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Conserved domains on  [gi|578816124|ref|XP_006716685|]
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thyroglobulin isoform X1 [Homo sapiens]

Protein Classification

TY and COesterase domain-containing protein( domain architecture ID 10828663)

protein containing domains TY, Ephrin_rec_like, and COesterase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COesterase pfam00135
Carboxylesterase family;
2176-2697 2.22e-175

Carboxylesterase family;


:

Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 549.60  E-value: 2.22e-175
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124  2176 SVPSVPISThGRLLGRSQAIQVGtswKQVDQFLGVPYAAPPLAERRFQAPEPL-NWTGSWDASKPRASCWQPGTRTSTSP 2254
Cdd:pfam00135    1 DSPVVTTSL-GRVRGKRLKVDGG---KPVYAFLGIPYAEPPVGELRFQPPEPPePWTGVRDATKFGPRCPQNGDLTSPGS 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124  2255 ---GVSEDCLYLNVFIPQNVAPNA---SVLVFFHNTMDREESegWPAIDGSFLAAVGNLIVVTASYRVGVFGFLSSGSGE 2328
Cdd:pfam00135   77 sglEGSEDCLYLNVYTPKELKENKnklPVMVWIHGGGFMFGS--GSLYDGSYLAAEGDVIVVTINYRLGPLGFLSTGDDE 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124  2329 VSGNWGLLDQVAALTWVQTHIRGFGGDPRRVSLAADRGGADVASIHLLTARAtnSQLFRRAVLMGGSALSPAAVISHERa 2408
Cdd:pfam00135  155 APGNYGLLDQVLALRWVQENIASFGGDPNRVTLFGESAGAASVSLLLLSPLS--KGLFHRAILMSGSALSPWAIQSNAR- 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124  2409 qQQAIALAKEVSCPMSSSQEVVSCLRQKPANVLNDAQTKLL-AVSGPFHYWGPVIDGHFLREPPARALKRSLWVEVDLLI 2487
Cdd:pfam00135  232 -QRAKELAKLVGCPTSDSAELVECLRSKPAEELLDAQLKLLvYGSVPFVPFGPVVDGDFLPEHPEELLKSGNFPKVPLLI 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124  2488 GSSQDDGLINRA------KAVKQFEESRGRTSSKTAFYQALqnslggEDSDARVEAAATWYYSLEHSTDDYASFSRALEN 2561
Cdd:pfam00135  311 GVTKDEGLLFAAyildnvDILKALEEKLLRSLLIDLLYLLL------VDLPEEISAALREEYLDWGDRDDPETSRRALVE 384

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124  2562 ATRDYFIICPIIDMASAWAKRaRGNVFMYH---------APENYG--HGSlellaDVQFALGLPFYPAYEgqFSLEEKSL 2630
Cdd:pfam00135  385 LLTDYLFNCPVIRFADLHASR-GTPVYMYSfdyrgsslrYPKWVGvdHGD-----ELPYVFGTPFVGALL--FTEEDEKL 456

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578816124  2631 SLKIMQYFSHFIRSGNPNYpyefsrkvPTFATPWPDFVPraggENYKEFSELLPNR--QGLKKADCSFW 2697
Cdd:pfam00135  457 SRKMMTYWTNFAKTGNPNG--------PEGLPKWPPYTD----ENGQYLSIDLEPRvkQGLKAERCAFW 513
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 95-160 8.02e-22

Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases


:

Pssm-ID: 238114  Cd Length: 66  Bit Score: 90.99  E-value: 8.02e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578816124   95 FCQLQKQQILLSGYINSTDTSYLPQCQDSGDYAPVQCDVQQVQCWCVDAEGMEVYGTRQLGRPKRC 160
Cdd:cd00191     1 PCERERASALESLAGPKLSGLYVPQCDEDGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRGGPPNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 300-358 7.05e-19

Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases


:

Pssm-ID: 238114  Cd Length: 66  Bit Score: 82.51  E-value: 7.05e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578816124  300 KCEVERFTATS------FGHPYVPSCRRNGDYQAVQCQTE-GPCWCVDAQGKEMHGTRQQGEPPSC 358
Cdd:cd00191     1 PCERERASALEslagpkLSGLYVPQCDEDGNYEPVQCHGStGYCWCVDPDGEEIPGTRTRGGPPNC 66
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 662-724 1.64e-18

Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the control of proteolytic degradation. The domain usually contains six conserved cysteines. These form three disulphide bridges. Cysteines 1 pairs with 2, 3 with 4 and 5 with 6.


:

Pssm-ID: 459665  Cd Length: 66  Bit Score: 81.58  E-value: 1.64e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578816124   662 CEKQRARMQSLMGSQPAGSTLFVPACTSEGHFLPVQCFNS--ECYCVDAEGQAIPGTRSAIGKPK 724
Cdd:pfam00086    1 CERERARALEQAASGRPASGLYIPNCDEDGFYKPVQCHGStgYCWCVDPEGQEIPGTRTRGGDPD 65
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1149-1210 2.81e-18

Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases


:

Pssm-ID: 238114  Cd Length: 66  Bit Score: 80.97  E-value: 2.81e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578816124 1149 CNVLKSGVLSRRVSPG----YVPACRaEDGGFSPVQCDQAQGSCWCVMDSGEEVPGTRVTGGQPAC 1210
Cdd:cd00191     2 CERERASALESLAGPKlsglYVPQCD-EDGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRGGPPNC 66
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 599-658 6.40e-18

Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the control of proteolytic degradation. The domain usually contains six conserved cysteines. These form three disulphide bridges. Cysteines 1 pairs with 2, 3 with 4 and 5 with 6.


:

Pssm-ID: 459665  Cd Length: 66  Bit Score: 80.04  E-value: 6.40e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578816124   599 METVLSSQTCEQTPERLFVPSCTTEGSYEDVQCFS--GECWCVNSWGKELPGSRVRGGQPRC 658
Cdd:pfam00086    5 RARALEQAASGRPASGLYIPNCDEDGFYKPVQCHGstGYCWCVDPEGQEIPGTRTRGGDPDC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 33-92 1.69e-17

Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases


:

Pssm-ID: 238114  Cd Length: 66  Bit Score: 78.66  E-value: 1.69e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578816124   33 PCELQRETAFLKQA------DYVPQCAEDGSFQTVQCQNDGRSCWCVGANGSEVLGSRQPGRPVAC 92
Cdd:cd00191     1 PCERERASALESLAgpklsgLYVPQCDEDGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRGGPPNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1004-1073 4.89e-17

Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases


:

Pssm-ID: 238114  Cd Length: 66  Bit Score: 77.50  E-value: 4.89e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124 1004 FYQRRRFSPDDSAgaSALLRSGPYMPQCDAFGSWEPVQCHAGTGHCWCVDEKGGFIPGSLTARslQIPQC 1073
Cdd:cd00191     1 PCERERASALESL--AGPKLSGLYVPQCDEDGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRG--GPPNC 66
Ephrin_rec_like pfam07699
Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region ...
 1465-1510 7.67e-15

Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region rich in cysteines. It is found in various ephrin type A and B receptors, which have tyrosine kinase activity.


:

Pssm-ID: 429604 [Multi-domain]  Cd Length: 48  Bit Score: 70.46  E-value: 7.67e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 578816124  1465 GSYSQDE--ECIPCPVGFYQEQAGSLACVPCPVGRTTISAGAFSQTHC 1510
Cdd:pfam07699    1 GTYSNTGlePCIPCPRGTYQPEEGQLSCLACPLGTTTDSPGATSISDC 48
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1520-1567 2.82e-08

Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases and binding partners of heparin.


:

Pssm-ID: 214561  Cd Length: 46  Bit Score: 51.99  E-value: 2.82e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 578816124   1520 GLQCDQNGQYRASQKDRGSGKAFCVDGEGRRLPWweTEAPLEDSQCLM 1567
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSSGQCWCVDATGREIPG--TRTEGGDPDCPS 46
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1077-1145 4.07e-05

Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases


:

Pssm-ID: 238114  Cd Length: 66  Bit Score: 43.61  E-value: 4.07e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578816124 1077 CEKSRTSGLLSSwkqarsqENPSPKDLFVPACLETGEYARLQ--ASGAGTWCVDPAsGEELrPGSSS---SAQC 1145
Cdd:cd00191     2 CERERASALESL-------AGPKLSGLYVPQCDEDGNYEPVQchGSTGYCWCVDPD-GEEI-PGTRTrggPPNC 66
TY super family cl00150
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 892-922 1.05e-03

Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases


The actual alignment was detected with superfamily member smart00211:

Pssm-ID: 469630  Cd Length: 46  Bit Score: 38.90  E-value: 1.05e-03
                            10        20        30
                    ....*....|....*....|....*....|.
gi 578816124    892 HFDLRNCWCVDEAGQELEGMRSEPSKlPTCP 922
Cdd:smart00211   16 DGSSGQCWCVDATGREIPGTRTEGGD-PDCP 45
TY super family cl00150
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 730-776 3.90e-03

Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases


The actual alignment was detected with superfamily member pfam00086:

Pssm-ID: 469630  Cd Length: 66  Bit Score: 38.05  E-value: 3.90e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 578816124   730 CQLQSEQAflrtvqaLLSNSSMLPtLSDTYIPQCSTDGQWRQVQCNG 776
Cdd:pfam00086    1 CERERARA-------LEQAASGRP-ASGLYIPNCDEDGFYKPVQCHG 39
 
Name Accession Description Interval E-value
COesterase pfam00135
Carboxylesterase family;
2176-2697 2.22e-175

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 549.60  E-value: 2.22e-175
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124  2176 SVPSVPISThGRLLGRSQAIQVGtswKQVDQFLGVPYAAPPLAERRFQAPEPL-NWTGSWDASKPRASCWQPGTRTSTSP 2254
Cdd:pfam00135    1 DSPVVTTSL-GRVRGKRLKVDGG---KPVYAFLGIPYAEPPVGELRFQPPEPPePWTGVRDATKFGPRCPQNGDLTSPGS 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124  2255 ---GVSEDCLYLNVFIPQNVAPNA---SVLVFFHNTMDREESegWPAIDGSFLAAVGNLIVVTASYRVGVFGFLSSGSGE 2328
Cdd:pfam00135   77 sglEGSEDCLYLNVYTPKELKENKnklPVMVWIHGGGFMFGS--GSLYDGSYLAAEGDVIVVTINYRLGPLGFLSTGDDE 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124  2329 VSGNWGLLDQVAALTWVQTHIRGFGGDPRRVSLAADRGGADVASIHLLTARAtnSQLFRRAVLMGGSALSPAAVISHERa 2408
Cdd:pfam00135  155 APGNYGLLDQVLALRWVQENIASFGGDPNRVTLFGESAGAASVSLLLLSPLS--KGLFHRAILMSGSALSPWAIQSNAR- 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124  2409 qQQAIALAKEVSCPMSSSQEVVSCLRQKPANVLNDAQTKLL-AVSGPFHYWGPVIDGHFLREPPARALKRSLWVEVDLLI 2487
Cdd:pfam00135  232 -QRAKELAKLVGCPTSDSAELVECLRSKPAEELLDAQLKLLvYGSVPFVPFGPVVDGDFLPEHPEELLKSGNFPKVPLLI 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124  2488 GSSQDDGLINRA------KAVKQFEESRGRTSSKTAFYQALqnslggEDSDARVEAAATWYYSLEHSTDDYASFSRALEN 2561
Cdd:pfam00135  311 GVTKDEGLLFAAyildnvDILKALEEKLLRSLLIDLLYLLL------VDLPEEISAALREEYLDWGDRDDPETSRRALVE 384

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124  2562 ATRDYFIICPIIDMASAWAKRaRGNVFMYH---------APENYG--HGSlellaDVQFALGLPFYPAYEgqFSLEEKSL 2630
Cdd:pfam00135  385 LLTDYLFNCPVIRFADLHASR-GTPVYMYSfdyrgsslrYPKWVGvdHGD-----ELPYVFGTPFVGALL--FTEEDEKL 456

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578816124  2631 SLKIMQYFSHFIRSGNPNYpyefsrkvPTFATPWPDFVPraggENYKEFSELLPNR--QGLKKADCSFW 2697
Cdd:pfam00135  457 SRKMMTYWTNFAKTGNPNG--------PEGLPKWPPYTD----ENGQYLSIDLEPRvkQGLKAERCAFW 513
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
2184-2672 1.34e-94

Carboxylesterase type B [Lipid transport and metabolism];


Pssm-ID: 441873  Cd Length: 500  Bit Score: 316.83  E-value: 1.34e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124 2184 THGRLLGRSQAiqvgtswkQVDQFLGVPYAAPPLAERRFQAPEPL-NWTGSWDASKPRASCWQPGTRTST--SPGVSEDC 2260
Cdd:COG2272    18 EAGRVRGVVEG--------GVRVFLGIPYAAPPVGELRWRAPQPVePWTGVRDATEFGPACPQPPRPGDPggPAPGSEDC 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124 2261 LYLNVFIPqNVAPNAS--VLVFFH---NTMdreeseGWPAI---DGSFLAAVGnLIVVTASYRVGVFGF-----LSSGSG 2327
Cdd:COG2272    90 LYLNVWTP-ALAAGAKlpVMVWIHgggFVS------GSGSEplyDGAALARRG-VVVVTINYRLGALGFlalpaLSGESY 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124 2328 EVSGNWGLLDQVAALTWVQTHIRGFGGDPRRVSLA---AdrGGADVASihLLTARATNSqLFRRAVLMGGSALSPAaviS 2404
Cdd:COG2272   162 GASGNYGLLDQIAALRWVRDNIAAFGGDPDNVTIFgesA--GAASVAA--LLASPLAKG-LFHRAIAQSGAGLSVL---T 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124 2405 HERAQQQAIALAKEVSCPMSSsqevVSCLRQKPANVLNDAQTKLLAVSGPFHYWGPVIDGHFLREPPARALKRSLWVEVD 2484
Cdd:COG2272   234 LAEAEAVGAAFAAALGVAPAT----LAALRALPAEELLAAQAALAAEGPGGLPFGPVVDGDVLPEDPLEAFAAGRAADVP 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124 2485 LLIGSSQDDGLINRAKAVKQFEESRGRtssktafYQALQNSLGGEDSDARVEAaatwyyslehstddY--ASFSRALENA 2562
Cdd:COG2272   310 LLIGTNRDEGRLFAALLGDLGPLTAAD-------YRAALRRRFGDDADEVLAA--------------YpaASPAEALAAL 368

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124 2563 TRDYFIICPIIDMASAWAkRARGNVFMY---HAPENYG-------HGslellADVQFALGLPFYPAYEGqFSLEEKSLSL 2632
Cdd:COG2272   369 ATDRVFRCPARRLAEAHA-AAGAPVYLYrfdWRSPPLRgfglgafHG-----AELPFVFGNLDAPALTG-LTPADRALSD 441

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 578816124 2633 KIMQYFSHFIRSGNPNYPYefsrkvptfATPWPDFVPRAG 2672
Cdd:COG2272   442 QMQAYWVNFARTGDPNGPG---------LPEWPAYDPEDR 472
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 2204-2676 1.09e-92

Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on carboxylic esters (EC: 3.1.1.-). The catalytic apparatus involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine.These catalytic residues are responsible for the nucleophilic attack on the carbonyl carbon atom of the ester bond. In contrast with other alpha/beta hydrolase fold family members, p-nitrobenzyl esterase and acetylcholine esterase have a Glu instead of Asp at the active site carboxylate.


Pssm-ID: 238191 [Multi-domain]  Cd Length: 493  Bit Score: 311.19  E-value: 1.09e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124 2204 VDQFLGVPYAAPPLAERRFQAPEPLN-WTGSWDASKPRASC-----WQPGTRTSTSPGvSEDCLYLNVFIPQNVAPNAS- 2276
Cdd:cd00312    17 VYSFLGIPYAEPPVGDLRFKEPQPYEpWSDVLDATSYPPSCmqwdqLGGGLWNAKLPG-SEDCLYLNVYTPKNTKPGNSl 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124 2277 -VLVFFHntmdreeSEGW----PAIDG--SFLAAVGNLIVVTASYRVGVFGFLSSGSGEVSGNWGLLDQVAALTWVQTHI 2349
Cdd:cd00312    96 pVMVWIH-------GGGFmfgsGSLYPgdGLAREGDNVIVVSINYRLGVLGFLSTGDIELPGNYGLKDQRLALKWVQDNI 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124 2350 RGFGGDPRRVSLAADRGGAdvASIHLLTARATNSQLFRRAVLMGGSALSPAAVisHERAQQQAIALAKEVSCPMSSSQEV 2429
Cdd:cd00312   169 AAFGGDPDSVTIFGESAGG--ASVSLLLLSPDSKGLFHRAISQSGSALSPWAI--QENARGRAKRLARLLGCNDTSSAEL 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124 2430 VSCLRQKPANVLNDAQTKLLAVSG-PFHYWGPVIDGHFLREPPARALKRSLWVEVDLLIGSSQDDGLINRAKAVKQFEES 2508
Cdd:cd00312   245 LDCLRSKSAEELLDATRKLLLFSYsPFLPFGPVVDGDFIPDDPEELIKEGKFAKVPLIIGVTKDEGGYFAAMLLNFDAKL 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124 2509 RGRTSskTAFYQALQNSLGGEDsDARVEAAATWYY-SLEHSTDDYASFSRALEnatrDYFIICPIIDMASAWAKRARGNV 2587
Cdd:cd00312   325 IIETN--DRWLELLPYLLFYAD-DALADKVLEKYPgDVDDSVESRKNLSDMLT----DLLFKCPARYFLAQHRKAGGSPV 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124 2588 FMYH-----------APENYG--HGSlellaDVQFALGLPFypaYEGQFSLEEKSLSLKIMQYFSHFIRSGNPNypYEFS 2654
Cdd:cd00312   398 YAYVfdhrsslsvgrWPPWLGtvHGD-----EIFFVFGNPL---LKEGLREEEEKLSRTMMKYWANFAKTGNPN--TEGN 467

                         490       500
                  ....*....|....*....|..
gi 578816124 2655 RKVptfatpWPDFVprAGGENY 2676
Cdd:cd00312   468 LVV------WPAYT--SESEKY 481
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 95-160 8.02e-22

Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases


Pssm-ID: 238114  Cd Length: 66  Bit Score: 90.99  E-value: 8.02e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578816124   95 FCQLQKQQILLSGYINSTDTSYLPQCQDSGDYAPVQCDVQQVQCWCVDAEGMEVYGTRQLGRPKRC 160
Cdd:cd00191     1 PCERERASALESLAGPKLSGLYVPQCDEDGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRGGPPNC 66
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 96-160 6.61e-19

Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the control of proteolytic degradation. The domain usually contains six conserved cysteines. These form three disulphide bridges. Cysteines 1 pairs with 2, 3 with 4 and 5 with 6.


Pssm-ID: 459665  Cd Length: 66  Bit Score: 82.74  E-value: 6.61e-19
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578816124    96 CQLQKQQILLS-GYINSTDTSYLPQCQDSGDYAPVQCDVQQVQCWCVDAEGMEVYGTRQLGRPKRC 160
Cdd:pfam00086    1 CERERARALEQaASGRPASGLYIPNCDEDGFYKPVQCHGSTGYCWCVDPEGQEIPGTRTRGGDPDC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 300-358 7.05e-19

Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases


Pssm-ID: 238114  Cd Length: 66  Bit Score: 82.51  E-value: 7.05e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578816124  300 KCEVERFTATS------FGHPYVPSCRRNGDYQAVQCQTE-GPCWCVDAQGKEMHGTRQQGEPPSC 358
Cdd:cd00191     1 PCERERASALEslagpkLSGLYVPQCDEDGNYEPVQCHGStGYCWCVDPDGEEIPGTRTRGGPPNC 66
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 662-724 1.64e-18

Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the control of proteolytic degradation. The domain usually contains six conserved cysteines. These form three disulphide bridges. Cysteines 1 pairs with 2, 3 with 4 and 5 with 6.


Pssm-ID: 459665  Cd Length: 66  Bit Score: 81.58  E-value: 1.64e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578816124   662 CEKQRARMQSLMGSQPAGSTLFVPACTSEGHFLPVQCFNS--ECYCVDAEGQAIPGTRSAIGKPK 724
Cdd:pfam00086    1 CERERARALEQAASGRPASGLYIPNCDEDGFYKPVQCHGStgYCWCVDPEGQEIPGTRTRGGDPD 65
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1149-1210 2.81e-18

Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases


Pssm-ID: 238114  Cd Length: 66  Bit Score: 80.97  E-value: 2.81e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578816124 1149 CNVLKSGVLSRRVSPG----YVPACRaEDGGFSPVQCDQAQGSCWCVMDSGEEVPGTRVTGGQPAC 1210
Cdd:cd00191     2 CERERASALESLAGPKlsglYVPQCD-EDGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRGGPPNC 66
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 599-658 6.40e-18

Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the control of proteolytic degradation. The domain usually contains six conserved cysteines. These form three disulphide bridges. Cysteines 1 pairs with 2, 3 with 4 and 5 with 6.


Pssm-ID: 459665  Cd Length: 66  Bit Score: 80.04  E-value: 6.40e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578816124   599 METVLSSQTCEQTPERLFVPSCTTEGSYEDVQCFS--GECWCVNSWGKELPGSRVRGGQPRC 658
Cdd:pfam00086    5 RARALEQAASGRPASGLYIPNCDEDGFYKPVQCHGstGYCWCVDPEGQEIPGTRTRGGDPDC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 33-92 1.69e-17

Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases


Pssm-ID: 238114  Cd Length: 66  Bit Score: 78.66  E-value: 1.69e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578816124   33 PCELQRETAFLKQA------DYVPQCAEDGSFQTVQCQNDGRSCWCVGANGSEVLGSRQPGRPVAC 92
Cdd:cd00191     1 PCERERASALESLAgpklsgLYVPQCDEDGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRGGPPNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 612-658 1.88e-17

Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases


Pssm-ID: 238114  Cd Length: 66  Bit Score: 78.66  E-value: 1.88e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 578816124  612 PERLFVPSCTTEGSYEDVQCFS--GECWCVNSWGKELPGSRVRGGQPRC 658
Cdd:cd00191    18 LSGLYVPQCDEDGNYEPVQCHGstGYCWCVDPDGEEIPGTRTRGGPPNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 662-724 3.58e-17

Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases


Pssm-ID: 238114  Cd Length: 66  Bit Score: 77.89  E-value: 3.58e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578816124  662 CEKQRARMQSLMgSQPAGSTLFVPACTSEGHFLPVQCFNS--ECYCVDAEGQAIPGTRSAIGKPK 724
Cdd:cd00191     2 CERERASALESL-AGPKLSGLYVPQCDEDGNYEPVQCHGStgYCWCVDPDGEEIPGTRTRGGPPN 65
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1004-1073 4.89e-17

Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases


Pssm-ID: 238114  Cd Length: 66  Bit Score: 77.50  E-value: 4.89e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124 1004 FYQRRRFSPDDSAgaSALLRSGPYMPQCDAFGSWEPVQCHAGTGHCWCVDEKGGFIPGSLTARslQIPQC 1073
Cdd:cd00191     1 PCERERASALESL--AGPKLSGLYVPQCDEDGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRG--GPPNC 66
Ephrin_rec_like pfam07699
Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region ...
 1465-1510 7.67e-15

Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region rich in cysteines. It is found in various ephrin type A and B receptors, which have tyrosine kinase activity.


Pssm-ID: 429604 [Multi-domain]  Cd Length: 48  Bit Score: 70.46  E-value: 7.67e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 578816124  1465 GSYSQDE--ECIPCPVGFYQEQAGSLACVPCPVGRTTISAGAFSQTHC 1510
Cdd:pfam07699    1 GTYSNTGlePCIPCPRGTYQPEEGQLSCLACPLGTTTDSPGATSISDC 48
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 1151-1210 9.05e-15

Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the control of proteolytic degradation. The domain usually contains six conserved cysteines. These form three disulphide bridges. Cysteines 1 pairs with 2, 3 with 4 and 5 with 6.


Pssm-ID: 459665  Cd Length: 66  Bit Score: 70.79  E-value: 9.05e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124  1151 VLKSGVLSRRVSPGYVPACRaEDGGFSPVQCDQAQGSCWCVMDSGEEVPGTRVTGGQPAC 1210
Cdd:pfam00086    8 ALEQAASGRPASGLYIPNCD-EDGFYKPVQCHGSTGYCWCVDPEGQEIPGTRTRGGDPDC 66
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 1024-1073 1.19e-14

Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the control of proteolytic degradation. The domain usually contains six conserved cysteines. These form three disulphide bridges. Cysteines 1 pairs with 2, 3 with 4 and 5 with 6.


Pssm-ID: 459665  Cd Length: 66  Bit Score: 70.79  E-value: 1.19e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 578816124  1024 SGPYMPQCDAFGSWEPVQCHAGTGHCWCVDEKGGFIPGSLTARSlqIPQC 1073
Cdd:pfam00086   19 SGLYIPNCDEDGFYKPVQCHGSTGYCWCVDPEGQEIPGTRTRGG--DPDC 66
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 117-162 4.15e-14

Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases and binding partners of heparin.


Pssm-ID: 214561  Cd Length: 46  Bit Score: 68.56  E-value: 4.15e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 578816124    117 LPQCQDSGDYAPVQCDVQQVQCWCVDAEGMEVYGTRQLGRPKRCPR 162
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSSGQCWCVDATGREIPGTRTEGGDPDCPS 46
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 301-358 4.48e-14

Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the control of proteolytic degradation. The domain usually contains six conserved cysteines. These form three disulphide bridges. Cysteines 1 pairs with 2, 3 with 4 and 5 with 6.


Pssm-ID: 459665  Cd Length: 66  Bit Score: 68.87  E-value: 4.48e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578816124   301 CEVERFTA---TSFGHP----YVPSCRRNGDYQAVQCQTE-GPCWCVDAQGKEMHGTRQQGEPPSC 358
Cdd:pfam00086    1 CERERARAleqAASGRPasglYIPNCDEDGFYKPVQCHGStGYCWCVDPEGQEIPGTRTRGGDPDC 66
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1166-1212 5.67e-14

Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases and binding partners of heparin.


Pssm-ID: 214561  Cd Length: 46  Bit Score: 68.17  E-value: 5.67e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 578816124   1166 VPACRaEDGGFSPVQCDQAQGSCWCVMDSGEEVPGTRVTGGQPACES 1212
Cdd:smart00211    1 IPQCD-EDGNYEPVQCDGSSGQCWCVDATGREIPGTRTEGGDPDCPS 46
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 34-92 7.38e-13

Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the control of proteolytic degradation. The domain usually contains six conserved cysteines. These form three disulphide bridges. Cysteines 1 pairs with 2, 3 with 4 and 5 with 6.


Pssm-ID: 459665  Cd Length: 66  Bit Score: 65.40  E-value: 7.38e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578816124    34 CELQRETAFLKQAD-------YVPQCAEDGSFQTVQCQNDGRSCWCVGANGSEVLGSRQPGRPVAC 92
Cdd:pfam00086    1 CERERARALEQAASgrpasglYIPNCDEDGFYKPVQCHGSTGYCWCVDPEGQEIPGTRTRGGDPDC 66
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 316-360 1.02e-12

Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases and binding partners of heparin.


Pssm-ID: 214561  Cd Length: 46  Bit Score: 64.71  E-value: 1.02e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 578816124    316 VPSCRRNGDYQAVQCQTE-GPCWCVDAQGKEMHGTRQQGEPPSCAE 360
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSsGQCWCVDATGREIPGTRTEGGDPDCPS 46
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 49-94 1.18e-12

Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases and binding partners of heparin.


Pssm-ID: 214561  Cd Length: 46  Bit Score: 64.32  E-value: 1.18e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 578816124     49 VPQCAEDGSFQTVQCQNDGRSCWCVGANGSEVLGSRQPGRPVACLS 94
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSSGQCWCVDATGREIPGTRTEGGDPDCPS 46
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1028-1075 1.54e-12

Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases and binding partners of heparin.


Pssm-ID: 214561  Cd Length: 46  Bit Score: 63.94  E-value: 1.54e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 578816124   1028 MPQCDAFGSWEPVQCHAGTGHCWCVDEKGGFIPGSLTARSlqIPQCPT 1075
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSSGQCWCVDATGREIPGTRTEGG--DPDCPS 46
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 617-660 3.04e-12

Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases and binding partners of heparin.


Pssm-ID: 214561  Cd Length: 46  Bit Score: 63.17  E-value: 3.04e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 578816124    617 VPSCTTEGSYEDVQCF--SGECWCVNSWGKELPGSRVRGGQPRCPT 660
Cdd:smart00211    1 IPQCDEDGNYEPVQCDgsSGQCWCVDATGREIPGTRTEGGDPDCPS 46
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 684-728 5.39e-11

Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases and binding partners of heparin.


Pssm-ID: 214561  Cd Length: 46  Bit Score: 59.70  E-value: 5.39e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 578816124    684 VPACTSEGHFLPVQCFNS--ECYCVDAEGQAIPGTRSAIGKPkKCPT 728
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSsgQCWCVDATGREIPGTRTEGGDP-DCPS 46
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1520-1567 2.82e-08

Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases and binding partners of heparin.


Pssm-ID: 214561  Cd Length: 46  Bit Score: 51.99  E-value: 2.82e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 578816124   1520 GLQCDQNGQYRASQKDRGSGKAFCVDGEGRRLPWweTEAPLEDSQCLM 1567
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSSGQCWCVDATGREIPG--TRTEGGDPDCPS 46
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1077-1145 4.07e-05

Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases


Pssm-ID: 238114  Cd Length: 66  Bit Score: 43.61  E-value: 4.07e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578816124 1077 CEKSRTSGLLSSwkqarsqENPSPKDLFVPACLETGEYARLQ--ASGAGTWCVDPAsGEELrPGSSS---SAQC 1145
Cdd:cd00191     2 CERERASALESL-------AGPKLSGLYVPQCDEDGNYEPVQchGSTGYCWCVDPD-GEEI-PGTRTrggPPNC 66
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 892-922 1.05e-03

Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases and binding partners of heparin.


Pssm-ID: 214561  Cd Length: 46  Bit Score: 38.90  E-value: 1.05e-03
                            10        20        30
                    ....*....|....*....|....*....|.
gi 578816124    892 HFDLRNCWCVDEAGQELEGMRSEPSKlPTCP 922
Cdd:smart00211   16 DGSSGQCWCVDATGREIPGTRTEGGD-PDCP 45
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 730-776 3.90e-03

Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the control of proteolytic degradation. The domain usually contains six conserved cysteines. These form three disulphide bridges. Cysteines 1 pairs with 2, 3 with 4 and 5 with 6.


Pssm-ID: 459665  Cd Length: 66  Bit Score: 38.05  E-value: 3.90e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 578816124   730 CQLQSEQAflrtvqaLLSNSSMLPtLSDTYIPQCSTDGQWRQVQCNG 776
Cdd:pfam00086    1 CERERARA-------LEQAASGRP-ASGLYIPNCDEDGFYKPVQCHG 39
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 1522-1552 4.10e-03

Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the control of proteolytic degradation. The domain usually contains six conserved cysteines. These form three disulphide bridges. Cysteines 1 pairs with 2, 3 with 4 and 5 with 6.


Pssm-ID: 459665  Cd Length: 66  Bit Score: 38.05  E-value: 4.10e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 578816124  1522 QCDQNGQYRASQKDRGSGKAFCVDGEGRRLP 1552
Cdd:pfam00086   25 NCDEDGFYKPVQCHGSTGYCWCVDPEGQEIP 55
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 729-776 4.42e-03

Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases


Pssm-ID: 238114  Cd Length: 66  Bit Score: 37.83  E-value: 4.42e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 578816124  729 PCQLQSEQAFLRTVQALLSNSsmlptlsdtYIPQCSTDGQWRQVQCNG 776
Cdd:cd00191     1 PCERERASALESLAGPKLSGL---------YVPQCDEDGNYEPVQCHG 39
TNFRSF16 cd13416
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ...
 1440-1493 4.95e-03

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


Pssm-ID: 276921 [Multi-domain]  Cd Length: 159  Bit Score: 39.98  E-value: 4.95e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578816124 1440 CSEGFYQvltSEASQDGLGCVKCPEGSY-------SQDEECIPCPVGFYQEQAGSL-ACVPC 1493
Cdd:cd13416    80 CAYGYYL---DEDSGTCEPCTVCPPGQGvvqscgpNQDTVCEACPEGTYSDEDSSTdPCLPC 138
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 892-921 6.36e-03

Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases


Pssm-ID: 238114  Cd Length: 66  Bit Score: 37.44  E-value: 6.36e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 578816124  892 HFDLRNCWCVDEAGQELEGMRSEPSKlPTC 921
Cdd:cd00191    38 HGSTGYCWCVDPDGEEIPGTRTRGGP-PNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1522-1565 6.68e-03

Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases


Pssm-ID: 238114  Cd Length: 66  Bit Score: 37.44  E-value: 6.68e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 578816124 1522 QCDQNGQYRASQKDRGSGKAFCVDGEGRRLPwwETEAPLEDSQC 1565
Cdd:cd00191    25 QCDEDGNYEPVQCHGSTGYCWCVDPDGEEIP--GTRTRGGPPNC 66
 
Name Accession Description Interval E-value
COesterase pfam00135
Carboxylesterase family;
2176-2697 2.22e-175

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 549.60  E-value: 2.22e-175
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124  2176 SVPSVPISThGRLLGRSQAIQVGtswKQVDQFLGVPYAAPPLAERRFQAPEPL-NWTGSWDASKPRASCWQPGTRTSTSP 2254
Cdd:pfam00135    1 DSPVVTTSL-GRVRGKRLKVDGG---KPVYAFLGIPYAEPPVGELRFQPPEPPePWTGVRDATKFGPRCPQNGDLTSPGS 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124  2255 ---GVSEDCLYLNVFIPQNVAPNA---SVLVFFHNTMDREESegWPAIDGSFLAAVGNLIVVTASYRVGVFGFLSSGSGE 2328
Cdd:pfam00135   77 sglEGSEDCLYLNVYTPKELKENKnklPVMVWIHGGGFMFGS--GSLYDGSYLAAEGDVIVVTINYRLGPLGFLSTGDDE 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124  2329 VSGNWGLLDQVAALTWVQTHIRGFGGDPRRVSLAADRGGADVASIHLLTARAtnSQLFRRAVLMGGSALSPAAVISHERa 2408
Cdd:pfam00135  155 APGNYGLLDQVLALRWVQENIASFGGDPNRVTLFGESAGAASVSLLLLSPLS--KGLFHRAILMSGSALSPWAIQSNAR- 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124  2409 qQQAIALAKEVSCPMSSSQEVVSCLRQKPANVLNDAQTKLL-AVSGPFHYWGPVIDGHFLREPPARALKRSLWVEVDLLI 2487
Cdd:pfam00135  232 -QRAKELAKLVGCPTSDSAELVECLRSKPAEELLDAQLKLLvYGSVPFVPFGPVVDGDFLPEHPEELLKSGNFPKVPLLI 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124  2488 GSSQDDGLINRA------KAVKQFEESRGRTSSKTAFYQALqnslggEDSDARVEAAATWYYSLEHSTDDYASFSRALEN 2561
Cdd:pfam00135  311 GVTKDEGLLFAAyildnvDILKALEEKLLRSLLIDLLYLLL------VDLPEEISAALREEYLDWGDRDDPETSRRALVE 384

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124  2562 ATRDYFIICPIIDMASAWAKRaRGNVFMYH---------APENYG--HGSlellaDVQFALGLPFYPAYEgqFSLEEKSL 2630
Cdd:pfam00135  385 LLTDYLFNCPVIRFADLHASR-GTPVYMYSfdyrgsslrYPKWVGvdHGD-----ELPYVFGTPFVGALL--FTEEDEKL 456

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578816124  2631 SLKIMQYFSHFIRSGNPNYpyefsrkvPTFATPWPDFVPraggENYKEFSELLPNR--QGLKKADCSFW 2697
Cdd:pfam00135  457 SRKMMTYWTNFAKTGNPNG--------PEGLPKWPPYTD----ENGQYLSIDLEPRvkQGLKAERCAFW 513
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
2184-2672 1.34e-94

Carboxylesterase type B [Lipid transport and metabolism];


Pssm-ID: 441873  Cd Length: 500  Bit Score: 316.83  E-value: 1.34e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124 2184 THGRLLGRSQAiqvgtswkQVDQFLGVPYAAPPLAERRFQAPEPL-NWTGSWDASKPRASCWQPGTRTST--SPGVSEDC 2260
Cdd:COG2272    18 EAGRVRGVVEG--------GVRVFLGIPYAAPPVGELRWRAPQPVePWTGVRDATEFGPACPQPPRPGDPggPAPGSEDC 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124 2261 LYLNVFIPqNVAPNAS--VLVFFH---NTMdreeseGWPAI---DGSFLAAVGnLIVVTASYRVGVFGF-----LSSGSG 2327
Cdd:COG2272    90 LYLNVWTP-ALAAGAKlpVMVWIHgggFVS------GSGSEplyDGAALARRG-VVVVTINYRLGALGFlalpaLSGESY 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124 2328 EVSGNWGLLDQVAALTWVQTHIRGFGGDPRRVSLA---AdrGGADVASihLLTARATNSqLFRRAVLMGGSALSPAaviS 2404
Cdd:COG2272   162 GASGNYGLLDQIAALRWVRDNIAAFGGDPDNVTIFgesA--GAASVAA--LLASPLAKG-LFHRAIAQSGAGLSVL---T 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124 2405 HERAQQQAIALAKEVSCPMSSsqevVSCLRQKPANVLNDAQTKLLAVSGPFHYWGPVIDGHFLREPPARALKRSLWVEVD 2484
Cdd:COG2272   234 LAEAEAVGAAFAAALGVAPAT----LAALRALPAEELLAAQAALAAEGPGGLPFGPVVDGDVLPEDPLEAFAAGRAADVP 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124 2485 LLIGSSQDDGLINRAKAVKQFEESRGRtssktafYQALQNSLGGEDSDARVEAaatwyyslehstddY--ASFSRALENA 2562
Cdd:COG2272   310 LLIGTNRDEGRLFAALLGDLGPLTAAD-------YRAALRRRFGDDADEVLAA--------------YpaASPAEALAAL 368

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124 2563 TRDYFIICPIIDMASAWAkRARGNVFMY---HAPENYG-------HGslellADVQFALGLPFYPAYEGqFSLEEKSLSL 2632
Cdd:COG2272   369 ATDRVFRCPARRLAEAHA-AAGAPVYLYrfdWRSPPLRgfglgafHG-----AELPFVFGNLDAPALTG-LTPADRALSD 441

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 578816124 2633 KIMQYFSHFIRSGNPNYPYefsrkvptfATPWPDFVPRAG 2672
Cdd:COG2272   442 QMQAYWVNFARTGDPNGPG---------LPEWPAYDPEDR 472
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 2204-2676 1.09e-92

Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on carboxylic esters (EC: 3.1.1.-). The catalytic apparatus involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine.These catalytic residues are responsible for the nucleophilic attack on the carbonyl carbon atom of the ester bond. In contrast with other alpha/beta hydrolase fold family members, p-nitrobenzyl esterase and acetylcholine esterase have a Glu instead of Asp at the active site carboxylate.


Pssm-ID: 238191 [Multi-domain]  Cd Length: 493  Bit Score: 311.19  E-value: 1.09e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124 2204 VDQFLGVPYAAPPLAERRFQAPEPLN-WTGSWDASKPRASC-----WQPGTRTSTSPGvSEDCLYLNVFIPQNVAPNAS- 2276
Cdd:cd00312    17 VYSFLGIPYAEPPVGDLRFKEPQPYEpWSDVLDATSYPPSCmqwdqLGGGLWNAKLPG-SEDCLYLNVYTPKNTKPGNSl 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124 2277 -VLVFFHntmdreeSEGW----PAIDG--SFLAAVGNLIVVTASYRVGVFGFLSSGSGEVSGNWGLLDQVAALTWVQTHI 2349
Cdd:cd00312    96 pVMVWIH-------GGGFmfgsGSLYPgdGLAREGDNVIVVSINYRLGVLGFLSTGDIELPGNYGLKDQRLALKWVQDNI 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124 2350 RGFGGDPRRVSLAADRGGAdvASIHLLTARATNSQLFRRAVLMGGSALSPAAVisHERAQQQAIALAKEVSCPMSSSQEV 2429
Cdd:cd00312   169 AAFGGDPDSVTIFGESAGG--ASVSLLLLSPDSKGLFHRAISQSGSALSPWAI--QENARGRAKRLARLLGCNDTSSAEL 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124 2430 VSCLRQKPANVLNDAQTKLLAVSG-PFHYWGPVIDGHFLREPPARALKRSLWVEVDLLIGSSQDDGLINRAKAVKQFEES 2508
Cdd:cd00312   245 LDCLRSKSAEELLDATRKLLLFSYsPFLPFGPVVDGDFIPDDPEELIKEGKFAKVPLIIGVTKDEGGYFAAMLLNFDAKL 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124 2509 RGRTSskTAFYQALQNSLGGEDsDARVEAAATWYY-SLEHSTDDYASFSRALEnatrDYFIICPIIDMASAWAKRARGNV 2587
Cdd:cd00312   325 IIETN--DRWLELLPYLLFYAD-DALADKVLEKYPgDVDDSVESRKNLSDMLT----DLLFKCPARYFLAQHRKAGGSPV 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124 2588 FMYH-----------APENYG--HGSlellaDVQFALGLPFypaYEGQFSLEEKSLSLKIMQYFSHFIRSGNPNypYEFS 2654
Cdd:cd00312   398 YAYVfdhrsslsvgrWPPWLGtvHGD-----EIFFVFGNPL---LKEGLREEEEKLSRTMMKYWANFAKTGNPN--TEGN 467

                         490       500
                  ....*....|....*....|..
gi 578816124 2655 RKVptfatpWPDFVprAGGENY 2676
Cdd:cd00312   468 LVV------WPAYT--SESEKY 481
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 95-160 8.02e-22

Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases


Pssm-ID: 238114  Cd Length: 66  Bit Score: 90.99  E-value: 8.02e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578816124   95 FCQLQKQQILLSGYINSTDTSYLPQCQDSGDYAPVQCDVQQVQCWCVDAEGMEVYGTRQLGRPKRC 160
Cdd:cd00191     1 PCERERASALESLAGPKLSGLYVPQCDEDGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRGGPPNC 66
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 96-160 6.61e-19

Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the control of proteolytic degradation. The domain usually contains six conserved cysteines. These form three disulphide bridges. Cysteines 1 pairs with 2, 3 with 4 and 5 with 6.


Pssm-ID: 459665  Cd Length: 66  Bit Score: 82.74  E-value: 6.61e-19
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578816124    96 CQLQKQQILLS-GYINSTDTSYLPQCQDSGDYAPVQCDVQQVQCWCVDAEGMEVYGTRQLGRPKRC 160
Cdd:pfam00086    1 CERERARALEQaASGRPASGLYIPNCDEDGFYKPVQCHGSTGYCWCVDPEGQEIPGTRTRGGDPDC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 300-358 7.05e-19

Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases


Pssm-ID: 238114  Cd Length: 66  Bit Score: 82.51  E-value: 7.05e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578816124  300 KCEVERFTATS------FGHPYVPSCRRNGDYQAVQCQTE-GPCWCVDAQGKEMHGTRQQGEPPSC 358
Cdd:cd00191     1 PCERERASALEslagpkLSGLYVPQCDEDGNYEPVQCHGStGYCWCVDPDGEEIPGTRTRGGPPNC 66
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 662-724 1.64e-18

Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the control of proteolytic degradation. The domain usually contains six conserved cysteines. These form three disulphide bridges. Cysteines 1 pairs with 2, 3 with 4 and 5 with 6.


Pssm-ID: 459665  Cd Length: 66  Bit Score: 81.58  E-value: 1.64e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578816124   662 CEKQRARMQSLMGSQPAGSTLFVPACTSEGHFLPVQCFNS--ECYCVDAEGQAIPGTRSAIGKPK 724
Cdd:pfam00086    1 CERERARALEQAASGRPASGLYIPNCDEDGFYKPVQCHGStgYCWCVDPEGQEIPGTRTRGGDPD 65
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1149-1210 2.81e-18

Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases


Pssm-ID: 238114  Cd Length: 66  Bit Score: 80.97  E-value: 2.81e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578816124 1149 CNVLKSGVLSRRVSPG----YVPACRaEDGGFSPVQCDQAQGSCWCVMDSGEEVPGTRVTGGQPAC 1210
Cdd:cd00191     2 CERERASALESLAGPKlsglYVPQCD-EDGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRGGPPNC 66
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 599-658 6.40e-18

Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the control of proteolytic degradation. The domain usually contains six conserved cysteines. These form three disulphide bridges. Cysteines 1 pairs with 2, 3 with 4 and 5 with 6.


Pssm-ID: 459665  Cd Length: 66  Bit Score: 80.04  E-value: 6.40e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578816124   599 METVLSSQTCEQTPERLFVPSCTTEGSYEDVQCFS--GECWCVNSWGKELPGSRVRGGQPRC 658
Cdd:pfam00086    5 RARALEQAASGRPASGLYIPNCDEDGFYKPVQCHGstGYCWCVDPEGQEIPGTRTRGGDPDC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 33-92 1.69e-17

Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases


Pssm-ID: 238114  Cd Length: 66  Bit Score: 78.66  E-value: 1.69e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578816124   33 PCELQRETAFLKQA------DYVPQCAEDGSFQTVQCQNDGRSCWCVGANGSEVLGSRQPGRPVAC 92
Cdd:cd00191     1 PCERERASALESLAgpklsgLYVPQCDEDGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRGGPPNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 612-658 1.88e-17

Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases


Pssm-ID: 238114  Cd Length: 66  Bit Score: 78.66  E-value: 1.88e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 578816124  612 PERLFVPSCTTEGSYEDVQCFS--GECWCVNSWGKELPGSRVRGGQPRC 658
Cdd:cd00191    18 LSGLYVPQCDEDGNYEPVQCHGstGYCWCVDPDGEEIPGTRTRGGPPNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 662-724 3.58e-17

Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases


Pssm-ID: 238114  Cd Length: 66  Bit Score: 77.89  E-value: 3.58e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578816124  662 CEKQRARMQSLMgSQPAGSTLFVPACTSEGHFLPVQCFNS--ECYCVDAEGQAIPGTRSAIGKPK 724
Cdd:cd00191     2 CERERASALESL-AGPKLSGLYVPQCDEDGNYEPVQCHGStgYCWCVDPDGEEIPGTRTRGGPPN 65
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1004-1073 4.89e-17

Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases


Pssm-ID: 238114  Cd Length: 66  Bit Score: 77.50  E-value: 4.89e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124 1004 FYQRRRFSPDDSAgaSALLRSGPYMPQCDAFGSWEPVQCHAGTGHCWCVDEKGGFIPGSLTARslQIPQC 1073
Cdd:cd00191     1 PCERERASALESL--AGPKLSGLYVPQCDEDGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRG--GPPNC 66
Ephrin_rec_like pfam07699
Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region ...
 1465-1510 7.67e-15

Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region rich in cysteines. It is found in various ephrin type A and B receptors, which have tyrosine kinase activity.


Pssm-ID: 429604 [Multi-domain]  Cd Length: 48  Bit Score: 70.46  E-value: 7.67e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 578816124  1465 GSYSQDE--ECIPCPVGFYQEQAGSLACVPCPVGRTTISAGAFSQTHC 1510
Cdd:pfam07699    1 GTYSNTGlePCIPCPRGTYQPEEGQLSCLACPLGTTTDSPGATSISDC 48
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 1151-1210 9.05e-15

Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the control of proteolytic degradation. The domain usually contains six conserved cysteines. These form three disulphide bridges. Cysteines 1 pairs with 2, 3 with 4 and 5 with 6.


Pssm-ID: 459665  Cd Length: 66  Bit Score: 70.79  E-value: 9.05e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124  1151 VLKSGVLSRRVSPGYVPACRaEDGGFSPVQCDQAQGSCWCVMDSGEEVPGTRVTGGQPAC 1210
Cdd:pfam00086    8 ALEQAASGRPASGLYIPNCD-EDGFYKPVQCHGSTGYCWCVDPEGQEIPGTRTRGGDPDC 66
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 1024-1073 1.19e-14

Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the control of proteolytic degradation. The domain usually contains six conserved cysteines. These form three disulphide bridges. Cysteines 1 pairs with 2, 3 with 4 and 5 with 6.


Pssm-ID: 459665  Cd Length: 66  Bit Score: 70.79  E-value: 1.19e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 578816124  1024 SGPYMPQCDAFGSWEPVQCHAGTGHCWCVDEKGGFIPGSLTARSlqIPQC 1073
Cdd:pfam00086   19 SGLYIPNCDEDGFYKPVQCHGSTGYCWCVDPEGQEIPGTRTRGG--DPDC 66
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 117-162 4.15e-14

Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases and binding partners of heparin.


Pssm-ID: 214561  Cd Length: 46  Bit Score: 68.56  E-value: 4.15e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 578816124    117 LPQCQDSGDYAPVQCDVQQVQCWCVDAEGMEVYGTRQLGRPKRCPR 162
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSSGQCWCVDATGREIPGTRTEGGDPDCPS 46
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 301-358 4.48e-14

Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the control of proteolytic degradation. The domain usually contains six conserved cysteines. These form three disulphide bridges. Cysteines 1 pairs with 2, 3 with 4 and 5 with 6.


Pssm-ID: 459665  Cd Length: 66  Bit Score: 68.87  E-value: 4.48e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578816124   301 CEVERFTA---TSFGHP----YVPSCRRNGDYQAVQCQTE-GPCWCVDAQGKEMHGTRQQGEPPSC 358
Cdd:pfam00086    1 CERERARAleqAASGRPasglYIPNCDEDGFYKPVQCHGStGYCWCVDPEGQEIPGTRTRGGDPDC 66
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1166-1212 5.67e-14

Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases and binding partners of heparin.


Pssm-ID: 214561  Cd Length: 46  Bit Score: 68.17  E-value: 5.67e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 578816124   1166 VPACRaEDGGFSPVQCDQAQGSCWCVMDSGEEVPGTRVTGGQPACES 1212
Cdd:smart00211    1 IPQCD-EDGNYEPVQCDGSSGQCWCVDATGREIPGTRTEGGDPDCPS 46
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 34-92 7.38e-13

Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the control of proteolytic degradation. The domain usually contains six conserved cysteines. These form three disulphide bridges. Cysteines 1 pairs with 2, 3 with 4 and 5 with 6.


Pssm-ID: 459665  Cd Length: 66  Bit Score: 65.40  E-value: 7.38e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578816124    34 CELQRETAFLKQAD-------YVPQCAEDGSFQTVQCQNDGRSCWCVGANGSEVLGSRQPGRPVAC 92
Cdd:pfam00086    1 CERERARALEQAASgrpasglYIPNCDEDGFYKPVQCHGSTGYCWCVDPEGQEIPGTRTRGGDPDC 66
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 316-360 1.02e-12

Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases and binding partners of heparin.


Pssm-ID: 214561  Cd Length: 46  Bit Score: 64.71  E-value: 1.02e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 578816124    316 VPSCRRNGDYQAVQCQTE-GPCWCVDAQGKEMHGTRQQGEPPSCAE 360
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSsGQCWCVDATGREIPGTRTEGGDPDCPS 46
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 49-94 1.18e-12

Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases and binding partners of heparin.


Pssm-ID: 214561  Cd Length: 46  Bit Score: 64.32  E-value: 1.18e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 578816124     49 VPQCAEDGSFQTVQCQNDGRSCWCVGANGSEVLGSRQPGRPVACLS 94
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSSGQCWCVDATGREIPGTRTEGGDPDCPS 46
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1028-1075 1.54e-12

Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases and binding partners of heparin.


Pssm-ID: 214561  Cd Length: 46  Bit Score: 63.94  E-value: 1.54e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 578816124   1028 MPQCDAFGSWEPVQCHAGTGHCWCVDEKGGFIPGSLTARSlqIPQCPT 1075
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSSGQCWCVDATGREIPGTRTEGG--DPDCPS 46
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 617-660 3.04e-12

Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases and binding partners of heparin.


Pssm-ID: 214561  Cd Length: 46  Bit Score: 63.17  E-value: 3.04e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 578816124    617 VPSCTTEGSYEDVQCF--SGECWCVNSWGKELPGSRVRGGQPRCPT 660
Cdd:smart00211    1 IPQCDEDGNYEPVQCDgsSGQCWCVDATGREIPGTRTEGGDPDCPS 46
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 684-728 5.39e-11

Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases and binding partners of heparin.


Pssm-ID: 214561  Cd Length: 46  Bit Score: 59.70  E-value: 5.39e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 578816124    684 VPACTSEGHFLPVQCFNS--ECYCVDAEGQAIPGTRSAIGKPkKCPT 728
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSsgQCWCVDATGREIPGTRTEGGDP-DCPS 46
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1520-1567 2.82e-08

Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases and binding partners of heparin.


Pssm-ID: 214561  Cd Length: 46  Bit Score: 51.99  E-value: 2.82e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 578816124   1520 GLQCDQNGQYRASQKDRGSGKAFCVDGEGRRLPWweTEAPLEDSQCLM 1567
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSSGQCWCVDATGREIPG--TRTEGGDPDCPS 46
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
2265-2400 5.85e-07

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 52.57  E-value: 5.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578816124 2265 VFIPQNVAPNASVLVFFH---------NTMDREesegwpaidGSFLAAVGNLIVVTASYRVgvfgflssgSGEVSGNWGL 2335
Cdd:COG0657     3 VYRPAGAKGPLPVVVYFHgggwvsgskDTHDPL---------ARRLAARAGAAVVSVDYRL---------APEHPFPAAL 64

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578816124 2336 LDQVAALTWVQTHIRGFGGDPRRVSLAADRGGADVASIHLLTARATNSQLFRRAVLMGGS---ALSPA 2400
Cdd:COG0657    65 EDAYAALRWLRANAAELGIDPDRIAVAGDSAGGHLAAALALRARDRGGPRPAAQVLIYPVldlTASPL 132
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1077-1145 4.07e-05

Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases


Pssm-ID: 238114  Cd Length: 66  Bit Score: 43.61  E-value: 4.07e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578816124 1077 CEKSRTSGLLSSwkqarsqENPSPKDLFVPACLETGEYARLQ--ASGAGTWCVDPAsGEELrPGSSS---SAQC 1145
Cdd:cd00191     2 CERERASALESL-------AGPKLSGLYVPQCDEDGNYEPVQchGSTGYCWCVDPD-GEEI-PGTRTrggPPNC 66
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 892-922 1.05e-03

Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases and binding partners of heparin.


Pssm-ID: 214561  Cd Length: 46  Bit Score: 38.90  E-value: 1.05e-03
                            10        20        30
                    ....*....|....*....|....*....|.
gi 578816124    892 HFDLRNCWCVDEAGQELEGMRSEPSKlPTCP 922
Cdd:smart00211   16 DGSSGQCWCVDATGREIPGTRTEGGD-PDCP 45
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 730-776 3.90e-03

Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the control of proteolytic degradation. The domain usually contains six conserved cysteines. These form three disulphide bridges. Cysteines 1 pairs with 2, 3 with 4 and 5 with 6.


Pssm-ID: 459665  Cd Length: 66  Bit Score: 38.05  E-value: 3.90e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 578816124   730 CQLQSEQAflrtvqaLLSNSSMLPtLSDTYIPQCSTDGQWRQVQCNG 776
Cdd:pfam00086    1 CERERARA-------LEQAASGRP-ASGLYIPNCDEDGFYKPVQCHG 39
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 1522-1552 4.10e-03

Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the control of proteolytic degradation. The domain usually contains six conserved cysteines. These form three disulphide bridges. Cysteines 1 pairs with 2, 3 with 4 and 5 with 6.


Pssm-ID: 459665  Cd Length: 66  Bit Score: 38.05  E-value: 4.10e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 578816124  1522 QCDQNGQYRASQKDRGSGKAFCVDGEGRRLP 1552
Cdd:pfam00086   25 NCDEDGFYKPVQCHGSTGYCWCVDPEGQEIP 55
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 729-776 4.42e-03

Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases


Pssm-ID: 238114  Cd Length: 66  Bit Score: 37.83  E-value: 4.42e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 578816124  729 PCQLQSEQAFLRTVQALLSNSsmlptlsdtYIPQCSTDGQWRQVQCNG 776
Cdd:cd00191     1 PCERERASALESLAGPKLSGL---------YVPQCDEDGNYEPVQCHG 39
TNFRSF16 cd13416
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ...
 1440-1493 4.95e-03

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


Pssm-ID: 276921 [Multi-domain]  Cd Length: 159  Bit Score: 39.98  E-value: 4.95e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578816124 1440 CSEGFYQvltSEASQDGLGCVKCPEGSY-------SQDEECIPCPVGFYQEQAGSL-ACVPC 1493
Cdd:cd13416    80 CAYGYYL---DEDSGTCEPCTVCPPGQGvvqscgpNQDTVCEACPEGTYSDEDSSTdPCLPC 138
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 892-921 6.36e-03

Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases


Pssm-ID: 238114  Cd Length: 66  Bit Score: 37.44  E-value: 6.36e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 578816124  892 HFDLRNCWCVDEAGQELEGMRSEPSKlPTC 921
Cdd:cd00191    38 HGSTGYCWCVDPDGEEIPGTRTRGGP-PNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1522-1565 6.68e-03

Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 repeats TY repeats are proposed to be inhibitors of cysteine proteases


Pssm-ID: 238114  Cd Length: 66  Bit Score: 37.44  E-value: 6.68e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 578816124 1522 QCDQNGQYRASQKDRGSGKAFCVDGEGRRLPwwETEAPLEDSQC 1565
Cdd:cd00191    25 QCDEDGNYEPVQCHGSTGYCWCVDPDGEEIP--GTRTRGGPPNC 66
 
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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