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Conserved domains on  [gi|5817132|emb|CAB53676|]
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hypothetical protein, partial [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 597-801 2.70e-131

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: 394.44  E-value: 2.70e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  597 YINASCVEGLSPYCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTERGQPMVHGALSLALSS 676
Cdd:cd14539   1 YINASLIEDLTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALVYGAITVSLQS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  677 VRSTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQEVHAHYLHQRPLHTPIIVHCSSGVGRTGAF 756
Cdd:cd14539  81 VRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQRSLQTPIVVHCSSGVGRTGAF 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 5817132  757 ALLYAAVQEVEAGNGIPELPQLVRRMRQQRKHMLQEKLHLRFCYE 801
Cdd:cd14539 161 CLLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
V_Alix_like super family cl14654
Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains ...
 2-54 9.01e-20

Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains the V-shaped (V) domain of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, and related domains. Alix, HD-PTP, Bro1, and Rim20 all interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Alix, also known as apoptosis-linked gene-2 interacting protein 1 (AIP1), participates in membrane remodeling processes during the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), and the abscission reactions of mammalian cell division. It also functions in apoptosis. HD-PTP functions in cell migration and endosomal trafficking, Bro1 in endosomal trafficking, and Rim20 in the response to the external pH via the Rim101 pathway. The Alix V-domain contains a binding site, partially conserved in this superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. Members of this superfamily have an N-terminal Bro1-like domain, which binds components of the ESCRT-III complex. The Bro1-like domains of Alix and HD-PTP can also bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. Many members, including Alix, HD-PTP, and Bro1, also have a proline-rich region (PRR), which binds multiple partners in Alix, including Tsg101 (tumor susceptibility gene 101, a component of ESCRT-1) and the apoptotic protein ALG-2. The C-terminal portion (V-domain and PRR) of Bro1 interacts with Doa4, a ubiquitin thiolesterase needed to remove ubiquitin from MVB cargoes; it interacts with a YPxL motif in Doa4s catalytic domain to stimulate its deubiquitination activity. Rim20 may bind the ESCRT-III subunit Snf7, bringing the protease Rim13 (a YPxL-containing transcription factor) into proximity with Rim101, and promoting the proteolytic activation of Rim101. HD-PTP is encoded by the PTPN23 gene, a tumor suppressor gene candidate often absent in human kidney, breast, lung, and cervical tumors. HD-PTP has a C-terminal catalytically inactive tyrosine phosphatase domain.


The actual alignment was detected with superfamily member cd09234:

Pssm-ID: 353824 [Multi-domain]  Cd Length: 337  Bit Score: 91.97  E-value: 9.01e-20
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 5817132    2 DQKWNSTLQTLVASYEAYEDLMKKSQEGRDFYADLESKVAALLERTQSTCQAR 54
Cdd:cd09234 285 KQKRESTISSLIASYEAYEDLLKKSQKGIDFYKKLEGNVSKLLQRIKSVCKVQ 337
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 81-422 2.85e-08

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 58.41  E-value: 2.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132     81 LPRREESEAVEAGdppeelRSLPPDMVAGPRLPDTfLGSATPLHFPPSPFPSSTGPGPHYLSG-PLPPGTYSG----PTQ 155
Cdd:PHA03247 2663 RPRRARRLGRAAQ------ASSPPQRPRRRAARPT-VGSLTSLADPPPPPPTPEPAPHALVSAtPLPPGPAAArqasPAL 2735

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132    156 LIQPRAPGPHAMPVAPG-PALYPAPAYT-----PELGLVPRSSPQHGVVSSPYVGVGPAPPVAGLPSAPPPQfsgPELAM 229
Cdd:PHA03247 2736 PAAPAPPAVPAGPATPGgPARPARPPTTagppaPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADP---PAAVL 2812

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132    230 AVRPATTTVDSIQAPIPSHTAPRPNPTPAPPPpcfpvpppqPLPTPYTYPAGAKQPIPAQHHFSSGIPTGFPAPRIGPQP 309
Cdd:PHA03247 2813 APAAALPPAASPAGPLPPPTSAQPTAPPPPPG---------PPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPV 2883

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132    310 QPHPQPHPSQAFGPQPPQQPLPLQHPHLFPPQAPGLLPPQSPYPY-APQPGVLGQPPPPLHTQLYPGPAQDPLPAHSGAL 388
Cdd:PHA03247 2884 RRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQpQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPW 2963

                         330       340       350
                  ....*....|....*....|....*....|....
gi 5817132    389 PFPSPGPPQPPHPPLAYGPAPSTRPMGPQAAPLT 422
Cdd:PHA03247 2964 LGALVPGRVAVPRFRVPQPAPSREAPASSTPPLT 2997
 
Name Accession Description Interval E-value
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 597-801 2.70e-131

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: 394.44  E-value: 2.70e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  597 YINASCVEGLSPYCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTERGQPMVHGALSLALSS 676
Cdd:cd14539   1 YINASLIEDLTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALVYGAITVSLQS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  677 VRSTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQEVHAHYLHQRPLHTPIIVHCSSGVGRTGAF 756
Cdd:cd14539  81 VRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQRSLQTPIVVHCSSGVGRTGAF 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 5817132  757 ALLYAAVQEVEAGNGIPELPQLVRRMRQQRKHMLQEKLHLRFCYE 801
Cdd:cd14539 161 CLLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
574-804 2.18e-86

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 277.20  E-value: 2.18e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132    574 KNRHQDVMPYDSNRVVL--RSGKDDYINASCVEGlSPYCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQ 651
Cdd:pfam00102   4 KNRYKDVLPYDHTRVKLtgDPGPSDYINASYIDG-YKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKGRE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132    652 KVARYFPTERGQPMVHGALSLALSSVRSTETH-VERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQEVHA 730
Cdd:pfam00102  83 KCAQYWPEEEGESLEYGDFTVTLKKEKEDEKDyTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLRKVRK 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5817132    731 HYlhQRPLHTPIIVHCSSGVGRTGAFALLYAAVQEVEAgNGIPELPQLVRRMRQQRKHMLQEKLHLRFCYEAVV 804
Cdd:pfam00102 163 SS--LDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEA-EGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
574-805 1.53e-83

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 270.30  E-value: 1.53e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132     574 KNRHQDVMPYDSNRVVLRSGK---DDYINASCVEGLSPYcPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEK 650
Cdd:smart00194  30 KNRYKDVLPYDHTRVKLKPPPgegSDYINASYIDGPNGP-KAYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGR 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132     651 QKVARYFPTERGQPMVHGALSLALSSVRSTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQEVHA 730
Cdd:smart00194 109 EKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRK 188

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5817132     731 HYLHQRplhTPIIVHCSSGVGRTGAFALLYAAVQEVEAGnGIPELPQLVRRMRQQRKHMLQEKLHLRFCYEAVVR 805
Cdd:smart00194 189 SQSTST---GPIVVHCSAGVGRTGTFIAIDILLQQLEAG-KEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
PHA02738 PHA02738
hypothetical protein; Provisional
 575-808 2.16e-37

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 143.14  E-value: 2.16e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132   575 NRHQDVMPYDSNRVVLRSGKD--DYINASCVEGLSpYCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQK 652
Cdd:PHA02738  53 NRYLDAVCFDHSRVILPAERNrgDYINANYVDGFE-YKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREK 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132   653 VARYFPTERGQPMVHGALSLALSSVRSTETHVERVLSLQfRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQEV---- 728
Cdd:PHA02738 132 CFPYWSDVEQGSIRFGKFKITTTQVETHPHYVKSTLLLT-DGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVrqcq 210

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132   729 ---HAHYL---HQRPLHTPIIVHCSSGVGRTGAFALLYAAVQEVEAGNGIpELPQLVRRMRQQRKHMLQEKLHLRFCYEA 802
Cdd:PHA02738 211 kelAQESLqigHNRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATV-SIPSIVSSIRNQRYYSLFIPFQYFFCYRA 289


                 ....*.
gi 5817132   803 VVRHVE 808
Cdd:PHA02738 290 VKRYVN 295
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
545-793 1.87e-33

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 130.60  E-value: 1.87e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  545 LDTVWREL----QDAQEHDARGRSIaiarcyslKNRHQDVMPYDSNRVvlrSGKDDYINASCVEGLSPYCppLVATQAPL 620
Cdd:COG5599  20 LSTLTNELapshNDPQYLQNINGSP--------LNRFRDIQPYKETAL---RANLGYLNANYIQVIGNHR--YIATQYPL 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  621 PGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKV--ARYFPTErGQpmvHGALSLALSSVRST--ETHVE-RVLSLQFRDQ 695
Cdd:COG5599  87 EEQLEDFFQMLFDNNTPVLVVLASDDEISKPKVkmPVYFRQD-GE---YGKYEVSSELTESIqlRDGIEaRTYVLTIKGT 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  696 SLK-RSLVHLHFPTWPELGLPDSpSNLLRFIQEVHAHYLHQRPLHTPIIVHCSSGVGRTGAFALLYAAVQEVEAGNGIPE 774
Cdd:COG5599 163 GQKkIEIPVLHVKNWPDHGAISA-EALKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVQITL 241

                       250       260
                ....*....|....*....|.
gi 5817132  775 -LPQLVRRMRQQR-KHMLQEK 793
Cdd:COG5599 242 sVEEIVIDMRTSRnGGMVQTS 262
V_HD-PTP_like cd09234
Protein-interacting V-domain of mammalian His-Domain type N23 protein tyrosine phosphatase and ...
 2-54 9.01e-20

Protein-interacting V-domain of mammalian His-Domain type N23 protein tyrosine phosphatase and related domains; This family contains the V-shaped (V) domain of mammalian His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23) and related domains. It belongs to the V_Alix_like superfamily which includes the V domains of Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, mammalian Alix (apoptosis-linked gene-2 interacting protein X/ also known as apoptosis-linked gene-2 interacting protein 1, AIP1), and related domains. HD_PTP interacts with the ESCRT (Endosomal Sorting Complexes Required for Transport) system, and participates in cell migration and endosomal trafficking. The related Alix V-domain (belonging to a different family in this superfamily) contains a binding site, partially conserved in the superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. In addition to the V-domain, HD_PTP also has an N-terminal Bro1-like domain, a proline-rich region (PRR), a catalytically inactive tyrosine phosphatase domain, and a region containing a PEST motif. Bro1-like domains bind components of the ESCRT-III complex, specifically to CHMP4 in the case of HD-PTP. The Bro1-like domain of HD-PTP can also bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. HD-PTP is encoded by the PTPN23 gene, a tumor suppressor gene candidate frequently absent in human kidney, breast, lung, and cervical tumors. This family also contains Drosophila Myopic, which promotes epidermal growth factor receptor (EGFR) signaling, and Caenorhabditis elegans (enhancer of glp-1) EGO-2 which promotes Notch signaling.


Pssm-ID: 185747 [Multi-domain]  Cd Length: 337  Bit Score: 91.97  E-value: 9.01e-20
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 5817132    2 DQKWNSTLQTLVASYEAYEDLMKKSQEGRDFYADLESKVAALLERTQSTCQAR 54
Cdd:cd09234 285 KQKRESTISSLIASYEAYEDLLKKSQKGIDFYKKLEGNVSKLLQRIKSVCKVQ 337
ALIX_LYPXL_bnd pfam13949
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV ...
 3-55 2.01e-09

ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV p9Gag to this domain is necessary for viral budding.This domain is generally central between an N-terminal Bro1 domain, pfam03097 and a C-terminal proline-rich domain. The retroviruses thus used this domain to hijack the ESCRT system of the cell.


Pssm-ID: 464053 [Multi-domain]  Cd Length: 294  Bit Score: 59.94  E-value: 2.01e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 5817132      3 QKWNSTLQTLVASYEAYEDLMKKSQEGRDFYADLESKVAALLERTQSTCQARE 55
Cdd:pfam13949 240 RQREEALQKLENAYDKYKELVSNLQEGLKFYNDLTEILEKLLKKVKDFVNARR 292
PHA03247 PHA03247
large tegument protein UL36; Provisional
 81-422 2.85e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 58.41  E-value: 2.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132     81 LPRREESEAVEAGdppeelRSLPPDMVAGPRLPDTfLGSATPLHFPPSPFPSSTGPGPHYLSG-PLPPGTYSG----PTQ 155
Cdd:PHA03247 2663 RPRRARRLGRAAQ------ASSPPQRPRRRAARPT-VGSLTSLADPPPPPPTPEPAPHALVSAtPLPPGPAAArqasPAL 2735

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132    156 LIQPRAPGPHAMPVAPG-PALYPAPAYT-----PELGLVPRSSPQHGVVSSPYVGVGPAPPVAGLPSAPPPQfsgPELAM 229
Cdd:PHA03247 2736 PAAPAPPAVPAGPATPGgPARPARPPTTagppaPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADP---PAAVL 2812

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132    230 AVRPATTTVDSIQAPIPSHTAPRPNPTPAPPPpcfpvpppqPLPTPYTYPAGAKQPIPAQHHFSSGIPTGFPAPRIGPQP 309
Cdd:PHA03247 2813 APAAALPPAASPAGPLPPPTSAQPTAPPPPPG---------PPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPV 2883

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132    310 QPHPQPHPSQAFGPQPPQQPLPLQHPHLFPPQAPGLLPPQSPYPY-APQPGVLGQPPPPLHTQLYPGPAQDPLPAHSGAL 388
Cdd:PHA03247 2884 RRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQpQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPW 2963

                         330       340       350
                  ....*....|....*....|....*....|....
gi 5817132    389 PFPSPGPPQPPHPPLAYGPAPSTRPMGPQAAPLT 422
Cdd:PHA03247 2964 LGALVPGRVAVPRFRVPQPAPSREAPASSTPPLT 2997
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 56-436 1.91e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.06  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132     56 AARQQLLDRELKKKPPPRPTAPKPLLPRREESEAVEAGDPPEELR---------SLPPDMVAGPRLPDTFLGSATPLHFP 126
Cdd:pfam03154 161 SAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSvppqgspatSQPPNQTQSTAAPHTLIQQTPTLHPQ 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132    127 --PSPFPSSTG-----PGPHYLSGPLPPGTYSGPTQliqpraPGPHamPVAPGPALYPAPAYTPELGLVPRSSPQHGVVS 199
Cdd:pfam03154 241 rlPSPHPPLQPmtqppPPSQVSPQPLPQPSLHGQMP------PMPH--SLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPG 312

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132    200 SPYVGVGPAPPVAGLP-SAPPPQFSGPELAMAVRPATTTVDSIQAPipshtaprpnptpappppCFPVPPPQPLPTPYTY 278
Cdd:pfam03154 313 PSPAAPGQSQQRIHTPpSQSQLQSQQPPREQPLPPAPLSMPHIKPP------------------PTTPIPQLPNPQSHKH 374

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132    279 PAGAKQPIPAQhhfssgIPTGFPAPRIGPQPQPHPQPHPSQAFGPQPPQQPLPLQHPHLfPPQAPGLLPPQSPYPYAPQp 358
Cdd:pfam03154 375 PPHLSGPSPFQ------MNSNLPPPPALKPLSSLSTHHPPSAHPPPLQLMPQSQQLPPP-PAQPPVLTQSQSLPPPAAS- 446

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5817132    359 gvlgQPPPplhTQLYPGPAQDPLPAHSGALPFPSPGPPQPPHPPLAYGPAPSTRPmgPQAAPLTIRGPSSAGQSTPSP 436
Cdd:pfam03154 447 ----HPPT---SGLHQVPSQSPFPQHPFVPGGPPPITPPSGPPTSTSSAMPGIQP--PSSASVSSSGPVPAAVSCPLP 515
 
Name Accession Description Interval E-value
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 597-801 2.70e-131

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: 394.44  E-value: 2.70e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  597 YINASCVEGLSPYCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTERGQPMVHGALSLALSS 676
Cdd:cd14539   1 YINASLIEDLTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERGQALVYGAITVSLQS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  677 VRSTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQEVHAHYLHQRPLHTPIIVHCSSGVGRTGAF 756
Cdd:cd14539  81 VRTTPTHVERIISIQHKDTRLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQRSLQTPIVVHCSSGVGRTGAF 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 5817132  757 ALLYAAVQEVEAGNGIPELPQLVRRMRQQRKHMLQEKLHLRFCYE 801
Cdd:cd14539 161 CLLYAAVQEIEAGNGIPDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
574-804 2.18e-86

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 277.20  E-value: 2.18e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132    574 KNRHQDVMPYDSNRVVL--RSGKDDYINASCVEGlSPYCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQ 651
Cdd:pfam00102   4 KNRYKDVLPYDHTRVKLtgDPGPSDYINASYIDG-YKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEEKGRE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132    652 KVARYFPTERGQPMVHGALSLALSSVRSTETH-VERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQEVHA 730
Cdd:pfam00102  83 KCAQYWPEEEGESLEYGDFTVTLKKEKEDEKDyTVRTLEVSNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLLRKVRK 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5817132    731 HYlhQRPLHTPIIVHCSSGVGRTGAFALLYAAVQEVEAgNGIPELPQLVRRMRQQRKHMLQEKLHLRFCYEAVV 804
Cdd:pfam00102 163 SS--LDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEA-EGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAIL 233
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
574-805 1.53e-83

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 270.30  E-value: 1.53e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132     574 KNRHQDVMPYDSNRVVLRSGK---DDYINASCVEGLSPYcPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEK 650
Cdd:smart00194  30 KNRYKDVLPYDHTRVKLKPPPgegSDYINASYIDGPNGP-KAYIATQGPLPSTVEDFWRMVWEQKVTVIVMLTELVEKGR 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132     651 QKVARYFPTERGQPMVHGALSLALSSVRSTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQEVHA 730
Cdd:smart00194 109 EKCAQYWPDEEGEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGCSETRTVTHYHYTNWPDHGVPESPESILDLIRAVRK 188

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5817132     731 HYLHQRplhTPIIVHCSSGVGRTGAFALLYAAVQEVEAGnGIPELPQLVRRMRQQRKHMLQEKLHLRFCYEAVVR 805
Cdd:smart00194 189 SQSTST---GPIVVHCSAGVGRTGTFIAIDILLQQLEAG-KEVDIFEIVKELRSQRPGMVQTEEQYIFLYRAILE 259
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 597-801 6.47e-69

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: 228.32  E-value: 6.47e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  597 YINASCVEGLSPyCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTERGQPMVHGALSLALSS 676
Cdd:cd00047   1 YINASYIDGYRG-PKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGKPLEYGDITVTLVS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  677 VRSTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQEVHAhylHQRPLHTPIIVHCSSGVGRTGAF 756
Cdd:cd00047  80 EEELSDYTIRTLELSPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRK---EARKPNGPIVVHCSAGVGRTGTF 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 5817132  757 ALLYAAVQEVEAGNgIPELPQLVRRMRQQRKHMLQEKLHLRFCYE 801
Cdd:cd00047 157 IAIDILLERLEAEG-EVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 565-800 2.64e-50

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: 178.71  E-value: 2.64e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  565 IAIARCYSLKNRHQDVMPYDSNRVVL--RSGKD--DYINASCVEGLS---PYcpplVATQAPLPGTAADFWLMVHEQKVS 637
Cdd:cd14543  23 CSLAPANQEKNRYGDVLCLDQSRVKLpkRNGDErtDYINANFMDGYKqknAY----IATQGPLPKTYSDFWRMVWEQKVL 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  638 VIVMLVSEAEMEKQKVARYFPTERGQPMVHGALSLALSSVRSTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDS 717
Cdd:cd14543  99 VIVMTTRVVERGRVKCGQYWPLEEGSSLRYGDLTVTNLSVENKEHYKKTTLEIHNTETDESRQVTHFQFTSWPDFGVPSS 178

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  718 PSNLLRFIQEVHAhylHQR-------------PLHTPIIVHCSSGVGRTGAFALLYAAVQEVEaGNGIPELPQLVRRMRQ 784
Cdd:cd14543 179 AAALLDFLGEVRQ---QQAlavkamgdrwkghPPGPPIVVHCSAGIGRTGTFCTLDICLSQLE-DVGTLNVMQTVRRMRT 254

                       250
                ....*....|....*.
gi 5817132  785 QRKHMLQEKLHLRFCY 800
Cdd:cd14543 255 QRAFSIQTPDQYYFCY 270
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 597-803 1.28e-46

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: 166.01  E-value: 1.28e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  597 YINASCVE---GLSPYcpPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTERGQP-MVHGALSL 672
Cdd:cd14538   1 YINASHIRipvGGDTY--HYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPDSLNKPlICGGRLEV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  673 ALSSVRSTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQevHAHYLHQRplhTPIIVHCSSGVGR 752
Cdd:cd14538  79 SLEKYQSLQDFVIRRISLRDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIR--YMRRIHNS---GPIVVHCSAGIGR 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 5817132  753 TGAFALLYAAVQEVEagNGIP-ELPQLVRRMRQQRKHMLQEKLHLRFCYEAV 803
Cdd:cd14538 154 TGVLITIDVALGLIE--RDLPfDIQDIVKDLREQRQGMIQTKDQYIFCYKAC 203
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 576-791 1.88e-46

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: 165.99  E-value: 1.88e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  576 RHQDVMPYDSNRVVLRSGKD----DYINASCVEGlsPYCP-PLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEK 650
Cdd:cd14548   1 RYTNILPYDHSRVKLIPINEeegsDYINANYIPG--YNSPrEFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  651 QKVARYFPtERGQPMVHGALSLALSSVRSTETHVERVLSLQFRDQSlkRSLVHLHFPTWPELGLPDSPSNLLRFIQEVHA 730
Cdd:cd14548  79 VKCDHYWP-FDQDPVYYGDITVTMLSESVLPDWTIREFKLERGDEV--RSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRD 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5817132  731 hYLHQRplHTPIIVHCSSGVGRTGAFALLYAAVQEVEAGNGIpELPQLVRRMRQQRKHMLQ 791
Cdd:cd14548 156 -YIKQE--KGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYV-DIFGIVYDLRKHRPLMVQ 212
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 575-791 6.03e-46

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: 164.49  E-value: 6.03e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  575 NRHQDVMPYDSNRVVLRSGKDD----YINASCVEGLSPYCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMeK 650
Cdd:cd14547   1 NRYKTILPNEHSRVCLPSVDDDplssYINANYIRGYDGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA-K 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  651 QKVARYFPTErgQPMVHGALSLALSSVRSTETHVERVLSLQFRDQslKRSLVHLHFPTWPELGLPDSPSNLLRFIQEVHA 730
Cdd:cd14547  80 EKCAQYWPEE--ENETYGDFEVTVQSVKETDGYTVRKLTLKYGGE--KRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEE 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5817132  731 HYLHQRPlHTPIIVHCSSGVGRTGAFALLYAAVQEVEAgNGIPELPQLVRRMRQQRKHMLQ 791
Cdd:cd14547 156 ARQTEPH-RGPIVVHCSAGIGRTGCFIATSIGCQQLRE-EGVVDVLGIVCQLRLDRGGMVQ 214
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 574-803 1.01e-45

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: 165.38  E-value: 1.01e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  574 KNRHQDVMPYDSNRVVL----RSGKDDYINASCVEGLS---PYcpplVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEA 646
Cdd:cd14603  33 KNRYKDILPYDQTRVILsllqEEGHSDYINANFIKGVDgsrAY----IATQGPLSHTVLDFWRMIWQYGVKVILMACREI 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  647 EMEKQKVARYFPTERgQPMVHGALSLA-LSSVRSTETHVERVLSLQFRDQSlkRSLVHLHFPTWPELGLPDSPSNLLRFI 725
Cdd:cd14603 109 EMGKKKCERYWAQEQ-EPLQTGPFTITlVKEKRLNEEVILRTLKVTFQKES--RSVSHFQYMAWPDHGIPDSPDCMLAMI 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  726 QEVHAHYLHQRplhTPIIVHCSSGVGRTGAF-ALLYaaVQEVEAGNGIPE---LPQLVRRMRQQRKHMLQEKLHLRFCYE 801
Cdd:cd14603 186 ELARRLQGSGP---EPLCVHCSAGCGRTGVIcTVDY--VRQLLLTQRIPPdfsIFDVVLEMRKQRPAAVQTEEQYEFLYH 260


                ..
gi 5817132  802 AV 803
Cdd:cd14603 261 TV 262
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 574-807 1.28e-45

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: 164.11  E-value: 1.28e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  574 KNRHQDVMPYDSNRVVLRSGK----DDYINASCVEGlspYCPP--LVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAE 647
Cdd:cd14553   6 KNRYANVIAYDHSRVILQPIEgvpgSDYINANYCDG---YRKQnaYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  648 MEKQKVARYFPTeRGQPmVHGALSLALSSVRSTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQE 727
Cdd:cd14553  83 RSRVKCDQYWPT-RGTE-TYGLIQVTLLDTVELATYTVRTFALHKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  728 VHAHYlhqRPLHTPIIVHCSSGVGRTGAFALLYAAVQEVEAGNGIpELPQLVRRMRQQRKHMLQEKLHLRFCYEAVVRHV 807
Cdd:cd14553 161 VKACN---PPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTV-DIYGHVTCLRAQRNYMVQTEDQYIFIHDALLEAV 236
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 574-805 1.71e-45

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: 165.02  E-value: 1.71e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  574 KNRHQDVMPYDSNRVVLRsGKDDYINASCVEGLSPYCPPL---VATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEK 650
Cdd:cd14600  43 KNRYKDVLPYDATRVVLQ-GNEDYINASYVNMEIPSANIVnkyIATQGPLPHTCAQFWQVVWEQKLSLIVMLTTLTERGR 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  651 QKVARYFPtERGQPMVHGALSLALSSVRSTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQEVHA 730
Cdd:cd14600 122 TKCHQYWP-DPPDVMEYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTVTHLQYVAWPDHGVPDDSSDFLEFVNYVRS 200

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5817132  731 hylhQRPLHTPIIVHCSSGVGRTGAFALLYAAVQEVEagNGIPELP-QLVRRMRQQRKHMLQEKLHLRFCYEAVVR 805
Cdd:cd14600 201 ----KRVENEPVLVHCSAGIGRTGVLVTMETAMCLTE--RNQPVYPlDIVRKMRDQRAMMVQTSSQYKFVCEAILR 270
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 574-804 1.36e-44

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: 161.15  E-value: 1.36e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  574 KNRHQDVMPYDSNRVVLrsGKD-DYINASCVE---GLSPYCppLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEME 649
Cdd:cd14597   6 KNRYKNILPYDTTRVPL--GDEgGYINASFIKmpvGDEEFV--YIACQGPLPTTVADFWQMVWEQKSTVIAMMTQEVEGG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  650 KQKVARYFPTERGQP-MVHGALSLALSSVRSTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQev 728
Cdd:cd14597  82 KIKCQRYWPEILGKTtMVDNRLQLTLVRMQQLKNFVIRVLELEDIQTREVRHITHLNFTAWPDHDTPSQPEQLLTFIS-- 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5817132  729 hahYLHQRPLHTPIIVHCSSGVGRTGAFALLyAAVQEVEAGNGIPELPQLVRRMRQQRKHMLQEKLHLRFCYEAVV 804
Cdd:cd14597 160 ---YMRHIHKSGPIITHCSAGIGRSGTLICI-DVVLGLISKDLDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVIL 231
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 570-802 3.16e-44

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: 160.38  E-value: 3.16e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  570 CYSLKNRHQDVMPYDSNRVVLR--SGKD--DYINASCVEGLSpYCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSE 645
Cdd:cd14554   5 CNKFKNRLVNILPYESTRVCLQpiRGVEgsDYINASFIDGYR-QRGAYIATQGPLAETTEDFWRMLWEHNSTIIVMLTKL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  646 AEMEKQKVARYFPTERGQPmvHGALSLALSSVRSTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFI 725
Cdd:cd14554  84 REMGREKCHQYWPAERSAR--YQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFI 161

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5817132  726 QEVHAHYlHQRPLHTPIIVHCSSGVGRTGAFALLYAAVQEVEAgNGIPELPQLVRRMRQQRKHMLQEKLHLRFCYEA 802
Cdd:cd14554 162 GQVHKTK-EQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRY-EGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYRA 236
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 574-800 3.20e-44

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: 159.86  E-value: 3.20e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  574 KNRHQDVMPYDSNRVVLR--SGKDDYINASCVEGLSP---YcpplVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEM 648
Cdd:cd14545   1 LNRYRDRDPYDHDRSRVKlkQGDNDYINASLVEVEEAkrsY----ILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEK 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  649 EKQKVARYFPTERGQPMV--HGALSLALSSVRSTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQ 726
Cdd:cd14545  77 GQIKCAQYWPQGEGNAMIfeDTGLKVTLLSEEDKSYYTVRTLELENLKTQETREVLHFHYTTWPDFGVPESPAAFLNFLQ 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5817132  727 EVHAHYLHQrPLHTPIIVHCSSGVGRTGAFALLYAAVQEVEAGNGIP-ELPQLVRRMRQQRKHMLQEKLHLRFCY 800
Cdd:cd14545 157 KVRESGSLS-SDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNPSSvDVKKVLLEMRKYRMGLIQTPDQLRFSY 230
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 573-808 3.66e-44

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: 160.32  E-value: 3.66e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  573 LKNRHQDVMPYDSNRVVLRSGK-----DDYINASCV-----EGLSPYC-PPLVATQAPLPGTAADFWLMVHEQKVSVIVM 641
Cdd:cd14544   3 GKNRYKNILPFDHTRVILKDRDpnvpgSDYINANYIrneneGPTTDENaKTYIATQGCLENTVSDFWSMVWQENSRVIVM 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  642 LVSEAEMEKQKVARYFPTErGQPMVHGALSLALSSVRSTETHVERVLSLQFRDQ-SLKRSLVHLHFPTWPELGLPDSPSN 720
Cdd:cd14544  83 TTKEVERGKNKCVRYWPDE-GMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQgDPIREIWHYQYLSWPDHGVPSDPGG 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  721 LLRFIQEVHAHYLHqRPLHTPIIVHCSSGVGRTGAFALLYAAVQEVEAgNGIP---ELPQLVRRMRQQRKHMLQEKLHLR 797
Cdd:cd14544 162 VLNFLEDVNQRQES-LPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKR-KGLDcdiDIQKTIQMVRSQRSGMVQTEAQYK 239

                       250
                ....*....|.
gi 5817132  798 FCYEAVVRHVE 808
Cdd:cd14544 240 FIYVAVAQYIE 250
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 574-803 1.26e-43

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


Pssm-ID: 350455 [Multi-domain]  Cd Length: 257  Bit Score: 159.36  E-value: 1.26e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  574 KNRHQDVMPYDSNRVVLRSGKDDYINASCV---EGLSPYcpplVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEK 650
Cdd:cd14607  27 RNRYRDVSPYDHSRVKLQNTENDYINASLVvieEAQRSY----ILTQGPLPNTCCHFWLMVWQQKTKAVVMLNRIVEKDS 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  651 QKVARYFPTERGQPMVHG--ALSLALSSVRSTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQEV 728
Cdd:cd14607 103 VKCAQYWPTDEEEVLSFKetGFSVKLLSEDVKSYYTVHLLQLENINSGETRTISHFHYTTWPDFGVPESPASFLNFLFKV 182

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5817132  729 HAHYlHQRPLHTPIIVHCSSGVGRTGAFALLYAAVQEVEAGNGIP-ELPQLVRRMRQQRKHMLQEKLHLRFCYEAV 803
Cdd:cd14607 183 RESG-SLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDPDSvDIKQVLLDMRKYRMGLIQTPDQLRFSYMAV 257
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 597-801 1.28e-42

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: 154.71  E-value: 1.28e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  597 YINASCVEglSPYCPPL--VATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTERGqPMVHGALSLal 674
Cdd:cd18533   1 YINASYIT--LPGTSSKryIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEY-EGEYGDLTV-- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  675 sSVRSTETHVE-----RVLSLQfRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQEVHaHYLHQRPLHTPIIVHCSSG 749
Cdd:cd18533  76 -ELVSEEENDDggfivREFELS-KEDGKVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKR-ELNDSASLDPPIIVHCSAG 152

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  750 VGRTGAFALLYAAVQEVEAG-NGIPELP-------QLVRRMRQQRKHMLQEKLHLRFCYE 801
Cdd:cd18533 153 VGRTGTFIALDSLLDELKRGlSDSQDLEdsedpvyEIVNQLRKQRMSMVQTLRQYIFLYD 212
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 574-814 1.80e-42

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: 157.40  E-value: 1.80e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  574 KNRHQDVMPYDSNRVVL----RSGKDDYINASCVEGLspYCP-PLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEM 648
Cdd:cd14604  60 KNRYKDILPFDHSRVKLtlktSSQDSDYINANFIKGV--YGPkAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEM 137

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  649 EKQKVARYFPTERGQPMVHGALSLALSSVRSTETHVERVLSLQFRDQSlkRSLVHLHFPTWPELGLPDSPSNLLRFIQEV 728
Cdd:cd14604 138 GRKKCERYWPLYGEEPMTFGPFRISCEAEQARTDYFIRTLLLEFQNET--RRLYQFHYVNWPDHDVPSSFDSILDMISLM 215

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  729 HAHYLHQRplhTPIIVHCSSGVGRTGAFALLYAAVQEVEAGNgIPE---LPQLVRRMRQQRKHMLQEKLHlrfcYEAVVR 805
Cdd:cd14604 216 RKYQEHED---VPICIHCSAGCGRTGAICAIDYTWNLLKAGK-IPEefnVFNLIQEMRTQRHSAVQTKEQ----YELVHR 287


                ....*....
gi 5817132  806 HVEQVLQRH 814
Cdd:cd14604 288 AIAQLFEKQ 296
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 575-791 6.05e-41

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: 150.35  E-value: 6.05e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  575 NRHQDVMPYDSNRV---VLRSGKDDYINASCVEGlspYCPP--LVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEME 649
Cdd:cd14615   1 NRYNNVLPYDISRVklsVQSHSTDDYINANYMPG---YNSKkeFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  650 KQKVARYFPTErgQPMVHGALSLALSSVRSTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQEVH 729
Cdd:cd14615  78 RTKCEEYWPSK--QKKDYGDITVTMTSEIVLPEWTIRDFTVKNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVR 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5817132  730 aHYLHQRPLHTPIIVHCSSGVGRTGAFALLYAAVQEVEAGNGIpELPQLVRRMRQQRKHMLQ 791
Cdd:cd14615 156 -EYMKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVV-DVYGIVYDLRMHRPLMVQ 215
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 574-804 8.01e-41

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: 151.72  E-value: 8.01e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  574 KNRHQDVMPYDSNRVVLRSGKDDYINASCV---EGLSPYcpplVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEK 650
Cdd:cd14608  28 RNRYRDVSPFDHSRIKLHQEDNDYINASLIkmeEAQRSY----ILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGS 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  651 QKVARYFPTERGQPMV--HGALSLALSSVRSTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQEV 728
Cdd:cd14608 104 LKCAQYWPQKEEKEMIfeDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKV 183

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5817132  729 HAHYlHQRPLHTPIIVHCSSGVGRTGAFALLYAA--VQEVEAGNGIPELPQLVRRMRQQRKHMLQEKLHLRFCYEAVV 804
Cdd:cd14608 184 RESG-SLSPEHGPVVVHCSAGIGRSGTFCLADTCllLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVI 260
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 596-805 1.18e-40

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: 149.02  E-value: 1.18e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  596 DYINASCVEGLSP-------YcpplVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPtERGQPMVHG 668
Cdd:cd14541   1 DYINANYVNMEIPgsgivnrY----IAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWP-DLGETMQFG 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  669 ALSLALSSVRSTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQEVhahylhqRPLHT----PIIV 744
Cdd:cd14541  76 NLQITCVSEEVTPSFAFREFILTNTNTGEERHITQMQYLAWPDHGVPDDSSDFLDFVKRV-------RQNRVgmvePTVV 148

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5817132  745 HCSSGVGRTGAFALLYAAVQEVEAGNGIPELpQLVRRMRQQRKHMLQEKLHLRFCYEAVVR 805
Cdd:cd14541 149 HCSAGIGRTGVLITMETAMCLIEANEPVYPL-DIVRTMRDQRAMLIQTPSQYRFVCEAILR 208
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 575-801 3.14e-40

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: 148.53  E-value: 3.14e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  575 NRHQDVMPYDSNRVVLRSGKD----DYINASCVEGLSpYCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEK 650
Cdd:cd14617   1 NRYNNILPYDSTRVKLSNVDDdpcsDYINASYIPGNN-FRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  651 QKVARYFPTERgQPMVHGALSLALSSVRSTETHVERVLSLQFRDQ-SLKRSLVHLHFPTWPELGLPDSPSNLLRFIQEVH 729
Cdd:cd14617  80 VKCDHYWPADQ-DSLYYGDLIVQMLSESVLPEWTIREFKICSEEQlDAPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVR 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5817132  730 aHYLHQRPLHTPIIVHCSSGVGRTGAFALLYAAVQEVEAGNGIpELPQLVRRMRQQRKHMLQEKLHLRFCYE 801
Cdd:cd14617 159 -DYINRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSV-DIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 546-810 2.05e-39

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: 147.88  E-value: 2.05e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  546 DTVWRELQDAQEHDARGRSIAIARCYS--LKNRHQDVMPYDSNRVVLRS----GKDDYINASCVEGLSPYCPPLVATQAP 619
Cdd:cd14609  15 DRLAKEWQALCAYQAEPNTCSTAQGEAnvKKNRNPDFVPYDHARIKLKAesnpSRSDYINASPIIEHDPRMPAYIATQGP 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  620 LPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTErGQPMVHGALSLALSSVRSTETHVERVLSLQFRDQSLKR 699
Cdd:cd14609  95 LSHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDE-GSSLYHIYEVNLVSEHIWCEDFLVRSFYLKNVQTQETR 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  700 SLVHLHFPTWPELGLPDSPSNLLRFIQEVHAHYlhqRPLHTPIIVHCSSGVGRTGAFALLYAAVQEVEAGNGIPELPQLV 779
Cdd:cd14609 174 TLTQFHFLSWPAEGIPSSTRPLLDFRRKVNKCY---RGRSCPIIVHCSDGAGRTGTYILIDMVLNRMAKGVKEIDIAATL 250

                       250       260       270
                ....*....|....*....|....*....|.
gi 5817132  780 RRMRQQRKHMLQEKLHLRFCYEAVVRHVEQV 810
Cdd:cd14609 251 EHVRDQRPGMVRTKDQFEFALTAVAEEVNAI 281
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 597-812 2.48e-39

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: 144.89  E-value: 2.48e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  597 YINASCVEglSPYCPP---LVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTERGQPMVHGALSLA 673
Cdd:cd14596   1 YINASYIT--MPVGEEelfYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETLQEPMELENYQLR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  674 LSSVRSTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQevhahYLHQRPLHTPIIVHCSSGVGRT 753
Cdd:cd14596  79 LENYQALQYFIIRIIKLVEKETGENRLIKHLQFTTWPDHGTPQSSDQLVKFIC-----YMRKVHNTGPIVVHCSAGIGRA 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 5817132  754 GAFALLYAAVQEVEAGNGIpELPQLVRRMRQQRKHMLQEKLHLRFCYEAVVrhveQVLQ 812
Cdd:cd14596 154 GVLICVDVLLSLIEKDLSF-NIKDIVREMRQQRYGMIQTKDQYLFCYKVVL----EVLQ 207
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 575-805 6.09e-39

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: 145.03  E-value: 6.09e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  575 NRHQDVMPYDSNRVVLR----SGKDDYINASCVEGL-SPycPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEME 649
Cdd:cd14619   1 NRFRNVLPYDWSRVPLKpiheEPGSDYINANYMPGYwSS--QEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  650 KQKVARYFPTERgQPMVHGALSLALSSVRSTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQEVH 729
Cdd:cd14619  79 RVKCEHYWPLDY-TPCTYGHLRVTVVSEEVMENWTVREFLLKQVEEQKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLR 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5817132  730 aHYLHQRPLHTPIIVHCSSGVGRTGAFALLYAAVQEVEAgNGIPELPQLVRRMRQQRKHMLQEKLHLRFCYEAVVR 805
Cdd:cd14619 158 -QWLDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQS-EGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILD 231
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 574-808 1.60e-38

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: 144.39  E-value: 1.60e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  574 KNRHQDVMPYDSNRVVLRSGK-----DDYINASCV----EGLSPYCPP---LVATQAPLPGTAADFWLMVHEQKVSVIVM 641
Cdd:cd14605   5 KNRYKNILPFDHTRVVLHDGDpnepvSDYINANIImpefETKCNNSKPkksYIATQGCLQNTVNDFWRMVFQENSRVIVM 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  642 LVSEAEMEKQKVARYFPTERGQPMvHGALSlaLSSVRSTETH--VERVLSLQFRDQ-SLKRSLVHLHFPTWPELGLPDSP 718
Cdd:cd14605  85 TTKEVERGKSKCVKYWPDEYALKE-YGVMR--VRNVKESAAHdyILRELKLSKVGQgNTERTVWQYHFRTWPDHGVPSDP 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  719 SNLLRFIQEVHahyLHQRPLHT--PIIVHCSSGVGRTGAFA---LLYAAVQEVEAGNGIpELPQLVRRMRQQRKHMLQEK 793
Cdd:cd14605 162 GGVLDFLEEVH---HKQESIMDagPVVVHCSAGIGRTGTFIvidILIDIIREKGVDCDI-DVPKTIQMVRSQRSGMVQTE 237

                       250
                ....*....|....*
gi 5817132  794 LHLRFCYEAVVRHVE 808
Cdd:cd14605 238 AQYRFIYMAVQHYIE 252
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 597-801 1.73e-38

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: 142.53  E-value: 1.73e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  597 YINASCVEGLspYCP-PLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTERgqpMVHGALSLALS 675
Cdd:cd14558   1 YINASFIDGY--WGPkSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEK---KTYGDIEVELK 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  676 SVRSTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQEVHaHYLHQRPL----HTPIIVHCSSGVG 751
Cdd:cd14558  76 DTEKSPTYTVRVFEITHLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIK-QKLPYKNSkhgrSVPIVVHCSDGSS 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 5817132  752 RTGAFA----LLYAAVQEveagnGIPELPQLVRRMRQQRKHMLQEKLHLRFCYE 801
Cdd:cd14558 155 RTGIFCalwnLLESAETE-----KVVDVFQVVKALRKQRPGMVSTLEQYQFLYD 203
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 574-805 2.07e-38

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: 145.14  E-value: 2.07e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  574 KNRHQDVMPYDSNRVVLRSGKDD---YINAS----CVEGLSPYcppLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEA 646
Cdd:cd14599  41 RNRIREVVPYEENRVELVPTKENntgYINAShikvTVGGEEWH---YIATQGPLPHTCHDFWQMVWEQGVNVIAMVTAEE 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  647 EMEKQKVARYFPTergqpmvhgalslaLSSVRSTETHVERVLSLQFRDQS-------LK---------RSLVHLHFPTWP 710
Cdd:cd14599 118 EGGRSKSHRYWPK--------------LGSKHSSATYGKFKVTTKFRTDSgcyattgLKvkhllsgqeRTVWHLQYTDWP 183

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  711 ELGLPDSPSNLLRFIQEVHAHYLHQRPL-------HTPIIVHCSSGVGRTGAFALLYAAVQEVEAGNGIpELPQLVRRMR 783
Cdd:cd14599 184 DHGCPEEVQGFLSYLEEIQSVRRHTNSMldstkncNPPIVVHCSAGVGRTGVVILTELMIGCLEHNEKV-EVPVMLRHLR 262

                       250       260
                ....*....|....*....|..
gi 5817132  784 QQRKHMLQEKLHLRFCYEAVVR 805
Cdd:cd14599 263 EQRMFMIQTIAQYKFVYQVLIQ 284
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 580-803 2.52e-38

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: 142.88  E-value: 2.52e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  580 VMPYDSNRVVL--RSGKD--DYINASCVEGLSPYCPPlVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVAR 655
Cdd:cd14623   5 IIPYEFNRVIIpvKRGEEntDYVNASFIDGYRQKDSY-IASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEKCAQ 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  656 YFPTErgQPMVHGALSLALSSVRSTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQEVHAHylHQ 735
Cdd:cd14623  84 YWPSD--GSVSYGDITIELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQ--QQ 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5817132  736 RPLHTPIIVHCSSGVGRTGAFALLYAAVQEVEAgNGIPELPQLVRRMRQQRKHMLQEKLHLRFCYEAV 803
Cdd:cd14623 160 QSGNHPITVHCSAGAGRTGTFCALSTVLERVKA-EGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVV 226
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 597-791 3.28e-38

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: 141.72  E-value: 3.28e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  597 YINASCVEGLSPyCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTERGqpMVHGALSLALSS 676
Cdd:cd14549   1 YINANYVDGYNK-ARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGT--ETYGNIQVTLLS 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  677 VRSTETHVERVLSLQ------FRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQEVHAHylhqRPLHT-PIIVHCSSG 749
Cdd:cd14549  78 TEVLATYTVRTFSLKnlklkkVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAA----NPPGAgPIVVHCSAG 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 5817132  750 VGRTGAFALLYAAVQEVEAGNGIpELPQLVRRMRQQRKHMLQ 791
Cdd:cd14549 154 VGRTGTYIVIDSMLQQIQDKGTV-NVFGFLKHIRTQRNYLVQ 194
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 596-803 3.28e-38

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: 141.68  E-value: 3.28e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  596 DYINASCVEGL--SPYcppLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTErgQPMVHGALSLA 673
Cdd:cd14622   1 DYINASFIDGYrqKDY---FIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPSE--GSVTHGEITIE 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  674 LSSVRSTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQEVHAHylHQRPLHTPIIVHCSSGVGRT 753
Cdd:cd14622  76 IKNDTLLETISIRDFLVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQ--QQQTGNHPIVVHCSAGAGRT 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 5817132  754 GAFALLYAAVQEVEAgNGIPELPQLVRRMRQQRKHMLQEKLHLRFCYEAV 803
Cdd:cd14622 154 GTFIALSNILERVKA-EGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVV 202
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 597-804 4.69e-38

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


Pssm-ID: 350400 [Multi-domain]  Cd Length: 202  Bit Score: 141.25  E-value: 4.69e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  597 YINASCVEGLSPYcPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTErgQPMVHGALSLALSS 676
Cdd:cd14552   1 YINASFIDGYRQK-DAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPED--GSVSSGDITVELKD 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  677 VRSTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQEVHAHylHQRPLHTPIIVHCSSGVGRTGAF 756
Cdd:cd14552  78 QTDYEDYTLRDFLVTKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQ--QQQSGNHPITVHCSAGAGRTGTF 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 5817132  757 ALLYAAVQEVEAgNGIPELPQLVRRMRQQRKHMLQEKLHLRFCYEAVV 804
Cdd:cd14552 156 CALSTVLERVKA-EGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVVQ 202
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 597-801 5.10e-38

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: 141.06  E-value: 5.10e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  597 YINASCVE-GLSPYCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAE-MEKQKVARYFPTERGQPMVHGALSLAL 674
Cdd:cd17658   1 YINASLVEtPASESLPKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDnYSTAKCADYFPAEENESREFGRISVTN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  675 SSVRSTETHVE-RVLSLQFRDQSLK-RSLVHLHFPTWPELGLPDSPsnllRFIQEVHAHYLHQRPLHTPIIVHCSSGVGR 752
Cdd:cd17658  81 KKLKHSQHSITlRVLEVQYIESEEPpLSVLHIQYPEWPDHGVPKDT----RSVRELLKRLYGIPPSAGPIVVHCSAGIGR 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 5817132  753 TGAFALLYAAVQEVEAGN-GIPELPQLVRRMRQQRKHMLQEKLHLRFCYE 801
Cdd:cd17658 157 TGAYCTIHNTIRRILEGDmSAVDLSKTVRKFRSQRIGMVQTQDQYIFCYA 206
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 574-804 5.55e-38

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


Pssm-ID: 350450 [Multi-domain]  Cd Length: 234  Bit Score: 142.29  E-value: 5.55e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  574 KNRHQDVMPYDSNRVVLR---SGKD-DYINASCVEGLspYCP-PLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEM 648
Cdd:cd14602   1 KNRYKDILPYDHSRVELSlitSDEDsDYINANFIKGV--YGPrAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEM 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  649 EKQKVARYFPTERGQPMVHGALSLALSSVRSTETHVERVLSLQFrdQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQEV 728
Cdd:cd14602  79 GKKKCERYWAEPGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVKF--NSETRTIYQFHYKNWPDHDVPSSIDPILELIWDV 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5817132  729 HAHYLHQRPlhtPIIVHCSSGVGRTGAFALLYAAVQEVEAGNgIPE---LPQLVRRMRQQRKHMLQEKLHLRFCYEAVV 804
Cdd:cd14602 157 RCYQEDDSV---PICIHCSAGCGRTGVICAIDYTWMLLKDGI-IPEnfsVFSLIQEMRTQRPSLVQTKEQYELVYNAVI 231
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 574-810 7.47e-38

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: 143.27  E-value: 7.47e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  574 KNRHQDVMPYDSNRVVLRS----GKDDYINASCVEGLSPYCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEME 649
Cdd:cd14610  47 KNRSLAVLPYDHSRIILKAenshSHSDYINASPIMDHDPRNPAYIATQGPLPATVADFWQMVWESGCVVIVMLTPLAENG 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  650 KQKVARYFPTErGQPMVHgalslaLSSVRSTETHV--ERVLSLQFRDQSLK----RSLVHLHFPTWPELGLPDSPSNLLR 723
Cdd:cd14610 127 VKQCYHYWPDE-GSNLYH------IYEVNLVSEHIwcEDFLVRSFYLKNLQtnetRTVTQFHFLSWNDQGVPASTRSLLD 199

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  724 FIQEVHAHYlhqRPLHTPIIVHCSSGVGRTGAFALLYAAVQEVEAGNGIPELPQLVRRMRQQRKHMLQEKLHLRFCYEAV 803
Cdd:cd14610 200 FRRKVNKCY---RGRSCPIIVHCSDGAGRSGTYILIDMVLNKMAKGAKEIDIAATLEHLRDQRPGMVQTKEQFEFALTAV 276


                ....*..
gi 5817132  804 VRHVEQV 810
Cdd:cd14610 277 AEEVNAI 283
PHA02738 PHA02738
hypothetical protein; Provisional
 575-808 2.16e-37

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 143.14  E-value: 2.16e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132   575 NRHQDVMPYDSNRVVLRSGKD--DYINASCVEGLSpYCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQK 652
Cdd:PHA02738  53 NRYLDAVCFDHSRVILPAERNrgDYINANYVDGFE-YKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKENGREK 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132   653 VARYFPTERGQPMVHGALSLALSSVRSTETHVERVLSLQfRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQEV---- 728
Cdd:PHA02738 132 CFPYWSDVEQGSIRFGKFKITTTQVETHPHYVKSTLLLT-DGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVLEVrqcq 210

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132   729 ---HAHYL---HQRPLHTPIIVHCSSGVGRTGAFALLYAAVQEVEAGNGIpELPQLVRRMRQQRKHMLQEKLHLRFCYEA 802
Cdd:PHA02738 211 kelAQESLqigHNRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATV-SIPSIVSSIRNQRYYSLFIPFQYFFCYRA 289


                 ....*.
gi 5817132   803 VVRHVE 808
Cdd:PHA02738 290 VKRYVN 295
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 597-805 4.52e-37

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: 139.13  E-value: 4.52e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  597 YINAS----CVEGLSPYcppLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTERGQ--PMVHGAL 670
Cdd:cd14540   1 YINAShitaTVGGKQRF---YIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTLGGEhdALTFGEY 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  671 SLALSSVRSTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQEVHA---HYLHQRPLHT---PIIV 744
Cdd:cd14540  78 KVSTKFSVSSGCYTTTGLRVKHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFLEEINSvrrHTNQDVAGHNrnpPTLV 157

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5817132  745 HCSSGVGRTGAFAL----LYAAVQEVEagngiPELPQLVRRMRQQRKHMLQEKLHLRFCYEAVVR 805
Cdd:cd14540 158 HCSAGVGRTGVVILadlmLYCLDHNEE-----LDIPRVLALLRHQRMLLVQTLAQYKFVYNVLIQ 217
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 597-800 5.17e-37

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: 138.32  E-value: 5.17e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  597 YINASCVEGlsPYCPPL-VATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTERGQPMVHGALSLAL- 674
Cdd:cd14542   1 YINANFIKG--VSGSKAyIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGEEQLQFGPFKISLe 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  675 SSVRSTETHVERVLSLQFrdQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQEVHAHYLHQRPlhtPIIVHCSSGVGRTG 754
Cdd:cd14542  79 KEKRVGPDFLIRTLKVTF--QKESRTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDYQGSEDV---PICVHCSAGCGRTG 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 5817132  755 AFALLYAAVQEVEAGnGIPE---LPQLVRRMRQQRKHMLQEKLHLRFCY 800
Cdd:cd14542 154 TICAIDYVWNLLKTG-KIPEefsLFDLVREMRKQRPAMVQTKEQYELVY 201
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 597-807 6.80e-37

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: 137.96  E-value: 6.80e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  597 YINASCVEGLSPYCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTERGQpmVHGALSLALSS 676
Cdd:cd14546   1 YINASTIYDHDPRNPAYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSE--VYHIYEVHLVS 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  677 VRS-TETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQEVHAHYlhqRPLHTPIIVHCSSGVGRTGA 755
Cdd:cd14546  79 EHIwCDDYLVRSFYLKNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVNKSY---RGRSCPIVVHCSDGAGRTGT 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 5817132  756 FALLYAAVQEVEAGNGIPELPQLVRRMRQQRKHMLQEKLHLRFCYEAVVRHV 807
Cdd:cd14546 156 YILIDMVLNRMAKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAVAEEV 207
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 574-804 1.26e-36

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: 139.79  E-value: 1.26e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  574 KNRHQDVMPYDSNRVVLRS----GKDDYINASCVEGLSPYcPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEME 649
Cdd:cd14626  44 KNRYANVIAYDHSRVILTSvdgvPGSDYINANYIDGYRKQ-NAYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKS 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  650 KQKVARYFPTeRGQPmVHGALSLALSSVRSTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQEVH 729
Cdd:cd14626 123 RVKCDQYWPI-RGTE-TYGMIQVTLLDTVELATYSVRTFALYKNGSSEKREVRQFQFMAWPDHGVPEYPTPILAFLRRVK 200

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5817132  730 AhylHQRPLHTPIIVHCSSGVGRTGAFALLYAAVQEVEAGNGIpELPQLVRRMRQQRKHMLQEKLHLRFCYEAVV 804
Cdd:cd14626 201 A---CNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTV-DIYGHVTCMRSQRNYMVQTEDQYIFIHEALL 271
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 556-810 1.53e-36

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 140.14  E-value: 1.53e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132   556 QEHDARGRSIAIARCYSL-------KNRHQDVMPYDSNRVVL--RSGKDDYINASCVEGLSPYcPPLVATQAPLPGTAAD 626
Cdd:PHA02742  30 EEHEHIMQEIVAFSCNESlelknmkKCRYPDAPCFDRNRVILkiEDGGDDFINASYVDGHNAK-GRFICTQAPLEETALD 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132   627 FWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTERGQPMVHGALSLALSSVRSTETHveRVLSLQFRDQSLKRSL--VHL 704
Cdd:PHA02742 109 FWQAIFQDQVRVIVMITKIMEDGKEACYPYWMPHERGKATHGEFKIKTKKIKSFRNY--AVTNLCLTDTNTGASLdiKHF 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132   705 HFPTWPELGLPDSPSNLLRFIQEV-HAHYLHQRPL-------HTPIIVHCSSGVGRTGAFALLYAAVQEVEAGNGIPeLP 776
Cdd:PHA02742 187 AYEDWPHGGLPRDPNKFLDFVLAVrEADLKADVDIkgenivkEPPILVHCSAGLDRAGAFCAIDICISKYNERAIIP-LL 265

                        250       260       270
                 ....*....|....*....|....*....|....
gi 5817132   777 QLVRRMRQQRKHMLQEKLHLRFCYEAVVRHVEQV 810
Cdd:PHA02742 266 SIVRDLRKQRHNCLSLPQQYIFCYFIVLIFAKLM 299
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 542-807 5.80e-36

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: 138.33  E-value: 5.80e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  542 VGALDTVWRELQDAQEHDARGRSIAIArCYSLKNRHQDVMPYDSNRVVLRSGK----DDYINASCVEGLSPYcPPLVATQ 617
Cdd:cd14627  25 VTGMELEFKRLANSKAHTSRFISANLP-CNKFKNRLVNIMPYETTRVCLQPIRgvegSDYINASFIDGYRQQ-KAYIATQ 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  618 APLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTERGQPMVHgaLSLALSSVRSTETHVERVLSLQFRDQSL 697
Cdd:cd14627 103 GPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPAERSARYQY--FVVDPMAEYNMPQYILREFKVTDARDGQ 180

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  698 KRSLVHLHFPTWPELGLPDSPSNLLRFIQEVHAHYlHQRPLHTPIIVHCSSGVGRTGAFALLYAAVQEVEAgNGIPELPQ 777
Cdd:cd14627 181 SRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTK-EQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRY-EGVVDIFQ 258

                       250       260       270
                ....*....|....*....|....*....|
gi 5817132  778 LVRRMRQQRKHMLQEKLHLRFCYEAVVRHV 807
Cdd:cd14627 259 TVKMLRTQRPAMVQTEDEYQFCYQAALEYL 288
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 575-791 6.21e-36

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: 136.23  E-value: 6.21e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  575 NRHQDVMPYDSNRVVLRS-GKD---DYINASCVEGLSpYCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEK 650
Cdd:cd14618   1 NRYPHVLPYDHSRVRLSQlGGEphsDYINANFIPGYT-SPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  651 QKVARYFPTErGQPMVHGALSLALSSVRSTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQEVHA 730
Cdd:cd14618  80 VLCDHYWPSE-STPVSYGHITVHLLAQSSEDEWTRREFKLWHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVRE 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5817132  731 HyLHQRPLHTPIIVHCSSGVGRTGAFALLYAAVQEVEAgNGIPELPQLVRRMRQQRKHMLQ 791
Cdd:cd14618 159 H-VQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKE-EKVVDVFNTVYILRMHRYLMIQ 217
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 558-803 1.38e-35

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: 135.79  E-value: 1.38e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  558 HDARgrSIAIARCyslKNRHQDVMPYDSNRVVLRSGKD----DYINASCVEGlspYCPP--LVATQAPLPGTAADFWLMV 631
Cdd:cd14614   4 HFAA--DLPVNRC---KNRYTNILPYDFSRVKLVSMHEeegsDYINANYIPG---YNSPqeYIATQGPLPETRNDFWKMV 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  632 HEQKVSVIVMLVSEAEMEKQKVARYFPTERgQPMVHGALSLALSSVRSTETHVERVLSLQFRDQSlkRSLVHLHFPTWPE 711
Cdd:cd14614  76 LQQKSQIIVMLTQCNEKRRVKCDHYWPFTE-EPVAYGDITVEMLSEEEQPDWAIREFRVSYADEV--QDVMHFNYTAWPD 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  712 LGLP--DSPSNLLRFIQEVHAHYLHQRplhTPIIVHCSSGVGRTGAFALLYAAVQEVEAGNGIPELpQLVRRMRQQRKHM 789
Cdd:cd14614 153 HGVPtaNAAESILQFVQMVRQQAVKSK---GPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDIL-GLVSEMRSYRMSM 228

                       250
                ....*....|....
gi 5817132  790 LQEKLHLRFCYEAV 803
Cdd:cd14614 229 VQTEEQYIFIHQCV 242
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 574-807 2.30e-35

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: 135.93  E-value: 2.30e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  574 KNRHQDVMPYDSNRVVLR--SGKD----DYINASCVEGLSPyCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAE 647
Cdd:cd17667  30 KNRYINILAYDHSRVKLRplPGKDskhsDYINANYVDGYNK-AKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMITNLVE 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  648 MEKQKVARYFPTERGQPM-----------VHGALSLALSSVRSTEthVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPD 716
Cdd:cd17667 109 KGRRKCDQYWPTENSEEYgniivtlkstkIHACYTVRRFSIRNTK--VKKGQKGNPKGRQNERTVIQYHYTQWPDMGVPE 186

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  717 SPSNLLRFIQEVHAhylHQRPLHTPIIVHCSSGVGRTGAFALLYAAVQEVEAGNGIPELpQLVRRMRQQRKHMLQEKLHL 796
Cdd:cd17667 187 YALPVLTFVRRSSA---ARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVL-GFLKHIRTQRNYLVQTEEQY 262

                       250
                ....*....|.
gi 5817132  797 RFCYEAVVRHV 807
Cdd:cd17667 263 IFIHDALLEAI 273
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 575-791 2.56e-35

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: 134.26  E-value: 2.56e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  575 NRHQDVMPYDSNRVVLRSGK----DDYINASCVEGLspYCP-PLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEME 649
Cdd:cd14616   1 NRFPNIKPYNNNRVKLIADAgvpgSDYINASYISGY--LCPnEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  650 KQKVARYFPtERGQPM-VHGalSLALSSVRSTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQEV 728
Cdd:cd14616  79 RIRCHQYWP-EDNKPVtVFG--DIVITKLMEDVQIDWTIRDLKIERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLV 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5817132  729 HAHYLHQrplHTPIIVHCSSGVGRTGAFALLYAAVQEVEAGNGIpELPQLVRRMRQQRKHMLQ 791
Cdd:cd14616 156 RASRAHD---NTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFV-DIYGLVAELRSERMCMVQ 214
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 516-807 2.92e-35

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: 136.01  E-value: 2.92e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  516 RDPYEHPERLRQLQQeleafrGQlgDVGALDTVWRELQDAQEHDARGRSIAIArCYSLKNRHQDVMPYDSNRVVLRSGK- 594
Cdd:cd14628   6 RNLYAYIQKLTQIET------GE--NVTGMELEFKRLASSKAHTSRFISANLP-CNKFKNRLVNIMPYESTRVCLQPIRg 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  595 ---DDYINASCVEGLSPYcPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTERGQPMVHgaLS 671
Cdd:cd14628  77 vegSDYINASFIDGYRQQ-KAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQY--FV 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  672 LALSSVRSTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQEVHAHYlHQRPLHTPIIVHCSSGVG 751
Cdd:cd14628 154 VDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTK-EQFGQDGPISVHCSAGVG 232

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5817132  752 RTGAFALLYAAVQEVEAgNGIPELPQLVRRMRQQRKHMLQEKLHLRFCYEAVVRHV 807
Cdd:cd14628 233 RTGVFITLSIVLERMRY-EGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAALEYL 287
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 579-804 1.17e-34

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: 132.37  E-value: 1.17e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  579 DVMPYDSNRVVLRSGK----DDYINASCVEGLSPYcPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVA 654
Cdd:cd14620   3 NILPYDHSRVILSQLDgipcSDYINASYIDGYKEK-NKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKCY 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  655 RYFPtERGqPMVHGALSLALSSVRSTETHVERVLSLQFR-DQSLK--RSLVHLHFPTWPELGLPDSPSNLLRFIQEVHAh 731
Cdd:cd14620  82 QYWP-DQG-CWTYGNIRVAVEDCVVLVDYTIRKFCIQPQlPDGCKapRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVKS- 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5817132  732 ylhQRPLHT-PIIVHCSSGVGRTGAFALLYAAVQEVEAGNGIpELPQLVRRMRQQRKHMLQEKLHLRFCYEAVV 804
Cdd:cd14620 159 ---VNPVHAgPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKV-DVFEFVSRIRNQRPQMVQTDMQYSFIYQALL 228
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 571-800 1.53e-34

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: 132.65  E-value: 1.53e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  571 YSLKNRHQDVMPYDSNRVVLRSGK-----DDYINASCVEGLSPYCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSE 645
Cdd:cd14612  15 HASKDRYKTILPNPQSRVCLRRAGsqeeeGSYINANYIRGYDGKEKAYIATQGPMLNTVSDFWEMVWQEECPIIVMITKL 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  646 AEmEKQKVARYFPTERGQpmvHGALSLALSSVRSTETHVERVLSLQFRDQSlkRSLVHLHFPTWPELGLPDSPSNLLRFI 725
Cdd:cd14612  95 KE-KKEKCVHYWPEKEGT---YGRFEIRVQDMKECDGYTIRDLTIQLEEES--RSVKHYWFSSWPDHQTPESAGPLLRLV 168

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5817132  726 QEVHAHyLHQRPLHTPIIVHCSSGVGRTGAFALLYAAVQEVEAgNGIPELPQLVRRMRQQRKHMLQEKLHLRFCY 800
Cdd:cd14612 169 AEVEES-RQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKD-TGKVDILGIVCQLRLDRGGMIQTSEQYQFLH 241
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 596-809 8.35e-34

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: 129.29  E-value: 8.35e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  596 DYINASCVEGLSPYCPPL---VATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTERGQPmVHGALSL 672
Cdd:cd14601   1 DYINANYINMEIPSSSIInryIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSS-SYGGFQV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  673 ALSSVRSTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQEVHAHYLHQrplHTPIIVHCSSGVGR 752
Cdd:cd14601  80 TCHSEEGNPAYVFREMTLTNLEKNESRPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRNKRAGK---DEPVVVHCSAGIGR 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 5817132  753 TGAFALLYAAVQEVEAGNGIPELpQLVRRMRQQRKHMLQEKLHLRFCYEAVVRHVEQ 809
Cdd:cd14601 157 TGVLITMETAMCLIECNQPVYPL-DIVRTMRDQRAMMIQTPSQYRFVCEAILKVYEE 212
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
545-793 1.87e-33

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 130.60  E-value: 1.87e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  545 LDTVWREL----QDAQEHDARGRSIaiarcyslKNRHQDVMPYDSNRVvlrSGKDDYINASCVEGLSPYCppLVATQAPL 620
Cdd:COG5599  20 LSTLTNELapshNDPQYLQNINGSP--------LNRFRDIQPYKETAL---RANLGYLNANYIQVIGNHR--YIATQYPL 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  621 PGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKV--ARYFPTErGQpmvHGALSLALSSVRST--ETHVE-RVLSLQFRDQ 695
Cdd:COG5599  87 EEQLEDFFQMLFDNNTPVLVVLASDDEISKPKVkmPVYFRQD-GE---YGKYEVSSELTESIqlRDGIEaRTYVLTIKGT 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  696 SLK-RSLVHLHFPTWPELGLPDSpSNLLRFIQEVHAHYLHQRPLHTPIIVHCSSGVGRTGAFALLYAAVQEVEAGNGIPE 774
Cdd:COG5599 163 GQKkIEIPVLHVKNWPDHGAISA-EALKNLADLIDKKEKIKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVQITL 241

                       250       260
                ....*....|....*....|.
gi 5817132  775 -LPQLVRRMRQQR-KHMLQEK 793
Cdd:COG5599 242 sVEEIVIDMRTSRnGGMVQTS 262
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 574-808 2.90e-33

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: 129.61  E-value: 2.90e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  574 KNRHQDVMPYDSNRVVLRSGKD-----DYINASCVEG--LSPYCPP--LVATQAPLPGTAADFWLMVHEQKVSVIVMLVS 644
Cdd:cd14606  21 KNRYKNILPFDHSRVILQGRDSnipgsDYINANYVKNqlLGPDENAktYIASQGCLEATVNDFWQMAWQENSRVIVMTTR 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  645 EAEMEKQKVARYFPTERGQPMVhGALSLALSSVRSTETHVERVLSLQFRDQS-LKRSLVHLHFPTWPELGLPDSPSNLLR 723
Cdd:cd14606 101 EVEKGRNKCVPYWPEVGMQRAY-GPYSVTNCGEHDTTEYKLRTLQVSPLDNGeLIREIWHYQYLSWPDHGVPSEPGGVLS 179

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  724 FIQEVHAHYlHQRPLHTPIIVHCSSGVGRTGAFALLYAAVQEVEAgNGIP---ELPQLVRRMRQQRKHMLQEKLHLRFCY 800
Cdd:cd14606 180 FLDQINQRQ-ESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENIST-KGLDcdiDIQKTIQMVRAQRSGMVQTEAQYKFIY 257


                ....*...
gi 5817132  801 EAVVRHVE 808
Cdd:cd14606 258 VAIAQFIE 265
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 516-807 3.90e-33

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: 129.85  E-value: 3.90e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  516 RDPYEHPERLRQLQQeleafrGQlgDVGALDTVWRELQDAQEHDARGRSIAIArCYSLKNRHQDVMPYDSNRVVLRSGK- 594
Cdd:cd14629   7 RNLYAHIQKLTQVPP------GE--SVTAMELEFKLLANSKAHTSRFISANLP-CNKFKNRLVNIMPYELTRVCLQPIRg 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  595 ---DDYINASCVEGLSPYcPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTERGQPMVHgaLS 671
Cdd:cd14629  78 vegSDYINASFIDGYRQQ-KAYIATQGPLAETTEDFWRMLWEHNSTIVVMLTKLREMGREKCHQYWPAERSARYQY--FV 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  672 LALSSVRSTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQEVHAHYlHQRPLHTPIIVHCSSGVG 751
Cdd:cd14629 155 VDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVHKTK-EQFGQDGPITVHCSAGVG 233

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 5817132  752 RTGAFALLYAAVQEVEAgNGIPELPQLVRRMRQQRKHMLQEKLHLRFCYEAVVRHV 807
Cdd:cd14629 234 RTGVFITLSIVLERMRY-EGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEYL 288
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 574-807 4.62e-33

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: 129.44  E-value: 4.62e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  574 KNRHQDVMPYDSNRVVLRSGK----DDYINASCVEGLSPYcPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEME 649
Cdd:cd14625  50 KNRYANVIAYDHSRVILQPIEgimgSDYINANYIDGYRKQ-NAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKS 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  650 KQKVARYFPTeRGQPmVHGALSLALSSVRSTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQEVH 729
Cdd:cd14625 129 RIKCDQYWPS-RGTE-TYGMIQVTLLDTIELATFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVK 206

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5817132  730 AhylHQRPLHTPIIVHCSSGVGRTGAFALLYAAVQEVEAGNGIpELPQLVRRMRQQRKHMLQEKLHLRFCYEAVVRHV 807
Cdd:cd14625 207 T---CNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKHEKTV-DIYGHVTLMRSQRNYMVQTEDQYSFIHDALLEAV 280
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 597-791 2.78e-32

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: 124.55  E-value: 2.78e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  597 YINASCVEGlspYCPPL--VATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTERGQPMVHGALSLAL 674
Cdd:cd14557   1 YINASYIDG---FKEPRkyIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSMEEGSRAFGDVVVKI 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  675 SSVRSTETHVERVLSL-QFRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQEVHAhylHQRPLHTPIIVHCSSGVGRT 753
Cdd:cd14557  78 NEEKICPDYIIRKLNInNKKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNA---FNNFFSGPIVVHCSAGVGRT 154

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 5817132  754 GAFALLYAAVQEVEAgNGIPELPQLVRRMRQQRKHMLQ 791
Cdd:cd14557 155 GTYIGIDAMLEGLEA-EGRVDVYGYVVKLRRQRCLMVQ 191
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 574-804 3.15e-32

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: 125.52  E-value: 3.15e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  574 KNRHQDVMPYDSNRVVLR----SGKDDYINASCVEGlspYCPP--LVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAE 647
Cdd:cd14630   6 KNRYGNIISYDHSRVRLQlldgDPHSDYINANYIDG---YHRPrhYIATQGPMQETVKDFWRMIWQENSASVVMVTNLVE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  648 MEKQKVARYFPTErgqPMVHGALSLALSSVRSTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQE 727
Cdd:cd14630  83 VGRVKCVRYWPDD---TEVYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEIREIRQFHFTSWPDHGVPCYATGLLGFVRQ 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5817132  728 VhaHYLHQrPLHTPIIVHCSSGVGRTGAFALLYAAVQEVEAgNGIPELPQLVRRMRQQRKHMLQEKLHLRFCYEAVV 804
Cdd:cd14630 160 V--KFLNP-PDAGPIVVHCSAGAGRTGCFIAIDIMLDMAEN-EGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAIL 232
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 574-807 8.85e-32

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: 126.00  E-value: 8.85e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  574 KNRHQDVMPYDSNRVVLRSGK----DDYINASCVEGLSPYcPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEME 649
Cdd:cd14624  50 KNRYANVIAYDHSRVLLSAIEgipgSDYINANYIDGYRKQ-NAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERS 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  650 KQKVARYFPTeRGQPmVHGALSLALSSVRSTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQEVH 729
Cdd:cd14624 129 RVKCDQYWPS-RGTE-TYGLIQVTLLDTVELATYCVRTFALYKNGSSEKREVRQFQFTAWPDHGVPEHPTPFLAFLRRVK 206

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5817132  730 AhylHQRPLHTPIIVHCSSGVGRTGAFALLYAAVQEVEAGNGIpELPQLVRRMRQQRKHMLQEKLHLRFCYEAVVRHV 807
Cdd:cd14624 207 T---CNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERIKHEKTV-DIYGHVTLMRAQRNYMVQTEDQYIFIHDALLEAV 280
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 597-801 8.98e-32

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: 123.10  E-value: 8.98e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  597 YINASCVEGLSPYcPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPtERGQpMVHGALSLALSS 676
Cdd:cd14551   1 YINASYIDGYQEK-NKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWP-DQGC-WTYGNLRVRVED 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  677 VRSTETHVERVLSLQ--FRDQSLK--RSLVHLHFPTWPELGLPDSPSNLLRFIQEVHAhylhQRPLHT-PIIVHCSSGVG 751
Cdd:cd14551  78 TVVLVDYTTRKFCIQkvNRGIGEKrvRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKS----ANPPRAgPIVVHCSAGVG 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 5817132  752 RTGAFALLYAAVQEVEAGNGIpELPQLVRRMRQQRKHMLQEKLHLRFCYE 801
Cdd:cd14551 154 RTGTFIVIDAMLDMMHAEGKV-DVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 573-807 1.29e-31

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: 124.59  E-value: 1.29e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  573 LKNRHQDVMPYDSNRVVLRSGKDD-----YINASCVEGLSPYCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAE 647
Cdd:cd14613  27 RKNRYKTILPNPHSRVCLTSPDQDdplssYINANYIRGYGGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEE 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  648 MeKQKVARYFPTERGqpmVHGALSLALSSVRSTETHVERVLSLqfRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQE 727
Cdd:cd14613 107 M-NEKCTEYWPEEQV---TYEGIEITVKQVIHADDYRLRLITL--KSGGEERGLKHYWYTSWPDQKTPDNAPPLLQLVQE 180

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  728 VHAHYLHQRPLHTPIIVHCSSGVGRTGAFALLYAAVQEVEAGnGIPELPQLVRRMRQQRKHMLQEKLHLRFcyeavVRHV 807
Cdd:cd14613 181 VEEARQQAEPNCGPVIVHCSAGIGRTGCFIATSICCKQLRNE-GVVDILRTTCQLRLDRGGMIQTCEQYQF-----VHHV 254
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 574-806 2.25e-31

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: 125.14  E-value: 2.25e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  574 KNRHQDVMPYDSNRVVLRSGK----DDYINASCVEGLSPYcPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEME 649
Cdd:cd14621  55 KNRYVNILPYDHSRVHLTPVEgvpdSDYINASFINGYQEK-NKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERK 133

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  650 KQKVARYFPTErgQPMVHGALSLALSSVRSTETHVERVLSLQ----FRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFI 725
Cdd:cd14621 134 ECKCAQYWPDQ--GCWTYGNIRVSVEDVTVLVDYTVRKFCIQqvgdVTNKKPQRLITQFHFTSWPDFGVPFTPIGMLKFL 211

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  726 QEVHAhylhQRPLHT-PIIVHCSSGVGRTGAFALLYAAVQEVEAGNGIpELPQLVRRMRQQRKHMLQEKLHLRFCYEAVV 804
Cdd:cd14621 212 KKVKN----CNPQYAgAIVVHCSAGVGRTGTFIVIDAMLDMMHAERKV-DVYGFVSRIRAQRCQMVQTDMQYVFIYQALL 286


                ..
gi 5817132  805 RH 806
Cdd:cd14621 287 EH 288
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 597-804 5.30e-31

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: 121.24  E-value: 5.30e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  597 YINASCVEGlspYCPP--LVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTERGQPmvHGALSLAL 674
Cdd:cd17668   1 YINANYVDG---YNKPkaYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSEE--YGNFLVTQ 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  675 SSVRSTETHVERVLSLqfRDQSLK----------RSLVHLHFPTWPELGLPDSPSNLLRFIQEVHAHYLHQrplHTPIIV 744
Cdd:cd17668  76 KSVQVLAYYTVRNFTL--RNTKIKkgsqkgrpsgRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASYAKRHA---VGPVVV 150

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  745 HCSSGVGRTGAFALLYAAVQEVEAgNGIPELPQLVRRMRQQRKHMLQEKLHLRFCYEAVV 804
Cdd:cd17668 151 HCSAGVGRTGTYIVLDSMLQQIQH-EGTVNIFGFLKHIRSQRNYLVQTEEQYVFIHDALV 209
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
700-803 7.59e-31

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 117.07  E-value: 7.59e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132     700 SLVHLHFPTWPELGLPDSPSNLLRFIQEVHAHYlHQRPLHTPIIVHCSSGVGRTGAFALLYAAVQEVEAGNGIPELPQLV 779
Cdd:smart00404   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNL-NQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVDIFDTV 79

                           90       100
                   ....*....|....*....|....
gi 5817132     780 RRMRQQRKHMLQEKLHLRFCYEAV 803
Cdd:smart00404  80 KELRSQRPGMVQTEEQYLFLYRAL 103
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 700-803 7.59e-31

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: 117.07  E-value: 7.59e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132     700 SLVHLHFPTWPELGLPDSPSNLLRFIQEVHAHYlHQRPLHTPIIVHCSSGVGRTGAFALLYAAVQEVEAGNGIPELPQLV 779
Cdd:smart00012   1 TVKHYHYTGWPDHGVPESPDSILELLRAVKKNL-NQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAEAGEVDIFDTV 79

                           90       100
                   ....*....|....*....|....
gi 5817132     780 RRMRQQRKHMLQEKLHLRFCYEAV 803
Cdd:smart00012  80 KELRSQRPGMVQTEEQYLFLYRAL 103
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 574-800 5.57e-30

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: 118.87  E-value: 5.57e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  574 KNRHQDVMPYDSNRVVLRSGKDD-----YINASCVEGLSPYCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEm 648
Cdd:cd14611   2 KNRYKTILPNPHSRVCLKPKNSNdslstYINANYIRGYGGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKE- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  649 EKQKVARYFPTERGqpmVHGALSLALSSVRSTETHVERVLSLQFRDQSlkRSLVHLHFPTWPELGLPDSPSNLLRFIQEV 728
Cdd:cd14611  81 KNEKCVLYWPEKRG---IYGKVEVLVNSVKECDNYTIRNLTLKQGSQS--RSVKHYWYTSWPDHKTPDSAQPLLQLMLDV 155

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5817132  729 HAHYLhQRPLHTPIIVHCSSGVGRTGAFALLYAAVQEVEAgNGIPELPQLVRRMRQQRKHMLQEKLHLRFCY 800
Cdd:cd14611 156 EEDRL-ASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKE-EGVVDVLSIVCQLRVDRGGMVQTSEQYEFVH 225
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 597-801 2.39e-29

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: 115.97  E-value: 2.39e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  597 YINASCVEGlspYCPP--LVATQAPLPGTAADFWLMVHEQKVSVIVMLvSEAEMEKQKVARYFPTERGQpmVHGALSLAL 674
Cdd:cd14556   1 YINAALLDS---YKQPaaFIVTQHPLPNTVTDFWRLVYDYGCTSIVML-NQLDPKDQSCPQYWPDEGSG--TYGPIQVEF 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  675 SSVRSTETHVERVLSLQ--FRDQSLKRSLVHLHFPTWPELGL-PDSPSNLLRFIQEVHAhyLHQRPLHTPIIVHCSSGVG 751
Cdd:cd14556  75 VSTTIDEDVISRIFRLQntTRPQEGYRMVQQFQFLGWPRDRDtPPSKRALLKLLSEVEK--WQEQSGEGPIVVHCLNGVG 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 5817132  752 RTGAFALLYAAVQEVEAGNGIpELPQLVRRMRQQRKHMLQEKLHLRFCYE 801
Cdd:cd14556 153 RSGVFCAISSVCERIKVENVV-DVFQAVKTLRNHRPNMVETEEQYKFCYD 201
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 597-804 3.79e-29

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: 115.78  E-value: 3.79e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  597 YINASCVEGlspYCPP--LVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTERGqpmVHGALSLAL 674
Cdd:cd14555   1 YINANYIDG---YHRPnhYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTE---VYGDIKVTL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  675 SSVRSTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQEVHAhylHQRPLHTPIIVHCSSGVGRTG 754
Cdd:cd14555  75 VETEPLAEYVVRTFALERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVKA---SNPPSAGPIVVHCSAGAGRTG 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 5817132  755 AFALLYAAVQEVEAgNGIPELPQLVRRMRQQRKHMLQEKLHLRFCYEAVV 804
Cdd:cd14555 152 CYIVIDIMLDMAER-EGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAIL 200
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 597-804 4.51e-29

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: 115.53  E-value: 4.51e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  597 YINASCVEGLSpYCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTERGqpmVHGALSLALSS 676
Cdd:cd14632   1 YINANYIDGYH-RSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSD---TYGDIKITLLK 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  677 VRSTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQEVHAhylHQRPLHTPIIVHCSSGVGRTGAF 756
Cdd:cd14632  77 TETLAEYSVRTFALERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKA---STPPDAGPVVVHCSAGAGRTGCY 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 5817132  757 ALLYAAVQEVEAgNGIPELPQLVRRMRQQRKHMLQEKLHLRFCYEAVV 804
Cdd:cd14632 154 IVLDVMLDMAEC-EGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAIL 200
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 573-804 1.18e-28

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: 116.30  E-value: 1.18e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  573 LKNRHQDVMPYDSNRVVLRS----GKDDYINASCVEGlspYCPP--LVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEA 646
Cdd:cd14633  42 MKNRYGNIIAYDHSRVRLQPiegeTSSDYINGNYIDG---YHRPnhYIATQGPMQETIYDFWRMVWHENTASIIMVTNLV 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  647 EMEKQKVARYFPTErgqPMVHGALSLALSSVRSTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQ 726
Cdd:cd14633 119 EVGRVKCCKYWPDD---TEIYKDIKVTLIETELLAEYVIRTFAVEKRGVHEIREIRQFHFTGWPDHGVPYHATGLLGFVR 195

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5817132  727 EVHAhylHQRPLHTPIIVHCSSGVGRTGAFALLYAAVQEVEAgNGIPELPQLVRRMRQQRKHMLQEKLHLRFCYEAVV 804
Cdd:cd14633 196 QVKS---KSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAER-EGVVDIYNCVRELRSRRVNMVQTEEQYVFIHDAIL 269
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 587-804 1.60e-26

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: 108.57  E-value: 1.60e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  587 RVVLRSGKDD----YINASCVEGlspYCPP--LVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPTE 660
Cdd:cd14631   1 RVILQPVEDDpssdYINANYIDG---YQRPshYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDD 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  661 rgqPMVHGALSLALSSVRSTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQEVHahyLHQRPLHT 740
Cdd:cd14631  78 ---TEVYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVK---LSNPPSAG 151

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5817132  741 PIIVHCSSGVGRTGAFALLYAAVQEVEAgNGIPELPQLVRRMRQQRKHMLQEKLHLRFCYEAVV 804
Cdd:cd14631 152 PIVVHCSAGAGRTGCYIVIDIMLDMAER-EGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAIL 214
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 572-803 1.61e-26

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 111.66  E-value: 1.61e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132   572 SLKNRHQDVMPYDSNRVVLRS---------GKDD--------------YINASCVEGLSPyCPPLVATQAPLPGTAADFW 628
Cdd:PHA02746  52 LKKNRFHDIPCWDHSRVVINAheslkmfdvGDSDgkkievtsednaenYIHANFVDGFKE-ANKFICAQGPKEDTSEDFF 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132   629 LMVHEQKVSVIVMLvSEAEMEKQKVARYFPTERGQPMVHGALSLALSSVRSTETHVERVLSLQFRDQSLKRSLVHLHFPT 708
Cdd:PHA02746 131 KLISEHESQVIVSL-TDIDDDDEKCFELWTKEEDSELAFGRFVAKILDIIEELSFTKTRLMITDKISDTSREIHHFWFPD 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132   709 WPELGLPDSPSNLLRFIQEVHAHYL-------HQRPLHTPIIVHCSSGVGRTGAFALLYAAVQEVEAGNGIpELPQLVRR 781
Cdd:PHA02746 210 WPDNGIPTGMAEFLELINKVNEEQAelikqadNDPQTLGPIVVHCSAGIGRAGTFCAIDNALEQLEKEKEV-CLGEIVLK 288

                        250       260
                 ....*....|....*....|..
gi 5817132   782 MRQQRKHMLQEKLHLRFCYEAV 803
Cdd:PHA02746 289 IRKQRHSSVFLPEQYAFCYKAL 310
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 597-805 3.20e-26

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: 107.75  E-value: 3.20e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  597 YINASCVE-GLSPYCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYFPT--ERGQPMVHGALSLA 673
Cdd:cd14598   1 YINASHIKvTVGGKEWDYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPRlgSRHNTVTYGRFKIT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  674 LSSVRSTETHVERVLSLQFRDQSLKRSLVHLHFPTWPELGLPDSPSNLLRFIQEVHAHYLHQ------RPLHTPIIVHCS 747
Cdd:cd14598  81 TRFRTDSGCYATTGLKIKHLLTGQERTVWHLQYTDWPEHGCPEDLKGFLSYLEEIQSVRRHTnstidpKSPNPPVLVHCS 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 5817132  748 SGVGRTGAFALLYAAVQEVEAgNGIPELPQLVRRMRQQRKHMLQEKLHLRFCYEAVVR 805
Cdd:cd14598 161 AGVGRTGVVILSEIMIACLEH-NEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQ 217
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 574-786 7.64e-26

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 109.32  E-value: 7.64e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132   574 KNRHQDVMPYDSNRVVLRSG---KDDYINASCVEGLSPYcPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLV-SEAEME 649
Cdd:PHA02747  54 KNRYWDIPCWDHNRVILDSGggsTSDYIHANWIDGFEDD-KKFIATQGPFAETCADFWKAVWQEHCSIIVMLTpTKGTNG 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132   650 KQKVARYF-PTERGQPMVHG-ALSLALSSVRSTETHVervlSLQFRDQSLK--RSLVHLHFPTWPELglpDSPSNLLRFI 725
Cdd:PHA02747 133 EEKCYQYWcLNEDGNIDMEDfRIETLKTSVRAKYILT----LIEITDKILKdsRKISHFQCSEWFED---ETPSDHPDFI 205

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5817132   726 QEVH----------AHYLHQRPLHTPIIVHCSSGVGRTGAFALLYAAVQEVEAGNGIpELPQLVRRMRQQR 786
Cdd:PHA02747 206 KFIKiidinrkksgKLFNPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAI-CLAKTAEKIREQR 275
V_HD-PTP_like cd09234
Protein-interacting V-domain of mammalian His-Domain type N23 protein tyrosine phosphatase and ...
 2-54 9.01e-20

Protein-interacting V-domain of mammalian His-Domain type N23 protein tyrosine phosphatase and related domains; This family contains the V-shaped (V) domain of mammalian His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23) and related domains. It belongs to the V_Alix_like superfamily which includes the V domains of Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, mammalian Alix (apoptosis-linked gene-2 interacting protein X/ also known as apoptosis-linked gene-2 interacting protein 1, AIP1), and related domains. HD_PTP interacts with the ESCRT (Endosomal Sorting Complexes Required for Transport) system, and participates in cell migration and endosomal trafficking. The related Alix V-domain (belonging to a different family in this superfamily) contains a binding site, partially conserved in the superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. In addition to the V-domain, HD_PTP also has an N-terminal Bro1-like domain, a proline-rich region (PRR), a catalytically inactive tyrosine phosphatase domain, and a region containing a PEST motif. Bro1-like domains bind components of the ESCRT-III complex, specifically to CHMP4 in the case of HD-PTP. The Bro1-like domain of HD-PTP can also bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. HD-PTP is encoded by the PTPN23 gene, a tumor suppressor gene candidate frequently absent in human kidney, breast, lung, and cervical tumors. This family also contains Drosophila Myopic, which promotes epidermal growth factor receptor (EGFR) signaling, and Caenorhabditis elegans (enhancer of glp-1) EGO-2 which promotes Notch signaling.


Pssm-ID: 185747 [Multi-domain]  Cd Length: 337  Bit Score: 91.97  E-value: 9.01e-20
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 5817132    2 DQKWNSTLQTLVASYEAYEDLMKKSQEGRDFYADLESKVAALLERTQSTCQAR 54
Cdd:cd09234 285 KQKRESTISSLIASYEAYEDLLKKSQKGIDFYKKLEGNVSKLLQRIKSVCKVQ 337
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 597-801 4.42e-19

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


Pssm-ID: 350398 [Multi-domain]  Cd Length: 200  Bit Score: 86.61  E-value: 4.42e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  597 YINASCVEGlspY--CPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVarYFPTErGQPMVHGALSLAL 674
Cdd:cd14550   1 YINASYLQG---YrrSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPI--YWPTK-EKPLECETFKVTL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  675 SSvrstETHV-----ERVLSLQFRDQSLKRSLV----HLHFPTWPElglPDSP-SNLLRFIQEVHAHYLHQrplHTPIIV 744
Cdd:cd14550  75 SG----EDHSclsneIRLIVRDFILESTQDDYVlevrQFQCPSWPN---PCSPiHTVFELINTVQEWAQQR---DGPIVV 144

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 5817132  745 HCSSGVGRTGAFALLYAAVQEVEAGNGIpELPQLVRRMRQQRKHMLQEKLHLRFCYE 801
Cdd:cd14550 145 HDRYGGVQAATFCALTTLHQQLEHESSV-DVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 597-801 3.24e-16

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: 78.52  E-value: 3.24e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  597 YINASCVEglSPYCPP-LVATQAPLPGTAADFWLMVHEQKVSVIVMLvseAEMEK-QKVARYFPTErgQPMVHGALSLAL 674
Cdd:cd14634   1 YINAALMD--SHKQPAaFIVTQHPLPNTVADFWRLVFDYNCSSVVML---NEMDAaQLCMQYWPEK--TSCCYGPIQVEF 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  675 SSVRSTETHVERVLSL--QFRDQSLKRSLVHLHFPTWPEL-GLPDSPSNLLRFIQEVHAHYLHQRPLHTPIIVHCSSGVG 751
Cdd:cd14634  74 VSADIDEDIISRIFRIcnMARPQDGYRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQYDGREGRTVVHCLNGGG 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 5817132  752 RTGAFALLYAAVQEVEAGNgIPELPQLVRRMRQQRKHMLQEKLHLRFCYE 801
Cdd:cd14634 154 RSGTFCAICSVCEMIQQQN-IIDVFHTVKTLRNNKSNMVETLEQYKFVYE 202
V_Alix_like cd08915
Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains ...
 2-54 3.39e-13

Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains the V-shaped (V) domain of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, and related domains. Alix, HD-PTP, Bro1, and Rim20 all interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Alix, also known as apoptosis-linked gene-2 interacting protein 1 (AIP1), participates in membrane remodeling processes during the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), and the abscission reactions of mammalian cell division. It also functions in apoptosis. HD-PTP functions in cell migration and endosomal trafficking, Bro1 in endosomal trafficking, and Rim20 in the response to the external pH via the Rim101 pathway. The Alix V-domain contains a binding site, partially conserved in this superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. Members of this superfamily have an N-terminal Bro1-like domain, which binds components of the ESCRT-III complex. The Bro1-like domains of Alix and HD-PTP can also bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. Many members, including Alix, HD-PTP, and Bro1, also have a proline-rich region (PRR), which binds multiple partners in Alix, including Tsg101 (tumor susceptibility gene 101, a component of ESCRT-1) and the apoptotic protein ALG-2. The C-terminal portion (V-domain and PRR) of Bro1 interacts with Doa4, a ubiquitin thiolesterase needed to remove ubiquitin from MVB cargoes; it interacts with a YPxL motif in Doa4s catalytic domain to stimulate its deubiquitination activity. Rim20 may bind the ESCRT-III subunit Snf7, bringing the protease Rim13 (a YPxL-containing transcription factor) into proximity with Rim101, and promoting the proteolytic activation of Rim101. HD-PTP is encoded by the PTPN23 gene, a tumor suppressor gene candidate often absent in human kidney, breast, lung, and cervical tumors. HD-PTP has a C-terminal catalytically inactive tyrosine phosphatase domain.


Pssm-ID: 185746 [Multi-domain]  Cd Length: 342  Bit Score: 71.99  E-value: 3.39e-13
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 5817132    2 DQKWNSTLQTLVASYEAYEDLMKKSQEGRDFYADLESKVAALLERTQSTCQAR 54
Cdd:cd08915 290 LDPREEALQDLEASYKKYLELKENLNEGSKFYNDLIEKVNRLLEECEDFVNAR 342
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 597-804 1.16e-12

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


Pssm-ID: 350508 [Multi-domain]  Cd Length: 205  Bit Score: 68.17  E-value: 1.16e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  597 YINASCVEGLSpYCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVArYFPTeRGQPMVHGALSLAL-S 675
Cdd:cd17670   1 YINASYIMGYY-RSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQGLAEDEFV-YWPS-REESMNCEAFTVTLiS 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  676 SVRSTETHVERVLSLQFRDQSLKRSLV----HLHFPTWPElglPDSP-SNLLRFIQEVHAHYLHQrplHTPIIVHCSSGV 750
Cdd:cd17670  78 KDRLCLSNEEQIIIHDFILEATQDDYVlevrHFQCPKWPN---PDAPiSSTFELINVIKEEALTR---DGPTIVHDEFGA 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 5817132  751 GRTGAFALLYAAVQEVEAGNGIpELPQLVRRMRQQRKHMLQEKLHLRFCYEAVV 804
Cdd:cd17670 152 VSAGTLCALTTLSQQLENENAV-DVYQVAKMINLMRPGVFTDIEQYQFLYKAML 204
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 597-804 2.41e-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: 66.94  E-value: 2.41e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  597 YINASCVEGLSpYCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVArYFPTeRGQPMVHGALSLALSS 676
Cdd:cd17669   1 YINASYIMGYY-QSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEFV-YWPN-KDEPINCETFKVTLIA 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  677 vrstETHV-----ERVLSLQFRDQSLKRSLV----HLHFPTWPElglPDSPSN----LLRFIQEVHAHYlhqrplHTPII 743
Cdd:cd17669  78 ----EEHKclsneEKLIIQDFILEATQDDYVlevrHFQCPKWPN---PDSPISktfeLISIIKEEAANR------DGPMI 144

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5817132  744 VHCSSGVGRTGAFALLYAAVQEVEAGNGIpELPQLVRRMRQQRKHMLQEKLHLRFCYEAVV 804
Cdd:cd17669 145 VHDEHGGVTAGTFCALTTLMHQLEKENSV-DVYQVAKMINLMRPGVFTDIEQYQFLYKAIL 204
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 597-804 1.20e-11

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: 65.09  E-value: 1.20e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  597 YINASCVEGlspYCPP--LVATQAPLPGTAADFWLMVHEQKVSVIVML--VSEAEMEKQkvarYFPtERGQPMvHGALSL 672
Cdd:cd14635   1 YINAALMDS---YKQPsaFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLndVDPAQLCPQ----YWP-ENGVHR-HGPIQV 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  673 ALSSVRSTETHVERVLSL--QFRDQSLKRSLVHLHFPTWPEL-GLPDSPSNLLRFIQEVHAHYLHQRPLHTPIIVHCSSG 749
Cdd:cd14635  72 EFVSADLEEDIISRIFRIynAARPQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEYNGGEGRTVVHCLNG 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 5817132  750 VGRTGAFALLYAAVQEVEAGNGIpELPQLVRRMRQQRKHMLQEKLHLRFCYEAVV 804
Cdd:cd14635 152 GGRSGTFCAISIVCEMLRHQRAV-DVFHAVKTLRNNKPNMVDLLDQYKFCYEVAL 205
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 597-801 1.51e-11

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: 64.66  E-value: 1.51e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  597 YINASCVEGlspYCPP--LVATQAPLPGTAADFWLMVHEQKVSVIVMLvSEAEMeKQKVARYFPTErgqpmvhGALSLAL 674
Cdd:cd14636   1 YINAALMDS---YRQPaaFIVTQHPLPNTVKDFWRLVYDYGCTSIVML-NEVDL-AQGCPQYWPEE-------GMLRYGP 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  675 SSVRSTETHVE-RVLSLQFRDQSLKRSLV-HLHFPTWPELG------LPDSPSNLLRFIQEVHAHYLHQRPLHTPIIVHC 746
Cdd:cd14636  69 IQVECMSCSMDcDVISRIFRICNLTRPQEgYLMVQQFQYLGwashreVPGSKRSFLKLILQVEKWQEECDEGEGRTIIHC 148

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 5817132  747 SSGVGRTGAFALLYAAVQEVEAGNgIPELPQLVRRMRQQRKHMLQEKLHLRFCYE 801
Cdd:cd14636 149 LNGGGRSGMFCAISIVCEMIKRQN-VVDVFHAVKTLRNSKPNMVETPEQYRFCYD 202
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 597-804 7.72e-11

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: 62.62  E-value: 7.72e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  597 YINASCVEGLSpYCPPLVATQAPLPGTAADFWLMVHEQKVSVIVMLvseAEMEKQKVA----RYFPTERGQPmvHGALSL 672
Cdd:cd14637   1 YINAALTDSYT-RSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVML---NQLNQSNSAwpclQYWPEPGLQQ--YGPMEV 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  673 ALSSVRSTETHVERVLSLQ--FRDQSLKRSLVHLHFPTW-PELGLPDSPSNLLRFIQEVHAHYLHQRPLHTpiIVHCSSG 749
Cdd:cd14637  75 EFVSGSADEDIVTRLFRVQniTRLQEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKWQRESGEGRT--VVHCLNG 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 5817132  750 VGRTGAFALLyAAVQEVEAGNGIPELPQLVRRMRQQRKHMLQEKLHLRFCYEAVV 804
Cdd:cd14637 153 GGRSGTYCAS-AMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIAL 206
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 614-793 8.89e-10

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: 60.11  E-value: 8.89e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  614 VATQAPLPGTAADFWLMVHEQKVSVIVMLVSEAEMEKQKVARYF-PTER-GQPMVHGALSLALSSVRSTETHVervLSLQ 691
Cdd:cd14559  32 IACQYPKNEQLEDHLKMLADNRTPCLVVLASNKDIQRKGLPPYFrQSGTyGSVTVKSKKTGKDELVDGLKADM---YNLK 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  692 FRDQSLKRSLVHLHFPTWPELG---------LPD----SPSNLLRFIQEVHAHYLHQRPLHTPIIvHCSSGVGRTGAFAl 758
Cdd:cd14559 109 ITDGNKTITIPVVHVTNWPDHTaisseglkeLADlvnkSAEEKRNFYKSKGSSAINDKNKLLPVI-HCRAGVGRTGQLA- 186

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 5817132  759 lyAAVQEVEAGNGIpELPQLVRRMRQQRK-HMLQEK 793
Cdd:cd14559 187 --AAMELNKSPNNL-SVEDIVSDMRTSRNgKMVQKD 219
ALIX_LYPXL_bnd pfam13949
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV ...
 3-55 2.01e-09

ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV p9Gag to this domain is necessary for viral budding.This domain is generally central between an N-terminal Bro1 domain, pfam03097 and a C-terminal proline-rich domain. The retroviruses thus used this domain to hijack the ESCRT system of the cell.


Pssm-ID: 464053 [Multi-domain]  Cd Length: 294  Bit Score: 59.94  E-value: 2.01e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 5817132      3 QKWNSTLQTLVASYEAYEDLMKKSQEGRDFYADLESKVAALLERTQSTCQARE 55
Cdd:pfam13949 240 RQREEALQKLENAYDKYKELVSNLQEGLKFYNDLTEILEKLLKKVKDFVNARR 292
PHA03247 PHA03247
large tegument protein UL36; Provisional
 81-422 2.85e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 58.41  E-value: 2.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132     81 LPRREESEAVEAGdppeelRSLPPDMVAGPRLPDTfLGSATPLHFPPSPFPSSTGPGPHYLSG-PLPPGTYSG----PTQ 155
Cdd:PHA03247 2663 RPRRARRLGRAAQ------ASSPPQRPRRRAARPT-VGSLTSLADPPPPPPTPEPAPHALVSAtPLPPGPAAArqasPAL 2735

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132    156 LIQPRAPGPHAMPVAPG-PALYPAPAYT-----PELGLVPRSSPQHGVVSSPYVGVGPAPPVAGLPSAPPPQfsgPELAM 229
Cdd:PHA03247 2736 PAAPAPPAVPAGPATPGgPARPARPPTTagppaPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADP---PAAVL 2812

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132    230 AVRPATTTVDSIQAPIPSHTAPRPNPTPAPPPpcfpvpppqPLPTPYTYPAGAKQPIPAQHHFSSGIPTGFPAPRIGPQP 309
Cdd:PHA03247 2813 APAAALPPAASPAGPLPPPTSAQPTAPPPPPG---------PPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPV 2883

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132    310 QPHPQPHPSQAFGPQPPQQPLPLQHPHLFPPQAPGLLPPQSPYPY-APQPGVLGQPPPPLHTQLYPGPAQDPLPAHSGAL 388
Cdd:PHA03247 2884 RRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQpQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPW 2963

                         330       340       350
                  ....*....|....*....|....*....|....
gi 5817132    389 PFPSPGPPQPPHPPLAYGPAPSTRPMGPQAAPLT 422
Cdd:PHA03247 2964 LGALVPGRVAVPRFRVPQPAPSREAPASSTPPLT 2997
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
684-783 2.20e-07

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 51.12  E-value: 2.20e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  684 VERVLSLQFRDQSL-----KRSLVHLHFPtWPELGLPDsPSNLLRFIQEVHAHYLHQRPLHtpiiVHCSSGVGRTGAFAL 758
Cdd:COG2453  26 IDAVVSLTEEEELLlglleEAGLEYLHLP-IPDFGAPD-DEQLQEAVDFIDEALREGKKVL----VHCRGGIGRTGTVAA 99

                        90       100
                ....*....|....*....|....*
gi 5817132  759 LYAAVQEVEAGNGIpelpQLVRRMR 783
Cdd:COG2453 100 AYLVLLGLSAEEAL----ARVRAAR 120
PHA03247 PHA03247
large tegument protein UL36; Provisional
 64-437 4.04e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.09  E-value: 4.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132     64 RELKKKPPPRPTAPKPLLPRREESEAVEAGDPPEELRSLPPDMVAGPRLPDTFLGSATPLHFPPSPFPSSTGPG-----P 138
Cdd:PHA03247 2585 RARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPgrvsrP 2664

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132    139 HYLSGPLPPGTYSGPTQLIQPRAPGPHAMPVA-----PGPALYPAPAYTPELGLVPRS-SPQHGVVSSPYVGVGPAPPVA 212
Cdd:PHA03247 2665 RRARRLGRAAQASSPPQRPRRRAARPTVGSLTsladpPPPPPTPEPAPHALVSATPLPpGPAAARQASPALPAAPAPPAV 2744

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132    213 ----------------------------GLPSAPPPQFSGPELAMAVRPATTTVDSIQAPIPSHTAPRPNPTPAPPPPCF 264
Cdd:PHA03247 2745 pagpatpggparparppttagppapappAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASP 2824

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132    265 PVPPPQPLPTPYTYPAGAKQPIPAQHHFSSGIPTGFPAPRIGPQPQPHPQPHPSQAFGPQPPQQPLPLQHPHLF---PPQ 341
Cdd:PHA03247 2825 AGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFalpPDQ 2904

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132    342 APGLLPPQSPYPYAPQPG--VLGQPPPPLHTQLYPGPAQDPLPAHSGAlPFPSPGPPQPPHPPLAYGPAPSTRPMGPQAA 419
Cdd:PHA03247 2905 PERPPQPQAPPPPQPQPQppPPPQPQPPPPPPPRPQPPLAPTTDPAGA-GEPSGAVPQPWLGALVPGRVAVPRFRVPQPA 2983

                         410
                  ....*....|....*...
gi 5817132    420 PlTIRGPSSagqSTPSPH 437
Cdd:PHA03247 2984 P-SREAPAS---STPPLT 2997
PHA03247 PHA03247
large tegument protein UL36; Provisional
 85-523 1.17e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.55  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132     85 EESEAVEAGDPPEELRSLPPdmvagPRLPDTFLGSATPLHFPPSPFPSS--TGPG-PHYLSGPLPPGTYSGPTQLIQPRA 161
Cdd:PHA03247 2541 EELASDDAGDPPPPLPPAAP-----PAAPDRSVPPPRPAPRPSEPAVTSraRRPDaPPQSARPRAPVDDRGDPRGPAPPS 2615

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132    162 PGPHAMPVAPGPALYPAPAYTPELG---------LVPRSSPQHGVVSSPYVGVGPAPPVAglPSAPPPQFSGPELAMAVR 232
Cdd:PHA03247 2616 PLPPDTHAPDPPPPSPSPAANEPDPhppptvpppERPRDDPAPGRVSRPRRARRLGRAAQ--ASSPPQRPRRRAARPTVG 2693

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132    233 PATTTVD-----SIQAPIPSHTAPRPNPTPAPPPPCFPVPPPQPLPTPYTYPAGAKQPIPAQHHFSSGIPTGFPAPRIGP 307
Cdd:PHA03247 2694 SLTSLADpppppPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPA 2773

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132    308 QPQPHPQPHPSQAFGPQPPQQPLPLQHPHLFPPQAPGLLPPQSPYPYAPQPGVLGQPPP---PLHTQLYPGPAQDPLPAH 384
Cdd:PHA03247 2774 APAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTsaqPTAPPPPPGPPPPSLPLG 2853

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132    385 SGALPFPSPGPPQPPHPPLAYGPAPSTRPMGPQAAPLTIRGPSSAGQSTPSPhlvppPAPSPGPGPVPPRPPAAEPPPCL 464
Cdd:PHA03247 2854 GSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQP-----ERPPQPQAPPPPQPQPQPPPPPQ 2928

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5817132    465 RRGAAAADLLSSSPESQHGGTQSPGGGQPL--------LQPTKVDAAEGRRPQAlrlieRDPYEHPE 523
Cdd:PHA03247 2929 PQPPPPPPPRPQPPLAPTTDPAGAGEPSGAvpqpwlgaLVPGRVAVPRFRVPQP-----APSREAPA 2990
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 722-801 2.25e-05

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: 44.65  E-value: 2.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132  722 LRFIQEVHAHYlhqrplhTPIIVHCSSGVGRTGAFALLYAavqeVEAGNGIPElpQLVRRMRQQRKHMLQEKL-HLRFCY 800
Cdd:cd14494  46 LEVLDQAEKPG-------EPVLVHCKAGVGRTGTLVACYL----VLLGGMSAE--EAVRIVRLIRPGGIPQTIeQLDFLI 112


                .
gi 5817132  801 E 801
Cdd:cd14494 113 K 113
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 56-436 1.91e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 42.06  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132     56 AARQQLLDRELKKKPPPRPTAPKPLLPRREESEAVEAGDPPEELR---------SLPPDMVAGPRLPDTFLGSATPLHFP 126
Cdd:pfam03154 161 SAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSvppqgspatSQPPNQTQSTAAPHTLIQQTPTLHPQ 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132    127 --PSPFPSSTG-----PGPHYLSGPLPPGTYSGPTQliqpraPGPHamPVAPGPALYPAPAYTPELGLVPRSSPQHGVVS 199
Cdd:pfam03154 241 rlPSPHPPLQPmtqppPPSQVSPQPLPQPSLHGQMP------PMPH--SLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPG 312

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132    200 SPYVGVGPAPPVAGLP-SAPPPQFSGPELAMAVRPATTTVDSIQAPipshtaprpnptpappppCFPVPPPQPLPTPYTY 278
Cdd:pfam03154 313 PSPAAPGQSQQRIHTPpSQSQLQSQQPPREQPLPPAPLSMPHIKPP------------------PTTPIPQLPNPQSHKH 374

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132    279 PAGAKQPIPAQhhfssgIPTGFPAPRIGPQPQPHPQPHPSQAFGPQPPQQPLPLQHPHLfPPQAPGLLPPQSPYPYAPQp 358
Cdd:pfam03154 375 PPHLSGPSPFQ------MNSNLPPPPALKPLSSLSTHHPPSAHPPPLQLMPQSQQLPPP-PAQPPVLTQSQSLPPPAAS- 446

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5817132    359 gvlgQPPPplhTQLYPGPAQDPLPAHSGALPFPSPGPPQPPHPPLAYGPAPSTRPmgPQAAPLTIRGPSSAGQSTPSP 436
Cdd:pfam03154 447 ----HPPT---SGLHQVPSQSPFPQHPFVPGGPPPITPPSGPPTSTSSAMPGIQP--PSSASVSSSGPVPAAVSCPLP 515
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 134-367 4.68e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 4.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132   134 TGPGPHYLSGPLPPGTYSGPTQLIQPRAPGPHAMPVAP---GPALYPAPAYTPELGLVPRSSPQHGVVSSPYVGVGPAPP 210
Cdd:PRK07764 590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPapaGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGW 669

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5817132   211 VAGLPSAPPPQFSGPELAMAVRPATTTVDSIQAPIPSHTAPRPnptpappppcfpvpppqplptpytyPAGAKQPIPAQH 290
Cdd:PRK07764 670 PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAG-------------------------QADDPAAQPPQA 724

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5817132   291 HFSSGIPTGFPAPRIGPQPQPHPQPHPSQAfgpqppqqplplqhphlfPPQAPGLLPPQSPYPYAPQPGVLGQPPPP 367
Cdd:PRK07764 725 AQGASAPSPAADDPVPLPPEPDDPPDPAGA------------------PAQPPPPPAPAPAAAPAAAPPPSPPSEEE 783
 
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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