATgsfthSQRERQKNRYLDILAYDQTRVRLG--DDGSGSDYINANYVTFPSTPTpfRFIAS 4530
Cdd:cd14633    16 GFKEEYESFfegQSAPWDSAK-----KDENRMKNRYGNIIAYDHSRVRLQpiEGETSSDYINGNYIDGYHRPN--HYIAT 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4531 QGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGGRQKCAQYWPPGAG--QTMTTPLLEVTHVSstpddpydpEIITTKLKV 4608
Cdd:cd14633    89 QGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTEiyKDIKVTLIETELLA---------EYVIRTFAV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4609 RHRINGQVREITHVQYVGWPDHGVPESPDKFLDLVDRVqrlRSQLPEDAPYILVHCSAGIGRSGVLIVVLVMLDRLRKKK 4688
Cdd:cd14633   160 EKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVRQV---KSKSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREG 236

                         250       260       270
                  ....*....|....*....|....*....|...
gi 514686563 4689 LPNAREIVKALREQRMGLVQVAAQYRFCFTACL 4721
Cdd:cd14633   237 VVDIYNCVRELRSRRVNMVQTEEQYVFIHDAIL 269
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 4510-4715 1.01e-44

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: 162.59  E-value: 1.01e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4510 YINANYVTFPSTPTPFrfIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGGRQKCAQYWPPGAGQTMTTPLLEVTHV 4589
Cdd:cd14542     1 YINANFIKGVSGSKAY--IATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLQFGPFKISLE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4590 SstpDDPYDPEIITTKLKVRHriNGQVREITHVQYVGWPDHGVPESPDKFLDLVDRVQRLrsQLPEDAPyILVHCSAGIG 4669
Cdd:cd14542    79 K---EKRVGPDFLIRTLKVTF--QKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDY--QGSEDVP-ICVHCSAGCG 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 514686563 4670 RSGVLIVVLVMLDRLRKKKLP---NAREIVKALREQRMGLVQVAAQYRF 4715
Cdd:cd14542   151 RTGTICAIDYVWNLLKTGKIPeefSLFDLVREMRKQRPAMVQTKEQYEL 199
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 4484-4719 2.47e-44

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: 164.72  E-value: 2.47e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4484 QKNRYLDILAYDQTRVRLGDDGSG--SDYINANYVTfpSTPTPFRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVE 4561
Cdd:cd14604    59 KKNRYKDILPFDHSRVKLTLKTSSqdSDYINANFIK--GVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFE 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4562 GGRQKCAQYWPPGAGQTMTtplLEVTHVSSTPDDPYDPEIITTKLKvrhRINGQVREITHVQYVGWPDHGVPESPDKFLD 4641
Cdd:cd14604   137 MGRKKCERYWPLYGEEPMT---FGPFRISCEAEQARTDYFIRTLLL---EFQNETRRLYQFHYVNWPDHDVPSSFDSILD 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4642 LVDRVQRLrsQLPEDAPyILVHCSAGIGRSGVLIVVLVMLDRLRKKKLP---NAREIVKALREQRMGLVQVAAQYRFCFT 4718
Cdd:cd14604   211 MISLMRKY--QEHEDVP-ICIHCSAGCGRTGAICAIDYTWNLLKAGKIPeefNVFNLIQEMRTQRHSAVQTKEQYELVHR 287


                  .
gi 514686563 4719 A 4719
Cdd:cd14604   288 A 288
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 4510-4717 3.56e-44

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: 161.01  E-value: 3.56e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4510 YINANYVTFPSTPTPfRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGGRQKCAQYWPPGAGQTMTTPLLEVThV 4589
Cdd:cd14539     1 YINASLIEDLTPYCP-RFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALVYGAITVS-L 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4590 SSTPDDPYDPEIIttkLKVRHRINGQVREITHVQYVGWPDHGVPESPDKFLDLVDRVQR-LRSQLPEDAPyILVHCSAGI 4668
Cdd:cd14539    79 QSVRTTPTHVERI---ISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHShYLQQRSLQTP-IVVHCSSGV 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 514686563 4669 GRSGVL-IVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRFCF 4717
Cdd:cd14539   155 GRTGAFcLLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCY 204
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 4485-4721 5.29e-43

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: 159.23  E-value: 5.29e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4485 KNRYLDILAYDQTRVRLGDDGSG---SDYINANYVTfPSTPTPFRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVE 4561
Cdd:cd14612    18 KDRYKTILPNPQSRVCLRRAGSQeeeGSYINANYIR-GYDGKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKLKE 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4562 gGRQKCAQYWPPGAGqTMTTPLLEVTHVSSTpddpydPEIITTKLKVRHRinGQVREITHVQYVGWPDHGVPESPDKFLD 4641
Cdd:cd14612    97 -KKEKCVHYWPEKEG-TYGRFEIRVQDMKEC------DGYTIRDLTIQLE--EESRSVKHYWFSSWPDHQTPESAGPLLR 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4642 LVDRVQRLRSQLPEDAPyILVHCSAGIGRSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRFCF-TAC 4720
Cdd:cd14612   167 LVAEVEESRQTAASPGP-IVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLHhTLA 245


                  .
gi 514686563 4721 L 4721
Cdd:cd14612   246 L 246
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 4488-4721 2.22e-42

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: 156.64  E-value: 2.22e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4488 YLDILAYDQTRVRLG--DDGSGSDYINANYVTFPSTPTpfRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGGRQ 4565
Cdd:cd14620     1 YPNILPYDHSRVILSqlDGIPCSDYINASYIDGYKEKN--KFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4566 KCAQYWPPGAGQTMTTPLLEVTHVSSTPDDPYDPEIITTKLkvrHRINGQVREITHVQYVGWPDHGVPESPDKFLDLVDR 4645
Cdd:cd14620    79 KCYQYWPDQGCWTYGNIRVAVEDCVVLVDYTIRKFCIQPQL---PDGCKAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKK 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 514686563 4646 VQRLRsqlPEDAPYILVHCSAGIGRSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRFCFTACL 4721
Cdd:cd14620   156 VKSVN---PVHAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQALL 228
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 4485-4721 1.12e-41

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: 155.00  E-value: 1.12e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4485 KNRYLDILAYDQTRVRLG--DDGSGSDYINANYVTfpSTPTPFRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEG 4562
Cdd:cd14602     1 KNRYKDILPYDHSRVELSliTSDEDSDYINANFIK--GVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4563 GRQKCAQYWP-PGAGQTMTTPlLEVTHVSSTPDDPYdpeIITTkLKVrhRINGQVREITHVQYVGWPDHGVPESPDKFLD 4641
Cdd:cd14602    79 GKKKCERYWAePGEMQLEFGP-FSVTCEAEKRKSDY---IIRT-LKV--KFNSETRTIYQFHYKNWPDHDVPSSIDPILE 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4642 LVDRVqrlRSQLPEDAPYILVHCSAGIGRSGVLIVVLVMLDRLRKKKLP---NAREIVKALREQRMGLVQVAAQYRFCFT 4718
Cdd:cd14602   152 LIWDV---RCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPenfSVFSLIQEMRTQRPSLVQTKEQYELVYN 228


                  ...
gi 514686563 4719 ACL 4721
Cdd:cd14602   229 AVI 231
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 4439-4721 1.73e-41

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: 156.72  E-value: 1.73e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4439 PHDASNIRDEQQRFLDEGMKGAIEEFQTIPKTSATGSFTHSQRE--RQKNRYLDILAYDQTRVRLG--DDGSGSDYINAN 4514
Cdd:cd14621     7 PLPVDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEenKEKNRYVNILPYDHSRVHLTpvEGVPDSDYINAS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4515 YVTFPSTPTpfRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGGRQKCAQYWPPGAGQTMTTPLLEVTHVSSTPD 4594
Cdd:cd14621    87 FINGYQEKN--KFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWTYGNIRVSVEDVTVLVD 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4595 DPYDPEIITTKLKVRHRinGQVREITHVQYVGWPDHGVPESPDKFLDLVDRVQRLRsqlPEDAPYILVHCSAGIGRSGVL 4674
Cdd:cd14621   165 YTVRKFCIQQVGDVTNK--KPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKNCN---PQYAGAIVVHCSAGVGRTGTF 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 514686563 4675 IVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRFCFTACL 4721
Cdd:cd14621   240 IVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALL 286
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 4460-4727 2.50e-41

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: 155.60  E-value: 2.50e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4460 AIEEFQTIPKTSATGsfthsQRER--QKNRYLDILAYDQTRV--RLGDDGSGSDYINANYVTF--PSTPTpfrFIASQGP 4533
Cdd:cd14610    25 ALCAYQAEPNATNVA-----QREEnvQKNRSLAVLPYDHSRIilKAENSHSHSDYINASPIMDhdPRNPA---YIATQGP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4534 KPNTVNEHWQMLWEQRVHVIVMLAQVVEGGRQKCAQYWPPGAgqtmtTPLLEVTHVSSTPDDPYDPEIITTKLKVRHRIN 4613
Cdd:cd14610    97 LPATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEG-----SNLYHIYEVNLVSEHIWCEDFLVRSFYLKNLQT 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4614 GQVREITHVQYVGWPDHGVPESPDKFLDL---VDRVQRLRSqlpedAPyILVHCSAGIGRSGVLIVVLVMLDRLRKkklp 4690
Cdd:cd14610   172 NETRTVTQFHFLSWNDQGVPASTRSLLDFrrkVNKCYRGRS-----CP-IIVHCSDGAGRSGTYILIDMVLNKMAK---- 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 514686563 4691 NAREI-----VKALREQRMGLVQVAAQYRFCFTACLAKLDSI 4727
Cdd:cd14610   242 GAKEIdiaatLEHLRDQRPGMVQTKEQFEFALTAVAEEVNAI 283
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 4510-4718 6.46e-41

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: 151.39  E-value: 6.46e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4510 YINANYVT---FPSTptpfrFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGGRQKCAQYWPPGaGQTMTTPLLEV 4586
Cdd:cd14558     1 YINASFIDgywGPKS-----LIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDE-KKTYGDIEVEL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4587 THVSSTpddpydPEIITTKLKVRHRINGQVREITHVQYVGWPDHGVPESPdkfLDLVDRVQRLRSQLPED------APYI 4660
Cdd:cd14558    75 KDTEKS------PTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKP---KDLVDMIKSIKQKLPYKnskhgrSVPI 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 514686563 4661 LVHCSAGIGRSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRFCFT 4718
Cdd:cd14558   146 VVHCSDGSSRTGIFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
PHA02738 PHA02738
hypothetical protein; Provisional
 4462-4728 7.90e-41

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 155.47  E-value: 7.90e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4462 EEFQTIPKTSATGSFTHSQRERQKNRYLDILAYDQTRVRLGDDGSGSDYINANYVT-FPSTPtpfRFIASQGPKPNTVNE 4540
Cdd:PHA02738   29 REHQKVISEKVDGTFNAEKKNRKLNRYLDAVCFDHSRVILPAERNRGDYINANYVDgFEYKK---KFICGQAPTRQTCYD 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4541 HWQMLWEQRVHVIVMLAQVVEGGRQKCAQYWPPGAGQTMTTPLLEVTHVSSTPddpyDPEIITTKLKVRHRiNGQVREIT 4620
Cdd:PHA02738  106 FYRMLWMEHVQIIVMLCKKKENGREKCFPYWSDVEQGSIRFGKFKITTTQVET----HPHYVKSTLLLTDG-TSATQTVT 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4621 HVQYVGWPDHGVPESPDKFLDLVDRVQRLRSQLPEDA----------PYILVHCSAGIGRSGVLIVVLVMLDRLRKKKLP 4690
Cdd:PHA02738  181 HFNFTAWPDHDVPKNTSEFLNFVLEVRQCQKELAQESlqighnrlqpPPIVVHCNAGLGRTPCYCVVDISISRFDACATV 260

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 514686563 4691 NAREIVKALREQRMGLVQVAAQYRFCFTACLAKLDSID 4728
Cdd:PHA02738  261 SIPSIVSSIRNQRYYSLFIPFQYFFCYRAVKRYVNLTV 298
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 4510-4717 1.91e-40

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: 150.31  E-value: 1.91e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4510 YINANYVTFPSTPTPFRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGGRQ-KCAQYWPPGAGQTMTTPLLEVTH 4588
Cdd:cd17658     1 YINASLVETPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYSTaKCADYFPAEENESREFGRISVTN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4589 VSSTPDdpyDPEIITTKLKVRHR-INGQVREITHVQYVGWPDHGVPESPDKFLDLVDRVqrlrSQLPEDAPYILVHCSAG 4667
Cdd:cd17658    81 KKLKHS---QHSITLRVLEVQYIeSEEPPLSVLHIQYPEWPDHGVPKDTRSVRELLKRL----YGIPPSAGPIVVHCSAG 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 514686563 4668 IGRSGVLIVVLVMLDRLRKKKLP--NAREIVKALREQRMGLVQVAAQYRFCF 4717
Cdd:cd17658   154 IGRTGAYCTIHNTIRRILEGDMSavDLSKTVRKFRSQRIGMVQTQDQYIFCY 205
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 4510-4717 4.07e-40

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: 149.29  E-value: 4.07e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4510 YINANYVTfpSTPTPFRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGGRQKCAQYWPPGAGQTMTTPLLEVTHV 4589
Cdd:cd14551     1 YINASYID--GYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWPDQGCWTYGNLRVRVEDT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4590 SSTPDdpydpeIITTKLKVRHRING----QVREITHVQYVGWPDHGVPESPDKFLDLVDRVqrlRSQLPEDAPYILVHCS 4665
Cdd:cd14551    79 VVLVD------YTTRKFCIQKVNRGigekRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKV---KSANPPRAGPIVVHCS 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 514686563 4666 AGIGRSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRFCF 4717
Cdd:cd14551   150 AGVGRTGTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIY 201
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 4510-4721 1.30e-39

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: 147.76  E-value: 1.30e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4510 YINANYVTFPSTPTpfRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGGRQKCAQYWPPgagQTMTTPLLEVTHV 4589
Cdd:cd14555     1 YINANYIDGYHRPN--HYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPD---DTEVYGDIKVTLV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4590 SSTPDDPYdpeIITTkLKVRHRINGQVREITHVQYVGWPDHGVPESPDKFLDLVDRVqrlRSQLPEDAPYILVHCSAGIG 4669
Cdd:cd14555    76 ETEPLAEY---VVRT-FALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRV---KASNPPSAGPIVVHCSAGAG 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 514686563 4670 RSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRFCFTACL 4721
Cdd:cd14555   149 RTGCYIVIDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAIL 200
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 4510-4719 1.70e-39

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: 147.59  E-value: 1.70e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4510 YINANYVT--FPSTPTpfrFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGGRQKCAQYWPPGAGQTMTTplLEVT 4587
Cdd:cd14546     1 YINASTIYdhDPRNPA---YIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEVYHI--YEVH 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4588 HVSstpDDPYDPEIITTKLKVRHRINGQVREITHVQYVGWPDHGVPESPDKFLDL---VDRVQRLRSqlpedAPyILVHC 4664
Cdd:cd14546    76 LVS---EHIWCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFrrkVNKSYRGRS-----CP-IVVHC 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4665 SAGIGRSGVLIVVLVMLDRLRKkklpNAREI-----VKALREQRMGLVQVAAQYRFCFTA 4719
Cdd:cd14546   147 SDGAGRTGTYILIDMVLNRMAK----GAKEIdiaatLEHLRDQRPGMVKTKDQFEFVLTA 202
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 4485-4715 2.78e-39

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: 147.76  E-value: 2.78e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4485 KNRYLDILAYDQTRVRL---GDDGSGSDYINANYVTFPSTPTPfRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVE 4561
Cdd:cd14611     2 KNRYKTILPNPHSRVCLkpkNSNDSLSTYINANYIRGYGGKEK-AFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4562 GGrQKCAQYWPPGAGqtmTTPLLEVTHVSSTPDDPYdpeiITTKLKVRHriNGQVREITHVQYVGWPDHGVPESPDKFLD 4641
Cdd:cd14611    81 KN-EKCVLYWPEKRG---IYGKVEVLVNSVKECDNY----TIRNLTLKQ--GSQSRSVKHYWYTSWPDHKTPDSAQPLLQ 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514686563 4642 LVDRVQRLRSQLPEDAPyILVHCSAGIGRSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRF 4715
Cdd:cd14611   151 LMLDVEEDRLASPGRGP-VVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEF 223
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 4503-4721 1.19e-38

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: 145.55  E-value: 1.19e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4503 DDGSGSDYINANYVTFPSTPTpfRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGGRQKCAQYWPPgagQTMTTP 4582
Cdd:cd14631     8 EDDPSSDYINANYIDGYQRPS--HYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPD---DTEVYG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4583 LLEVTHVSSTPDDPYdpeiITTKLKVRHRINGQVREITHVQYVGWPDHGVPESPDKFLDLVDRVQRlrSQLPEDAPyILV 4662
Cdd:cd14631    83 DFKVTCVEMEPLAEY----VVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKL--SNPPSAGP-IVV 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 514686563 4663 HCSAGIGRSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRFCFTACL 4721
Cdd:cd14631   156 HCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAIL 214
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 4484-4721 1.66e-38

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 148.23  E-value: 1.66e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4484 QKNRYLDILAYDQTRVRLGDDGSGSDYINANYVTFPSTPTpfRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGG 4563
Cdd:PHA02742   54 KKCRYPDAPCFDRNRVILKIEDGGDDFINASYVDGHNAKG--RFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDG 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4564 RQKCAQYWPPGAGQTMTTPLLEVTHVSSTPDDPYDpeiiTTKLKVRHRINGQVREITHVQYVGWPDHGVPESPDKFLDLV 4643
Cdd:PHA02742  132 KEACYPYWMPHERGKATHGEFKIKTKKIKSFRNYA----VTNLCLTDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFV 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4644 DRVQ--RLRSQLP------EDAPYILVHCSAGIGRSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRF 4715
Cdd:PHA02742  208 LAVReaDLKADVDikgeniVKEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIF 287


                  ....*.
gi 514686563 4716 CFTACL 4721
Cdd:PHA02742  288 CYFIVL 293
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 4460-4727 1.77e-38

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: 147.49  E-value: 1.77e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4460 AIEEFQTIPKTSATGsftHSQRERQKNRYLDILAYDQTRVRLGDDG--SGSDYINANYVTF--PSTPTpfrFIASQGPKP 4535
Cdd:cd14609    23 ALCAYQAEPNTCSTA---QGEANVKKNRNPDFVPYDHARIKLKAESnpSRSDYINASPIIEhdPRMPA---YIATQGPLS 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4536 NTVNEHWQMLWEQRVHVIVMLAQVVEGGRQKCAQYWPPGAgqtmtTPLLEVTHVSSTPDDPYDPEIITTKLKVRHRINGQ 4615
Cdd:cd14609    97 HTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEG-----SSLYHIYEVNLVSEHIWCEDFLVRSFYLKNVQTQE 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4616 VREITHVQYVGWPDHGVPESPDKFLDL---VDRVQRLRSqlpedAPyILVHCSAGIGRSGVLIVVLVMLDRLRKkklpNA 4692
Cdd:cd14609   172 TRTLTQFHFLSWPAEGIPSSTRPLLDFrrkVNKCYRGRS-----CP-IIVHCSDGAGRTGTYILIDMVLNRMAK----GV 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 514686563 4693 REI-----VKALREQRMGLVQVAAQYRFCFTACLAKLDSI 4727
Cdd:cd14609   242 KEIdiaatLEHVRDQRPGMVRTKDQFEFALTAVAEEVNAI 281
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 4484-4715 7.73e-38

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: 144.62  E-value: 7.73e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4484 QKNRYLDILAYDQTRVRL---GDDGSGSDYINANYVTFPSTPTPFrFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVv 4560
Cdd:cd14613    27 RKNRYKTILPNPHSRVCLtspDQDDPLSSYINANYIRGYGGEEKV-YIATQGPTVNTVGDFWRMVWQERSPIIVMITNI- 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4561 EGGRQKCAQYWPPgagQTMTTPLLEVTHVSSTPDDPYDPEIITTKlkvrhrINGQVREITHVQYVGWPDHGVPESPDKFL 4640
Cdd:cd14613   105 EEMNEKCTEYWPE---EQVTYEGIEITVKQVIHADDYRLRLITLK------SGGEERGLKHYWYTSWPDQKTPDNAPPLL 175

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 514686563 4641 DLVDRVQRLRSQLPEDAPYILVHCSAGIGRSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRF 4715
Cdd:cd14613   176 QLVQEVEEARQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQF 250
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 4510-4719 1.10e-37

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


Pssm-ID: 350400 [Multi-domain]  Cd Length: 202  Bit Score: 142.41  E-value: 1.10e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4510 YINANYVTfpstptPFR----FIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGGRQKCAQYWPpgagqtmTTPLLE 4585
Cdd:cd14552     1 YINASFID------GYRqkdaYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWP-------EDGSVS 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4586 VTHVSSTPDDPYDPEIITTK-LKVRHRINGQVREITHVQYVGWPDHGVPESPDKFLDLVDRVQRlRSQLPEDAPyILVHC 4664
Cdd:cd14552    68 SGDITVELKDQTDYEDYTLRdFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQK-QQQQSGNHP-ITVHC 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 514686563 4665 SAGIGRSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRFCFTA 4719
Cdd:cd14552   146 SAGAGRTGTFCALSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKV 200
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 4510-4715 5.56e-37

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: 140.50  E-value: 5.56e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4510 YINANYVTFPSTPTPFrfIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGGRQKCAQYWPPGAGQTMTTPLleVTHV 4589
Cdd:cd17668     1 YINANYVDGYNKPKAY--IAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEEYGNFL--VTQK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4590 SSTPDDPYDPEIIT---TKLK---VRHRINGqvREITHVQYVGWPDHGVPESPDKFLDLVDRVQRLRSQlpEDAPyILVH 4663
Cdd:cd17668    77 SVQVLAYYTVRNFTlrnTKIKkgsQKGRPSG--RVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRH--AVGP-VVVH 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 514686563 4664 CSAGIGRSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRF 4715
Cdd:cd17668   152 CSAGVGRTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVF 203
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 4509-4717 5.76e-37

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


Pssm-ID: 350470 [Multi-domain]  Cd Length: 205  Bit Score: 140.14  E-value: 5.76e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4509 DYINANYVTfpstptPFR----FIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGGRQKCAQYWPPGAGQTMTTPLL 4584
Cdd:cd14622     1 DYINASFID------GYRqkdyFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSEGSVTHGEITI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4585 EVThvsstpDDPYDPEIITTKLKVRHRINGQVREITHVQYVGWPDHGVPESPDKFLDLVDRVQRLRSQLPEDApyILVHC 4664
Cdd:cd14622    75 EIK------NDTLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQTGNHP--IVVHC 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 514686563 4665 SAGIGRSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRFCF 4717
Cdd:cd14622   147 SAGAGRTGTFIALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCY 199
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 4445-4715 9.11e-37

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 143.60  E-value: 9.11e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4445 IRDEQQRFLDEGMKGAIEEFQtipktsatgsfthSQRERQKNRYLDILAYDQTRVRL-GDDGSGSDYINANYVTfpSTPT 4523
Cdd:PHA02747   27 IRDEHHQIILKPFDGLIANFE-------------KPENQPKNRYWDIPCWDHNRVILdSGGGSTSDYIHANWID--GFED 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4524 PFRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQV-VEGGRQKCAQYWPPGAGQTMTTPLLEVTHVSSTpddpYDPEII 4602
Cdd:PHA02747   92 DKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPTkGTNGEEKCYQYWCLNEDGNIDMEDFRIETLKTS----VRAKYI 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4603 TTKLKVRHRINGQVREITHVQYVGWPDHGVPES-PD--KFLDLVDRVQRLRSQL--PEDAPY--ILVHCSAGIGRSGVLI 4675
Cdd:PHA02747  168 LTLIEITDKILKDSRKISHFQCSEWFEDETPSDhPDfiKFIKIIDINRKKSGKLfnPKDALLcpIVVHCSDGVGKTGIFC 247

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 514686563 4676 VVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRF 4715
Cdd:PHA02747  248 AVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYLF 287
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 4463-4719 6.34e-36

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 141.32  E-value: 6.34e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4463 EFQTIPKTSATGSFTHSQRERqKNRYLDILAYDQTRVRL-----------GD-DG---------SGSDYINANYVT-FPS 4520
Cdd:PHA02746   33 EVMDIPIRGTTNHFLKKENLK-KNRFHDIPCWDHSRVVInaheslkmfdvGDsDGkkievtsedNAENYIHANFVDgFKE 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4521 TPtpfRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVvEGGRQKCAQYWPPGAGQTMTTPllevTHVSSTPDDPYDPE 4600
Cdd:PHA02746  112 AN---KFICAQGPKEDTSEDFFKLISEHESQVIVSLTDI-DDDDEKCFELWTKEEDSELAFG----RFVAKILDIIEELS 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4601 IITTKLKVRHRINGQVREITHVQYVGWPDHGVPESPDKFLDLVDRVQRLRSQL-------PEDAPYILVHCSAGIGRSGV 4673
Cdd:PHA02746  184 FTKTRLMITDKISDTSREIHHFWFPDWPDNGIPTGMAEFLELINKVNEEQAELikqadndPQTLGPIVVHCSAGIGRAGT 263

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 514686563 4674 LIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRFCFTA 4719
Cdd:PHA02746  264 FCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKA 309
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 4510-4721 1.20e-35

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: 136.33  E-value: 1.20e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4510 YINANYVTFPSTPTpfRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGGRQKCAQYWPPgagQTMTTPLLEVTHV 4589
Cdd:cd14632     1 YINANYIDGYHRSN--HFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPD---DSDTYGDIKITLL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4590 SSTPDDPYDPEIITTKLK---VRHringqvrEITHVQYVGWPDHGVPESPDKFLDLVDRVqrlRSQLPEDAPYILVHCSA 4666
Cdd:cd14632    76 KTETLAEYSVRTFALERRgysARH-------EVKQFHFTSWPEHGVPYHATGLLAFIRRV---KASTPPDAGPVVVHCSA 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 514686563 4667 GIGRSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRFCFTACL 4721
Cdd:cd14632   146 GAGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAIL 200
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
4485-4713 6.70e-35

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 137.14  E-value: 6.70e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4485 KNRYLDILAYDQTRVRlGDDGsgsdYINANYVtfpSTPTPFRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGG- 4563
Cdd:COG5599    45 LNRFRDIQPYKETALR-ANLG----YLNANYI---QVIGNHRYIATQYPLEEQLEDFFQMLFDNNTPVLVVLASDDEISk 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4564 -RQKCAQYWPPgAGQTmttpLLEVTHVSSTPDDPYDPEIITTKLKVRHRINGQ-VREITHVQYVGWPDHGVPeSPDKFLD 4641
Cdd:COG5599   117 pKVKMPVYFRQ-DGEY----GKYEVSSELTESIQLRDGIEARTYVLTIKGTGQkKIEIPVLHVKNWPDHGAI-SAEALKN 190

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 514686563 4642 LVDRVQRLRSQLPEDAPYILVHCSAGIGRSGVLIVVLVMLDRLRKKKLP--NAREIVKALREQR-MGLVQVAAQY 4713
Cdd:COG5599   191 LADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVQItlSVEEIVIDMRTSRnGGMVQTSEQL 265
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 4510-4717 1.86e-33

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: 130.22  E-value: 1.86e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4510 YINANYVTfpSTPTPFRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVvEGGRQKCAQYWPPGAGQTMTtpLLEVTHV 4589
Cdd:cd14556     1 YINAALLD--SYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQL-DPKDQSCPQYWPDEGSGTYG--PIQVEFV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4590 SSTpddpYDPEIITTKLKVRH--RINGQVREITHVQYVGWPDHG-VPESPDKFLDLVDRVQRLRSQlPEDAPyILVHCSA 4666
Cdd:cd14556    76 STT----IDEDVISRIFRLQNttRPQEGYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQEQ-SGEGP-IVVHCLN 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 514686563 4667 GIGRSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRFCF 4717
Cdd:cd14556   150 GVGRSGVFCAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCY 200
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 4487-4717 3.03e-33

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: 130.55  E-value: 3.03e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4487 RYLDILAYDQTRV----RLGDDGSgsDYINANYVT-FPSTPTPfrfIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVE 4561
Cdd:cd14623     1 RVLQIIPYEFNRViipvKRGEENT--DYVNASFIDgYRQKDSY---IASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4562 GGRQKCAQYWPpgagqtmTTPLLEVTHVSSTPDDPYDPEIITTK-LKVRHRINGQVREITHVQYVGWPDHGVPESPDKFL 4640
Cdd:cd14623    76 RGQEKCAQYWP-------SDGSVSYGDITIELKKEEECESYTVRdLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMI 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 514686563 4641 DLVDRVQRlRSQLPEDAPyILVHCSAGIGRSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRFCF 4717
Cdd:cd14623   149 NIIAAVQK-QQQQSGNHP-ITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCY 223
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
4618-4721 2.04e-32

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 123.24  E-value: 2.04e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563   4618 EITHVQYVGWPDHGVPESPDKFLDLVDRVQRLRSQLPEDAPyILVHCSAGIGRSGVLIVVLVMLDRLRKKKL-PNAREIV 4696
Cdd:smart00404    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGP-VVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTV 79

                            90       100
                    ....*....|....*....|....*
gi 514686563   4697 KALREQRMGLVQVAAQYRFCFTACL 4721
Cdd:smart00404   80 KELRSQRPGMVQTEEQYLFLYRALL 104
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 4618-4721 2.04e-32

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: 123.24  E-value: 2.04e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563   4618 EITHVQYVGWPDHGVPESPDKFLDLVDRVQRLRSQLPEDAPyILVHCSAGIGRSGVLIVVLVMLDRLRKKKL-PNAREIV 4696
Cdd:smart00012    1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGP-VVVHCSAGVGRTGTFVAIDILLQQLEAEAGeVDIFDTV 79

                            90       100
                    ....*....|....*....|....*
gi 514686563   4697 KALREQRMGLVQVAAQYRFCFTACL 4721
Cdd:smart00012   80 KELRSQRPGMVQTEEQYLFLYRALL 104
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 359-432 1.13e-29

Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like receptors. Can occur in up to 38 copies (in apolipoprotein(a)). Plasminogen-like kringles possess affinity for free lysine and lysine- containing peptides.


Pssm-ID: 214527  Cd Length: 83  Bit Score: 114.79  E-value: 1.13e-29
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 514686563    359 YDANNMGYRGPIATTRNGRTCQRWDSQSPHPHSFTPLLFPDADLRENYCRNPDG-ERTAWCFTTDPSRQWELCDV 432
Cdd:smart00130    4 YAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGdSEGPWCYTTDPNVRWEYCDI 78
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 359-432 3.74e-28

Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, prothrombin, and apolipoprotein A. Structure is disulfide-rich, nearly all-beta.


Pssm-ID: 395005  Cd Length: 79  Bit Score: 110.09  E-value: 3.74e-28
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 514686563   359 YDANNMGYRGPIATTRNGRTCQRWDSQSPHPHSF-TPLLFPDADLRENYCRNPDGERTAWCFTTDPSRQWELCDV 432
Cdd:pfam00051    2 YHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDI 76
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 359-432 4.55e-28

Kringle domain; Kringle domains are believed to play a role in binding mediators, such as peptides, other proteins, membranes, or phospholipids. They are autonomous structural domains, found in a varying number of copies, in blood clotting and fibrinolytic proteins, some serine proteases and plasma proteins. Plasminogen-like kringles possess affinity for free lysine and lysine-containing peptides.


Pssm-ID: 238056  Cd Length: 83  Bit Score: 110.16  E-value: 4.55e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 514686563  359 YDANNMGYRGPIATTRNGRTCQRWDSQSPHPHSFTPLLFPDADLRENYCRNPDGE-RTAWCFTTDPSRQWELCDV 432
Cdd:cd00108     5 YWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDpEGPWCYTTDPNVRWEYCDI 79
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 4510-4721 2.50e-23

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: 101.25  E-value: 2.50e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4510 YINANYVTfpSTPTPFRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVveGGRQKCAQYWPPGAGQTMTTplLEVTHV 4589
Cdd:cd14634     1 YINAALMD--SHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNEM--DAAQLCMQYWPEKTSCCYGP--IQVEFV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4590 SSTPDDpydpEIITTKLKVRHRINGQ--VREITHVQYVGWPDH-GVPESPDKFLDLVDRVQRLRSQLPEDAPYILVHCSA 4666
Cdd:cd14634    75 SADIDE----DIISRIFRICNMARPQdgYRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQYDGREGRTVVHCLN 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 514686563 4667 GIGRSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRFCFTACL 4721
Cdd:cd14634   151 GGGRSGTFCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYEVAL 205
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 4350-4414 5.31e-23

CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 460154 [Multi-domain]  Cd Length: 65  Bit Score: 95.16  E-value: 5.31e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 514686563  4350 VGMRVLVKGYGPGTLLYYGKHATKPGYRCGVALDDPIGRNNGTVGGFWYFDCDDNHGILCDPRKV 4414
Cdd:pfam01302    1 VGDRVEVPGGRRGTVRYVGPVPFAPGVWVGVELDEPVGKNDGSVKGVRYFECPPKHGVFVRPSKV 65
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 4510-4721 7.75e-21

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: 93.94  E-value: 7.75e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4510 YINANYVTfpSTPTPFRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVveGGRQKCAQYWPPgAGQTMTTPLlEVTHV 4589
Cdd:cd14636     1 YINAALMD--SYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEV--DLAQGCPQYWPE-EGMLRYGPI-QVECM 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4590 SSTpddpYDPEIITTKLKVRHRINGQ--VREITHVQYVGWPDH-GVPESPDKFLDLVDRVQRLRSQLPEDAPYILVHCSA 4666
Cdd:cd14636    75 SCS----MDCDVISRIFRICNLTRPQegYLMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEECDEGEGRTIIHCLN 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 514686563 4667 GIGRSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRFCFTACL 4721
Cdd:cd14636   151 GGGRSGMFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCYDVAL 205
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 4510-4721 6.42e-20

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: 91.29  E-value: 6.42e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4510 YINAnyVTFPSTPTPFRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGgrQKCAQYWPPGaGQTMTTPLlEVTHV 4589
Cdd:cd14635     1 YINA--ALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLNDVDPA--QLCPQYWPEN-GVHRHGPI-QVEFV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4590 SSTPDDpydpEIITTKLKVRHRINGQ--VREITHVQYVGWPDH-GVPESPDKFLDLVDRVQRLRSQLPEDAPYILVHCSA 4666
Cdd:cd14635    75 SADLEE----DIISRIFRIYNAARPQdgYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEYNGGEGRTVVHCLN 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 514686563 4667 GIGRSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRFCFTACL 4721
Cdd:cd14635   151 GGGRSGTFCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYEVAL 205
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 4510-4721 2.69e-19

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: 89.58  E-value: 2.69e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4510 YINAnyVTFPSTPTPFRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGGRQ-KCAQYWP-PGAGQTmttPLLEVT 4587
Cdd:cd14637     1 YINA--ALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWPePGLQQY---GPMEVE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4588 HVSSTPDDpydpEIITTKLKVRH--RINGQVREITHVQYVGW-PDHGVPESPDKFLDLVDRVQRLRSQLPEDApyILVHC 4664
Cdd:cd14637    76 FVSGSADE----DIVTRLFRVQNitRLQEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQRESGEGR--TVVHC 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 514686563 4665 SAGIGRSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRFCFTACL 4721
Cdd:cd14637   150 LNGGGRSGTYCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIAL 206
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 4461-4717 1.26e-17

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 86.94  E-value: 1.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4461 IEEFQTI-PKTSATGSFTHSQRE---RQKNRYLDILAYDQTRVRLGDDGSgsdYINANYVTfpSTPTPFRFIASQGPKPN 4536
Cdd:PHA02740   28 IKEYRAIvPEHEDEANKACAQAEnkaKDENLALHITRLLHRRIKLFNDEK---VLDARFVD--GYDFEQKFICIINLCED 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4537 TVNEHWQMLWEQRVHVIVMLAQVVEggrQKC-AQYWPPGAGQTMTTPLLEVthvsSTPDDPYDPEIITTKLKVRHRInGQ 4615
Cdd:PHA02740  103 ACDKFLQALSDNKVQIIVLISRHAD---KKCfNQFWSLKEGCVITSDKFQI----ETLEIIIKPHFNLTLLSLTDKF-GQ 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4616 VREITHVQYVGWPDHGVPESPDKFLDLVDRVQRLRSQLPED------APyILVHCSAGIGRSGVLIVVLVMLDRLRKKKL 4689
Cdd:PHA02740  175 AQKISHFQYTAWPADGFSHDPDAFIDFFCNIDDLCADLEKHkadgkiAP-IIIDCIDGISSSAVFCVFDICATEFDKTGM 253

                         250       260
                  ....*....|....*....|....*...
gi 514686563 4690 PNAREIVKALREQRMGLVQVAAQYRFCF 4717
Cdd:PHA02740  254 LSIANALKKVRQKKYGCMNCLDDYVFCY 281
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 4486-4713 3.87e-17

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: 83.60  E-value: 3.87e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4486 NRYLDIlaydQTRVRLGDDGSgsdyINANYVTFPSTPtpfRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGGRQ 4565
Cdd:cd14559     1 NRFTNI----QTRVSTPVGKN----LNANRVQIGNKN---VAIACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRK 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4566 KCAQYWppgaGQTMTTPLLEVTHVSSTPDDPYDPEIITT-KLKVRHRINGQVREITHVQyvGWPDHG-VPESPDKFL-DL 4642
Cdd:cd14559    70 GLPPYF----RQSGTYGSVTVKSKKTGKDELVDGLKADMyNLKITDGNKTITIPVVHVT--NWPDHTaISSEGLKELaDL 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4643 VDRVQRLRSQLPEDAPYI----------LVHCSAGIGRSGVLIVVLVMLDRLRKKKLPnarEIVKALREQRMG-LVQVAA 4711
Cdd:cd14559   144 VNKSAEEKRNFYKSKGSSaindknkllpVIHCRAGVGRTGQLAAAMELNKSPNNLSVE---DIVSDMRTSRNGkMVQKDE 220


                  ..
gi 514686563 4712 QY 4713
Cdd:cd14559   221 QL 222
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 4350-4415 5.35e-15

Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and transportation of vesicles and organelles along the cytoskeletal network; A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 214997 [Multi-domain]  Cd Length: 68  Bit Score: 72.23  E-value: 5.35e-15
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 514686563   4350 VGMRVLVKGYG-PGTLLYYGKHATKPGYRCGVALDDP-IGRNNGTVGGFWYFDCDDNHGILCDPRKVR 4415
Cdd:smart01052    1 VGDRVEVGGGGrRGTVRYVGPTPFAPGVWVGVELDEPlRGKNDGSVKGVRYFECPPKHGIFVRPSKVE 68
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 4510-4721 1.50e-12

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: 69.64  E-value: 1.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4510 YINANYVT--FPSTptpfRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEGGRQKCAqYWP----PGAGQTMTTPL 4583
Cdd:cd17669     1 YINASYIMgyYQSN----EFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPnkdePINCETFKVTL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4584 LEVTHVSSTPDDpydpEIITTKLKVRHRINGQVREITHVQYVGWPDhgvPESP-DKFLDLVDRVQRLRSQlpEDAPyILV 4662
Cdd:cd17669    76 IAEEHKCLSNEE----KLIIQDFILEATQDDYVLEVRHFQCPKWPN---PDSPiSKTFELISIIKEEAAN--RDGP-MIV 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 514686563 4663 HCSAGIGRSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRFCFTACL 4721
Cdd:cd17669   146 HDEHGGVTAGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 4510-4667 1.59e-12

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: 69.66  E-value: 1.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4510 YINANYVTfpstptPFR----FIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQVVEggRQKCAQYWP----PGAGQTMTT 4581
Cdd:cd14550     1 YINASYLQ------GYRrsneFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNEL--NEDEPIYWPtkekPLECETFKV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4582 PLLEVTHVSSTPDDpydpeiittKLKVRHRI-----NGQVREITHVQYVGWPDHGVPESpdKFLDLVDRVQRLRSQlpED 4656
Cdd:cd14550    73 TLSGEDHSCLSNEI---------RLIVRDFIlestqDDYVLEVRQFQCPSWPNPCSPIH--TVFELINTVQEWAQQ--RD 139

                         170
                  ....*....|....*.
gi 514686563 4657 APyILVH-----CSAG 4667
Cdd:cd14550   140 GP-IVVHdryggVQAA 154
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 4510-4722 1.42e-11

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: 67.01  E-value: 1.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4510 YINANYVT--FPSTptpfRFIASQGPKPNTVNEHWQMLWEQRVHVIVMLAQvVEGGRQKCAQYWpPGAGQTMTTPLLEVT 4587
Cdd:cd17670     1 YINASYIMgyYRSN----EFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD-NQGLAEDEFVYW-PSREESMNCEAFTVT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4588 HVSStpDD---PYDPEIITTKLKVRHRINGQVREITHVQYVGWPDhgvPESP-DKFLDLVDRVQrlRSQLPEDAPYIlVH 4663
Cdd:cd17670    75 LISK--DRlclSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPN---PDAPiSSTFELINVIK--EEALTRDGPTI-VH 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 514686563 4664 CSAGIGRSGVLIVVLVMLDRLRKKKLPNAREIVKALREQRMGLVQVAAQYRFCFTACLA 4722
Cdd:cd17670   147 DEFGAVSAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAMLS 205
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
4622-4715 4.04e-10

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 60.75  E-value: 4.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4622 VQYVGWPDHGVPEsPDKFLDLVDRvqrLRSQLPEDAPyILVHCSAGIGRSG-VLIVVLVMLDRlrkkklpNAREIVKALR 4700
Cdd:COG2453    50 YLHLPIPDFGAPD-DEQLQEAVDF---IDEALREGKK-VLVHCRGGIGRTGtVAAAYLVLLGL-------SAEEALARVR 117

                          90
                  ....*....|....*
gi 514686563 4701 EQRMGLVQVAAQYRF 4715
Cdd:COG2453   118 AARPGAVETPAQRAF 132
TNFRSF16 cd13416
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ...
 934-1057 5.17e-10

Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 neurotrophin receptor (p75NTR) or CD271; TNFRSF16 (also known as nerve growth factor receptor (NGFR) or p75 neurotrophin receptor (p75NTR or p75(NTR)), CD271, Gp80-LNGFR) is a common receptor for both neurotrophins and proneurotrophins, and plays a diverse role in many tissues, including the nervous system. It has been shown to be expressed in various types of stem cells and has been used to prospectively isolate stem cells with different degrees of potency. p75NTR owes its signaling to the recruitment of intracellular binding proteins, leading to the activation of different signaling pathways. It binds nerve growth factor (NGF) and the complex can initiate a signaling cascade which has been associated with both neuronal apoptosis and neuronal survival of discrete populations of neurons, depending on the presence or absence of intracellular signaling molecules downstream of p75NTR (e.g. NF-kB, JNK, or p75NTR intracellular death domain). p75NTR can also bind NGF in concert with the neurotrophic tyrosine kinase receptor type 1 (TrkA) protein where it is thought to modulate the formation of the high-affinity neurotrophin binding complex. On melanoma cell, p75NTR is an immunosuppressive factor, induced by interferon (IFN)-gamma, and mediates down-regulation of melanoma antigens. It can interact with the aggregated form of amyloid beta (Abeta) peptides, and plays an important role in etiopathogenesis of Alzheimer's disease by influencing protein tau hyper-phosphorylation. p75(NTR) is involved in the formation and progression of retina diseases; its expression is induced in retinal pigment epithelium (RPE) cells and its knockdown rescues RPE cell proliferation activity and inhibits RPE apoptosis induced by hypoxia. It can therefore be a potential therapeutic target for RPE hypoxia or oxidative stress diseases.


Pssm-ID: 276921 [Multi-domain]  Cd Length: 159  Bit Score: 61.16  E-value: 5.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563  934 RRC-QNYTTCELGSTFQTVGPTPTTDRKCDACTVCPSTHRQIAECTLLLNAECEE---------------CSSCPSGTYM 997
Cdd:cd13416    26 RPCgDNQTVCEPCLDGVTFSDVVSHTEPCQPCTRCPGLMSMRAPCTATHDTVCECaygyyldedsgtcepCTVCPPGQGV 105

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514686563  998 DQACTDDHDTICAPcdtCATGKY--EAAACDPlhntqCEPCDVCSPSQYQLRACRATLNTVC 1057
Cdd:cd13416   106 VQSCGPNQDTVCEA---CPEGTYsdEDSSTDP-----CLPCTVCEDGEVELRECTPVSDTVC 159
TNFRSF16 cd13416
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ...
 985-1093 6.73e-08

Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 neurotrophin receptor (p75NTR) or CD271; TNFRSF16 (also known as nerve growth factor receptor (NGFR) or p75 neurotrophin receptor (p75NTR or p75(NTR)), CD271, Gp80-LNGFR) is a common receptor for both neurotrophins and proneurotrophins, and plays a diverse role in many tissues, including the nervous system. It has been shown to be expressed in various types of stem cells and has been used to prospectively isolate stem cells with different degrees of potency. p75NTR owes its signaling to the recruitment of intracellular binding proteins, leading to the activation of different signaling pathways. It binds nerve growth factor (NGF) and the complex can initiate a signaling cascade which has been associated with both neuronal apoptosis and neuronal survival of discrete populations of neurons, depending on the presence or absence of intracellular signaling molecules downstream of p75NTR (e.g. NF-kB, JNK, or p75NTR intracellular death domain). p75NTR can also bind NGF in concert with the neurotrophic tyrosine kinase receptor type 1 (TrkA) protein where it is thought to modulate the formation of the high-affinity neurotrophin binding complex. On melanoma cell, p75NTR is an immunosuppressive factor, induced by interferon (IFN)-gamma, and mediates down-regulation of melanoma antigens. It can interact with the aggregated form of amyloid beta (Abeta) peptides, and plays an important role in etiopathogenesis of Alzheimer's disease by influencing protein tau hyper-phosphorylation. p75(NTR) is involved in the formation and progression of retina diseases; its expression is induced in retinal pigment epithelium (RPE) cells and its knockdown rescues RPE cell proliferation activity and inhibits RPE apoptosis induced by hypoxia. It can therefore be a potential therapeutic target for RPE hypoxia or oxidative stress diseases.


Pssm-ID: 276921 [Multi-domain]  Cd Length: 159  Bit Score: 55.00  E-value: 6.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563  985 CEECSSCPSGTYMDQACTDDHDTICApcdtCATGKYEAAAcdplhNTQCEPCDVCSPSQYQLRACRATLNTVCEPLRNCT 1064
Cdd:cd13416    54 CQPCTRCPGLMSMRAPCTATHDTVCE----CAYGYYLDED-----SGTCEPCTVCPPGQGVVQSCGPNQDTVCEACPEGT 124

                          90       100
                  ....*....|....*....|....*....
gi 514686563 1065 LGQQYESTAPTPTSdRQCSDVTQCVHECT 1093
Cdd:cd13416   125 YSDEDSSTDPCLPC-TVCEDGEVELRECT 152
PTP_PTPDC1 cd14506
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ...
 4596-4715 1.82e-07

protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine phosphatase domain-containing protein 1 (PTPDC1) is an uncharacterized non-receptor class protein-tyrosine phosphatase (PTP). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Small interfering RNA (siRNA) knockdown of the ptpdc1 gene is associated with elongated cilia.


Pssm-ID: 350356 [Multi-domain]  Cd Length: 206  Bit Score: 55.05  E-value: 1.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4596 PYDPEIIttklkvrhringQVREITHVQYvGWPDHGVPeSPDKFLDLVdrvQRLRSQLPEDAPyILVHCSAGIGRSGVLI 4675
Cdd:cd14506    66 SYLPEAF------------MRAGIYFYNF-GWKDYGVP-SLTTILDIV---KVMAFALQEGGK-VAVHCHAGLGRTGVLI 127

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 514686563 4676 V-VLVMLDRLRkkklpnAREIVKALREQRMGLVQVAAQYRF 4715
Cdd:cd14506   128 AcYLVYALRMS------ADQAIRLVRSKRPNSIQTRGQVLC 162
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 4628-4715 7.57e-07

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


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 52.27  E-value: 7.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4628 PDHGVPESPDKFLDLVdrvQRLRSQLpEDAPYILVHCSAGIGRSGVLIVVLVmldrLRKKKLPNAREIVKALREQRMGLV 4707
Cdd:cd14505    81 PDGGVPSDIAQWQELL---EELLSAL-ENGKKVLIHCKGGLGRTGLIAACLL----LELGDTLDPEQAIAAVRALRPGAI 152


                  ....*...
gi 514686563 4708 QVAAQYRF 4715
Cdd:cd14505   153 QTPKQENF 160
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 4350-4411 9.51e-07

Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 227569 [Multi-domain]  Cd Length: 669  Bit Score: 55.46  E-value: 9.51e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514686563 4350 VGMRVLVKGYgPGTLLYYGKHATKPGYRCGVALDDPIGRNNGTVGGFWYFDCDDNHGILCDP 4411
Cdd:COG5244     6 VNDRVLLGDK-FGTVRFIGKTKFKDGIWIGLELDDPVGKNDGSVNGVRYFHCKKRHGIFIRP 66
TNFRSF cd00185
Tumor necrosis factor receptor superfamily (TNFRSF); Members of TNFR superfamily (TNFRSF) ...
 988-1058 2.56e-06

Tumor necrosis factor receptor superfamily (TNFRSF); Members of TNFR superfamily (TNFRSF) interactions with TNF superfamily (TNFSF) ligands (TNFL) control key cellular processes such as differentiation, proliferation, apoptosis, and cell growth. Dysregulation of these pathways has been shown to result in a wide range of pathological conditions, including autoimmune diseases, inflammation, cancer, and viral infection. There are 29 very diverse family members of TNFRSF reported in humans: 22 are type I transmembrane receptors (single pass with the N terminus on extracellular side of the cell membrane) and have a clear signal peptide; the remaining 7 members are either type III transmembrane receptors (single pass with the N terminus on extracellular side of the membrane but no signal sequence; TNFR13B, TNFR13C, TNFR17, and XEDAR), or attached to the membrane via a glycosylphosphatidylinositol (GPI) linker (TNFR10C), or secreted as soluble receptors (TNFR11B and TNFR6B). All TNFRs contain relatively short cysteine-rich domains (CRDs) in the ectodomain, and are involved in interaction with the TNF homology domain (THD) of their ligands. TNFRs often have multiple CRDs (between one and six), with the most frequent configurations of three or four copies; most CRDs possess three disulfide bridges, but could have between one and four. Localized or genome-wide duplication and evolution of the TNFRSF members appear to have paralleled the emergence of the adaptive immune system; teleosts (i.e. ray-finned, bony fish), which possess an immune system with B and T cells, possess primary and secondary lymphoid organs, and are capable of adaptive responses to pathogens also display several characteristics that are different from the mammalian immune system, making teleost TNFSF orthologs and paralogs of interest to better understand immune system evolution and the immunological pathways elicited to pathogens.


Pssm-ID: 276900 [Multi-domain]  Cd Length: 87  Bit Score: 48.36  E-value: 2.56e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514686563  988 CSSCPSGTYMDQACTDDHDTICAPCDtcaTGKYEAaacDPLHNTQCEPCDVCSP-SQYQLRACRATLNTVCE 1058
Cdd:cd00185     2 CQRCPPGEYLSSDCTATTDTVCSPCP---PGTYSE---SWNSLSKCLPCTTCGGgNQVEKTPCTATDNRCCT 67
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 4640-4717 3.34e-06

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: 48.89  E-value: 3.34e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 514686563 4640 LDLVDRVQRLRSQLPEDAPYILVHCSAGIGRSGVLIVVLVMLDRLRKkklpnAREIVKALREQR-MGLVQVAAQYRFCF 4717
Cdd:cd14494    39 LAMVDRFLEVLDQAEKPGEPVLVHCKAGVGRTGTLVACYLVLLGGMS-----AEEAVRIVRLIRpGGIPQTIEQLDFLI 112
TNFRSF21 cd10583
Tumor necrosis factor receptor superfamily member 21 (TNFRSF21), also known as death receptor ...
 3682-3816 5.98e-06

Tumor necrosis factor receptor superfamily member 21 (TNFRSF21), also known as death receptor (DR6); TNFRSF21 (also known as death receptor 6 (DR6), CD358, BM-018) is highly expressed in differentiating neurons as well as in the adult brain, and is upregulated in injured neurons. DR6 negatively regulates neurondendrocyte, axondendrocyte, and oligodendrocyte survival, hinders axondendrocyte and oligodendrocyte regeneration and its inhibition has a neuro-protective effect in nerve injury. It activates nuclear factor kappa-B (NFkB) and mitogen-activated protein kinase 8 (MAPK8, also called c-Jun N-terminal kinase 1), and induces cell apoptosis by associating with TNFRSF1A-associated via death domain (TRADD), which is known to mediate signal transduction of tumor necrosis factor receptors. TNFRSF21 plays a role in T-helper cell activation, and may be involved in inflammation and immune regulation. Its possible ligand is alpha-amyloid precursor protein (APP), hence probably involved in the development of Alzheimer's disease; when released, APP binds in an autocrine/paracrine manner to activate a caspase-dependent self-destruction program that removes unnecessary or connectionless axons. Increasing beta-catenin levels in brain endothelium upregulates TNFRSF21 and TNFRSF19, indicating that these death receptors are downstream target genes of Wnt/beta-catenin signaling, which has been shown to be required for blood-brain barrier development. DR6 is up-regulated in numerous solid tumors as well as in tumor vascular cells, including ovarian cancer and may be a clinically useful diagnostic and predictive serum biomarker for some adult sarcoma subtypes.


Pssm-ID: 276909 [Multi-domain]  Cd Length: 159  Bit Score: 49.36  E-value: 5.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 3682 VCSPCNAGEYQLLPCLPRSDRECEPCnpctPGNTTLVAECTLERdtiCTEC-ASCRSDQWISSPCTVSSDTVCSnitqCd 3760
Cdd:cd10583    14 TCDKCPAGTYVSKHCTETSLRECSPC----PNGTFTRHENGIEQ---CHRCrKPCPAPMIEKTPCTALTDRECT----C- 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 514686563 3761 fpreyrdVPATLTSNAVCKNVSTCAPGQFISAQATPTNDVTCAnvslPCSGETYEA 3816
Cdd:cd10583    82 -------PPGTFLSNDTCVPHSVCPVGWGVRKKGTETEDVRCK----PCPRGTFSD 126
TNFRSF6B cd10575
Tumor necrosis factor receptor superfamily member 6B (TNFRSF6B), also known as decoy receptor ...
 988-1058 1.37e-05

Tumor necrosis factor receptor superfamily member 6B (TNFRSF6B), also known as decoy receptor 3 (DcR3); The subfamily TNFRSF6B is also known as decoy receptor 3 (DcR3), M68, or TR6. This protein is a soluble receptor without death domain and cytoplasmic domain, and secreted by cells. It acts as a decoy receptor that competes with death receptors for ligand binding. It is a pleiotropic immunomodulator and biomarker for inflammatory diseases, autoimmune diseases, and cancer. Over-expression of this gene has been noted in several cancers, including pancreatic carcinoma, and gastrointestinal tract tumors. It can neutralize the biological effects of three tumor necrosis factor superfamily (TNFSF) members: TNFSF6 (Fas ligand/FasL/CD95L) and TNFSF14 (LIGHT) which are both involved in apoptosis and inflammation, and TNFSF15 (TNF-like molecule 1A/TL1A), which is a T cell co-stimulator and involved in gut inflammation. DcR3 is a novel inflammatory marker; higher DcR3 levels strongly correlate with inflammation and independently predict cardiovascular and all-cause mortality in chronic kidney disease (CKD) patients on hemodialysis. Increased synovial inflammatory cells infiltration in rheumatoid arthritis and ankylosing spondylitis is also associated with the elevated DcR3 expression. In cartilaginous fish, mRNA expression of DcR3 in the thymus and leydig, which are the representative lymphoid tissues of elasmobranchs, suggests that DcR3 may act as a modulator in the immune system. Interestingly, in banded dogfish (Triakis scyllia), DcR3 mRNA is strongly expressed in the gill, compared with human expression in the normal lung; both are respiratory organs, suggesting potential relevance of DcR3 to respiratory function.


Pssm-ID: 276901 [Multi-domain]  Cd Length: 163  Bit Score: 48.56  E-value: 1.37e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 514686563  988 CSSCPSGTYMDQACTDDHDTICAPcdtcatgkyeaaaCDPLHNTQ-------CEPCDV-CSPSQYQLRACRATLNTVCE 1058
Cdd:cd10575    16 CDQCPPGTFVAKHCTRDRPTVCGP-------------CPDLHYTQfwnylekCRYCNVfCTERQVEKRQCNATHNRVCE 81
TNFRSF1B cd10577
Tumor necrosis factor receptor superfamily member 1B (TNFRSF1B), also known as TNFR2; TNFRSF1B ...
 3683-3853 1.50e-05

Tumor necrosis factor receptor superfamily member 1B (TNFRSF1B), also known as TNFR2; TNFRSF1B (also known as TNFR2, type 2 TNFR, TNFBR, TNFR80, TNF-R75, TNF-R-II, p75, CD120b) binds TNF-alpha, but lacks the death domain (DD) that is associated with the cytoplasmic domain of TNFRSF1A (TNFR1). It is inducible and expressed exclusively by oligodendrocytes, astrocytes, T cells, thymocytes, myocytes, endothelial cells, and in human mesenchymal stem cells. TNFRSF1B protects oligodendrocyte progenitor cells (OLGs) against oxidative stress, and induces the up-regulation of cell survival genes. While pro-inflammatory and pathogen-clearing activities of TNF are mediated mainly through activation of TNFRSF1A, a strong activator of NF-kappaB, TNFRSF1B is more responsible for suppression of inflammation. Although the affinities of both receptors for soluble TNF are similar, TNFRSF1B is sometimes more abundantly expressed and thought to associate with TNF, thereby increasing its concentration near TNFRSF1A receptors, and making TNF available to activate TNFRSF1A (a ligand-passing mechanism).


Pssm-ID: 276903 [Multi-domain]  Cd Length: 163  Bit Score: 48.24  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 3683 CSPCNAGEYQLLPCLPRSDRECEPCNPCTpgNTTLvaectLERDTICTECAS-CRSDQWISSPCTVSSDTVCSnitqCDf 3761
Cdd:cd10577    16 CSKCPPGQHVKHSCTKTSDTVCAPCEEST--YTQL-----WNWVPECLSCSSpCSSDQVETQACTRQQNRICS----CK- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 3762 PREYRdVPATLTSNAVCKNVSTCAPGQFISAQATPTNDVTCAnvslPCSGETYearAPTATSDRLCLPLAQCdvstQYIA 3841
Cdd:cd10577    84 PGWYC-VLKLQEGCRQCRPLKKCGPGFGVARPGTASSDVECK----PCAPGTF---SDTTSSTDTCRPHRIC----SSVA 151

                         170
                  ....*....|..
gi 514686563 3842 ANETATSNRVCA 3853
Cdd:cd10577   152 IPGNASMDAVCA 163
TNFRSF11B cd10581
Tumor necrosis factor receptor superfamily member 11B (TNFRSF11B), also known as ...
 988-1058 4.52e-05

Tumor necrosis factor receptor superfamily member 11B (TNFRSF11B), also known as Osteoprotegerin (OPG); TNFRSF11B (also known as Osteoprotegerin, OPG, TR1, OCIF) is a secreted glycoprotein that regulates bone resorption. It binds to two ligands, RANKL (receptor activator of nuclear factor kappaB ligand, also known as osteoprotegerin ligand, OPGL, TRANCE, TNF-related activation induced cytokine), a critical cytokine for osteoclast differentiation, and TRAIL (TNF-related apoptosis-inducing ligand), involved in immune surveillance. Therefore, acting as a decoy receptor for RANKL and TRAIL, OPG inhibits the regulatory effects of nuclear factor-kappaB on inflammation, skeletal, and vascular systems, and prevents TRAIL-induced apoptosis. Studies in mice counterparts suggest that this protein and its ligand also play a role in lymph-node organogenesis and vascular calcification. Circulating OPG levels have emerged as independent biomarkers of cardiovascular disease (CVD) in patients with acute or chronic heart disease. OPG has also been implicated in various inflammations and linked to diabetes and poor glycemic control. Alternatively spliced transcript variants of this gene have been reported, although their full length nature has not been determined.


Pssm-ID: 276907 [Multi-domain]  Cd Length: 147  Bit Score: 46.70  E-value: 4.52e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514686563  988 CSSCPSGTYMDQACTDDHDTICAPC-DTCATGKYEAaacdplhNTQCEPCD-VCSPSQYQLRACRATLNTVCE 1058
Cdd:cd10581    36 CDQCPPGTYVKQHCSASRKTVCAPCpDHHYADDWNS-------NDECQYCNtVCKELQYVKQECNSTHNRVCE 101
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 4621-4716 5.70e-05

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


Pssm-ID: 350347 [Multi-domain]  Cd Length: 160  Bit Score: 46.42  E-value: 5.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4621 HVQYVGWPDHgvpeSPDKFLDLVDRVQRLRSQLPEDAPY-ILVHCSAGIGRSGVLIVVLVMLdrlrKKKLPNAREIVKAL 4699
Cdd:cd14497    62 RVLHYGFPDH----HPPPLGLLLEIVDDIDSWLSEDPNNvAVVHCKAGKGRTGTVICAYLLY----YGQYSTADEALEYF 133

                          90       100
                  ....*....|....*....|.
gi 514686563 4700 REQRMG----LVQVAAQYRFC 4716
Cdd:cd14497   134 AKKRFKeglpGVTIPSQLRYL 154
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
4660-4702 1.47e-04

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 44.97  E-value: 1.47e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 514686563   4660 ILVHCSAGIGRSGVLIVVLVMldRLRKKKLPNAREIVKALREQ 4702
Cdd:smart00195   81 VLVHCQAGVSRSATLIIAYLM--KTRNMSLNDAYDFVKDRRPI 121
TNFRSF16 cd13416
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ...
 3675-3852 2.52e-04

Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 neurotrophin receptor (p75NTR) or CD271; TNFRSF16 (also known as nerve growth factor receptor (NGFR) or p75 neurotrophin receptor (p75NTR or p75(NTR)), CD271, Gp80-LNGFR) is a common receptor for both neurotrophins and proneurotrophins, and plays a diverse role in many tissues, including the nervous system. It has been shown to be expressed in various types of stem cells and has been used to prospectively isolate stem cells with different degrees of potency. p75NTR owes its signaling to the recruitment of intracellular binding proteins, leading to the activation of different signaling pathways. It binds nerve growth factor (NGF) and the complex can initiate a signaling cascade which has been associated with both neuronal apoptosis and neuronal survival of discrete populations of neurons, depending on the presence or absence of intracellular signaling molecules downstream of p75NTR (e.g. NF-kB, JNK, or p75NTR intracellular death domain). p75NTR can also bind NGF in concert with the neurotrophic tyrosine kinase receptor type 1 (TrkA) protein where it is thought to modulate the formation of the high-affinity neurotrophin binding complex. On melanoma cell, p75NTR is an immunosuppressive factor, induced by interferon (IFN)-gamma, and mediates down-regulation of melanoma antigens. It can interact with the aggregated form of amyloid beta (Abeta) peptides, and plays an important role in etiopathogenesis of Alzheimer's disease by influencing protein tau hyper-phosphorylation. p75(NTR) is involved in the formation and progression of retina diseases; its expression is induced in retinal pigment epithelium (RPE) cells and its knockdown rescues RPE cell proliferation activity and inhibits RPE apoptosis induced by hypoxia. It can therefore be a potential therapeutic target for RPE hypoxia or oxidative stress diseases.


Pssm-ID: 276921 [Multi-domain]  Cd Length: 159  Bit Score: 44.60  E-value: 2.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 3675 TSNRECdvCSPCNAGEYQLLPClPRSDRECEPCNPCTPGNTTLVAEctlerdTICTECASCRSDQWISSPCTVSSDTVCs 3754
Cdd:cd13416     9 TSSGEC--CEQCPPGEGVARPC-GDNQTVCEPCLDGVTFSDVVSHT------EPCQPCTRCPGLMSMRAPCTATHDTVC- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 3755 nitQCDFPReYRDVPATLtsnavCKNVSTCAPGQFISAQATPTNDVTCAnvslPCSGETYEARAPTATSdrlCLPLAQCD 3834
Cdd:cd13416    79 ---ECAYGY-YLDEDSGT-----CEPCTVCPPGQGVVQSCGPNQDTVCE----ACPEGTYSDEDSSTDP---CLPCTVCE 142

                         170
                  ....*....|....*...
gi 514686563 3835 VSTQYIAANeTATSNRVC 3852
Cdd:cd13416   143 DGEVELREC-TPVSDTVC 159
TNFRSF1A cd10576
Tumor necrosis factor receptor superfamily member 1A (TNFRSF1A), also known as TNFR1; TNFRSF1A ...
 3683-3802 3.63e-04

Tumor necrosis factor receptor superfamily member 1A (TNFRSF1A), also known as TNFR1; TNFRSF1A (also known as type I TNFR, TNFR1, DR1, TNFRSF1A, CD120a, p55) binds TNF-alpha, through the death domain (DD), and activates NF-kappaB, mediates apoptosis and activates signaling pathways controlling inflammatory, immune, and stress responses. It mediates signal transduction by interacting with antiapoptotic protein BCL2-associated athanogene 4 (BAG4/SODD) and adaptor proteins TRAF2 and TRADD that play regulatory roles. The human genetic disorder called tumor necrosis factor associated periodic syndrome (TRAPS), or periodic fever syndrome, is associated with germline mutations of the extracellular domains of this receptor, possibly due to impaired receptor clearance. TNFRSF1A polymorphisms rs1800693 and rs4149584 are associated with elevated risk of multiple sclerosis. Serum levels of TNFRSF1A are elevated in schizophrenia and bipolar disorder, and high levels are also associated with cognitive impairment and dementia. Patients with idiopathic recurrent acute pericarditis (IRAP), presumed to be an autoimmune process, have also been shown to carry rare mutations (R104Q and D12E) in the TNFRSF1A gene.


Pssm-ID: 276902 [Multi-domain]  Cd Length: 130  Bit Score: 43.50  E-value: 3.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 3683 CSPCNAGEYQLLPCL-PRSDRECEPCnpctPGNTTLVAECTLERdtiCTECASCRS--DQWISSPCTVSSDTVCSnitqC 3759
Cdd:cd10576    15 CTKCHKGTYLYNDCPgPGQDTVCREC----ENGTFTASENYLRK---CLSCSRCRKemGQVEISPCTVDQDTVCG----C 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 514686563 3760 DfPREYRDvpaTLTSNAVCKNVSTCAPGQfISAQATPTNDVTC 3802
Cdd:cd10576    84 R-KNQYQH---YWSSLFQCKNCSLCLNGT-IRQPCQEKQDTIC 121
TNFRSF14_teleost cd13405
Tumor necrosis factor receptor superfamily member 14 (TNFRSF14) in teleost; also known as ...
 986-1060 4.44e-04

Tumor necrosis factor receptor superfamily member 14 (TNFRSF14) in teleost; also known as herpes virus entry mediator (HVEM); This subfamily of TNFRSF14 (also known as herpes virus entry mediator or HVEM, ATAR, CD270, HVEA, LIGHTR, TR2) is found in teleosts, many of which are as yet uncharacterized. It regulates T-cell immune responses by activating inflammatory as well as inhibitory signaling pathways. HVEM acts as a receptor for the canonical TNF-related ligand LIGHT (lymphotoxin-like), which exhibits inducible expression, and competes with herpes simplex virus glycoprotein D for HVEM. It also acts as a ligand for the immunoglobulin superfamily proteins BTLA (B and T lymphocyte attenuator) and CD160, a feature distinguishing HVEM from other immune regulatory molecules, thus, creating a functionally diverse set of intrinsic and bidirectional signaling pathways. HVEM is highly expressed in the gut epithelium. Genome-wide association studies have shown that HVEM is an inflammatory bowel disease (IBD) risk gene, suggesting that HVEM could have a regulatory role influencing the regulation of epithelial barrier, host defense, and the microbiota. Mouse models have revealed that HVEM is involved in colitis pathogenesis, mucosal host defense, and epithelial immunity, thus acting as a mucosal gatekeeper with multiple regulatory functions in the mucosa. HVEM plays a critical role in both tumor progression and resistance to antitumor immune responses, possibly through direct and indirect mechanisms. It is known to be expressed in several human malignancies, including esophageal squamous cell carcinoma, follicular lymphoma, and melanoma. HVEM network may therefore be an attractive target for drug intervention. In Asian seabass, the up-regulation of differentially expressed TNFRSF14 gene has been observed.


Pssm-ID: 276910 [Multi-domain]  Cd Length: 111  Bit Score: 42.70  E-value: 4.44e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 514686563  986 EECSSCPSGTYMDQACTDDHDTICAPcdtCATGKYEAAacdPLHNTQCEPCDVCSPSQ--YQLRACRATLNTVCEPL 1060
Cdd:cd13405    11 ECCPMCPPGSRVSRHCTEDTSTSCVP---CPDGTYMDE---PNGLEKCFPCTNCDPGFglRVKQGCTYTSDTVCEPL 81
TNFRSF16 cd13416
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ...
 887-1033 5.32e-04

Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 neurotrophin receptor (p75NTR) or CD271; TNFRSF16 (also known as nerve growth factor receptor (NGFR) or p75 neurotrophin receptor (p75NTR or p75(NTR)), CD271, Gp80-LNGFR) is a common receptor for both neurotrophins and proneurotrophins, and plays a diverse role in many tissues, including the nervous system. It has been shown to be expressed in various types of stem cells and has been used to prospectively isolate stem cells with different degrees of potency. p75NTR owes its signaling to the recruitment of intracellular binding proteins, leading to the activation of different signaling pathways. It binds nerve growth factor (NGF) and the complex can initiate a signaling cascade which has been associated with both neuronal apoptosis and neuronal survival of discrete populations of neurons, depending on the presence or absence of intracellular signaling molecules downstream of p75NTR (e.g. NF-kB, JNK, or p75NTR intracellular death domain). p75NTR can also bind NGF in concert with the neurotrophic tyrosine kinase receptor type 1 (TrkA) protein where it is thought to modulate the formation of the high-affinity neurotrophin binding complex. On melanoma cell, p75NTR is an immunosuppressive factor, induced by interferon (IFN)-gamma, and mediates down-regulation of melanoma antigens. It can interact with the aggregated form of amyloid beta (Abeta) peptides, and plays an important role in etiopathogenesis of Alzheimer's disease by influencing protein tau hyper-phosphorylation. p75(NTR) is involved in the formation and progression of retina diseases; its expression is induced in retinal pigment epithelium (RPE) cells and its knockdown rescues RPE cell proliferation activity and inhibits RPE apoptosis induced by hypoxia. It can therefore be a potential therapeutic target for RPE hypoxia or oxidative stress diseases.


Pssm-ID: 276921 [Multi-domain]  Cd Length: 159  Bit Score: 43.83  E-value: 5.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563  887 QCTPHTFCFLGQYESAPATFTSNRECDpitqCSDDQFELAPftattdrrcqnyttcelgstfqtvgptpttDRKCDACTV 966
Cdd:cd13416    53 PCQPCTRCPGLMSMRAPCTATHDTVCE----CAYGYYLDED------------------------------SGTCEPCTV 98

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 514686563  967 CPSTHRQIAECTLLLNAECEEcssCPSGTYMDQACTDDHdtiCAPCDTCATGKYEAAACDPLHNTQC 1033
Cdd:cd13416    99 CPPGQGVVQSCGPNQDTVCEA---CPEGTYSDEDSSTDP---CLPCTVCEDGEVELRECTPVSDTVC 159
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 45-189 6.44e-04

von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.


Pssm-ID: 214621 [Multi-domain]  Cd Length: 175  Bit Score: 43.98  E-value: 6.44e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563     45 VVVLVEGSFYVAEGEFAAFTQAALDVsTALLTASPTGTHLtSVIEFST-----FPCSAESqctpfvsDAEELADRIDSID 119
Cdd:smart00327    2 VVFLLDGSGSMGGNRFELAKEFVLKL-VEQLDIGPDGDRV-GLVTFSDdarvlFPLNDSR-------SKDALLEALASLS 72

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 514686563    120 -QSFGLVRTAGAIQYALDN---RFQVPDPDRRSVLLAIAKSAPLNPSEPVRQA---LQDAGVDAFFVLLDPDNSTVQ 189
Cdd:smart00327   73 yKLGGGTNLGAALQYALENlfsKSAGSRRGAPKVVILITDGESNDGPKDLLKAakeLKRSGVKVFVVGVGNDVDEEE 149
TNFRSF1B cd10577
Tumor necrosis factor receptor superfamily member 1B (TNFRSF1B), also known as TNFR2; TNFRSF1B ...
 516-669 7.36e-04

Tumor necrosis factor receptor superfamily member 1B (TNFRSF1B), also known as TNFR2; TNFRSF1B (also known as TNFR2, type 2 TNFR, TNFBR, TNFR80, TNF-R75, TNF-R-II, p75, CD120b) binds TNF-alpha, but lacks the death domain (DD) that is associated with the cytoplasmic domain of TNFRSF1A (TNFR1). It is inducible and expressed exclusively by oligodendrocytes, astrocytes, T cells, thymocytes, myocytes, endothelial cells, and in human mesenchymal stem cells. TNFRSF1B protects oligodendrocyte progenitor cells (OLGs) against oxidative stress, and induces the up-regulation of cell survival genes. While pro-inflammatory and pathogen-clearing activities of TNF are mediated mainly through activation of TNFRSF1A, a strong activator of NF-kappaB, TNFRSF1B is more responsible for suppression of inflammation. Although the affinities of both receptors for soluble TNF are similar, TNFRSF1B is sometimes more abundantly expressed and thought to associate with TNF, thereby increasing its concentration near TNFRSF1A receptors, and making TNF available to activate TNFRSF1A (a ligand-passing mechanism).


Pssm-ID: 276903 [Multi-domain]  Cd Length: 163  Bit Score: 43.23  E-value: 7.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563  516 MCASVnpCYPHQYEASPPTVTSDRVCVAISNCTTSQFQTAAPtatsnrECRSIRPPCMLGsEYLVAEPTTTTDRICedvk 595
Cdd:cd10577    14 MCCSK--CPPGQHVKHSCTKTSDTVCAPCEESTYTQLWNWVP------ECLSCSSPCSSD-QVETQACTRQQNRIC---- 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 514686563  596 NCTESQFqVVAPTATSDRVCAKLRECRDDQYIAVPATPTSNRICLRLAECTedqyelVEPTETSNRVCAPCTPC 669
Cdd:cd10577    81 SCKPGWY-CVLKLQEGCRQCRPLKKCGPGFGVARPGTASSDVECKPCAPGT------FSDTTSSTDTCRPHRIC 147
TNFRSF1B_teleost cd15835
Tumor necrosis factor receptor superfamily member 1B (TNFRSF1B) in teleost; also known as ...
 988-1088 8.01e-04

Tumor necrosis factor receptor superfamily member 1B (TNFRSF1B) in teleost; also known as TNFR2; This subfamily of TNFRSF1B (also known as TNFR2, type 2 TNFR, TNFBR, TNFR80, TNF-R75, TNF-R-II, p75, CD120b) is found in teleosts. It binds TNF-alpha, but lacks the death domain (DD) that is associated with the cytoplasmic domain of TNFRSF1A (TNFR1). It is inducible and expressed exclusively by oligodendrocytes, astrocytes, T cells, thymocytes, myocytes, endothelial cells, and in human mesenchymal stem cells. TNFRSF1B protects oligodendrocyte progenitor cells (OLGs) against oxidative stress, and induces the up-regulation of cell survival genes. While pro-inflammatory and pathogen-clearing activities of TNF are mediated mainly through activation of TNFRSF1A, a strong activator of NF-kappaB, TNFRSF1B is more responsible for suppression of inflammation. Although the affinities of both receptors for soluble TNF are similar, TNFRSF1B is sometimes more abundantly expressed and thought to associate with TNF, thereby increasing its concentration near TNFRSF1A receptors, and making TNF available to activate TNFRSF1A (a ligand-passing mechanism). Knockout studies in zebrafish embryos have shown that a signaling balance between TNFRSF1A and TNFRSF1B is required for endothelial cell integrity. TNFRSF1A signals apoptosis through caspase-8, whereas TNFRSF1B signals survival via NF-kB in endothelial cells. In goldfish (Carassius aurutus L.), TNFRSF1B expression is substantially higher than that of TNFRSF1 in tissues and various immune cell types. Both receptors are most robustly expressed in monocytes; mRNA levels of TNFRSF1B are lowest in peripheral blood leukocytes.


Pssm-ID: 276931 [Multi-domain]  Cd Length: 130  Bit Score: 42.42  E-value: 8.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563  988 CSSCPSGTYMDQACTDDHDTICAPCDtcaTGKYEAAACdplHNTQCEPCDVCSPS---QYqLRACRATLNT--VCEPLRN 1062
Cdd:cd15835    21 CSKCRPGTRLKTKCSETSDTVCEPCP---SGQYSENWN---YYPNCFSCPKCKERkglQY-AQNCSSTTNAvcVCKPGMY 93

                          90       100
                  ....*....|....*....|....*.
gi 514686563 1063 CTLGQQYESTAptptsdrQCSDVTQC 1088
Cdd:cd15835    94 CIMGFDHPSCS-------ECKKYRTC 112
DSPc pfam00782
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
 4660-4702 9.00e-04

Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The enzyme's tertiary fold is highly similar to that of tyrosine-specific phosphatases, except for a "recognition" region.


Pssm-ID: 395632 [Multi-domain]  Cd Length: 127  Bit Score: 42.25  E-value: 9.00e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 514686563  4660 ILVHCSAGIGRSGVLIVVLVMldRLRKKKLPNAREIVKALREQ 4702
Cdd:pfam00782   72 VLVHCQAGISRSATLIIAYLM--KTRNLSLNEAYSFVKERRPG 112
TNFRSF cd00185
Tumor necrosis factor receptor superfamily (TNFRSF); Members of TNFR superfamily (TNFRSF) ...
 964-1034 9.68e-04

Tumor necrosis factor receptor superfamily (TNFRSF); Members of TNFR superfamily (TNFRSF) interactions with TNF superfamily (TNFSF) ligands (TNFL) control key cellular processes such as differentiation, proliferation, apoptosis, and cell growth. Dysregulation of these pathways has been shown to result in a wide range of pathological conditions, including autoimmune diseases, inflammation, cancer, and viral infection. There are 29 very diverse family members of TNFRSF reported in humans: 22 are type I transmembrane receptors (single pass with the N terminus on extracellular side of the cell membrane) and have a clear signal peptide; the remaining 7 members are either type III transmembrane receptors (single pass with the N terminus on extracellular side of the membrane but no signal sequence; TNFR13B, TNFR13C, TNFR17, and XEDAR), or attached to the membrane via a glycosylphosphatidylinositol (GPI) linker (TNFR10C), or secreted as soluble receptors (TNFR11B and TNFR6B). All TNFRs contain relatively short cysteine-rich domains (CRDs) in the ectodomain, and are involved in interaction with the TNF homology domain (THD) of their ligands. TNFRs often have multiple CRDs (between one and six), with the most frequent configurations of three or four copies; most CRDs possess three disulfide bridges, but could have between one and four. Localized or genome-wide duplication and evolution of the TNFRSF members appear to have paralleled the emergence of the adaptive immune system; teleosts (i.e. ray-finned, bony fish), which possess an immune system with B and T cells, possess primary and secondary lymphoid organs, and are capable of adaptive responses to pathogens also display several characteristics that are different from the mammalian immune system, making teleost TNFSF orthologs and paralogs of interest to better understand immune system evolution and the immunological pathways elicited to pathogens.


Pssm-ID: 276900 [Multi-domain]  Cd Length: 87  Bit Score: 41.04  E-value: 9.68e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514686563  964 CTVCPSTHRQIAECTLLLNAECEecsSCPSGTYMDqacTDDHDTICAPCDTC-ATGKYEAAACDPLHNTQCE 1034
Cdd:cd00185     2 CQRCPPGEYLSSDCTATTDTVCS---PCPPGTYSE---SWNSLSKCLPCTTCgGGNQVEKTPCTATDNRCCT 67
TNFRSF1B cd10577
Tumor necrosis factor receptor superfamily member 1B (TNFRSF1B), also known as TNFR2; TNFRSF1B ...
 3612-3778 2.10e-03

Tumor necrosis factor receptor superfamily member 1B (TNFRSF1B), also known as TNFR2; TNFRSF1B (also known as TNFR2, type 2 TNFR, TNFBR, TNFR80, TNF-R75, TNF-R-II, p75, CD120b) binds TNF-alpha, but lacks the death domain (DD) that is associated with the cytoplasmic domain of TNFRSF1A (TNFR1). It is inducible and expressed exclusively by oligodendrocytes, astrocytes, T cells, thymocytes, myocytes, endothelial cells, and in human mesenchymal stem cells. TNFRSF1B protects oligodendrocyte progenitor cells (OLGs) against oxidative stress, and induces the up-regulation of cell survival genes. While pro-inflammatory and pathogen-clearing activities of TNF are mediated mainly through activation of TNFRSF1A, a strong activator of NF-kappaB, TNFRSF1B is more responsible for suppression of inflammation. Although the affinities of both receptors for soluble TNF are similar, TNFRSF1B is sometimes more abundantly expressed and thought to associate with TNF, thereby increasing its concentration near TNFRSF1A receptors, and making TNF available to activate TNFRSF1A (a ligand-passing mechanism).


Pssm-ID: 276903 [Multi-domain]  Cd Length: 163  Bit Score: 42.08  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 3612 MCPPGMYEAEAPTPTSDRQCkriSKC--DLATQYISAAPTITSDRicanlTVCGSDMFELVAPTPTSNRecdVCSpCNAG 3689
Cdd:cd10577    18 KCPPGQHVKHSCTKTSDTVC---APCeeSTYTQLWNWVPECLSCS-----SPCSSDQVETQACTRQQNR---ICS-CKPG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 3690 EYQLLPcLPRSDRECEPCNPCTPGnTTLVAECTLERDTICTECASCRSDQWISSPCTVSSDTVCSNITqcdfpreyrdVP 3769
Cdd:cd10577    86 WYCVLK-LQEGCRQCRPLKKCGPG-FGVARPGTASSDVECKPCAPGTFSDTTSSTDTCRPHRICSSVA----------IP 153


                  ....*....
gi 514686563 3770 ATLTSNAVC 3778
Cdd:cd10577   154 GNASMDAVC 162
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 4628-4715 3.06e-03

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: 41.11  E-value: 3.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 4628 PDHGVP--ESPDKFLDLVDrvQRLRSQLPedapyILVHCSAGIGRSG-VLIVVLVMldrlrKKKLPnAREIVKALREQRM 4704
Cdd:cd14504    58 EDYTPPtlEQIDEFLDIVE--EANAKNEA-----VLVHCLAGKGRTGtMLACYLVK-----TGKIS-AVDAINEIRRIRP 124

                          90
                  ....*....|.
gi 514686563 4705 GLVQVAAQYRF 4715
Cdd:cd14504   125 GSIETSEQEKF 135
TNFRSF6B cd10575
Tumor necrosis factor receptor superfamily member 6B (TNFRSF6B), also known as decoy receptor ...
 666-789 3.21e-03

Tumor necrosis factor receptor superfamily member 6B (TNFRSF6B), also known as decoy receptor 3 (DcR3); The subfamily TNFRSF6B is also known as decoy receptor 3 (DcR3), M68, or TR6. This protein is a soluble receptor without death domain and cytoplasmic domain, and secreted by cells. It acts as a decoy receptor that competes with death receptors for ligand binding. It is a pleiotropic immunomodulator and biomarker for inflammatory diseases, autoimmune diseases, and cancer. Over-expression of this gene has been noted in several cancers, including pancreatic carcinoma, and gastrointestinal tract tumors. It can neutralize the biological effects of three tumor necrosis factor superfamily (TNFSF) members: TNFSF6 (Fas ligand/FasL/CD95L) and TNFSF14 (LIGHT) which are both involved in apoptosis and inflammation, and TNFSF15 (TNF-like molecule 1A/TL1A), which is a T cell co-stimulator and involved in gut inflammation. DcR3 is a novel inflammatory marker; higher DcR3 levels strongly correlate with inflammation and independently predict cardiovascular and all-cause mortality in chronic kidney disease (CKD) patients on hemodialysis. Increased synovial inflammatory cells infiltration in rheumatoid arthritis and ankylosing spondylitis is also associated with the elevated DcR3 expression. In cartilaginous fish, mRNA expression of DcR3 in the thymus and leydig, which are the representative lymphoid tissues of elasmobranchs, suggests that DcR3 may act as a modulator in the immune system. Interestingly, in banded dogfish (Triakis scyllia), DcR3 mRNA is strongly expressed in the gill, compared with human expression in the normal lung; both are respiratory organs, suggesting potential relevance of DcR3 to respiratory function.


Pssm-ID: 276901 [Multi-domain]  Cd Length: 163  Bit Score: 41.62  E-value: 3.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563  666 CTPCPVGVaFEERACTNVSNTVCSVC-------------------RTCGEGTFESSPCNTT-NRVCdpisECTATQY--- 722
Cdd:cd10575    16 CDQCPPGT-FVAKHCTRDRPTVCGPCpdlhytqfwnylekcrycnVFCTERQVEKRQCNAThNRVC----ECKPGYYmeh 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 514686563  723 EFdpptattdrvCRNLTQCLPFiEYESQPPTPTSNRECAltSCDPGTFEVVPptiTSARECDPVKQC 789
Cdd:cd10575    91 GF----------CLRHSSCPPG-EGVIKLGTPYSDTQCE--PCPPGFFSASS---SSTEPCQPHTNC 141
TNFRSF26 cd15837
Tumor necrosis factor receptor superfamily member 26 (TNFRSF26), also known as tumor necrosis ...
 903-1009 3.35e-03

Tumor necrosis factor receptor superfamily member 26 (TNFRSF26), also known as tumor necrosis factor receptor homolog 3 (TNFRH3); TNFRSF26 (also known as tumor necrosis factor receptor homolog 3 (TNFRH3) or TNFRSF24) is predominantly expressed in embryos and lymphoid cell types, along with its closely related TNFRSF22 and TNFRSF23 orthologs, and is developmentally regulated. Unlike TNFRSF22/23, TNFRSF26 does not serve as a TRAIL decoy receptor; it remains an orphan receptor.


Pssm-ID: 276933 [Multi-domain]  Cd Length: 118  Bit Score: 40.43  E-value: 3.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563  903 PATFTSNR----ECDPITQCSDDQFELAPFTATTDRRCQnyttCELGSTFqtvgptpttdrkCDACTVcpsthrqiaect 978
Cdd:cd15837    40 PGTFTAHPngetSCFPCSQCRDDQEVVAECSATSDRQCQ----CKQGHFY------------CDENCL------------ 91

                          90       100       110
                  ....*....|....*....|....*....|.
gi 514686563  979 lllnAECEECSSCPSGTYMDQACTDDHDTIC 1009
Cdd:cd15837    92 ----ESCFRCSRCPGGRVVLQPCNATRDTVC 118
TNFRSF1B_teleost cd15835
Tumor necrosis factor receptor superfamily member 1B (TNFRSF1B) in teleost; also known as ...
 964-1082 3.98e-03

Tumor necrosis factor receptor superfamily member 1B (TNFRSF1B) in teleost; also known as TNFR2; This subfamily of TNFRSF1B (also known as TNFR2, type 2 TNFR, TNFBR, TNFR80, TNF-R75, TNF-R-II, p75, CD120b) is found in teleosts. It binds TNF-alpha, but lacks the death domain (DD) that is associated with the cytoplasmic domain of TNFRSF1A (TNFR1). It is inducible and expressed exclusively by oligodendrocytes, astrocytes, T cells, thymocytes, myocytes, endothelial cells, and in human mesenchymal stem cells. TNFRSF1B protects oligodendrocyte progenitor cells (OLGs) against oxidative stress, and induces the up-regulation of cell survival genes. While pro-inflammatory and pathogen-clearing activities of TNF are mediated mainly through activation of TNFRSF1A, a strong activator of NF-kappaB, TNFRSF1B is more responsible for suppression of inflammation. Although the affinities of both receptors for soluble TNF are similar, TNFRSF1B is sometimes more abundantly expressed and thought to associate with TNF, thereby increasing its concentration near TNFRSF1A receptors, and making TNF available to activate TNFRSF1A (a ligand-passing mechanism). Knockout studies in zebrafish embryos have shown that a signaling balance between TNFRSF1A and TNFRSF1B is required for endothelial cell integrity. TNFRSF1A signals apoptosis through caspase-8, whereas TNFRSF1B signals survival via NF-kB in endothelial cells. In goldfish (Carassius aurutus L.), TNFRSF1B expression is substantially higher than that of TNFRSF1 in tissues and various immune cell types. Both receptors are most robustly expressed in monocytes; mRNA levels of TNFRSF1B are lowest in peripheral blood leukocytes.


Pssm-ID: 276931 [Multi-domain]  Cd Length: 130  Bit Score: 40.50  E-value: 3.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563  964 CTVCPSTHRQIAECTLLLNAECEEcssCPSGTYMDqacTDDHDTICAPCDTCATGK--YEAAACDPLHNTQCepcdVCSP 1041
Cdd:cd15835    21 CSKCRPGTRLKTKCSETSDTVCEP---CPSGQYSE---NWNYYPNCFSCPKCKERKglQYAQNCSSTTNAVC----VCKP 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 514686563 1042 SQYQLRACRATLNTVCEPLRNCTLGqQYESTAPTPTSDRQC 1082
Cdd:cd15835    91 GMYCIMGFDHPSCSECKKYRTCKPG-YGVSVPGTPTSDVKC 130
TNFR_c6 pfam00020
TNFR/NGFR cysteine-rich region;
991-1033 4.46e-03

TNFR/NGFR cysteine-rich region;


Pssm-ID: 459633 [Multi-domain]  Cd Length: 39  Bit Score: 37.68  E-value: 4.46e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 514686563   991 CPSGTYMDQactdDHDTICAPCDTCATGKYEAAACDPLHNTQC 1033
Cdd:pfam00020    1 CPPGTYTDN----WNGLKCLPCTVCPPGQVVVRPCTPTSDTVC 39
TNFR_c6 pfam00020
TNFR/NGFR cysteine-rich region;
1015-1057 5.22e-03

TNFR/NGFR cysteine-rich region;


Pssm-ID: 459633 [Multi-domain]  Cd Length: 39  Bit Score: 37.68  E-value: 5.22e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 514686563  1015 CATGKYeaaaCDPLHNTQCEPCDVCSPSQYQLRACRATLNTVC 1057
Cdd:pfam00020    1 CPPGTY----TDNWNGLKCLPCTVCPPGQVVVRPCTPTSDTVC 39
TNFRSF_viral cd15839
Tumor necrosis factor receptor superfamily members, virus-encoded; This family contains viral ...
 988-1058 5.90e-03

Tumor necrosis factor receptor superfamily members, virus-encoded; This family contains viral TNFR homologs that include vaccinia virus (VACV) cytokine response modifier E (CrmE), an encoded TNFR that shares significant sequence similarity with mammalian type 2 TNF receptors (TNFSFR1B, p75, TNFR type 2), a cowpox virus encoded cytokine-response modifier B (crmB), which is a secreted form of TNF receptor that can contribute to the modification of TNF-mediated antiviral processes, and a myxoma virus (MYXV) T2 (M-T2) protein that binds and inhibits rabbit TNF-alpha. The CrmE structure confirms that the canonical TNFR fold is adopted, but only one of the two "ligand-binding" loops of TNFRSF1A is conserved, suggesting a mechanism for the higher affinity of poxvirus TNFRs for TNFalpha over lymphotoxin-alpha. CrmB protein specifically binds TNF-alpha and TNF-beta indicating that cowpox virus seeks to invade antiviral processes mediated by TNF. Intracellular M-T2 blocks virus-induced lymphocyte apoptosis via a highly conserved viral preligand assembly domain (vPLAD), which controls receptor signaling competency prior to ligand binding.


Pssm-ID: 276935 [Multi-domain]  Cd Length: 125  Bit Score: 39.85  E-value: 5.90e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514686563  988 CSSCPSGTYMDQACTDDHDTICAPCdtcatgKYEAAACDPLHNTQCEPCD-VCSPSQYQLRACRATLNTVCE 1058
Cdd:cd15839    15 CKSCPPGTYASHLCDTTSNTKCDPC------PSDTFTSIPNHIPACLSCRgRCSSNQVETKSCSNTQNRICS 80
TNFRSF26 cd15837
Tumor necrosis factor receptor superfamily member 26 (TNFRSF26), also known as tumor necrosis ...
 3683-3802 5.92e-03

Tumor necrosis factor receptor superfamily member 26 (TNFRSF26), also known as tumor necrosis factor receptor homolog 3 (TNFRH3); TNFRSF26 (also known as tumor necrosis factor receptor homolog 3 (TNFRH3) or TNFRSF24) is predominantly expressed in embryos and lymphoid cell types, along with its closely related TNFRSF22 and TNFRSF23 orthologs, and is developmentally regulated. Unlike TNFRSF22/23, TNFRSF26 does not serve as a TRAIL decoy receptor; it remains an orphan receptor.


Pssm-ID: 276933 [Multi-domain]  Cd Length: 118  Bit Score: 39.66  E-value: 5.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563 3683 CSPCNAGEYQLLPC-LPRSDRECEPCNPctpgnTTLVAECTLErdTICTECASCRSDQWISSPCTVSSDTVCsnitQCDF 3761
Cdd:cd15837    13 CQLCPAGHYVSEPCqENHGVGECAPCEP-----GTFTAHPNGE--TSCFPCSQCRDDQEVVAECSATSDRQC----QCKQ 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 514686563 3762 PREYRDvPATLTSnavCKNVSTCAPGQFISAQATPTNDVTC 3802
Cdd:cd15837    82 GHFYCD-ENCLES---CFRCSRCPGGRVVLQPCNATRDTVC 118
TNFRSF1B cd10577
Tumor necrosis factor receptor superfamily member 1B (TNFRSF1B), also known as TNFR2; TNFRSF1B ...
 988-1083 7.99e-03

Tumor necrosis factor receptor superfamily member 1B (TNFRSF1B), also known as TNFR2; TNFRSF1B (also known as TNFR2, type 2 TNFR, TNFBR, TNFR80, TNF-R75, TNF-R-II, p75, CD120b) binds TNF-alpha, but lacks the death domain (DD) that is associated with the cytoplasmic domain of TNFRSF1A (TNFR1). It is inducible and expressed exclusively by oligodendrocytes, astrocytes, T cells, thymocytes, myocytes, endothelial cells, and in human mesenchymal stem cells. TNFRSF1B protects oligodendrocyte progenitor cells (OLGs) against oxidative stress, and induces the up-regulation of cell survival genes. While pro-inflammatory and pathogen-clearing activities of TNF are mediated mainly through activation of TNFRSF1A, a strong activator of NF-kappaB, TNFRSF1B is more responsible for suppression of inflammation. Although the affinities of both receptors for soluble TNF are similar, TNFRSF1B is sometimes more abundantly expressed and thought to associate with TNF, thereby increasing its concentration near TNFRSF1A receptors, and making TNF available to activate TNFRSF1A (a ligand-passing mechanism).


Pssm-ID: 276903 [Multi-domain]  Cd Length: 163  Bit Score: 40.54  E-value: 7.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563  988 CSSCPSGTYMDQACTDDHDTICAPCDT-------------------CATGKYEAAACDPLHNTQCEpcdvCSPSQYqlra 1048
Cdd:cd10577    16 CSKCPPGQHVKHSCTKTSDTVCAPCEEstytqlwnwvpeclscsspCSSDQVETQACTRQQNRICS----CKPGWY---- 87

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 514686563 1049 CRATLNT---VCEPLRNCTLGqqYESTAP-TPTSDRQCS 1083
Cdd:cd10577    88 CVLKLQEgcrQCRPLKKCGPG--FGVARPgTASSDVECK 124
TNFRSF3 cd10578
Tumor necrosis factor receptor superfamily member 3 (TNFRSF3), also known as lymphotoxin beta ...
 988-1082 9.38e-03

Tumor necrosis factor receptor superfamily member 3 (TNFRSF3), also known as lymphotoxin beta receptor (LTBR); TNFRSF3 (also known as lymphotoxin beta receptor, LTbetaR, CD18, TNFCR, TNFR3, D12S370, TNFR-RP, TNFR2-RP, LT-BETA-R, TNF-R-III) plays a role in signaling during development of lymphoid and other organs, lipid metabolism, immune response, and programmed cell death. Its ligands include lymphotoxin (LT) alpha/beta membrane form (heterotrimer) and tumor necrosis factor ligand superfamily member 14 (also known as LIGHT). TNFRSF3 agonism by these ligands initiates canonical, as well as non-canonical nuclear factor-kappaB (NF-kappaB) signaling, and preferentially results in the translocation of p52-RELB complexes into the nucleus. While these ligands are often expressed by T and B cells, TNFRSF3 is conspicuous absence on T and B lymphocytes and NK cells, suggesting that signaling may be unidirectional for TNFRSF3. Activity of this receptor has also been linked to carcinogenesis; it helps trigger apoptosis and can also lead to release of the interleukin 8 (IL8). Alternatively spliced transcript variants encoding multiple isoforms have been observed.


Pssm-ID: 276904 [Multi-domain]  Cd Length: 158  Bit Score: 40.14  E-value: 9.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563  988 CSSCPSGTYMDQACTDDHDTICAPC------------DTC--------ATGKYEAAACDPLHNTQCEpcdvCSPSQYQlr 1047
Cdd:cd10578    49 CSRCPPGTHVSAECSRSQDTVCATCpensynehwnhlSICqlcrpcdpVLGFEEVAPCTSDRKTQCR----CQPGMFC-- 122

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 514686563 1048 ACRATLNTVCEPLRNCTLGQQYESTAPTPTSDRQC 1082
Cdd:cd10578   123 VHWDNECEHCEPLSDCPPGTEAELTDEVGEADNNC 157
TNFRSF4 cd13406
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; ...
 988-1057 9.45e-03

Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; TNFRSF4 (also known as OX40, ACT35, CD134, IMD16, TXGP1L) activates NF-kappaB through its interaction with adaptor proteins TRAF2 and TRAF5. It also promotes the expression of apoptosis inhibitors BCL2 and BCL2lL1/BCL2-XL, and thus suppresses apoptosis. It is primarily expressed on activated CD4+ and CD8+ T cells, where it is transiently expressed and upregulated on the most recently antigen-activated T cells within inflammatory lesions. This makes it an attractive target to modulate immune responses, i.e. TNFRSF4 (OX40) blocking agents to inhibit adverse inflammation or agonists to enhance immune responses. An artificially created biologic fusion protein, OX40-immunoglobulin (OX40-Ig), prevents OX40 from reaching the T-cell receptors, thus reducing the T-cell response. Some single nucleotide polymorphisms (SNPs) of its natural ligand OX40 ligand (OX40L, CD252), which is also found on activated T cells, have been associated with systemic lupus erythematosus.


Pssm-ID: 276911 [Multi-domain]  Cd Length: 142  Bit Score: 39.69  E-value: 9.45e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514686563  988 CSSCPSGTYMDQACTDDHDTICAPCDtcaTGKYEaaacDPLHNTQCEPCDVCS--PSQYQLRACRATLNTVC 1057
Cdd:cd13406    15 CHECPPGEGMESRCTGTQDTVCSPCE---PGFYN----EAVNYEPCKPCTQCNqrSGSEEKQKCTKTSDTVC 79
TNFRSF1A_teleost cd15834
Tumor necrosis factor receptor superfamily member 1A (TNFRSF1A) in teleosts; also known as ...
 645-743 9.65e-03

Tumor necrosis factor receptor superfamily member 1A (TNFRSF1A) in teleosts; also known as TNFR1; This subfamily of TNFRSF1 ((also known as type I TNFR, TNFR1, DR1, TNFRSF1A, CD120a, p55) is found in teleosts. It binds TNF-alpha, through the death domain (DD), and activates NF-kappaB, mediates apoptosis and activates signaling pathways controlling inflammatory, immune, and stress responses. It mediates signal transduction by interacting with antiapoptotic protein BCL2-associated athanogene 4 (BAG4/SODD) and adaptor proteins TRAF2 and TRADD that play regulatory roles. The human genetic disorder called tumor necrosis factor associated periodic syndrome (TRAPS), or periodic fever syndrome, is associated with germline mutations of the extracellular domains of this receptor, possibly due to impaired receptor clearance. Serum levels of TNFRSF1A are elevated in schizophrenia and bipolar disorder, and high levels are also associated with cognitive impairment and dementia. Knockout studies in zebrafish embryos have shown that a signaling balance between TNFRSF1A and TNFRSF1B is required for endothelial cell integrity. TNFRSF1A signals apoptosis through caspase-8, whereas TNFRSF1B signals survival via NF-kappaB in endothelial cells. Thus, this apoptotic pathway seems to be evolutionarily conserved, as TNFalpha promotes apoptosis of human endothelial cells and triggers caspase-2 and P53 activation in these cells via TNFRSF1A.


Pssm-ID: 276930 [Multi-domain]  Cd Length: 150  Bit Score: 39.78  E-value: 9.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563  645 CTEDQYelvepTETSNRV--CAPCTPCPVGVAFEERACTNVSNTVCSvcrtCGEGtFESSPCNTTNRVCDPISECTATQY 722
Cdd:cd15834    39 CPEGTY-----LEQINYSpnCRRCTLCKVKNEEEVSPCKKSSNTVCR----CKKG-YYKSRIDSETRECLKCKTCGPGEI 108

                          90       100
                  ....*....|....*....|....*...
gi 514686563  723 EFDPPTATTDRVC-------RNLTQCLP 743
Cdd:cd15834   109 EIQPCTPESNTVCeckdnyyRNNNKCKP 136
TNFRSF26 cd15837
Tumor necrosis factor receptor superfamily member 26 (TNFRSF26), also known as tumor necrosis ...
 987-1057 9.88e-03

Tumor necrosis factor receptor superfamily member 26 (TNFRSF26), also known as tumor necrosis factor receptor homolog 3 (TNFRH3); TNFRSF26 (also known as tumor necrosis factor receptor homolog 3 (TNFRH3) or TNFRSF24) is predominantly expressed in embryos and lymphoid cell types, along with its closely related TNFRSF22 and TNFRSF23 orthologs, and is developmentally regulated. Unlike TNFRSF22/23, TNFRSF26 does not serve as a TRAIL decoy receptor; it remains an orphan receptor.


Pssm-ID: 276933 [Multi-domain]  Cd Length: 118  Bit Score: 39.27  E-value: 9.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514686563  987 ECSSCPSGTYMDQActdDHDTICAPCDTCATGKYEAAACDPLHNTQCE-----------------PCDVCSPSQYQLRAC 1049
Cdd:cd15837    34 ECAPCEPGTFTAHP---NGETSCFPCSQCRDDQEVVAECSATSDRQCQckqghfycdenclescfRCSRCPGGRVVLQPC 110


                  ....*...
gi 514686563 1050 RATLNTVC 1057
Cdd:cd15837   111 NATRDTVC 118
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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