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Conserved domains on  [gi|1489787667|ref|NP_997954|]
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type II iodothyronine deiodinase [Danio rerio]

Protein Classification

thioredoxin domain-containing protein( domain architecture ID 144)

thioredoxin domain-containing protein may function as a thiol disulfide oxidoreductase that catalyzes the oxidation or reduction of protein disulfide bonds using an active site dithiol, present in a CXXC motif

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Thioredoxin_like super family cl00388
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ...
4-253 9.72e-109

Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin (TRX)-like superfamily is a large, diverse group of proteins containing a TRX fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include the families of TRX, protein disulfide isomerase (PDI), tlpA, glutaredoxin, NrdH redoxin, and bacterial Dsb proteins (DsbA, DsbC, DsbG, DsbE, DsbDgamma). Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins, glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


The actual alignment was detected with superfamily member pfam00837:

Pssm-ID: 469754  Cd Length: 237  Bit Score: 313.34  E-value: 9.72e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489787667   4 LSVDLLVTLQILPGFFSNCLFFVLYDSIVLVKRVVSLLSCSGST--GEWQRMLTTAGVRSIWNSFLLDAYKQVKLGEAAP 81
Cdd:pfam00837   1 LWLRRLWVLLQVPVFVAVGKVLLLLDPARVKKHIVAMNGRNPHFsyDNWARLYTMQYLWFVWKVQWLDLEKQTEPGGLAP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489787667  82 NSKVVKVTGinrcwsisgktHNQCHLLDFESPDRPLVVNFGSATUPPFISQLPVFRRMVEEFSDVADFLLVYIDEAHPSD 161
Cdd:pfam00837  81 NSPVVRLSG-----------QRGCHILDFAQGNRPLVLNFGSCTUPPFLFKFDAFKRLVEDFCSTADFLIIYIEEAHPSD 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489787667 162 GWVGPpmeNFSFEVRKHRNLEERMFAARTLLEHFslpPQCQLVADCMDNNANIAYGVSYERVCIVQKNKIAYLGGKGPFF 241
Cdd:pfam00837 150 GWAFK---NNSVNIRTHQTLEDRLQAARLLLDRA---PPCPVVVDTMRNQSSQAYGALFERLFVLQEGRILYKGGPGPWN 223
                         250
                  ....*....|..
gi 1489787667 242 YNLKDVRRWLEK 253
Cdd:pfam00837 224 YHPEEVRAWLEK 235
 
Name Accession Description Interval E-value
T4_deiodinase pfam00837
Iodothyronine deiodinase; Iodothyronine deiodinase converts thyroxine (T4) to 3,5,3 ...
4-253 9.72e-109

Iodothyronine deiodinase; Iodothyronine deiodinase converts thyroxine (T4) to 3,5,3'-triiodothyronine (T3).


Pssm-ID: 279210  Cd Length: 237  Bit Score: 313.34  E-value: 9.72e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489787667   4 LSVDLLVTLQILPGFFSNCLFFVLYDSIVLVKRVVSLLSCSGST--GEWQRMLTTAGVRSIWNSFLLDAYKQVKLGEAAP 81
Cdd:pfam00837   1 LWLRRLWVLLQVPVFVAVGKVLLLLDPARVKKHIVAMNGRNPHFsyDNWARLYTMQYLWFVWKVQWLDLEKQTEPGGLAP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489787667  82 NSKVVKVTGinrcwsisgktHNQCHLLDFESPDRPLVVNFGSATUPPFISQLPVFRRMVEEFSDVADFLLVYIDEAHPSD 161
Cdd:pfam00837  81 NSPVVRLSG-----------QRGCHILDFAQGNRPLVLNFGSCTUPPFLFKFDAFKRLVEDFCSTADFLIIYIEEAHPSD 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489787667 162 GWVGPpmeNFSFEVRKHRNLEERMFAARTLLEHFslpPQCQLVADCMDNNANIAYGVSYERVCIVQKNKIAYLGGKGPFF 241
Cdd:pfam00837 150 GWAFK---NNSVNIRTHQTLEDRLQAARLLLDRA---PPCPVVVDTMRNQSSQAYGALFERLFVLQEGRILYKGGPGPWN 223
                         250
                  ....*....|..
gi 1489787667 242 YNLKDVRRWLEK 253
Cdd:pfam00837 224 YHPEEVRAWLEK 235
deiodinase_rel NF038285
deiodinase family protein; Members of this protein family are related to iodothyronine ...
114-240 3.99e-19

deiodinase family protein; Members of this protein family are related to iodothyronine deiodinase, a human selenoprotein. Some members of this family (although not of the seed alignment) likewise are selenoproteins, with the selenium-containing motif GSYTUPPF.


Pssm-ID: 468451 [Multi-domain]  Cd Length: 347  Bit Score: 84.95  E-value: 3.99e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489787667 114 DRPLVVNFGSATUPPFISQLPVFRRMVEEFSDVADFLLVYIDEAHPSDGWVgppME-NFSF--EVRKHRNLEERMFAA-- 188
Cdd:NF038285  204 PKPVVLIFGNFTCGPFRSQYGNVEKLYRRYKDRATFLMVYVREAHPTDGWR---MEsNDRVgvAVAQPTTFEERVAVAqq 280
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1489787667 189 -RTLLEhFSLPpqcqLVADCMDNNANIAYGVSYERV-CIVQKNKIAYLGGKGPF 240
Cdd:NF038285  281 cRAKLK-LGMP----MLVDDIDDPVGNAYSGMPARLyVIDRAGKVAFKSGRGPF 329
 
Name Accession Description Interval E-value
T4_deiodinase pfam00837
Iodothyronine deiodinase; Iodothyronine deiodinase converts thyroxine (T4) to 3,5,3 ...
4-253 9.72e-109

Iodothyronine deiodinase; Iodothyronine deiodinase converts thyroxine (T4) to 3,5,3'-triiodothyronine (T3).


Pssm-ID: 279210  Cd Length: 237  Bit Score: 313.34  E-value: 9.72e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489787667   4 LSVDLLVTLQILPGFFSNCLFFVLYDSIVLVKRVVSLLSCSGST--GEWQRMLTTAGVRSIWNSFLLDAYKQVKLGEAAP 81
Cdd:pfam00837   1 LWLRRLWVLLQVPVFVAVGKVLLLLDPARVKKHIVAMNGRNPHFsyDNWARLYTMQYLWFVWKVQWLDLEKQTEPGGLAP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489787667  82 NSKVVKVTGinrcwsisgktHNQCHLLDFESPDRPLVVNFGSATUPPFISQLPVFRRMVEEFSDVADFLLVYIDEAHPSD 161
Cdd:pfam00837  81 NSPVVRLSG-----------QRGCHILDFAQGNRPLVLNFGSCTUPPFLFKFDAFKRLVEDFCSTADFLIIYIEEAHPSD 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489787667 162 GWVGPpmeNFSFEVRKHRNLEERMFAARTLLEHFslpPQCQLVADCMDNNANIAYGVSYERVCIVQKNKIAYLGGKGPFF 241
Cdd:pfam00837 150 GWAFK---NNSVNIRTHQTLEDRLQAARLLLDRA---PPCPVVVDTMRNQSSQAYGALFERLFVLQEGRILYKGGPGPWN 223
                         250
                  ....*....|..
gi 1489787667 242 YNLKDVRRWLEK 253
Cdd:pfam00837 224 YHPEEVRAWLEK 235
deiodinase_rel NF038285
deiodinase family protein; Members of this protein family are related to iodothyronine ...
114-240 3.99e-19

deiodinase family protein; Members of this protein family are related to iodothyronine deiodinase, a human selenoprotein. Some members of this family (although not of the seed alignment) likewise are selenoproteins, with the selenium-containing motif GSYTUPPF.


Pssm-ID: 468451 [Multi-domain]  Cd Length: 347  Bit Score: 84.95  E-value: 3.99e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1489787667 114 DRPLVVNFGSATUPPFISQLPVFRRMVEEFSDVADFLLVYIDEAHPSDGWVgppME-NFSF--EVRKHRNLEERMFAA-- 188
Cdd:NF038285  204 PKPVVLIFGNFTCGPFRSQYGNVEKLYRRYKDRATFLMVYVREAHPTDGWR---MEsNDRVgvAVAQPTTFEERVAVAqq 280
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1489787667 189 -RTLLEhFSLPpqcqLVADCMDNNANIAYGVSYERV-CIVQKNKIAYLGGKGPF 240
Cdd:NF038285  281 cRAKLK-LGMP----MLVDDIDDPVGNAYSGMPARLyVIDRAGKVAFKSGRGPF 329
 
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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