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Conserved domains on  [gi|12643975|sp|P06882|]
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RecName: Full=Thyroglobulin; Short=Tg; Flags: Precursor

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COesterase pfam00135
Carboxylesterase family;
2198-2719 5.63e-175

Carboxylesterase family;


:

Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 548.45  E-value: 5.63e-175
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975   2198 STPSVHIdSFGQLQGGSQVVKVGtawKQVYQFLGVPYAAPPLAENRFQAPE-VLNWTGSWDATKLRSSCWQPGTRTPTPP 2276
Cdd:pfam00135    1 DSPVVTT-SLGRVRGKRLKVDGG---KPVYAFLGIPYAEPPVGELRFQPPEpPEPWTGVRDATKFGPRCPQNGDLTSPGS 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975   2277 Q---ISEDCLYLNVFVPENLVSNA---SVLVFFHNTVEMEGSGGQlnIDGSILAAVGNLIVVTANYRLGVFGFLSSGSDE 2350
Cdd:pfam00135   77 SgleGSEDCLYLNVYTPKELKENKnklPVMVWIHGGGFMFGSGSL--YDGSYLAAEGDVIVVTINYRLGPLGFLSTGDDE 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975   2351 VAGNWGLLDQVAALTWVQTHIGAFGGDPQRVTLAADRGGADVASIHLLitRPTRLQLFRKALLMGGSALSPAAIISPDRa 2430
Cdd:pfam00135  155 APGNYGLLDQVLALRWVQENIASFGGDPNRVTLFGESAGAASVSLLLL--SPLSKGLFHRAILMSGSALSPWAIQSNAR- 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975   2431 qQQAAALAKEVGCPNSSVQEVVSCFRQKPANILNEAQTKLL-AVSGPFHYWGPVVDGQYLRELPSRRLKRPLPVKVDLLI 2509
Cdd:pfam00135  232 -QRAKELAKLVGCPTSDSAELVECLRSKPAEELLDAQLKLLvYGSVPFVPFGPVVDGDFLPEHPEELLKSGNFPKVPLLI 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975   2510 GGSQDDGLINRA------KAVKQFEESQGRTNSKTAFYQALqnslggEDSDARILAAAIWYYSLEHSTDDYASFSRALEN 2583
Cdd:pfam00135  311 GVTKDEGLLFAAyildnvDILKALEEKLLRSLLIDLLYLLL------VDLPEEISAALREEYLDWGDRDDPETSRRALVE 384

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975   2584 ATRDYFIICPIVNMASLWARRtRGNVFMYH---------VPESYG--HGSlellaDVQYAFGLPFYSAYQgyFSTEEQSL 2652
Cdd:pfam00135  385 LLTDYLFNCPVIRFADLHASR-GTPVYMYSfdyrgsslrYPKWVGvdHGD-----ELPYVFGTPFVGALL--FTEEDEKL 456

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 12643975   2653 SLKVMQYFSNFIRSGNPNYPhefsqkaaEFATPWPDFVPgaggESYKELSAQLPNR--QGLKKADCSFW 2719
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 2.41e-23

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: 95.22  E-value: 2.41e-23
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12643975   96 FCQLHKQRILLSSYINSTDALYLPQCQDSGNYAPVQCDLQQVQCWCVDTEGMEVYGTRQQGRPTRC 161
Cdd:cd00191    1 PCERERASALESLAGPKLSGLYVPQCDEDGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRGGPPNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1005-1074 5.27e-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: 85.98  E-value: 5.27e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975 1005 FYQKLRASLGESNgtASLLWSGPYMPQCNTIGGWEPVQCHPGTGQCWCVDGWGELIPGSLMARssQMPQC 1074
Cdd:cd00191    1 PCERERASALESL--AGPKLSGLYVPQCDEDGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRG--GPPNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 34-93 4.67e-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: 4.67e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12643975   34 PCELQREKAF------LKQDEYVPQCSEDGSFQTVQCQNDGQSCWCVDSDGTEVPGSRQLGRPTAC 93
Cdd:cd00191    1 PCERERASALeslagpKLSGLYVPQCDEDGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRGGPPNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 661-724 3.79e-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: 80.59  E-value: 3.79e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12643975  661 KCEKQRAQMQNLAgAQPAGSSFFVPTCTSEGYFLPVQCFNS--ECYCVDAEGQVIPGTQSTIGEPK 724
Cdd:cd00191    1 PCERERASALESL-AGPKLSGLYVPQCDEDGNYEPVQCHGStgYCWCVDPDGEEIPGTRTRGGPPN 65
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 301-359 7.80e-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: 79.82  E-value: 7.80e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12643975  301 KCEVEQFTATS------FGHPYIPSCHRDGHYQTVQCQME-RMCWCVDAQGIEIPGTRQQGQPLFC 359
Cdd:cd00191    1 PCERERASALEslagpkLSGLYVPQCDEDGNYEPVQCHGStGYCWCVDPDGEEIPGTRTRGGPPNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1150-1211 9.19e-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: 9.19e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12643975 1150 CDALKSRVLSRKVGLG----YTPVCEAlDGGFSPVQCDLAQGSCWCVLASGEEVPGTRVVGTQPAC 1211
Cdd:cd00191    2 CERERASALESLAGPKlsglYVPQCDE-DGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRGGPPNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 613-658 2.61e-16

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: 75.58  E-value: 2.61e-16
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 12643975  613 GRFFVPSCTAEGSYEDIQCYA--GECWCVNSQGKEVEGSRVSGGHPRC 658
Cdd:cd00191   19 SGLYVPQCDEDGNYEPVQCHGstGYCWCVDPDGEEIPGTRTRGGPPNC 66
Ephrin_rec_like pfam07699
Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region ...
 1464-1509 8.03e-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: 8.03e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 12643975   1464 GSFSQDG--KCTPCPAGTYQGQAGSSACIPCPRGRTTTITGAFSKTHC 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 2.84e-07

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: 48.91  E-value: 2.84e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 12643975    1519 GLQCDQNGQYQANQKDMDSGEVFCVDSEGQRLQWlqTEAGLSESQCLM 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 1.73e-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: 44.76  E-value: 1.73e-05
                         10        20        30
                 ....*....|....*....|....*....|
gi 12643975  893 HFNLRSCWCVDEAGQELDGTRTRAGEiPAC 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 ...
 730-776 1.74e-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 pfam00086:

Pssm-ID: 469630  Cd Length: 66  Bit Score: 41.90  E-value: 1.74e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 12643975    730 CQLQAEQAflgvvgvlLSNSSMVPPISSVYIPQCSTSGQWMPVQCDG 776
Cdd:pfam00086    1 CERERARA--------LEQAASGRPASGLYIPNCDEDGFYKPVQCHG 39
TY super family cl00150
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 164-249 2.18e-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: 2.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975  164 SCEIRSRRLLHGVGDKSP-----PQCDADGEFMPVQCkfvnttdmmifdliHNYNrfpdafvtfsafrnrfpevsGYCYC 238
Cdd:cd00191    1 PCERERASALESLAGPKLsglyvPQCDEDGNYEPVQC--------------HGST--------------------GYCWC 46

                         90
                 ....*....|.
gi 12643975  239 ADSQGRELAET 249
Cdd:cd00191   47 VDPDGEEIPGT 57
 
Name Accession Description Interval E-value
COesterase pfam00135
Carboxylesterase family;
2198-2719 5.63e-175

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 548.45  E-value: 5.63e-175
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975   2198 STPSVHIdSFGQLQGGSQVVKVGtawKQVYQFLGVPYAAPPLAENRFQAPE-VLNWTGSWDATKLRSSCWQPGTRTPTPP 2276
Cdd:pfam00135    1 DSPVVTT-SLGRVRGKRLKVDGG---KPVYAFLGIPYAEPPVGELRFQPPEpPEPWTGVRDATKFGPRCPQNGDLTSPGS 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975   2277 Q---ISEDCLYLNVFVPENLVSNA---SVLVFFHNTVEMEGSGGQlnIDGSILAAVGNLIVVTANYRLGVFGFLSSGSDE 2350
Cdd:pfam00135   77 SgleGSEDCLYLNVYTPKELKENKnklPVMVWIHGGGFMFGSGSL--YDGSYLAAEGDVIVVTINYRLGPLGFLSTGDDE 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975   2351 VAGNWGLLDQVAALTWVQTHIGAFGGDPQRVTLAADRGGADVASIHLLitRPTRLQLFRKALLMGGSALSPAAIISPDRa 2430
Cdd:pfam00135  155 APGNYGLLDQVLALRWVQENIASFGGDPNRVTLFGESAGAASVSLLLL--SPLSKGLFHRAILMSGSALSPWAIQSNAR- 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975   2431 qQQAAALAKEVGCPNSSVQEVVSCFRQKPANILNEAQTKLL-AVSGPFHYWGPVVDGQYLRELPSRRLKRPLPVKVDLLI 2509
Cdd:pfam00135  232 -QRAKELAKLVGCPTSDSAELVECLRSKPAEELLDAQLKLLvYGSVPFVPFGPVVDGDFLPEHPEELLKSGNFPKVPLLI 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975   2510 GGSQDDGLINRA------KAVKQFEESQGRTNSKTAFYQALqnslggEDSDARILAAAIWYYSLEHSTDDYASFSRALEN 2583
Cdd:pfam00135  311 GVTKDEGLLFAAyildnvDILKALEEKLLRSLLIDLLYLLL------VDLPEEISAALREEYLDWGDRDDPETSRRALVE 384

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975   2584 ATRDYFIICPIVNMASLWARRtRGNVFMYH---------VPESYG--HGSlellaDVQYAFGLPFYSAYQgyFSTEEQSL 2652
Cdd:pfam00135  385 LLTDYLFNCPVIRFADLHASR-GTPVYMYSfdyrgsslrYPKWVGvdHGD-----ELPYVFGTPFVGALL--FTEEDEKL 456

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 12643975   2653 SLKVMQYFSNFIRSGNPNYPhefsqkaaEFATPWPDFVPgaggESYKELSAQLPNR--QGLKKADCSFW 2719
Cdd:pfam00135  457 SRKMMTYWTNFAKTGNPNGP--------EGLPKWPPYTD----ENGQYLSIDLEPRvkQGLKAERCAFW 513
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
2198-2694 4.40e-95

Carboxylesterase type B [Lipid transport and metabolism];


Pssm-ID: 441873  Cd Length: 500  Bit Score: 318.37  E-value: 4.40e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975 2198 STPSVHIDSfGQLQGgsqVVKVGtawkqVYQFLGVPYAAPPLAENRFQAPE-VLNWTGSWDATKLRSSCWQPGTRT--PT 2274
Cdd:COG2272   11 AAPVVRTEA-GRVRG---VVEGG-----VRVFLGIPYAAPPVGELRWRAPQpVEPWTGVRDATEFGPACPQPPRPGdpGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975 2275 PPQISEDCLYLNVFVPENLVS-NASVLVFFH---NTVemeGSGGQLNIDGSILAAVGnLIVVTANYRLGVFGF-----LS 2345
Cdd:COG2272   82 PAPGSEDCLYLNVWTPALAAGaKLPVMVWIHgggFVS---GSGSEPLYDGAALARRG-VVVVTINYRLGALGFlalpaLS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975 2346 SGSDEVAGNWGLLDQVAALTWVQTHIGAFGGDPQRVTLAADRGGAdvASIHLLITRPTRLQLFRKALLMGGSALSPAaii 2425
Cdd:COG2272  158 GESYGASGNYGLLDQIAALRWVRDNIAAFGGDPDNVTIFGESAGA--ASVAALLASPLAKGLFHRAIAQSGAGLSVL--- 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975 2426 SPDRAQQQAAALAKEVGCPNSSVQevvsCFRQKPANILNEAQTKLLAVSGPFHYWGPVVDGQYLRELPSRRLKRPLPVKV 2505
Cdd:COG2272  233 TLAEAEAVGAAFAAALGVAPATLA----ALRALPAEELLAAQAALAAEGPGGLPFGPVVDGDVLPEDPLEAFAAGRAADV 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975 2506 DLLIGGSQDDGLInrakavkqFEESQGRTNSKT-AFYQALQNSLGGEDSDaRILAAaiwyyslehstddY--ASFSRALE 2582
Cdd:COG2272  309 PLLIGTNRDEGRL--------FAALLGDLGPLTaADYRAALRRRFGDDAD-EVLAA-------------YpaASPAEALA 366

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975 2583 NATRDYFIICPIVNMASLWArRTRGNVFMY---HVPESYG-------HGslellADVQYAFGLPFYSAYQGyFSTEEQSL 2652
Cdd:COG2272  367 ALATDRVFRCPARRLAEAHA-AAGAPVYLYrfdWRSPPLRgfglgafHG-----AELPFVFGNLDAPALTG-LTPADRAL 439

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|..
gi 12643975 2653 SLKVMQYFSNFIRSGNPNyphefsqkaAEFATPWPDFVPGAG 2694
Cdd:COG2272  440 SDQMQAYWVNFARTGDPN---------GPGLPEWPAYDPEDR 472
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 2226-2703 5.15e-95

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: 317.74  E-value: 5.15e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975 2226 VYQFLGVPYAAPPLAENRFQAPEVLN-WTGSWDATKLRSSCWQP----GTRTPTPPQISEDCLYLNVFVPENLVSNAS-- 2298
Cdd:cd00312   17 VYSFLGIPYAEPPVGDLRFKEPQPYEpWSDVLDATSYPPSCMQWdqlgGGLWNAKLPGSEDCLYLNVYTPKNTKPGNSlp 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975 2299 VLVFFHNTVEMEGSGGQLNIDGsILAAVGNLIVVTANYRLGVFGFLSSGSDEVAGNWGLLDQVAALTWVQTHIGAFGGDP 2378
Cdd:cd00312   97 VMVWIHGGGFMFGSGSLYPGDG-LAREGDNVIVVSINYRLGVLGFLSTGDIELPGNYGLKDQRLALKWVQDNIAAFGGDP 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975 2379 QRVTLAADRGGAdvASIHLLITRPTRLQLFRKALLMGGSALSPAAIisPDRAQQQAAALAKEVGCPNSSVQEVVSCFRQK 2458
Cdd:cd00312  176 DSVTIFGESAGG--ASVSLLLLSPDSKGLFHRAISQSGSALSPWAI--QENARGRAKRLARLLGCNDTSSAELLDCLRSK 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975 2459 PANILNEAQTKLLAVSG-PFHYWGPVVDGQYLRELPSRRLKRPLPVKVDLLIGGSQDDGLINRAKAVKQFEESQGRTNsk 2537
Cdd:cd00312  252 SAEELLDATRKLLLFSYsPFLPFGPVVDGDFIPDDPEELIKEGKFAKVPLIIGVTKDEGGYFAAMLLNFDAKLIIETN-- 329

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975 2538 TAFYQALQNSLGGEDSD-ARILAAAiwYY-SLEHSTDDYASFSRALEnatrDYFIICPIVNMASLWARRTRGNVFMY--- 2612
Cdd:cd00312  330 DRWLELLPYLLFYADDAlADKVLEK--YPgDVDDSVESRKNLSDMLT----DLLFKCPARYFLAQHRKAGGSPVYAYvfd 403

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975 2613 HVPE-SYGHGSLELLA----DVQYAFGLPFYSayqGYFSTEEQSLSLKVMQYFSNFIRSGNPNYPHEFSQkaaefatpWP 2687
Cdd:cd00312  404 HRSSlSVGRWPPWLGTvhgdEIFFVFGNPLLK---EGLREEEEKLSRTMMKYWANFAKTGNPNTEGNLVV--------WP 472

                        490
                 ....*....|....*.
gi 12643975 2688 DFVpgAGGESYKELSA 2703
Cdd:cd00312  473 AYT--SESEKYLDINI 486
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 96-161 2.41e-23

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: 95.22  E-value: 2.41e-23
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12643975   96 FCQLHKQRILLSSYINSTDALYLPQCQDSGNYAPVQCDLQQVQCWCVDTEGMEVYGTRQQGRPTRC 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 2.48e-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: 2.48e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12643975     97 CQLHKQRILLS-SYINSTDALYLPQCQDSGNYAPVQCDLQQVQCWCVDTEGMEVYGTRQQGRPTRC 161
Cdd:pfam00086    1 CERERARALEQaASGRPASGLYIPNCDEDGFYKPVQCHGSTGYCWCVDPEGQEIPGTRTRGGDPDC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1005-1074 5.27e-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: 85.98  E-value: 5.27e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975 1005 FYQKLRASLGESNgtASLLWSGPYMPQCNTIGGWEPVQCHPGTGQCWCVDGWGELIPGSLMARssQMPQC 1074
Cdd:cd00191    1 PCERERASALESL--AGPKLSGLYVPQCDEDGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRG--GPPNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 34-93 4.67e-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: 4.67e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12643975   34 PCELQREKAF------LKQDEYVPQCSEDGSFQTVQCQNDGQSCWCVDSDGTEVPGSRQLGRPTAC 93
Cdd:cd00191    1 PCERERASALeslagpKLSGLYVPQCDEDGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRGGPPNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 661-724 3.79e-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: 80.59  E-value: 3.79e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12643975  661 KCEKQRAQMQNLAgAQPAGSSFFVPTCTSEGYFLPVQCFNS--ECYCVDAEGQVIPGTQSTIGEPK 724
Cdd:cd00191    1 PCERERASALESL-AGPKLSGLYVPQCDEDGNYEPVQCHGStgYCWCVDPDGEEIPGTRTRGGPPN 65
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 662-724 7.25e-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: 7.25e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 12643975    662 CEKQRAQMQNLAGAQPAGSSFFVPTCTSEGYFLPVQCFNS--ECYCVDAEGQVIPGTQSTIGEPK 724
Cdd:pfam00086    1 CERERARALEQAASGRPASGLYIPNCDEDGFYKPVQCHGStgYCWCVDPEGQEIPGTRTRGGDPD 65
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 301-359 7.80e-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: 79.82  E-value: 7.80e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12643975  301 KCEVEQFTATS------FGHPYIPSCHRDGHYQTVQCQME-RMCWCVDAQGIEIPGTRQQGQPLFC 359
Cdd:cd00191    1 PCERERASALEslagpkLSGLYVPQCDEDGNYEPVQCHGStGYCWCVDPDGEEIPGTRTRGGPPNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1150-1211 9.19e-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: 9.19e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12643975 1150 CDALKSRVLSRKVGLG----YTPVCEAlDGGFSPVQCDLAQGSCWCVLASGEEVPGTRVVGTQPAC 1211
Cdd:cd00191    2 CERERASALESLAGPKlsglYVPQCDE-DGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRGGPPNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 613-658 2.61e-16

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: 75.58  E-value: 2.61e-16
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 12643975  613 GRFFVPSCTAEGSYEDIQCYA--GECWCVNSQGKEVEGSRVSGGHPRC 658
Cdd:cd00191   19 SGLYVPQCDEDGNYEPVQCHGstGYCWCVDPDGEEIPGTRTRGGPPNC 66
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 35-93 3.95e-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: 75.03  E-value: 3.95e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12643975     35 CELQREKAFLKQDE-------YVPQCSEDGSFQTVQCQNDGQSCWCVDSDGTEVPGSRQLGRPTAC 93
Cdd:pfam00086    1 CERERARALEQAASgrpasglYIPNCDEDGFYKPVQCHGSTGYCWCVDPEGQEIPGTRTRGGDPDC 66
Ephrin_rec_like pfam07699
Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region ...
 1464-1509 8.03e-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: 8.03e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 12643975   1464 GSFSQDG--KCTPCPAGTYQGQAGSSACIPCPRGRTTTITGAFSKTHC 1509
Cdd:pfam07699    1 GTYSNTGlePCIPCPRGTYQPEEGQLSCLACPLGTTTDSPGATSISDC 48
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 1007-1074 8.35e-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: 71.18  E-value: 8.35e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 12643975   1007 QKLRAS-LGESNGTASLlwSGPYMPQCNTIGGWEPVQCHPGTGQCWCVDGWGELIPGSlmARSSQMPQC 1074
Cdd:pfam00086    2 ERERARaLEQAASGRPA--SGLYIPNCDEDGFYKPVQCHGSTGYCWCVDPEGQEIPGT--RTRGGDPDC 66
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 118-163 8.60e-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: 70.48  E-value: 8.60e-15
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 12643975     118 LPQCQDSGNYAPVQCDLQQVQCWCVDTEGMEVYGTRQQGRPTRCPR 163
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSSGQCWCVDATGREIPGTRTEGGDPDCPS 46
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 50-95 7.36e-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: 67.79  E-value: 7.36e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 12643975      50 VPQCSEDGSFQTVQCQNDGQSCWCVDSDGTEVPGSRQLGRPTACLS 95
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSSGQCWCVDATGREIPGTRTEGGDPDCPS 46
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 614-658 2.20e-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: 66.94  E-value: 2.20e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 12643975    614 RFFVPSCTAEGSYEDIQCY--AGECWCVNSQGKEVEGSRVSGGHPRC 658
Cdd:pfam00086   20 GLYIPNCDEDGFYKPVQCHgsTGYCWCVDPEGQEIPGTRTRGGDPDC 66
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 302-359 3.94e-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: 66.17  E-value: 3.94e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12643975    302 CEVEQFTA---TSFGHP----YIPSCHRDGHYQTVQCQMER-MCWCVDAQGIEIPGTRQQGQPLFC 359
Cdd:pfam00086    1 CERERARAleqAASGRPasglYIPNCDEDGFYKPVQCHGSTgYCWCVDPEGQEIPGTRTRGGDPDC 66
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1168-1213 1.05e-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: 1.05e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 12643975    1168 PVCEAlDGGFSPVQCDLAQGSCWCVLASGEEVPGTRVVGTQPACES 1213
Cdd:smart00211    2 PQCDE-DGNYEPVQCDGSSGQCWCVDATGREIPGTRTEGGDPDCPS 46
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 317-359 1.30e-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: 1.30e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 12643975     317 IPSCHRDGHYQTVQCQMER-MCWCVDAQGIEIPGTRQQGQPLFC 359
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSSgQCWCVDATGREIPGTRTEGGDPDC 44
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 617-660 3.13e-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: 3.13e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 12643975     617 VPSCTAEGSYEDIQCYA--GECWCVNSQGKEVEGSRVSGGHPRCPT 660
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGssGQCWCVDATGREIPGTRTEGGDPDCPS 46
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 1150-1211 8.55e-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: 8.55e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12643975   1150 CDALKSRVLSRKVGLG-----YTPVCEAlDGGFSPVQCDLAQGSCWCVLASGEEVPGTRVVGTQPAC 1211
Cdd:pfam00086    1 CERERARALEQAASGRpasglYIPNCDE-DGFYKPVQCHGSTGYCWCVDPEGQEIPGTRTRGGDPDC 66
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 684-728 2.36e-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: 60.47  E-value: 2.36e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 12643975     684 VPTCTSEGYFLPVQCFNS--ECYCVDAEGQVIPGTQSTIGEPKlCPS 728
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSsgQCWCVDATGREIPGTRTEGGDPD-CPS 46
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1029-1076 2.96e-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: 60.47  E-value: 2.96e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 12643975    1029 MPQCNTIGGWEPVQCHPGTGQCWCVDGWGELIPGSLMARSSqmPQCPT 1076
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSSGQCWCVDATGREIPGTRTEGGD--PDCPS 46
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1519-1566 2.84e-07

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: 48.91  E-value: 2.84e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 12643975    1519 GLQCDQNGQYQANQKDMDSGEVFCVDSEGQRLQWlqTEAGLSESQCLM 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 1.73e-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: 44.76  E-value: 1.73e-05
                         10        20        30
                 ....*....|....*....|....*....|
gi 12643975  893 HFNLRSCWCVDEAGQELDGTRTRAGEiPAC 922
Cdd:cd00191   38 HGSTGYCWCVDPDGEEIPGTRTRGGP-PNC 66
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 893-923 3.77e-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 and binding partners of heparin.


Pssm-ID: 214561  Cd Length: 46  Bit Score: 43.14  E-value: 3.77e-05
                            10        20        30
                    ....*....|....*....|....*....|.
gi 12643975     893 HFNLRSCWCVDEAGQELDGTRTRAGEiPACP 923
Cdd:smart00211   16 DGSSGQCWCVDATGREIPGTRTEGGD-PDCP 45
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 899-922 8.26e-05

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: 42.68  E-value: 8.26e-05
                           10        20
                   ....*....|....*....|....
gi 12643975    899 CWCVDEAGQELDGTRTRAGEiPAC 922
Cdd:pfam00086   44 CWCVDPEGQEIPGTRTRGGD-PDC 66
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 730-776 1.74e-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: 41.90  E-value: 1.74e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 12643975    730 CQLQAEQAflgvvgvlLSNSSMVPPISSVYIPQCSTSGQWMPVQCDG 776
Cdd:pfam00086    1 CERERARA--------LEQAASGRPASGLYIPNCDEDGFYKPVQCHG 39
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 164-249 2.18e-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: 2.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975  164 SCEIRSRRLLHGVGDKSP-----PQCDADGEFMPVQCkfvnttdmmifdliHNYNrfpdafvtfsafrnrfpevsGYCYC 238
Cdd:cd00191    1 PCERERASALESLAGPKLsglyvPQCDEDGNYEPVQC--------------HGST--------------------GYCWC 46

                         90
                 ....*....|.
gi 12643975  239 ADSQGRELAET 249
Cdd:cd00191   47 VDPDGEEIPGT 57
TNFRSF21 cd10583
Tumor necrosis factor receptor superfamily member 21 (TNFRSF21), also known as death receptor ...
 1450-1514 2.51e-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: 43.97  E-value: 2.51e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12643975 1450 TTSQDPLgCVkCPEGSFSQDGKCTP---CPAGTYQGQAGSSA----CIPCPRGRTTTITGAFSKTHCVTDCQ 1514
Cdd:cd10583   72 TALTDRE-CT-CPPGTFLSNDTCVPhsvCPVGWGVRKKGTETedvrCKPCPRGTFSDVPSSVLKCKTYTDCL 141
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 730-776 7.08e-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: 40.14  E-value: 7.08e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 12643975  730 CQLQAEQAFlgvvgvllsNSSMVPPISSVYIPQCSTSGQWMPVQCDG 776
Cdd:cd00191    2 CERERASAL---------ESLAGPKLSGLYVPQCDEDGNYEPVQCHG 39
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 1521-1550 8.06e-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: 37.28  E-value: 8.06e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 12643975   1521 QCDQNGQYQANQKDMDSGEVFCVDSEGQRL 1550
Cdd:pfam00086   25 NCDEDGFYKPVQCHGSTGYCWCVDPEGQEI 54
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1521-1551 8.44e-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: 37.06  E-value: 8.44e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 12643975 1521 QCDQNGQYQANQKDMDSGEVFCVDSEGQRLQ 1551
Cdd:cd00191   25 QCDEDGNYEPVQCHGSTGYCWCVDPDGEEIP 55
 
Name Accession Description Interval E-value
COesterase pfam00135
Carboxylesterase family;
2198-2719 5.63e-175

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 548.45  E-value: 5.63e-175
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975   2198 STPSVHIdSFGQLQGGSQVVKVGtawKQVYQFLGVPYAAPPLAENRFQAPE-VLNWTGSWDATKLRSSCWQPGTRTPTPP 2276
Cdd:pfam00135    1 DSPVVTT-SLGRVRGKRLKVDGG---KPVYAFLGIPYAEPPVGELRFQPPEpPEPWTGVRDATKFGPRCPQNGDLTSPGS 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975   2277 Q---ISEDCLYLNVFVPENLVSNA---SVLVFFHNTVEMEGSGGQlnIDGSILAAVGNLIVVTANYRLGVFGFLSSGSDE 2350
Cdd:pfam00135   77 SgleGSEDCLYLNVYTPKELKENKnklPVMVWIHGGGFMFGSGSL--YDGSYLAAEGDVIVVTINYRLGPLGFLSTGDDE 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975   2351 VAGNWGLLDQVAALTWVQTHIGAFGGDPQRVTLAADRGGADVASIHLLitRPTRLQLFRKALLMGGSALSPAAIISPDRa 2430
Cdd:pfam00135  155 APGNYGLLDQVLALRWVQENIASFGGDPNRVTLFGESAGAASVSLLLL--SPLSKGLFHRAILMSGSALSPWAIQSNAR- 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975   2431 qQQAAALAKEVGCPNSSVQEVVSCFRQKPANILNEAQTKLL-AVSGPFHYWGPVVDGQYLRELPSRRLKRPLPVKVDLLI 2509
Cdd:pfam00135  232 -QRAKELAKLVGCPTSDSAELVECLRSKPAEELLDAQLKLLvYGSVPFVPFGPVVDGDFLPEHPEELLKSGNFPKVPLLI 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975   2510 GGSQDDGLINRA------KAVKQFEESQGRTNSKTAFYQALqnslggEDSDARILAAAIWYYSLEHSTDDYASFSRALEN 2583
Cdd:pfam00135  311 GVTKDEGLLFAAyildnvDILKALEEKLLRSLLIDLLYLLL------VDLPEEISAALREEYLDWGDRDDPETSRRALVE 384

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975   2584 ATRDYFIICPIVNMASLWARRtRGNVFMYH---------VPESYG--HGSlellaDVQYAFGLPFYSAYQgyFSTEEQSL 2652
Cdd:pfam00135  385 LLTDYLFNCPVIRFADLHASR-GTPVYMYSfdyrgsslrYPKWVGvdHGD-----ELPYVFGTPFVGALL--FTEEDEKL 456

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 12643975   2653 SLKVMQYFSNFIRSGNPNYPhefsqkaaEFATPWPDFVPgaggESYKELSAQLPNR--QGLKKADCSFW 2719
Cdd:pfam00135  457 SRKMMTYWTNFAKTGNPNGP--------EGLPKWPPYTD----ENGQYLSIDLEPRvkQGLKAERCAFW 513
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
2198-2694 4.40e-95

Carboxylesterase type B [Lipid transport and metabolism];


Pssm-ID: 441873  Cd Length: 500  Bit Score: 318.37  E-value: 4.40e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975 2198 STPSVHIDSfGQLQGgsqVVKVGtawkqVYQFLGVPYAAPPLAENRFQAPE-VLNWTGSWDATKLRSSCWQPGTRT--PT 2274
Cdd:COG2272   11 AAPVVRTEA-GRVRG---VVEGG-----VRVFLGIPYAAPPVGELRWRAPQpVEPWTGVRDATEFGPACPQPPRPGdpGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975 2275 PPQISEDCLYLNVFVPENLVS-NASVLVFFH---NTVemeGSGGQLNIDGSILAAVGnLIVVTANYRLGVFGF-----LS 2345
Cdd:COG2272   82 PAPGSEDCLYLNVWTPALAAGaKLPVMVWIHgggFVS---GSGSEPLYDGAALARRG-VVVVTINYRLGALGFlalpaLS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975 2346 SGSDEVAGNWGLLDQVAALTWVQTHIGAFGGDPQRVTLAADRGGAdvASIHLLITRPTRLQLFRKALLMGGSALSPAaii 2425
Cdd:COG2272  158 GESYGASGNYGLLDQIAALRWVRDNIAAFGGDPDNVTIFGESAGA--ASVAALLASPLAKGLFHRAIAQSGAGLSVL--- 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975 2426 SPDRAQQQAAALAKEVGCPNSSVQevvsCFRQKPANILNEAQTKLLAVSGPFHYWGPVVDGQYLRELPSRRLKRPLPVKV 2505
Cdd:COG2272  233 TLAEAEAVGAAFAAALGVAPATLA----ALRALPAEELLAAQAALAAEGPGGLPFGPVVDGDVLPEDPLEAFAAGRAADV 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975 2506 DLLIGGSQDDGLInrakavkqFEESQGRTNSKT-AFYQALQNSLGGEDSDaRILAAaiwyyslehstddY--ASFSRALE 2582
Cdd:COG2272  309 PLLIGTNRDEGRL--------FAALLGDLGPLTaADYRAALRRRFGDDAD-EVLAA-------------YpaASPAEALA 366

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975 2583 NATRDYFIICPIVNMASLWArRTRGNVFMY---HVPESYG-------HGslellADVQYAFGLPFYSAYQGyFSTEEQSL 2652
Cdd:COG2272  367 ALATDRVFRCPARRLAEAHA-AAGAPVYLYrfdWRSPPLRgfglgafHG-----AELPFVFGNLDAPALTG-LTPADRAL 439

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|..
gi 12643975 2653 SLKVMQYFSNFIRSGNPNyphefsqkaAEFATPWPDFVPGAG 2694
Cdd:COG2272  440 SDQMQAYWVNFARTGDPN---------GPGLPEWPAYDPEDR 472
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 2226-2703 5.15e-95

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: 317.74  E-value: 5.15e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975 2226 VYQFLGVPYAAPPLAENRFQAPEVLN-WTGSWDATKLRSSCWQP----GTRTPTPPQISEDCLYLNVFVPENLVSNAS-- 2298
Cdd:cd00312   17 VYSFLGIPYAEPPVGDLRFKEPQPYEpWSDVLDATSYPPSCMQWdqlgGGLWNAKLPGSEDCLYLNVYTPKNTKPGNSlp 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975 2299 VLVFFHNTVEMEGSGGQLNIDGsILAAVGNLIVVTANYRLGVFGFLSSGSDEVAGNWGLLDQVAALTWVQTHIGAFGGDP 2378
Cdd:cd00312   97 VMVWIHGGGFMFGSGSLYPGDG-LAREGDNVIVVSINYRLGVLGFLSTGDIELPGNYGLKDQRLALKWVQDNIAAFGGDP 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975 2379 QRVTLAADRGGAdvASIHLLITRPTRLQLFRKALLMGGSALSPAAIisPDRAQQQAAALAKEVGCPNSSVQEVVSCFRQK 2458
Cdd:cd00312  176 DSVTIFGESAGG--ASVSLLLLSPDSKGLFHRAISQSGSALSPWAI--QENARGRAKRLARLLGCNDTSSAELLDCLRSK 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975 2459 PANILNEAQTKLLAVSG-PFHYWGPVVDGQYLRELPSRRLKRPLPVKVDLLIGGSQDDGLINRAKAVKQFEESQGRTNsk 2537
Cdd:cd00312  252 SAEELLDATRKLLLFSYsPFLPFGPVVDGDFIPDDPEELIKEGKFAKVPLIIGVTKDEGGYFAAMLLNFDAKLIIETN-- 329

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975 2538 TAFYQALQNSLGGEDSD-ARILAAAiwYY-SLEHSTDDYASFSRALEnatrDYFIICPIVNMASLWARRTRGNVFMY--- 2612
Cdd:cd00312  330 DRWLELLPYLLFYADDAlADKVLEK--YPgDVDDSVESRKNLSDMLT----DLLFKCPARYFLAQHRKAGGSPVYAYvfd 403

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975 2613 HVPE-SYGHGSLELLA----DVQYAFGLPFYSayqGYFSTEEQSLSLKVMQYFSNFIRSGNPNYPHEFSQkaaefatpWP 2687
Cdd:cd00312  404 HRSSlSVGRWPPWLGTvhgdEIFFVFGNPLLK---EGLREEEEKLSRTMMKYWANFAKTGNPNTEGNLVV--------WP 472

                        490
                 ....*....|....*.
gi 12643975 2688 DFVpgAGGESYKELSA 2703
Cdd:cd00312  473 AYT--SESEKYLDINI 486
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 96-161 2.41e-23

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: 95.22  E-value: 2.41e-23
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12643975   96 FCQLHKQRILLSSYINSTDALYLPQCQDSGNYAPVQCDLQQVQCWCVDTEGMEVYGTRQQGRPTRC 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 2.48e-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: 2.48e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12643975     97 CQLHKQRILLS-SYINSTDALYLPQCQDSGNYAPVQCDLQQVQCWCVDTEGMEVYGTRQQGRPTRC 161
Cdd:pfam00086    1 CERERARALEQaASGRPASGLYIPNCDEDGFYKPVQCHGSTGYCWCVDPEGQEIPGTRTRGGDPDC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1005-1074 5.27e-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: 85.98  E-value: 5.27e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975 1005 FYQKLRASLGESNgtASLLWSGPYMPQCNTIGGWEPVQCHPGTGQCWCVDGWGELIPGSLMARssQMPQC 1074
Cdd:cd00191    1 PCERERASALESL--AGPKLSGLYVPQCDEDGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRG--GPPNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 34-93 4.67e-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: 4.67e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12643975   34 PCELQREKAF------LKQDEYVPQCSEDGSFQTVQCQNDGQSCWCVDSDGTEVPGSRQLGRPTAC 93
Cdd:cd00191    1 PCERERASALeslagpKLSGLYVPQCDEDGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRGGPPNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 661-724 3.79e-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: 80.59  E-value: 3.79e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12643975  661 KCEKQRAQMQNLAgAQPAGSSFFVPTCTSEGYFLPVQCFNS--ECYCVDAEGQVIPGTQSTIGEPK 724
Cdd:cd00191    1 PCERERASALESL-AGPKLSGLYVPQCDEDGNYEPVQCHGStgYCWCVDPDGEEIPGTRTRGGPPN 65
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 662-724 7.25e-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: 7.25e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 12643975    662 CEKQRAQMQNLAGAQPAGSSFFVPTCTSEGYFLPVQCFNS--ECYCVDAEGQVIPGTQSTIGEPK 724
Cdd:pfam00086    1 CERERARALEQAASGRPASGLYIPNCDEDGFYKPVQCHGStgYCWCVDPEGQEIPGTRTRGGDPD 65
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 301-359 7.80e-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: 79.82  E-value: 7.80e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12643975  301 KCEVEQFTATS------FGHPYIPSCHRDGHYQTVQCQME-RMCWCVDAQGIEIPGTRQQGQPLFC 359
Cdd:cd00191    1 PCERERASALEslagpkLSGLYVPQCDEDGNYEPVQCHGStGYCWCVDPDGEEIPGTRTRGGPPNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1150-1211 9.19e-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: 9.19e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12643975 1150 CDALKSRVLSRKVGLG----YTPVCEAlDGGFSPVQCDLAQGSCWCVLASGEEVPGTRVVGTQPAC 1211
Cdd:cd00191    2 CERERASALESLAGPKlsglYVPQCDE-DGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRGGPPNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 613-658 2.61e-16

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: 75.58  E-value: 2.61e-16
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 12643975  613 GRFFVPSCTAEGSYEDIQCYA--GECWCVNSQGKEVEGSRVSGGHPRC 658
Cdd:cd00191   19 SGLYVPQCDEDGNYEPVQCHGstGYCWCVDPDGEEIPGTRTRGGPPNC 66
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 35-93 3.95e-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: 75.03  E-value: 3.95e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12643975     35 CELQREKAFLKQDE-------YVPQCSEDGSFQTVQCQNDGQSCWCVDSDGTEVPGSRQLGRPTAC 93
Cdd:pfam00086    1 CERERARALEQAASgrpasglYIPNCDEDGFYKPVQCHGSTGYCWCVDPEGQEIPGTRTRGGDPDC 66
Ephrin_rec_like pfam07699
Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region ...
 1464-1509 8.03e-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: 8.03e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 12643975   1464 GSFSQDG--KCTPCPAGTYQGQAGSSACIPCPRGRTTTITGAFSKTHC 1509
Cdd:pfam07699    1 GTYSNTGlePCIPCPRGTYQPEEGQLSCLACPLGTTTDSPGATSISDC 48
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 1007-1074 8.35e-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: 71.18  E-value: 8.35e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 12643975   1007 QKLRAS-LGESNGTASLlwSGPYMPQCNTIGGWEPVQCHPGTGQCWCVDGWGELIPGSlmARSSQMPQC 1074
Cdd:pfam00086    2 ERERARaLEQAASGRPA--SGLYIPNCDEDGFYKPVQCHGSTGYCWCVDPEGQEIPGT--RTRGGDPDC 66
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 118-163 8.60e-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: 70.48  E-value: 8.60e-15
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 12643975     118 LPQCQDSGNYAPVQCDLQQVQCWCVDTEGMEVYGTRQQGRPTRCPR 163
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSSGQCWCVDATGREIPGTRTEGGDPDCPS 46
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 50-95 7.36e-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: 67.79  E-value: 7.36e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 12643975      50 VPQCSEDGSFQTVQCQNDGQSCWCVDSDGTEVPGSRQLGRPTACLS 95
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSSGQCWCVDATGREIPGTRTEGGDPDCPS 46
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 614-658 2.20e-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: 66.94  E-value: 2.20e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 12643975    614 RFFVPSCTAEGSYEDIQCY--AGECWCVNSQGKEVEGSRVSGGHPRC 658
Cdd:pfam00086   20 GLYIPNCDEDGFYKPVQCHgsTGYCWCVDPEGQEIPGTRTRGGDPDC 66
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 302-359 3.94e-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: 66.17  E-value: 3.94e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12643975    302 CEVEQFTA---TSFGHP----YIPSCHRDGHYQTVQCQMER-MCWCVDAQGIEIPGTRQQGQPLFC 359
Cdd:pfam00086    1 CERERARAleqAASGRPasglYIPNCDEDGFYKPVQCHGSTgYCWCVDPEGQEIPGTRTRGGDPDC 66
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1168-1213 1.05e-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: 1.05e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 12643975    1168 PVCEAlDGGFSPVQCDLAQGSCWCVLASGEEVPGTRVVGTQPACES 1213
Cdd:smart00211    2 PQCDE-DGNYEPVQCDGSSGQCWCVDATGREIPGTRTEGGDPDCPS 46
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 317-359 1.30e-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: 1.30e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 12643975     317 IPSCHRDGHYQTVQCQMER-MCWCVDAQGIEIPGTRQQGQPLFC 359
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSSgQCWCVDATGREIPGTRTEGGDPDC 44
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 617-660 3.13e-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: 3.13e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 12643975     617 VPSCTAEGSYEDIQCYA--GECWCVNSQGKEVEGSRVSGGHPRCPT 660
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGssGQCWCVDATGREIPGTRTEGGDPDCPS 46
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 1150-1211 8.55e-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: 8.55e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12643975   1150 CDALKSRVLSRKVGLG-----YTPVCEAlDGGFSPVQCDLAQGSCWCVLASGEEVPGTRVVGTQPAC 1211
Cdd:pfam00086    1 CERERARALEQAASGRpasglYIPNCDE-DGFYKPVQCHGSTGYCWCVDPEGQEIPGTRTRGGDPDC 66
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 684-728 2.36e-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: 60.47  E-value: 2.36e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 12643975     684 VPTCTSEGYFLPVQCFNS--ECYCVDAEGQVIPGTQSTIGEPKlCPS 728
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSsgQCWCVDATGREIPGTRTEGGDPD-CPS 46
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1029-1076 2.96e-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: 60.47  E-value: 2.96e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 12643975    1029 MPQCNTIGGWEPVQCHPGTGQCWCVDGWGELIPGSLMARSSqmPQCPT 1076
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSSGQCWCVDATGREIPGTRTEGGD--PDCPS 46
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1519-1566 2.84e-07

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: 48.91  E-value: 2.84e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 12643975    1519 GLQCDQNGQYQANQKDMDSGEVFCVDSEGQRLQWlqTEAGLSESQCLM 1566
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSSGQCWCVDATGREIPG--TRTEGGDPDCPS 46
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
2287-2386 1.69e-06

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 51.41  E-value: 1.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975 2287 VFVPENLVSNASVLVFFHntvemeGSG---GQLNIDGSI---LAAVGNLIVVTANYRLgvfgflssgSDEVAGNWGLLDQ 2360
Cdd:COG0657    3 VYRPAGAKGPLPVVVYFH------GGGwvsGSKDTHDPLarrLAARAGAAVVSVDYRL---------APEHPFPAALEDA 67

                         90       100
                 ....*....|....*....|....*.
gi 12643975 2361 VAALTWVQTHIGAFGGDPQRVTLAAD 2386
Cdd:COG0657   68 YAALRWLRANAAELGIDPDRIAVAGD 93
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 893-922 1.73e-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: 44.76  E-value: 1.73e-05
                         10        20        30
                 ....*....|....*....|....*....|
gi 12643975  893 HFNLRSCWCVDEAGQELDGTRTRAGEiPAC 922
Cdd:cd00191   38 HGSTGYCWCVDPDGEEIPGTRTRGGP-PNC 66
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 893-923 3.77e-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 and binding partners of heparin.


Pssm-ID: 214561  Cd Length: 46  Bit Score: 43.14  E-value: 3.77e-05
                            10        20        30
                    ....*....|....*....|....*....|.
gi 12643975     893 HFNLRSCWCVDEAGQELDGTRTRAGEiPACP 923
Cdd:smart00211   16 DGSSGQCWCVDATGREIPGTRTEGGD-PDCP 45
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 899-922 8.26e-05

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: 42.68  E-value: 8.26e-05
                           10        20
                   ....*....|....*....|....
gi 12643975    899 CWCVDEAGQELDGTRTRAGEiPAC 922
Cdd:pfam00086   44 CWCVDPEGQEIPGTRTRGGD-PDC 66
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 730-776 1.74e-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: 41.90  E-value: 1.74e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 12643975    730 CQLQAEQAflgvvgvlLSNSSMVPPISSVYIPQCSTSGQWMPVQCDG 776
Cdd:pfam00086    1 CERERARA--------LEQAASGRPASGLYIPNCDEDGFYKPVQCHG 39
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 164-249 2.18e-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: 2.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12643975  164 SCEIRSRRLLHGVGDKSP-----PQCDADGEFMPVQCkfvnttdmmifdliHNYNrfpdafvtfsafrnrfpevsGYCYC 238
Cdd:cd00191    1 PCERERASALESLAGPKLsglyvPQCDEDGNYEPVQC--------------HGST--------------------GYCWC 46

                         90
                 ....*....|.
gi 12643975  239 ADSQGRELAET 249
Cdd:cd00191   47 VDPDGEEIPGT 57
TNFRSF21 cd10583
Tumor necrosis factor receptor superfamily member 21 (TNFRSF21), also known as death receptor ...
 1450-1514 2.51e-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: 43.97  E-value: 2.51e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12643975 1450 TTSQDPLgCVkCPEGSFSQDGKCTP---CPAGTYQGQAGSSA----CIPCPRGRTTTITGAFSKTHCVTDCQ 1514
Cdd:cd10583   72 TALTDRE-CT-CPPGTFLSNDTCVPhsvCPVGWGVRKKGTETedvrCKPCPRGTFSDVPSSVLKCKTYTDCL 141
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 730-776 7.08e-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: 40.14  E-value: 7.08e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 12643975  730 CQLQAEQAFlgvvgvllsNSSMVPPISSVYIPQCSTSGQWMPVQCDG 776
Cdd:cd00191    2 CERERASAL---------ESLAGPKLSGLYVPQCDEDGNYEPVQCHG 39
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 1521-1550 8.06e-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: 37.28  E-value: 8.06e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 12643975   1521 QCDQNGQYQANQKDMDSGEVFCVDSEGQRL 1550
Cdd:pfam00086   25 NCDEDGFYKPVQCHGSTGYCWCVDPEGQEI 54
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1521-1551 8.44e-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: 37.06  E-value: 8.44e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 12643975 1521 QCDQNGQYQANQKDMDSGEVFCVDSEGQRLQ 1551
Cdd:cd00191   25 QCDEDGNYEPVQCHGSTGYCWCVDPDGEEIP 55
 
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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