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Conserved domains on  [gi|1049017891|ref|NP_001316794|]
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thyroglobulin precursor [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COesterase pfam00135
Carboxylesterase family;
2172-2678 1.80e-136

Carboxylesterase family;


:

Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 438.28  E-value: 1.80e-136
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 2172 GTLLGEseVKPITGSDSkrVTYFLGVPYARPPIGDLRFSPPQPAD-WTGTWNATFFRSSCLQPGDLTDSSS-----SEDC 2245
Cdd:pfam00135   10 GRVRGK--RLKVDGGKP--VYAFLGIPYAEPPVGELRFQPPEPPEpWTGVRDATKFGPRCPQNGDLTSPGSsglegSEDC 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 2246 LYLNVFV---ASSVAKNAPVLVFFHN------SGSdLLDGSYLAAVGNIIVVTASFRMAAFGFLSAGSSALPGNYGLQDQ 2316
Cdd:pfam00135   86 LYLNVYTpkeLKENKNKLPVMVWIHGggfmfgSGS-LYDGSYLAAEGDVIVVTINYRLGPLGFLSTGDDEAPGNYGLLDQ 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 2317 AAALGWVQKNIALFGGDPTKVTVGAERNGADIASLHLTSPSASSLFSRALLMGGSVFSPAVVMSSSKAQAQTssLARELD 2396
Cdd:pfam00135  165 VLALRWVQENIASFGGDPNRVTLFGESAGAASVSLLLLSPLSKGLFHRAILMSGSALSPWAIQSNARQRAKE--LAKLVG 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 2397 CQAADPSQLLDCLRSKPAHSINAAQTKLL-AVSGPLQAWSPVVDGNVVREMPSVALQSGRFHKAEILLGSSFEDGLISRA 2475
Cdd:pfam00135  243 CPTSDSAELVECLRSKPAEELLDAQLKLLvYGSVPFVPFGPVVDGDFLPEHPEELLKSGNFPKVPLLIGVTKDEGLLFAA 322

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 2476 KN------IKNFEQLQGRADSKTAFYAALsnslggDDANAFVKEAATWFYSLQHSptPSGYNVFSRALENATRDLFIICP 2549
Cdd:pfam00135  323 YIldnvdiLKALEEKLLRSLLIDLLYLLL------VDLPEEISAALREEYLDWGD--RDDPETSRRALVELLTDYLFNCP 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 2550 TVDMAEFWAANTqTGVYMYHlpenAAYNSVDLSVP--------MDVQYLFGVPLaaEQRDLFSYKEKTFTLQIMNYMANF 2621
Cdd:pfam00135  395 VIRFADLHASRG-TPVYMYS----FDYRGSSLRYPkwvgvdhgDELPYVFGTPF--VGALLFTEEDEKLSRKMMTYWTNF 467

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1049017891 2622 IKSGNPNLPLaasrtsfgkFLPPWPQFMPHvgGRAYKELSSTLVNRKNLQRSQCSFW 2678
Cdd:pfam00135  468 AKTGNPNGPE---------GLPKWPPYTDE--NGQYLSIDLEPRVKQGLKAERCAFW 513
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 301-358 2.43e-17

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


:

Pssm-ID: 238114  Cd Length: 66  Bit Score: 78.27  E-value: 2.43e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1049017891  301 PCESERAAASQ------AGNSFVPSCTDNGAYVPTQCQ-SGGQCWCVDTYGKEIFGTR-QNGVPKC 358
Cdd:cd00191      1 PCERERASALEslagpkLSGLYVPQCDEDGNYEPVQCHgSTGYCWCVDPDGEEIPGTRtRGGPPNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 594-639 2.82e-17

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


:

Pssm-ID: 238114  Cd Length: 66  Bit Score: 78.27  E-value: 2.82e-17
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1049017891  594 SAPYLPQCTEDGLYQDVQCQGS--ECWCVDSRGLEVPGSRTTGSRPRC 639
Cdd:cd00191     19 SGLYVPQCDEDGNYEPVQCHGStgYCWCVDPDGEEIPGTRTRGGPPNC 66
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 102-161 1.56e-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: 75.80  E-value: 1.56e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1049017891  102 CQLQRQRALQTEDATL------VPVCLDSGEYQQVQCDASRSQCWCVDLEGMEIYGTRQNGKPSKC 161
Cdd:pfam00086    1 CERERARALEQAASGRpasglyIPNCDEDGFYKPVQCHGSTGYCWCVDPEGQEIPGTRTRGGDPDC 66
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 40-98 1.16e-14

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


:

Pssm-ID: 459665  Cd Length: 66  Bit Score: 70.79  E-value: 1.16e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1049017891   40 CEQLR-------SVSAEQERQHVPQCFEDGRFRHVQCNRGGGECWCVNAEGFEIPGSRQNGSSVYC 98
Cdd:pfam00086    1 CERERaraleqaASGRPASGLYIPNCDEDGFYKPVQCHGSTGYCWCVDPEGQEIPGTRTRGGDPDC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 990-1047 2.24e-13

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: 67.10  E-value: 2.24e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1049017891  990 RLMASDRDRQSLMLGYQPYIPQCDAYGQWLPNQCYQSTGLCWCVDEEGQYIADSLTSR 1047
Cdd:cd00191      4 RERASALESLAGPKLSGLYVPQCDEDGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRG 61
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 643-705 1.03e-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: 65.02  E-value: 1.03e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1049017891  643 CEKERQMAIAVKASSSAGSEVFIPKCETDGAYVARQCLGKS--CFCVDRSGTKL-GIQSSGSSLQC 705
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 ...
 1425-1470 1.03e-11

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: 61.60  E-value: 1.03e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1049017891 1425 GSFFSGGV--CTPCPRDTFQEDEGQVFCSPCPAGTSTVAQGAFSASHC 1470
Cdd:pfam07699    1 GTYSNTGLepCIPCPRGTYQPEEGQLSCLACPLGTTTDSPGATSISDC 48
TY super family cl00150
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1133-1194 1.41e-06

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: 47.68  E-value: 1.41e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1049017891 1133 SLQKTLALQREVALGYEPECVQDGqHFSPLQCDLSD--CWCVSDSGKELPMTRSPrstGQTPAC 1194
Cdd:pfam00086    7 RALEQAASGRPASGLYIPNCDEDG-FYKPVQCHGSTgyCWCVDPEGQEIPGTRTR---GGDPDC 66
TY super family cl00150
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 165-249 1.77e-03

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


The actual alignment was detected with superfamily member pfam00086:

Pssm-ID: 469630  Cd Length: 66  Bit Score: 38.82  E-value: 1.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891  165 CEvRER-RLLHGIGERSP------PQCSDDGGFLPVQCkfvnttdrmifdllHTfnrqpevfqtfsgfrkaypeLSSYCF 237
Cdd:pfam00086    1 CE-RERaRALEQAASGRPasglyiPNCDEDGFYKPVQC--------------HG--------------------STGYCW 45

                           90
                   ....*....|..
gi 1049017891  238 CADSRGREMPST 249
Cdd:pfam00086   46 CVDPEGQEIPGT 57
 
Name Accession Description Interval E-value
COesterase pfam00135
Carboxylesterase family;
2172-2678 1.80e-136

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 438.28  E-value: 1.80e-136
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 2172 GTLLGEseVKPITGSDSkrVTYFLGVPYARPPIGDLRFSPPQPAD-WTGTWNATFFRSSCLQPGDLTDSSS-----SEDC 2245
Cdd:pfam00135   10 GRVRGK--RLKVDGGKP--VYAFLGIPYAEPPVGELRFQPPEPPEpWTGVRDATKFGPRCPQNGDLTSPGSsglegSEDC 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 2246 LYLNVFV---ASSVAKNAPVLVFFHN------SGSdLLDGSYLAAVGNIIVVTASFRMAAFGFLSAGSSALPGNYGLQDQ 2316
Cdd:pfam00135   86 LYLNVYTpkeLKENKNKLPVMVWIHGggfmfgSGS-LYDGSYLAAEGDVIVVTINYRLGPLGFLSTGDDEAPGNYGLLDQ 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 2317 AAALGWVQKNIALFGGDPTKVTVGAERNGADIASLHLTSPSASSLFSRALLMGGSVFSPAVVMSSSKAQAQTssLARELD 2396
Cdd:pfam00135  165 VLALRWVQENIASFGGDPNRVTLFGESAGAASVSLLLLSPLSKGLFHRAILMSGSALSPWAIQSNARQRAKE--LAKLVG 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 2397 CQAADPSQLLDCLRSKPAHSINAAQTKLL-AVSGPLQAWSPVVDGNVVREMPSVALQSGRFHKAEILLGSSFEDGLISRA 2475
Cdd:pfam00135  243 CPTSDSAELVECLRSKPAEELLDAQLKLLvYGSVPFVPFGPVVDGDFLPEHPEELLKSGNFPKVPLLIGVTKDEGLLFAA 322

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 2476 KN------IKNFEQLQGRADSKTAFYAALsnslggDDANAFVKEAATWFYSLQHSptPSGYNVFSRALENATRDLFIICP 2549
Cdd:pfam00135  323 YIldnvdiLKALEEKLLRSLLIDLLYLLL------VDLPEEISAALREEYLDWGD--RDDPETSRRALVELLTDYLFNCP 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 2550 TVDMAEFWAANTqTGVYMYHlpenAAYNSVDLSVP--------MDVQYLFGVPLaaEQRDLFSYKEKTFTLQIMNYMANF 2621
Cdd:pfam00135  395 VIRFADLHASRG-TPVYMYS----FDYRGSSLRYPkwvgvdhgDELPYVFGTPF--VGALLFTEEDEKLSRKMMTYWTNF 467

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1049017891 2622 IKSGNPNLPLaasrtsfgkFLPPWPQFMPHvgGRAYKELSSTLVNRKNLQRSQCSFW 2678
Cdd:pfam00135  468 AKTGNPNGPE---------GLPKWPPYTDE--NGQYLSIDLEPRVKQGLKAERCAFW 513
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
2182-2682 2.88e-102

Carboxylesterase type B [Lipid transport and metabolism];


Pssm-ID: 441873  Cd Length: 500  Bit Score: 338.79  E-value: 2.88e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 2182 PITGSDSKRVTYFLGVPYARPPIGDLRFSPPQPAD-WTGTWNATFFRSSCLQPGDLTDS----SSSEDCLYLNVFV-ASS 2255
Cdd:COG2272     21 RVRGVVEGGVRVFLGIPYAAPPVGELRWRAPQPVEpWTGVRDATEFGPACPQPPRPGDPggpaPGSEDCLYLNVWTpALA 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 2256 VAKNAPVLVFFH-------NSGSDLLDGSYLAAVGnIIVVTASFRMAAFGF-----LSAGSSALPGNYGLQDQAAALGWV 2323
Cdd:COG2272    101 AGAKLPVMVWIHgggfvsgSGSEPLYDGAALARRG-VVVVTINYRLGALGFlalpaLSGESYGASGNYGLLDQIAALRWV 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 2324 QKNIALFGGDPTKVTVGAERNGADIASLHLTSPSASSLFSRALLMGGSVFSpavVMSSSKAQAQTSSLARELDCQAADps 2403
Cdd:COG2272    180 RDNIAAFGGDPDNVTIFGESAGAASVAALLASPLAKGLFHRAIAQSGAGLS---VLTLAEAEAVGAAFAAALGVAPAT-- 254

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 2404 qlLDCLRSKPAHSINAAQTKLLAVSGPLQAWSPVVDGNVVREMPSVALQSGRFHKAEILLGSSFEDGlisrakniKNFEQ 2483
Cdd:COG2272    255 --LAALRALPAEELLAAQAALAAEGPGGLPFGPVVDGDVLPEDPLEAFAAGRAADVPLLIGTNRDEG--------RLFAA 324

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 2484 LQGRADSKT-AFYAALSNSLGGDDANAFVKEaatwfYslqhsPTPSgynvFSRALENATRDLFIICPTVDMAEFWAANTQ 2562
Cdd:COG2272    325 LLGDLGPLTaADYRAALRRRFGDDADEVLAA-----Y-----PAAS----PAEALAALATDRVFRCPARRLAEAHAAAGA 390

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 2563 TgVYMYHL-PENAAYNSVDLSVP--MDVQYLFG-------VPLAAEQRDLfsykektfTLQIMNYMANFIKSGNPNlpla 2632
Cdd:COG2272    391 P-VYLYRFdWRSPPLRGFGLGAFhgAELPFVFGnldapalTGLTPADRAL--------SDQMQAYWVNFARTGDPN---- 457

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1049017891 2633 asrtsfGKFLPPWPQFMPhvGGRAYKELSSTL-VNRKNLQRSQCSFWSQYV 2682
Cdd:COG2272    458 ------GPGLPEWPAYDP--EDRAVMVFDAEPrVVNDPDAEERLDLWDGVV 500
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 2182-2648 2.71e-99

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: 330.06  E-value: 2.71e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 2182 PITGSDSKRVTYFLGVPYARPPIGDLRFSPPQPAD-WTGTWNATFFRSSCLQPGDL------TDSSSSEDCLYLNVFV-- 2252
Cdd:cd00312      8 KVRGVDEGGVYSFLGIPYAEPPVGDLRFKEPQPYEpWSDVLDATSYPPSCMQWDQLggglwnAKLPGSEDCLYLNVYTpk 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 2253 ASSVAKNAPVLVFFHN------SGSDLLDGSYLAAVGNIIVVTASFRMAAFGFLSAGSSALPGNYGLQDQAAALGWVQKN 2326
Cdd:cd00312     88 NTKPGNSLPVMVWIHGggfmfgSGSLYPGDGLAREGDNVIVVSINYRLGVLGFLSTGDIELPGNYGLKDQRLALKWVQDN 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 2327 IALFGGDPTKVTVGAERNGADIASLHLTSPSASSLFSRALLMGGSVFSPAVVMSSSKAQAQtsSLARELDCQAADPSQLL 2406
Cdd:cd00312    168 IAAFGGDPDSVTIFGESAGGASVSLLLLSPDSKGLFHRAISQSGSALSPWAIQENARGRAK--RLARLLGCNDTSSAELL 245

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 2407 DCLRSKPAHSINAAQTKLLAVSGPLQ-AWSPVVDGNVVREMPSVALQSGRFHKAEILLGSSFEDGLISRAKNIKNFEQLQ 2485
Cdd:cd00312    246 DCLRSKSAEELLDATRKLLLFSYSPFlPFGPVVDGDFIPDDPEELIKEGKFAKVPLIIGVTKDEGGYFAAMLLNFDAKLI 325

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 2486 GRADskTAFYAALSNSL-GGDDANAfvkEAATWFYSLQHSPTPSGYNVFSRALEnatrDLFIICPTVDMAEFWAANTQTG 2564
Cdd:cd00312    326 IETN--DRWLELLPYLLfYADDALA---DKVLEKYPGDVDDSVESRKNLSDMLT----DLLFKCPARYFLAQHRKAGGSP 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 2565 VYMY---HLPEN-AAYNSVDLSVPM--DVQYLFGVPLAAEQRDlfsYKEKTFTLQIMNYMANFIKSGNPNLPLAasrtsf 2638
Cdd:cd00312    397 VYAYvfdHRSSLsVGRWPPWLGTVHgdEIFFVFGNPLLKEGLR---EEEEKLSRTMMKYWANFAKTGNPNTEGN------ 467

                          490
                   ....*....|
gi 1049017891 2639 gkfLPPWPQF 2648
Cdd:cd00312    468 ---LVVWPAY 474
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 301-358 2.43e-17

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


Pssm-ID: 238114  Cd Length: 66  Bit Score: 78.27  E-value: 2.43e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1049017891  301 PCESERAAASQ------AGNSFVPSCTDNGAYVPTQCQ-SGGQCWCVDTYGKEIFGTR-QNGVPKC 358
Cdd:cd00191      1 PCERERASALEslagpkLSGLYVPQCDEDGNYEPVQCHgSTGYCWCVDPDGEEIPGTRtRGGPPNC 66
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 302-358 2.59e-17

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


Pssm-ID: 459665  Cd Length: 66  Bit Score: 78.11  E-value: 2.59e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1049017891  302 CESERAAASQAGNS-------FVPSCTDNGAYVPTQC-QSGGQCWCVDTYGKEIFGTR-QNGVPKC 358
Cdd:pfam00086    1 CERERARALEQAASgrpasglYIPNCDEDGFYKPVQChGSTGYCWCVDPEGQEIPGTRtRGGDPDC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 594-639 2.82e-17

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


Pssm-ID: 238114  Cd Length: 66  Bit Score: 78.27  E-value: 2.82e-17
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1049017891  594 SAPYLPQCTEDGLYQDVQCQGS--ECWCVDSRGLEVPGSRTTGSRPRC 639
Cdd:cd00191     19 SGLYVPQCDEDGNYEPVQCHGStgYCWCVDPDGEEIPGTRTRGGPPNC 66
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 102-161 1.56e-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: 75.80  E-value: 1.56e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1049017891  102 CQLQRQRALQTEDATL------VPVCLDSGEYQQVQCDASRSQCWCVDLEGMEIYGTRQNGKPSKC 161
Cdd:pfam00086    1 CERERARALEQAASGRpasglyIPNCDEDGFYKPVQCHGSTGYCWCVDPEGQEIPGTRTRGGDPDC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 102-161 1.81e-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: 75.96  E-value: 1.81e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1049017891  102 CQLQRQRALQTEDATL-----VPVCLDSGEYQQVQCDASRSQCWCVDLEGMEIYGTRQNGKPSKC 161
Cdd:cd00191      2 CERERASALESLAGPKlsglyVPQCDEDGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRGGPPNC 66
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 597-639 2.39e-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: 72.72  E-value: 2.39e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1049017891  597 YLPQCTEDGLYQDVQCQGS--ECWCVDSRGLEVPGSRTTGSRPRC 639
Cdd:pfam00086   22 YIPNCDEDGFYKPVQCHGStgYCWCVDPEGQEIPGTRTRGGDPDC 66
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 598-641 8.32e-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: 8.32e-15
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1049017891   598 LPQCTEDGLYQDVQCQGS--ECWCVDSRGLEVPGSRTTGSRPRCPS 641
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSsgQCWCVDATGREIPGTRTEGGDPDCPS 46
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 118-162 1.14e-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: 70.10  E-value: 1.14e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 1049017891   118 VPVCLDSGEYQQVQCDASRSQCWCVDLEGMEIYGTRQNGKPSKCP 162
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSSGQCWCVDATGREIPGTRTEGGDPDCP 45
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 40-98 1.16e-14

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


Pssm-ID: 459665  Cd Length: 66  Bit Score: 70.79  E-value: 1.16e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1049017891   40 CEQLR-------SVSAEQERQHVPQCFEDGRFRHVQCNRGGGECWCVNAEGFEIPGSRQNGSSVYC 98
Cdd:pfam00086    1 CERERaraleqaASGRPASGLYIPNCDEDGFYKPVQCHGSTGYCWCVDPEGQEIPGTRTRGGDPDC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 40-98 4.48e-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


Pssm-ID: 238114  Cd Length: 66  Bit Score: 69.03  E-value: 4.48e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1049017891   40 CEQLRSVSAEQ------ERQHVPQCFEDGRFRHVQCNRGGGECWCVNAEGFEIPGSRQNGSSVYC 98
Cdd:cd00191      2 CERERASALESlagpklSGLYVPQCDEDGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRGGPPNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 990-1047 2.24e-13

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: 67.10  E-value: 2.24e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1049017891  990 RLMASDRDRQSLMLGYQPYIPQCDAYGQWLPNQCYQSTGLCWCVDEEGQYIADSLTSR 1047
Cdd:cd00191      4 RERASALESLAGPKLSGLYVPQCDEDGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRG 61
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 55-100 4.38e-13

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: 65.48  E-value: 4.38e-13
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1049017891    55 VPQCFEDGRFRHVQCNRGGGECWCVNAEGFEIPGSRQNGSSVYCLT 100
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSSGQCWCVDATGREIPGTRTEGGDPDCPS 46
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 1008-1051 4.73e-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: 4.73e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1049017891 1008 YIPQCDAYGQWLPNQCYQSTGLCWCVDEEGQYIADSLTSRSSLP 1051
Cdd:pfam00086   22 YIPNCDEDGFYKPVQCHGSTGYCWCVDPEGQEIPGTRTRGGDPD 65
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 643-705 1.03e-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: 65.02  E-value: 1.03e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1049017891  643 CEKERQMAIAVKASSSAGSEVFIPKCETDGAYVARQCLGKS--CFCVDRSGTKL-GIQSSGSSLQC 705
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 ...
 1425-1470 1.03e-11

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: 61.60  E-value: 1.03e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1049017891 1425 GSFFSGGV--CTPCPRDTFQEDEGQVFCSPCPAGTSTVAQGAFSASHC 1470
Cdd:pfam07699    1 GTYSNTGLepCIPCPRGTYQPEEGQLSCLACPLGTTTDSPGATSISDC 48
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 317-360 1.04e-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: 61.62  E-value: 1.04e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1049017891   317 VPSCTDNGAYVPTQC-QSGGQCWCVDTYGKEIFGTR-QNGVPKCST 360
Cdd:smart00211    1 IPQCDEDGNYEPVQCdGSSGQCWCVDATGREIPGTRtEGGDPDCPS 46
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1009-1049 2.54e-10

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: 57.77  E-value: 2.54e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1049017891  1009 IPQCDAYGQWLPNQCYQSTGLCWCVDEEGQYIADSLTSRSS 1049
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSSGQCWCVDATGREIPGTRTEGGD 41
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 643-705 8.42e-08

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


Pssm-ID: 238114  Cd Length: 66  Bit Score: 51.31  E-value: 8.42e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1049017891  643 CEKERQMAIAVKASSSAGSeVFIPKCETDGAYVARQCLGK--SCFCVDRSGTKL-GIQSSGSSLQC 705
Cdd:cd00191      2 CERERASALESLAGPKLSG-LYVPQCDEDGNYEPVQCHGStgYCWCVDPDGEEIpGTRTRGGPPNC 66
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 1133-1194 1.41e-06

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: 47.68  E-value: 1.41e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1049017891 1133 SLQKTLALQREVALGYEPECVQDGqHFSPLQCDLSD--CWCVSDSGKELPMTRSPrstGQTPAC 1194
Cdd:pfam00086    7 RALEQAASGRPASGLYIPNCDEDG-FYKPVQCHGSTgyCWCVDPEGQEIPGTRTR---GGDPDC 66
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 665-707 4.17e-06

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: 45.83  E-value: 4.17e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1049017891   665 IPKCETDGAYVARQCLGKS--CFCVDRSGTKL-GIQSSGSSLQCPT 707
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSSgqCWCVDATGREIpGTRTEGGDPDCPS 46
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 165-249 1.77e-03

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


Pssm-ID: 459665  Cd Length: 66  Bit Score: 38.82  E-value: 1.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891  165 CEvRER-RLLHGIGERSP------PQCSDDGGFLPVQCkfvnttdrmifdllHTfnrqpevfqtfsgfrkaypeLSSYCF 237
Cdd:pfam00086    1 CE-RERaRALEQAASGRPasglyiPNCDEDGFYKPVQC--------------HG--------------------STGYCW 45

                           90
                   ....*....|..
gi 1049017891  238 CADSRGREMPST 249
Cdd:pfam00086   46 CVDPEGQEIPGT 57
TNFRSF cd00185
Tumor necrosis factor receptor superfamily (TNFRSF); Members of TNFR superfamily (TNFRSF) ...
 1419-1475 2.00e-03

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


Pssm-ID: 276900 [Multi-domain]  Cd Length: 87  Bit Score: 39.50  E-value: 2.00e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 1419 CVLCPAGSF-------FSGGVCTPCPRDTFQEDEGQVF----CSPCPAGTSTVAQG--AFSASHCltECK 1475
Cdd:cd00185      2 CQRCPPGEYlssdctaTTDTVCSPCPPGTYSESWNSLSkclpCTTCGGGNQVEKTPctATDNRCC--TCK 69
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 165-249 6.08e-03

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


Pssm-ID: 238114  Cd Length: 66  Bit Score: 37.44  E-value: 6.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891  165 CEVRERRLLHGIGERSP-----PQCSDDGGFLPVQCkfvnttdrmifdllhtfnrqpevfqtfsgfrkaYPELsSYCFCA 239
Cdd:cd00191      2 CERERASALESLAGPKLsglyvPQCDEDGNYEPVQC---------------------------------HGST-GYCWCV 47

                           90
                   ....*....|
gi 1049017891  240 DSRGREMPST 249
Cdd:cd00191     48 DPDGEEIPGT 57
 
Name Accession Description Interval E-value
COesterase pfam00135
Carboxylesterase family;
2172-2678 1.80e-136

Carboxylesterase family;


Pssm-ID: 395084 [Multi-domain]  Cd Length: 513  Bit Score: 438.28  E-value: 1.80e-136
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 2172 GTLLGEseVKPITGSDSkrVTYFLGVPYARPPIGDLRFSPPQPAD-WTGTWNATFFRSSCLQPGDLTDSSS-----SEDC 2245
Cdd:pfam00135   10 GRVRGK--RLKVDGGKP--VYAFLGIPYAEPPVGELRFQPPEPPEpWTGVRDATKFGPRCPQNGDLTSPGSsglegSEDC 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 2246 LYLNVFV---ASSVAKNAPVLVFFHN------SGSdLLDGSYLAAVGNIIVVTASFRMAAFGFLSAGSSALPGNYGLQDQ 2316
Cdd:pfam00135   86 LYLNVYTpkeLKENKNKLPVMVWIHGggfmfgSGS-LYDGSYLAAEGDVIVVTINYRLGPLGFLSTGDDEAPGNYGLLDQ 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 2317 AAALGWVQKNIALFGGDPTKVTVGAERNGADIASLHLTSPSASSLFSRALLMGGSVFSPAVVMSSSKAQAQTssLARELD 2396
Cdd:pfam00135  165 VLALRWVQENIASFGGDPNRVTLFGESAGAASVSLLLLSPLSKGLFHRAILMSGSALSPWAIQSNARQRAKE--LAKLVG 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 2397 CQAADPSQLLDCLRSKPAHSINAAQTKLL-AVSGPLQAWSPVVDGNVVREMPSVALQSGRFHKAEILLGSSFEDGLISRA 2475
Cdd:pfam00135  243 CPTSDSAELVECLRSKPAEELLDAQLKLLvYGSVPFVPFGPVVDGDFLPEHPEELLKSGNFPKVPLLIGVTKDEGLLFAA 322

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 2476 KN------IKNFEQLQGRADSKTAFYAALsnslggDDANAFVKEAATWFYSLQHSptPSGYNVFSRALENATRDLFIICP 2549
Cdd:pfam00135  323 YIldnvdiLKALEEKLLRSLLIDLLYLLL------VDLPEEISAALREEYLDWGD--RDDPETSRRALVELLTDYLFNCP 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 2550 TVDMAEFWAANTqTGVYMYHlpenAAYNSVDLSVP--------MDVQYLFGVPLaaEQRDLFSYKEKTFTLQIMNYMANF 2621
Cdd:pfam00135  395 VIRFADLHASRG-TPVYMYS----FDYRGSSLRYPkwvgvdhgDELPYVFGTPF--VGALLFTEEDEKLSRKMMTYWTNF 467

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1049017891 2622 IKSGNPNLPLaasrtsfgkFLPPWPQFMPHvgGRAYKELSSTLVNRKNLQRSQCSFW 2678
Cdd:pfam00135  468 AKTGNPNGPE---------GLPKWPPYTDE--NGQYLSIDLEPRVKQGLKAERCAFW 513
PnbA COG2272
Carboxylesterase type B [Lipid transport and metabolism];
2182-2682 2.88e-102

Carboxylesterase type B [Lipid transport and metabolism];


Pssm-ID: 441873  Cd Length: 500  Bit Score: 338.79  E-value: 2.88e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 2182 PITGSDSKRVTYFLGVPYARPPIGDLRFSPPQPAD-WTGTWNATFFRSSCLQPGDLTDS----SSSEDCLYLNVFV-ASS 2255
Cdd:COG2272     21 RVRGVVEGGVRVFLGIPYAAPPVGELRWRAPQPVEpWTGVRDATEFGPACPQPPRPGDPggpaPGSEDCLYLNVWTpALA 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 2256 VAKNAPVLVFFH-------NSGSDLLDGSYLAAVGnIIVVTASFRMAAFGF-----LSAGSSALPGNYGLQDQAAALGWV 2323
Cdd:COG2272    101 AGAKLPVMVWIHgggfvsgSGSEPLYDGAALARRG-VVVVTINYRLGALGFlalpaLSGESYGASGNYGLLDQIAALRWV 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 2324 QKNIALFGGDPTKVTVGAERNGADIASLHLTSPSASSLFSRALLMGGSVFSpavVMSSSKAQAQTSSLARELDCQAADps 2403
Cdd:COG2272    180 RDNIAAFGGDPDNVTIFGESAGAASVAALLASPLAKGLFHRAIAQSGAGLS---VLTLAEAEAVGAAFAAALGVAPAT-- 254

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 2404 qlLDCLRSKPAHSINAAQTKLLAVSGPLQAWSPVVDGNVVREMPSVALQSGRFHKAEILLGSSFEDGlisrakniKNFEQ 2483
Cdd:COG2272    255 --LAALRALPAEELLAAQAALAAEGPGGLPFGPVVDGDVLPEDPLEAFAAGRAADVPLLIGTNRDEG--------RLFAA 324

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 2484 LQGRADSKT-AFYAALSNSLGGDDANAFVKEaatwfYslqhsPTPSgynvFSRALENATRDLFIICPTVDMAEFWAANTQ 2562
Cdd:COG2272    325 LLGDLGPLTaADYRAALRRRFGDDADEVLAA-----Y-----PAAS----PAEALAALATDRVFRCPARRLAEAHAAAGA 390

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 2563 TgVYMYHL-PENAAYNSVDLSVP--MDVQYLFG-------VPLAAEQRDLfsykektfTLQIMNYMANFIKSGNPNlpla 2632
Cdd:COG2272    391 P-VYLYRFdWRSPPLRGFGLGAFhgAELPFVFGnldapalTGLTPADRAL--------SDQMQAYWVNFARTGDPN---- 457

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1049017891 2633 asrtsfGKFLPPWPQFMPhvGGRAYKELSSTL-VNRKNLQRSQCSFWSQYV 2682
Cdd:COG2272    458 ------GPGLPEWPAYDP--EDRAVMVFDAEPrVVNDPDAEERLDLWDGVV 500
Esterase_lipase cd00312
Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on ...
 2182-2648 2.71e-99

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: 330.06  E-value: 2.71e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 2182 PITGSDSKRVTYFLGVPYARPPIGDLRFSPPQPAD-WTGTWNATFFRSSCLQPGDL------TDSSSSEDCLYLNVFV-- 2252
Cdd:cd00312      8 KVRGVDEGGVYSFLGIPYAEPPVGDLRFKEPQPYEpWSDVLDATSYPPSCMQWDQLggglwnAKLPGSEDCLYLNVYTpk 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 2253 ASSVAKNAPVLVFFHN------SGSDLLDGSYLAAVGNIIVVTASFRMAAFGFLSAGSSALPGNYGLQDQAAALGWVQKN 2326
Cdd:cd00312     88 NTKPGNSLPVMVWIHGggfmfgSGSLYPGDGLAREGDNVIVVSINYRLGVLGFLSTGDIELPGNYGLKDQRLALKWVQDN 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 2327 IALFGGDPTKVTVGAERNGADIASLHLTSPSASSLFSRALLMGGSVFSPAVVMSSSKAQAQtsSLARELDCQAADPSQLL 2406
Cdd:cd00312    168 IAAFGGDPDSVTIFGESAGGASVSLLLLSPDSKGLFHRAISQSGSALSPWAIQENARGRAK--RLARLLGCNDTSSAELL 245

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 2407 DCLRSKPAHSINAAQTKLLAVSGPLQ-AWSPVVDGNVVREMPSVALQSGRFHKAEILLGSSFEDGLISRAKNIKNFEQLQ 2485
Cdd:cd00312    246 DCLRSKSAEELLDATRKLLLFSYSPFlPFGPVVDGDFIPDDPEELIKEGKFAKVPLIIGVTKDEGGYFAAMLLNFDAKLI 325

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 2486 GRADskTAFYAALSNSL-GGDDANAfvkEAATWFYSLQHSPTPSGYNVFSRALEnatrDLFIICPTVDMAEFWAANTQTG 2564
Cdd:cd00312    326 IETN--DRWLELLPYLLfYADDALA---DKVLEKYPGDVDDSVESRKNLSDMLT----DLLFKCPARYFLAQHRKAGGSP 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 2565 VYMY---HLPEN-AAYNSVDLSVPM--DVQYLFGVPLAAEQRDlfsYKEKTFTLQIMNYMANFIKSGNPNLPLAasrtsf 2638
Cdd:cd00312    397 VYAYvfdHRSSLsVGRWPPWLGTVHgdEIFFVFGNPLLKEGLR---EEEEKLSRTMMKYWANFAKTGNPNTEGN------ 467

                          490
                   ....*....|
gi 1049017891 2639 gkfLPPWPQF 2648
Cdd:cd00312    468 ---LVVWPAY 474
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 301-358 2.43e-17

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


Pssm-ID: 238114  Cd Length: 66  Bit Score: 78.27  E-value: 2.43e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1049017891  301 PCESERAAASQ------AGNSFVPSCTDNGAYVPTQCQ-SGGQCWCVDTYGKEIFGTR-QNGVPKC 358
Cdd:cd00191      1 PCERERASALEslagpkLSGLYVPQCDEDGNYEPVQCHgSTGYCWCVDPDGEEIPGTRtRGGPPNC 66
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 302-358 2.59e-17

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


Pssm-ID: 459665  Cd Length: 66  Bit Score: 78.11  E-value: 2.59e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1049017891  302 CESERAAASQAGNS-------FVPSCTDNGAYVPTQC-QSGGQCWCVDTYGKEIFGTR-QNGVPKC 358
Cdd:pfam00086    1 CERERARALEQAASgrpasglYIPNCDEDGFYKPVQChGSTGYCWCVDPEGQEIPGTRtRGGDPDC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 594-639 2.82e-17

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


Pssm-ID: 238114  Cd Length: 66  Bit Score: 78.27  E-value: 2.82e-17
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1049017891  594 SAPYLPQCTEDGLYQDVQCQGS--ECWCVDSRGLEVPGSRTTGSRPRC 639
Cdd:cd00191     19 SGLYVPQCDEDGNYEPVQCHGStgYCWCVDPDGEEIPGTRTRGGPPNC 66
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 102-161 1.56e-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: 75.80  E-value: 1.56e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1049017891  102 CQLQRQRALQTEDATL------VPVCLDSGEYQQVQCDASRSQCWCVDLEGMEIYGTRQNGKPSKC 161
Cdd:pfam00086    1 CERERARALEQAASGRpasglyIPNCDEDGFYKPVQCHGSTGYCWCVDPEGQEIPGTRTRGGDPDC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 102-161 1.81e-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: 75.96  E-value: 1.81e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1049017891  102 CQLQRQRALQTEDATL-----VPVCLDSGEYQQVQCDASRSQCWCVDLEGMEIYGTRQNGKPSKC 161
Cdd:cd00191      2 CERERASALESLAGPKlsglyVPQCDEDGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRGGPPNC 66
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 597-639 2.39e-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: 72.72  E-value: 2.39e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1049017891  597 YLPQCTEDGLYQDVQCQGS--ECWCVDSRGLEVPGSRTTGSRPRC 639
Cdd:pfam00086   22 YIPNCDEDGFYKPVQCHGStgYCWCVDPEGQEIPGTRTRGGDPDC 66
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 598-641 8.32e-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: 8.32e-15
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1049017891   598 LPQCTEDGLYQDVQCQGS--ECWCVDSRGLEVPGSRTTGSRPRCPS 641
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSsgQCWCVDATGREIPGTRTEGGDPDCPS 46
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 118-162 1.14e-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: 70.10  E-value: 1.14e-14
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 1049017891   118 VPVCLDSGEYQQVQCDASRSQCWCVDLEGMEIYGTRQNGKPSKCP 162
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSSGQCWCVDATGREIPGTRTEGGDPDCP 45
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 40-98 1.16e-14

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


Pssm-ID: 459665  Cd Length: 66  Bit Score: 70.79  E-value: 1.16e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1049017891   40 CEQLR-------SVSAEQERQHVPQCFEDGRFRHVQCNRGGGECWCVNAEGFEIPGSRQNGSSVYC 98
Cdd:pfam00086    1 CERERaraleqaASGRPASGLYIPNCDEDGFYKPVQCHGSTGYCWCVDPEGQEIPGTRTRGGDPDC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 40-98 4.48e-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


Pssm-ID: 238114  Cd Length: 66  Bit Score: 69.03  E-value: 4.48e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1049017891   40 CEQLRSVSAEQ------ERQHVPQCFEDGRFRHVQCNRGGGECWCVNAEGFEIPGSRQNGSSVYC 98
Cdd:cd00191      2 CERERASALESlagpklSGLYVPQCDEDGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRGGPPNC 66
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 990-1047 2.24e-13

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: 67.10  E-value: 2.24e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1049017891  990 RLMASDRDRQSLMLGYQPYIPQCDAYGQWLPNQCYQSTGLCWCVDEEGQYIADSLTSR 1047
Cdd:cd00191      4 RERASALESLAGPKLSGLYVPQCDEDGNYEPVQCHGSTGYCWCVDPDGEEIPGTRTRG 61
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 55-100 4.38e-13

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: 65.48  E-value: 4.38e-13
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1049017891    55 VPQCFEDGRFRHVQCNRGGGECWCVNAEGFEIPGSRQNGSSVYCLT 100
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSSGQCWCVDATGREIPGTRTEGGDPDCPS 46
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 1008-1051 4.73e-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: 4.73e-13
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1049017891 1008 YIPQCDAYGQWLPNQCYQSTGLCWCVDEEGQYIADSLTSRSSLP 1051
Cdd:pfam00086   22 YIPNCDEDGFYKPVQCHGSTGYCWCVDPEGQEIPGTRTRGGDPD 65
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 643-705 1.03e-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: 65.02  E-value: 1.03e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1049017891  643 CEKERQMAIAVKASSSAGSEVFIPKCETDGAYVARQCLGKS--CFCVDRSGTKL-GIQSSGSSLQC 705
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 ...
 1425-1470 1.03e-11

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: 61.60  E-value: 1.03e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1049017891 1425 GSFFSGGV--CTPCPRDTFQEDEGQVFCSPCPAGTSTVAQGAFSASHC 1470
Cdd:pfam07699    1 GTYSNTGLepCIPCPRGTYQPEEGQLSCLACPLGTTTDSPGATSISDC 48
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 317-360 1.04e-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: 61.62  E-value: 1.04e-11
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1049017891   317 VPSCTDNGAYVPTQC-QSGGQCWCVDTYGKEIFGTR-QNGVPKCST 360
Cdd:smart00211    1 IPQCDEDGNYEPVQCdGSSGQCWCVDATGREIPGTRtEGGDPDCPS 46
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 1009-1049 2.54e-10

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: 57.77  E-value: 2.54e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1049017891  1009 IPQCDAYGQWLPNQCYQSTGLCWCVDEEGQYIADSLTSRSS 1049
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSSGQCWCVDATGREIPGTRTEGGD 41
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 643-705 8.42e-08

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


Pssm-ID: 238114  Cd Length: 66  Bit Score: 51.31  E-value: 8.42e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1049017891  643 CEKERQMAIAVKASSSAGSeVFIPKCETDGAYVARQCLGK--SCFCVDRSGTKL-GIQSSGSSLQC 705
Cdd:cd00191      2 CERERASALESLAGPKLSG-LYVPQCDEDGNYEPVQCHGStgYCWCVDPDGEEIpGTRTRGGPPNC 66
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 1133-1194 1.41e-06

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: 47.68  E-value: 1.41e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1049017891 1133 SLQKTLALQREVALGYEPECVQDGqHFSPLQCDLSD--CWCVSDSGKELPMTRSPrstGQTPAC 1194
Cdd:pfam00086    7 RALEQAASGRPASGLYIPNCDEDG-FYKPVQCHGSTgyCWCVDPEGQEIPGTRTR---GGDPDC 66
TY smart00211
Thyroglobulin type I repeats; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 665-707 4.17e-06

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: 45.83  E-value: 4.17e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1049017891   665 IPKCETDGAYVARQCLGKS--CFCVDRSGTKL-GIQSSGSSLQCPT 707
Cdd:smart00211    1 IPQCDEDGNYEPVQCDGSSgqCWCVDATGREIpGTRTEGGDPDCPS 46
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
2250-2340 7.01e-06

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 49.49  E-value: 7.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 2250 VFVASSVAKNAPVLVFFH----NSGS-DLLDG--SYLAAVGNIIVVTASFRMA-AFGFlsagssalPGnyGLQDQAAALG 2321
Cdd:COG0657      3 VYRPAGAKGPLPVVVYFHgggwVSGSkDTHDPlaRRLAARAGAAVVSVDYRLApEHPF--------PA--ALEDAYAALR 72

                           90
                   ....*....|....*....
gi 1049017891 2322 WVQKNIALFGGDPTKVTVG 2340
Cdd:COG0657     73 WLRANAAELGIDPDRIAVA 91
Thyroglobulin_1 pfam00086
Thyroglobulin type-1 repeat; Thyroglobulin type 1 repeats are thought to be involved in the ...
 165-249 1.77e-03

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


Pssm-ID: 459665  Cd Length: 66  Bit Score: 38.82  E-value: 1.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891  165 CEvRER-RLLHGIGERSP------PQCSDDGGFLPVQCkfvnttdrmifdllHTfnrqpevfqtfsgfrkaypeLSSYCF 237
Cdd:pfam00086    1 CE-RERaRALEQAASGRPasglyiPNCDEDGFYKPVQC--------------HG--------------------STGYCW 45

                           90
                   ....*....|..
gi 1049017891  238 CADSRGREMPST 249
Cdd:pfam00086   46 CVDPEGQEIPGT 57
TNFRSF cd00185
Tumor necrosis factor receptor superfamily (TNFRSF); Members of TNFR superfamily (TNFRSF) ...
 1419-1475 2.00e-03

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


Pssm-ID: 276900 [Multi-domain]  Cd Length: 87  Bit Score: 39.50  E-value: 2.00e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891 1419 CVLCPAGSF-------FSGGVCTPCPRDTFQEDEGQVF----CSPCPAGTSTVAQG--AFSASHCltECK 1475
Cdd:cd00185      2 CQRCPPGEYlssdctaTTDTVCSPCPPGTYSESWNSLSkclpCTTCGGGNQVEKTPctATDNRCC--TCK 69
TY cd00191
Thyroglobulin type I repeats.; The N-terminal region of human thyroglobulin contains 11 type-1 ...
 165-249 6.08e-03

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


Pssm-ID: 238114  Cd Length: 66  Bit Score: 37.44  E-value: 6.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049017891  165 CEVRERRLLHGIGERSP-----PQCSDDGGFLPVQCkfvnttdrmifdllhtfnrqpevfqtfsgfrkaYPELsSYCFCA 239
Cdd:cd00191      2 CERERASALESLAGPKLsglyvPQCDEDGNYEPVQC---------------------------------HGST-GYCWCV 47

                           90
                   ....*....|
gi 1049017891  240 DSRGREMPST 249
Cdd:cd00191     48 DPDGEEIPGT 57
 
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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