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Conserved domains on  [gi|398650656|ref|NP_001257712|]
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thyroglobulin isoform 2 precursor [Rattus norvegicus]

Protein Classification

carboxylesterase/lipase family protein( domain architecture ID 10076381)

carboxylesterase/lipase family protein similar to carboxylesterase, which catalyzes the hydrolysis of a carboxylic ester to form an alcohol and a carboxylate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COesterase pfam00135
Carboxylesterase family;
2150-2671 2.42e-174

Carboxylesterase family;


:

Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 546.52  E-value: 2.42e-174
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656  2150 STPSVHIdSFGQLQGGSQVVKVGtawKQVYQFLGVPYAAPPLAENRFQAPE-VLNWTGSWDATKLRSSCWQPGTRTPTPP 2228
Cdd:pfam00135    1 DSPVVTT-SLGRVRGKRLKVDGG---KPVYAFLGIPYAEPPVGELRFQPPEpPEPWTGVRDATKFGPRCPQNGDLTSPGS 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656  2229 Q---ISEDCLYLNVFVPENLVSNA---SVLVFFHNTVEMEGSGGQlnIDGSILAAVGNLIVVTANYRLGVFGFLSSGSDE 2302
Cdd:pfam00135   77 SgleGSEDCLYLNVYTPKELKENKnklPVMVWIHGGGFMFGSGSL--YDGSYLAAEGDVIVVTINYRLGPLGFLSTGDDE 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656  2303 VAGNWGLLDQVAALTWVQTHIGAFGGDPQRVTLAADRGGADVASIHLLitRPTRLQLFRKALLMGGSALSPAAIISPDRa 2382
Cdd:pfam00135  155 APGNYGLLDQVLALRWVQENIASFGGDPNRVTLFGESAGAASVSLLLL--SPLSKGLFHRAILMSGSALSPWAIQSNAR- 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656  2383 qQQAAALAKEVGCPNSSVQEVVSCFRQKPANILNEAQTKLL-AVSGPFHYWGPVVDGQYLRELPSRRLKRPLPVKVDLLI 2461
Cdd:pfam00135  232 -QRAKELAKLVGCPTSDSAELVECLRSKPAEELLDAQLKLLvYGSVPFVPFGPVVDGDFLPEHPEELLKSGNFPKVPLLI 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656  2462 GGSQDDGLINRA------KAVKQFEESQGRTNSKTAFYQALqnslggEDSDARILAAAIWYYSLEHSTDDYASFSRALEN 2535
Cdd:pfam00135  311 GVTKDEGLLFAAyildnvDILKALEEKLLRSLLIDLLYLLL------VDLPEEISAALREEYLDWGDRDDPETSRRALVE 384

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656  2536 ATRDYFIICPIVNMASLWARRtRGNVFMYH---------VPESYG--HGSlellaDVQYAFGLPFYSAYQgyFSMEEQSL 2604
Cdd:pfam00135  385 LLTDYLFNCPVIRFADLHASR-GTPVYMYSfdyrgsslrYPKWVGvdHGD-----ELPYVFGTPFVGALL--FTEEDEKL 456

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398650656  2605 SLKVMQYFSNFIRSGNPNYPhefsqkaaEFATPWPDFVPgaggESYKELSAQLPNR--QGLKKADCSFW 2671
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 2.58e-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: 2.58e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398650656   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 ...
 957-1026 5.71e-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: 5.71e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656  957 FYQKLRASLGESNgtASLLWSGPYMPQCNTIGGWEPVQCHPGTGQCWCVDGWGELIPGSLMARssQMPQC 1026
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 4.96e-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: 4.96e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398650656   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 ...
 613-676 4.23e-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: 4.23e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398650656  613 KCEKQRAQMQNLAgAQPAGSSFFVPTCTSEGYFLPVQCFNS--ECYCVDAEGQVIPGTQSTIGEPK 676
Cdd:cd00191     1 PCERERASALESL-AGPKLSGLYVPQCDEDGNYEPVQCHGStgYCWCVDPDGEEIPGTRTRGGPPN 65
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 253-311 8.29e-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: 8.29e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398650656  253 KCEVEQFTATS------FGHPYIPSCHRDGHYQTVQCQME-RMCWCVDAQGIEIPGTRQQGQPLFC 311
Cdd:cd00191     1 PCERERASALEslagpkLSGLYVPQCDEDGNYEPVQCHGStGYCWCVDPDGEEIPGTRTRGGPPNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1102-1163 9.95e-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: 9.95e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398650656 1102 CDALKSRVLSRKVGLG----YTPVCEAlDGGFSPVQCDLAQGSCWCVLASGEEVPGTRVVGTQPAC 1163
Cdd:cd00191     2 CERERASALESLAGPKlsglYVPQCDE-DGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRGGPPNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 565-610 2.85e-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: 75.19  E-value: 2.85e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 398650656  565 GRFFVPSCTAEGSYEDIQCYA--GECWCVNSQGKEVEGSRVSGGHPRC 610
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 ...
 1416-1461 8.70e-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: 8.70e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 398650656  1416 GSFSQDG--KCTPCPAGTYQGQAGSSACIPCPRGRTTTITGAFSKTHC 1461
Cdd:pfam07699    1 GTYSNTGlePCIPCPRGTYQPEEGQLSCLACPLGTTTDSPGATSISDC 48
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1471-1518 3.02e-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: 3.02e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 398650656   1471 GLQCDQNGQYQANQKDMDSGEVFCVDSEGQRLQWlqTEAGLSESQCLM 1518
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSSGQCWCVDATGREIPG--TRTEGGDPDCPS 46
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 845-874 1.78e-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: 1.78e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 398650656  845 HFNLRSCWCVDEAGQELDGTRTRAGEiPAC 874
Cdd:cd00191    38 HGSTGYCWCVDPDGEEIPGTRTRGGP-PNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 164-254 9.01e-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: 42.84  E-value: 9.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656  164 SCEIRSRRLLHGVGDKSP-----PQCDADGEFMPVQCkfvnttdmmifdliHNYNrfpdafvtfsafrnrfpevsGYCYC 238
Cdd:cd00191     1 PCERERASALESLAGPKLsglyvPQCDEDGNYEPVQC--------------HGST--------------------GYCWC 46

                          90       100
                  ....*....|....*....|
gi 398650656  239 ADSQGRELAET----GPTKC 254
Cdd:cd00191    47 VDPDGEEIPGTrtrgGPPNC 66
TY super family cl00150
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 682-728 1.80e-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: 1.80e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 398650656   682 CQLQAEQAflgvvgvlLSNSSMVPPISSVYIPQCSTSGQWMPVQCDG 728
Cdd:pfam00086    1 CERERARA--------LEQAASGRPASGLYIPNCDEDGFYKPVQCHG 39
 
Name Accession Description Interval E-value
COesterase pfam00135
Carboxylesterase family;
2150-2671 2.42e-174

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 546.52  E-value: 2.42e-174
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656  2150 STPSVHIdSFGQLQGGSQVVKVGtawKQVYQFLGVPYAAPPLAENRFQAPE-VLNWTGSWDATKLRSSCWQPGTRTPTPP 2228
Cdd:pfam00135    1 DSPVVTT-SLGRVRGKRLKVDGG---KPVYAFLGIPYAEPPVGELRFQPPEpPEPWTGVRDATKFGPRCPQNGDLTSPGS 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656  2229 Q---ISEDCLYLNVFVPENLVSNA---SVLVFFHNTVEMEGSGGQlnIDGSILAAVGNLIVVTANYRLGVFGFLSSGSDE 2302
Cdd:pfam00135   77 SgleGSEDCLYLNVYTPKELKENKnklPVMVWIHGGGFMFGSGSL--YDGSYLAAEGDVIVVTINYRLGPLGFLSTGDDE 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656  2303 VAGNWGLLDQVAALTWVQTHIGAFGGDPQRVTLAADRGGADVASIHLLitRPTRLQLFRKALLMGGSALSPAAIISPDRa 2382
Cdd:pfam00135  155 APGNYGLLDQVLALRWVQENIASFGGDPNRVTLFGESAGAASVSLLLL--SPLSKGLFHRAILMSGSALSPWAIQSNAR- 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656  2383 qQQAAALAKEVGCPNSSVQEVVSCFRQKPANILNEAQTKLL-AVSGPFHYWGPVVDGQYLRELPSRRLKRPLPVKVDLLI 2461
Cdd:pfam00135  232 -QRAKELAKLVGCPTSDSAELVECLRSKPAEELLDAQLKLLvYGSVPFVPFGPVVDGDFLPEHPEELLKSGNFPKVPLLI 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656  2462 GGSQDDGLINRA------KAVKQFEESQGRTNSKTAFYQALqnslggEDSDARILAAAIWYYSLEHSTDDYASFSRALEN 2535
Cdd:pfam00135  311 GVTKDEGLLFAAyildnvDILKALEEKLLRSLLIDLLYLLL------VDLPEEISAALREEYLDWGDRDDPETSRRALVE 384

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656  2536 ATRDYFIICPIVNMASLWARRtRGNVFMYH---------VPESYG--HGSlellaDVQYAFGLPFYSAYQgyFSMEEQSL 2604
Cdd:pfam00135  385 LLTDYLFNCPVIRFADLHASR-GTPVYMYSfdyrgsslrYPKWVGvdHGD-----ELPYVFGTPFVGALL--FTEEDEKL 456

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398650656  2605 SLKVMQYFSNFIRSGNPNYPhefsqkaaEFATPWPDFVPgaggESYKELSAQLPNR--QGLKKADCSFW 2671
Cdd:pfam00135  457 SRKMMTYWTNFAKTGNPNGP--------EGLPKWPPYTD----ENGQYLSIDLEPRvkQGLKAERCAFW 513
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 2178-2655 6.60e-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: 317.35  E-value: 6.60e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656 2178 VYQFLGVPYAAPPLAENRFQAPEVLN-WTGSWDATKLRSSCWQP----GTRTPTPPQISEDCLYLNVFVPENLVSNAS-- 2250
Cdd:cd00312    17 VYSFLGIPYAEPPVGDLRFKEPQPYEpWSDVLDATSYPPSCMQWdqlgGGLWNAKLPGSEDCLYLNVYTPKNTKPGNSlp 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656 2251 VLVFFHNTVEMEGSGGQLNIDGsILAAVGNLIVVTANYRLGVFGFLSSGSDEVAGNWGLLDQVAALTWVQTHIGAFGGDP 2330
Cdd:cd00312    97 VMVWIHGGGFMFGSGSLYPGDG-LAREGDNVIVVSINYRLGVLGFLSTGDIELPGNYGLKDQRLALKWVQDNIAAFGGDP 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656 2331 QRVTLAADRGGAdvASIHLLITRPTRLQLFRKALLMGGSALSPAAIisPDRAQQQAAALAKEVGCPNSSVQEVVSCFRQK 2410
Cdd:cd00312   176 DSVTIFGESAGG--ASVSLLLLSPDSKGLFHRAISQSGSALSPWAI--QENARGRAKRLARLLGCNDTSSAELLDCLRSK 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656 2411 PANILNEAQTKLLAVSG-PFHYWGPVVDGQYLRELPSRRLKRPLPVKVDLLIGGSQDDGLINRAKAVKQFEESQGRTNsk 2489
Cdd:cd00312   252 SAEELLDATRKLLLFSYsPFLPFGPVVDGDFIPDDPEELIKEGKFAKVPLIIGVTKDEGGYFAAMLLNFDAKLIIETN-- 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656 2490 TAFYQALQNSLGGEDSD-ARILAAAiwYY-SLEHSTDDYASFSRALEnatrDYFIICPIVNMASLWARRTRGNVFMY--- 2564
Cdd:cd00312   330 DRWLELLPYLLFYADDAlADKVLEK--YPgDVDDSVESRKNLSDMLT----DLLFKCPARYFLAQHRKAGGSPVYAYvfd 403

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656 2565 HVPE-SYGHGSLELLA----DVQYAFGLPFYSayqGYFSMEEQSLSLKVMQYFSNFIRSGNPNYPHEFSQkaaefatpWP 2639
Cdd:cd00312   404 HRSSlSVGRWPPWLGTvhgdEIFFVFGNPLLK---EGLREEEEKLSRTMMKYWANFAKTGNPNTEGNLVV--------WP 472

                         490
                  ....*....|....*.
gi 398650656 2640 DFVpgAGGESYKELSA 2655
Cdd:cd00312   473 AYT--SESEKYLDINI 486
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
2150-2646 1.22e-94

Carboxylesterase type B [Lipid transport and metabolism];


Pssm-ID: 441873  Cd Length: 500  Bit Score: 316.83  E-value: 1.22e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656 2150 STPSVHIDSfGQLQGgsqVVKVGtawkqVYQFLGVPYAAPPLAENRFQAPE-VLNWTGSWDATKLRSSCWQPGTRT--PT 2226
Cdd:COG2272    11 AAPVVRTEA-GRVRG---VVEGG-----VRVFLGIPYAAPPVGELRWRAPQpVEPWTGVRDATEFGPACPQPPRPGdpGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656 2227 PPQISEDCLYLNVFVPENLVS-NASVLVFFH---NTVemeGSGGQLNIDGSILAAVGnLIVVTANYRLGVFGF-----LS 2297
Cdd:COG2272    82 PAPGSEDCLYLNVWTPALAAGaKLPVMVWIHgggFVS---GSGSEPLYDGAALARRG-VVVVTINYRLGALGFlalpaLS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656 2298 SGSDEVAGNWGLLDQVAALTWVQTHIGAFGGDPQRVTLAADRGGAdvASIHLLITRPTRLQLFRKALLMGGSALSPAaii 2377
Cdd:COG2272   158 GESYGASGNYGLLDQIAALRWVRDNIAAFGGDPDNVTIFGESAGA--ASVAALLASPLAKGLFHRAIAQSGAGLSVL--- 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656 2378 SPDRAQQQAAALAKEVGCPNSSVQevvsCFRQKPANILNEAQTKLLAVSGPFHYWGPVVDGQYLRELPSRRLKRPLPVKV 2457
Cdd:COG2272   233 TLAEAEAVGAAFAAALGVAPATLA----ALRALPAEELLAAQAALAAEGPGGLPFGPVVDGDVLPEDPLEAFAAGRAADV 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656 2458 DLLIGGSQDDGLInrakavkqFEESQGRTNSKT-AFYQALQNSLGGEDSDaRILAAaiwyyslehstddY--ASFSRALE 2534
Cdd:COG2272   309 PLLIGTNRDEGRL--------FAALLGDLGPLTaADYRAALRRRFGDDAD-EVLAA-------------YpaASPAEALA 366

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656 2535 NATRDYFIICPIVNMASLWArRTRGNVFMY---HVPESYG-------HGslellADVQYAFGLPFYSAYQGyFSMEEQSL 2604
Cdd:COG2272   367 ALATDRVFRCPARRLAEAHA-AAGAPVYLYrfdWRSPPLRgfglgafHG-----AELPFVFGNLDAPALTG-LTPADRAL 439

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 398650656 2605 SLKVMQYFSNFIRSGNPNyphefsqkaAEFATPWPDFVPGAG 2646
Cdd:COG2272   440 SDQMQAYWVNFARTGDPN---------GPGLPEWPAYDPEDR 472
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 96-161 2.58e-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: 2.58e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398650656   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 2.60e-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: 86.59  E-value: 2.60e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398650656    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 ...
 957-1026 5.71e-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: 5.71e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656  957 FYQKLRASLGESNgtASLLWSGPYMPQCNTIGGWEPVQCHPGTGQCWCVDGWGELIPGSLMARssQMPQC 1026
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 4.96e-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: 4.96e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398650656   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 ...
 613-676 4.23e-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: 4.23e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398650656  613 KCEKQRAQMQNLAgAQPAGSSFFVPTCTSEGYFLPVQCFNS--ECYCVDAEGQVIPGTQSTIGEPK 676
Cdd:cd00191     1 PCERERASALESL-AGPKLSGLYVPQCDEDGNYEPVQCHGStgYCWCVDPDGEEIPGTRTRGGPPN 65
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 614-676 7.78e-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: 7.78e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398650656   614 CEKQRAQMQNLAGAQPAGSSFFVPTCTSEGYFLPVQCFNS--ECYCVDAEGQVIPGTQSTIGEPK 676
Cdd:pfam00086    1 CERERARALEQAASGRPASGLYIPNCDEDGFYKPVQCHGStgYCWCVDPEGQEIPGTRTRGGDPD 65
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 253-311 8.29e-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: 8.29e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398650656  253 KCEVEQFTATS------FGHPYIPSCHRDGHYQTVQCQME-RMCWCVDAQGIEIPGTRQQGQPLFC 311
Cdd:cd00191     1 PCERERASALEslagpkLSGLYVPQCDEDGNYEPVQCHGStGYCWCVDPDGEEIPGTRTRGGPPNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1102-1163 9.95e-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: 9.95e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398650656 1102 CDALKSRVLSRKVGLG----YTPVCEAlDGGFSPVQCDLAQGSCWCVLASGEEVPGTRVVGTQPAC 1163
Cdd:cd00191     2 CERERASALESLAGPKlsglYVPQCDE-DGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRGGPPNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 565-610 2.85e-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: 75.19  E-value: 2.85e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 398650656  565 GRFFVPSCTAEGSYEDIQCYA--GECWCVNSQGKEVEGSRVSGGHPRC 610
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 4.19e-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: 74.65  E-value: 4.19e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398650656    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 ...
 1416-1461 8.70e-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: 8.70e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 398650656  1416 GSFSQDG--KCTPCPAGTYQGQAGSSACIPCPRGRTTTITGAFSKTHC 1461
Cdd:pfam07699    1 GTYSNTGlePCIPCPRGTYQPEEGQLSCLACPLGTTTDSPGATSISDC 48
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 118-163 9.50e-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: 70.10  E-value: 9.50e-15
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 398650656    118 LPQCQDSGNYAPVQCDLQQVQCWCVDTEGMEVYGTRQQGRPTRCPR 163
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSSGQCWCVDATGREIPGTRTEGGDPDCPS 46
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 959-1026 9.78e-15

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


Pssm-ID: 459665  Cd Length: 66  Bit Score: 70.79  E-value: 9.78e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398650656   959 QKLRAS-LGESNGTASLlwSGPYMPQCNTIGGWEPVQCHPGTGQCWCVDGWGELIPGSlmARSSQMPQC 1026
Cdd:pfam00086    2 ERERARaLEQAASGRPA--SGLYIPNCDEDGFYKPVQCHGSTGYCWCVDPEGQEIPGT--RTRGGDPDC 66
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 50-95 8.05e-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: 8.05e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 398650656     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 ...
 566-610 2.38e-13

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


Pssm-ID: 459665  Cd Length: 66  Bit Score: 66.94  E-value: 2.38e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 398650656   566 RFFVPSCTAEGSYEDIQCY--AGECWCVNSQGKEVEGSRVSGGHPRC 610
Cdd:pfam00086   20 GLYIPNCDEDGFYKPVQCHgsTGYCWCVDPEGQEIPGTRTRGGDPDC 66
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 254-311 4.15e-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: 4.15e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398650656   254 CEVEQFTA---TSFGHP----YIPSCHRDGHYQTVQCQMER-MCWCVDAQGIEIPGTRQQGQPLFC 311
Cdd:pfam00086    1 CERERARAleqAASGRPasglYIPNCDEDGFYKPVQCHGSTgYCWCVDPEGQEIPGTRTRGGDPDC 66
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1120-1165 1.16e-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: 1.16e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 398650656   1120 PVCEAlDGGFSPVQCDLAQGSCWCVLASGEEVPGTRVVGTQPACES 1165
Cdd:smart00211    2 PQCDE-DGNYEPVQCDGSSGQCWCVDATGREIPGTRTEGGDPDCPS 46
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 269-311 1.45e-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: 1.45e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 398650656    269 IPSCHRDGHYQTVQCQMER-MCWCVDAQGIEIPGTRQQGQPLFC 311
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSSgQCWCVDATGREIPGTRTEGGDPDC 44
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 569-612 3.36e-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: 3.36e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 398650656    569 VPSCTAEGSYEDIQCYA--GECWCVNSQGKEVEGSRVSGGHPRCPT 612
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGssGQCWCVDATGREIPGTRTEGGDPDCPS 46
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 1102-1163 8.99e-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: 62.32  E-value: 8.99e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398650656  1102 CDALKSRVLSRKVGLG-----YTPVCEAlDGGFSPVQCDLAQGSCWCVLASGEEVPGTRVVGTQPAC 1163
Cdd:pfam00086    1 CERERARALEQAASGRpasglYIPNCDE-DGFYKPVQCHGSTGYCWCVDPEGQEIPGTRTRGGDPDC 66
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 636-680 2.59e-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: 2.59e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 398650656    636 VPTCTSEGYFLPVQCFNS--ECYCVDAEGQVIPGTQSTIGEPKlCPS 680
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSsgQCWCVDATGREIPGTRTEGGDPD-CPS 46
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 981-1028 3.15e-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: 3.15e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 398650656    981 MPQCNTIGGWEPVQCHPGTGQCWCVDGWGELIPGSLMARSSqmPQCPT 1028
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSSGQCWCVDATGREIPGTRTEGGD--PDCPS 46
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1471-1518 3.02e-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: 3.02e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 398650656   1471 GLQCDQNGQYQANQKDMDSGEVFCVDSEGQRLQWlqTEAGLSESQCLM 1518
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSSGQCWCVDATGREIPG--TRTEGGDPDCPS 46
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 845-874 1.78e-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: 1.78e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 398650656  845 HFNLRSCWCVDEAGQELDGTRTRAGEiPAC 874
Cdd:cd00191    38 HGSTGYCWCVDPDGEEIPGTRTRGGP-PNC 66
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 845-875 3.93e-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: 3.93e-05
                            10        20        30
                    ....*....|....*....|....*....|.
gi 398650656    845 HFNLRSCWCVDEAGQELDGTRTRAGEiPACP 875
Cdd:smart00211   16 DGSSGQCWCVDATGREIPGTRTEGGD-PDCP 45
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 851-874 8.61e-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: 8.61e-05
                           10        20
                   ....*....|....*....|....
gi 398650656   851 CWCVDEAGQELDGTRTRAGEiPAC 874
Cdd:pfam00086   44 CWCVDPEGQEIPGTRTRGGD-PDC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 164-254 9.01e-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: 42.84  E-value: 9.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656  164 SCEIRSRRLLHGVGDKSP-----PQCDADGEFMPVQCkfvnttdmmifdliHNYNrfpdafvtfsafrnrfpevsGYCYC 238
Cdd:cd00191     1 PCERERASALESLAGPKLsglyvPQCDEDGNYEPVQC--------------HGST--------------------GYCWC 46

                          90       100
                  ....*....|....*....|
gi 398650656  239 ADSQGRELAET----GPTKC 254
Cdd:cd00191    47 VDPDGEEIPGTrtrgGPPNC 66
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 682-728 1.80e-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: 1.80e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 398650656   682 CQLQAEQAflgvvgvlLSNSSMVPPISSVYIPQCSTSGQWMPVQCDG 728
Cdd:pfam00086    1 CERERARA--------LEQAASGRPASGLYIPNCDEDGFYKPVQCHG 39
TNFRSF21 cd10583
Tumor necrosis factor receptor superfamily member 21 (TNFRSF21), also known as death receptor ...
 1402-1466 2.68e-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: 2.68e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398650656 1402 TTSQDPLgCVkCPEGSFSQDGKCTP---CPAGTYQGQAGSSA----CIPCPRGRTTTITGAFSKTHCVTDCQ 1466
Cdd:cd10583    72 TALTDRE-CT-CPPGTFLSNDTCVPhsvCPVGWGVRKKGTETedvrCKPCPRGTFSDVPSSVLKCKTYTDCL 141
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 682-728 7.45e-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: 7.45e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 398650656  682 CQLQAEQAFlgvvgvllsNSSMVPPISSVYIPQCSTSGQWMPVQCDG 728
Cdd:cd00191     2 CERERASAL---------ESLAGPKLSGLYVPQCDEDGNYEPVQCHG 39
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 1473-1502 8.32e-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: 8.32e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 398650656  1473 QCDQNGQYQANQKDMDSGEVFCVDSEGQRL 1502
Cdd:pfam00086   25 NCDEDGFYKPVQCHGSTGYCWCVDPEGQEI 54
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1473-1503 8.37e-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: 8.37e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 398650656 1473 QCDQNGQYQANQKDMDSGEVFCVDSEGQRLQ 1503
Cdd:cd00191    25 QCDEDGNYEPVQCHGSTGYCWCVDPDGEEIP 55
 
Name Accession Description Interval E-value
COesterase pfam00135
Carboxylesterase family;
2150-2671 2.42e-174

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 546.52  E-value: 2.42e-174
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656  2150 STPSVHIdSFGQLQGGSQVVKVGtawKQVYQFLGVPYAAPPLAENRFQAPE-VLNWTGSWDATKLRSSCWQPGTRTPTPP 2228
Cdd:pfam00135    1 DSPVVTT-SLGRVRGKRLKVDGG---KPVYAFLGIPYAEPPVGELRFQPPEpPEPWTGVRDATKFGPRCPQNGDLTSPGS 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656  2229 Q---ISEDCLYLNVFVPENLVSNA---SVLVFFHNTVEMEGSGGQlnIDGSILAAVGNLIVVTANYRLGVFGFLSSGSDE 2302
Cdd:pfam00135   77 SgleGSEDCLYLNVYTPKELKENKnklPVMVWIHGGGFMFGSGSL--YDGSYLAAEGDVIVVTINYRLGPLGFLSTGDDE 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656  2303 VAGNWGLLDQVAALTWVQTHIGAFGGDPQRVTLAADRGGADVASIHLLitRPTRLQLFRKALLMGGSALSPAAIISPDRa 2382
Cdd:pfam00135  155 APGNYGLLDQVLALRWVQENIASFGGDPNRVTLFGESAGAASVSLLLL--SPLSKGLFHRAILMSGSALSPWAIQSNAR- 231

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656  2383 qQQAAALAKEVGCPNSSVQEVVSCFRQKPANILNEAQTKLL-AVSGPFHYWGPVVDGQYLRELPSRRLKRPLPVKVDLLI 2461
Cdd:pfam00135  232 -QRAKELAKLVGCPTSDSAELVECLRSKPAEELLDAQLKLLvYGSVPFVPFGPVVDGDFLPEHPEELLKSGNFPKVPLLI 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656  2462 GGSQDDGLINRA------KAVKQFEESQGRTNSKTAFYQALqnslggEDSDARILAAAIWYYSLEHSTDDYASFSRALEN 2535
Cdd:pfam00135  311 GVTKDEGLLFAAyildnvDILKALEEKLLRSLLIDLLYLLL------VDLPEEISAALREEYLDWGDRDDPETSRRALVE 384

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656  2536 ATRDYFIICPIVNMASLWARRtRGNVFMYH---------VPESYG--HGSlellaDVQYAFGLPFYSAYQgyFSMEEQSL 2604
Cdd:pfam00135  385 LLTDYLFNCPVIRFADLHASR-GTPVYMYSfdyrgsslrYPKWVGvdHGD-----ELPYVFGTPFVGALL--FTEEDEKL 456

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398650656  2605 SLKVMQYFSNFIRSGNPNYPhefsqkaaEFATPWPDFVPgaggESYKELSAQLPNR--QGLKKADCSFW 2671
Cdd:pfam00135  457 SRKMMTYWTNFAKTGNPNGP--------EGLPKWPPYTD----ENGQYLSIDLEPRvkQGLKAERCAFW 513
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 2178-2655 6.60e-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: 317.35  E-value: 6.60e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656 2178 VYQFLGVPYAAPPLAENRFQAPEVLN-WTGSWDATKLRSSCWQP----GTRTPTPPQISEDCLYLNVFVPENLVSNAS-- 2250
Cdd:cd00312    17 VYSFLGIPYAEPPVGDLRFKEPQPYEpWSDVLDATSYPPSCMQWdqlgGGLWNAKLPGSEDCLYLNVYTPKNTKPGNSlp 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656 2251 VLVFFHNTVEMEGSGGQLNIDGsILAAVGNLIVVTANYRLGVFGFLSSGSDEVAGNWGLLDQVAALTWVQTHIGAFGGDP 2330
Cdd:cd00312    97 VMVWIHGGGFMFGSGSLYPGDG-LAREGDNVIVVSINYRLGVLGFLSTGDIELPGNYGLKDQRLALKWVQDNIAAFGGDP 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656 2331 QRVTLAADRGGAdvASIHLLITRPTRLQLFRKALLMGGSALSPAAIisPDRAQQQAAALAKEVGCPNSSVQEVVSCFRQK 2410
Cdd:cd00312   176 DSVTIFGESAGG--ASVSLLLLSPDSKGLFHRAISQSGSALSPWAI--QENARGRAKRLARLLGCNDTSSAELLDCLRSK 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656 2411 PANILNEAQTKLLAVSG-PFHYWGPVVDGQYLRELPSRRLKRPLPVKVDLLIGGSQDDGLINRAKAVKQFEESQGRTNsk 2489
Cdd:cd00312   252 SAEELLDATRKLLLFSYsPFLPFGPVVDGDFIPDDPEELIKEGKFAKVPLIIGVTKDEGGYFAAMLLNFDAKLIIETN-- 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656 2490 TAFYQALQNSLGGEDSD-ARILAAAiwYY-SLEHSTDDYASFSRALEnatrDYFIICPIVNMASLWARRTRGNVFMY--- 2564
Cdd:cd00312   330 DRWLELLPYLLFYADDAlADKVLEK--YPgDVDDSVESRKNLSDMLT----DLLFKCPARYFLAQHRKAGGSPVYAYvfd 403

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656 2565 HVPE-SYGHGSLELLA----DVQYAFGLPFYSayqGYFSMEEQSLSLKVMQYFSNFIRSGNPNYPHEFSQkaaefatpWP 2639
Cdd:cd00312   404 HRSSlSVGRWPPWLGTvhgdEIFFVFGNPLLK---EGLREEEEKLSRTMMKYWANFAKTGNPNTEGNLVV--------WP 472

                         490
                  ....*....|....*.
gi 398650656 2640 DFVpgAGGESYKELSA 2655
Cdd:cd00312   473 AYT--SESEKYLDINI 486
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
2150-2646 1.22e-94

Carboxylesterase type B [Lipid transport and metabolism];


Pssm-ID: 441873  Cd Length: 500  Bit Score: 316.83  E-value: 1.22e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656 2150 STPSVHIDSfGQLQGgsqVVKVGtawkqVYQFLGVPYAAPPLAENRFQAPE-VLNWTGSWDATKLRSSCWQPGTRT--PT 2226
Cdd:COG2272    11 AAPVVRTEA-GRVRG---VVEGG-----VRVFLGIPYAAPPVGELRWRAPQpVEPWTGVRDATEFGPACPQPPRPGdpGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656 2227 PPQISEDCLYLNVFVPENLVS-NASVLVFFH---NTVemeGSGGQLNIDGSILAAVGnLIVVTANYRLGVFGF-----LS 2297
Cdd:COG2272    82 PAPGSEDCLYLNVWTPALAAGaKLPVMVWIHgggFVS---GSGSEPLYDGAALARRG-VVVVTINYRLGALGFlalpaLS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656 2298 SGSDEVAGNWGLLDQVAALTWVQTHIGAFGGDPQRVTLAADRGGAdvASIHLLITRPTRLQLFRKALLMGGSALSPAaii 2377
Cdd:COG2272   158 GESYGASGNYGLLDQIAALRWVRDNIAAFGGDPDNVTIFGESAGA--ASVAALLASPLAKGLFHRAIAQSGAGLSVL--- 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656 2378 SPDRAQQQAAALAKEVGCPNSSVQevvsCFRQKPANILNEAQTKLLAVSGPFHYWGPVVDGQYLRELPSRRLKRPLPVKV 2457
Cdd:COG2272   233 TLAEAEAVGAAFAAALGVAPATLA----ALRALPAEELLAAQAALAAEGPGGLPFGPVVDGDVLPEDPLEAFAAGRAADV 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656 2458 DLLIGGSQDDGLInrakavkqFEESQGRTNSKT-AFYQALQNSLGGEDSDaRILAAaiwyyslehstddY--ASFSRALE 2534
Cdd:COG2272   309 PLLIGTNRDEGRL--------FAALLGDLGPLTaADYRAALRRRFGDDAD-EVLAA-------------YpaASPAEALA 366

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656 2535 NATRDYFIICPIVNMASLWArRTRGNVFMY---HVPESYG-------HGslellADVQYAFGLPFYSAYQGyFSMEEQSL 2604
Cdd:COG2272   367 ALATDRVFRCPARRLAEAHA-AAGAPVYLYrfdWRSPPLRgfglgafHG-----AELPFVFGNLDAPALTG-LTPADRAL 439

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 398650656 2605 SLKVMQYFSNFIRSGNPNyphefsqkaAEFATPWPDFVPGAG 2646
Cdd:COG2272   440 SDQMQAYWVNFARTGDPN---------GPGLPEWPAYDPEDR 472
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 96-161 2.58e-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: 2.58e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398650656   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 2.60e-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: 86.59  E-value: 2.60e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398650656    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 ...
 957-1026 5.71e-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: 5.71e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656  957 FYQKLRASLGESNgtASLLWSGPYMPQCNTIGGWEPVQCHPGTGQCWCVDGWGELIPGSLMARssQMPQC 1026
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 4.96e-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: 4.96e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398650656   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 ...
 613-676 4.23e-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: 4.23e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398650656  613 KCEKQRAQMQNLAgAQPAGSSFFVPTCTSEGYFLPVQCFNS--ECYCVDAEGQVIPGTQSTIGEPK 676
Cdd:cd00191     1 PCERERASALESL-AGPKLSGLYVPQCDEDGNYEPVQCHGStgYCWCVDPDGEEIPGTRTRGGPPN 65
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 614-676 7.78e-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: 7.78e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398650656   614 CEKQRAQMQNLAGAQPAGSSFFVPTCTSEGYFLPVQCFNS--ECYCVDAEGQVIPGTQSTIGEPK 676
Cdd:pfam00086    1 CERERARALEQAASGRPASGLYIPNCDEDGFYKPVQCHGStgYCWCVDPEGQEIPGTRTRGGDPD 65
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 253-311 8.29e-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: 8.29e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398650656  253 KCEVEQFTATS------FGHPYIPSCHRDGHYQTVQCQME-RMCWCVDAQGIEIPGTRQQGQPLFC 311
Cdd:cd00191     1 PCERERASALEslagpkLSGLYVPQCDEDGNYEPVQCHGStGYCWCVDPDGEEIPGTRTRGGPPNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1102-1163 9.95e-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: 9.95e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398650656 1102 CDALKSRVLSRKVGLG----YTPVCEAlDGGFSPVQCDLAQGSCWCVLASGEEVPGTRVVGTQPAC 1163
Cdd:cd00191     2 CERERASALESLAGPKlsglYVPQCDE-DGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRGGPPNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 565-610 2.85e-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: 75.19  E-value: 2.85e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 398650656  565 GRFFVPSCTAEGSYEDIQCYA--GECWCVNSQGKEVEGSRVSGGHPRC 610
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 4.19e-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: 74.65  E-value: 4.19e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398650656    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 ...
 1416-1461 8.70e-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: 8.70e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 398650656  1416 GSFSQDG--KCTPCPAGTYQGQAGSSACIPCPRGRTTTITGAFSKTHC 1461
Cdd:pfam07699    1 GTYSNTGlePCIPCPRGTYQPEEGQLSCLACPLGTTTDSPGATSISDC 48
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 118-163 9.50e-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: 70.10  E-value: 9.50e-15
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 398650656    118 LPQCQDSGNYAPVQCDLQQVQCWCVDTEGMEVYGTRQQGRPTRCPR 163
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSSGQCWCVDATGREIPGTRTEGGDPDCPS 46
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 959-1026 9.78e-15

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


Pssm-ID: 459665  Cd Length: 66  Bit Score: 70.79  E-value: 9.78e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398650656   959 QKLRAS-LGESNGTASLlwSGPYMPQCNTIGGWEPVQCHPGTGQCWCVDGWGELIPGSlmARSSQMPQC 1026
Cdd:pfam00086    2 ERERARaLEQAASGRPA--SGLYIPNCDEDGFYKPVQCHGSTGYCWCVDPEGQEIPGT--RTRGGDPDC 66
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 50-95 8.05e-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: 8.05e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 398650656     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 ...
 566-610 2.38e-13

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


Pssm-ID: 459665  Cd Length: 66  Bit Score: 66.94  E-value: 2.38e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 398650656   566 RFFVPSCTAEGSYEDIQCY--AGECWCVNSQGKEVEGSRVSGGHPRC 610
Cdd:pfam00086   20 GLYIPNCDEDGFYKPVQCHgsTGYCWCVDPEGQEIPGTRTRGGDPDC 66
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 254-311 4.15e-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: 4.15e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398650656   254 CEVEQFTA---TSFGHP----YIPSCHRDGHYQTVQCQMER-MCWCVDAQGIEIPGTRQQGQPLFC 311
Cdd:pfam00086    1 CERERARAleqAASGRPasglYIPNCDEDGFYKPVQCHGSTgYCWCVDPEGQEIPGTRTRGGDPDC 66
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1120-1165 1.16e-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: 1.16e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 398650656   1120 PVCEAlDGGFSPVQCDLAQGSCWCVLASGEEVPGTRVVGTQPACES 1165
Cdd:smart00211    2 PQCDE-DGNYEPVQCDGSSGQCWCVDATGREIPGTRTEGGDPDCPS 46
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 269-311 1.45e-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: 1.45e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 398650656    269 IPSCHRDGHYQTVQCQMER-MCWCVDAQGIEIPGTRQQGQPLFC 311
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSSgQCWCVDATGREIPGTRTEGGDPDC 44
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 569-612 3.36e-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: 3.36e-12
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 398650656    569 VPSCTAEGSYEDIQCYA--GECWCVNSQGKEVEGSRVSGGHPRCPT 612
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGssGQCWCVDATGREIPGTRTEGGDPDCPS 46
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 1102-1163 8.99e-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: 62.32  E-value: 8.99e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398650656  1102 CDALKSRVLSRKVGLG-----YTPVCEAlDGGFSPVQCDLAQGSCWCVLASGEEVPGTRVVGTQPAC 1163
Cdd:pfam00086    1 CERERARALEQAASGRpasglYIPNCDE-DGFYKPVQCHGSTGYCWCVDPEGQEIPGTRTRGGDPDC 66
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 636-680 2.59e-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: 2.59e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 398650656    636 VPTCTSEGYFLPVQCFNS--ECYCVDAEGQVIPGTQSTIGEPKlCPS 680
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSsgQCWCVDATGREIPGTRTEGGDPD-CPS 46
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 981-1028 3.15e-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: 3.15e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 398650656    981 MPQCNTIGGWEPVQCHPGTGQCWCVDGWGELIPGSLMARSSqmPQCPT 1028
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSSGQCWCVDATGREIPGTRTEGGD--PDCPS 46
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1471-1518 3.02e-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: 3.02e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 398650656   1471 GLQCDQNGQYQANQKDMDSGEVFCVDSEGQRLQWlqTEAGLSESQCLM 1518
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSSGQCWCVDATGREIPG--TRTEGGDPDCPS 46
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
2239-2338 1.66e-06

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 51.41  E-value: 1.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656 2239 VFVPENLVSNASVLVFFHntvemeGSG---GQLNIDGSI---LAAVGNLIVVTANYRLgvfgflssgSDEVAGNWGLLDQ 2312
Cdd:COG0657     3 VYRPAGAKGPLPVVVYFH------GGGwvsGSKDTHDPLarrLAARAGAAVVSVDYRL---------APEHPFPAALEDA 67

                          90       100
                  ....*....|....*....|....*.
gi 398650656 2313 VAALTWVQTHIGAFGGDPQRVTLAAD 2338
Cdd:COG0657    68 YAALRWLRANAAELGIDPDRIAVAGD 93
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 845-874 1.78e-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: 1.78e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 398650656  845 HFNLRSCWCVDEAGQELDGTRTRAGEiPAC 874
Cdd:cd00191    38 HGSTGYCWCVDPDGEEIPGTRTRGGP-PNC 66
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 845-875 3.93e-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: 3.93e-05
                            10        20        30
                    ....*....|....*....|....*....|.
gi 398650656    845 HFNLRSCWCVDEAGQELDGTRTRAGEiPACP 875
Cdd:smart00211   16 DGSSGQCWCVDATGREIPGTRTEGGD-PDCP 45
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 851-874 8.61e-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: 8.61e-05
                           10        20
                   ....*....|....*....|....
gi 398650656   851 CWCVDEAGQELDGTRTRAGEiPAC 874
Cdd:pfam00086   44 CWCVDPEGQEIPGTRTRGGD-PDC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 164-254 9.01e-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: 42.84  E-value: 9.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398650656  164 SCEIRSRRLLHGVGDKSP-----PQCDADGEFMPVQCkfvnttdmmifdliHNYNrfpdafvtfsafrnrfpevsGYCYC 238
Cdd:cd00191     1 PCERERASALESLAGPKLsglyvPQCDEDGNYEPVQC--------------HGST--------------------GYCWC 46

                          90       100
                  ....*....|....*....|
gi 398650656  239 ADSQGRELAET----GPTKC 254
Cdd:cd00191    47 VDPDGEEIPGTrtrgGPPNC 66
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 682-728 1.80e-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: 1.80e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 398650656   682 CQLQAEQAflgvvgvlLSNSSMVPPISSVYIPQCSTSGQWMPVQCDG 728
Cdd:pfam00086    1 CERERARA--------LEQAASGRPASGLYIPNCDEDGFYKPVQCHG 39
TNFRSF21 cd10583
Tumor necrosis factor receptor superfamily member 21 (TNFRSF21), also known as death receptor ...
 1402-1466 2.68e-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: 2.68e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398650656 1402 TTSQDPLgCVkCPEGSFSQDGKCTP---CPAGTYQGQAGSSA----CIPCPRGRTTTITGAFSKTHCVTDCQ 1466
Cdd:cd10583    72 TALTDRE-CT-CPPGTFLSNDTCVPhsvCPVGWGVRKKGTETedvrCKPCPRGTFSDVPSSVLKCKTYTDCL 141
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 682-728 7.45e-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: 7.45e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 398650656  682 CQLQAEQAFlgvvgvllsNSSMVPPISSVYIPQCSTSGQWMPVQCDG 728
Cdd:cd00191     2 CERERASAL---------ESLAGPKLSGLYVPQCDEDGNYEPVQCHG 39
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 1473-1502 8.32e-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: 8.32e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 398650656  1473 QCDQNGQYQANQKDMDSGEVFCVDSEGQRL 1502
Cdd:pfam00086   25 NCDEDGFYKPVQCHGSTGYCWCVDPEGQEI 54
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1473-1503 8.37e-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: 8.37e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 398650656 1473 QCDQNGQYQANQKDMDSGEVFCVDSEGQRLQ 1503
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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