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Conserved domains on  [gi|488994062|ref|WP_002904788|]
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MULTISPECIES: hydroxyisourate hydrolase [Klebsiella]

Protein Classification

hydroxyisourate hydrolase( domain architecture ID 10006399)

hydroxyisourate hydrolase catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU) in the second step of a three-step ureide pathway

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HiuH COG2351
5-hydroxyisourate hydrolase (purine catabolism), transthyretin-related family [Nucleotide ...
 1-108 2.17e-47

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


:

Pssm-ID: 441918  Cd Length: 111  Bit Score: 147.21  E-value: 2.17e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994062   1 MSTLSTHILDISTGTPAEGVTVSLSR----EGETLANLVTNAQGRIATFSAAPLPAGRYCLTAETGAWFARAGRESVFTR 76
Cdd:COG2351    1 MGRLSTHVLDTARGRPAAGVRVELYRldgdGWTLLAEGVTNADGRIDALGGEALAAGTYRLVFDTGDYFAARGVPPFLPE 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 488994062  77 AQIDFVIGEAAEdHFHLPFLIAPGGWSTYRGS 108
Cdd:COG2351   81 VPVRFGIADPEE-HYHVPLLLSPWGYSTYRGS 111
 
Name Accession Description Interval E-value
HiuH COG2351
5-hydroxyisourate hydrolase (purine catabolism), transthyretin-related family [Nucleotide ...
 1-108 2.17e-47

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


Pssm-ID: 441918  Cd Length: 111  Bit Score: 147.21  E-value: 2.17e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994062   1 MSTLSTHILDISTGTPAEGVTVSLSR----EGETLANLVTNAQGRIATFSAAPLPAGRYCLTAETGAWFARAGRESVFTR 76
Cdd:COG2351    1 MGRLSTHVLDTARGRPAAGVRVELYRldgdGWTLLAEGVTNADGRIDALGGEALAAGTYRLVFDTGDYFAARGVPPFLPE 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 488994062  77 AQIDFVIGEAAEdHFHLPFLIAPGGWSTYRGS 108
Cdd:COG2351   81 VPVRFGIADPEE-HYHVPLLLSPWGYSTYRGS 111
TLP_HIUase cd05822
HIUase (5-hydroxyisourate hydrolase) catalyzes the second step in a three-step ureide pathway ...
 2-108 1.85e-42

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: 134.59  E-value: 1.85e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994062   2 STLSTHILDISTGTPAEGVTVSLSREGE----TLANLVTNAQGRIATFS--AAPLPAGRYCLTAETGAWFARAGRESVFT 75
Cdd:cd05822    1 GPLSTHVLDTATGKPAAGVAVTLYRLDGngwtLLATGVTNADGRCDDLLppGAQLAAGTYKLTFDTGAYFAARGQESFYP 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 488994062  76 RAQIDFVIGEAAEdHFHLPFLIAPGGWSTYRGS 108
Cdd:cd05822   81 EVEVRFTITDPTE-HYHVPLLLSPFGYSTYRGS 112
Transthyretin pfam00576
HIUase/Transthyretin family; This family includes transthyretin that is a thyroid ...
 4-107 8.34e-40

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: 127.95  E-value: 8.34e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994062    4 LSTHILDISTGTPAEGVTVSLSREGE----TLANLVTNAQGRIATF--SAAPLPAGRYCLTAETGAWFARAGRESVFTRA 77
Cdd:pfam00576   1 LTTHVLDTARGRPAAGVRVTLYRLDGdgwtLLAEGTTNADGRCDDLllEGEALEPGTYRLVFDTGAYFAARGVESFYPEV 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 488994062   78 QIDFVIGEAAedHFHLPFLIAPGGWSTYRG 107
Cdd:pfam00576  81 EVRFGITDAE--HYHVPLLLSPFGYSTYRG 108
hdxy_isourate TIGR02962
hydroxyisourate hydrolase; Members of this family, hydroxyisourate hydrolase, represent a ...
 2-108 2.23e-35

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: 116.88  E-value: 2.23e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994062    2 STLSTHILDISTGTPAEGVTVSLSREGE----TLANLVTNAQGRIATF--SAAPLPAGRYCLTAETGAWFARAGRESVFT 75
Cdd:TIGR02962   1 SPLSTHVLDTTSGKPAAGVPVTLYRLDGggwtPLATGVTNADGRCDGPlpEGEDLAPGIYKLRFDTGDYFAARGVESFYP 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 488994062   76 RAQIDFVIGEAAEdHFHLPFLIAPGGWSTYRGS 108
Cdd:TIGR02962  81 EVEVVFTIADPGQ-HYHVPLLLSPYGYSTYRGS 112
PRK15036 PRK15036
hydroxyisourate hydrolase; Provisional
 4-108 6.70e-19

hydroxyisourate hydrolase; Provisional


Pssm-ID: 184996  Cd Length: 137  Bit Score: 75.79  E-value: 6.70e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994062   4 LSTHILDISTGTPAEGVTVSLSREGET----LANLVTNAQGRIATF----SAAPlpaGRYCLTAETGAWFARAGRESVFT 75
Cdd:PRK15036  29 LSVHILNQQTGKPAADVTVTLEKKADNgwlqLNTAKTDKDGRIKALwpeqTATT---GDYRVVFKTGDYFKKQNLESFFP 105

                         90       100       110
                 ....*....|....*....|....*....|...
gi 488994062  76 RAQIDFVIGEAAEdHFHLPFLIAPGGWSTYRGS 108
Cdd:PRK15036 106 EIPVEFHINKVNE-HYHVPLLLSQYGYSTYRGS 137
 
Name Accession Description Interval E-value
HiuH COG2351
5-hydroxyisourate hydrolase (purine catabolism), transthyretin-related family [Nucleotide ...
 1-108 2.17e-47

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


Pssm-ID: 441918  Cd Length: 111  Bit Score: 147.21  E-value: 2.17e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994062   1 MSTLSTHILDISTGTPAEGVTVSLSR----EGETLANLVTNAQGRIATFSAAPLPAGRYCLTAETGAWFARAGRESVFTR 76
Cdd:COG2351    1 MGRLSTHVLDTARGRPAAGVRVELYRldgdGWTLLAEGVTNADGRIDALGGEALAAGTYRLVFDTGDYFAARGVPPFLPE 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 488994062  77 AQIDFVIGEAAEdHFHLPFLIAPGGWSTYRGS 108
Cdd:COG2351   81 VPVRFGIADPEE-HYHVPLLLSPWGYSTYRGS 111
TLP_HIUase cd05822
HIUase (5-hydroxyisourate hydrolase) catalyzes the second step in a three-step ureide pathway ...
 2-108 1.85e-42

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: 134.59  E-value: 1.85e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994062   2 STLSTHILDISTGTPAEGVTVSLSREGE----TLANLVTNAQGRIATFS--AAPLPAGRYCLTAETGAWFARAGRESVFT 75
Cdd:cd05822    1 GPLSTHVLDTATGKPAAGVAVTLYRLDGngwtLLATGVTNADGRCDDLLppGAQLAAGTYKLTFDTGAYFAARGQESFYP 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 488994062  76 RAQIDFVIGEAAEdHFHLPFLIAPGGWSTYRGS 108
Cdd:cd05822   81 EVEVRFTITDPTE-HYHVPLLLSPFGYSTYRGS 112
Transthyretin pfam00576
HIUase/Transthyretin family; This family includes transthyretin that is a thyroid ...
 4-107 8.34e-40

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: 127.95  E-value: 8.34e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994062    4 LSTHILDISTGTPAEGVTVSLSREGE----TLANLVTNAQGRIATF--SAAPLPAGRYCLTAETGAWFARAGRESVFTRA 77
Cdd:pfam00576   1 LTTHVLDTARGRPAAGVRVTLYRLDGdgwtLLAEGTTNADGRCDDLllEGEALEPGTYRLVFDTGAYFAARGVESFYPEV 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 488994062   78 QIDFVIGEAAedHFHLPFLIAPGGWSTYRG 107
Cdd:pfam00576  81 EVRFGITDAE--HYHVPLLLSPFGYSTYRG 108
hdxy_isourate TIGR02962
hydroxyisourate hydrolase; Members of this family, hydroxyisourate hydrolase, represent a ...
 2-108 2.23e-35

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: 116.88  E-value: 2.23e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994062    2 STLSTHILDISTGTPAEGVTVSLSREGE----TLANLVTNAQGRIATF--SAAPLPAGRYCLTAETGAWFARAGRESVFT 75
Cdd:TIGR02962   1 SPLSTHVLDTTSGKPAAGVPVTLYRLDGggwtPLATGVTNADGRCDGPlpEGEDLAPGIYKLRFDTGDYFAARGVESFYP 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 488994062   76 RAQIDFVIGEAAEdHFHLPFLIAPGGWSTYRGS 108
Cdd:TIGR02962  81 EVEVVFTIADPGQ-HYHVPLLLSPYGYSTYRGS 112
PRK15036 PRK15036
hydroxyisourate hydrolase; Provisional
 4-108 6.70e-19

hydroxyisourate hydrolase; Provisional


Pssm-ID: 184996  Cd Length: 137  Bit Score: 75.79  E-value: 6.70e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994062   4 LSTHILDISTGTPAEGVTVSLSREGET----LANLVTNAQGRIATF----SAAPlpaGRYCLTAETGAWFARAGRESVFT 75
Cdd:PRK15036  29 LSVHILNQQTGKPAADVTVTLEKKADNgwlqLNTAKTDKDGRIKALwpeqTATT---GDYRVVFKTGDYFKKQNLESFFP 105

                         90       100       110
                 ....*....|....*....|....*....|...
gi 488994062  76 RAQIDFVIGEAAEdHFHLPFLIAPGGWSTYRGS 108
Cdd:PRK15036 106 EIPVEFHINKVNE-HYHVPLLLSQYGYSTYRGS 137
Transthyretin_like cd05469
Transthyretin_like. This domain is present in the transthyretin-like protein (TLP) family ...
 2-108 2.54e-17

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: 71.03  E-value: 2.54e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994062   2 STLSTHILDISTGTPAEGVTVSLSREGET-----LANLVTNAQGRI-ATFSAAPLPAGRYCLTAETGAWFARAGRESVFT 75
Cdd:cd05469    1 CPLMVKVLDAVRGSPAANVAIKVFRKTADgsweiFATGKTNEDGELhGLITEEEF*AGVYRVEFDTKSYWKALGITPFHE 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 488994062  76 RAQIDFVIGEAAEDHFHLPFLIAPGGWSTYRGS 108
Cdd:cd05469   81 YAEVVFTANDSGHRHYTIALLLSPFSYSTTAVV 113
YfaS COG2373
Uncharacterized conserved protein YfaS, alpha-2-macroglobulin family [General function ...
 10-49 4.39e-05

Uncharacterized conserved protein YfaS, alpha-2-macroglobulin family [General function prediction only];


Pssm-ID: 441940 [Multi-domain]  Cd Length: 1605  Bit Score: 40.83  E-value: 4.39e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 488994062   10 DISTGTPAEGVTVSL-SREGETLANLVTNAQGrIATFSAAP 49
Cdd:COG2373   284 SLSTGKPVAGAEVELyDRNGQVLATATTDADG-LARFPAGD 323
bMG3 pfam11974
Bacterial alpha-2-macroglobulin MG3 domain; This is the MG3 domain from bacterial ...
 4-66 6.40e-05

Bacterial alpha-2-macroglobulin MG3 domain; This is the MG3 domain from bacterial alpha2-macroglobulins.


Pssm-ID: 432232 [Multi-domain]  Cd Length: 102  Bit Score: 38.73  E-value: 6.40e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488994062    4 LSTHILDISTGTPAEGVTVSL-SREGETLANLVTNAQG--RIATFSAAPLPAGRYCLTAETGAWFA 66
Cdd:pfam11974  15 LLVWVTSLDSGKPVAGVEVRLlDCNGQVLATGTTDAQGhaRFEGPLTRDGGAAPALVSARKDGDFA 80
TLP_Transthyretin cd05821
Transthyretin (TTR) is a 55 kDa protein responsible for the transport of thyroid hormones and ...
 4-104 2.84e-04

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: 37.53  E-value: 2.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994062   4 LSTHILDISTGTPAEGVTVSLSREG-----ETLANLVTNAQGRIATFSA-APLPAGRYCLTAETGAWFARAGRESVFTRA 77
Cdd:cd05821    9 LMVKVLDAVRGSPAANVAVKVFKKTadgswEPFASGKTTETGEIHGLTTdEQFTEGVYKVEFDTKAYWKKLGISPFHEYA 88

                         90       100
                 ....*....|....*....|....*..
gi 488994062  78 QIDFVIGEAAEDHFHLPFLIAPGGWST 104
Cdd:cd05821   89 EVVFTANDSGHRHYTIAALLSPYSYST 115
CarboxypepD_reg pfam13620
Carboxypeptidase regulatory-like domain;
3-93 4.98e-04

Carboxypeptidase regulatory-like domain;


Pssm-ID: 433354 [Multi-domain]  Cd Length: 81  Bit Score: 36.10  E-value: 4.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488994062    3 TLSTHILDiSTGTPAEGVTVSLSR-EGETLANLVTNAQGRiatFSAAPLPAGRYCLTAEtgawfaRAGRESvFTRAQIDF 81
Cdd:pfam13620   1 TISGTVTD-PSGAPVPGATVTVTNtDTGTVRTTTTDADGR---YRFPGLPPGTYTVTVS------APGFKT-ATRTGVTV 69

                          90
                  ....*....|..
gi 488994062   82 VIGEAAEDHFHL 93
Cdd:pfam13620  70 TAGQTTTLDVTL 81
ClfA COG4932
Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing ...
 10-63 3.62e-03

Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing adhesive matrix molecules) family, DEv-IgG fold [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443959 [Multi-domain]  Cd Length: 689  Bit Score: 35.33  E-value: 3.62e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488994062  10 DISTG-TPAEGVTVSL-SREGETLANLVTNAQGRiATFSAapLPAGRYCLTaETGA 63
Cdd:COG4932  366 DADDGeAPLAGAEFTLtDADGTVVATITTDADGT-ASFKG--LAPGTYTLT-ETKA 417
 
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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