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Conserved domains on  [gi|1002252607|ref|XP_015630533|]
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uric acid degradation bifunctional protein TTL isoform X1 [Oryza sativa Japonica Group]

Protein Classification

2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase( domain architecture ID 11182740)

2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase catalyzes the decarboxylation of 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU) into S(+)-allantoin, the third step of the conversion of uric acid (a purine derivative) to allantoin

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Transthyretin pfam00576
HIUase/Transthyretin family; This family includes transthyretin that is a thyroid ...
 215-333 6.06e-44

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: 146.44  E-value: 6.06e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252607 215 ITTHVLDVARGSPASGIEVHLEMWKDastppsfnnkdfNGWATLGSSVTNNDGRSGQLMDIVNNVAPGFYRISFNTSKY- 293
Cdd:pfam00576   1 LTTHVLDTARGRPAAGVRVTLYRLDG------------DGWTLLAEGTTNADGRCDDLLLEGEALEPGTYRLVFDTGAYf 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1002252607 294 ----APSgFFPYVSIIFEIKKNQtteHFHVPLLHSPFSFTTYRG 333
Cdd:pfam00576  69 aargVES-FYPEVEVRFGITDAE---HYHVPLLLSPFGYSTYRG 108
PucL super family cl43809
2-oxo-4-hydroxy-4-carboxy--5-ureidoimidazoline (OHCU) decarboxylase (uric acid degradation) ...
 55-159 1.41e-32

2-oxo-4-hydroxy-4-carboxy--5-ureidoimidazoline (OHCU) decarboxylase (uric acid degradation) [Nucleotide transport and metabolism];


The actual alignment was detected with superfamily member COG3195:

Pssm-ID: 442428 [Multi-domain]  Cd Length: 169  Bit Score: 119.11  E-value: 1.41e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252607  55 WLEAFAAHPAIG--------TTSSSApkwcKEEQSAALATATDSTAQELADWNARYREKFGFVFMICASGRTAPEVLAEL 126
Cdd:COG3195    61 QLALLRAHPDLGgkaagagrLTAEST----SEQAGAGLDDLTDEERARLAALNAAYEARFGFPFIIAVRGRSKAEILAAL 136

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1002252607 127 KRRYENRPIVELEIAAQEELKITELRLAKLFAS 159
Cdd:COG3195   137 ERRLANDPETEFAEALAQIRRIARLRLEDLLAA 169
 
Name Accession Description Interval E-value
Transthyretin pfam00576
HIUase/Transthyretin family; This family includes transthyretin that is a thyroid ...
 215-333 6.06e-44

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: 146.44  E-value: 6.06e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252607 215 ITTHVLDVARGSPASGIEVHLEMWKDastppsfnnkdfNGWATLGSSVTNNDGRSGQLMDIVNNVAPGFYRISFNTSKY- 293
Cdd:pfam00576   1 LTTHVLDTARGRPAAGVRVTLYRLDG------------DGWTLLAEGTTNADGRCDDLLLEGEALEPGTYRLVFDTGAYf 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1002252607 294 ----APSgFFPYVSIIFEIKKNQtteHFHVPLLHSPFSFTTYRG 333
Cdd:pfam00576  69 aargVES-FYPEVEVRFGITDAE---HYHVPLLLSPFGYSTYRG 108
TLP_HIUase cd05822
HIUase (5-hydroxyisourate hydrolase) catalyzes the second step in a three-step ureide pathway ...
 213-334 4.25e-41

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: 139.21  E-value: 4.25e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252607 213 PPITTHVLDVARGSPASGIEVHLEMWKDastppsfnnkdfNGWATLGSSVTNNDGRSGQLMDIVNNVAPGFYRISFNTSK 292
Cdd:cd05822     1 GPLSTHVLDTATGKPAAGVAVTLYRLDG------------NGWTLLATGVTNADGRCDDLLPPGAQLAAGTYKLTFDTGA 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1002252607 293 Y----APSGFFPYVSIIFEIKKnqTTEHFHVPLLHSPFSFTTYRGS 334
Cdd:cd05822    69 YfaarGQESFYPEVEVRFTITD--PTEHYHVPLLLSPFGYSTYRGS 112
hdxy_isourate TIGR02962
hydroxyisourate hydrolase; Members of this family, hydroxyisourate hydrolase, represent a ...
 213-334 1.18e-36

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: 127.66  E-value: 1.18e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252607 213 PPITTHVLDVARGSPASGIEVHLEmwkdastppsfnNKDFNGWATLGSSVTNNDGRSGQLMDIVNNVAPGFYRISFNTSK 292
Cdd:TIGR02962   1 SPLSTHVLDTTSGKPAAGVPVTLY------------RLDGGGWTPLATGVTNADGRCDGPLPEGEDLAPGIYKLRFDTGD 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1002252607 293 Y----APSGFFPYVSIIFEIKknQTTEHFHVPLLHSPFSFTTYRGS 334
Cdd:TIGR02962  69 YfaarGVESFYPEVEVVFTIA--DPGQHYHVPLLLSPYGYSTYRGS 112
HiuH COG2351
5-hydroxyisourate hydrolase (purine catabolism), transthyretin-related family [Nucleotide ...
 214-334 2.65e-34

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


Pssm-ID: 441918  Cd Length: 111  Bit Score: 121.40  E-value: 2.65e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252607 214 PITTHVLDVARGSPASGIEVHLEmwkdastppsfnNKDFNGWATLGSSVTNNDGRSGQLMDivNNVAPGFYRISFNTSKY 293
Cdd:COG2351     3 RLSTHVLDTARGRPAAGVRVELY------------RLDGDGWTLLAEGVTNADGRIDALGG--EALAAGTYRLVFDTGDY 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1002252607 294 -APSG---FFPYVSIIFEIKknQTTEHFHVPLLHSPFSFTTYRGS 334
Cdd:COG2351    69 fAARGvppFLPEVPVRFGIA--DPEEHYHVPLLLSPWGYSTYRGS 111
PucL COG3195
2-oxo-4-hydroxy-4-carboxy--5-ureidoimidazoline (OHCU) decarboxylase (uric acid degradation) ...
 55-159 1.41e-32

2-oxo-4-hydroxy-4-carboxy--5-ureidoimidazoline (OHCU) decarboxylase (uric acid degradation) [Nucleotide transport and metabolism];


Pssm-ID: 442428 [Multi-domain]  Cd Length: 169  Bit Score: 119.11  E-value: 1.41e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252607  55 WLEAFAAHPAIG--------TTSSSApkwcKEEQSAALATATDSTAQELADWNARYREKFGFVFMICASGRTAPEVLAEL 126
Cdd:COG3195    61 QLALLRAHPDLGgkaagagrLTAEST----SEQAGAGLDDLTDEERARLAALNAAYEARFGFPFIIAVRGRSKAEILAAL 136

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1002252607 127 KRRYENRPIVELEIAAQEELKITELRLAKLFAS 159
Cdd:COG3195   137 ERRLANDPETEFAEALAQIRRIARLRLEDLLAA 169
OHCU_decarbox pfam09349
OHCU decarboxylase; The proteins in this family are OHCU decarboxylase - enzymes of the purine ...
 55-154 9.02e-31

OHCU decarboxylase; The proteins in this family are OHCU decarboxylase - enzymes of the purine catabolism that catalyze the conversion of OHCU into S(+)-allantoin. This is the third step of the conversion of uric acid (a purine derivative) to allantoin. Step one is catalyzed by urate oxidase (pfam01014) and step two is catalyzed by HIUases (pfam00576).


Pssm-ID: 462765 [Multi-domain]  Cd Length: 156  Bit Score: 113.77  E-value: 9.02e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252607  55 WLEAFAAHPAIGTTSSSAPK---WCKEEQSAA-LATATDSTAQELADWNARYREKFGFVFMICASGRTAPEVLAELKRRY 130
Cdd:pfam09349  53 QLELLRAHPRLGGKAAAAGTlsaESAREQAGAgLDALDEEERARLAALNAAYEERFGFPFVVCVRGRSAREILAALERRL 132

                          90       100
                  ....*....|....*....|....
gi 1002252607 131 ENRPIVELEIAAQEELKITELRLA 154
Cdd:pfam09349 133 ANDPETERAEALEELAKIARLRLE 156
UraD_2 TIGR03180
OHCU decarboxylase; Previously thought to only proceed spontaneously, the decarboxylation of ...
 55-156 4.92e-27

OHCU decarboxylase; Previously thought to only proceed spontaneously, the decarboxylation of 2-oxo-4-hydroxy-4-carboxy--5-ureidoimidazoline (OHCU) has been recently been shown to be catalyzed by this enzyme in Mus musculus. Homologs of this enzyme are found adjacent to and fused with uricase in a number of prokaryotes and are represented by this model. This model is a separate (but related) clade from that represented by TIGR3164. This model places a second homolog in streptomyces species which (are not in the vicinity of other urate catabolism associated genes) below the trusted cutoff.


Pssm-ID: 188295 [Multi-domain]  Cd Length: 158  Bit Score: 104.08  E-value: 4.92e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252607  55 WLEAFAAHPAIGTTSSSAPKWCKE---EQsAALATATDSTAQELADWNARYREKFGFVFMICASGRTAPEVLAELKRRYE 131
Cdd:TIGR03180  54 LNEALAGHPRIGEKPAGQAAHAATsrrEQ-AGVDGADEETRAALLEGNAAYEEKFGRIFLIRAAGRSAEEMLDALQARLQ 132

                          90       100
                  ....*....|....*....|....*
gi 1002252607 132 NRPIVELEIAAQEELKITELRLAKL 156
Cdd:TIGR03180 133 NDPEEELRIAAEQLREITRLRLSRL 157
PRK13798 PRK13798
putative OHCU decarboxylase; Provisional
 55-160 4.28e-26

putative OHCU decarboxylase; Provisional


Pssm-ID: 184333 [Multi-domain]  Cd Length: 166  Bit Score: 101.96  E-value: 4.28e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252607  55 WLEAFAAHPAIGTTSSSAPKwcKEEQSAAlATATDSTAQELADWNARYREKFGFVFMICASGRTAPEVLAELKRRYENRP 134
Cdd:PRK13798   64 IDEALAGHPRIGERPASKAS--AREQAGV-ADADEAVMAALAAGNRAYEEKFGFVFLICATGRSADEMLAALQQRLHNDP 140

                          90       100
                  ....*....|....*....|....*.
gi 1002252607 135 IVELEIAAQEELKITELRLAKLFASE 160
Cdd:PRK13798  141 ETERKVVREELAKINRLRLERLLGPE 166
PRK15036 PRK15036
hydroxyisourate hydrolase; Provisional
 215-334 3.70e-23

hydroxyisourate hydrolase; Provisional


Pssm-ID: 184996  Cd Length: 137  Bit Score: 93.13  E-value: 3.70e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252607 215 ITTHVLDVARGSPASGIEVHLEMWKDastppsfnnkdfNGWATLGSSVTNNDGRSGQLMDiVNNVAPGFYRISFNTSKYA 294
Cdd:PRK15036   29 LSVHILNQQTGKPAADVTVTLEKKAD------------NGWLQLNTAKTDKDGRIKALWP-EQTATTGDYRVVFKTGDYF 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1002252607 295 PS----GFFPYVSIIFEIkkNQTTEHFHVPLLHSPFSFTTYRGS 334
Cdd:PRK15036   96 KKqnleSFFPEIPVEFHI--NKVNEHYHVPLLLSQYGYSTYRGS 137
TR_THY smart00095
Transthyretin;
214-330 6.27e-06

Transthyretin;


Pssm-ID: 128406  Cd Length: 121  Bit Score: 44.87  E-value: 6.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252607  214 PITTHVLDVARGSPASGIEVHLemwkdastppsFNNKDFNGWATLGSSVTNNdgrSGQLMDIVNN--VAPGFYRISFNTS 291
Cdd:smart00095   5 PLMVKVLDAVRGSPAVNVAVKV-----------FKKTEEGTWEPFASGKTNE---SGEIHELTTDekFVEGLYKVEFDTK 70

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1002252607  292 KY----APSGFFPYVSIIFEiKKNQTTEHFHVPLLHSPFSFTT 330
Cdd:smart00095  71 SYwkalGISPFHEYADVVFT-ANDSGHRHYTIAALLSPYSYST 112
 
Name Accession Description Interval E-value
Transthyretin pfam00576
HIUase/Transthyretin family; This family includes transthyretin that is a thyroid ...
 215-333 6.06e-44

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: 146.44  E-value: 6.06e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252607 215 ITTHVLDVARGSPASGIEVHLEMWKDastppsfnnkdfNGWATLGSSVTNNDGRSGQLMDIVNNVAPGFYRISFNTSKY- 293
Cdd:pfam00576   1 LTTHVLDTARGRPAAGVRVTLYRLDG------------DGWTLLAEGTTNADGRCDDLLLEGEALEPGTYRLVFDTGAYf 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1002252607 294 ----APSgFFPYVSIIFEIKKNQtteHFHVPLLHSPFSFTTYRG 333
Cdd:pfam00576  69 aargVES-FYPEVEVRFGITDAE---HYHVPLLLSPFGYSTYRG 108
TLP_HIUase cd05822
HIUase (5-hydroxyisourate hydrolase) catalyzes the second step in a three-step ureide pathway ...
 213-334 4.25e-41

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: 139.21  E-value: 4.25e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252607 213 PPITTHVLDVARGSPASGIEVHLEMWKDastppsfnnkdfNGWATLGSSVTNNDGRSGQLMDIVNNVAPGFYRISFNTSK 292
Cdd:cd05822     1 GPLSTHVLDTATGKPAAGVAVTLYRLDG------------NGWTLLATGVTNADGRCDDLLPPGAQLAAGTYKLTFDTGA 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1002252607 293 Y----APSGFFPYVSIIFEIKKnqTTEHFHVPLLHSPFSFTTYRGS 334
Cdd:cd05822    69 YfaarGQESFYPEVEVRFTITD--PTEHYHVPLLLSPFGYSTYRGS 112
hdxy_isourate TIGR02962
hydroxyisourate hydrolase; Members of this family, hydroxyisourate hydrolase, represent a ...
 213-334 1.18e-36

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: 127.66  E-value: 1.18e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252607 213 PPITTHVLDVARGSPASGIEVHLEmwkdastppsfnNKDFNGWATLGSSVTNNDGRSGQLMDIVNNVAPGFYRISFNTSK 292
Cdd:TIGR02962   1 SPLSTHVLDTTSGKPAAGVPVTLY------------RLDGGGWTPLATGVTNADGRCDGPLPEGEDLAPGIYKLRFDTGD 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1002252607 293 Y----APSGFFPYVSIIFEIKknQTTEHFHVPLLHSPFSFTTYRGS 334
Cdd:TIGR02962  69 YfaarGVESFYPEVEVVFTIA--DPGQHYHVPLLLSPYGYSTYRGS 112
HiuH COG2351
5-hydroxyisourate hydrolase (purine catabolism), transthyretin-related family [Nucleotide ...
 214-334 2.65e-34

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


Pssm-ID: 441918  Cd Length: 111  Bit Score: 121.40  E-value: 2.65e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252607 214 PITTHVLDVARGSPASGIEVHLEmwkdastppsfnNKDFNGWATLGSSVTNNDGRSGQLMDivNNVAPGFYRISFNTSKY 293
Cdd:COG2351     3 RLSTHVLDTARGRPAAGVRVELY------------RLDGDGWTLLAEGVTNADGRIDALGG--EALAAGTYRLVFDTGDY 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1002252607 294 -APSG---FFPYVSIIFEIKknQTTEHFHVPLLHSPFSFTTYRGS 334
Cdd:COG2351    69 fAARGvppFLPEVPVRFGIA--DPEEHYHVPLLLSPWGYSTYRGS 111
PucL COG3195
2-oxo-4-hydroxy-4-carboxy--5-ureidoimidazoline (OHCU) decarboxylase (uric acid degradation) ...
 55-159 1.41e-32

2-oxo-4-hydroxy-4-carboxy--5-ureidoimidazoline (OHCU) decarboxylase (uric acid degradation) [Nucleotide transport and metabolism];


Pssm-ID: 442428 [Multi-domain]  Cd Length: 169  Bit Score: 119.11  E-value: 1.41e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252607  55 WLEAFAAHPAIG--------TTSSSApkwcKEEQSAALATATDSTAQELADWNARYREKFGFVFMICASGRTAPEVLAEL 126
Cdd:COG3195    61 QLALLRAHPDLGgkaagagrLTAEST----SEQAGAGLDDLTDEERARLAALNAAYEARFGFPFIIAVRGRSKAEILAAL 136

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1002252607 127 KRRYENRPIVELEIAAQEELKITELRLAKLFAS 159
Cdd:COG3195   137 ERRLANDPETEFAEALAQIRRIARLRLEDLLAA 169
OHCU_decarbox pfam09349
OHCU decarboxylase; The proteins in this family are OHCU decarboxylase - enzymes of the purine ...
 55-154 9.02e-31

OHCU decarboxylase; The proteins in this family are OHCU decarboxylase - enzymes of the purine catabolism that catalyze the conversion of OHCU into S(+)-allantoin. This is the third step of the conversion of uric acid (a purine derivative) to allantoin. Step one is catalyzed by urate oxidase (pfam01014) and step two is catalyzed by HIUases (pfam00576).


Pssm-ID: 462765 [Multi-domain]  Cd Length: 156  Bit Score: 113.77  E-value: 9.02e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252607  55 WLEAFAAHPAIGTTSSSAPK---WCKEEQSAA-LATATDSTAQELADWNARYREKFGFVFMICASGRTAPEVLAELKRRY 130
Cdd:pfam09349  53 QLELLRAHPRLGGKAAAAGTlsaESAREQAGAgLDALDEEERARLAALNAAYEERFGFPFVVCVRGRSAREILAALERRL 132

                          90       100
                  ....*....|....*....|....
gi 1002252607 131 ENRPIVELEIAAQEELKITELRLA 154
Cdd:pfam09349 133 ANDPETERAEALEELAKIARLRLE 156
UraD_2 TIGR03180
OHCU decarboxylase; Previously thought to only proceed spontaneously, the decarboxylation of ...
 55-156 4.92e-27

OHCU decarboxylase; Previously thought to only proceed spontaneously, the decarboxylation of 2-oxo-4-hydroxy-4-carboxy--5-ureidoimidazoline (OHCU) has been recently been shown to be catalyzed by this enzyme in Mus musculus. Homologs of this enzyme are found adjacent to and fused with uricase in a number of prokaryotes and are represented by this model. This model is a separate (but related) clade from that represented by TIGR3164. This model places a second homolog in streptomyces species which (are not in the vicinity of other urate catabolism associated genes) below the trusted cutoff.


Pssm-ID: 188295 [Multi-domain]  Cd Length: 158  Bit Score: 104.08  E-value: 4.92e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252607  55 WLEAFAAHPAIGTTSSSAPKWCKE---EQsAALATATDSTAQELADWNARYREKFGFVFMICASGRTAPEVLAELKRRYE 131
Cdd:TIGR03180  54 LNEALAGHPRIGEKPAGQAAHAATsrrEQ-AGVDGADEETRAALLEGNAAYEEKFGRIFLIRAAGRSAEEMLDALQARLQ 132

                          90       100
                  ....*....|....*....|....*
gi 1002252607 132 NRPIVELEIAAQEELKITELRLAKL 156
Cdd:TIGR03180 133 NDPEEELRIAAEQLREITRLRLSRL 157
PRK13798 PRK13798
putative OHCU decarboxylase; Provisional
 55-160 4.28e-26

putative OHCU decarboxylase; Provisional


Pssm-ID: 184333 [Multi-domain]  Cd Length: 166  Bit Score: 101.96  E-value: 4.28e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252607  55 WLEAFAAHPAIGTTSSSAPKwcKEEQSAAlATATDSTAQELADWNARYREKFGFVFMICASGRTAPEVLAELKRRYENRP 134
Cdd:PRK13798   64 IDEALAGHPRIGERPASKAS--AREQAGV-ADADEAVMAALAAGNRAYEEKFGFVFLICATGRSADEMLAALQQRLHNDP 140

                          90       100
                  ....*....|....*....|....*.
gi 1002252607 135 IVELEIAAQEELKITELRLAKLFASE 160
Cdd:PRK13798  141 ETERKVVREELAKINRLRLERLLGPE 166
PRK15036 PRK15036
hydroxyisourate hydrolase; Provisional
 215-334 3.70e-23

hydroxyisourate hydrolase; Provisional


Pssm-ID: 184996  Cd Length: 137  Bit Score: 93.13  E-value: 3.70e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252607 215 ITTHVLDVARGSPASGIEVHLEMWKDastppsfnnkdfNGWATLGSSVTNNDGRSGQLMDiVNNVAPGFYRISFNTSKYA 294
Cdd:PRK15036   29 LSVHILNQQTGKPAADVTVTLEKKAD------------NGWLQLNTAKTDKDGRIKALWP-EQTATTGDYRVVFKTGDYF 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1002252607 295 PS----GFFPYVSIIFEIkkNQTTEHFHVPLLHSPFSFTTYRGS 334
Cdd:PRK15036   96 KKqnleSFFPEIPVEFHI--NKVNEHYHVPLLLSQYGYSTYRGS 137
PRK13797 PRK13797
allantoicase;
55-156 2.35e-22

allantoicase;


Pssm-ID: 106738 [Multi-domain]  Cd Length: 516  Bit Score: 97.35  E-value: 2.35e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252607  55 WLEAFAAHPAIGTTSSSAP-------------KWCKEEQsAALATATDSTAQELADWNARYREKFGFVFMICASGRTAPE 121
Cdd:PRK13797  399 WLEAFTAHPRIGERPTQAPapptsaratvvslDAPRREQ-AAMDQAAEDVRAAFARGNAAYEERFGFIFLVRAAGRGAEE 477

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1002252607 122 VLAELKRRYENRPIVELEIAAQEELKITELRLAKL 156
Cdd:PRK13797  478 MLELLRARLAHDPEQELRIAAGQQAEITALRLRHL 512
Transthyretin_like cd05469
Transthyretin_like. This domain is present in the transthyretin-like protein (TLP) family ...
 214-334 3.78e-21

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: 86.82  E-value: 3.78e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252607 214 PITTHVLDVARGSPASGIEVHLEMwKDAStppsfnnkdfNGWATLGSSVTNNDGRSGQLMdIVNNVAPGFYRISFNTSKY 293
Cdd:cd05469     2 PLMVKVLDAVRGSPAANVAIKVFR-KTAD----------GSWEIFATGKTNEDGELHGLI-TEEEF*AGVYRVEFDTKSY 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1002252607 294 ----APSGFFPYVSIIFEIKkNQTTEHFHVPLLHSPFSFTTYRGS 334
Cdd:cd05469    70 wkalGITPFHEYAEVVFTAN-DSGHRHYTIALLLSPFSYSTTAVV 113
UHCUDC TIGR03164
OHCU decarboxylase; Previously thought to only proceed spontaneously, the decarboxylation of ...
 61-156 2.12e-11

OHCU decarboxylase; Previously thought to only proceed spontaneously, the decarboxylation of 2-oxo-4-hydroxy-4-carboxy--5-ureidoimidazoline (OHCU) has been recently been shown to be catalyzed by this enzyme in Mus musculus. Homologs of this enzyme are found adjacent to and fused with uricase in a number of prokaryotes and are represented by this model.


Pssm-ID: 132208 [Multi-domain]  Cd Length: 157  Bit Score: 61.22  E-value: 2.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252607  61 AHPAIGT--------TSSSApkwcKEEQSAALATATDSTAQELADWNARYREKFGFVFMICASGRTAPEVLAELKRRYEN 132
Cdd:TIGR03164  58 AHPDLAGklavagelTAEST----SEQASAGLDQLSQEEFARFTRLNNAYRARFGFPFIMAVKGKTKQSILAAFEARLNN 133

                          90       100
                  ....*....|....*....|....
gi 1002252607 133 RPIVELEIAAQEELKITELRLAKL 156
Cdd:TIGR03164 134 DRETEFARALREIERIARFRLRDL 157
TLP_Transthyretin cd05821
Transthyretin (TTR) is a 55 kDa protein responsible for the transport of thyroid hormones and ...
 211-330 3.86e-09

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: 54.09  E-value: 3.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252607 211 TRPPITTHVLDVARGSPASGIEVHLemwkdastppsFNNKDFNGWATLGSSVTNNDGRSGQLMDIVNNVApGFYRISFNT 290
Cdd:cd05821     5 SKCPLMVKVLDAVRGSPAANVAVKV-----------FKKTADGSWEPFASGKTTETGEIHGLTTDEQFTE-GVYKVEFDT 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1002252607 291 SKY----APSGFFPYVSIIFEiKKNQTTEHFHVPLLHSPFSFTT 330
Cdd:cd05821    73 KAYwkklGISPFHEYAEVVFT-ANDSGHRHYTIAALLSPYSYST 115
PRK13590 PRK13590
putative bifunctional OHCU decarboxylase/allantoate amidohydrolase; Provisional
 47-162 1.52e-07

putative bifunctional OHCU decarboxylase/allantoate amidohydrolase; Provisional


Pssm-ID: 184168 [Multi-domain]  Cd Length: 591  Bit Score: 52.83  E-value: 1.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252607  47 LNEVDVNGWLEAFAAHPAIGTTSSSAPKWCKE---EQSAAlaTATDSTAQELA---DWNARYREKFGFVFMIC-----AS 115
Cdd:PRK13590   54 VREAGRDAQLGLIRAHPELAGKAMVAGSLTAEsthEQGKA--GLTHCTPEEFAriqQLNADYNARFGFPFILAvrgprGL 131

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1002252607 116 GRTAPEVLAELKRRYENRPIVELEIAAQEELKITELRLAKLFASEPV 162
Cdd:PRK13590  132 GLSRQEIIATFARRLDNHPDFELAEALRNIHRIAEIRLNDKFGAEPV 178
PRK13799 PRK13799
unknown domain/N-carbamoyl-L-amino acid hydrolase fusion protein; Provisional
 47-161 5.85e-07

unknown domain/N-carbamoyl-L-amino acid hydrolase fusion protein; Provisional


Pssm-ID: 106740 [Multi-domain]  Cd Length: 591  Bit Score: 51.17  E-value: 5.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252607  47 LNEVDVNGWLEAFAAHPAIGTTSSSAPKWCKE---EQS-AALATATDSTAQELADWNARYREKFGFVFMICASGRTAP-- 120
Cdd:PRK13799   54 LDAADRAAKLDLIRAHPELAGKAAEAGELTAEstgEQAkAGLNLCTPEEFAAIQKLNADYGKKFGFPFILAVKGARGAgl 133

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1002252607 121 ---EVLAELKRRYENRPIVELEIAAQEELKITELRLAKLFASEP 161
Cdd:PRK13799  134 akaEIIATFERRLHNHPDDELGEALRNIGRIAEIRINDKFGYTP 177
TR_THY smart00095
Transthyretin;
214-330 6.27e-06

Transthyretin;


Pssm-ID: 128406  Cd Length: 121  Bit Score: 44.87  E-value: 6.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002252607  214 PITTHVLDVARGSPASGIEVHLemwkdastppsFNNKDFNGWATLGSSVTNNdgrSGQLMDIVNN--VAPGFYRISFNTS 291
Cdd:smart00095   5 PLMVKVLDAVRGSPAVNVAVKV-----------FKKTEEGTWEPFASGKTNE---SGEIHELTTDekFVEGLYKVEFDTK 70

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1002252607  292 KY----APSGFFPYVSIIFEiKKNQTTEHFHVPLLHSPFSFTT 330
Cdd:smart00095  71 SYwkalGISPFHEYADVVFT-ANDSGHRHYTIAALLSPYSYST 112
 
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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