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Conserved domains on  [gi|446174017|ref|WP_000251872|]
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phosphoglucosamine mutase, partial [Escherichia coli]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
phosphohexomutase super family cl38939
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ...
 5-81 5.24e-44

The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this family include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). These enzymes play important and diverse roles in carbohydrate metabolism in organisms from bacteria to humans. Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.


The actual alignment was detected with superfamily member cd05802:

Pssm-ID: 476822  Cd Length: 434  Bit Score: 146.48  E-value: 5.24e-44
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446174017   5 YFGTDGIRGKANEGaMTAETALRVGMAAGRVFRRGDHRHRVVIGKDTRLSGYMLEPALTAGFTSMGMDVFLFGPLPT 81
Cdd:cd05802    1 LFGTDGIRGVANEP-LTPELALKLGRAAGKVLGKGGGRPKVLIGKDTRISGYMLESALAAGLTSAGVDVLLLGVIPT 76
 
Name Accession Description Interval E-value
GlmM cd05802
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ...
 5-81 5.24e-44

GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the alpha-D-phosphohexomutase superfamily. It is required for the interconversion of glucosamine-6-phosphate and glucosamine-1-phosphate in the biosynthetic pathway of UDP-N-acetylglucosamine, an essential precursor to components of the cell envelope. In order to be active, GlmM must be phosphorylated, which can occur via autophosphorylation or by the Ser/Thr kinase StkP. GlmM functions in a classical ping-pong bi-bi mechanism with glucosamine-1,6-diphosphate as an intermediate. Other members of the alpha-D-phosphohexomutase superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.


Pssm-ID: 100095  Cd Length: 434  Bit Score: 146.48  E-value: 5.24e-44
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446174017   5 YFGTDGIRGKANEGaMTAETALRVGMAAGRVFRRGDHRHRVVIGKDTRLSGYMLEPALTAGFTSMGMDVFLFGPLPT 81
Cdd:cd05802    1 LFGTDGIRGVANEP-LTPELALKLGRAAGKVLGKGGGRPKVLIGKDTRISGYMLESALAAGLTSAGVDVLLLGVIPT 76
glmM PRK10887
phosphoglucosamine mutase; Provisional
 3-81 2.63e-39

phosphoglucosamine mutase; Provisional


Pssm-ID: 236787  Cd Length: 443  Bit Score: 134.11  E-value: 2.63e-39
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446174017   3 RKYFGTDGIRGKANEGAMTAETALRVGMAAGRVFRRGdHRHRVVIGKDTRLSGYMLEPALTAGFTSMGMDVFLFGPLPT 81
Cdd:PRK10887   1 RKYFGTDGIRGKVGQAPITPDFVLKLGWAAGKVLARQ-GRPKVLIGKDTRISGYMLESALEAGLAAAGVDVLLTGPMPT 78
ManB COG1109
Phosphomannomutase [Carbohydrate transport and metabolism];
3-81 2.54e-31

Phosphomannomutase [Carbohydrate transport and metabolism];


Pssm-ID: 440726 [Multi-domain]  Cd Length: 456  Bit Score: 112.99  E-value: 2.54e-31
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446174017   3 RKYFGTDGIRGKANEGaMTAETALRVGMAAGRVFRRGDhRHRVVIGKDTRLSGYMLEPALTAGFTSMGMDVFLFGPLPT 81
Cdd:COG1109    4 KKLFGTDGIRGIVGEE-LTPEFVLKLGRAFGTYLKEKG-GPKVVVGRDTRLSSPMLARALAAGLASAGIDVYDLGLVPT 80
PGM_PMM_I pfam02878
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
3-81 3.27e-30

Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;


Pssm-ID: 427032  Cd Length: 138  Bit Score: 103.46  E-value: 3.27e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446174017    3 RKYFGTDGIRGKANEGAMTAETALRVGMAAGRVFRRGDHRHRVVIGKDTRLSGYMLEPALTAGFTSMGMDVFLFGPLPT 81
Cdd:pfam02878   1 RQLFGTSGIRGKVGVGELTPEFALKLGQAIASYLRAQGGGGKVVVGRDTRYSSRELARALAAGLASNGVEVILLGLLPT 79
 
Name Accession Description Interval E-value
GlmM cd05802
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ...
 5-81 5.24e-44

GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the alpha-D-phosphohexomutase superfamily. It is required for the interconversion of glucosamine-6-phosphate and glucosamine-1-phosphate in the biosynthetic pathway of UDP-N-acetylglucosamine, an essential precursor to components of the cell envelope. In order to be active, GlmM must be phosphorylated, which can occur via autophosphorylation or by the Ser/Thr kinase StkP. GlmM functions in a classical ping-pong bi-bi mechanism with glucosamine-1,6-diphosphate as an intermediate. Other members of the alpha-D-phosphohexomutase superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.


Pssm-ID: 100095  Cd Length: 434  Bit Score: 146.48  E-value: 5.24e-44
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446174017   5 YFGTDGIRGKANEGaMTAETALRVGMAAGRVFRRGDHRHRVVIGKDTRLSGYMLEPALTAGFTSMGMDVFLFGPLPT 81
Cdd:cd05802    1 LFGTDGIRGVANEP-LTPELALKLGRAAGKVLGKGGGRPKVLIGKDTRISGYMLESALAAGLTSAGVDVLLLGVIPT 76
glmM PRK10887
phosphoglucosamine mutase; Provisional
 3-81 2.63e-39

phosphoglucosamine mutase; Provisional


Pssm-ID: 236787  Cd Length: 443  Bit Score: 134.11  E-value: 2.63e-39
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446174017   3 RKYFGTDGIRGKANEGAMTAETALRVGMAAGRVFRRGdHRHRVVIGKDTRLSGYMLEPALTAGFTSMGMDVFLFGPLPT 81
Cdd:PRK10887   1 RKYFGTDGIRGKVGQAPITPDFVLKLGWAAGKVLARQ-GRPKVLIGKDTRISGYMLESALEAGLAAAGVDVLLTGPMPT 78
ManB COG1109
Phosphomannomutase [Carbohydrate transport and metabolism];
3-81 2.54e-31

Phosphomannomutase [Carbohydrate transport and metabolism];


Pssm-ID: 440726 [Multi-domain]  Cd Length: 456  Bit Score: 112.99  E-value: 2.54e-31
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446174017   3 RKYFGTDGIRGKANEGaMTAETALRVGMAAGRVFRRGDhRHRVVIGKDTRLSGYMLEPALTAGFTSMGMDVFLFGPLPT 81
Cdd:COG1109    4 KKLFGTDGIRGIVGEE-LTPEFVLKLGRAFGTYLKEKG-GPKVVVGRDTRLSSPMLARALAAGLASAGIDVYDLGLVPT 80
PGM_PMM_I pfam02878
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
3-81 3.27e-30

Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;


Pssm-ID: 427032  Cd Length: 138  Bit Score: 103.46  E-value: 3.27e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446174017    3 RKYFGTDGIRGKANEGAMTAETALRVGMAAGRVFRRGDHRHRVVIGKDTRLSGYMLEPALTAGFTSMGMDVFLFGPLPT 81
Cdd:pfam02878   1 RQLFGTSGIRGKVGVGELTPEFALKLGQAIASYLRAQGGGGKVVVGRDTRYSSRELARALAAGLASNGVEVILLGLLPT 79
PGM_like1 cd03087
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ...
 5-81 3.30e-23

This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this superfamily include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.


Pssm-ID: 100089  Cd Length: 439  Bit Score: 90.71  E-value: 3.30e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446174017   5 YFGTDGIRGKANEGaMTAETALRVGMAAGRVFRRGdhrhRVVIGKDTRLSGYMLEPALTAGFTSMGMDVFLFGPLPT 81
Cdd:cd03087    1 LFGTSGIRGVVGEE-LTPELALKVGKALGTYLGGG----TVVVGRDTRTSGPMLKNAVIAGLLSAGCDVIDIGIVPT 72
PMM_PGM cd03089
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ...
 11-81 2.16e-11

The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the reversible conversion of 1-phospho to 6-phospho-sugars (e.g. between mannose-1-phosphate and mannose-6-phosphate or glucose-1-phosphate and glucose-6-phosphate) via a bisphosphorylated sugar intermediate. The reaction involves two phosphoryl transfers, with an intervening 180 degree reorientation of the reaction intermediate during catalysis. Reorientation of the intermediate occurs without dissociation from the active site of the enzyme and is thus, a simple example of processivity, as defined by multiple rounds of catalysis without release of substrate. Glucose-6-phosphate and glucose-1-phosphate are known to be utilized for energy metabolism and cell surface construction, respectively. PMM/PGM belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the phosphoglucomutases (PGM1 and PGM2). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.


Pssm-ID: 100091  Cd Length: 443  Bit Score: 57.52  E-value: 2.16e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446174017  11 IRGKANEgAMTAETALRVGMAAGRVFRRGDHRhRVVIGKDTRLSGYMLEPALTAGFTSMGMDVFLFGPLPT 81
Cdd:cd03089    7 IRGIAGE-ELTEEIAYAIGRAFGSWLLEKGAK-KVVVGRDGRLSSPELAAALIEGLLAAGCDVIDIGLVPT 75
MPG1_transferase cd05805
GTP-mannose-1-phosphate guanyltransferase (MPG1 transferase), also known as GDP-mannose ...
 6-81 3.71e-09

GTP-mannose-1-phosphate guanyltransferase (MPG1 transferase), also known as GDP-mannose pyrophosphorylase, is a bifunctional enzyme with both phosphomannose isomerase (PMI) activity and GDP-mannose phosphorylase (GMP) activity. The protein contains an N-terminal NTP transferase domain, an L-beta-H domain, and a C-terminal PGM-like domain that belongs to the alpha-D-phosphohexomutase superfamily. This subfamily is limited to bacteria and archaea. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this group appear to lack conserved residues necessary for metal binding and catalytic activity. Other members of this superfamily include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.


Pssm-ID: 100097  Cd Length: 441  Bit Score: 51.09  E-value: 3.71e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446174017   6 FGTDGIRGKANeGAMTAETALRVGMAAGRVFRRGDhrhRVVIGKDTRLSGYMLEPALTAGFTSMGMDVFLFGPLPT 81
Cdd:cd05805    2 FGGRGVSGLIN-VDITPEFATRLGAAYGSTLPPGS---TVTVSRDASRASRMLKRALISGLLSTGVNVRDLGALPL 73
PGM_like4 cd05803
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ...
 10-81 4.66e-08

This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate guanyltransferase domain in a protein of unknown function that is found in both prokaryotes and eukaryotes. This domain belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this superfamily include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.


Pssm-ID: 100096  Cd Length: 445  Bit Score: 48.07  E-value: 4.66e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446174017  10 GIRGKANEGaMTAETALRVGMAAGRVFRRGDHRHRVVIGKDTRLSGYMLEPALTAGFTSMGMDVFLFGPLPT 81
Cdd:cd05803    6 GIRGIVGEG-LTPEVITRYVAAFATWQPERTKGGKIVVGRDGRPSGPMLEKIVIGALLACGCDVIDLGIAPT 76
PLN02371 PLN02371
phosphoglucosamine mutase family protein
 7-77 1.35e-07

phosphoglucosamine mutase family protein


Pssm-ID: 215211 [Multi-domain]  Cd Length: 583  Bit Score: 46.59  E-value: 1.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446174017   7 GTDgIRGKANEG------AMTAETALRVGMAAGRVFR-----RGDHRHRVVIGKDTRLSGYMLEPALTAGFTSMGMDVFL 75
Cdd:PLN02371  70 GSD-IRGVAVEGvegepvTLTPPAVEAIGAAFAEWLLekkkaDGSGELRVSVGRDPRISGPRLADAVFAGLASAGLDVVD 148


                 ..
gi 446174017  76 FG 77
Cdd:PLN02371 149 MG 150
phosphohexomutase cd03084
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ...
 5-35 8.97e-06

The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this family include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). These enzymes play important and diverse roles in carbohydrate metabolism in organisms from bacteria to humans. Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.


Pssm-ID: 100086 [Multi-domain]  Cd Length: 355  Bit Score: 41.57  E-value: 8.97e-06
                         10        20        30
                 ....*....|....*....|....*....|.
gi 446174017   5 YFGTDGIRGKANEgAMTAETALRVGMAAGRV 35
Cdd:cd03084    1 IFGTSGVRGVVGD-DITPETAVALGQAIGST 30
PGM2 cd05799
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ...
 6-81 7.78e-04

This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The mammalian PGM2 is thought to be a phosphopentomutase that catalyzes the conversion of the nucleoside breakdown products, ribose-1-phosphate and deoxyribose-1-phosphate to the corresponding 5-phosphopentoses. PGM2L1 is thought to catalyze the 1,3-bisphosphoglycerate-dependent synthesis of glucose 1,6-bisphosphate and other aldose-bisphosphates that serve as cofactors for several sugar phosphomutases and possibly also as regulators of glycolytic enzymes. PGM2 and PGM2L1 belong to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.


Pssm-ID: 100092  Cd Length: 487  Bit Score: 35.95  E-value: 7.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446174017   6 FGTDGIRGK--ANEGAMTAETALRV--GMAA--GRVFRRGDHRhRVVIGKDTRLSGYmlEPA-LTAG-FTSMGMDVFLF- 76
Cdd:cd05799    4 FGTAGLRGKmgAGTNRMNDYTVRQAtqGLANylKKKGPDAKNR-GVVIGYDSRHNSR--EFAeLTAAvLAANGIKVYLFd 80


                 ....*
gi 446174017  77 GPLPT 81
Cdd:cd05799   81 DLRPT 85
PGM_like2 cd05800
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ...
 6-81 2.32e-03

This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the alpha-D-phosphohexomutase superfamily and is found in both archaea and bacteria. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four structural domains (subdomains) with a centrally located active site formed by four loops, one from each subdomain. All four subdomains are included in this alignment model.


Pssm-ID: 100093  Cd Length: 461  Bit Score: 34.84  E-value: 2.32e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446174017   6 FGTDGIRGKANEGaMTAETALRVGMAAGRVF-RRGDHRHRVVIGKDTR-LSGYMLEpALTAGFTSMGMDVFLF-GPLPT 81
Cdd:cd05800    3 FGTDGWRGIIAED-FTFENVRRVAQAIADYLkEEGGGGRGVVVGYDTRfLSEEFAR-AVAEVLAANGIDVYLSdRPVPT 79
PTZ00150 PTZ00150
phosphoglucomutase-2-like protein; Provisional
 3-81 5.17e-03

phosphoglucomutase-2-like protein; Provisional


Pssm-ID: 240294  Cd Length: 584  Bit Score: 33.89  E-value: 5.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446174017   3 RKYFGTDGIRGKANEG--AMTAETALRV--GMAAG--RVFRRGDHRHRVVIGKDTRLSGYMLEPALTAGFTSMGMDVFLF 76
Cdd:PTZ00150  44 RMEFGTAGLRGKMGAGfnCMNDLTVQQTaqGLCAYviETFGQALKSRGVVIGYDGRYHSRRFAEITASVFLSKGFKVYLF 123


                 ....*.
gi 446174017  77 GPL-PT 81
Cdd:PTZ00150 124 GQTvPT 129
 
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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