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Conserved domains on  [gi|1725351434|ref|NP_001359063|]
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receptor-type tyrosine-protein phosphatase beta precursor [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 1734-1961 7.38e-177

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: 535.27  E-value: 7.38e-177
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1734 NRYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRV 1813
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1814 KCDHYWPADQDPLYYGDLILQMVSESVLPEWTIREFKICSEEQLDAHRLLRHFHYTVWPDHGVPETTQSLIQFVRTVRDY 1893
Cdd:cd14617     81 KCDHYWPADQDSLYYGDLIVQMLSESVLPEWTIREFKICSEEQLDAPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVRDY 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1725351434 1894 INRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 1961
Cdd:cd14617    161 INRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
PTP_tm pfam18861
TM proximal of protein tyrosine phosphatase, receptor type J; Protein tyrosine phosphatases ...
 1474-1613 1.32e-32

TM proximal of protein tyrosine phosphatase, receptor type J; Protein tyrosine phosphatases (PTPs) are known to be signaling molecules that regulate a variety of cellular processes, including cell growth, differentiation, mitotic cycle, and oncogenic transformation. PTP receptor type J possesses an extracellular region containing five fibronectin type III repeats, the transmembrane region included in this Pfam entry, and a intracytoplasmic catalytic domain. This entry probably contains part of a Fn3 domain at the N-terminus.


:

Pssm-ID: 465889  Cd Length: 126  Bit Score: 123.49  E-value: 1.32e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1474 VNCSWFSDTNGAVKYFAVVVREADSmdELRPEQQHPLPSYLEYRhNASIRVYQTNYFASKCAEspdPDRSSKSFNIKLGG 1553
Cdd:pfam18861    1 IQFSLFNSSNGPIKAYGVIVTTNDS--LNRPLKEYLNKTYYDWK-YKKTDSYLATVTPNPFTS---PRSSSRSLTVPVGT 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1725351434 1554 EMDSlggkcdpsqQKFCDGPLKPHTAYRISIRAFTQL-FDEGLKEFTKPLYSDTFFSMPIT 1613
Cdd:pfam18861   75 GSKW---------QGYCNGPLKPLGSYRFSVAAFTRLeFDDGLIDGEESYVSFTPFSEPIA 126
fn3 pfam00041
Fibronectin type III domain;
1263-1345 5.28e-13

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 66.28  E-value: 5.28e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1263 SPPSLLSFADVANTSLAITWKGPPDWT-DYNDFELQWLPGDALTVFNPYSSKKSEGR-IVNGLRPGRSYQFSVKTVSGDS 1340
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNgPITGYEVEYRPKNSGEPWNEITVPGTTTSvTLTGLKPGTEYEVRVQAVNGGG 80


                   ....*
gi 1725351434 1341 WKTYS 1345
Cdd:pfam00041   81 EGPPS 85
fn3 pfam00041
Fibronectin type III domain;
1357-1436 7.87e-11

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 60.12  E-value: 7.87e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1357 DKIQNLHCRPQNSTAIACSWIPP---DSDFDGYSIECRKMDTQEIEFSRKLEKEKSLLNIMMLVPHRRYLVSIKVQSAGV 1433
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ...
gi 1725351434 1434 TSE 1436
Cdd:pfam00041   81 EGP 83
FN3 super family cl27307
Fibronectin type 3 domain [General function prediction only];
903-1293 8.34e-10

Fibronectin type 3 domain [General function prediction only];


The actual alignment was detected with superfamily member COG3401:

Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 63.87  E-value: 8.34e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  903 EGLTVPSTVKNIHISANGATDRLTVTWSPGGGDVDSYVVSAFRQDEKVESHTLPKHGSEHTFHRLEAGATYRIAIVSVS- 981
Cdd:COG3401    135 AATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDt 214

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  982 ---GSLRNQIDVL-GQTVPASVHGVVADnAYSSNSLTVSWQKALGM-AERYDILLLSENGvllSNTSEPATVKQHKFED- 1055
Cdd:COG3401    215 ggeSAPSNEVSVTtPTTPPSAPTGLTAT-ADTPGSVTLSWDPVTESdATGYRVYRSNSGD---GPFTKVATVTTTSYTDt 290

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1056 -LTPGKKYKMQILTVSG----GLFSKEVE-TEGRTVPAAVTNLRITENSSRHLSFSWTASEGE-LSWYNIFLYNPDKTLQ 1128
Cdd:COG3401    291 gLTNGTTYYYRVTAVDAagneSAPSNVVSvTTDLTPPAAPSGLTATAVGSSSITLSWTASSDAdVTGYNVYRSTSGGGTY 370

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1129 ERAQVDPLVQSFSFQNLLQGRM--YKMVIVTHSGELSNESF-IFGRTVPAAV-NHLKGSNRNMTDSLWFSWSPASGDFDF 1204
Cdd:COG3401    371 TKIAETVTTTSYTDTGLTPGTTyyYKVTAVDAAGNESAPSEeVSATTASAASgESLTASVDAVPLTDVAGATAAASAASN 450

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1205 YELILYNPNGTKKENWREKDVTEWRFQGLIPGRKYTLYVVTHSGDLSNK-VTGEGRTAPSPPSLLSFADVANTSLAITWK 1283
Cdd:COG3401    451 PGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGsGASSVTNSVSVIGASAAAAVGGAPDGTPNV 530

                          410
                   ....*....|
gi 1725351434 1284 GPPDWTDYND 1293
Cdd:COG3401    531 TGASPVTVGA 540
fn3 pfam00041
Fibronectin type III domain;
292-371 1.40e-09

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 56.65  E-value: 1.40e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  292 EVSNLKVTSGGSlTSLNVKWQKPL---GVIDSYSITLSHQGTVKESK--TLPPRATEIQFKDLVPGRFYQVTIRCVSGEL 366
Cdd:pfam00041    2 APSNLTVTDVTS-TSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNeiTVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....*
gi 1725351434  367 SAEKS 371
Cdd:pfam00041   81 EGPPS 85
fn3 pfam00041
Fibronectin type III domain;
113-195 1.93e-09

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 56.27  E-value: 1.93e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  113 PPARLEVNPerTTSTTLQVRWTPS---SGKVTWYEVQLFDQNNQKiQEVQVQESATWSQYTFLNLTAGSSYKIGITAVSG 189
Cdd:pfam00041    2 APSNLTVTD--VTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGE-PWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78


                   ....*.
gi 1725351434  190 GKRSFP 195
Cdd:pfam00041   79 GGEGPP 84
fn3 pfam00041
Fibronectin type III domain;
470-548 8.78e-09

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 54.34  E-value: 8.78e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  470 AVLQLRIKQANETSLGITWRAPL---GEWEKYTISL--MDRELFVIHKSLSKDAKEYTFTNLMPGRNYKATVTSMSGDLK 544
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYrpKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ....
gi 1725351434  545 QSAS 548
Cdd:pfam00041   82 GPPS 85
fn3 pfam00041
Fibronectin type III domain;
733-809 1.38e-08

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 53.57  E-value: 1.38e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  733 DKVQGISVSNsARSDYLKVSWVHAT---GDFDHYEVTIKNRDSF--IQTKSIPKSENECVFARLVPGRLYSITVTTKSGQ 807
Cdd:pfam00041    1 SAPSNLTVTD-VTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGepWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ..
gi 1725351434  808 YE 809
Cdd:pfam00041   80 GE 81
fn3 pfam00041
Fibronectin type III domain;
822-895 9.10e-07

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 48.57  E-value: 9.10e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1725351434  822 PVKNLTLLNRSTEDLHVTWSRA---NGDVDQYEVQLL-FNDMKVFPPIYLVNTATEYQFSALTPGRHYKILVLTISGD 895
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRpKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 204-273 6.03e-06

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


:

Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 46.07  E-value: 6.03e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1725351434   204 PSPVEDIGISP-NPNSLLISWSRGPGN-----VEQFRLMLMDKGAIVQDTNVDKRDTSYAFRGLTPGHLYNVTIVT 273
Cdd:smart00060    1 PSPPSNLRVTDvTSTSVTLSWEPPPDDgitgyIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRA 76
fn3 pfam00041
Fibronectin type III domain;
394-455 8.29e-06

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 45.87  E-value: 8.29e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1725351434  394 SFAVNWTPPA---GDWDHYRILLF--NDSLVLLNTTVGKEETHFALEGLEliPGRQYEVEVIVESGN 455
Cdd:pfam00041   15 SLTVSWTPPPdgnGPITGYEVEYRpkNSGEPWNEITVPGTTTSVTLTGLK--PGTEYEVRVQAVNGG 79
fn3 pfam00041
Fibronectin type III domain;
645-723 1.14e-05

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 45.48  E-value: 1.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  645 SSVSGVTVNNSGrNDYLSVSWLPAP---GEVHHYVVTLSH--DSKVVQSLITAKFVSECSFSSLTPGRLYNVTITTKSGN 719
Cdd:pfam00041    1 SAPSNLTVTDVT-STSLTVSWTPPPdgnGPITGYEVEYRPknSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ....
gi 1725351434  720 YESH 723
Cdd:pfam00041   80 GEGP 83
 
Name Accession Description Interval E-value
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 1734-1961 7.38e-177

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: 535.27  E-value: 7.38e-177
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1734 NRYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRV 1813
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1814 KCDHYWPADQDPLYYGDLILQMVSESVLPEWTIREFKICSEEQLDAHRLLRHFHYTVWPDHGVPETTQSLIQFVRTVRDY 1893
Cdd:cd14617     81 KCDHYWPADQDSLYYGDLIVQMLSESVLPEWTIREFKICSEEQLDAPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVRDY 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1725351434 1894 INRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 1961
Cdd:cd14617    161 INRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1705-1963 5.51e-115

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 365.06  E-value: 5.51e-115
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  1705 LLSKEYEDLKDVGRS-QSCDIALLPENRGKNRYNNILPYDASRVKLcNVDDDPCSDYINASYIPGNNFRREYIATQGPLP 1783
Cdd:smart00194    1 GLEEEFEKLDRLKPDdESCTVAAFPENRDKNRYKDVLPYDHTRVKL-KPPPGEGSDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  1784 GTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQ-DPLYYGDLILQMVSESVLPEWTIREFKICSEEQlDAHRL 1862
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEgEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGC-SETRT 158

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  1863 LRHFHYTVWPDHGVPETTQSLIQFVRTVRDYinRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDL 1942
Cdd:smart00194  159 VTHYHYTNWPDHGVPESPESILDLIRAVRKS--QSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKEL 236

                           250       260
                    ....*....|....*....|.
gi 1725351434  1943 RLHRVHMVQTECQYVYLHQCV 1963
Cdd:smart00194  237 RSQRPGMVQTEEQYIFLYRAI 257
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1730-1963 2.68e-100

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 321.88  E-value: 2.68e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1730 NRGKNRYNNILPYDASRVKLcnVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVE 1809
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKL--TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1810 KGRVKCDHYWP-ADQDPLYYGDLILQMVSE-SVLPEWTIREFKIcSEEQLDAHRLLRHFHYTVWPDHGVPETTQSLIQFV 1887
Cdd:pfam00102   79 KGREKCAQYWPeEEGESLEYGDFTVTLKKEkEDEKDYTVRTLEV-SNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLL 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1725351434 1888 RTVRDYiNRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 1963
Cdd:pfam00102  158 RKVRKS-SLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 1687-1972 3.43e-41

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 154.77  E-value: 3.43e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1687 KINQFEGHFMKLQADSN--YLLSKEYEDLKDVGRSQSCDIALLPENRGKNRYNNILPYDASRVKLCNvdDDPCSDYINAS 1764
Cdd:PHA02742     7 KKNSFAKNCEQLIEESNlaEILKEEHEHIMQEIVAFSCNESLELKNMKKCRYPDAPCFDRNRVILKI--EDGGDDFINAS 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1765 YIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYW-PADQDPLYYGDLILQMVSESVLPE 1843
Cdd:PHA02742    85 YVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYWmPHERGKATHGEFKIKTKKIKSFRN 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1844 WTIREFKIcSEEQLDAHRLLRHFHYTVWPDHGVPETTQSLIQFVRTVR--DYINRSPGAG-------PTVVHCSAGVGRT 1914
Cdd:PHA02742   165 YAVTNLCL-TDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFVLAVReaDLKADVDIKGenivkepPILVHCSAGLDRA 243

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1725351434 1915 GTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYlhqCVRDVLRARKL 1972
Cdd:PHA02742   244 GAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIF---CYFIVLIFAKL 298
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
1728-1956 9.17e-41

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 152.94  E-value: 9.17e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1728 PENRGKNRYNNILPYDASRVKlcnvDDDPcsdYINASYIPGNNFRReYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQC 1807
Cdd:COG5599     40 INGSPLNRFRDIQPYKETALR----ANLG---YLNANYIQVIGNHR-YIATQYPLEEQLEDFFQMLFDNNTPVLVVLASD 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1808 VE--KGRVKCDHYWPADqdplyyGDLILQMVS------ESVLPEWTIREFKI----CSEEQLDAHrllrHFHYTVWPDHG 1875
Cdd:COG5599    112 DEisKPKVKMPVYFRQD------GEYGKYEVSseltesIQLRDGIEARTYVLtikgTGQKKIEIP----VLHVKNWPDHG 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1876 VPETTQsLIQFVRTVRDYIN-RSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKD--SVDIYGAVHDLRLHR-VHMVQ 1951
Cdd:COG5599    182 AISAEA-LKNLADLIDKKEKiKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRnGGMVQ 260


                   ....*
gi 1725351434 1952 TECQY 1956
Cdd:COG5599    261 TSEQL 265
PTP_tm pfam18861
TM proximal of protein tyrosine phosphatase, receptor type J; Protein tyrosine phosphatases ...
 1474-1613 1.32e-32

TM proximal of protein tyrosine phosphatase, receptor type J; Protein tyrosine phosphatases (PTPs) are known to be signaling molecules that regulate a variety of cellular processes, including cell growth, differentiation, mitotic cycle, and oncogenic transformation. PTP receptor type J possesses an extracellular region containing five fibronectin type III repeats, the transmembrane region included in this Pfam entry, and a intracytoplasmic catalytic domain. This entry probably contains part of a Fn3 domain at the N-terminus.


Pssm-ID: 465889  Cd Length: 126  Bit Score: 123.49  E-value: 1.32e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1474 VNCSWFSDTNGAVKYFAVVVREADSmdELRPEQQHPLPSYLEYRhNASIRVYQTNYFASKCAEspdPDRSSKSFNIKLGG 1553
Cdd:pfam18861    1 IQFSLFNSSNGPIKAYGVIVTTNDS--LNRPLKEYLNKTYYDWK-YKKTDSYLATVTPNPFTS---PRSSSRSLTVPVGT 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1725351434 1554 EMDSlggkcdpsqQKFCDGPLKPHTAYRISIRAFTQL-FDEGLKEFTKPLYSDTFFSMPIT 1613
Cdd:pfam18861   75 GSKW---------QGYCNGPLKPLGSYRFSVAAFTRLeFDDGLIDGEESYVSFTPFSEPIA 126
fn3 pfam00041
Fibronectin type III domain;
1263-1345 5.28e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 66.28  E-value: 5.28e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1263 SPPSLLSFADVANTSLAITWKGPPDWT-DYNDFELQWLPGDALTVFNPYSSKKSEGR-IVNGLRPGRSYQFSVKTVSGDS 1340
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNgPITGYEVEYRPKNSGEPWNEITVPGTTTSvTLTGLKPGTEYEVRVQAVNGGG 80


                   ....*
gi 1725351434 1341 WKTYS 1345
Cdd:pfam00041   81 EGPPS 85
fn3 pfam00041
Fibronectin type III domain;
1357-1436 7.87e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 60.12  E-value: 7.87e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1357 DKIQNLHCRPQNSTAIACSWIPP---DSDFDGYSIECRKMDTQEIEFSRKLEKEKSLLNIMMLVPHRRYLVSIKVQSAGV 1433
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ...
gi 1725351434 1434 TSE 1436
Cdd:pfam00041   81 EGP 83
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
903-1293 8.34e-10

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 63.87  E-value: 8.34e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  903 EGLTVPSTVKNIHISANGATDRLTVTWSPGGGDVDSYVVSAFRQDEKVESHTLPKHGSEHTFHRLEAGATYRIAIVSVS- 981
Cdd:COG3401    135 AATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDt 214

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  982 ---GSLRNQIDVL-GQTVPASVHGVVADnAYSSNSLTVSWQKALGM-AERYDILLLSENGvllSNTSEPATVKQHKFED- 1055
Cdd:COG3401    215 ggeSAPSNEVSVTtPTTPPSAPTGLTAT-ADTPGSVTLSWDPVTESdATGYRVYRSNSGD---GPFTKVATVTTTSYTDt 290

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1056 -LTPGKKYKMQILTVSG----GLFSKEVE-TEGRTVPAAVTNLRITENSSRHLSFSWTASEGE-LSWYNIFLYNPDKTLQ 1128
Cdd:COG3401    291 gLTNGTTYYYRVTAVDAagneSAPSNVVSvTTDLTPPAAPSGLTATAVGSSSITLSWTASSDAdVTGYNVYRSTSGGGTY 370

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1129 ERAQVDPLVQSFSFQNLLQGRM--YKMVIVTHSGELSNESF-IFGRTVPAAV-NHLKGSNRNMTDSLWFSWSPASGDFDF 1204
Cdd:COG3401    371 TKIAETVTTTSYTDTGLTPGTTyyYKVTAVDAAGNESAPSEeVSATTASAASgESLTASVDAVPLTDVAGATAAASAASN 450

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1205 YELILYNPNGTKKENWREKDVTEWRFQGLIPGRKYTLYVVTHSGDLSNK-VTGEGRTAPSPPSLLSFADVANTSLAITWK 1283
Cdd:COG3401    451 PGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGsGASSVTNSVSVIGASAAAAVGGAPDGTPNV 530

                          410
                   ....*....|
gi 1725351434 1284 GPPDWTDYND 1293
Cdd:COG3401    531 TGASPVTVGA 540
fn3 pfam00041
Fibronectin type III domain;
292-371 1.40e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 56.65  E-value: 1.40e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  292 EVSNLKVTSGGSlTSLNVKWQKPL---GVIDSYSITLSHQGTVKESK--TLPPRATEIQFKDLVPGRFYQVTIRCVSGEL 366
Cdd:pfam00041    2 APSNLTVTDVTS-TSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNeiTVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....*
gi 1725351434  367 SAEKS 371
Cdd:pfam00041   81 EGPPS 85
fn3 pfam00041
Fibronectin type III domain;
113-195 1.93e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 56.27  E-value: 1.93e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  113 PPARLEVNPerTTSTTLQVRWTPS---SGKVTWYEVQLFDQNNQKiQEVQVQESATWSQYTFLNLTAGSSYKIGITAVSG 189
Cdd:pfam00041    2 APSNLTVTD--VTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGE-PWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78


                   ....*.
gi 1725351434  190 GKRSFP 195
Cdd:pfam00041   79 GGEGPP 84
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 111-198 1.98e-09

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 56.35  E-value: 1.98e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  111 PLPPARLEVNPerTTSTTLQVRWTPSS---GKVTWYEVQLFDQNNQKIQEVQVQESATwSQYTFLNLTAGSSYKIGITAV 187
Cdd:cd00063      1 PSPPTNLRVTD--VTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSE-TSYTLTGLKPGTEYEFRVRAV 77

                           90
                   ....*....|.
gi 1725351434  188 SGGKRSFPVYT 198
Cdd:cd00063     78 NGGGESPPSES 88
fn3 pfam00041
Fibronectin type III domain;
470-548 8.78e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 54.34  E-value: 8.78e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  470 AVLQLRIKQANETSLGITWRAPL---GEWEKYTISL--MDRELFVIHKSLSKDAKEYTFTNLMPGRNYKATVTSMSGDLK 544
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYrpKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ....
gi 1725351434  545 QSAS 548
Cdd:pfam00041   82 GPPS 85
fn3 pfam00041
Fibronectin type III domain;
733-809 1.38e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 53.57  E-value: 1.38e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  733 DKVQGISVSNsARSDYLKVSWVHAT---GDFDHYEVTIKNRDSF--IQTKSIPKSENECVFARLVPGRLYSITVTTKSGQ 807
Cdd:pfam00041    1 SAPSNLTVTD-VTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGepWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ..
gi 1725351434  808 YE 809
Cdd:pfam00041   80 GE 81
fn3 pfam00041
Fibronectin type III domain;
1176-1249 1.90e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 53.19  E-value: 1.90e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1725351434 1176 AVNHLKGSNRNmTDSLWFSWSPA---SGDFDFYELILYNPNGTKKENWRE--KDVTEWRFQGLIPGRKYTLYVVTHSGD 1249
Cdd:pfam00041    2 APSNLTVTDVT-STSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEITvpGTTTSVTLTGLKPGTEYEVRVQAVNGG 79
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1262-1349 6.70e-07

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 49.03  E-value: 6.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1262 PSPPSLLSFADVANTSLAITWKGPPDWTDYND-FELQWLPGDALTVFNPYSSKKSEGR-IVNGLRPGRSYQFSVKTVSGD 1339
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITgYVVEYREKGSGDWKEVEVTPGSETSyTLTGLKPGTEYEFRVRAVNGG 80

                           90
                   ....*....|
gi 1725351434 1340 SWKTYSKPIS 1349
Cdd:cd00063     81 GESPPSESVT 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1356-1444 7.03e-07

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 49.03  E-value: 7.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1356 PDKIQNLHCRPQNSTAIACSWIPPDSD---FDGYSIECRKMDTQEIEFSRKLEKEKSLLNIMMLVPHRRYLVSIKVQSAG 1432
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDggpITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                           90
                   ....*....|..
gi 1725351434 1433 VTSEVVEDSTIT 1444
Cdd:cd00063     81 GESPPSESVTVT 92
fn3 pfam00041
Fibronectin type III domain;
822-895 9.10e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 48.57  E-value: 9.10e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1725351434  822 PVKNLTLLNRSTEDLHVTWSRA---NGDVDQYEVQLL-FNDMKVFPPIYLVNTATEYQFSALTPGRHYKILVLTISGD 895
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRpKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 111-193 2.06e-06

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 47.61  E-value: 2.06e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434   111 PLPPARLEVnpERTTSTTLQVRWT-PSSGKVTWYEVQLFDQNNQK-IQEVQVQESATWSQYTFLNLTAGSSYKIGITAVS 188
Cdd:smart00060    1 PSPPSNLRV--TDVTSTSVTLSWEpPPDDGITGYIVGYRVEYREEgSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78


                    ....*
gi 1725351434   189 GGKRS 193
Cdd:smart00060   79 GAGEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 290-365 2.25e-06

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 47.88  E-value: 2.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  290 PMEVSNLKVTSGGSlTSLNVKWQKPL---GVIDSYSITLS--HQGTVKESKTLPPRATEIQFKDLVPGRFYQVTIRCVSG 364
Cdd:cd00063      1 PSPPTNLRVTDVTS-TSVTLSWTPPEddgGPITGYVVEYRekGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79


                   .
gi 1725351434  365 E 365
Cdd:cd00063     80 G 80
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1262-1341 4.20e-06

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 46.45  E-value: 4.20e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  1262 PSPPSLLSFADVANTSLAITWKGPPD--WTDYND-FELQWLPGDALTVFNPYSSKKSEGrIVNGLRPGRSYQFSVKTVSG 1338
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDdgITGYIVgYRVEYREEGSEWKEVNVTPSSTSY-TLTGLKPGTEYEFRVRAVNG 79


                    ...
gi 1725351434  1339 DSW 1341
Cdd:smart00060   80 AGE 82
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 204-273 6.03e-06

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 46.07  E-value: 6.03e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1725351434   204 PSPVEDIGISP-NPNSLLISWSRGPGN-----VEQFRLMLMDKGAIVQDTNVDKRDTSYAFRGLTPGHLYNVTIVT 273
Cdd:smart00060    1 PSPPSNLRVTDvTSTSVTLSWEPPPDDgitgyIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRA 76
fn3 pfam00041
Fibronectin type III domain;
394-455 8.29e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 45.87  E-value: 8.29e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1725351434  394 SFAVNWTPPA---GDWDHYRILLF--NDSLVLLNTTVGKEETHFALEGLEliPGRQYEVEVIVESGN 455
Cdd:pfam00041   15 SLTVSWTPPPdgnGPITGYEVEYRpkNSGEPWNEITVPGTTTSVTLTGLK--PGTEYEVRVQAVNGG 79
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 290-364 8.75e-06

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 45.68  E-value: 8.75e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434   290 PMEVSNLKVTSGGSlTSLNVKWQKP-----LGVIDSYSITLSHQGTVKESKTLPPRATEIQFKDLVPGRFYQVTIRCVSG 364
Cdd:smart00060    1 PSPPSNLRVTDVTS-TSVTLSWEPPpddgiTGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79
fn3 pfam00041
Fibronectin type III domain;
645-723 1.14e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 45.48  E-value: 1.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  645 SSVSGVTVNNSGrNDYLSVSWLPAP---GEVHHYVVTLSH--DSKVVQSLITAKFVSECSFSSLTPGRLYNVTITTKSGN 719
Cdd:pfam00041    1 SAPSNLTVTDVT-STSLTVSWTPPPdgnGPITGYEVEYRPknSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ....
gi 1725351434  720 YESH 723
Cdd:pfam00041   80 GEGP 83
fn3 pfam00041
Fibronectin type III domain;
205-273 3.10e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 44.33  E-value: 3.10e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1725351434  205 SPVEDIGISP-NPNSLLISWSR---GPGNVEQFRLML--MDKGAIVQDTNVDKRDTSYAFRGLTPGHLYNVTIVT 273
Cdd:pfam00041    1 SAPSNLTVTDvTSTSLTVSWTPppdGNGPITGYEVEYrpKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQA 75
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 732-818 1.46e-04

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 42.48  E-value: 1.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  732 PDKVQGISVSNSaRSDYLKVSWVHATGD---FDHYEVTIK--NRDSFIQTKSIPKSENECVFARLVPGRLYSITVT--TK 804
Cdd:cd00063      1 PSPPTNLRVTDV-TSTSVTLSWTPPEDDggpITGYVVEYRekGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRavNG 79

                           90
                   ....*....|....
gi 1725351434  805 SGQYEASEQGTGRT 818
Cdd:cd00063     80 GGESPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 468-553 2.79e-04

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 41.71  E-value: 2.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  468 PLAVLQLRIKQANETSLGITWRAPL---GEWEKYTISL--MDRELFVIHKSLSKDAKEYTFTNLMPGRNYKATVTSMSGD 542
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYreKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                           90
                   ....*....|...
gi 1725351434  543 L--KQSASIQGRT 553
Cdd:cd00063     81 GesPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 644-731 2.96e-04

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 41.71  E-value: 2.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  644 PSSVSGVTVNNSGRnDYLSVSWLPAP---GEVHHYVVTLSHDSKVVQSLITAKFVSECSF--SSLTPGRLYNVTITTKSG 718
Cdd:cd00063      1 PSPPTNLRVTDVTS-TSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYtlTGLKPGTEYEFRVRAVNG 79

                           90
                   ....*....|...
gi 1725351434  719 NYEShSFSEERTV 731
Cdd:cd00063     80 GGES-PPSESVTV 91
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 204-272 3.17e-04

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 41.71  E-value: 3.17e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1725351434  204 PSPVEDIGISP-NPNSLLISWSRGP---GNVEQFRLMLMDKGA--IVQDTNVDKRDTSYAFRGLTPGHLYNVTIV 272
Cdd:cd00063      1 PSPPTNLRVTDvTSTSVTLSWTPPEddgGPITGYVVEYREKGSgdWKEVEVTPGSETSYTLTGLKPGTEYEFRVR 75
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 908-982 3.86e-04

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 41.06  E-value: 3.86e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434   908 PSTVKNIHISANGATdRLTVTWSP-----GGGDVDSYVVSAFRQDEKVESHTLPKHGSEHTFHRLEAGATYRIAIVSVSG 982
Cdd:smart00060    1 PSPPSNLRVTDVTST-SVTLSWEPppddgITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 468-541 5.50e-04

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 40.68  E-value: 5.50e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1725351434   468 PLAVLQLRIKQANETSLGITWRAP-----LGEWEKYTISLMDRELFVIHKSLSKDAKEYTFTNLMPGRNYKATVTSMSG 541
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPpddgiTGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
1190-1340 6.57e-04

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 44.94  E-value: 6.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1190 SLWFSWSPASGDFDfYELILYNPNGtkkeNWR---EKDVTEWRFQGLIPGRkYTLYVVTHS--GDLSN-----KVTGEGR 1259
Cdd:COG4733    553 TLTVSWDAPAGAVA-YEVEWRRDDG----NWVsvpRTSGTSFEVPGIYAGD-YEVRVRAINalGVSSAwaassETTVTGK 626

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1260 TAPsPPSLLSF-ADVANTSLAITWKGPPDwTDYNDFELQWLP----GDALTVFNPYSSKKSegrIVNGLRPGRSYQFSVK 1334
Cdd:COG4733    627 TAP-PPAPTGLtATGGLGGITLSWSFPVD-ADTLRTEIRYSTtgdwASATVAQALYPGNTY---TLAGLKAGQTYYYRAR 701


                   ....*...
gi 1725351434 1335 TV--SGDS 1340
Cdd:COG4733    702 AVdrSGNV 709
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 644-722 1.30e-03

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 39.52  E-value: 1.30e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434   644 PSSVSGVTVNNSGRNdYLSVSWLPAP-----GEVHHYVVTLSHDSKVVQSLITAKFVSECSFSSLTPGRLYNVTITTKSG 718
Cdd:smart00060    1 PSPPSNLRVTDVTST-SVTLSWEPPPddgitGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79


                    ....
gi 1725351434   719 NYES 722
Cdd:smart00060   80 AGEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1174-1266 2.77e-03

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 39.02  E-value: 2.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1174 PAAVNHLKGSNRNmTDSLWFSWSPASGD---FDFYELILYNPNGTKKENWREKDV--TEWRFQGLIPGRKYTLYVVThsg 1248
Cdd:cd00063      1 PSPPTNLRVTDVT-STSVTLSWTPPEDDggpITGYVVEYREKGSGDWKEVEVTPGseTSYTLTGLKPGTEYEFRVRA--- 76

                           90
                   ....*....|....*...
gi 1725351434 1249 dlsnkVTGEGRTAPSPPS 1266
Cdd:cd00063     77 -----VNGGGESPPSESV 89
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 732-807 5.08e-03

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 37.98  E-value: 5.08e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434   732 PDKVQGISVSNSArSDYLKVSWVH-----ATGDFDHYEVTIKNRDSFIQTKSIPKSENECVFARLVPGRLYSITVTTKSG 806
Cdd:smart00060    1 PSPPSNLRVTDVT-STSVTLSWEPppddgITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79


                    .
gi 1725351434   807 Q 807
Cdd:smart00060   80 A 80
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 820-895 8.01e-03

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 37.48  E-value: 8.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  820 PEPVKNLTLLNRSTEDLHVTWSRA---NGDVDQYEVQL---LFNDMKVFPPiyLVNTATEYQFSALTPGRHYKILVLTIS 893
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPeddGGPITGYVVEYrekGSGDWKEVEV--TPGSETSYTLTGLKPGTEYEFRVRAVN 78


                   ..
gi 1725351434  894 GD 895
Cdd:cd00063     79 GG 80
 
Name Accession Description Interval E-value
R-PTPc-B cd14617
catalytic domain of receptor-type tyrosine-protein phosphatase B; Receptor-type ...
 1734-1961 7.38e-177

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: 535.27  E-value: 7.38e-177
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1734 NRYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRV 1813
Cdd:cd14617      1 NRYNNILPYDSTRVKLSNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMVWEQNVHNIVMVTQCVEKGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1814 KCDHYWPADQDPLYYGDLILQMVSESVLPEWTIREFKICSEEQLDAHRLLRHFHYTVWPDHGVPETTQSLIQFVRTVRDY 1893
Cdd:cd14617     81 KCDHYWPADQDSLYYGDLIVQMLSESVLPEWTIREFKICSEEQLDAPRLVRHFHYTVWPDHGVPETTQSLIQFVRTVRDY 160

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1725351434 1894 INRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 1961
Cdd:cd14617    161 INRTPGSGPTVVHCSAGVGRTGTFIALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 228
R3-PTPc cd14548
catalytic domain of R3 subfamily receptor-type tyrosine-protein phosphatases and similar ...
 1735-1961 6.94e-142

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: 439.10  E-value: 6.94e-142
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1735 RYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVK 1814
Cdd:cd14548      1 RYTNILPYDHSRVKLIPINEEEGSDYINANYIPGYNSPREFIATQGPLPGTKDDFWRMVWEQNSHTIVMLTQCMEKGRVK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1815 CDHYWPADQDPLYYGDLILQMVSESVLPEWTIREFKICseeQLDAHRLLRHFHYTVWPDHGVPETTQSLIQFVRTVRDYI 1894
Cdd:cd14548     81 CDHYWPFDQDPVYYGDITVTMLSESVLPDWTIREFKLE---RGDEVRSVRQFHFTAWPDHGVPEAPDSLLRFVRLVRDYI 157

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1725351434 1895 NRspGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 1961
Cdd:cd14548    158 KQ--EKGPTIVHCSAGVGRTGTFIALDRLLQQIESEDYVDIFGIVYDLRKHRPLMVQTEAQYIFLHQ 222
PTPc smart00194
Protein tyrosine phosphatase, catalytic domain;
1705-1963 5.51e-115

Protein tyrosine phosphatase, catalytic domain;


Pssm-ID: 214550 [Multi-domain]  Cd Length: 259  Bit Score: 365.06  E-value: 5.51e-115
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  1705 LLSKEYEDLKDVGRS-QSCDIALLPENRGKNRYNNILPYDASRVKLcNVDDDPCSDYINASYIPGNNFRREYIATQGPLP 1783
Cdd:smart00194    1 GLEEEFEKLDRLKPDdESCTVAAFPENRDKNRYKDVLPYDHTRVKL-KPPPGEGSDYINASYIDGPNGPKAYIATQGPLP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  1784 GTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQ-DPLYYGDLILQMVSESVLPEWTIREFKICSEEQlDAHRL 1862
Cdd:smart00194   80 STVEDFWRMVWEQKVTVIVMLTELVEKGREKCAQYWPDEEgEPLTYGDITVTLKSVEKVDDYTIRTLEVTNTGC-SETRT 158

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  1863 LRHFHYTVWPDHGVPETTQSLIQFVRTVRDYinRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDL 1942
Cdd:smart00194  159 VTHYHYTNWPDHGVPESPESILDLIRAVRKS--QSTSTGPIVVHCSAGVGRTGTFIAIDILLQQLEAGKEVDIFEIVKEL 236

                           250       260
                    ....*....|....*....|.
gi 1725351434  1943 RLHRVHMVQTECQYVYLHQCV 1963
Cdd:smart00194  237 RSQRPGMVQTEEQYIFLYRAI 257
R-PTPc-J cd14615
catalytic domain of receptor-type tyrosine-protein phosphatase J; Receptor-type ...
 1734-1965 2.72e-112

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: 356.05  E-value: 2.72e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1734 NRYNNILPYDASRVKLCNvDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRV 1813
Cdd:cd14615      1 NRYNNVLPYDISRVKLSV-QSHSTDDYINANYMPGYNSKKEFIAAQGPLPNTVKDFWRMVWEKNVYAIVMLTKCVEQGRT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1814 KCDHYWPADQdPLYYGDLILQMVSESVLPEWTIREFKIcSEEQLDAHRLLRHFHYTVWPDHGVPETTQSLIQFVRTVRDY 1893
Cdd:cd14615     80 KCEEYWPSKQ-KKDYGDITVTMTSEIVLPEWTIRDFTV-KNAQTNESRTVRHFHFTSWPDHGVPETTDLLINFRHLVREY 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1725351434 1894 INRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRD 1965
Cdd:cd14615    158 MKQNPPNSPILVHCSAGVGRTGTFIAIDRLIYQIENENVVDVYGIVYDLRMHRPLMVQTEDQYVFLNQCALD 229
R-PTPc-O cd14614
catalytic domain of receptor-type tyrosine-protein phosphatase O; Receptor-type ...
 1723-1964 1.62e-105

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: 337.25  E-value: 1.62e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1723 DIALLPENRGKNRYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIV 1802
Cdd:cd14614      5 FAADLPVNRCKNRYTNILPYDFSRVKLVSMHEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIV 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1803 MVTQCVEKGRVKCDHYWPADQDPLYYGDLILQMVSESVLPEWTIREFKIcseEQLDAHRLLRHFHYTVWPDHGVP--ETT 1880
Cdd:cd14614     85 MLTQCNEKRRVKCDHYWPFTEEPVAYGDITVEMLSEEEQPDWAIREFRV---SYADEVQDVMHFNYTAWPDHGVPtaNAA 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1881 QSLIQFVRTVRDYINRSPgaGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 1960
Cdd:cd14614    162 ESILQFVQMVRQQAVKSK--GPMIIHCSAGVGRTGTFIALDRLLQHIRDHEFVDILGLVSEMRSYRMSMVQTEEQYIFIH 239


                   ....
gi 1725351434 1961 QCVR 1964
Cdd:cd14614    240 QCVQ 243
R-PTPc-H cd14619
catalytic domain of receptor-type tyrosine-protein phosphatase H; Receptor-type ...
 1734-1967 8.48e-101

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: 323.38  E-value: 8.48e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1734 NRYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRV 1813
Cdd:cd14619      1 NRFRNVLPYDWSRVPLKPIHEEPGSDYINANYMPGYWSSQEFIATQGPLPQTVGDFWRMIWEQQSSTIVMLTNCMEAGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1814 KCDHYWPADQDPLYYGDLILQMVSESVLPEWTIREFKICSEEQlDAHRLLRHFHYTVWPDHGVPETTQSLIQFVRTVRDY 1893
Cdd:cd14619     81 KCEHYWPLDYTPCTYGHLRVTVVSEEVMENWTVREFLLKQVEE-QKTLSVRHFHFTAWPDHGVPSSTDTLLAFRRLLRQW 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1725351434 1894 INRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRDVL 1967
Cdd:cd14619    160 LDQTMSGGPTVVHCSAGVGRTGTLIALDVLLQQLQSEGLLGPFSFVQKMRENRPLMVQTESQYVFLHQCILDFL 233
Y_phosphatase pfam00102
Protein-tyrosine phosphatase;
1730-1963 2.68e-100

Protein-tyrosine phosphatase;


Pssm-ID: 459674 [Multi-domain]  Cd Length: 234  Bit Score: 321.88  E-value: 2.68e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1730 NRGKNRYNNILPYDASRVKLcnVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVE 1809
Cdd:pfam00102    1 NLEKNRYKDVLPYDHTRVKL--TGDPGPSDYINASYIDGYKKPKKYIATQGPLPNTVEDFWRMVWEEKVTIIVMLTELEE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1810 KGRVKCDHYWP-ADQDPLYYGDLILQMVSE-SVLPEWTIREFKIcSEEQLDAHRLLRHFHYTVWPDHGVPETTQSLIQFV 1887
Cdd:pfam00102   79 KGREKCAQYWPeEEGESLEYGDFTVTLKKEkEDEKDYTVRTLEV-SNGGSEETRTVKHFHYTGWPDHGVPESPNSLLDLL 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1725351434 1888 RTVRDYiNRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 1963
Cdd:pfam00102  158 RKVRKS-SLDGRSGPIVVHCSAGIGRTGTFIAIDIALQQLEAEGEVDIFQIVKELRSQRPGMVQTLEQYIFLYDAI 232
R-PTPc-V cd14618
catalytic domain of receptor-type tyrosine-protein phosphatase V; Receptor-type ...
 1734-1963 1.34e-96

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: 311.11  E-value: 1.34e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1734 NRYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRV 1813
Cdd:cd14618      1 NRYPHVLPYDHSRVRLSQLGGEPHSDYINANFIPGYTSPQEFIATQGPLKKTIEDFWRLVWEQQVCNIIMLTVGMENGRV 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1814 KCDHYWPADQDPLYYGDLILQMVSESVLPEWTIREFKIcSEEQLDAHRLLRHFHYTVWPDHGVPETTQSLIQFVRTVRDY 1893
Cdd:cd14618     81 LCDHYWPSESTPVSYGHITVHLLAQSSEDEWTRREFKL-WHEDLRKERRVKHLHYTAWPDHGIPESTSSLMAFRELVREH 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1894 INRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 1963
Cdd:cd14618    160 VQATKGKGPTLVHCSAGVGRSGTFIALDRLLRQLKEEKVVDVFNTVYILRMHRYLMIQTLSQYIFLHSCI 229
R-PTPc-LAR-1 cd14553
catalytic domain of LAR family receptor-type tyrosine-protein phosphatases, repeat 1; The LAR ...
 1730-1963 1.94e-88

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: 288.14  E-value: 1.94e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1730 NRGKNRYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVE 1809
Cdd:cd14553      3 NKPKNRYANVIAYDHSRVILQPIEGVPGSDYINANYCDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTKLEE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1810 KGRVKCDHYWPADqDPLYYGDLILQMVSESVLPEWTIREFKICSEEQLDaHRLLRHFHYTVWPDHGVPETTQSLIQFVRT 1889
Cdd:cd14553     83 RSRVKCDQYWPTR-GTETYGLIQVTLLDTVELATYTVRTFALHKNGSSE-KREVRQFQFTAWPDHGVPEHPTPFLAFLRR 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1725351434 1890 VRDYinRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 1963
Cdd:cd14553    161 VKAC--NPPDAGPIVVHCSAGVGRTGCFIVIDSMLERIKHEKTVDIYGHVTCLRAQRNYMVQTEDQYIFIHDAL 232
PTPc cd00047
catalytic domain of protein tyrosine phosphatases; Protein tyrosine phosphatases (PTP, EC 3.1. ...
 1760-1961 3.97e-88

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: 285.72  E-value: 3.97e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1760 YINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQD-PLYYGDLILQMVSE 1838
Cdd:cd00047      1 YINASYIDGYRGPKEYIATQGPLPNTVEDFWRMVWEQKVSVIVMLTNLVEKGREKCERYWPEEGGkPLEYGDITVTLVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1839 SVLPEWTIREFKIcSEEQLDAHRLLRHFHYTVWPDHGVPETTQSLIQFVRTVRDYinRSPGAGPTVVHCSAGVGRTGTFV 1918
Cdd:cd00047     81 EELSDYTIRTLEL-SPKGCSESREVTHLHYTGWPDHGVPSSPEDLLALVRRVRKE--ARKPNGPIVVHCSAGVGRTGTFI 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1725351434 1919 ALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 1961
Cdd:cd00047    158 AIDILLERLEAEGEVDVFEIVKALRKQRPGMVQTLEQYEFIYE 200
PTPc-N9 cd14543
catalytic domain of tyrosine-protein phosphatase non-receptor type 9; Tyrosine-protein ...
 1708-1960 7.95e-83

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: 273.47  E-value: 7.95e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1708 KEYEDLKDVGRSQSCDIALLPENRGKNRYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKD 1787
Cdd:cd14543      7 EEYEDIRREPPAGTFLCSLAPANQEKNRYGDVLCLDQSRVKLPKRNGDERTDYINANFMDGYKQKNAYIATQGPLPKTYS 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1788 DFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDP-LYYGDLILQMVSESVLPEWTIREFKICSEEQlDAHRLLRHF 1866
Cdd:cd14543     87 DFWRMVWEQKVLVIVMTTRVVERGRVKCGQYWPLEEGSsLRYGDLTVTNLSVENKEHYKKTTLEIHNTET-DESRQVTHF 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1867 HYTVWPDHGVPETTQSLIQFVRTVRDYINRS-----------PGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDI 1935
Cdd:cd14543    166 QFTSWPDFGVPSSAAALLDFLGEVRQQQALAvkamgdrwkghPPGPPIVVHCSAGIGRTGTFCTLDICLSQLEDVGTLNV 245

                          250       260
                   ....*....|....*....|....*
gi 1725351434 1936 YGAVHDLRLHRVHMVQTECQYVYLH 1960
Cdd:cd14543    246 MQTVRRMRTQRAFSIQTPDQYYFCY 270
R-PTPc-Q cd14616
catalytic domain of receptor-type tyrosine-protein phosphatase Q; Receptor-type ...
 1734-1961 8.14e-83

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: 271.39  E-value: 8.14e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1734 NRYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRV 1813
Cdd:cd14616      1 NRFPNIKPYNNNRVKLIADAGVPGSDYINASYISGYLCPNEFIATQGPLPGTVGDFWRMVWETRAKTIVMLTQCFEKGRI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1814 KCDHYWPADQDPL-YYGDLILQMVSESVLPEWTIREFKIcseEQLDAHRLLRHFHYTVWPDHGVPETTQSLIQFVRTVRd 1892
Cdd:cd14616     81 RCHQYWPEDNKPVtVFGDIVITKLMEDVQIDWTIRDLKI---ERHGDYMMVRQCNFTSWPEHGVPESSAPLIHFVKLVR- 156

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1725351434 1893 yINRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 1961
Cdd:cd14616    157 -ASRAHDNTPMIVHCSAGVGRTGVFIALDHLTQHINDHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQ 224
R5-PTPc-1 cd14549
catalytic domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The R5 ...
 1760-1960 1.31e-81

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: 267.29  E-value: 1.31e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1760 YINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDPlYYGDLILQMVSES 1839
Cdd:cd14549      1 YINANYVDGYNKARAYIATQGPLPSTFDDFWRMVWEQNSAIIVMITNLVERGRRKCDQYWPKEGTE-TYGNIQVTLLSTE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1840 VLPEWTIREF-----KICSEEQLDAHRLLRHFHYTVWPDHGVPETTQSLIQFVRTVRDYinRSPGAGPTVVHCSAGVGRT 1914
Cdd:cd14549     80 VLATYTVRTFslknlKLKKVKGRSSERVVYQYHYTQWPDHGVPDYTLPVLSFVRKSSAA--NPPGAGPIVVHCSAGVGRT 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1725351434 1915 GTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 1960
Cdd:cd14549    158 GTYIVIDSMLQQIQDKGTVNVFGFLKHIRTQRNYLVQTEEQYIFIH 203
R-PTPc-F-1 cd14626
catalytic domain of receptor-type tyrosine-protein phosphatase F, repeat 1; Receptor-type ...
 1694-1963 8.07e-75

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


Pssm-ID: 350474 [Multi-domain]  Cd Length: 276  Bit Score: 250.72  E-value: 8.07e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1694 HFMKLQADSNYLLSKEYEDLkDVGRSQSCDIALLPENRGKNRYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRR 1773
Cdd:cd14626      6 NIERLKANDGLKFSQEYESI-DPGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSVDGVPGSDYINANYIDGYRKQN 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1774 EYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPAdQDPLYYGDLILQMVSESVLPEWTIREF---K 1850
Cdd:cd14626     85 AYIATQGPLPETLSDFWRMVWEQRTATIVMMTRLEEKSRVKCDQYWPI-RGTETYGMIQVTLLDTVELATYSVRTFalyK 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1851 ICSEEQldahRLLRHFHYTVWPDHGVPETTQSLIQFVRTVRdyINRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSK 1930
Cdd:cd14626    164 NGSSEK----REVRQFQFMAWPDHGVPEYPTPILAFLRRVK--ACNPPDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHE 237

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1725351434 1931 DSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 1963
Cdd:cd14626    238 KTVDIYGHVTCMRSQRNYMVQTEDQYIFIHEAL 270
R-PTPc-T-1 cd14630
catalytic domain of receptor-type tyrosine-protein phosphatase T, repeat 1; Receptor-type ...
 1729-1963 1.01e-74

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: 248.79  E-value: 1.01e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1729 ENRGKNRYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCV 1808
Cdd:cd14630      2 ENRNKNRYGNIISYDHSRVRLQLLDGDPHSDYINANYIDGYHRPRHYIATQGPMQETVKDFWRMIWQENSASVVMVTNLV 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1809 EKGRVKCDHYWPADQDplYYGDLILQMVSESVLPEWTIREFKICSEEQLDAhRLLRHFHYTVWPDHGVPETTQSLIQFVR 1888
Cdd:cd14630     82 EVGRVKCVRYWPDDTE--VYGDIKVTLIETEPLAEYVIRTFTVQKKGYHEI-REIRQFHFTSWPDHGVPCYATGLLGFVR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1725351434 1889 TVRdYINrSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 1963
Cdd:cd14630    159 QVK-FLN-PPDAGPIVVHCSAGAGRTGCFIAIDIMLDMAENEGVVDIFNCVRELRAQRVNMVQTEEQYVFVHDAI 231
R-PTPc-G-1 cd17667
catalytic domain of receptor-type tyrosine-protein phosphatase G, repeat 1; Receptor-type ...
 1728-1967 9.12e-74

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: 247.64  E-value: 9.12e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1728 PENRGKNRYNNILPYDASRVKLCNV--DDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVT 1805
Cdd:cd17667     25 PDNKHKNRYINILAYDHSRVKLRPLpgKDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIVMIT 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1806 QCVEKGRVKCDHYWPADQDPlYYGDLILQMVSESVLPEWTIREFKICSEEQLDAH----------RLLRHFHYTVWPDHG 1875
Cdd:cd17667    105 NLVEKGRRKCDQYWPTENSE-EYGNIIVTLKSTKIHACYTVRRFSIRNTKVKKGQkgnpkgrqneRTVIQYHYTQWPDMG 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1876 VPETTQSLIQFVRtvRDYINRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQ 1955
Cdd:cd17667    184 VPEYALPVLTFVR--RSSAARTPEMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQ 261

                          250
                   ....*....|..
gi 1725351434 1956 YVYLHQCVRDVL 1967
Cdd:cd17667    262 YIFIHDALLEAI 273
PTPc-KIM cd14547
catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; ...
 1734-1961 2.64e-73

catalytic domain of the kinase interaction motif (KIM) family of protein-tyrosine phosphatases; The kinase interaction motif (KIM) family of protein-tyrosine phosphatases (PTPs) includes tyrosine-protein phosphatases non-receptor type 7 (PTPN7) and non-receptor type 5 (PTPN5), and protein-tyrosine phosphatase receptor type R (PTPRR). PTPN7 is also called hematopoietic protein-tyrosine phosphatase (HePTP) while PTPN5 is also called striatal-enriched protein-tyrosine phosphatase (STEP). They belong to the family of classical tyrosine-specific PTPs (EC 3.1.3.48) that catalyze the dephosphorylation of phosphotyrosine peptides. KIM-PTPs are characterized by the presence of a 16-amino-acid KIM that binds specifically to members of the MAPK (mitogen-activated protein kinase) family. They are highly specific to the MAPKs ERK1/2 (extracellular-signal-regulated kinase 1/2) and p38, over JNK (c-Jun N-terminal kinase); they dephosphorylate these kinases and thereby critically modulate cell proliferation and differentiation.


Pssm-ID: 350395 [Multi-domain]  Cd Length: 224  Bit Score: 244.23  E-value: 2.64e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1734 NRYNNILPYDASRVKLCNVDDDPCSDYINASYIPG-NNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKgR 1812
Cdd:cd14547      1 NRYKTILPNEHSRVCLPSVDDDPLSSYINANYIRGyDGEEKAYIATQGPLPNTVADFWRMVWQEKTPIIVMITNLTEA-K 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1813 VKCDHYWPADQdPLYYGDLILQMVSESVLPEWTIREFKICSEEQldaHRLLRHFHYTVWPDHGVPETTQSLIQFVRTVRD 1892
Cdd:cd14547     80 EKCAQYWPEEE-NETYGDFEVTVQSVKETDGYTVRKLTLKYGGE---KRYLKHYWYTSWPDHKTPEAAQPLLSLVQEVEE 155

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1725351434 1893 YINRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 1961
Cdd:cd14547    156 ARQTEPHRGPIVVHCSAGIGRTGCFIATSIGCQQLREEGVVDVLGIVCQLRLDRGGMVQTAEQYEFVHR 224
R-PTPc-A-1 cd14621
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 1; Receptor-type ...
 1679-1963 1.04e-71

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: 242.62  E-value: 1.04e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1679 NRKTScPIKINQFEGHFMKLQADSNYLLSKEYEDLKDVGRSQSCDIALLPENRGKNRYNNILPYDASRVKLCNVDDDPCS 1758
Cdd:cd14621      2 NRKYP-PLPVDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1759 DYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPaDQDPLYYGDLILQMVSE 1838
Cdd:cd14621     81 DYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWP-DQGCWTYGNIRVSVEDV 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1839 SVLPEWTIREFkiCSEEQLDA-----HRLLRHFHYTVWPDHGVPETTQSLIQFVRTVRdyiNRSPG-AGPTVVHCSAGVG 1912
Cdd:cd14621    160 TVLVDYTVRKF--CIQQVGDVtnkkpQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVK---NCNPQyAGAIVVHCSAGVG 234

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1725351434 1913 RTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 1963
Cdd:cd14621    235 RTGTFIVIDAMLDMMHAERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQAL 285
PTPc-N11_6 cd14544
catalytic domain of tyrosine-protein phosphatase non-receptor type 11 and type 6; ...
 1730-1963 2.67e-71

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: 239.67  E-value: 2.67e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1730 NRGKNRYNNILPYDASRVKLCNVDDD-PCSDYINASYI-PGNNFRRE------YIATQGPLPGTKDDFWKMAWEQNVHNI 1801
Cdd:cd14544      1 NKGKNRYKNILPFDHTRVILKDRDPNvPGSDYINANYIrNENEGPTTdenaktYIATQGCLENTVSDFWSMVWQENSRVI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1802 VMVTQCVEKGRVKCDHYWPADQDPLYYGDLILQMVSESVLPEWTIREFKICSEEQLDAHRLLRHFHYTVWPDHGVPETTQ 1881
Cdd:cd14544     81 VMTTKEVERGKNKCVRYWPDEGMQKQYGPYRVQNVSEHDTTDYTLRELQVSKLDQGDPIREIWHYQYLSWPDHGVPSDPG 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1882 SLIQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKD---SVDIYGAVHDLRLHRVHMVQTECQYVY 1958
Cdd:cd14544    161 GVLNFLEDVNQRQESLPHAGPIVVHCSAGIGRTGTFIVIDMLLDQIKRKGldcDIDIQKTIQMVRSQRSGMVQTEAQYKF 240


                   ....*
gi 1725351434 1959 LHQCV 1963
Cdd:cd14544    241 IYVAV 245
R-PTPc-M-1 cd14633
catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type ...
 1694-1963 6.97e-71

catalytic domain of receptor-type tyrosine-protein phosphatase M, repeat 1; Receptor-type tyrosine-protein phosphatase M (PTPRM), also known as protein-tyrosine phosphatase mu (R-PTP-mu or PTPmu), belongs to the type IIb subfamily of receptor protein tyrosine phosphatases (RPTPs), which belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRM/PTPmu is a homophilic cell adhesion molecule expressed in CNS neurons and glia. It is required for E-, N-, and R-cadherin-dependent neurite outgrowth. Loss of PTPmu contributes to tumor cell migration and dispersal of human glioblastomas. PTPRM contains an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350481 [Multi-domain]  Cd Length: 273  Bit Score: 239.17  E-value: 6.97e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1694 HFMKLQADSNYLLSKEYEDLKDvGRSQSCDIALLPENRGKNRYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRR 1773
Cdd:cd14633      5 HITQMKCAEGYGFKEEYESFFE-GQSAPWDSAKKDENRMKNRYGNIIAYDHSRVRLQPIEGETSSDYINGNYIDGYHRPN 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1774 EYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDplYYGDLILQMVSESVLPEWTIREFKIcs 1853
Cdd:cd14633     84 HYIATQGPMQETIYDFWRMVWHENTASIIMVTNLVEVGRVKCCKYWPDDTE--IYKDIKVTLIETELLAEYVIRTFAV-- 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1854 eEQLDAH--RLLRHFHYTVWPDHGVPETTQSLIQFVRTVRDyiNRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKD 1931
Cdd:cd14633    160 -EKRGVHeiREIRQFHFTGWPDHGVPYHATGLLGFVRQVKS--KSPPNAGPLVVHCSAGAGRTGCFIVIDIMLDMAEREG 236

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1725351434 1932 SVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 1963
Cdd:cd14633    237 VVDIYNCVRELRSRRVNMVQTEEQYVFIHDAI 268
R-PTP-LAR-2 cd14554
PTP-like domain of the LAR family receptor-type tyrosine-protein phosphatases, repeat 2; The ...
 1725-1961 7.16e-70

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: 234.73  E-value: 7.16e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1725 ALLPENRGKNRYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMV 1804
Cdd:cd14554      1 ANLPCNKFKNRLVNILPYESTRVCLQPIRGVEGSDYINASFIDGYRQRGAYIATQGPLAETTEDFWRMLWEHNSTIIVML 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1805 TQCVEKGRVKCDHYWPADQDpLYYGDLILQMVSESVLPEWTIREFKIcSEEQLDAHRLLRHFHYTVWPDHGVPETTQSLI 1884
Cdd:cd14554     81 TKLREMGREKCHQYWPAERS-ARYQYFVVDPMAEYNMPQYILREFKV-TDARDGQSRTVRQFQFTDWPEQGVPKSGEGFI 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1725351434 1885 QFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 1961
Cdd:cd14554    159 DFIGQVHKTKEQFGQEGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDVFQTVKLLRTQRPAMVQTEDQYQFCYR 235
PTP_fungal cd18533
fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae ...
 1760-1961 3.76e-69

fungal protein tyrosine phosphatases; This subfamily contains Saccharomyces cerevisiae protein-tyrosine phosphatases 1 (PTP1) and 2 (PTP2), Schizosaccharomyces pombe PTP1, PTP2, and PTP3, and similar fungal proteins. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides; they regulate phosphotyrosine levels in signal transduction pathways. PTP2, together with PTP3, is the major phosphatase that dephosphorylates and inactivates the MAP kinase HOG1 and also modulates its subcellular localization.


Pssm-ID: 350509 [Multi-domain]  Cd Length: 212  Bit Score: 231.75  E-value: 3.76e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1760 YINASYI-PGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDPLYYGDLILQMVSE 1838
Cdd:cd18533      1 YINASYItLPGTSSKRYIATQGPLPATIGDFWKMIWQNNVGVIVMLTPLVENGREKCDQYWPSGEYEGEYGDLTVELVSE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1839 SVLPEW--TIREFKICSEEQldAHRLLRHFHYTVWPDHGVPETTQSLIQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGT 1916
Cdd:cd18533     81 EENDDGgfIVREFELSKEDG--KVKKVYHIQYKSWPDFGVPDSPEDLLTLIKLKRELNDSASLDPPIIVHCSAGVGRTGT 158

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1725351434 1917 FVALDRILQQLDS--------KDSVD-IYGAVHDLRLHRVHMVQTECQYVYLHQ 1961
Cdd:cd18533    159 FIALDSLLDELKRglsdsqdlEDSEDpVYEIVNQLRKQRMSMVQTLRQYIFLYD 212
R-PTPc-D-1 cd14624
catalytic domain of receptor-type tyrosine-protein phosphatase D, repeat 1; Receptor-type ...
 1685-1963 7.80e-69

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: 233.86  E-value: 7.80e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1685 PIKINQFEGHFMKLQADSNYLLSKEYEDLkDVGRSQSCDIALLPENRGKNRYNNILPYDASRVKLCNVDDDPCSDYINAS 1764
Cdd:cd14624      3 PIPILELADHIERLKANDNLKFSQEYESI-DPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVLLSAIEGIPGSDYINAN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1765 YIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPAdQDPLYYGDLILQMVSESVLPEW 1844
Cdd:cd14624     82 YIDGYRKQNAYIATQGALPETFGDFWRMIWEQRSATVVMMTKLEERSRVKCDQYWPS-RGTETYGLIQVTLLDTVELATY 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1845 TIREFKICSEEQLDaHRLLRHFHYTVWPDHGVPETTQSLIQFVRTVRdyINRSPGAGPTVVHCSAGVGRTGTFVALDRIL 1924
Cdd:cd14624    161 CVRTFALYKNGSSE-KREVRQFQFTAWPDHGVPEHPTPFLAFLRRVK--TCNPPDAGPMVVHCSAGVGRTGCFIVIDAML 237

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1725351434 1925 QQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 1963
Cdd:cd14624    238 ERIKHEKTVDIYGHVTLMRAQRNYMVQTEDQYIFIHDAL 276
R-PTPc-S-1 cd14625
catalytic domain of receptor-type tyrosine-protein phosphatase S, repeat 1; Receptor-type ...
 1685-1963 8.60e-69

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: 233.45  E-value: 8.60e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1685 PIKINQFEGHFMKLQADSNYLLSKEYEDLkDVGRSQSCDIALLPENRGKNRYNNILPYDASRVKLCNVDDDPCSDYINAS 1764
Cdd:cd14625      3 PIPISELAEHTERLKANDNLKLSQEYESI-DPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINAN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1765 YIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPaDQDPLYYGDLILQMVSESVLPEW 1844
Cdd:cd14625     82 YIDGYRKQNAYIATQGPLPETFGDFWRMVWEQRSATVVMMTKLEEKSRIKCDQYWP-SRGTETYGMIQVTLLDTIELATF 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1845 TIREFKIcSEEQLDAHRLLRHFHYTVWPDHGVPETTQSLIQFVRTVRdyINRSPGAGPTVVHCSAGVGRTGTFVALDRIL 1924
Cdd:cd14625    161 CVRTFSL-HKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVK--TCNPPDAGPIVVHCSAGVGRTGCFIVIDAML 237

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1725351434 1925 QQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 1963
Cdd:cd14625    238 ERIKHEKTVDIYGHVTLMRSQRNYMVQTEDQYSFIHDAL 276
PTPc-N1 cd14608
catalytic domain of tyrosine-protein phosphatase non-receptor type 1; Tyrosine-protein ...
 1710-1959 1.99e-66

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: 226.45  E-value: 1.99e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1710 YEDLKDVGRSQSCDIALLPENRGKNRYNNILPYDASRVKLcnvdDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDF 1789
Cdd:cd14608      5 YQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKL----HQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1790 WKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQD-PLYYGD--LILQMVSESVLPEWTIREFKIcseEQLDAH--RLLR 1864
Cdd:cd14608     81 WEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEkEMIFEDtnLKLTLISEDIKSYYTVRQLEL---ENLTTQetREIL 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1865 HFHYTVWPDHGVPETTQSLIQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSK---DSVDIYGAVHD 1941
Cdd:cd14608    158 HFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRkdpSSVDIKKVLLE 237

                          250       260
                   ....*....|....*....|
gi 1725351434 1942 LRLHRVHMVQT--ECQYVYL 1959
Cdd:cd14608    238 MRKFRMGLIQTadQLRFSYL 257
R-PTPc-E-1 cd14620
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 1; Receptor-type ...
 1736-1961 2.49e-65

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: 221.35  E-value: 2.49e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1736 YNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKC 1815
Cdd:cd14620      1 YPNILPYDHSRVILSQLDGIPCSDYINASYIDGYKEKNKFIAAQGPKQETVNDFWRMVWEQKSATIVMLTNLKERKEEKC 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1816 DHYWPaDQDPLYYGDLILQMVSESVLPEWTIREFkiCSEEQLD----AHRLLRHFHYTVWPDHGVPETTQSLIQFVRTVR 1891
Cdd:cd14620     81 YQYWP-DQGCWTYGNIRVAVEDCVVLVDYTIRKF--CIQPQLPdgckAPRLVTQLHFTSWPDFGVPFTPIGMLKFLKKVK 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1725351434 1892 dyiNRSPG-AGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 1961
Cdd:cd14620    158 ---SVNPVhAGPIVVHCSAGVGRTGTFIVIDAMIDMMHAEQKVDVFEFVSRIRNQRPQMVQTDMQYSFIYQ 225
PTPc-N6 cd14606
catalytic domain of tyrosine-protein phosphatase non-receptor type 6; Tyrosine-protein ...
 1728-1963 1.03e-64

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: 221.29  E-value: 1.03e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1728 PENRGKNRYNNILPYDASRVKLCNVDDD-PCSDYINASYI------PGNNFRReYIATQGPLPGTKDDFWKMAWEQNVHN 1800
Cdd:cd14606     16 PENKSKNRYKNILPFDHSRVILQGRDSNiPGSDYINANYVknqllgPDENAKT-YIASQGCLEATVNDFWQMAWQENSRV 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1801 IVMVTQCVEKGRVKCDHYWPADQDPLYYGDLILQMVSESVLPEWTIREFKICSEEQLDAHRLLRHFHYTVWPDHGVPETT 1880
Cdd:cd14606     95 IVMTTREVEKGRNKCVPYWPEVGMQRAYGPYSVTNCGEHDTTEYKLRTLQVSPLDNGELIREIWHYQYLSWPDHGVPSEP 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1881 QSLIQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSK--DS-VDIYGAVHDLRLHRVHMVQTECQYV 1957
Cdd:cd14606    175 GGVLSFLDQINQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMENISTKglDCdIDIQKTIQMVRAQRSGMVQTEAQYK 254


                   ....*.
gi 1725351434 1958 YLHQCV 1963
Cdd:cd14606    255 FIYVAI 260
R-PTPc-Z-1 cd17668
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 1; Receptor-type ...
 1760-1960 1.12e-64

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: 218.69  E-value: 1.12e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1760 YINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDPlYYGDLILQMVSES 1839
Cdd:cd17668      1 YINANYVDGYNKPKAYIAAQGPLKSTAEDFWRMIWEHNVEVIVMITNLVEKGRRKCDQYWPADGSE-EYGNFLVTQKSVQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1840 VLPEWTIREF-------KICSEEQLDAHRLLRHFHYTVWPDHGVPETTQSLIQFVRTVRDyiNRSPGAGPTVVHCSAGVG 1912
Cdd:cd17668     80 VLAYYTVRNFtlrntkiKKGSQKGRPSGRVVTQYHYTQWPDMGVPEYTLPVLTFVRKASY--AKRHAVGPVVVHCSAGVG 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1725351434 1913 RTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 1960
Cdd:cd17668    158 RTGTYIVLDSMLQQIQHEGTVNIFGFLKHIRSQRNYLVQTEEQYVFIH 205
PTPc-N20_13 cd14538
catalytic domain of tyrosine-protein phosphatase non-receptor type 20 and type 13; ...
 1760-1967 2.56e-64

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: 217.63  E-value: 2.56e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1760 YINASYI--PGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWP--ADQDPLYYGDLILQM 1835
Cdd:cd14538      1 YINASHIriPVGGDTYHYIACQGPLPNTTGDFWQMVWEQKSEVIAMVTQDVEGGKVKCHRYWPdsLNKPLICGGRLEVSL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1836 VSESVLPEWTIREFKIcSEEQLDAHRLLRHFHYTVWPDHGVPETTQSLIQFVRtvrdYINRSPGAGPTVVHCSAGVGRTG 1915
Cdd:cd14538     81 EKYQSLQDFVIRRISL-RDKETGEVHHITHLNFTTWPDHGTPQSADPLLRFIR----YMRRIHNSGPIVVHCSAGIGRTG 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1725351434 1916 TFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRDVL 1967
Cdd:cd14538    156 VLITIDVALGLIERDLPFDIQDIVKDLREQRQGMIQTKDQYIFCYKACLEVL 207
R-PTPc-C-1 cd14557
catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type ...
 1760-1961 4.24e-64

catalytic domain of receptor-type tyrosine-protein phosphatase C, repeat 1; Receptor-type tyrosine-protein phosphatase C (PTPRC), also known as CD45, leukocyte common antigen (LCA) or GP180, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPRC/CD45 is found in all nucleated hematopoietic cells and is an essential regulator of T- and B-cell antigen receptor signaling. It controls immune response, both positively and negatively, by dephosphorylating a number of signaling molecules such as the Src family kinases, the CD3zeta chain of TCY, and ZAP-70 kinase. Mutations in the human PTPRC/CD45 gene are associated with severe combined immunodeficiency (SCID) and multiple sclerosis. PTPRC/CD45 contains an extracellular receptor-like region with fibronectin type III (FN3) repeats, a short transmembrane segment, and a cytoplasmic region comprising of a membrane proximal catalytically active PTP domain (repeat 1 or D1) and a membrane distal catalytically impaired PTP-like domain (repeat 2, or D2). This model represents repeat 1.


Pssm-ID: 350405 [Multi-domain]  Cd Length: 201  Bit Score: 217.00  E-value: 4.24e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1760 YINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPA-DQDPLYYGDLILQMVSE 1838
Cdd:cd14557      1 YINASYIDGFKEPRKYIAAQGPKDETVDDFWRMIWEQKSTVIVMVTRCEEGNRNKCAQYWPSmEEGSRAFGDVVVKINEE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1839 SVLPEWTIREFKICSEEQLDAHRLLRHFHYTVWPDHGVPETTQSLIQFVRTVRDYINRspGAGPTVVHCSAGVGRTGTFV 1918
Cdd:cd14557     81 KICPDYIIRKLNINNKKEKGSGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFNNF--FSGPIVVHCSAGVGRTGTYI 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1725351434 1919 ALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 1961
Cdd:cd14557    159 GIDAMLEGLEAEGRVDVYGYVVKLRRQRCLMVQVEAQYILIHQ 201
R-PTPc-typeIIb-1 cd14555
catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, ...
 1760-1963 8.00e-64

catalytic domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat 1; The type II (or R2B) subfamily of receptor protein tyrosine phosphatases (RPTPs) include the prototypical member PTPmu (or PTPRM), PCP-2 (or PTPRU), PTPrho (or PTPRT), and PTPkappa (or PTPRK). They belong to the larger family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Type IIb RPTPs mediate cell-cell adhesion though homophilic interactions; their ligand is an identical molecule on an adjacent cell. No heterophilic interactions between the subfamily members have been observed. They also commonly function as tumor suppressors. They contain an extracellular region with an Meprin-A5 (neuropilin)-mu (MAM) domain, an immunoglobulin (Ig) domain, and four fibronectin type III (FN3) repeats, a transmembrane domain, and an intracellular segment with a juxtamembrane domain similar to the cytoplasmic domain of classical cadherins and two tandem PTP domains. This model represents the first (repeat 1) PTP domain.


Pssm-ID: 350403 [Multi-domain]  Cd Length: 204  Bit Score: 216.32  E-value: 8.00e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1760 YINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDplYYGDLILQMVSES 1839
Cdd:cd14555      1 YINANYIDGYHRPNHYIATQGPMQETVYDFWRMVWQENSASIVMVTNLVEVGRVKCSRYWPDDTE--VYGDIKVTLVETE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1840 VLPEWTIREFKIcSEEQLDAHRLLRHFHYTVWPDHGVPETTQSLIQFVRTVRdyINRSPGAGPTVVHCSAGVGRTGTFVA 1919
Cdd:cd14555     79 PLAEYVVRTFAL-ERRGYHEIREVRQFHFTGWPDHGVPYHATGLLGFIRRVK--ASNPPSAGPIVVHCSAGAGRTGCYIV 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1725351434 1920 LDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 1963
Cdd:cd14555    156 IDIMLDMAEREGVVDIYNCVKELRSRRVNMVQTEEQYIFIHDAI 199
PTPc-N18 cd14603
catalytic domain of tyrosine-protein phosphatase non-receptor type 18; Tyrosine-protein ...
 1728-1963 1.27e-63

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: 218.16  E-value: 1.27e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1728 PENRGKNRYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQC 1807
Cdd:cd14603     28 KENVKKNRYKDILPYDQTRVILSLLQEEGHSDYINANFIKGVDGSRAYIATQGPLSHTVLDFWRMIWQYGVKVILMACRE 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1808 VEKGRVKCDHYWPADQDPLYYGDLILQMVSESVL-PEWTIREFKI--CSEEqldahRLLRHFHYTVWPDHGVPETTQSLI 1884
Cdd:cd14603    108 IEMGKKKCERYWAQEQEPLQTGPFTITLVKEKRLnEEVILRTLKVtfQKES-----RSVSHFQYMAWPDHGIPDSPDCML 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1885 QFVRTVRDYINRSPgaGPTVVHCSAGVGRTGTFVALDRILQQLDSK---DSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 1961
Cdd:cd14603    183 AMIELARRLQGSGP--EPLCVHCSAGCGRTGVICTVDYVRQLLLTQripPDFSIFDVVLEMRKQRPAAVQTEEQYEFLYH 260


                   ..
gi 1725351434 1962 CV 1963
Cdd:cd14603    261 TV 262
PTPc-N7 cd14612
catalytic domain of tyrosine-protein phosphatase non-receptor type 7; Tyrosine-protein ...
 1727-1960 4.81e-63

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


Pssm-ID: 350460 [Multi-domain]  Cd Length: 247  Bit Score: 215.86  E-value: 4.81e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1727 LPENRGKNRYNNILPYDASRVKLCNV-DDDPCSDYINASYIPGNNFR-REYIATQGPLPGTKDDFWKMAWEQNVHNIVMV 1804
Cdd:cd14612     12 IPGHASKDRYKTILPNPQSRVCLRRAgSQEEEGSYINANYIRGYDGKeKAYIATQGPMLNTVSDFWEMVWQEECPIIVMI 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1805 TQCVEKgRVKCDHYWPADQDPlyYGDLILQMVSESVLPEWTIREFKICSEEqldAHRLLRHFHYTVWPDHGVPETTQSLI 1884
Cdd:cd14612     92 TKLKEK-KEKCVHYWPEKEGT--YGRFEIRVQDMKECDGYTIRDLTIQLEE---ESRSVKHYWFSSWPDHQTPESAGPLL 165

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1725351434 1885 QFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 1960
Cdd:cd14612    166 RLVAEVEESRQTAASPGPIVVHCSAGIGRTGCFIATSIGCQQLKDTGKVDILGIVCQLRLDRGGMIQTSEQYQFLH 241
PTPc-N1_2 cd14545
catalytic domain of tyrosine-protein phosphatase non-receptor type 1 and type 2; ...
 1733-1955 1.32e-62

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


Pssm-ID: 350393 [Multi-domain]  Cd Length: 231  Bit Score: 213.79  E-value: 1.32e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1733 KNRYNNILPYDASRVKLCNVDDDpcSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGR 1812
Cdd:cd14545      1 LNRYRDRDPYDHDRSRVKLKQGD--NDYINASLVEVEEAKRSYILTQGPLPNTSGHFWQMVWEQNSKAVIMLNKLMEKGQ 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1813 VKCDHYWPADQDPLY---YGDLILQMVSESVLPEWTIREFKIcseEQLDAH--RLLRHFHYTVWPDHGVPETTQSLIQFV 1887
Cdd:cd14545     79 IKCAQYWPQGEGNAMifeDTGLKVTLLSEEDKSYYTVRTLEL---ENLKTQetREVLHFHYTTWPDFGVPESPAAFLNFL 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1888 RTVRDYINRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKD--SVDIYGAVHDLRLHRVHMVQTECQ 1955
Cdd:cd14545    156 QKVRESGSLSSDVGPPVVHCSAGIGRSGTFCLVDTCLVLIEKGNpsSVDVKKVLLEMRKYRMGLIQTPDQ 225
R-PTPc-K-1 cd14631
catalytic domain of receptor-type tyrosine-protein phosphatase K, repeat 1; Receptor-type ...
 1746-1963 5.11e-62

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: 211.42  E-value: 5.11e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1746 RVKLCNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDp 1825
Cdd:cd14631      1 RVILQPVEDDPSSDYINANYIDGYQRPSHYIATQGPVHETVYDFWRMIWQEQSACIVMVTNLVEVGRVKCYKYWPDDTE- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1826 lYYGDLILQMVSESVLPEWTIREFKIcSEEQLDAHRLLRHFHYTVWPDHGVPETTQSLIQFVRTVRdyINRSPGAGPTVV 1905
Cdd:cd14631     80 -VYGDFKVTCVEMEPLAEYVVRTFTL-ERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVK--LSNPPSAGPIVV 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1725351434 1906 HCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 1963
Cdd:cd14631    156 HCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAI 213
PTPc-N2 cd14607
catalytic domain of tyrosine-protein phosphatase non-receptor type 2; Tyrosine-protein ...
 1710-1955 8.41e-62

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: 212.52  E-value: 8.41e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1710 YEDLKDVGRSQSCDIALLPENRGKNRYNNILPYDASRVKLCNVDDDpcsdYINASYIPGNNFRREYIATQGPLPGTKDDF 1789
Cdd:cd14607      4 YLEIRNESHDYPHRVAKYPENRNRNRYRDVSPYDHSRVKLQNTEND----YINASLVVIEEAQRSYILTQGPLPNTCCHF 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1790 WKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPA-DQDPLYYGD--LILQMVSESVLPEWTIREFKIcSEEQLDAHRLLRHF 1866
Cdd:cd14607     80 WLMVWQQKTKAVVMLNRIVEKDSVKCAQYWPTdEEEVLSFKEtgFSVKLLSEDVKSYYTVHLLQL-ENINSGETRTISHF 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1867 HYTVWPDHGVPETTQSLIQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKD--SVDIYGAVHDLRL 1944
Cdd:cd14607    159 HYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPAVVHCSAGIGRSGTFSLVDTCLVLMEKKDpdSVDIKQVLLDMRK 238

                          250
                   ....*....|.
gi 1725351434 1945 HRVHMVQTECQ 1955
Cdd:cd14607    239 YRMGLIQTPDQ 249
PTPc-N13 cd14597
catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein ...
 1729-1967 1.14e-60

catalytic domain of tyrosine-protein phosphatase non-receptor type 13; Tyrosine-protein phosphatase non-receptor type 13 (PTPN13, also known as PTPL1) belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Human PTPN13 is an important regulator of tumor aggressiveness. It regulates breast cancer cell aggressiveness through direct inactivation of Src kinase. In hepatocellular carcinoma, PTPN13 is a tumor suppressor. PTPN13 contains a FERM domain, five PDZ domains, and a C-terminal catalytic PTP domain. With its PDZ domains, PTPN13 has numerous interacting partners that can actively participate in the regulation of its phosphatase activity or can permit direct or indirect recruitment of tyrosine phosphorylated substrates. Its FERM domain is necessary for localization to the membrane.


Pssm-ID: 350445 [Multi-domain]  Cd Length: 234  Bit Score: 208.15  E-value: 1.14e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1729 ENRGKNRYNNILPYDASRVKLCNVdddpcSDYINASYI--PGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQ 1806
Cdd:cd14597      2 ENRKKNRYKNILPYDTTRVPLGDE-----GGYINASFIkmPVGDEEFVYIACQGPLPTTVADFWQMVWEQKSTVIAMMTQ 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1807 CVEKGRVKCDHYWP-ADQDPLYYGD-LILQMVSESVLPEWTIREFKIcSEEQLDAHRLLRHFHYTVWPDHGVPETTQSLI 1884
Cdd:cd14597     77 EVEGGKIKCQRYWPeILGKTTMVDNrLQLTLVRMQQLKNFVIRVLEL-EDIQTREVRHITHLNFTAWPDHDTPSQPEQLL 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1885 QFVRTVRdYINRSpgaGPTVVHCSAGVGRTGTFVALDRILqQLDSKD-SVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 1963
Cdd:cd14597    156 TFISYMR-HIHKS---GPIITHCSAGIGRSGTLICIDVVL-GLISKDlDFDISDIVRTMRLQRHGMVQTEDQYIFCYQVI 230


                   ....
gi 1725351434 1964 RDVL 1967
Cdd:cd14597    231 LYVL 234
PTPc-N3_4 cd14541
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1759-1963 2.04e-60

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: 206.80  E-value: 2.04e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1759 DYINASY----IPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDPLYYGDLILQ 1834
Cdd:cd14541      1 DYINANYvnmeIPGSGIVNRYIAAQGPLPNTCADFWQMVWEQKSTLIVMLTTLVERGRVKCHQYWPDLGETMQFGNLQIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1835 MVSESVLPEWTIREFKICSEEQLDAhRLLRHFHYTVWPDHGVPETTQSLIQFVRTVRDYinRSPGAGPTVVHCSAGVGRT 1914
Cdd:cd14541     81 CVSEEVTPSFAFREFILTNTNTGEE-RHITQMQYLAWPDHGVPDDSSDFLDFVKRVRQN--RVGMVEPTVVHCSAGIGRT 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1725351434 1915 GTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 1963
Cdd:cd14541    158 GVLITMETAMCLIEANEPVYPLDIVRTMRDQRAMLIQTPSQYRFVCEAI 206
PTPc-N11 cd14605
catalytic domain of tyrosine-protein phosphatase non-receptor type 11; Tyrosine-protein ...
 1729-1964 8.65e-60

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: 206.41  E-value: 8.65e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1729 ENRGKNRYNNILPYDASRVKLCNVD-DDPCSDYINASYI-PGNNF-------RREYIATQGPLPGTKDDFWKMAWEQNVH 1799
Cdd:cd14605      1 ENKNKNRYKNILPFDHTRVVLHDGDpNEPVSDYINANIImPEFETkcnnskpKKSYIATQGCLQNTVNDFWRMVFQENSR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1800 NIVMVTQCVEKGRVKCDHYWPADQDPLYYGDLILQMVSESVLPEWTIREFKICSEEQLDAHRLLRHFHYTVWPDHGVPET 1879
Cdd:cd14605     81 VIVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYILRELKLSKVGQGNTERTVWQYHFRTWPDHGVPSD 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1880 TQSLIQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKD---SVDIYGAVHDLRLHRVHMVQTECQY 1956
Cdd:cd14605    161 PGGVLDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGvdcDIDVPKTIQMVRSQRSGMVQTEAQY 240


                   ....*...
gi 1725351434 1957 VYLHQCVR 1964
Cdd:cd14605    241 RFIYMAVQ 248
R-PTPc-U-1 cd14632
catalytic domain of receptor-type tyrosine-protein phosphatase U, repeat 1; Receptor-type ...
 1760-1963 9.36e-60

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: 204.51  E-value: 9.36e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1760 YINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDplYYGDLILQMVSES 1839
Cdd:cd14632      1 YINANYIDGYHRSNHFIATQGPKQEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSKYWPDDSD--TYGDIKITLLKTE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1840 VLPEWTIREFKIcSEEQLDAHRLLRHFHYTVWPDHGVPETTQSLIQFVRTVRDyiNRSPGAGPTVVHCSAGVGRTGTFVA 1919
Cdd:cd14632     79 TLAEYSVRTFAL-ERRGYSARHEVKQFHFTSWPEHGVPYHATGLLAFIRRVKA--STPPDAGPVVVHCSAGAGRTGCYIV 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1725351434 1920 LDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 1963
Cdd:cd14632    156 LDVMLDMAECEGVVDIYNCVKTLCSRRINMIQTEEQYIFIHDAI 199
R-PTPc-A-E-1 cd14551
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 1; ...
 1760-1961 4.56e-59

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: 202.45  E-value: 4.56e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1760 YINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPaDQDPLYYGDLILQMVSES 1839
Cdd:cd14551      1 YINASYIDGYQEKNKFIAAQGPKDETVNDFWRMIWEQGSATIVMVTNLKERKEKKCSQYWP-DQGCWTYGNLRVRVEDTV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1840 VLPEWTIREFkiCSEEQLD-----AHRLLRHFHYTVWPDHGVPETTQSLIQFVRTVRDYInrSPGAGPTVVHCSAGVGRT 1914
Cdd:cd14551     80 VLVDYTTRKF--CIQKVNRgigekRVRLVTQFHFTSWPDFGVPFTPIGMLKFLKKVKSAN--PPRAGPIVVHCSAGVGRT 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1725351434 1915 GTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 1961
Cdd:cd14551    156 GTFIVIDAMLDMMHAEGKVDVFGFVSRIRQQRSQMVQTDMQYVFIYQ 202
R-PTP-S-2 cd14627
PTP-like domain of receptor-type tyrosine-protein phosphatase S, repeat 2; Receptor-type ...
 1725-1967 1.04e-58

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: 204.97  E-value: 1.04e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1725 ALLPENRGKNRYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMV 1804
Cdd:cd14627     48 ANLPCNKFKNRLVNIMPYETTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVML 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1805 TQCVEKGRVKCDHYWPADQDPlYYGDLILQMVSESVLPEWTIREFKIcSEEQLDAHRLLRHFHYTVWPDHGVPETTQSLI 1884
Cdd:cd14627    128 TKLREMGREKCHQYWPAERSA-RYQYFVVDPMAEYNMPQYILREFKV-TDARDGQSRTVRQFQFTDWPEQGVPKSGEGFI 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1885 QFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVR 1964
Cdd:cd14627    206 DFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAAL 285


                   ...
gi 1725351434 1965 DVL 1967
Cdd:cd14627    286 EYL 288
R-PTP-D-2 cd14628
PTP-like domain of receptor-type tyrosine-protein phosphatase D, repeat 2; Receptor-type ...
 1725-1967 2.82e-58

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: 203.81  E-value: 2.82e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1725 ALLPENRGKNRYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMV 1804
Cdd:cd14628     47 ANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVML 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1805 TQCVEKGRVKCDHYWPADQDPlYYGDLILQMVSESVLPEWTIREFKIcSEEQLDAHRLLRHFHYTVWPDHGVPETTQSLI 1884
Cdd:cd14628    127 TKLREMGREKCHQYWPAERSA-RYQYFVVDPMAEYNMPQYILREFKV-TDARDGQSRTVRQFQFTDWPEQGVPKSGEGFI 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1885 QFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVR 1964
Cdd:cd14628    205 DFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDQYQFCYRAAL 284


                   ...
gi 1725351434 1965 DVL 1967
Cdd:cd14628    285 EYL 287
PTPc-N3 cd14600
catalytic domain of tyrosine-protein phosphatase non-receptor type 3; Tyrosine-protein ...
 1709-1968 7.34e-58

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: 202.00  E-value: 7.34e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1709 EYEDL--KDVGRSQSCdiALLPENRGKNRYNNILPYDASRVKLcnvddDPCSDYINASY----IPGNNFRREYIATQGPL 1782
Cdd:cd14600     19 QFEQLyrKKPGLAITC--AKLPQNMDKNRYKDVLPYDATRVVL-----QGNEDYINASYvnmeIPSANIVNKYIATQGPL 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1783 PGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDPLYYGDLILQMVSESVLPEWTIREFKICSEEQLDAHRL 1862
Cdd:cd14600     92 PHTCAQFWQVVWEQKLSLIVMLTTLTERGRTKCHQYWPDPPDVMEYGGFRVQCHSEDCTIAYVFREMLLTNTQTGEERTV 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1863 LrHFHYTVWPDHGVPETTQSLIQFVRTVRdyiNRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDL 1942
Cdd:cd14600    172 T-HLQYVAWPDHGVPDDSSDFLEFVNYVR---SKRVENEPVLVHCSAGIGRTGVLVTMETAMCLTERNQPVYPLDIVRKM 247

                          250       260
                   ....*....|....*....|....*.
gi 1725351434 1943 RLHRVHMVQTECQYVYLHQCVRDVLR 1968
Cdd:cd14600    248 RDQRAMMVQTSSQYKFVCEAILRVYE 273
R-PTP-F-2 cd14629
PTP-like domain of receptor-type tyrosine-protein phosphatase F, repeat 2; Receptor-type ...
 1725-1967 1.07e-57

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: 201.88  E-value: 1.07e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1725 ALLPENRGKNRYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMV 1804
Cdd:cd14629     48 ANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWEHNSTIVVML 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1805 TQCVEKGRVKCDHYWPADQDPlYYGDLILQMVSESVLPEWTIREFKIcSEEQLDAHRLLRHFHYTVWPDHGVPETTQSLI 1884
Cdd:cd14629    128 TKLREMGREKCHQYWPAERSA-RYQYFVVDPMAEYNMPQYILREFKV-TDARDGQSRTIRQFQFTDWPEQGVPKTGEGFI 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1885 QFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYvylHQCVR 1964
Cdd:cd14629    206 DFIGQVHKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQY---QLCYR 282


                   ...
gi 1725351434 1965 DVL 1967
Cdd:cd14629    283 AAL 285
PTPc-N20 cd14596
catalytic domain of tyrosine-protein phosphatase non-receptor type 20; Tyrosine-protein ...
 1760-1968 2.76e-56

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: 194.58  E-value: 2.76e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1760 YINASYI--PGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPAD-QDPLYYGDLILQMV 1836
Cdd:cd14596      1 YINASYItmPVGEEELFYIATQGPLPSTIDDFWQMVWENRSDVIAMMTREVERGKVKCHRYWPETlQEPMELENYQLRLE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1837 SESVLPEWTIREFKICSEEQLDAHrLLRHFHYTVWPDHGVPETTQSLIQFVRtvrdYINRSPGAGPTVVHCSAGVGRTGT 1916
Cdd:cd14596     81 NYQALQYFIIRIIKLVEKETGENR-LIKHLQFTTWPDHGTPQSSDQLVKFIC----YMRKVHNTGPIVVHCSAGIGRAGV 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1725351434 1917 FVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRDVLR 1968
Cdd:cd14596    156 LICVDVLLSLIEKDLSFNIKDIVREMRQQRYGMIQTKDQYLFCYKVVLEVLQ 207
R-PTPc-A-E-2 cd14552
catalytic domain of receptor-type tyrosine-protein phosphatase A and E, repeat 2; ...
 1760-1963 2.29e-55

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: 191.71  E-value: 2.29e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1760 YINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADqDPLYYGDLILQMVSES 1839
Cdd:cd14552      1 YINASFIDGYRQKDAYIATQGPLDHTVEDFWRMIWEWKSCSIVMLTEIKERSQNKCAQYWPED-GSVSSGDITVELKDQT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1840 VLPEWTIREFKIcSEEQLDAHRLLRHFHYTVWPDHGVPETTQSLIQFVRTVRDYINRSpGAGPTVVHCSAGVGRTGTFVA 1919
Cdd:cd14552     80 DYEDYTLRDFLV-TKGKGGSTRTVRQFHFHGWPEVGIPDNGKGMIDLIAAVQKQQQQS-GNHPITVHCSAGAGRTGTFCA 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1725351434 1920 LDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 1963
Cdd:cd14552    158 LSTVLERVKAEGVLDVFQVVKSLRLQRPHMVQTLEQYEFCYKVV 201
R-PTPc-E-2 cd14622
catalytic domain of receptor-type tyrosine-protein phosphatase E, repeat 2; Receptor-type ...
 1759-1965 6.19e-55

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: 190.60  E-value: 6.19e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1759 DYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPAdQDPLYYGDLILQMVSE 1838
Cdd:cd14622      1 DYINASFIDGYRQKDYFIATQGPLAHTVEDFWRMVWEWKCHTIVMLTELQEREQEKCVQYWPS-EGSVTHGEITIEIKND 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1839 SVLPEWTIREFkICSEEQLDAHRLLRHFHYTVWPDHGVPETTQSLIQFVRTVRDYINRSpGAGPTVVHCSAGVGRTGTFV 1918
Cdd:cd14622     80 TLLETISIRDF-LVTYNQEKQTRLVRQFHFHGWPEIGIPAEGKGMIDLIAAVQKQQQQT-GNHPIVVHCSAGAGRTGTFI 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1725351434 1919 ALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRD 1965
Cdd:cd14622    158 ALSNILERVKAEGLLDVFQTVKSLRLQRPHMVQTLEQYEFCYRVVQD 204
PTPc-N22_18_12 cd14542
catalytic domain of tyrosine-protein phosphatase non-receptor type 22, type 18 and type 12; ...
 1760-1961 7.06e-54

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: 187.63  E-value: 7.06e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1760 YINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQ-DPLYYGDLILQMVSE 1838
Cdd:cd14542      1 YINANFIKGVSGSKAYIATQGPLPNTVLDFWRMIWEYNVQVIVMACREFEMGKKKCERYWPEEGeEQLQFGPFKISLEKE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1839 S-VLPEWTIREFKI-CSEEQldahRLLRHFHYTVWPDHGVPETTQSLIQFVRTVRDYinRSPGAGPTVVHCSAGVGRTGT 1916
Cdd:cd14542     81 KrVGPDFLIRTLKVtFQKES----RTVYQFHYTAWPDHGVPSSVDPILDLVRLVRDY--QGSEDVPICVHCSAGCGRTGT 154

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1725351434 1917 FVALD---RILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 1961
Cdd:cd14542    155 ICAIDyvwNLLKTGKIPEEFSLFDLVREMRKQRPAMVQTKEQYELVYR 202
PTPc-N12 cd14604
catalytic domain of tyrosine-protein phosphatase non-receptor type 12; Tyrosine-protein ...
 1689-1963 4.68e-53

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: 188.99  E-value: 4.68e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1689 NQFEGHFMKLQAdsnylLSKEYEDLK----DVGRSQscdiallpENRGKNRYNNILPYDASRVKLCNVDDDPCSDYINAS 1764
Cdd:cd14604     25 DNFASDFMRLRR-----LSTKYRTEKiyptATGEKE--------ENVKKNRYKDILPFDHSRVKLTLKTSSQDSDYINAN 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1765 YIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPA-DQDPLYYGDLILQMVSESVLPE 1843
Cdd:cd14604     92 FIKGVYGPKAYIATQGPLANTVIDFWRMIWEYNVAIIVMACREFEMGRKKCERYWPLyGEEPMTFGPFRISCEAEQARTD 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1844 WTIREFKIcsEEQLDAHRLLRhFHYTVWPDHGVPETTQSLIQFVRTVRDYINRSpgAGPTVVHCSAGVGRTGTFVALD-- 1921
Cdd:cd14604    172 YFIRTLLL--EFQNETRRLYQ-FHYVNWPDHDVPSSFDSILDMISLMRKYQEHE--DVPICIHCSAGCGRTGAICAIDyt 246

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1725351434 1922 -RILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 1963
Cdd:cd14604    247 wNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAI 289
PTPc-N5 cd14613
catalytic domain of tyrosine-protein phosphatase non-receptor type 5; Tyrosine-protein ...
 1733-1960 1.67e-52

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: 185.84  E-value: 1.67e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1733 KNRYNNILPYDASRVKLCNVD-DDPCSDYINASYIPG-NNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEK 1810
Cdd:cd14613     28 KNRYKTILPNPHSRVCLTSPDqDDPLSSYINANYIRGyGGEEKVYIATQGPTVNTVGDFWRMVWQERSPIIVMITNIEEM 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1811 GRvKCDHYWPADQdPLYYGdliLQMVSESVLPE--WTIREFKICSEEQldaHRLLRHFHYTVWPDHGVPETTQSLIQFVR 1888
Cdd:cd14613    108 NE-KCTEYWPEEQ-VTYEG---IEITVKQVIHAddYRLRLITLKSGGE---ERGLKHYWYTSWPDQKTPDNAPPLLQLVQ 179

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1725351434 1889 TVRDYINRS-PGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 1960
Cdd:cd14613    180 EVEEARQQAePNCGPVIVHCSAGIGRTGCFIATSICCKQLRNEGVVDILRTTCQLRLDRGGMIQTCEQYQFVH 252
R-PTPc-A-2 cd14623
catalytic domain of receptor-type tyrosine-protein phosphatase A, repeat 2; Receptor-type ...
 1735-1965 6.46e-52

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: 182.94  E-value: 6.46e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1735 RYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVK 1814
Cdd:cd14623      1 RVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLQHTIEDFWRMIWEWKSCSIVMLTELEERGQEK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1815 CDHYWPADqDPLYYGDLILQMVSESVLPEWTIREFKICSEEQlDAHRLLRHFHYTVWPDHGVPETTQSLIQFVRTVRDYI 1894
Cdd:cd14623     81 CAQYWPSD-GSVSYGDITIELKKEEECESYTVRDLLVTNTRE-NKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQ 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1725351434 1895 NRSpGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRD 1965
Cdd:cd14623    159 QQS-GNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQE 228
PTPc-N22 cd14602
catalytic domain of tyrosine-protein phosphatase non-receptor type 22; Tyrosine-protein ...
 1733-1963 7.40e-52

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: 183.12  E-value: 7.40e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1733 KNRYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGR 1812
Cdd:cd14602      1 KNRYKDILPYDHSRVELSLITSDEDSDYINANFIKGVYGPRAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEFEMGK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1813 VKCDHYWP-ADQDPLYYGDLILQMVSESVLPEWTIREFKI-CSEEQldahRLLRHFHYTVWPDHGVPETTQSLIQFVRTV 1890
Cdd:cd14602     81 KKCERYWAePGEMQLEFGPFSVTCEAEKRKSDYIIRTLKVkFNSET----RTIYQFHYKNWPDHDVPSSIDPILELIWDV 156

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1725351434 1891 RDYinRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLdsKDSV-----DIYGAVHDLRLHRVHMVQTECQYVYLHQCV 1963
Cdd:cd14602    157 RCY--QEDDSVPICIHCSAGCGRTGVICAIDYTWMLL--KDGIipenfSVFSLIQEMRTQRPSLVQTKEQYELVYNAV 230
R-PTPc-R cd14611
catalytic domain of receptor-type tyrosine-protein phosphatase R; Receptor-type ...
 1733-1961 1.67e-51

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: 181.65  E-value: 1.67e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1733 KNRYNNILPYDASRVKLCNVD-DDPCSDYINASYIPG-NNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEK 1810
Cdd:cd14611      2 KNRYKTILPNPHSRVCLKPKNsNDSLSTYINANYIRGyGGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEK 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1811 GRvKCDHYWPADQDplYYGDLILQMVSESVLPEWTIREFKIcseEQLDAHRLLRHFHYTVWPDHGVPETTQSLIQFVRTV 1890
Cdd:cd14611     82 NE-KCVLYWPEKRG--IYGKVEVLVNSVKECDNYTIRNLTL---KQGSQSRSVKHYWYTSWPDHKTPDSAQPLLQLMLDV 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1725351434 1891 RDYINRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 1961
Cdd:cd14611    156 EEDRLASPGRGPVVVHCSAGIGRTGCFIATTIGCQQLKEEGVVDVLSIVCQLRVDRGGMVQTSEQYEFVHH 226
R-PTP-N2 cd14610
PTP-like domain of receptor-type tyrosine-protein phosphatase N2; Receptor-type ...
 1706-1958 8.45e-51

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: 181.79  E-value: 8.45e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1706 LSKEYEDLKDV-GRSQSCDIALLPENRGKNRYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRR-EYIATQGPLP 1783
Cdd:cd14610     19 LEKEWEALCAYqAEPNATNVAQREENVQKNRSLAVLPYDHSRIILKAENSHSHSDYINASPIMDHDPRNpAYIATQGPLP 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1784 GTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDPLYYgDLILQMVSESVLPE-WTIREFKIcSEEQLDAHRL 1862
Cdd:cd14610     99 ATVADFWQMVWESGCVVIVMLTPLAENGVKQCYHYWPDEGSNLYH-IYEVNLVSEHIWCEdFLVRSFYL-KNLQTNETRT 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1863 LRHFHYTVWPDHGVPETTQSLIQFVRTVRD-YINRSpgaGPTVVHCSAGVGRTGTFVALDRILQQL-DSKDSVDIYGAVH 1940
Cdd:cd14610    177 VTQFHFLSWNDQGVPASTRSLLDFRRKVNKcYRGRS---CPIIVHCSDGAGRSGTYILIDMVLNKMaKGAKEIDIAATLE 253

                          250
                   ....*....|....*...
gi 1725351434 1941 DLRLHRVHMVQTECQYVY 1958
Cdd:cd14610    254 HLRDQRPGMVQTKEQFEF 271
PTPc-N21_14 cd14540
catalytic domain of tyrosine-protein phosphatase non-receptor type 21 and type 14; ...
 1760-1961 1.93e-50

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: 178.42  E-value: 1.93e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1760 YINASYIP---GNNFRReYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPA---DQDPLYYGDLIL 1833
Cdd:cd14540      1 YINASHITatvGGKQRF-YIAAQGPLQNTVGDFWQMVWEQGVYLVVMVTAEEEGGREKCFRYWPTlggEHDALTFGEYKV 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1834 QMVSESVLPEWTIREFKIcSEEQLDAHRLLRHFHYTVWPDHGVPETTQSLIQF---VRTVRDYI-------NRSPgagPT 1903
Cdd:cd14540     80 STKFSVSSGCYTTTGLRV-KHTLSGQSRTVWHLQYTDWPDHGCPEDVSGFLDFleeINSVRRHTnqdvaghNRNP---PT 155

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1725351434 1904 VVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 1961
Cdd:cd14540    156 LVHCSAGVGRTGVVILADLMLYCLDHNEELDIPRVLALLRHQRMLLVQTLAQYKFVYN 213
R-PTP-N cd14609
PTP-like domain of receptor-type tyrosine-protein phosphatase N; Receptor-type ...
 1706-1958 4.08e-49

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: 176.77  E-value: 4.08e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1706 LSKEYEDLKDV-GRSQSCDIALLPENRGKNRYNNILPYDASRVKLcNVDDDPC-SDYINASYIPGNNFRR-EYIATQGPL 1782
Cdd:cd14609     17 LAKEWQALCAYqAEPNTCSTAQGEANVKKNRNPDFVPYDHARIKL-KAESNPSrSDYINASPIIEHDPRMpAYIATQGPL 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1783 PGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDPLYYgDLILQMVSESVLPE-WTIREFKIcSEEQLDAHR 1861
Cdd:cd14609     96 SHTIADFWQMVWENGCTVIVMLTPLVEDGVKQCDRYWPDEGSSLYH-IYEVNLVSEHIWCEdFLVRSFYL-KNVQTQETR 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1862 LLRHFHYTVWPDHGVPETTQSLIQFVRTV-RDYINRSpgaGPTVVHCSAGVGRTGTFVALDRILQQL-DSKDSVDIYGAV 1939
Cdd:cd14609    174 TLTQFHFLSWPAEGIPSSTRPLLDFRRKVnKCYRGRS---CPIIVHCSDGAGRTGTYILIDMVLNRMaKGVKEIDIAATL 250

                          250
                   ....*....|....*....
gi 1725351434 1940 HDLRLHRVHMVQTECQYVY 1958
Cdd:cd14609    251 EHVRDQRPGMVRTKDQFEF 269
PTPc-N4 cd14601
catalytic domain of tyrosine-protein phosphatase non-receptor type 4; Tyrosine-protein ...
 1759-1968 1.36e-48

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: 172.82  E-value: 1.36e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1759 DYINASYI----PGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDPLYYGDLILQ 1834
Cdd:cd14601      1 DYINANYInmeiPSSSIINRYIACQGPLPNTCSDFWQMTWEQGSSMVVMLTTQVERGRVKCHQYWPEPSGSSSYGGFQVT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1835 MVSESVLPEWTIREFKICSEEQLDAhRLLRHFHYTVWPDHGVPETTQSLIQFVRTVRDyiNRSPGAGPTVVHCSAGVGRT 1914
Cdd:cd14601     81 CHSEEGNPAYVFREMTLTNLEKNES-RPLTQIQYIAWPDHGVPDDSSDFLDFVCLVRN--KRAGKDEPVVVHCSAGIGRT 157

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1725351434 1915 GTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRDVLR 1968
Cdd:cd14601    158 GVLITMETAMCLIECNQPVYPLDIVRTMRDQRAMMIQTPSQYRFVCEAILKVYE 211
R-PTP-C-2 cd14558
PTP-like domain of receptor-type tyrosine-protein phosphatase C, repeat 2; Receptor-type ...
 1760-1960 8.15e-48

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: 170.27  E-value: 8.15e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1760 YINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDPlyYGDLILQMVSES 1839
Cdd:cd14558      1 YINASFIDGYWGPKSLIATQGPLPDTIADFWQMIFQKKVKVIVMLTELKEGDQEQCAQYWGDEKKT--YGDIEVELKDTE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1840 VLPEWTIREFKIcSEEQLDAHRLLRHFHYTVWPDHGVPETTQSLIQFVRTVR----DYINRSPGAGPTVVHCSAGVGRTG 1915
Cdd:cd14558     79 KSPTYTVRVFEI-THLKRKDSRTVYQYQYHKWKGEELPEKPKDLVDMIKSIKqklpYKNSKHGRSVPIVVHCSDGSSRTG 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1725351434 1916 TFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 1960
Cdd:cd14558    158 IFCALWNLLESAETEKVVDVFQVVKALRKQRPGMVSTLEQYQFLY 202
PTPc-N14 cd14599
catalytic domain of tyrosine-protein phosphatase non-receptor type 14; Tyrosine-protein ...
 1709-1961 5.70e-46

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: 168.25  E-value: 5.70e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1709 EYEDLKDVGRSQSCDIALLPENRGKNRYNNILPYDASRVKLCNVDDDPcSDYINASYIPGNNFRRE--YIATQGPLPGTK 1786
Cdd:cd14599     17 EYEQIPKKKADGVFTTATLPENAERNRIREVVPYEENRVELVPTKENN-TGYINASHIKVTVGGEEwhYIATQGPLPHTC 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1787 DDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWP---ADQDPLYYG--DLILQMVSESVLPEWTIREFKICSEEQldaHR 1861
Cdd:cd14599     96 HDFWQMVWEQGVNVIAMVTAEEEGGRSKSHRYWPklgSKHSSATYGkfKVTTKFRTDSGCYATTGLKVKHLLSGQ---ER 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1862 LLRHFHYTVWPDHGVPETTQSLIQF---VRTVRDYINRSPGAG-----PTVVHCSAGVGRTGTFVALDRILQQLDSKDSV 1933
Cdd:cd14599    173 TVWHLQYTDWPDHGCPEEVQGFLSYleeIQSVRRHTNSMLDSTkncnpPIVVHCSAGVGRTGVVILTELMIGCLEHNEKV 252

                          250       260
                   ....*....|....*....|....*...
gi 1725351434 1934 DIYGAVHDLRLHRVHMVQTECQYVYLHQ 1961
Cdd:cd14599    253 EVPVMLRHLREQRMFMIQTIAQYKFVYQ 280
R-PTPc-typeIIb-2 cd14556
PTP domain of type IIb (or R2B) subfamily receptor-type tyrosine-protein phosphatases, repeat ...
 1760-1961 1.18e-45

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: 164.12  E-value: 1.18e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1760 YINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQcVEKGRVKCDHYWPaDQDPLYYGDLILQMVSES 1839
Cdd:cd14556      1 YINAALLDSYKQPAAFIVTQHPLPNTVTDFWRLVYDYGCTSIVMLNQ-LDPKDQSCPQYWP-DEGSGTYGPIQVEFVSTT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1840 VLPEWTIREFKICSEEQL-DAHRLLRHFHYTVWPDHG-VPETTQSLIQFVRTVRDYINRSpGAGPTVVHCSAGVGRTGTF 1917
Cdd:cd14556     79 IDEDVISRIFRLQNTTRPqEGYRMVQQFQFLGWPRDRdTPPSKRALLKLLSEVEKWQEQS-GEGPIVVHCLNGVGRSGVF 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1725351434 1918 VALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 1961
Cdd:cd14556    158 CAISSVCERIKVENVVDVFQAVKTLRNHRPNMVETEEQYKFCYD 201
R-PTP-N-N2 cd14546
PTP-like domain of receptor-type tyrosine-protein phosphatase-like N and N2; Receptor-type ...
 1760-1963 3.04e-44

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: 160.30  E-value: 3.04e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1760 YINASYIPGNNFRRE-YIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDPLyYGDLILQMVSE 1838
Cdd:cd14546      1 YINASTIYDHDPRNPaYIATQGPLPHTIADFWQMIWEQGCVVIVMLTRLQENGVKQCARYWPEEGSEV-YHIYEVHLVSE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1839 SVLPE-WTIREFKIcSEEQLDAHRLLRHFHYTVWPDHGVPETTQSLIQFVRTV-RDYINRSpgaGPTVVHCSAGVGRTGT 1916
Cdd:cd14546     80 HIWCDdYLVRSFYL-KNLQTSETRTVTQFHFLSWPDEGIPASAKPLLEFRRKVnKSYRGRS---CPIVVHCSDGAGRTGT 155

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1725351434 1917 FVALDRILQQL-DSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 1963
Cdd:cd14546    156 YILIDMVLNRMaKGAKEIDIAATLEHLRDQRPGMVKTKDQFEFVLTAV 203
PTPc_plant_PTP1 cd17658
protein tyrosine phosphatase 1 from Arabidopsis thaliana and similar plant PTPs; Arabidopsis ...
 1760-1958 3.26e-44

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: 159.94  E-value: 3.26e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1760 YINASYIPGNNFRR--EYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGR-VKCDHYWPA-DQDPLYYGDLilqm 1835
Cdd:cd17658      1 YINASLVETPASESlpKFIATQGPLPHTFEDFWEMVIQQRCPVIIMLTRLVDNYStAKCADYFPAeENESREFGRI---- 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1836 vseSVLPEW--------TIREFKICSEEQLDAHRLLRHFHYTVWPDHGVPETTqsliqfvRTVRDYINRS----PGAGPT 1903
Cdd:cd17658     77 ---SVTNKKlkhsqhsiTLRVLEVQYIESEEPPLSVLHIQYPEWPDHGVPKDT-------RSVRELLKRLygipPSAGPI 146

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1725351434 1904 VVHCSAGVGRTGTFVALDRILQQLDSKD--SVDIYGAVHDLRLHRVHMVQTECQYVY 1958
Cdd:cd17658    147 VVHCSAGIGRTGAYCTIHNTIRRILEGDmsAVDLSKTVRKFRSQRIGMVQTQDQYIF 203
PTP-N23 cd14539
PTP-like domain of tyrosine-protein phosphatase non-receptor type 23; Tyrosine-protein ...
 1760-1961 4.80e-43

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: 156.78  E-value: 4.80e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1760 YINASYIPG-NNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQ-DPLYYGDLILQMVS 1837
Cdd:cd14539      1 YINASLIEDlTPYCPRFIATQAPLPGTAADFWLMVYEQQVSVIVMLVSEQENEKQKVHRYWPTERgQALVYGAITVSLQS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1838 ESVLPEWTIREFKICSEEQlDAHRLLRHFHYTVWPDHGVPETTQSLIQFVRTVRDYINRS-PGAGPTVVHCSAGVGRTGT 1916
Cdd:cd14539     81 VRTTPTHVERIISIQHKDT-RLSRSVVHLQFTTWPELGLPDSPNPLLRFIEEVHSHYLQQrSLQTPIVVHCSSGVGRTGA 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1725351434 1917 FVALDRILQQLDSKDSV-DIYGAVHDLRLHRVHMVQTECQYVYLHQ 1961
Cdd:cd14539    160 FCLLYAAVQEIEAGNGIpDLPQLVRKMRQQRKYMLQEKEHLKFCYE 205
PHA02742 PHA02742
protein tyrosine phosphatase; Provisional
 1687-1972 3.43e-41

protein tyrosine phosphatase; Provisional


Pssm-ID: 165109 [Multi-domain]  Cd Length: 303  Bit Score: 154.77  E-value: 3.43e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1687 KINQFEGHFMKLQADSN--YLLSKEYEDLKDVGRSQSCDIALLPENRGKNRYNNILPYDASRVKLCNvdDDPCSDYINAS 1764
Cdd:PHA02742     7 KKNSFAKNCEQLIEESNlaEILKEEHEHIMQEIVAFSCNESLELKNMKKCRYPDAPCFDRNRVILKI--EDGGDDFINAS 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1765 YIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYW-PADQDPLYYGDLILQMVSESVLPE 1843
Cdd:PHA02742    85 YVDGHNAKGRFICTQAPLEETALDFWQAIFQDQVRVIVMITKIMEDGKEACYPYWmPHERGKATHGEFKIKTKKIKSFRN 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1844 WTIREFKIcSEEQLDAHRLLRHFHYTVWPDHGVPETTQSLIQFVRTVR--DYINRSPGAG-------PTVVHCSAGVGRT 1914
Cdd:PHA02742   165 YAVTNLCL-TDTNTGASLDIKHFAYEDWPHGGLPRDPNKFLDFVLAVReaDLKADVDIKGenivkepPILVHCSAGLDRA 243

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1725351434 1915 GTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYlhqCVRDVLRARKL 1972
Cdd:PHA02742   244 GAFCAIDICISKYNERAIIPLLSIVRDLRKQRHNCLSLPQQYIF---CYFIVLIFAKL 298
COG5599 COG5599
Protein tyrosine phosphatase [Signal transduction mechanisms];
1728-1956 9.17e-41

Protein tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 444335 [Multi-domain]  Cd Length: 282  Bit Score: 152.94  E-value: 9.17e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1728 PENRGKNRYNNILPYDASRVKlcnvDDDPcsdYINASYIPGNNFRReYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQC 1807
Cdd:COG5599     40 INGSPLNRFRDIQPYKETALR----ANLG---YLNANYIQVIGNHR-YIATQYPLEEQLEDFFQMLFDNNTPVLVVLASD 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1808 VE--KGRVKCDHYWPADqdplyyGDLILQMVS------ESVLPEWTIREFKI----CSEEQLDAHrllrHFHYTVWPDHG 1875
Cdd:COG5599    112 DEisKPKVKMPVYFRQD------GEYGKYEVSseltesIQLRDGIEARTYVLtikgTGQKKIEIP----VLHVKNWPDHG 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1876 VPETTQsLIQFVRTVRDYIN-RSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKD--SVDIYGAVHDLRLHR-VHMVQ 1951
Cdd:COG5599    182 AISAEA-LKNLADLIDKKEKiKDPDKLLPVVHCRAGVGRTGTLIACLALSKSINALVqiTLSVEEIVIDMRTSRnGGMVQ 260


                   ....*
gi 1725351434 1952 TECQY 1956
Cdd:COG5599    261 TSEQL 265
PTPc_DSPc smart00012
Protein tyrosine phosphatase, catalytic domain, undefined specificity; Protein tyrosine ...
 1863-1963 8.21e-40

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: 143.27  E-value: 8.21e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  1863 LRHFHYTVWPDHGVPETTQSLIQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDS-KDSVDIYGAVHD 1941
Cdd:smart00012    2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAeAGEVDIFDTVKE 81

                            90       100
                    ....*....|....*....|..
gi 1725351434  1942 LRLHRVHMVQTECQYVYLHQCV 1963
Cdd:smart00012   82 LRSQRPGMVQTEEQYLFLYRAL 103
PTPc_motif smart00404
Protein tyrosine phosphatase, catalytic domain motif;
1863-1963 8.21e-40

Protein tyrosine phosphatase, catalytic domain motif;


Pssm-ID: 214649 [Multi-domain]  Cd Length: 105  Bit Score: 143.27  E-value: 8.21e-40
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  1863 LRHFHYTVWPDHGVPETTQSLIQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDS-KDSVDIYGAVHD 1941
Cdd:smart00404    2 VKHYHYTGWPDHGVPESPDSILELLRAVKKNLNQSESSGPVVVHCSAGVGRTGTFVAIDILLQQLEAeAGEVDIFDTVKE 81

                            90       100
                    ....*....|....*....|..
gi 1725351434  1942 LRLHRVHMVQTECQYVYLHQCV 1963
Cdd:smart00404   82 LRSQRPGMVQTEEQYLFLYRAL 103
PHA02747 PHA02747
protein tyrosine phosphatase; Provisional
 1728-1960 8.23e-39

protein tyrosine phosphatase; Provisional


Pssm-ID: 165114 [Multi-domain]  Cd Length: 312  Bit Score: 148.23  E-value: 8.23e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1728 PENRGKNRYNNILPYDASRVKLcNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQC 1807
Cdd:PHA02747    49 PENQPKNRYWDIPCWDHNRVIL-DSGGGSTSDYIHANWIDGFEDDKKFIATQGPFAETCADFWKAVWQEHCSIIVMLTPT 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1808 -VEKGRVKCDHYW-PADQDPLYYGDLILQMVSESVLPEWTIREFKIcSEEQLDAHRLLRHFHYTVWPDHGVPETTQSLIQ 1885
Cdd:PHA02747   128 kGTNGEEKCYQYWcLNEDGNIDMEDFRIETLKTSVRAKYILTLIEI-TDKILKDSRKISHFQCSEWFEDETPSDHPDFIK 206

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1886 FVRTV--------RDYINRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYV 1957
Cdd:PHA02747   207 FIKIIdinrkksgKLFNPKDALLCPIVVHCSDGVGKTGIFCAVDICLNQLVKRKAICLAKTAEKIREQRHAGIMNFDDYL 286


                   ...
gi 1725351434 1958 YLH 1960
Cdd:PHA02747   287 FIQ 289
PHA02738 PHA02738
hypothetical protein; Provisional
 1730-1964 1.17e-37

hypothetical protein; Provisional


Pssm-ID: 222923 [Multi-domain]  Cd Length: 320  Bit Score: 145.07  E-value: 1.17e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1730 NRGKNRYNNILPYDASRVKLCNVDDDpcSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVE 1809
Cdd:PHA02738    49 NRKLNRYLDAVCFDHSRVILPAERNR--GDYINANYVDGFEYKKKFICGQAPTRQTCYDFYRMLWMEHVQIIVMLCKKKE 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1810 KGRVKCDHYWP-ADQDPLYYGDLILQMVSESVLPEWTirEFKICSEEQLDAHRLLRHFHYTVWPDHGVPETTQSLIQFVR 1888
Cdd:PHA02738   127 NGREKCFPYWSdVEQGSIRFGKFKITTTQVETHPHYV--KSTLLLTDGTSATQTVTHFNFTAWPDHDVPKNTSEFLNFVL 204

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1889 TVRD-----YINR------SPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYV 1957
Cdd:PHA02738   205 EVRQcqkelAQESlqighnRLQPPPIVVHCNAGLGRTPCYCVVDISISRFDACATVSIPSIVSSIRNQRYYSLFIPFQYF 284


                   ....*..
gi 1725351434 1958 YLHQCVR 1964
Cdd:PHA02738   285 FCYRAVK 291
PHA02746 PHA02746
protein tyrosine phosphatase; Provisional
 1705-1967 1.67e-36

protein tyrosine phosphatase; Provisional


Pssm-ID: 165113 [Multi-domain]  Cd Length: 323  Bit Score: 141.70  E-value: 1.67e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1705 LLSKEYEDLKDVGRSQSCDIALLPENRGKNRYNNILPYDASRV--------KLCNVDD-----------DPCSDYINASY 1765
Cdd:PHA02746    26 FVLLEHAEVMDIPIRGTTNHFLKKENLKKNRFHDIPCWDHSRVvinaheslKMFDVGDsdgkkievtseDNAENYIHANF 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1766 IPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQcVEKGRVKCDHYWPADQD-PLYYGDL---ILQMVSESVL 1841
Cdd:PHA02746   106 VDGFKEANKFICAQGPKEDTSEDFFKLISEHESQVIVSLTD-IDDDDEKCFELWTKEEDsELAFGRFvakILDIIEELSF 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1842 PEWTIREFKICSeeqlDAHRLLRHFHYTVWPDHGVPETTQSLIQFV--------RTVRDYINRSPGAGPTVVHCSAGVGR 1913
Cdd:PHA02746   185 TKTRLMITDKIS----DTSREIHHFWFPDWPDNGIPTGMAEFLELInkvneeqaELIKQADNDPQTLGPIVVHCSAGIGR 260

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1725351434 1914 TGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRDVL 1967
Cdd:PHA02746   261 AGTFCAIDNALEQLEKEKEVCLGEIVLKIRKQRHSSVFLPEQYAFCYKALKYAI 314
PTPc-N21 cd14598
catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein ...
 1760-1968 3.32e-36

catalytic domain of tyrosine-protein phosphatase non-receptor type 21; Tyrosine-protein phosphatase non-receptor type 21 (PTPN21), also called protein-tyrosine phosphatase D1, belongs to the family of classical tyrosine-specific protein tyrosine phosphatases (PTPs). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. PTPN21 is a component of a multivalent scaffold complex nucleated by focal adhesion kinase (FAK) at specific intracellular sites. It promotes cytoskeleton events that induce cell adhesion and migration by modulating Src-FAK signaling. It can also selectively associate with and stimulate Tec family kinases and modulate Stat3 activation. Human PTPN21 may also play a pathologic role in gastrointestinal tract tumorigenesis. PTPN21 contains an N-terminal FERM domain and a C-terminal catalytic PTP domain, separated by a long intervening sequence.


Pssm-ID: 350446 [Multi-domain]  Cd Length: 220  Bit Score: 137.41  E-value: 3.32e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1760 YINASYIPGNNFRRE--YIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWP---ADQDPLYYG--DLI 1832
Cdd:cd14598      1 YINASHIKVTVGGKEwdYIATQGPLQNTCQDFWQMVWEQGVAIIAMVTAEEEGGREKSFRYWPrlgSRHNTVTYGrfKIT 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1833 LQMVSESVLPEWTIREFKICSEEQldaHRLLRHFHYTVWPDHGVPETTQSLIQF---VRTVRDYIN-----RSPGAgPTV 1904
Cdd:cd14598     81 TRFRTDSGCYATTGLKIKHLLTGQ---ERTVWHLQYTDWPEHGCPEDLKGFLSYleeIQSVRRHTNstidpKSPNP-PVL 156

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1725351434 1905 VHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRDVLR 1968
Cdd:cd14598    157 VHCSAGVGRTGVVILSEIMIACLEHNEMLDIPRVLDMLRQQRMMMVQTLSQYTFVYKVLIQFLK 220
R5-PTP-2 cd14550
PTP-like domain of R5 subfamily receptor-type tyrosine-protein phosphatases, repeat 2; The R5 ...
 1760-1961 1.71e-33

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: 128.98  E-value: 1.71e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1760 YINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCdhYWPADQDPLYYGDLILQMVSES 1839
Cdd:cd14550      1 YINASYLQGYRRSNEFIITQHPLEHTIKDFWQMIWDHNSQTIVMLTDNELNEDEPI--YWPTKEKPLECETFKVTLSGED 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1840 VLPEW-----TIREFKIcsEEQLDAHRL-LRHFHYTVWPDHGVP-ETTQSLIQFVRtvRDYINRSpgaGPTVVHCSAGVG 1912
Cdd:cd14550     79 HSCLSneirlIVRDFIL--ESTQDDYVLeVRQFQCPSWPNPCSPiHTVFELINTVQ--EWAQQRD---GPIVVHDRYGGV 151

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1725351434 1913 RTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 1961
Cdd:cd14550    152 QAATFCALTTLHQQLEHESSVDVYQVAKLYHLMRPGVFTSKEDYQFLYK 200
PTP_tm pfam18861
TM proximal of protein tyrosine phosphatase, receptor type J; Protein tyrosine phosphatases ...
 1474-1613 1.32e-32

TM proximal of protein tyrosine phosphatase, receptor type J; Protein tyrosine phosphatases (PTPs) are known to be signaling molecules that regulate a variety of cellular processes, including cell growth, differentiation, mitotic cycle, and oncogenic transformation. PTP receptor type J possesses an extracellular region containing five fibronectin type III repeats, the transmembrane region included in this Pfam entry, and a intracytoplasmic catalytic domain. This entry probably contains part of a Fn3 domain at the N-terminus.


Pssm-ID: 465889  Cd Length: 126  Bit Score: 123.49  E-value: 1.32e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1474 VNCSWFSDTNGAVKYFAVVVREADSmdELRPEQQHPLPSYLEYRhNASIRVYQTNYFASKCAEspdPDRSSKSFNIKLGG 1553
Cdd:pfam18861    1 IQFSLFNSSNGPIKAYGVIVTTNDS--LNRPLKEYLNKTYYDWK-YKKTDSYLATVTPNPFTS---PRSSSRSLTVPVGT 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1725351434 1554 EMDSlggkcdpsqQKFCDGPLKPHTAYRISIRAFTQL-FDEGLKEFTKPLYSDTFFSMPIT 1613
Cdd:pfam18861   75 GSKW---------QGYCNGPLKPLGSYRFSVAAFTRLeFDDGLIDGEESYVSFTPFSEPIA 126
R-PTPc-T-2 cd14634
PTP domain of receptor-type tyrosine-protein phosphatase T, repeat 2; Receptor-type ...
 1760-1961 7.62e-32

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: 124.36  E-value: 7.62e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1760 YINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQcVEKGRVkCDHYWPaDQDPLYYGDLILQMVSES 1839
Cdd:cd14634      1 YINAALMDSHKQPAAFIVTQHPLPNTVADFWRLVFDYNCSSVVMLNE-MDAAQL-CMQYWP-EKTSCCYGPIQVEFVSAD 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1840 VLPEWTIREFKICSEEQ-LDAHRLLRHFHYTVWPDH-GVPETTQSLIQFVRTVRDYINRSPGA-GPTVVHCSAGVGRTGT 1916
Cdd:cd14634     78 IDEDIISRIFRICNMARpQDGYRIVQHLQYIGWPAYrDTPPSKRSILKVVRRLEKWQEQYDGReGRTVVHCLNGGGRSGT 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1725351434 1917 FVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 1961
Cdd:cd14634    158 FCAICSVCEMIQQQNIIDVFHTVKTLRNNKSNMVETLEQYKFVYE 202
R-PTP-G-2 cd17670
PTP-like domain of receptor-type tyrosine-protein phosphatase G, repeat 2; Receptor-type ...
 1760-1963 4.28e-26

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: 107.84  E-value: 4.28e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1760 YINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQcvEKGRVKCDH-YWPADQDPLYYGDLILQMVSE 1838
Cdd:cd17670      1 YINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPD--NQGLAEDEFvYWPSREESMNCEAFTVTLISK 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1839 SVL-----PEWTIREFkICSEEQLDAHRLLRHFHYTVWPDHGVP-ETTQSLIQFVRtvRDYINRSpgaGPTVVHCSAGVG 1912
Cdd:cd17670     79 DRLclsneEQIIIHDF-ILEATQDDYVLEVRHFQCPKWPNPDAPiSSTFELINVIK--EEALTRD---GPTIVHDEFGAV 152

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1725351434 1913 RTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 1963
Cdd:cd17670    153 SAGTLCALTTLSQQLENENAVDVYQVAKMINLMRPGVFTDIEQYQFLYKAM 203
R-PTPc-U-2 cd14637
PTP domain of receptor-type tyrosine-protein phosphatase U, repeat 2; Receptor-type ...
 1760-1963 8.60e-26

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: 106.92  E-value: 8.60e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1760 YINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRV-KCDHYWPaDQDPLYYGDLILQMVSE 1838
Cdd:cd14637      1 YINAALTDSYTRSAAFIVTLHPLQNTTTDFWRLVYDYGCTSVVMLNQLNQSNSAwPCLQYWP-EPGLQQYGPMEVEFVSG 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1839 SVLPEWTIREFKICSEEQL-DAHRLLRHFHYTVW-PDHGVPETTQSLIQFVRTVRDYiNRSPGAGPTVVHCSAGVGRTGT 1916
Cdd:cd14637     80 SADEDIVTRLFRVQNITRLqEGHLMVRHFQFLRWsAYRDTPDSKKAFLHLLASVEKW-QRESGEGRTVVHCLNGGGRSGT 158

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1725351434 1917 FVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 1963
Cdd:cd14637    159 YCASAMILEMIRCHNIVDVFYAVKTLRNYKPNMVETLEQYRFCYEIA 205
R-PTPc-K-2 cd14636
PTP domain of receptor-type tyrosine-protein phosphatase K, repeat 2; Receptor-type ...
 1760-1960 2.27e-25

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: 105.88  E-value: 2.27e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1760 YINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQC-VEKGrvkCDHYWPaDQDPLYYGDLILQMVSE 1838
Cdd:cd14636      1 YINAALMDSYRQPAAFIVTQHPLPNTVKDFWRLVYDYGCTSIVMLNEVdLAQG---CPQYWP-EEGMLRYGPIQVECMSC 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1839 SVLPEWTIREFKICS-EEQLDAHRLLRHFHYTVWPDH-GVPETTQSLIQFVRTVRDYINR-SPGAGPTVVHCSAGVGRTG 1915
Cdd:cd14636     77 SMDCDVISRIFRICNlTRPQEGYLMVQQFQYLGWASHrEVPGSKRSFLKLILQVEKWQEEcDEGEGRTIIHCLNGGGRSG 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1725351434 1916 TFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLH 1960
Cdd:cd14636    157 MFCAISIVCEMIKRQNVVDVFHAVKTLRNSKPNMVETPEQYRFCY 201
R-PTP-Z-2 cd17669
catalytic domain of receptor-type tyrosine-protein phosphatase Z, repeat 2; Receptor-type ...
 1760-1963 6.84e-25

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


Pssm-ID: 350507 [Multi-domain]  Cd Length: 204  Bit Score: 104.31  E-value: 6.84e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1760 YINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCdHYWPADQDPLYYGDLILQMVSE- 1838
Cdd:cd17669      1 YINASYIMGYYQSNEFIITQHPLLHTIKDFWRMIWDHNAQLIVMLPDGQNMAEDEF-VYWPNKDEPINCETFKVTLIAEe 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1839 ----SVLPEWTIREFkICSEEQLDAHRLLRHFHYTVWPDHGVP-ETTQSLIQFVRtvRDYINRSpgaGPTVVHCSAGVGR 1913
Cdd:cd17669     80 hkclSNEEKLIIQDF-ILEATQDDYVLEVRHFQCPKWPNPDSPiSKTFELISIIK--EEAANRD---GPMIVHDEHGGVT 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1914 TGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCV 1963
Cdd:cd17669    154 AGTFCALTTLMHQLEKENSVDVYQVAKMINLMRPGVFTDIEQYQFLYKAI 203
R-PTPc-M-2 cd14635
PTP domain of receptor-type tyrosine-protein phosphatase M, repeat 2; Receptor-type ...
 1760-1961 2.00e-24

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: 103.23  E-value: 2.00e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1760 YINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQcVEKGRVkCDHYWPaDQDPLYYGDLILQMVSES 1839
Cdd:cd14635      1 YINAALMDSYKQPSAFIVTQHPLPNTVKDFWRLVLDYHCTSIVMLND-VDPAQL-CPQYWP-ENGVHRHGPIQVEFVSAD 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1840 VLPEWTIREFKICSEEQ-LDAHRLLRHFHYTVWPDH-GVPETTQSLIQFVRTVRDYINRSPGA-GPTVVHCSAGVGRTGT 1916
Cdd:cd14635     78 LEEDIISRIFRIYNAARpQDGYRMVQQFQFLGWPMYrDTPVSKRSFLKLIRQVDKWQEEYNGGeGRTVVHCLNGGGRSGT 157

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1725351434 1917 FVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 1961
Cdd:cd14635    158 FCAISIVCEMLRHQRAVDVFHAVKTLRNNKPNMVDLLDQYKFCYE 202
PHA02740 PHA02740
protein tyrosine phosphatase; Provisional
 1686-1961 2.87e-14

protein tyrosine phosphatase; Provisional


Pssm-ID: 165107 [Multi-domain]  Cd Length: 298  Bit Score: 75.77  E-value: 2.87e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1686 IKINQFEGHFMKlqADSNYLLSKEYEDL---KDVGRSQSCDIAllpENRGKNRYN--NILPYDASRVKLCNVDDdpcsdY 1760
Cdd:PHA02740     9 INGMDFINFINK--PDLLSCIIKEYRAIvpeHEDEANKACAQA---ENKAKDENLalHITRLLHRRIKLFNDEK-----V 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1761 INASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKgrvKC-DHYWPADQDPL-YYGDLILQMVSE 1838
Cdd:PHA02740    79 LDARFVDGYDFEQKFICIINLCEDACDKFLQALSDNKVQIIVLISRHADK---KCfNQFWSLKEGCViTSDKFQIETLEI 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1839 SVLPEWTIREFKIcsEEQLDAHRLLRHFHYTVWPDHGVPETTQSLIQFVRTVRDY---INRSPG---AGPTVVHCSAGVG 1912
Cdd:PHA02740   156 IIKPHFNLTLLSL--TDKFGQAQKISHFQYTAWPADGFSHDPDAFIDFFCNIDDLcadLEKHKAdgkIAPIIIDCIDGIS 233

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1725351434 1913 RTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQ 1961
Cdd:PHA02740   234 SSAVFCVFDICATEFDKTGMLSIANALKKVRQKKYGCMNCLDDYVFCYH 282
fn3 pfam00041
Fibronectin type III domain;
1263-1345 5.28e-13

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 66.28  E-value: 5.28e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1263 SPPSLLSFADVANTSLAITWKGPPDWT-DYNDFELQWLPGDALTVFNPYSSKKSEGR-IVNGLRPGRSYQFSVKTVSGDS 1340
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPPDGNgPITGYEVEYRPKNSGEPWNEITVPGTTTSvTLTGLKPGTEYEVRVQAVNGGG 80


                   ....*
gi 1725351434 1341 WKTYS 1345
Cdd:pfam00041   81 EGPPS 85
CDC14 COG2453
Protein-tyrosine phosphatase [Signal transduction mechanisms];
1863-1961 1.12e-11

Protein-tyrosine phosphatase [Signal transduction mechanisms];


Pssm-ID: 441989 [Multi-domain]  Cd Length: 140  Bit Score: 64.22  E-value: 1.12e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1863 LRHFHYTvWPDHGVPETTQsLIQFVRTVRDYINRSpgaGPTVVHCSAGVGRTGTFVALDRILQQLDSKDsvdiygAVHDL 1942
Cdd:COG2453     48 LEYLHLP-IPDFGAPDDEQ-LQEAVDFIDEALREG---KKVLVHCRGGIGRTGTVAAAYLVLLGLSAEE------ALARV 116

                           90
                   ....*....|....*....
gi 1725351434 1943 RLHRVHMVQTECQYVYLHQ 1961
Cdd:COG2453    117 RAARPGAVETPAQRAFLER 135
fn3 pfam00041
Fibronectin type III domain;
1357-1436 7.87e-11

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 60.12  E-value: 7.87e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1357 DKIQNLHCRPQNSTAIACSWIPP---DSDFDGYSIECRKMDTQEIEFSRKLEKEKSLLNIMMLVPHRRYLVSIKVQSAGV 1433
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ...
gi 1725351434 1434 TSE 1436
Cdd:pfam00041   81 EGP 83
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
903-1293 8.34e-10

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 63.87  E-value: 8.34e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  903 EGLTVPSTVKNIHISANGATDRLTVTWSPGGGDVDSYVVSAFRQDEKVESHTLPKHGSEHTFHRLEAGATYRIAIVSVS- 981
Cdd:COG3401    135 AATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAATDt 214

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  982 ---GSLRNQIDVL-GQTVPASVHGVVADnAYSSNSLTVSWQKALGM-AERYDILLLSENGvllSNTSEPATVKQHKFED- 1055
Cdd:COG3401    215 ggeSAPSNEVSVTtPTTPPSAPTGLTAT-ADTPGSVTLSWDPVTESdATGYRVYRSNSGD---GPFTKVATVTTTSYTDt 290

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1056 -LTPGKKYKMQILTVSG----GLFSKEVE-TEGRTVPAAVTNLRITENSSRHLSFSWTASEGE-LSWYNIFLYNPDKTLQ 1128
Cdd:COG3401    291 gLTNGTTYYYRVTAVDAagneSAPSNVVSvTTDLTPPAAPSGLTATAVGSSSITLSWTASSDAdVTGYNVYRSTSGGGTY 370

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1129 ERAQVDPLVQSFSFQNLLQGRM--YKMVIVTHSGELSNESF-IFGRTVPAAV-NHLKGSNRNMTDSLWFSWSPASGDFDF 1204
Cdd:COG3401    371 TKIAETVTTTSYTDTGLTPGTTyyYKVTAVDAAGNESAPSEeVSATTASAASgESLTASVDAVPLTDVAGATAAASAASN 450

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1205 YELILYNPNGTKKENWREKDVTEWRFQGLIPGRKYTLYVVTHSGDLSNK-VTGEGRTAPSPPSLLSFADVANTSLAITWK 1283
Cdd:COG3401    451 PGVSAAVLADGGDTGNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGsGASSVTNSVSVIGASAAAAVGGAPDGTPNV 530

                          410
                   ....*....|
gi 1725351434 1284 GPPDWTDYND 1293
Cdd:COG3401    531 TGASPVTVGA 540
fn3 pfam00041
Fibronectin type III domain;
292-371 1.40e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 56.65  E-value: 1.40e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  292 EVSNLKVTSGGSlTSLNVKWQKPL---GVIDSYSITLSHQGTVKESK--TLPPRATEIQFKDLVPGRFYQVTIRCVSGEL 366
Cdd:pfam00041    2 APSNLTVTDVTS-TSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNeiTVPGTTTSVTLTGLKPGTEYEVRVQAVNGGG 80


                   ....*
gi 1725351434  367 SAEKS 371
Cdd:pfam00041   81 EGPPS 85
fn3 pfam00041
Fibronectin type III domain;
113-195 1.93e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 56.27  E-value: 1.93e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  113 PPARLEVNPerTTSTTLQVRWTPS---SGKVTWYEVQLFDQNNQKiQEVQVQESATWSQYTFLNLTAGSSYKIGITAVSG 189
Cdd:pfam00041    2 APSNLTVTD--VTSTSLTVSWTPPpdgNGPITGYEVEYRPKNSGE-PWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78


                   ....*.
gi 1725351434  190 GKRSFP 195
Cdd:pfam00041   79 GGEGPP 84
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 111-198 1.98e-09

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 56.35  E-value: 1.98e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  111 PLPPARLEVNPerTTSTTLQVRWTPSS---GKVTWYEVQLFDQNNQKIQEVQVQESATwSQYTFLNLTAGSSYKIGITAV 187
Cdd:cd00063      1 PSPPTNLRVTD--VTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSE-TSYTLTGLKPGTEYEFRVRAV 77

                           90
                   ....*....|.
gi 1725351434  188 SGGKRSFPVYT 198
Cdd:cd00063     78 NGGGESPPSES 88
PTP_YopH-like cd14559
YopH and related bacterial protein tyrosine phosphatases; Yersinia outer protein H (YopH) ...
 1866-1959 2.12e-09

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


Pssm-ID: 350407 [Multi-domain]  Cd Length: 227  Bit Score: 59.72  E-value: 2.12e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1866 FHYTVWPDHG-------------VPETTQSLIQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFVAldrILQQLDSKDS 1932
Cdd:cd14559    121 VHVTNWPDHTaisseglkeladlVNKSAEEKRNFYKSKGSSAINDKNKLLPVIHCRAGVGRTGQLAA---AMELNKSPNN 197

                           90       100
                   ....*....|....*....|....*...
gi 1725351434 1933 VDIYGAVHDLRLHR-VHMVQTECQYVYL 1959
Cdd:cd14559    198 LSVEDIVSDMRTSRnGKMVQKDEQLDTL 225
fn3 pfam00041
Fibronectin type III domain;
470-548 8.78e-09

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 54.34  E-value: 8.78e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  470 AVLQLRIKQANETSLGITWRAPL---GEWEKYTISL--MDRELFVIHKSLSKDAKEYTFTNLMPGRNYKATVTSMSGDLK 544
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYrpKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGE 81


                   ....
gi 1725351434  545 QSAS 548
Cdd:pfam00041   82 GPPS 85
fn3 pfam00041
Fibronectin type III domain;
733-809 1.38e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 53.57  E-value: 1.38e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  733 DKVQGISVSNsARSDYLKVSWVHAT---GDFDHYEVTIKNRDSF--IQTKSIPKSENECVFARLVPGRLYSITVTTKSGQ 807
Cdd:pfam00041    1 SAPSNLTVTD-VTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGepWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ..
gi 1725351434  808 YE 809
Cdd:pfam00041   80 GE 81
fn3 pfam00041
Fibronectin type III domain;
1176-1249 1.90e-08

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 53.19  E-value: 1.90e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1725351434 1176 AVNHLKGSNRNmTDSLWFSWSPA---SGDFDFYELILYNPNGTKKENWRE--KDVTEWRFQGLIPGRKYTLYVVTHSGD 1249
Cdd:pfam00041    2 APSNLTVTDVT-STSLTVSWTPPpdgNGPITGYEVEYRPKNSGEPWNEITvpGTTTSVTLTGLKPGTEYEVRVQAVNGG 79
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
81-336 3.12e-08

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 58.86  E-value: 3.12e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434   81 DPKDLQAGTIYNFRIVSLDGEERS--------LVLQTDPLPPARLEVNPerTTSTTLQVRWTPSSGK-VTWYEVQLFDQN 151
Cdd:COG3401    195 GGGDIEPGTTYYYRVAATDTGGESapsnevsvTTPTTPPSAPTGLTATA--DTPGSVTLSWDPVTESdATGYRVYRSNSG 272

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  152 NQKIQEVqvqESATWSQYTFLNLTAGSSYKIGITAV-SGGKRSFP-----VYTNGSTGPSPVEDIGISPNPNSLLISWSR 225
Cdd:COG3401    273 DGPFTKV---ATVTTTSYTDTGLTNGTTYYYRVTAVdAAGNESAPsnvvsVTTDLTPPAAPSGLTATAVGSSSITLSWTA 349

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  226 GPGNVEQFRLMLMDKGAIVQDTNVDK--RDTSYAFRGLTPGHLYNVTIVTMASGLQNSrwklgrTAPMEVSNLKVTSGGS 303
Cdd:COG3401    350 SSDADVTGYNVYRSTSGGGTYTKIAEtvTTTSYTDTGLTPGTTYYYKVTAVDAAGNES------APSEEVSATTASAASG 423

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1725351434  304 LTSLNVKWQKPLGVIDSYSITLSHQGTVKESKT 336
Cdd:COG3401    424 ESLTASVDAVPLTDVAGATAAASAASNPGVSAA 456
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
636-1022 5.21e-08

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 58.09  E-value: 5.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  636 VVAEGRTVPSSVSGVTVNNSGRNDYLSVSWLPAPGEVHHYVVTLSHDSKVVQSLITAKFVSECSFSSLTPGRLYNVTITT 715
Cdd:COG3401    132 AGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTTYYYRVAA 211

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  716 KSGNYES-----HSFSEERTVPDKVQGISVSnSARSDYLKVSWV-HATGDFDHYEVTIKNRDSFIQTKSIPKSENECVFA 789
Cdd:COG3401    212 TDTGGESapsneVSVTTPTTPPSAPTGLTAT-ADTPGSVTLSWDpVTESDATGYRVYRSNSGDGPFTKVATVTTTSYTDT 290

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  790 RLVPGRLYSITVTTKSGQYEASEQ------GTGRTIPEPVKNLTLLNRSTEDLHVTWS-RANGDVDQYEVQLLFNDMKVF 862
Cdd:COG3401    291 GLTNGTTYYYRVTAVDAAGNESAPsnvvsvTTDLTPPAAPSGLTATAVGSSSITLSWTaSSDADVTGYNVYRSTSGGGTY 370

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  863 PPIYLVNTATEYQFSALTPGRHYKILVL-------------TISGDVQQPAFIEGLTVPSTVKNIHISAnGATDRLTVTW 929
Cdd:COG3401    371 TKIAETVTTTSYTDTGLTPGTTYYYKVTavdaagnesapseEVSATTASAASGESLTASVDAVPLTDVA-GATAAASAAS 449

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  930 SPGGGDVDSYVV----SAFRQDEKVESHTLPKHGSEHTFHRLEAGATYRIAIVSVSGSLRNQIDVLGQTVPASVHGVVAd 1005
Cdd:COG3401    450 NPGVSAAVLADGgdtgNAVPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTP- 528

                          410
                   ....*....|....*..
gi 1725351434 1006 NAYSSNSLTVSWQKALG 1022
Cdd:COG3401    529 NVTGASPVTVGASTGDV 545
PTP_DSP_cys cd14494
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
 1885-1961 5.26e-08

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: 53.12  E-value: 5.26e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1885 QFVRTVRDYINR--SPGaGPTVVHCSAGVGRTGTFVALDRILQQLDS-KDSVDIYGavhdlRLHRVHMVQTECQYVYLHQ 1961
Cdd:cd14494     40 AMVDRFLEVLDQaeKPG-EPVLVHCKAGVGRTGTLVACYLVLLGGMSaEEAVRIVR-----LIRPGGIPQTIEQLDFLIK 113
CDKN3-like cd14505
cyclin-dependent kinase inhibitor 3 and similar proteins; This family is composed of ...
 1852-1961 2.66e-07

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


Pssm-ID: 350355 [Multi-domain]  Cd Length: 163  Bit Score: 52.27  E-value: 2.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1852 CSEEQLDAHRL-----------LRHFHYTVwPDHGVPETTQsliQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFVAl 1920
Cdd:cd14505     51 CTDGELEELGVpdlleqyqqagITWHHLPI-PDGGVPSDIA---QWQELLEELLSALENGKKVLIHCKGGLGRTGLIAA- 125

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1725351434 1921 dRILQQLDSKDSVDiyGAVHDLRLHRVHMVQTECQYVYLHQ 1961
Cdd:cd14505    126 -CLLLELGDTLDPE--QAIAAVRALRPGAIQTPKQENFLHQ 163
fn3 pfam00041
Fibronectin type III domain;
1088-1161 2.76e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 50.11  E-value: 2.76e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1725351434 1088 AVTNLRITENSSRHLSFSWTASE---GELSWYNIFLYNPDKTLQERAQVDPLVQ-SFSFQNLLQGRMYKMVIVTHSGE 1161
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNEITVPGTTtSVTLTGLKPGTEYEVRVQAVNGG 79
PTP_VSP_TPTE cd14510
protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase ...
 1849-1960 4.16e-07

protein tyrosine phosphatase-like catalytic domain of voltage-sensitive phosphatase/transmembrane phosphatase with tensin homology; Voltage-sensitive phosphatase (VSP) proteins comprise a family of phosphoinositide phosphatases with substrates that include phosphatidylinositol-4,5-diphosphate and phosphatidylinositol-3,4,5-trisphosphate. This family is conserved in deuterostomes; VSP was first identified as a sperm flagellar plasma membrane protein in Ciona intestinalis. Gene duplication events in primates resulted in the presence of paralogs, transmembrane phosphatase with tensin homology (TPTE) and TPTE2, that retain protein domain architecture but, in the case of TPTE, have lost catalytic activity. TPTE, also called cancer/testis antigen 44 (CT44), may play a role in the signal transduction pathways of the endocrine or spermatogenic function of the testis. TPTE2, also called TPTE and PTEN homologous inositol lipid phosphatase (TPIP), occurs in several differentially spliced forms; TPIP alpha displays phosphoinositide 3-phosphatase activity and is localized on the endoplasmic reticulum, while TPIP beta is cytosolic and lacks detectable phosphatase activity. VSP/TPTE proteins contain an N-terminal voltage sensor consisting of four transmembrane segments, a protein tyrosine phosphatase (PTP)-like phosphoinositide phosphatase catalytic domain, followed by a regulatory C2 domain.


Pssm-ID: 350360 [Multi-domain]  Cd Length: 177  Bit Score: 51.98  E-value: 4.16e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1849 FKICSEEQLDAhrllRHFHYTV----WPDHGVPeTTQSLIQFVRTVRDYINRSPgAGPTVVHCSAGVGRTGTFVA--LDR 1922
Cdd:cd14510     59 YNLCSERGYDP----KYFHNRVervpIDDHNVP-TLDEMLSFTAEVREWMAADP-KNVVAIHCKGGKGRTGTMVCawLIY 132

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1725351434 1923 ILQQLDSKDSVDIYGAVH-DLRL-HRVHMVQTECQYVYLH 1960
Cdd:cd14510    133 SGQFESAKEALEYFGERRtDKSVsSKFQGVETPSQSRYVG 172
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1262-1349 6.70e-07

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 49.03  E-value: 6.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1262 PSPPSLLSFADVANTSLAITWKGPPDWTDYND-FELQWLPGDALTVFNPYSSKKSEGR-IVNGLRPGRSYQFSVKTVSGD 1339
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDGGPITgYVVEYREKGSGDWKEVEVTPGSETSyTLTGLKPGTEYEFRVRAVNGG 80

                           90
                   ....*....|
gi 1725351434 1340 SWKTYSKPIS 1349
Cdd:cd00063     81 GESPPSESVT 90
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1356-1444 7.03e-07

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 49.03  E-value: 7.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1356 PDKIQNLHCRPQNSTAIACSWIPPDSD---FDGYSIECRKMDTQEIEFSRKLEKEKSLLNIMMLVPHRRYLVSIKVQSAG 1432
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEDDggpITGYVVEYREKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                           90
                   ....*....|..
gi 1725351434 1433 VTSEVVEDSTIT 1444
Cdd:cd00063     81 GESPPSESVTVT 92
fn3 pfam00041
Fibronectin type III domain;
822-895 9.10e-07

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 48.57  E-value: 9.10e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1725351434  822 PVKNLTLLNRSTEDLHVTWSRA---NGDVDQYEVQLL-FNDMKVFPPIYLVNTATEYQFSALTPGRHYKILVLTISGD 895
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPpdgNGPITGYEVEYRpKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
1159-1389 9.80e-07

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 53.85  E-value: 9.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1159 SGELSNESFIFGRTVPAAVNHLKGSNRNMTDSLWFSWSPASGDFDFYELILYNPNGTKKENWREKDVTEWRFQGLIPGRK 1238
Cdd:COG3401    125 ATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVDGGGDIEPGTT 204

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1239 YTLYVVTHS----GDLSNKVTG-EGRTAPSPPSLLSFADVANTSLAITWKGPPDwtdyndfelqwlpgDALTVFNPYSSK 1313
Cdd:COG3401    205 YYYRVAATDtggeSAPSNEVSVtTPTTPPSAPTGLTATADTPGSVTLSWDPVTE--------------SDATGYRVYRSN 270

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1314 KSEGR------------IVNGLRPGRSYQFSVKTVSGDSWK-TYSKPISGSV-RTKPDKIQNLHCRPQNSTAIACSWIP- 1378
Cdd:COG3401    271 SGDGPftkvatvtttsyTDTGLTNGTTYYYRVTAVDAAGNEsAPSNVVSVTTdLTPPAAPSGLTATAVGSSSITLSWTAs 350

                          250
                   ....*....|.
gi 1725351434 1379 PDSDFDGYSIE 1389
Cdd:COG3401    351 SDADVTGYNVY 361
PTP_PTEN cd14509
protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; ...
 1852-1938 1.37e-06

protein tyrosine phosphatase-like catalytic domain of phosphatase and tensin homolog; Phosphatase and tensin homolog (PTEN), also phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN or mutated in multiple advanced cancers 1 (MMAC1), is a tumor suppressor that acts as a dual-specificity protein phosphatase and as a lipid phosphatase. It is a critical endogenous inhibitor of phosphoinositide signaling. It dephosphorylates phosphoinositide trisphosphate, and therefore, has the function of negatively regulating Akt. The PTEN/PI3K/AKT pathway regulates the signaling of multiple biological processes such as apoptosis, metabolism, cell proliferation, and cell growth. PTEN contains an N-terminal PIP-binding domain, a protein tyrosine phosphatase (PTP)-like catalytic domain, a regulatory C2 domain responsible for its cellular location, a C-tail containing phosphorylation sites, and a C-terminal PDZ domain.


Pssm-ID: 350359 [Multi-domain]  Cd Length: 158  Bit Score: 50.28  E-value: 1.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1852 CSEEQLDAHRllrhFHYTV----WPDHGVPeTTQSLIQFVRTVRDYINRSPGAgPTVVHCSAGVGRTGTFVA--LDRILQ 1925
Cdd:cd14509     48 CSERSYDPSK----FNGRVaeypFDDHNPP-PLELIKPFCEDVDEWLKEDEKN-VAAVHCKAGKGRTGVMICcyLLYLGK 121

                           90
                   ....*....|...
gi 1725351434 1926 QLDSKDSVDIYGA 1938
Cdd:cd14509    122 FPSAKEALDFYGA 134
fn3 pfam00041
Fibronectin type III domain;
909-982 1.57e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 47.79  E-value: 1.57e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1725351434  909 STVKNIHISANGATDrLTVTWSP---GGGDVDSYVVSAFRQDEKVESH--TLPKHGSEHTFHRLEAGATYRIAIVSVSG 982
Cdd:pfam00041    1 SAPSNLTVTDVTSTS-LTVSWTPppdGNGPITGYEVEYRPKNSGEPWNeiTVPGTTTSVTLTGLKPGTEYEVRVQAVNG 78
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 111-193 2.06e-06

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 47.61  E-value: 2.06e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434   111 PLPPARLEVnpERTTSTTLQVRWT-PSSGKVTWYEVQLFDQNNQK-IQEVQVQESATWSQYTFLNLTAGSSYKIGITAVS 188
Cdd:smart00060    1 PSPPSNLRV--TDVTSTSVTLSWEpPPDDGITGYIVGYRVEYREEgSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVN 78


                    ....*
gi 1725351434   189 GGKRS 193
Cdd:smart00060   79 GAGEG 83
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 290-365 2.25e-06

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 47.88  E-value: 2.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  290 PMEVSNLKVTSGGSlTSLNVKWQKPL---GVIDSYSITLS--HQGTVKESKTLPPRATEIQFKDLVPGRFYQVTIRCVSG 364
Cdd:cd00063      1 PSPPTNLRVTDVTS-TSVTLSWTPPEddgGPITGYVVEYRekGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNG 79


                   .
gi 1725351434  365 E 365
Cdd:cd00063     80 G 80
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1262-1341 4.20e-06

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 46.45  E-value: 4.20e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  1262 PSPPSLLSFADVANTSLAITWKGPPD--WTDYND-FELQWLPGDALTVFNPYSSKKSEGrIVNGLRPGRSYQFSVKTVSG 1338
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDdgITGYIVgYRVEYREEGSEWKEVNVTPSSTSY-TLTGLKPGTEYEFRVRAVNG 79


                    ...
gi 1725351434  1339 DSW 1341
Cdd:smart00060   80 AGE 82
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 204-273 6.03e-06

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 46.07  E-value: 6.03e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1725351434   204 PSPVEDIGISP-NPNSLLISWSRGPGN-----VEQFRLMLMDKGAIVQDTNVDKRDTSYAFRGLTPGHLYNVTIVT 273
Cdd:smart00060    1 PSPPSNLRVTDvTSTSVTLSWEPPPDDgitgyIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRA 76
fn3 pfam00041
Fibronectin type III domain;
1009-1077 7.89e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 45.87  E-value: 7.89e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1725351434 1009 SSNSLTVSWQKAL---GMAERYDILLLSENGVLLSNT-SEPATVKQHKFEDLTPGKKYKMQILTVSGGLFSKE 1077
Cdd:pfam00041   12 TSTSLTVSWTPPPdgnGPITGYEVEYRPKNSGEPWNEiTVPGTTTSVTLTGLKPGTEYEVRVQAVNGGGEGPP 84
fn3 pfam00041
Fibronectin type III domain;
394-455 8.29e-06

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 45.87  E-value: 8.29e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1725351434  394 SFAVNWTPPA---GDWDHYRILLF--NDSLVLLNTTVGKEETHFALEGLEliPGRQYEVEVIVESGN 455
Cdd:pfam00041   15 SLTVSWTPPPdgnGPITGYEVEYRpkNSGEPWNEITVPGTTTSVTLTGLK--PGTEYEVRVQAVNGG 79
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 290-364 8.75e-06

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 45.68  E-value: 8.75e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434   290 PMEVSNLKVTSGGSlTSLNVKWQKP-----LGVIDSYSITLSHQGTVKESKTLPPRATEIQFKDLVPGRFYQVTIRCVSG 364
Cdd:smart00060    1 PSPPSNLRVTDVTS-TSVTLSWEPPpddgiTGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79
fn3 pfam00041
Fibronectin type III domain;
645-723 1.14e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 45.48  E-value: 1.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  645 SSVSGVTVNNSGrNDYLSVSWLPAP---GEVHHYVVTLSH--DSKVVQSLITAKFVSECSFSSLTPGRLYNVTITTKSGN 719
Cdd:pfam00041    1 SAPSNLTVTDVT-STSLTVSWTPPPdgnGPITGYEVEYRPknSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQAVNGG 79


                   ....
gi 1725351434  720 YESH 723
Cdd:pfam00041   80 GEGP 83
fn3 pfam00041
Fibronectin type III domain;
205-273 3.10e-05

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 44.33  E-value: 3.10e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1725351434  205 SPVEDIGISP-NPNSLLISWSR---GPGNVEQFRLML--MDKGAIVQDTNVDKRDTSYAFRGLTPGHLYNVTIVT 273
Cdd:pfam00041    1 SAPSNLTVTDvTSTSLTVSWTPppdGNGPITGYEVEYrpKNSGEPWNEITVPGTTTSVTLTGLKPGTEYEVRVQA 75
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 732-818 1.46e-04

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 42.48  E-value: 1.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  732 PDKVQGISVSNSaRSDYLKVSWVHATGD---FDHYEVTIK--NRDSFIQTKSIPKSENECVFARLVPGRLYSITVT--TK 804
Cdd:cd00063      1 PSPPTNLRVTDV-TSTSVTLSWTPPEDDggpITGYVVEYRekGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRavNG 79

                           90
                   ....*....|....
gi 1725351434  805 SGQYEASEQGTGRT 818
Cdd:cd00063     80 GGESPPSESVTVTT 93
DUSP23 cd14504
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ...
 1857-1919 1.73e-04

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


Pssm-ID: 350354 [Multi-domain]  Cd Length: 142  Bit Score: 43.81  E-value: 1.73e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1725351434 1857 LDAHRLLRHFHYTVwPDHGVPeTTQSLIQFVRTVRDYINRSpgaGPTVVHCSAGVGRTGTFVA 1919
Cdd:cd14504     44 SDTCPGLRYHHIPI-EDYTPP-TLEQIDEFLDIVEEANAKN---EAVLVHCLAGKGRTGTMLA 101
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 468-553 2.79e-04

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 41.71  E-value: 2.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  468 PLAVLQLRIKQANETSLGITWRAPL---GEWEKYTISL--MDRELFVIHKSLSKDAKEYTFTNLMPGRNYKATVTSMSGD 542
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYreKGSGDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRAVNGG 80

                           90
                   ....*....|...
gi 1725351434  543 L--KQSASIQGRT 553
Cdd:cd00063     81 GesPPSESVTVTT 93
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 644-731 2.96e-04

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 41.71  E-value: 2.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  644 PSSVSGVTVNNSGRnDYLSVSWLPAP---GEVHHYVVTLSHDSKVVQSLITAKFVSECSF--SSLTPGRLYNVTITTKSG 718
Cdd:cd00063      1 PSPPTNLRVTDVTS-TSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGSETSYtlTGLKPGTEYEFRVRAVNG 79

                           90
                   ....*....|...
gi 1725351434  719 NYEShSFSEERTV 731
Cdd:cd00063     80 GGES-PPSESVTV 91
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 204-272 3.17e-04

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 41.71  E-value: 3.17e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1725351434  204 PSPVEDIGISP-NPNSLLISWSRGP---GNVEQFRLMLMDKGA--IVQDTNVDKRDTSYAFRGLTPGHLYNVTIV 272
Cdd:cd00063      1 PSPPTNLRVTDvTSTSVTLSWTPPEddgGPITGYVVEYREKGSgdWKEVEVTPGSETSYTLTGLKPGTEYEFRVR 75
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 908-982 3.86e-04

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 41.06  E-value: 3.86e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434   908 PSTVKNIHISANGATdRLTVTWSP-----GGGDVDSYVVSAFRQDEKVESHTLPKHGSEHTFHRLEAGATYRIAIVSVSG 982
Cdd:smart00060    1 PSPPSNLRVTDVTST-SVTLSWEPppddgITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
1151-1352 4.26e-04

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 45.38  E-value: 4.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1151 YKMVIVTHSGE--LSNE-SFIFGRTVPAAVNHLKGSNrNMTDSLWFSWSPASG-DFDFYElILYNPNGtkKENWR---EK 1223
Cdd:COG3401    207 YRVAATDTGGEsaPSNEvSVTTPTTPPSAPTGLTATA-DTPGSVTLSWDPVTEsDATGYR-VYRSNSG--DGPFTkvaTV 282

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1224 DVTEWRFQGLIPGRKYTLYVVTH-----SGDLSNKVTGE-GRTAPSPPSLLSFADVANTSLAITWKGPPDwtdyndfelq 1297
Cdd:COG3401    283 TTTSYTDTGLTNGTTYYYRVTAVdaagnESAPSNVVSVTtDLTPPAAPSGLTATAVGSSSITLSWTASSD---------- 352

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1725351434 1298 wlpgDALTVFNPYSSKKSEGR-------------IVNGLRPGRSYQFSVKTV-SGDSWKTYSKPISGSV 1352
Cdd:COG3401    353 ----ADVTGYNVYRSTSGGGTytkiaetvtttsyTDTGLTPGTTYYYKVTAVdAAGNESAPSEEVSATT 417
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
117-306 4.41e-04

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 45.32  E-value: 4.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  117 LEVNPERTTSTTLQVRWTPSSGKVTwYEVQLFDQNNqkiqEVQVQESATWSQYTFLNLTAGsSYKIGITAVS-GGKRSFP 195
Cdd:COG4733    542 LSVVAQGTAVTTLTVSWDAPAGAVA-YEVEWRRDDG----NWVSVPRTSGTSFEVPGIYAG-DYEVRVRAINaLGVSSAW 615

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  196 VYT-----NGSTG-PSPVEDIGISPNPNSLLISWSRGPG-NVEQFRLMLMDKGAIvQDTNVDK---RDTSYAFRGLTPGH 265
Cdd:COG4733    616 AASsettvTGKTApPPAPTGLTATGGLGGITLSWSFPVDaDTLRTEIRYSTTGDW-ASATVAQalyPGNTYTLAGLKAGQ 694

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1725351434  266 LYNVTIVTM-ASGLQNSRWKLGRTAPMEVSNLKVTSGGSLTS 306
Cdd:COG4733    695 TYYYRARAVdRSGNVSAWWVSGQASADAAGILDAITGQILET 736
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 468-541 5.50e-04

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 40.68  E-value: 5.50e-04
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1725351434   468 PLAVLQLRIKQANETSLGITWRAP-----LGEWEKYTISLMDRELFVIHKSLSKDAKEYTFTNLMPGRNYKATVTSMSG 541
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPpddgiTGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79
TpbA-like cd14529
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ...
 1865-1944 6.03e-04

bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa TpbA; This subfamily contains bacterial protein tyrosine phosphatases (PTPs) and dual-specificity phosphatases (DUSPs) related to Pseudomonas aeruginosa TpbA, a DUSP that negatively regulates biofilm formation by converting extracellular quorum sensing signals and to Mycobacterium tuberculosis PtpB, a PTP virulence factor that attenuates host immune defenses by interfering with signal transduction pathways in macrophages. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides, while DUSPs function as protein-serine/threonine phosphatases (EC 3.1.3.16) and PTPs.


Pssm-ID: 350378 [Multi-domain]  Cd Length: 158  Bit Score: 42.36  E-value: 6.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1865 HFHYTVWPDHGVPETTQSLIQFVRTVRDYINRspgaGPTVVHCSAGVGRTGTFVALDRILQQLDSKDsvdiygAVHDLRL 1944
Cdd:cd14529     58 GVKYVNLPLSATRPTESDVQSFLLIMDLKLAP----GPVLIHCKHGKDRTGLVSALYRIVYGGSKEE------ANEDYRL 127
DSPc smart00195
Dual specificity phosphatase, catalytic domain;
1865-1943 6.12e-04

Dual specificity phosphatase, catalytic domain;


Pssm-ID: 214551 [Multi-domain]  Cd Length: 138  Bit Score: 41.88  E-value: 6.12e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  1865 HFHYTVWPdhgVPETTQSLI-QFVRTVRDYINRS-PGAGPTVVHCSAGVGRTGTFVAldRILQQLDSKDSVDIYGAVHDL 1942
Cdd:smart00195   44 DFTYLGVP---IDDNTETKIsPYFPEAVEFIEDAeSKGGKVLVHCQAGVSRSATLII--AYLMKTRNMSLNDAYDFVKDR 118


                    .
gi 1725351434  1943 R 1943
Cdd:smart00195  119 R 119
COG4733 COG4733
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
1190-1340 6.57e-04

Phage-related protein, tail protein J [Mobilome: prophages, transposons];


Pssm-ID: 443767 [Multi-domain]  Cd Length: 978  Bit Score: 44.94  E-value: 6.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1190 SLWFSWSPASGDFDfYELILYNPNGtkkeNWR---EKDVTEWRFQGLIPGRkYTLYVVTHS--GDLSN-----KVTGEGR 1259
Cdd:COG4733    553 TLTVSWDAPAGAVA-YEVEWRRDDG----NWVsvpRTSGTSFEVPGIYAGD-YEVRVRAINalGVSSAwaassETTVTGK 626

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1260 TAPsPPSLLSF-ADVANTSLAITWKGPPDwTDYNDFELQWLP----GDALTVFNPYSSKKSegrIVNGLRPGRSYQFSVK 1334
Cdd:COG4733    627 TAP-PPAPTGLtATGGLGGITLSWSFPVD-ADTLRTEIRYSTtgdwASATVAQALYPGNTY---TLAGLKAGQTYYYRAR 701


                   ....*...
gi 1725351434 1335 TV--SGDS 1340
Cdd:COG4733    702 AVdrSGNV 709
PTP_PTEN-like cd14497
protein tyrosine phosphatase-like domain of phosphatase and tensin homolog and similar ...
 1853-1919 1.22e-03

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


Pssm-ID: 350347 [Multi-domain]  Cd Length: 160  Bit Score: 41.41  E-value: 1.22e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1725351434 1853 SEEQLDAHRLLRHF--HYTvWPDHGVPeTTQSLIQFVRTVRDYINRSPG--AgptVVHCSAGVGRTGTFVA 1919
Cdd:cd14497     49 SEEEYDDDSKFEGRvlHYG-FPDHHPP-PLGLLLEIVDDIDSWLSEDPNnvA---VVHCKAGKGRTGTVIC 114
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 644-722 1.30e-03

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 39.52  E-value: 1.30e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434   644 PSSVSGVTVNNSGRNdYLSVSWLPAP-----GEVHHYVVTLSHDSKVVQSLITAKFVSECSFSSLTPGRLYNVTITTKSG 718
Cdd:smart00060    1 PSPPSNLRVTDVTST-SVTLSWEPPPddgitGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79


                    ....
gi 1725351434   719 NYES 722
Cdd:smart00060   80 AGEG 83
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
244-742 1.33e-03

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 43.84  E-value: 1.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  244 VQDTNVDKRDTSYAFRGLTPGHLYNVTIVTMASGLQNSRWKLGRTAPMEVSNLKVTSGGSLTSLNVKWQKPLGVIDSYSI 323
Cdd:COG3401     13 IAASAAANTAVNALSKAGGSGKTILVYLAVVLSVTTKESPGTLLVAAGLSSGGGLGTGGRAGTTSGVAAVAVAAAPPTAT 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  324 TLSHQGTVKESKTLPPRATEIQFKDLVPGRFYqvtircvSGELSAEKSAMGRTVPEKVSNLVSYNEIWMKSFAVNWTPPA 403
Cdd:COG3401     93 GLTTLTGSGSVGGATNTGLTSSDEVPSPAVGT-------ATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAG 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  404 GDWDHYRILLFNDSLVLLNTTVGKEEThfALEGLELIPGRQYE--VEVIVESGNLRNSERC---QGRTVPLAVLQLRIKQ 478
Cdd:COG3401    166 AGVVVSPDTSATAAVATTSLTVTSTTL--VDGGGDIEPGTTYYyrVAATDTGGESAPSNEVsvtTPTTPPSAPTGLTATA 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  479 ANETSLGITWRAPlgewekytiSLMDRELFVIHKSLSKDAK----------EYTFTNLMPGRNYKATVTSMSGDLKQSA- 547
Cdd:COG3401    244 DTPGSVTLSWDPV---------TESDATGYRVYRSNSGDGPftkvatvtttSYTDTGLTNGTTYYYRVTAVDAAGNESAp 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  548 ----SIQ-GRTVPAQVTDLEVSNQGMTS-SLftNWTKALG-DVEFYQVL----------LIHENVvvknesvssDSSWYS 610
Cdd:COG3401    315 snvvSVTtDLTPPAAPSGLTATAVGSSSiTL--SWTASSDaDVTGYNVYrstsgggtytKIAETV---------TTTSYT 383

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  611 FRALRSGSLYSVVVTTV-SGGI---PSRQVVAEGRTVPSSVSGVTVNNSGRNDyLSVSWLPAPGEVHHYVVT-----LSH 681
Cdd:COG3401    384 DTGLTPGTTYYYKVTAVdAAGNesaPSEEVSATTASAASGESLTASVDAVPLT-DVAGATAAASAASNPGVSaavlaDGG 462

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1725351434  682 DSKVVqSLITAKFVSECSFSSLTPGRLYNVTITTKSGNYESHSFSEERTVPDKVQGISVSN 742
Cdd:COG3401    463 DTGNA-VPFTTTSSTVTATTTDTTTANLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGG 522
FN3 COG3401
Fibronectin type 3 domain [General function prediction only];
1235-1389 1.44e-03

Fibronectin type 3 domain [General function prediction only];


Pssm-ID: 442628 [Multi-domain]  Cd Length: 603  Bit Score: 43.45  E-value: 1.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1235 PGRKYTLYVVTHSGDLSNKVTGEGRTAPSPPSLLSFADVANTSLAITWKGPPDW-----TDYNDFELQWLPGDALTVFNP 1309
Cdd:COG3401    106 ATNTGLTSSDEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTassvaGAGVVVSPDTSATAAVATTSL 185

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1310 YSSKKSEGRIVNGLRPGRSYQFSVKTVSGDSWKTYSKPISGSV-RTKPDKIQNLHCRPQNSTAIACSWIP-PDSDFDGYS 1387
Cdd:COG3401    186 TVTSTTLVDGGGDIEPGTTYYYRVAATDTGGESAPSNEVSVTTpTTPPSAPTGLTATADTPGSVTLSWDPvTESDATGYR 265


                   ..
gi 1725351434 1388 IE 1389
Cdd:COG3401    266 VY 267
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1174-1266 2.77e-03

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 39.02  E-value: 2.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1174 PAAVNHLKGSNRNmTDSLWFSWSPASGD---FDFYELILYNPNGTKKENWREKDV--TEWRFQGLIPGRKYTLYVVThsg 1248
Cdd:cd00063      1 PSPPTNLRVTDVT-STSVTLSWTPPEDDggpITGYVVEYREKGSGDWKEVEVTPGseTSYTLTGLKPGTEYEFRVRA--- 76

                           90
                   ....*....|....*...
gi 1725351434 1249 dlsnkVTGEGRTAPSPPS 1266
Cdd:cd00063     77 -----VNGGGESPPSESV 89
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 1086-1161 2.90e-03

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 39.02  E-value: 2.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434 1086 PAAVTNLRITENSSRHLSFSWTASE---GELSWYNIFLYNPDKTLQERAQVDPL-VQSFSFQNLLQGRMYKMVIVTHSGE 1161
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPEddgGPITGYVVEYREKGSGDWKEVEVTPGsETSYTLTGLKPGTEYEFRVRAVNGG 80
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 732-807 5.08e-03

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 37.98  E-value: 5.08e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434   732 PDKVQGISVSNSArSDYLKVSWVH-----ATGDFDHYEVTIKNRDSFIQTKSIPKSENECVFARLVPGRLYSITVTTKSG 806
Cdd:smart00060    1 PSPPSNLRVTDVT-STSVTLSWEPppddgITGYIVGYRVEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79


                    .
gi 1725351434   807 Q 807
Cdd:smart00060   80 A 80
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1086-1160 6.06e-03

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 37.59  E-value: 6.06e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1725351434  1086 PAAVTNLRITENSSRHLSFSWTASEGE-LSWYNIF---LYNPDKTLQERAQVDPLVQSFSFQNLLQGRMYKMVIVTHSG 1160
Cdd:smart00060    1 PSPPSNLRVTDVTSTSVTLSWEPPPDDgITGYIVGyrvEYREEGSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAVNG 79
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 1174-1248 7.23e-03

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


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 37.59  E-value: 7.23e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  1174 PAAVNHLKGSNRNmTDSLWFSWSPASGDFDFYELILYNP-NGTKKENWREKDV----TEWRFQGLIPGRKYTLYVVTHSG 1248
Cdd:smart00060    1 PSPPSNLRVTDVT-STSVTLSWEPPPDDGITGYIVGYRVeYREEGSEWKEVNVtpssTSYTLTGLKPGTEYEFRVRAVNG 79
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 820-895 8.01e-03

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


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 37.48  E-value: 8.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725351434  820 PEPVKNLTLLNRSTEDLHVTWSRA---NGDVDQYEVQL---LFNDMKVFPPiyLVNTATEYQFSALTPGRHYKILVLTIS 893
Cdd:cd00063      1 PSPPTNLRVTDVTSTSVTLSWTPPeddGGPITGYVVEYrekGSGDWKEVEV--TPGSETSYTLTGLKPGTEYEFRVRAVN 78


                   ..
gi 1725351434  894 GD 895
Cdd:cd00063     79 GG 80
 
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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