NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|3915183|sp|O55245|]
View 

RecName: Full=Transthyretin; Short=crocTTR; AltName: Full=Prealbumin; Flags: Precursor

Protein Classification

peptidase associated/transthyretin-like domain-containing protein( domain architecture ID 10638769)

peptidase associated/transthyretin-like domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
TR_THY smart00095
Transthyretin;
30-150 1.97e-83

Transthyretin;


:

Pssm-ID: 128406  Cd Length: 121  Bit Score: 240.56  E-value: 1.97e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915183      30 DSKCPLMVKVLDAVRGSPAANVAIKVFKKTSDGDWQEFAAGKTTEFGEVHELTSDEKFVEGIYRVEFDTSSYWKALGLSP 109
Cdd:smart00095   1 DSKCPLMVKVLDAVRGSPAVNVAVKVFKKTEEGTWEPFASGKTNESGEIHELTTDEKFVEGLYKVEFDTKSYWKALGISP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 3915183     110 FHEYADVVFTANDSGHRHYTIAALLSPFSYSTTAVVSDPQE 150
Cdd:smart00095  81 FHEYADVVFTANDSGHRHYTIAALLSPYSYSTTAVVSNPKE 121
 
Name Accession Description Interval E-value
TR_THY smart00095
Transthyretin;
30-150 1.97e-83

Transthyretin;


Pssm-ID: 128406  Cd Length: 121  Bit Score: 240.56  E-value: 1.97e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915183      30 DSKCPLMVKVLDAVRGSPAANVAIKVFKKTSDGDWQEFAAGKTTEFGEVHELTSDEKFVEGIYRVEFDTSSYWKALGLSP 109
Cdd:smart00095   1 DSKCPLMVKVLDAVRGSPAVNVAVKVFKKTEEGTWEPFASGKTNESGEIHELTTDEKFVEGLYKVEFDTKSYWKALGISP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 3915183     110 FHEYADVVFTANDSGHRHYTIAALLSPFSYSTTAVVSDPQE 150
Cdd:smart00095  81 FHEYADVVFTANDSGHRHYTIAALLSPYSYSTTAVVSNPKE 121
TLP_Transthyretin cd05821
Transthyretin (TTR) is a 55 kDa protein responsible for the transport of thyroid hormones and ...
 27-147 1.36e-80

Transthyretin (TTR) is a 55 kDa protein responsible for the transport of thyroid hormones and retinol in vertebrates. TTR distributes the two thyroid hormones T3 (3,5,3'-triiodo-L-thyronine) and T4 (Thyroxin, or 3,5,3',5'-tetraiodo-L-thyronine), as well as retinol (vitamin A) through the formation of a macromolecular complex that includes each of these as well as retinol-binding protein. Misfolded forms of TTR are implicated in the amyloid diseases familial amyloidotic polyneuropathy and senile systemic amyloidosis. TTR forms a homotetramer with each subunit consisting of eight beta-strands arranged in two sheets and a short alpha-helix. The central channel of the tetramer contains two independent binding sites, each located between a pair of subunits, which differ in their ligand binding affinity. A negative cooperativity has been observed for the binding of T4 and other TTR ligands. A fraction of plasma TTR is carried in high density lipoproteins by binding to apolipoprotein AI (apoA-I). TTR is able to proteolytically process apoA-I by cleaving its C-terminus; therefore TTR has protease activity in addition to its function in protein transport.


Pssm-ID: 100113  Cd Length: 121  Bit Score: 233.21  E-value: 1.36e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915183   27 GSIDSKCPLMVKVLDAVRGSPAANVAIKVFKKTSDGDWQEFAAGKTTEFGEVHELTSDEKFVEGIYRVEFDTSSYWKALG 106
Cdd:cd05821   1 GGGDSKCPLMVKVLDAVRGSPAANVAVKVFKKTADGSWEPFASGKTTETGEIHGLTTDEQFTEGVYKVEFDTKAYWKKLG 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 3915183  107 LSPFHEYADVVFTANDSGHRHYTIAALLSPFSYSTTAVVSD 147
Cdd:cd05821  81 ISPFHEYAEVVFTANDSGHRHYTIAALLSPYSYSTTAVVSN 121
Transthyretin pfam00576
HIUase/Transthyretin family; This family includes transthyretin that is a thyroid ...
 39-141 1.42e-27

HIUase/Transthyretin family; This family includes transthyretin that is a thyroid hormone-binding protein that transports thyroxine from the bloodstream to the brain. However, most of the sequences listed in this family do not bind thyroid hormones. They are actually enzymes of the purine catabolism that catalyze the conversion of 5-hydroxyisourate (HIU) to OHCU. HIU hydrolysis is the original function of the family and is conserved from bacteria to mammals; transthyretins arose by gene duplications in the vertebrate lineage. HIUases are distinguished in the alignment from the conserved C-terminal YRGS sequence.


Pssm-ID: 459857  Cd Length: 108  Bit Score: 98.67  E-value: 1.42e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915183     39 VLDAVRGSPAANVAIKVFKkTSDGDWQEFAAGKTTEFGEVHELT-SDEKFVEGIYRVEFDTSSYWKALGLSPFHEYADVV 117
Cdd:pfam00576   5 VLDTARGRPAAGVRVTLYR-LDGDGWTLLAEGTTNADGRCDDLLlEGEALEPGTYRLVFDTGAYFAARGVESFYPEVEVR 83

                          90       100
                  ....*....|....*....|....
gi 3915183    118 FTANDSGHRHytIAALLSPFSYST 141
Cdd:pfam00576  84 FGITDAEHYH--VPLLLSPFGYST 105
hdxy_isourate TIGR02962
hydroxyisourate hydrolase; Members of this family, hydroxyisourate hydrolase, represent a ...
 34-141 8.53e-27

hydroxyisourate hydrolase; Members of this family, hydroxyisourate hydrolase, represent a distinct clade of transthyretin-related proteins. Bacterial members typically are encoded next to ureidoglycolate hydrolase and often near either xanthine dehydrogenase or xanthine/uracil permease genes and have been demonstrated to have hydroxyisourate hydrolase activity. In eukaryotes, a clade separate from the transthyretins (a family of thyroid-hormone binding proteins) has also been shown to have HIU hydrolase activity in urate catabolizing organisms. Transthyretin, then, would appear to be the recently diverged paralog of the more ancient HIUH family. [Purines, pyrimidines, nucleosides, and nucleotides, Other]


Pssm-ID: 274364  Cd Length: 112  Bit Score: 96.85  E-value: 8.53e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915183     34 PLMVKVLDAVRGSPAANVAIKVFKKTSDGdWQEFAAGKTTEFGEVHE-LTSDEKFVEGIYRVEFDTSSYWKALGLSPFHE 112
Cdd:TIGR02962   2 PLSTHVLDTTSGKPAAGVPVTLYRLDGGG-WTPLATGVTNADGRCDGpLPEGEDLAPGIYKLRFDTGDYFAARGVESFYP 80

                          90       100
                  ....*....|....*....|....*....
gi 3915183    113 YADVVFTANDSGhRHYTIAALLSPFSYST 141
Cdd:TIGR02962  81 EVEVVFTIADPG-QHYHVPLLLSPYGYST 108
HiuH COG2351
5-hydroxyisourate hydrolase (purine catabolism), transthyretin-related family [Nucleotide ...
 39-141 1.71e-26

5-hydroxyisourate hydrolase (purine catabolism), transthyretin-related family [Nucleotide transport and metabolism];


Pssm-ID: 441918  Cd Length: 111  Bit Score: 95.98  E-value: 1.71e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915183   39 VLDAVRGSPAANVAIKVFKKTSDGdWQEFAAGKTTEFGEVHELTsDEKFVEGIYRVEFDTSSYWKALGLSPFHEYADVVF 118
Cdd:COG2351   8 VLDTARGRPAAGVRVELYRLDGDG-WTLLAEGVTNADGRIDALG-GEALAAGTYRLVFDTGDYFAARGVPPFLPEVPVRF 85

                        90       100
                ....*....|....*....|...
gi 3915183  119 TANDSGhRHYTIAALLSPFSYST 141
Cdd:COG2351  86 GIADPE-EHYHVPLLLSPWGYST 107
PRK15036 PRK15036
hydroxyisourate hydrolase; Provisional
 35-141 3.83e-15

hydroxyisourate hydrolase; Provisional


Pssm-ID: 184996  Cd Length: 137  Bit Score: 67.70  E-value: 3.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915183    35 LMVKVLDAVRGSPAANVAIkVFKKTSDGDWQEFAAGKTTEFGEVHELTSDEKFVEGIYRVEFDTSSYWKALGLSPFHEYA 114
Cdd:PRK15036  29 LSVHILNQQTGKPAADVTV-TLEKKADNGWLQLNTAKTDKDGRIKALWPEQTATTGDYRVVFKTGDYFKKQNLESFFPEI 107

                         90       100
                 ....*....|....*....|....*..
gi 3915183   115 DVVFTANDSgHRHYTIAALLSPFSYST 141
Cdd:PRK15036 108 PVEFHINKV-NEHYHVPLLLSQYGYST 133
 
Name Accession Description Interval E-value
TR_THY smart00095
Transthyretin;
30-150 1.97e-83

Transthyretin;


Pssm-ID: 128406  Cd Length: 121  Bit Score: 240.56  E-value: 1.97e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915183      30 DSKCPLMVKVLDAVRGSPAANVAIKVFKKTSDGDWQEFAAGKTTEFGEVHELTSDEKFVEGIYRVEFDTSSYWKALGLSP 109
Cdd:smart00095   1 DSKCPLMVKVLDAVRGSPAVNVAVKVFKKTEEGTWEPFASGKTNESGEIHELTTDEKFVEGLYKVEFDTKSYWKALGISP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 3915183     110 FHEYADVVFTANDSGHRHYTIAALLSPFSYSTTAVVSDPQE 150
Cdd:smart00095  81 FHEYADVVFTANDSGHRHYTIAALLSPYSYSTTAVVSNPKE 121
TLP_Transthyretin cd05821
Transthyretin (TTR) is a 55 kDa protein responsible for the transport of thyroid hormones and ...
 27-147 1.36e-80

Transthyretin (TTR) is a 55 kDa protein responsible for the transport of thyroid hormones and retinol in vertebrates. TTR distributes the two thyroid hormones T3 (3,5,3'-triiodo-L-thyronine) and T4 (Thyroxin, or 3,5,3',5'-tetraiodo-L-thyronine), as well as retinol (vitamin A) through the formation of a macromolecular complex that includes each of these as well as retinol-binding protein. Misfolded forms of TTR are implicated in the amyloid diseases familial amyloidotic polyneuropathy and senile systemic amyloidosis. TTR forms a homotetramer with each subunit consisting of eight beta-strands arranged in two sheets and a short alpha-helix. The central channel of the tetramer contains two independent binding sites, each located between a pair of subunits, which differ in their ligand binding affinity. A negative cooperativity has been observed for the binding of T4 and other TTR ligands. A fraction of plasma TTR is carried in high density lipoproteins by binding to apolipoprotein AI (apoA-I). TTR is able to proteolytically process apoA-I by cleaving its C-terminus; therefore TTR has protease activity in addition to its function in protein transport.


Pssm-ID: 100113  Cd Length: 121  Bit Score: 233.21  E-value: 1.36e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915183   27 GSIDSKCPLMVKVLDAVRGSPAANVAIKVFKKTSDGDWQEFAAGKTTEFGEVHELTSDEKFVEGIYRVEFDTSSYWKALG 106
Cdd:cd05821   1 GGGDSKCPLMVKVLDAVRGSPAANVAVKVFKKTADGSWEPFASGKTTETGEIHGLTTDEQFTEGVYKVEFDTKAYWKKLG 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 3915183  107 LSPFHEYADVVFTANDSGHRHYTIAALLSPFSYSTTAVVSD 147
Cdd:cd05821  81 ISPFHEYAEVVFTANDSGHRHYTIAALLSPYSYSTTAVVSN 121
Transthyretin_like cd05469
Transthyretin_like. This domain is present in the transthyretin-like protein (TLP) family ...
 33-145 2.31e-63

Transthyretin_like. This domain is present in the transthyretin-like protein (TLP) family which includes transthyretin (TTR) and a transthyretin-related protein called 5-hydroxyisourate hydrolase (HIUase). TTR and HIUase are homotetrameric proteins with each subunit consisting of eight beta-strands arranged in two sheets and a short alpha-helix. The central channel of the tetramer contains two independent binding sites, each located between a pair of subunits. TTR transports thyroid hormones and retinol in the blood serum of vertebrates while HIUase catalyzes the second step in a three-step ureide pathway. TTRs are highly conserved and found only in vertebrates while the HIUases are found in a wide range of bacterial, plant, fungal, slime mold and vertebrate organisms.


Pssm-ID: 100112  Cd Length: 113  Bit Score: 189.67  E-value: 2.31e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915183   33 CPLMVKVLDAVRGSPAANVAIKVFKKTSDGDWQEFAAGKTTEFGEVHELTSDEKFVEGIYRVEFDTSSYWKALGLSPFHE 112
Cdd:cd05469   1 CPLMVKVLDAVRGSPAANVAIKVFRKTADGSWEIFATGKTNEDGELHGLITEEEF*AGVYRVEFDTKSYWKALGITPFHE 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 3915183  113 YADVVFTANDSGHRHYTIAALLSPFSYSTTAVV 145
Cdd:cd05469  81 YAEVVFTANDSGHRHYTIALLLSPFSYSTTAVV 113
Transthyretin pfam00576
HIUase/Transthyretin family; This family includes transthyretin that is a thyroid ...
 39-141 1.42e-27

HIUase/Transthyretin family; This family includes transthyretin that is a thyroid hormone-binding protein that transports thyroxine from the bloodstream to the brain. However, most of the sequences listed in this family do not bind thyroid hormones. They are actually enzymes of the purine catabolism that catalyze the conversion of 5-hydroxyisourate (HIU) to OHCU. HIU hydrolysis is the original function of the family and is conserved from bacteria to mammals; transthyretins arose by gene duplications in the vertebrate lineage. HIUases are distinguished in the alignment from the conserved C-terminal YRGS sequence.


Pssm-ID: 459857  Cd Length: 108  Bit Score: 98.67  E-value: 1.42e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915183     39 VLDAVRGSPAANVAIKVFKkTSDGDWQEFAAGKTTEFGEVHELT-SDEKFVEGIYRVEFDTSSYWKALGLSPFHEYADVV 117
Cdd:pfam00576   5 VLDTARGRPAAGVRVTLYR-LDGDGWTLLAEGTTNADGRCDDLLlEGEALEPGTYRLVFDTGAYFAARGVESFYPEVEVR 83

                          90       100
                  ....*....|....*....|....
gi 3915183    118 FTANDSGHRHytIAALLSPFSYST 141
Cdd:pfam00576  84 FGITDAEHYH--VPLLLSPFGYST 105
hdxy_isourate TIGR02962
hydroxyisourate hydrolase; Members of this family, hydroxyisourate hydrolase, represent a ...
 34-141 8.53e-27

hydroxyisourate hydrolase; Members of this family, hydroxyisourate hydrolase, represent a distinct clade of transthyretin-related proteins. Bacterial members typically are encoded next to ureidoglycolate hydrolase and often near either xanthine dehydrogenase or xanthine/uracil permease genes and have been demonstrated to have hydroxyisourate hydrolase activity. In eukaryotes, a clade separate from the transthyretins (a family of thyroid-hormone binding proteins) has also been shown to have HIU hydrolase activity in urate catabolizing organisms. Transthyretin, then, would appear to be the recently diverged paralog of the more ancient HIUH family. [Purines, pyrimidines, nucleosides, and nucleotides, Other]


Pssm-ID: 274364  Cd Length: 112  Bit Score: 96.85  E-value: 8.53e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915183     34 PLMVKVLDAVRGSPAANVAIKVFKKTSDGdWQEFAAGKTTEFGEVHE-LTSDEKFVEGIYRVEFDTSSYWKALGLSPFHE 112
Cdd:TIGR02962   2 PLSTHVLDTTSGKPAAGVPVTLYRLDGGG-WTPLATGVTNADGRCDGpLPEGEDLAPGIYKLRFDTGDYFAARGVESFYP 80

                          90       100
                  ....*....|....*....|....*....
gi 3915183    113 YADVVFTANDSGhRHYTIAALLSPFSYST 141
Cdd:TIGR02962  81 EVEVVFTIADPG-QHYHVPLLLSPYGYST 108
HiuH COG2351
5-hydroxyisourate hydrolase (purine catabolism), transthyretin-related family [Nucleotide ...
 39-141 1.71e-26

5-hydroxyisourate hydrolase (purine catabolism), transthyretin-related family [Nucleotide transport and metabolism];


Pssm-ID: 441918  Cd Length: 111  Bit Score: 95.98  E-value: 1.71e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915183   39 VLDAVRGSPAANVAIKVFKKTSDGdWQEFAAGKTTEFGEVHELTsDEKFVEGIYRVEFDTSSYWKALGLSPFHEYADVVF 118
Cdd:COG2351   8 VLDTARGRPAAGVRVELYRLDGDG-WTLLAEGVTNADGRIDALG-GEALAAGTYRLVFDTGDYFAARGVPPFLPEVPVRF 85

                        90       100
                ....*....|....*....|...
gi 3915183  119 TANDSGhRHYTIAALLSPFSYST 141
Cdd:COG2351  86 GIADPE-EHYHVPLLLSPWGYST 107
TLP_HIUase cd05822
HIUase (5-hydroxyisourate hydrolase) catalyzes the second step in a three-step ureide pathway ...
 34-141 2.83e-26

HIUase (5-hydroxyisourate hydrolase) catalyzes the second step in a three-step ureide pathway in which 5-hydroxyisourate (HIU), a product of the uricase (urate oxidase) reaction, is hydrolyzed to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU). HIUase has high sequence similarity with transthyretins and is a member of the transthyretin-like protein (TLP) family. HIUase is distinguished from transthyretins by a conserved signature motif at its C-terminus that forms part of the active site. In HIUase, this motif is YRGS, while transthyretins have a conserved TAVV sequence in the same location. Most HIUases are cytosolic but in plants and slime molds, they are peroxisomal based on the presence of N-terminal periplasmic localization sequences. HIUase forms a homotetramer with each subunit consisting of eight beta-strands arranged in two sheets and a short alpha-helix. The central channel of the tetramer contains two independent binding sites, each located between a pair of subunits.


Pssm-ID: 100114  Cd Length: 112  Bit Score: 95.30  E-value: 2.83e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915183   34 PLMVKVLDAVRGSPAANVAIKVFKKTSDGdWQEFAAGKTTEFGEVHELTSD-EKFVEGIYRVEFDTSSYWKALGLSPFHE 112
Cdd:cd05822   2 PLSTHVLDTATGKPAAGVAVTLYRLDGNG-WTLLATGVTNADGRCDDLLPPgAQLAAGTYKLTFDTGAYFAARGQESFYP 80

                        90       100
                ....*....|....*....|....*....
gi 3915183  113 YADVVFTANDSGhRHYTIAALLSPFSYST 141
Cdd:cd05822  81 EVEVRFTITDPT-EHYHVPLLLSPFGYST 108
PRK15036 PRK15036
hydroxyisourate hydrolase; Provisional
 35-141 3.83e-15

hydroxyisourate hydrolase; Provisional


Pssm-ID: 184996  Cd Length: 137  Bit Score: 67.70  E-value: 3.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3915183    35 LMVKVLDAVRGSPAANVAIkVFKKTSDGDWQEFAAGKTTEFGEVHELTSDEKFVEGIYRVEFDTSSYWKALGLSPFHEYA 114
Cdd:PRK15036  29 LSVHILNQQTGKPAADVTV-TLEKKADNGWLQLNTAKTDKDGRIKALWPEQTATTGDYRVVFKTGDYFKKQNLESFFPEI 107

                         90       100
                 ....*....|....*....|....*..
gi 3915183   115 DVVFTANDSgHRHYTIAALLSPFSYST 141
Cdd:PRK15036 108 PVEFHINKV-NEHYHVPLLLSQYGYST 133
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH