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Conserved domains on  [gi|47523508|ref|NP_999377|]
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transthyretin precursor [Sus scrofa]

Protein Classification

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

peptidase associated/transthyretin-like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TR_THY smart00095
Transthyretin;
27-147 7.72e-86

Transthyretin;


:

Pssm-ID: 128406  Cd Length: 121  Bit Score: 246.72  E-value: 7.72e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47523508     27 ESKCPLMVKVLDAVRGSPAVNVGVKVFKKAADGTWEPFALGKTSEFGELHGLTTDEKFVEGIYKVELDTKSYWKALGISP 106
Cdd:smart00095   1 DSKCPLMVKVLDAVRGSPAVNVAVKVFKKTEEGTWEPFASGKTNESGEIHELTTDEKFVEGLYKVEFDTKSYWKALGISP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 47523508    107 FHEYAEVVFTANDSGRRHYTIAALLSPYSYSTTALVSSPKE 147
Cdd:smart00095  81 FHEYADVVFTANDSGHRHYTIAALLSPYSYSTTAVVSNPKE 121
 
Name Accession Description Interval E-value
TR_THY smart00095
Transthyretin;
27-147 7.72e-86

Transthyretin;


Pssm-ID: 128406  Cd Length: 121  Bit Score: 246.72  E-value: 7.72e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47523508     27 ESKCPLMVKVLDAVRGSPAVNVGVKVFKKAADGTWEPFALGKTSEFGELHGLTTDEKFVEGIYKVELDTKSYWKALGISP 106
Cdd:smart00095   1 DSKCPLMVKVLDAVRGSPAVNVAVKVFKKTEEGTWEPFASGKTNESGEIHELTTDEKFVEGLYKVEFDTKSYWKALGISP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 47523508    107 FHEYAEVVFTANDSGRRHYTIAALLSPYSYSTTALVSSPKE 147
Cdd:smart00095  81 FHEYADVVFTANDSGHRHYTIAALLSPYSYSTTAVVSNPKE 121
TLP_Transthyretin cd05821
Transthyretin (TTR) is a 55 kDa protein responsible for the transport of thyroid hormones and ...
 24-144 4.49e-79

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: 229.74  E-value: 4.49e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47523508  24 GAGESKCPLMVKVLDAVRGSPAVNVGVKVFKKAADGTWEPFALGKTSEFGELHGLTTDEKFVEGIYKVELDTKSYWKALG 103
Cdd:cd05821   1 GGGDSKCPLMVKVLDAVRGSPAANVAVKVFKKTADGSWEPFASGKTTETGEIHGLTTDEQFTEGVYKVEFDTKAYWKKLG 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 47523508 104 ISPFHEYAEVVFTANDSGRRHYTIAALLSPYSYSTTALVSS 144
Cdd:cd05821  81 ISPFHEYAEVVFTANDSGHRHYTIAALLSPYSYSTTAVVSN 121
hdxy_isourate TIGR02962
hydroxyisourate hydrolase; Members of this family, hydroxyisourate hydrolase, represent a ...
 31-138 2.08e-25

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: 93.00  E-value: 2.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47523508    31 PLMVKVLDAVRGSPAVNVGVKVFKKAADGtWEPFALGKTSEFGELHG-LTTDEKFVEGIYKVELDTKSYWKALGISPFHE 109
Cdd:TIGR02962   2 PLSTHVLDTTSGKPAAGVPVTLYRLDGGG-WTPLATGVTNADGRCDGpLPEGEDLAPGIYKLRFDTGDYFAARGVESFYP 80

                          90       100
                  ....*....|....*....|....*....
gi 47523508   110 YAEVVFTANDSGRrHYTIAALLSPYSYST 138
Cdd:TIGR02962  81 EVEVVFTIADPGQ-HYHVPLLLSPYGYST 108
Transthyretin pfam00576
HIUase/Transthyretin family; This family includes transthyretin that is a thyroid ...
 36-138 3.75e-25

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: 92.51  E-value: 3.75e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47523508    36 VLDAVRGSPAVNVGVKVFKkAADGTWEPFALGKTSEFGELHGLT-TDEKFVEGIYKVELDTKSYWKALGISPFHEYAEVV 114
Cdd:pfam00576   5 VLDTARGRPAAGVRVTLYR-LDGDGWTLLAEGTTNADGRCDDLLlEGEALEPGTYRLVFDTGAYFAARGVESFYPEVEVR 83

                          90       100
                  ....*....|....*....|....
gi 47523508   115 FTANDSgrRHYTIAALLSPYSYST 138
Cdd:pfam00576  84 FGITDA--EHYHVPLLLSPFGYST 105
HiuH COG2351
5-hydroxyisourate hydrolase (purine catabolism), transthyretin-related family [Nucleotide ...
 36-138 1.88e-23

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


Pssm-ID: 441918  Cd Length: 111  Bit Score: 88.27  E-value: 1.88e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47523508  36 VLDAVRGSPAVNVGVKVFKkAADGTWEPFALGKTSEFGELHGLTtDEKFVEGIYKVELDTKSYWKALGISPFHEYAEVVF 115
Cdd:COG2351   8 VLDTARGRPAAGVRVELYR-LDGDGWTLLAEGVTNADGRIDALG-GEALAAGTYRLVFDTGDYFAARGVPPFLPEVPVRF 85

                        90       100
                ....*....|....*....|...
gi 47523508 116 TANDSGRrHYTIAALLSPYSYST 138
Cdd:COG2351  86 GIADPEE-HYHVPLLLSPWGYST 107
PRK15036 PRK15036
hydroxyisourate hydrolase; Provisional
 32-138 8.93e-13

hydroxyisourate hydrolase; Provisional


Pssm-ID: 184996  Cd Length: 137  Bit Score: 61.54  E-value: 8.93e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47523508   32 LMVKVLDAVRGSPAVNVGVkVFKKAADGTWEPFALGKTSEFGELHGLTTDEKFVEGIYKVELDTKSYWKALGISPFHEYA 111
Cdd:PRK15036  29 LSVHILNQQTGKPAADVTV-TLEKKADNGWLQLNTAKTDKDGRIKALWPEQTATTGDYRVVFKTGDYFKKQNLESFFPEI 107

                         90       100
                 ....*....|....*....|....*..
gi 47523508  112 EVVFTANDSgRRHYTIAALLSPYSYST 138
Cdd:PRK15036 108 PVEFHINKV-NEHYHVPLLLSQYGYST 133
 
Name Accession Description Interval E-value
TR_THY smart00095
Transthyretin;
27-147 7.72e-86

Transthyretin;


Pssm-ID: 128406  Cd Length: 121  Bit Score: 246.72  E-value: 7.72e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47523508     27 ESKCPLMVKVLDAVRGSPAVNVGVKVFKKAADGTWEPFALGKTSEFGELHGLTTDEKFVEGIYKVELDTKSYWKALGISP 106
Cdd:smart00095   1 DSKCPLMVKVLDAVRGSPAVNVAVKVFKKTEEGTWEPFASGKTNESGEIHELTTDEKFVEGLYKVEFDTKSYWKALGISP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 47523508    107 FHEYAEVVFTANDSGRRHYTIAALLSPYSYSTTALVSSPKE 147
Cdd:smart00095  81 FHEYADVVFTANDSGHRHYTIAALLSPYSYSTTAVVSNPKE 121
TLP_Transthyretin cd05821
Transthyretin (TTR) is a 55 kDa protein responsible for the transport of thyroid hormones and ...
 24-144 4.49e-79

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: 229.74  E-value: 4.49e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47523508  24 GAGESKCPLMVKVLDAVRGSPAVNVGVKVFKKAADGTWEPFALGKTSEFGELHGLTTDEKFVEGIYKVELDTKSYWKALG 103
Cdd:cd05821   1 GGGDSKCPLMVKVLDAVRGSPAANVAVKVFKKTADGSWEPFASGKTTETGEIHGLTTDEQFTEGVYKVEFDTKAYWKKLG 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 47523508 104 ISPFHEYAEVVFTANDSGRRHYTIAALLSPYSYSTTALVSS 144
Cdd:cd05821  81 ISPFHEYAEVVFTANDSGHRHYTIAALLSPYSYSTTAVVSN 121
Transthyretin_like cd05469
Transthyretin_like. This domain is present in the transthyretin-like protein (TLP) family ...
 30-142 3.47e-65

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: 194.29  E-value: 3.47e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47523508  30 CPLMVKVLDAVRGSPAVNVGVKVFKKAADGTWEPFALGKTSEFGELHGLTTDEKFVEGIYKVELDTKSYWKALGISPFHE 109
Cdd:cd05469   1 CPLMVKVLDAVRGSPAANVAIKVFRKTADGSWEIFATGKTNEDGELHGLITEEEF*AGVYRVEFDTKSYWKALGITPFHE 80

                        90       100       110
                ....*....|....*....|....*....|...
gi 47523508 110 YAEVVFTANDSGRRHYTIAALLSPYSYSTTALV 142
Cdd:cd05469  81 YAEVVFTANDSGHRHYTIALLLSPFSYSTTAVV 113
hdxy_isourate TIGR02962
hydroxyisourate hydrolase; Members of this family, hydroxyisourate hydrolase, represent a ...
 31-138 2.08e-25

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: 93.00  E-value: 2.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47523508    31 PLMVKVLDAVRGSPAVNVGVKVFKKAADGtWEPFALGKTSEFGELHG-LTTDEKFVEGIYKVELDTKSYWKALGISPFHE 109
Cdd:TIGR02962   2 PLSTHVLDTTSGKPAAGVPVTLYRLDGGG-WTPLATGVTNADGRCDGpLPEGEDLAPGIYKLRFDTGDYFAARGVESFYP 80

                          90       100
                  ....*....|....*....|....*....
gi 47523508   110 YAEVVFTANDSGRrHYTIAALLSPYSYST 138
Cdd:TIGR02962  81 EVEVVFTIADPGQ-HYHVPLLLSPYGYST 108
Transthyretin pfam00576
HIUase/Transthyretin family; This family includes transthyretin that is a thyroid ...
 36-138 3.75e-25

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: 92.51  E-value: 3.75e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47523508    36 VLDAVRGSPAVNVGVKVFKkAADGTWEPFALGKTSEFGELHGLT-TDEKFVEGIYKVELDTKSYWKALGISPFHEYAEVV 114
Cdd:pfam00576   5 VLDTARGRPAAGVRVTLYR-LDGDGWTLLAEGTTNADGRCDDLLlEGEALEPGTYRLVFDTGAYFAARGVESFYPEVEVR 83

                          90       100
                  ....*....|....*....|....
gi 47523508   115 FTANDSgrRHYTIAALLSPYSYST 138
Cdd:pfam00576  84 FGITDA--EHYHVPLLLSPFGYST 105
HiuH COG2351
5-hydroxyisourate hydrolase (purine catabolism), transthyretin-related family [Nucleotide ...
 36-138 1.88e-23

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


Pssm-ID: 441918  Cd Length: 111  Bit Score: 88.27  E-value: 1.88e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47523508  36 VLDAVRGSPAVNVGVKVFKkAADGTWEPFALGKTSEFGELHGLTtDEKFVEGIYKVELDTKSYWKALGISPFHEYAEVVF 115
Cdd:COG2351   8 VLDTARGRPAAGVRVELYR-LDGDGWTLLAEGVTNADGRIDALG-GEALAAGTYRLVFDTGDYFAARGVPPFLPEVPVRF 85

                        90       100
                ....*....|....*....|...
gi 47523508 116 TANDSGRrHYTIAALLSPYSYST 138
Cdd:COG2351  86 GIADPEE-HYHVPLLLSPWGYST 107
TLP_HIUase cd05822
HIUase (5-hydroxyisourate hydrolase) catalyzes the second step in a three-step ureide pathway ...
 31-138 2.58e-23

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: 87.98  E-value: 2.58e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47523508  31 PLMVKVLDAVRGSPAVNVGVKVFKKAADGtWEPFALGKTSEFGEL-HGLTTDEKFVEGIYKVELDTKSYWKALGISPFHE 109
Cdd:cd05822   2 PLSTHVLDTATGKPAAGVAVTLYRLDGNG-WTLLATGVTNADGRCdDLLPPGAQLAAGTYKLTFDTGAYFAARGQESFYP 80

                        90       100
                ....*....|....*....|....*....
gi 47523508 110 YAEVVFTANDSGrRHYTIAALLSPYSYST 138
Cdd:cd05822  81 EVEVRFTITDPT-EHYHVPLLLSPFGYST 108
PRK15036 PRK15036
hydroxyisourate hydrolase; Provisional
 32-138 8.93e-13

hydroxyisourate hydrolase; Provisional


Pssm-ID: 184996  Cd Length: 137  Bit Score: 61.54  E-value: 8.93e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47523508   32 LMVKVLDAVRGSPAVNVGVkVFKKAADGTWEPFALGKTSEFGELHGLTTDEKFVEGIYKVELDTKSYWKALGISPFHEYA 111
Cdd:PRK15036  29 LSVHILNQQTGKPAADVTV-TLEKKADNGWLQLNTAKTDKDGRIKALWPEQTATTGDYRVVFKTGDYFKKQNLESFFPEI 107

                         90       100
                 ....*....|....*....|....*..
gi 47523508  112 EVVFTANDSgRRHYTIAALLSPYSYST 138
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.
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