NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|755551362|ref|XP_006520808|]
View 

thyroglobulin isoform X1 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
COesterase pfam00135
Carboxylesterase family;
2196-2717 6.95e-173

Carboxylesterase family;


:

Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 542.67  E-value: 6.95e-173
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362  2196 STPSVRIdSFGQLQGGSQVIKVGtawKQVYRFLGVPYAAPPLADNRFRAPE-VLNWTGSWDATKPRASCWQPGTRTPTPP 2274
Cdd:pfam00135    1 DSPVVTT-SLGRVRGKRLKVDGG---KPVYAFLGIPYAEPPVGELRFQPPEpPEPWTGVRDATKFGPRCPQNGDLTSPGS 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362  2275 Q---INEDCLYLNVFVPENLVSNA---SVLVFFHNTMEMEGSGGQltIDGSILAAVGNFIVVTANYRLGVFGFLSSGSDE 2348
Cdd:pfam00135   77 SgleGSEDCLYLNVYTPKELKENKnklPVMVWIHGGGFMFGSGSL--YDGSYLAAEGDVIVVTINYRLGPLGFLSTGDDE 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362  2349 VAGNWGLLDQVAALTWVQSHIGAFGGDPQRVTLAADRSGADVASIHLLiSRPTRlQLFRKALLMGGSALSPAAIISPERa 2428
Cdd:pfam00135  155 APGNYGLLDQVLALRWVQENIASFGGDPNRVTLFGESAGAASVSLLLL-SPLSK-GLFHRAILMSGSALSPWAIQSNAR- 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362  2429 qQQAAALAKEVGCPTSSIQEVVSCLRQKPANILNDAQTKLL-AVSGPFHYWGPVVDGQYLRELPSRRLKRPLPVKVDLLI 2507
Cdd:pfam00135  232 -QRAKELAKLVGCPTSDSAELVECLRSKPAEELLDAQLKLLvYGSVPFVPFGPVVDGDFLPEHPEELLKSGNFPKVPLLI 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362  2508 GGSQDDGLINRA------KAVKQFEESQGRTNSKTAFYQALqnslggEDSDARILAAAVWYYSLEHSTDDYASFSRALEN 2581
Cdd:pfam00135  311 GVTKDEGLLFAAyildnvDILKALEEKLLRSLLIDLLYLLL------VDLPEEISAALREEYLDWGDRDDPETSRRALVE 384

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362  2582 ATRDYFIICPMVNMASLWARRtRGNVFMYH---------VPESYG--HGSlellaDVQYAFGLPFYSAYqgQFSTEEQSL 2650
Cdd:pfam00135  385 LLTDYLFNCPVIRFADLHASR-GTPVYMYSfdyrgsslrYPKWVGvdHGD-----ELPYVFGTPFVGAL--LFTEEDEKL 456

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755551362  2651 SLKVMQYFSNFIRSGNPNYPhefsrkaaEFATPWPDFIPgaggESYKELSAQLPNR--QGLKQADCSFW 2717
Cdd:pfam00135  457 SRKMMTYWTNFAKTGNPNGP--------EGLPKWPPYTD----ENGQYLSIDLEPRvkQGLKAERCAFW 513
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 96-161 2.23e-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: 92.53  E-value: 2.23e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755551362   96 FCQLHKQRILLGSYINSTDALYLPQCQDSGNYAPVQCDLQRVQCWCVDTEGMEVYGTRQQGRPTRC 161
Cdd:cd00191     1 PCERERASALESLAGPKLSGLYVPQCDEDGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRGGPPNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 301-359 2.77e-20

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: 86.75  E-value: 2.77e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755551362  301 KCEVEQFAAT------RFGHSYIPRCHRDGHYQTVQCQTE-GMCWCVDAQGREVPGTRQQGQPPSC 359
Cdd:cd00191     1 PCERERASALeslagpKLSGLYVPQCDEDGNYEPVQCHGStGYCWCVDPDGEEIPGTRTRGGPPNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 34-93 6.78e-20

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: 85.59  E-value: 6.78e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755551362   34 PCELQREKAFLKQAE------YVPQCSEDGSFQTVQCQNDGQSCWCVDSDGREVPGSRQLGRPTVC 93
Cdd:cd00191     1 PCERERASALESLAGpklsglYVPQCDEDGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRGGPPNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1005-1074 3.96e-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: 83.28  E-value: 3.96e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362 1005 FYQSLRASLGKSdgAASLLWSGPYMPQCNMIGGWEPVQCHAGTGQCWCVDGRGEFIPGSLMSRssQMPQC 1074
Cdd:cd00191     1 PCERERASALES--LAGPKLSGLYVPQCDEDGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRG--GPPNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 661-726 5.66e-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: 80.20  E-value: 5.66e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755551362  661 KCEKQRAQMQSLaSAQPAGSSFFVPTCTREGYFLPVQCFNS--ECYCVDTEGQVIPGTqSTVGEAKQC 726
Cdd:cd00191     1 PCERERASALES-LAGPKLSGLYVPQCDEDGNYEPVQCHGStgYCWCVDPDGEEIPGT-RTRGGPPNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 612-658 6.99e-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: 77.12  E-value: 6.99e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 755551362  612 PGKFFVPSCTAGGSYEDIQCYA--GECWCVDSRGKELDGSRVRGGRPRC 658
Cdd:cd00191    18 LSGLYVPQCDEDGNYEPVQCHGstGYCWCVDPDGEEIPGTRTRGGPPNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1150-1211 8.83e-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: 76.73  E-value: 8.83e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755551362 1150 CDVLKSRALSRKVGLG----YSPVCEAlDGAFSPVQCDLAQGSCWCVLGSGEEVPGTRVVGTQPAC 1211
Cdd:cd00191     2 CERERASALESLAGPKlsglYVPQCDE-DGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRGGPPNC 66
Ephrin_rec_like pfam07699
Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region ...
 1464-1509 3.12e-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: 71.61  E-value: 3.12e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 755551362  1464 GSFSQDG--RCTPCPAGTYQEQAGSSACIPCPRGRTTITTGAFSKTHC 1509
Cdd:pfam07699    1 GTYSNTGlePCIPCPRGTYQPEEGQLSCLACPLGTTTDSPGATSISDC 48
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1519-1566 4.01e-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: 51.61  E-value: 4.01e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 755551362   1519 GLQCDQNGQYQASQKNRDSGEVFCVDSEGRKLQWlqTEAGLSESQCLM 1566
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSSGQCWCVDATGREIPG--TRTEGGDPDCPS 46
TY super family cl00150
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 893-922 1.95e-04

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 cd00191:

Pssm-ID: 469630  Cd Length: 66  Bit Score: 41.68  E-value: 1.95e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 755551362  893 HFNLRSCWCVDEAGQKLDGTQTKPGEiPAC 922
Cdd:cd00191    38 HGSTGYCWCVDPDGEEIPGTRTRGGP-PNC 66
TY super family cl00150
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1078-1146 2.35e-04

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 cd00191:

Pssm-ID: 469630  Cd Length: 66  Bit Score: 41.68  E-value: 2.35e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755551362 1078 CELSRASGLISAwkqagpqRNPGPGDLFIPVCLQTGEYVRKQ--TSGTGTWCVDPasgEGMPV----NTNGSAQC 1146
Cdd:cd00191     2 CERERASALESL-------AGPKLSGLYVPQCDEDGNYEPVQchGSTGYCWCVDP---DGEEIpgtrTRGGPPNC 66
TY super family cl00150
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 730-776 5.42e-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


The actual alignment was detected with superfamily member cd00191:

Pssm-ID: 469630  Cd Length: 66  Bit Score: 37.83  E-value: 5.42e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 755551362  730 CQLQAEQAFlgvvgvllsNSSMVPSISNVYIPQCSASGQWRHVQCDG 776
Cdd:cd00191     2 CERERASAL---------ESLAGPKLSGLYVPQCDEDGNYEPVQCHG 39
 
Name Accession Description Interval E-value
COesterase pfam00135
Carboxylesterase family;
2196-2717 6.95e-173

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 542.67  E-value: 6.95e-173
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362  2196 STPSVRIdSFGQLQGGSQVIKVGtawKQVYRFLGVPYAAPPLADNRFRAPE-VLNWTGSWDATKPRASCWQPGTRTPTPP 2274
Cdd:pfam00135    1 DSPVVTT-SLGRVRGKRLKVDGG---KPVYAFLGIPYAEPPVGELRFQPPEpPEPWTGVRDATKFGPRCPQNGDLTSPGS 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362  2275 Q---INEDCLYLNVFVPENLVSNA---SVLVFFHNTMEMEGSGGQltIDGSILAAVGNFIVVTANYRLGVFGFLSSGSDE 2348
Cdd:pfam00135   77 SgleGSEDCLYLNVYTPKELKENKnklPVMVWIHGGGFMFGSGSL--YDGSYLAAEGDVIVVTINYRLGPLGFLSTGDDE 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362  2349 VAGNWGLLDQVAALTWVQSHIGAFGGDPQRVTLAADRSGADVASIHLLiSRPTRlQLFRKALLMGGSALSPAAIISPERa 2428
Cdd:pfam00135  155 APGNYGLLDQVLALRWVQENIASFGGDPNRVTLFGESAGAASVSLLLL-SPLSK-GLFHRAILMSGSALSPWAIQSNAR- 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362  2429 qQQAAALAKEVGCPTSSIQEVVSCLRQKPANILNDAQTKLL-AVSGPFHYWGPVVDGQYLRELPSRRLKRPLPVKVDLLI 2507
Cdd:pfam00135  232 -QRAKELAKLVGCPTSDSAELVECLRSKPAEELLDAQLKLLvYGSVPFVPFGPVVDGDFLPEHPEELLKSGNFPKVPLLI 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362  2508 GGSQDDGLINRA------KAVKQFEESQGRTNSKTAFYQALqnslggEDSDARILAAAVWYYSLEHSTDDYASFSRALEN 2581
Cdd:pfam00135  311 GVTKDEGLLFAAyildnvDILKALEEKLLRSLLIDLLYLLL------VDLPEEISAALREEYLDWGDRDDPETSRRALVE 384

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362  2582 ATRDYFIICPMVNMASLWARRtRGNVFMYH---------VPESYG--HGSlellaDVQYAFGLPFYSAYqgQFSTEEQSL 2650
Cdd:pfam00135  385 LLTDYLFNCPVIRFADLHASR-GTPVYMYSfdyrgsslrYPKWVGvdHGD-----ELPYVFGTPFVGAL--LFTEEDEKL 456

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755551362  2651 SLKVMQYFSNFIRSGNPNYPhefsrkaaEFATPWPDFIPgaggESYKELSAQLPNR--QGLKQADCSFW 2717
Cdd:pfam00135  457 SRKMMTYWTNFAKTGNPNGP--------EGLPKWPPYTD----ENGQYLSIDLEPRvkQGLKAERCAFW 513
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
2195-2692 1.20e-96

Carboxylesterase type B [Lipid transport and metabolism];


Pssm-ID: 441873  Cd Length: 500  Bit Score: 322.61  E-value: 1.20e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362 2195 TSTPSVRIDSfGQLQGGSQvikvgtawKQVYRFLGVPYAAPPLADNRFRAPE-VLNWTGSWDATKPRASCWQPGTRT--P 2271
Cdd:COG2272    10 AAAPVVRTEA-GRVRGVVE--------GGVRVFLGIPYAAPPVGELRWRAPQpVEPWTGVRDATEFGPACPQPPRPGdpG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362 2272 TPPQINEDCLYLNVFVPENLVS-NASVLVFFH---NTMemeGSGGQLTIDGSILAAVGnFIVVTANYRLGVFGF-----L 2342
Cdd:COG2272    81 GPAPGSEDCLYLNVWTPALAAGaKLPVMVWIHgggFVS---GSGSEPLYDGAALARRG-VVVVTINYRLGALGFlalpaL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362 2343 SSGSDEVAGNWGLLDQVAALTWVQSHIGAFGGDPQRVTLAADRSGAdvASIHLLISRPTRLQLFRKALLMGGSALSPAai 2422
Cdd:COG2272   157 SGESYGASGNYGLLDQIAALRWVRDNIAAFGGDPDNVTIFGESAGA--ASVAALLASPLAKGLFHRAIAQSGAGLSVL-- 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362 2423 iSPERAQQQAAALAKEVGCPTSSIQevvsCLRQKPANILNDAQTKLLAVSGPFHYWGPVVDGQYLRELPSRRLKRPLPVK 2502
Cdd:COG2272   233 -TLAEAEAVGAAFAAALGVAPATLA----ALRALPAEELLAAQAALAAEGPGGLPFGPVVDGDVLPEDPLEAFAAGRAAD 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362 2503 VDLLIGGSQDDGLInrakavkqFEESQGRTNSKT-AFYQALQNSLGGEDSDaRILAAavwyyslehstddY--ASFSRAL 2579
Cdd:COG2272   308 VPLLIGTNRDEGRL--------FAALLGDLGPLTaADYRAALRRRFGDDAD-EVLAA-------------YpaASPAEAL 365

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362 2580 ENATRDYFIICPMVNMASLWArRTRGNVFMY---HVPESYG-------HGslellADVQYAFGLPFYSAYQGqFSTEEQS 2649
Cdd:COG2272   366 AALATDRVFRCPARRLAEAHA-AAGAPVYLYrfdWRSPPLRgfglgafHG-----AELPFVFGNLDAPALTG-LTPADRA 438

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 755551362 2650 LSLKVMQYFSNFIRSGNPNyphefsrkaAEFATPWPDFIPGAG 2692
Cdd:COG2272   439 LSDQMQAYWVNFARTGDPN---------GPGLPEWPAYDPEDR 472
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 2224-2671 6.43e-96

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: 320.43  E-value: 6.43e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362 2224 VYRFLGVPYAAPPLADNRFRAPEVLN-WTGSWDATKPRASCWQP----GTRTPTPPQINEDCLYLNVFVPENLVSNAS-- 2296
Cdd:cd00312    17 VYSFLGIPYAEPPVGDLRFKEPQPYEpWSDVLDATSYPPSCMQWdqlgGGLWNAKLPGSEDCLYLNVYTPKNTKPGNSlp 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362 2297 VLVFFHNTMEMEGSGGQLTIDGsILAAVGNFIVVTANYRLGVFGFLSSGSDEVAGNWGLLDQVAALTWVQSHIGAFGGDP 2376
Cdd:cd00312    97 VMVWIHGGGFMFGSGSLYPGDG-LAREGDNVIVVSINYRLGVLGFLSTGDIELPGNYGLKDQRLALKWVQDNIAAFGGDP 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362 2377 QRVTLAADRSGAdvASIHLLISRPTRLQLFRKALLMGGSALSPAAIisPERAQQQAAALAKEVGCPTSSIQEVVSCLRQK 2456
Cdd:cd00312   176 DSVTIFGESAGG--ASVSLLLLSPDSKGLFHRAISQSGSALSPWAI--QENARGRAKRLARLLGCNDTSSAELLDCLRSK 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362 2457 PANILNDAQTKLLAVSG-PFHYWGPVVDGQYLRELPSRRLKRPLPVKVDLLIGGSQDDGLINRAKAVKQFEESQGRTNsk 2535
Cdd:cd00312   252 SAEELLDATRKLLLFSYsPFLPFGPVVDGDFIPDDPEELIKEGKFAKVPLIIGVTKDEGGYFAAMLLNFDAKLIIETN-- 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362 2536 TAFYQALQNSLGGEDSD-ARILAAAvwYY-SLEHSTDDYASFSRALEnatrDYFIICPMVNMASLWARRTRGNVFMY--- 2610
Cdd:cd00312   330 DRWLELLPYLLFYADDAlADKVLEK--YPgDVDDSVESRKNLSDMLT----DLLFKCPARYFLAQHRKAGGSPVYAYvfd 403

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755551362 2611 HVPE-SYGHGSLELLA----DVQYAFGLPFYSayqGQFSTEEQSLSLKVMQYFSNFIRSGNPNYPH 2671
Cdd:cd00312   404 HRSSlSVGRWPPWLGTvhgdEIFFVFGNPLLK---EGLREEEEKLSRTMMKYWANFAKTGNPNTEG 466
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 96-161 2.23e-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: 92.53  E-value: 2.23e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755551362   96 FCQLHKQRILLGSYINSTDALYLPQCQDSGNYAPVQCDLQRVQCWCVDTEGMEVYGTRQQGRPTRC 161
Cdd:cd00191     1 PCERERASALESLAGPKLSGLYVPQCDEDGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRGGPPNC 66
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 97-161 1.94e-20

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: 86.97  E-value: 1.94e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755551362    97 CQLHKQRILLG-SYINSTDALYLPQCQDSGNYAPVQCDLQRVQCWCVDTEGMEVYGTRQQGRPTRC 161
Cdd:pfam00086    1 CERERARALEQaASGRPASGLYIPNCDEDGFYKPVQCHGSTGYCWCVDPEGQEIPGTRTRGGDPDC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 301-359 2.77e-20

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: 86.75  E-value: 2.77e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755551362  301 KCEVEQFAAT------RFGHSYIPRCHRDGHYQTVQCQTE-GMCWCVDAQGREVPGTRQQGQPPSC 359
Cdd:cd00191     1 PCERERASALeslagpKLSGLYVPQCDEDGNYEPVQCHGStGYCWCVDPDGEEIPGTRTRGGPPNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 34-93 6.78e-20

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: 85.59  E-value: 6.78e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755551362   34 PCELQREKAFLKQAE------YVPQCSEDGSFQTVQCQNDGQSCWCVDSDGREVPGSRQLGRPTVC 93
Cdd:cd00191     1 PCERERASALESLAGpklsglYVPQCDEDGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRGGPPNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1005-1074 3.96e-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: 83.28  E-value: 3.96e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362 1005 FYQSLRASLGKSdgAASLLWSGPYMPQCNMIGGWEPVQCHAGTGQCWCVDGRGEFIPGSLMSRssQMPQC 1074
Cdd:cd00191     1 PCERERASALES--LAGPKLSGLYVPQCDEDGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRG--GPPNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 661-726 5.66e-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: 80.20  E-value: 5.66e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755551362  661 KCEKQRAQMQSLaSAQPAGSSFFVPTCTREGYFLPVQCFNS--ECYCVDTEGQVIPGTqSTVGEAKQC 726
Cdd:cd00191     1 PCERERASALES-LAGPKLSGLYVPQCDEDGNYEPVQCHGStgYCWCVDPDGEEIPGT-RTRGGPPNC 66
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 662-726 7.39e-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: 79.65  E-value: 7.39e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755551362   662 CEKQRAQMQSLASAQPAGSSFFVPTCTREGYFLPVQCFNS--ECYCVDTEGQVIPGTqSTVGEAKQC 726
Cdd:pfam00086    1 CERERARALEQAASGRPASGLYIPNCDEDGFYKPVQCHGStgYCWCVDPEGQEIPGT-RTRGGDPDC 66
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 35-93 4.90e-17

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: 77.34  E-value: 4.90e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755551362    35 CELQREKAFLKQAE-------YVPQCSEDGSFQTVQCQNDGQSCWCVDSDGREVPGSRQLGRPTVC 93
Cdd:pfam00086    1 CERERARALEQAASgrpasglYIPNCDEDGFYKPVQCHGSTGYCWCVDPEGQEIPGTRTRGGDPDC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 612-658 6.99e-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: 77.12  E-value: 6.99e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 755551362  612 PGKFFVPSCTAGGSYEDIQCYA--GECWCVDSRGKELDGSRVRGGRPRC 658
Cdd:cd00191    18 LSGLYVPQCDEDGNYEPVQCHGstGYCWCVDPDGEEIPGTRTRGGPPNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1150-1211 8.83e-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: 76.73  E-value: 8.83e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755551362 1150 CDVLKSRALSRKVGLG----YSPVCEAlDGAFSPVQCDLAQGSCWCVLGSGEEVPGTRVVGTQPAC 1211
Cdd:cd00191     2 CERERASALESLAGPKlsglYVPQCDE-DGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRGGPPNC 66
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 316-359 9.21e-16

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: 73.88  E-value: 9.21e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 755551362   316 YIPRCHRDGHYQTVQCQTE-GMCWCVDAQGREVPGTRQQGQPPSC 359
Cdd:pfam00086   22 YIPNCDEDGFYKPVQCHGStGYCWCVDPEGQEIPGTRTRGGDPDC 66
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 317-359 1.14e-15

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: 72.80  E-value: 1.14e-15
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 755551362    317 IPRCHRDGHYQTVQCQTE-GMCWCVDAQGREVPGTRQQGQPPSC 359
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSsGQCWCVDATGREIPGTRTEGGDPDC 44
Ephrin_rec_like pfam07699
Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region ...
 1464-1509 3.12e-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: 71.61  E-value: 3.12e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 755551362  1464 GSFSQDG--RCTPCPAGTYQEQAGSSACIPCPRGRTTITTGAFSKTHC 1509
Cdd:pfam07699    1 GTYSNTGlePCIPCPRGTYQPEEGQLSCLACPLGTTTDSPGATSISDC 48
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 118-163 3.50e-15

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: 71.64  E-value: 3.50e-15
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 755551362    118 LPQCQDSGNYAPVQCDLQRVQCWCVDTEGMEVYGTRQQGRPTRCPR 163
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSSGQCWCVDATGREIPGTRTEGGDPDCPS 46
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 612-658 1.35e-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: 70.41  E-value: 1.35e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 755551362   612 PGKFFVPSCTAGGSYEDIQCY--AGECWCVDSRGKELDGSRVRGGRPRC 658
Cdd:pfam00086   18 ASGLYIPNCDEDGFYKPVQCHgsTGYCWCVDPEGQEIPGTRTRGGDPDC 66
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 50-95 9.57e-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: 67.40  E-value: 9.57e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 755551362     50 VPQCSEDGSFQTVQCQNDGQSCWCVDSDGREVPGSRQLGRPTVCLS 95
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSSGQCWCVDATGREIPGTRTEGGDPDCPS 46
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 1025-1074 3.03e-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: 66.56  E-value: 3.03e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 755551362  1025 SGPYMPQCNMIGGWEPVQCHAGTGQCWCVDGRGEFIPGSlmSRSSQMPQC 1074
Cdd:pfam00086   19 SGLYIPNCDEDGFYKPVQCHGSTGYCWCVDPEGQEIPGT--RTRGGDPDC 66
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 617-660 1.42e-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: 1.42e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 755551362    617 VPSCTAGGSYEDIQCYA--GECWCVDSRGKELDGSRVRGGRPRCPT 660
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGssGQCWCVDATGREIPGTRTEGGDPDCPS 46
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1168-1213 2.43e-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: 63.55  E-value: 2.43e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 755551362   1168 PVCEAlDGAFSPVQCDLAQGSCWCVLGSGEEVPGTRVVGTQPACES 1213
Cdd:smart00211    2 PQCDE-DGNYEPVQCDGSSGQCWCVDATGREIPGTRTEGGDPDCPS 46
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 1152-1211 7.67e-12

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: 62.71  E-value: 7.67e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362  1152 VLKSRALSRKVGLGYSPVCEAlDGAFSPVQCDLAQGSCWCVLGSGEEVPGTRVVGTQPAC 1211
Cdd:pfam00086    8 ALEQAASGRPASGLYIPNCDE-DGFYKPVQCHGSTGYCWCVDPEGQEIPGTRTRGGDPDC 66
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1029-1076 5.92e-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: 5.92e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 755551362   1029 MPQCNMIGGWEPVQCHAGTGQCWCVDGRGEFIPGSLMSRSSqmPQCPT 1076
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSSGQCWCVDATGREIPGTRTEGGD--PDCPS 46
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 684-728 9.47e-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: 58.93  E-value: 9.47e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 755551362    684 VPTCTREGYFLPVQCFNS--ECYCVDTEGQVIPGTQSTVGEAkQCPS 728
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSsgQCWCVDATGREIPGTRTEGGDP-DCPS 46
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1519-1566 4.01e-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: 51.61  E-value: 4.01e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 755551362   1519 GLQCDQNGQYQASQKNRDSGEVFCVDSEGRKLQWlqTEAGLSESQCLM 1566
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSSGQCWCVDATGREIPG--TRTEGGDPDCPS 46
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 893-922 1.95e-04

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: 41.68  E-value: 1.95e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 755551362  893 HFNLRSCWCVDEAGQKLDGTQTKPGEiPAC 922
Cdd:cd00191    38 HGSTGYCWCVDPDGEEIPGTRTRGGP-PNC 66
TNFRSF16 cd13416
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ...
 1437-1492 2.00e-04

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


Pssm-ID: 276921 [Multi-domain]  Cd Length: 159  Bit Score: 44.22  E-value: 2.00e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755551362 1437 TQLGCMEGFYRVPTTRQdALGCVKCPEG-------SFSQDGRCTPCPAGTYQEQAGS-SACIPC 1492
Cdd:cd13416    76 TVCECAYGYYLDEDSGT-CEPCTVCPPGqgvvqscGPNQDTVCEACPEGTYSDEDSStDPCLPC 138
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1078-1146 2.35e-04

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: 41.68  E-value: 2.35e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755551362 1078 CELSRASGLISAwkqagpqRNPGPGDLFIPVCLQTGEYVRKQ--TSGTGTWCVDPasgEGMPV----NTNGSAQC 1146
Cdd:cd00191     2 CERERASALESL-------AGPKLSGLYVPQCDEDGNYEPVQchGSTGYCWCVDP---DGEEIpgtrTRGGPPNC 66
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 893-923 7.05e-04

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: 39.67  E-value: 7.05e-04
                            10        20        30
                    ....*....|....*....|....*....|.
gi 755551362    893 HFNLRSCWCVDEAGQKLDGTQTkPGEIPACP 923
Cdd:smart00211   16 DGSSGQCWCVDATGREIPGTRT-EGGDPDCP 45
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 899-922 9.35e-04

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: 39.98  E-value: 9.35e-04
                           10        20
                   ....*....|....*....|....
gi 755551362   899 CWCVDEAGQKLDGTQTKPGEiPAC 922
Cdd:pfam00086   44 CWCVDPEGQEIPGTRTRGGD-PDC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 730-776 5.42e-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: 5.42e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 755551362  730 CQLQAEQAFlgvvgvllsNSSMVPSISNVYIPQCSASGQWRHVQCDG 776
Cdd:cd00191     2 CERERASAL---------ESLAGPKLSGLYVPQCDEDGNYEPVQCHG 39
 
Name Accession Description Interval E-value
COesterase pfam00135
Carboxylesterase family;
2196-2717 6.95e-173

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 542.67  E-value: 6.95e-173
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362  2196 STPSVRIdSFGQLQGGSQVIKVGtawKQVYRFLGVPYAAPPLADNRFRAPE-VLNWTGSWDATKPRASCWQPGTRTPTPP 2274
Cdd:pfam00135    1 DSPVVTT-SLGRVRGKRLKVDGG---KPVYAFLGIPYAEPPVGELRFQPPEpPEPWTGVRDATKFGPRCPQNGDLTSPGS 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362  2275 Q---INEDCLYLNVFVPENLVSNA---SVLVFFHNTMEMEGSGGQltIDGSILAAVGNFIVVTANYRLGVFGFLSSGSDE 2348
Cdd:pfam00135   77 SgleGSEDCLYLNVYTPKELKENKnklPVMVWIHGGGFMFGSGSL--YDGSYLAAEGDVIVVTINYRLGPLGFLSTGDDE 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362  2349 VAGNWGLLDQVAALTWVQSHIGAFGGDPQRVTLAADRSGADVASIHLLiSRPTRlQLFRKALLMGGSALSPAAIISPERa 2428
Cdd:pfam00135  155 APGNYGLLDQVLALRWVQENIASFGGDPNRVTLFGESAGAASVSLLLL-SPLSK-GLFHRAILMSGSALSPWAIQSNAR- 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362  2429 qQQAAALAKEVGCPTSSIQEVVSCLRQKPANILNDAQTKLL-AVSGPFHYWGPVVDGQYLRELPSRRLKRPLPVKVDLLI 2507
Cdd:pfam00135  232 -QRAKELAKLVGCPTSDSAELVECLRSKPAEELLDAQLKLLvYGSVPFVPFGPVVDGDFLPEHPEELLKSGNFPKVPLLI 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362  2508 GGSQDDGLINRA------KAVKQFEESQGRTNSKTAFYQALqnslggEDSDARILAAAVWYYSLEHSTDDYASFSRALEN 2581
Cdd:pfam00135  311 GVTKDEGLLFAAyildnvDILKALEEKLLRSLLIDLLYLLL------VDLPEEISAALREEYLDWGDRDDPETSRRALVE 384

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362  2582 ATRDYFIICPMVNMASLWARRtRGNVFMYH---------VPESYG--HGSlellaDVQYAFGLPFYSAYqgQFSTEEQSL 2650
Cdd:pfam00135  385 LLTDYLFNCPVIRFADLHASR-GTPVYMYSfdyrgsslrYPKWVGvdHGD-----ELPYVFGTPFVGAL--LFTEEDEKL 456

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755551362  2651 SLKVMQYFSNFIRSGNPNYPhefsrkaaEFATPWPDFIPgaggESYKELSAQLPNR--QGLKQADCSFW 2717
Cdd:pfam00135  457 SRKMMTYWTNFAKTGNPNGP--------EGLPKWPPYTD----ENGQYLSIDLEPRvkQGLKAERCAFW 513
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
2195-2692 1.20e-96

Carboxylesterase type B [Lipid transport and metabolism];


Pssm-ID: 441873  Cd Length: 500  Bit Score: 322.61  E-value: 1.20e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362 2195 TSTPSVRIDSfGQLQGGSQvikvgtawKQVYRFLGVPYAAPPLADNRFRAPE-VLNWTGSWDATKPRASCWQPGTRT--P 2271
Cdd:COG2272    10 AAAPVVRTEA-GRVRGVVE--------GGVRVFLGIPYAAPPVGELRWRAPQpVEPWTGVRDATEFGPACPQPPRPGdpG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362 2272 TPPQINEDCLYLNVFVPENLVS-NASVLVFFH---NTMemeGSGGQLTIDGSILAAVGnFIVVTANYRLGVFGF-----L 2342
Cdd:COG2272    81 GPAPGSEDCLYLNVWTPALAAGaKLPVMVWIHgggFVS---GSGSEPLYDGAALARRG-VVVVTINYRLGALGFlalpaL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362 2343 SSGSDEVAGNWGLLDQVAALTWVQSHIGAFGGDPQRVTLAADRSGAdvASIHLLISRPTRLQLFRKALLMGGSALSPAai 2422
Cdd:COG2272   157 SGESYGASGNYGLLDQIAALRWVRDNIAAFGGDPDNVTIFGESAGA--ASVAALLASPLAKGLFHRAIAQSGAGLSVL-- 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362 2423 iSPERAQQQAAALAKEVGCPTSSIQevvsCLRQKPANILNDAQTKLLAVSGPFHYWGPVVDGQYLRELPSRRLKRPLPVK 2502
Cdd:COG2272   233 -TLAEAEAVGAAFAAALGVAPATLA----ALRALPAEELLAAQAALAAEGPGGLPFGPVVDGDVLPEDPLEAFAAGRAAD 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362 2503 VDLLIGGSQDDGLInrakavkqFEESQGRTNSKT-AFYQALQNSLGGEDSDaRILAAavwyyslehstddY--ASFSRAL 2579
Cdd:COG2272   308 VPLLIGTNRDEGRL--------FAALLGDLGPLTaADYRAALRRRFGDDAD-EVLAA-------------YpaASPAEAL 365

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362 2580 ENATRDYFIICPMVNMASLWArRTRGNVFMY---HVPESYG-------HGslellADVQYAFGLPFYSAYQGqFSTEEQS 2649
Cdd:COG2272   366 AALATDRVFRCPARRLAEAHA-AAGAPVYLYrfdWRSPPLRgfglgafHG-----AELPFVFGNLDAPALTG-LTPADRA 438

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 755551362 2650 LSLKVMQYFSNFIRSGNPNyphefsrkaAEFATPWPDFIPGAG 2692
Cdd:COG2272   439 LSDQMQAYWVNFARTGDPN---------GPGLPEWPAYDPEDR 472
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 2224-2671 6.43e-96

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: 320.43  E-value: 6.43e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362 2224 VYRFLGVPYAAPPLADNRFRAPEVLN-WTGSWDATKPRASCWQP----GTRTPTPPQINEDCLYLNVFVPENLVSNAS-- 2296
Cdd:cd00312    17 VYSFLGIPYAEPPVGDLRFKEPQPYEpWSDVLDATSYPPSCMQWdqlgGGLWNAKLPGSEDCLYLNVYTPKNTKPGNSlp 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362 2297 VLVFFHNTMEMEGSGGQLTIDGsILAAVGNFIVVTANYRLGVFGFLSSGSDEVAGNWGLLDQVAALTWVQSHIGAFGGDP 2376
Cdd:cd00312    97 VMVWIHGGGFMFGSGSLYPGDG-LAREGDNVIVVSINYRLGVLGFLSTGDIELPGNYGLKDQRLALKWVQDNIAAFGGDP 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362 2377 QRVTLAADRSGAdvASIHLLISRPTRLQLFRKALLMGGSALSPAAIisPERAQQQAAALAKEVGCPTSSIQEVVSCLRQK 2456
Cdd:cd00312   176 DSVTIFGESAGG--ASVSLLLLSPDSKGLFHRAISQSGSALSPWAI--QENARGRAKRLARLLGCNDTSSAELLDCLRSK 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362 2457 PANILNDAQTKLLAVSG-PFHYWGPVVDGQYLRELPSRRLKRPLPVKVDLLIGGSQDDGLINRAKAVKQFEESQGRTNsk 2535
Cdd:cd00312   252 SAEELLDATRKLLLFSYsPFLPFGPVVDGDFIPDDPEELIKEGKFAKVPLIIGVTKDEGGYFAAMLLNFDAKLIIETN-- 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362 2536 TAFYQALQNSLGGEDSD-ARILAAAvwYY-SLEHSTDDYASFSRALEnatrDYFIICPMVNMASLWARRTRGNVFMY--- 2610
Cdd:cd00312   330 DRWLELLPYLLFYADDAlADKVLEK--YPgDVDDSVESRKNLSDMLT----DLLFKCPARYFLAQHRKAGGSPVYAYvfd 403

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755551362 2611 HVPE-SYGHGSLELLA----DVQYAFGLPFYSayqGQFSTEEQSLSLKVMQYFSNFIRSGNPNYPH 2671
Cdd:cd00312   404 HRSSlSVGRWPPWLGTvhgdEIFFVFGNPLLK---EGLREEEEKLSRTMMKYWANFAKTGNPNTEG 466
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 96-161 2.23e-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: 92.53  E-value: 2.23e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755551362   96 FCQLHKQRILLGSYINSTDALYLPQCQDSGNYAPVQCDLQRVQCWCVDTEGMEVYGTRQQGRPTRC 161
Cdd:cd00191     1 PCERERASALESLAGPKLSGLYVPQCDEDGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRGGPPNC 66
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 97-161 1.94e-20

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: 86.97  E-value: 1.94e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755551362    97 CQLHKQRILLG-SYINSTDALYLPQCQDSGNYAPVQCDLQRVQCWCVDTEGMEVYGTRQQGRPTRC 161
Cdd:pfam00086    1 CERERARALEQaASGRPASGLYIPNCDEDGFYKPVQCHGSTGYCWCVDPEGQEIPGTRTRGGDPDC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 301-359 2.77e-20

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: 86.75  E-value: 2.77e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755551362  301 KCEVEQFAAT------RFGHSYIPRCHRDGHYQTVQCQTE-GMCWCVDAQGREVPGTRQQGQPPSC 359
Cdd:cd00191     1 PCERERASALeslagpKLSGLYVPQCDEDGNYEPVQCHGStGYCWCVDPDGEEIPGTRTRGGPPNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 34-93 6.78e-20

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: 85.59  E-value: 6.78e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755551362   34 PCELQREKAFLKQAE------YVPQCSEDGSFQTVQCQNDGQSCWCVDSDGREVPGSRQLGRPTVC 93
Cdd:cd00191     1 PCERERASALESLAGpklsglYVPQCDEDGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRGGPPNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1005-1074 3.96e-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: 83.28  E-value: 3.96e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362 1005 FYQSLRASLGKSdgAASLLWSGPYMPQCNMIGGWEPVQCHAGTGQCWCVDGRGEFIPGSLMSRssQMPQC 1074
Cdd:cd00191     1 PCERERASALES--LAGPKLSGLYVPQCDEDGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRG--GPPNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 661-726 5.66e-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: 80.20  E-value: 5.66e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755551362  661 KCEKQRAQMQSLaSAQPAGSSFFVPTCTREGYFLPVQCFNS--ECYCVDTEGQVIPGTqSTVGEAKQC 726
Cdd:cd00191     1 PCERERASALES-LAGPKLSGLYVPQCDEDGNYEPVQCHGStgYCWCVDPDGEEIPGT-RTRGGPPNC 66
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 662-726 7.39e-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: 79.65  E-value: 7.39e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755551362   662 CEKQRAQMQSLASAQPAGSSFFVPTCTREGYFLPVQCFNS--ECYCVDTEGQVIPGTqSTVGEAKQC 726
Cdd:pfam00086    1 CERERARALEQAASGRPASGLYIPNCDEDGFYKPVQCHGStgYCWCVDPEGQEIPGT-RTRGGDPDC 66
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 35-93 4.90e-17

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: 77.34  E-value: 4.90e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755551362    35 CELQREKAFLKQAE-------YVPQCSEDGSFQTVQCQNDGQSCWCVDSDGREVPGSRQLGRPTVC 93
Cdd:pfam00086    1 CERERARALEQAASgrpasglYIPNCDEDGFYKPVQCHGSTGYCWCVDPEGQEIPGTRTRGGDPDC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 612-658 6.99e-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: 77.12  E-value: 6.99e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 755551362  612 PGKFFVPSCTAGGSYEDIQCYA--GECWCVDSRGKELDGSRVRGGRPRC 658
Cdd:cd00191    18 LSGLYVPQCDEDGNYEPVQCHGstGYCWCVDPDGEEIPGTRTRGGPPNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1150-1211 8.83e-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: 76.73  E-value: 8.83e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755551362 1150 CDVLKSRALSRKVGLG----YSPVCEAlDGAFSPVQCDLAQGSCWCVLGSGEEVPGTRVVGTQPAC 1211
Cdd:cd00191     2 CERERASALESLAGPKlsglYVPQCDE-DGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRGGPPNC 66
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 316-359 9.21e-16

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: 73.88  E-value: 9.21e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 755551362   316 YIPRCHRDGHYQTVQCQTE-GMCWCVDAQGREVPGTRQQGQPPSC 359
Cdd:pfam00086   22 YIPNCDEDGFYKPVQCHGStGYCWCVDPEGQEIPGTRTRGGDPDC 66
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 317-359 1.14e-15

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: 72.80  E-value: 1.14e-15
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 755551362    317 IPRCHRDGHYQTVQCQTE-GMCWCVDAQGREVPGTRQQGQPPSC 359
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSsGQCWCVDATGREIPGTRTEGGDPDC 44
Ephrin_rec_like pfam07699
Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region ...
 1464-1509 3.12e-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: 71.61  E-value: 3.12e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 755551362  1464 GSFSQDG--RCTPCPAGTYQEQAGSSACIPCPRGRTTITTGAFSKTHC 1509
Cdd:pfam07699    1 GTYSNTGlePCIPCPRGTYQPEEGQLSCLACPLGTTTDSPGATSISDC 48
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 118-163 3.50e-15

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: 71.64  E-value: 3.50e-15
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 755551362    118 LPQCQDSGNYAPVQCDLQRVQCWCVDTEGMEVYGTRQQGRPTRCPR 163
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSSGQCWCVDATGREIPGTRTEGGDPDCPS 46
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 612-658 1.35e-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: 70.41  E-value: 1.35e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 755551362   612 PGKFFVPSCTAGGSYEDIQCY--AGECWCVDSRGKELDGSRVRGGRPRC 658
Cdd:pfam00086   18 ASGLYIPNCDEDGFYKPVQCHgsTGYCWCVDPEGQEIPGTRTRGGDPDC 66
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 50-95 9.57e-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: 67.40  E-value: 9.57e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 755551362     50 VPQCSEDGSFQTVQCQNDGQSCWCVDSDGREVPGSRQLGRPTVCLS 95
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSSGQCWCVDATGREIPGTRTEGGDPDCPS 46
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 1025-1074 3.03e-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: 66.56  E-value: 3.03e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 755551362  1025 SGPYMPQCNMIGGWEPVQCHAGTGQCWCVDGRGEFIPGSlmSRSSQMPQC 1074
Cdd:pfam00086   19 SGLYIPNCDEDGFYKPVQCHGSTGYCWCVDPEGQEIPGT--RTRGGDPDC 66
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 617-660 1.42e-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: 1.42e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 755551362    617 VPSCTAGGSYEDIQCYA--GECWCVDSRGKELDGSRVRGGRPRCPT 660
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGssGQCWCVDATGREIPGTRTEGGDPDCPS 46
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1168-1213 2.43e-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: 63.55  E-value: 2.43e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 755551362   1168 PVCEAlDGAFSPVQCDLAQGSCWCVLGSGEEVPGTRVVGTQPACES 1213
Cdd:smart00211    2 PQCDE-DGNYEPVQCDGSSGQCWCVDATGREIPGTRTEGGDPDCPS 46
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 1152-1211 7.67e-12

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: 62.71  E-value: 7.67e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362  1152 VLKSRALSRKVGLGYSPVCEAlDGAFSPVQCDLAQGSCWCVLGSGEEVPGTRVVGTQPAC 1211
Cdd:pfam00086    8 ALEQAASGRPASGLYIPNCDE-DGFYKPVQCHGSTGYCWCVDPEGQEIPGTRTRGGDPDC 66
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1029-1076 5.92e-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: 5.92e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 755551362   1029 MPQCNMIGGWEPVQCHAGTGQCWCVDGRGEFIPGSLMSRSSqmPQCPT 1076
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSSGQCWCVDATGREIPGTRTEGGD--PDCPS 46
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 684-728 9.47e-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: 58.93  E-value: 9.47e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 755551362    684 VPTCTREGYFLPVQCFNS--ECYCVDTEGQVIPGTQSTVGEAkQCPS 728
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSsgQCWCVDATGREIPGTRTEGGDP-DCPS 46
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1519-1566 4.01e-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: 51.61  E-value: 4.01e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 755551362   1519 GLQCDQNGQYQASQKNRDSGEVFCVDSEGRKLQWlqTEAGLSESQCLM 1566
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSSGQCWCVDATGREIPG--TRTEGGDPDCPS 46
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
2285-2427 6.29e-08

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 55.65  E-value: 6.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362 2285 VFVPENLVSNASVLVFFHntmemegsGGQLTIdGSI---------LAAVGNFIVVTANYRLgvfgflssgSDEVAGNWGL 2355
Cdd:COG0657     3 VYRPAGAKGPLPVVVYFH--------GGGWVS-GSKdthdplarrLAARAGAAVVSVDYRL---------APEHPFPAAL 64

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755551362 2356 LDQVAALTWVQSHIGAFGGDPQRVTLAADRSGADVASIHLLISRPTRLQLFRKALLMGGsALSPAAiiSPER 2427
Cdd:COG0657    65 EDAYAALRWLRANAAELGIDPDRIAVAGDSAGGHLAAALALRARDRGGPRPAAQVLIYP-VLDLTA--SPLR 133
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 893-922 1.95e-04

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: 41.68  E-value: 1.95e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 755551362  893 HFNLRSCWCVDEAGQKLDGTQTKPGEiPAC 922
Cdd:cd00191    38 HGSTGYCWCVDPDGEEIPGTRTRGGP-PNC 66
TNFRSF16 cd13416
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ...
 1437-1492 2.00e-04

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


Pssm-ID: 276921 [Multi-domain]  Cd Length: 159  Bit Score: 44.22  E-value: 2.00e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755551362 1437 TQLGCMEGFYRVPTTRQdALGCVKCPEG-------SFSQDGRCTPCPAGTYQEQAGS-SACIPC 1492
Cdd:cd13416    76 TVCECAYGYYLDEDSGT-CEPCTVCPPGqgvvqscGPNQDTVCEACPEGTYSDEDSStDPCLPC 138
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1078-1146 2.35e-04

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: 41.68  E-value: 2.35e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755551362 1078 CELSRASGLISAwkqagpqRNPGPGDLFIPVCLQTGEYVRKQ--TSGTGTWCVDPasgEGMPV----NTNGSAQC 1146
Cdd:cd00191     2 CERERASALESL-------AGPKLSGLYVPQCDEDGNYEPVQchGSTGYCWCVDP---DGEEIpgtrTRGGPPNC 66
TNFRSF21 cd10583
Tumor necrosis factor receptor superfamily member 21 (TNFRSF21), also known as death receptor ...
 1434-1514 5.87e-04

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


Pssm-ID: 276909 [Multi-domain]  Cd Length: 159  Bit Score: 42.82  E-value: 5.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551362 1434 SPRTQLGCMEgfyRVP-TTRQDALgCVkCPEGSFSQDGRCTP---CPAGTYQEQAGSSA----CIPCPRGRTTITTGAFS 1505
Cdd:cd10583    58 RKPCPAPMIE---KTPcTALTDRE-CT-CPPGTFLSNDTCVPhsvCPVGWGVRKKGTETedvrCKPCPRGTFSDVPSSVL 132


                  ....*....
gi 755551362 1506 KTHCVTDCQ 1514
Cdd:cd10583   133 KCKTYTDCL 141
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 893-923 7.05e-04

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: 39.67  E-value: 7.05e-04
                            10        20        30
                    ....*....|....*....|....*....|.
gi 755551362    893 HFNLRSCWCVDEAGQKLDGTQTkPGEIPACP 923
Cdd:smart00211   16 DGSSGQCWCVDATGREIPGTRT-EGGDPDCP 45
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 899-922 9.35e-04

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: 39.98  E-value: 9.35e-04
                           10        20
                   ....*....|....*....|....
gi 755551362   899 CWCVDEAGQKLDGTQTKPGEiPAC 922
Cdd:pfam00086   44 CWCVDPEGQEIPGTRTRGGD-PDC 66
TNFRSF cd00185
Tumor necrosis factor receptor superfamily (TNFRSF); Members of TNFR superfamily (TNFRSF) ...
 1458-1511 3.79e-03

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


Pssm-ID: 276900 [Multi-domain]  Cd Length: 87  Bit Score: 38.73  E-value: 3.79e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755551362 1458 CVKCPEGSF-------SQDGRCTPCPAGTYQEQAGS-SACIPC----PRGRTTITTGAFSKTHCVT 1511
Cdd:cd00185     2 CQRCPPGEYlssdctaTTDTVCSPCPPGTYSESWNSlSKCLPCttcgGGNQVEKTPCTATDNRCCT 67
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 730-776 5.42e-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: 5.42e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 755551362  730 CQLQAEQAFlgvvgvllsNSSMVPSISNVYIPQCSASGQWRHVQCDG 776
Cdd:cd00191     2 CERERASAL---------ESLAGPKLSGLYVPQCDEDGNYEPVQCHG 39
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH