NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|311350624|gb|ADP92497|]
View 

glycerol kinase, partial [Clostridium perfringens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ASKHA_ATPase-like super family cl49607
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ...
 1-174 1.30e-133

ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.


The actual alignment was detected with superfamily member PRK00047:

Pssm-ID: 483947 [Multi-domain]  Cd Length: 498  Bit Score: 382.25  E-value: 1.30e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624   1 ATQYSVLQEVMAKCNITQENIAAIGITNQRETTIVWDKNTGVPIYNAIVWQCRRTADICDELKeRDGLVDYIRENTGLVL 80
Cdd:PRK00047  55 ASQLSVIAEALAKAGISPDQIAAIGITNQRETTVVWDKETGRPIYNAIVWQDRRTADICEELK-RDGYEDYIREKTGLVI 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624  81 DAYFSGTKIKWILDNVEGAREKAEKGELLFGTVDSWLVWKLTNGKVHVTDYTNASRTMIFNIKNLEWDERMLKELDIPRS 160
Cdd:PRK00047 134 DPYFSGTKIKWILDNVEGARERAEKGELLFGTIDTWLVWKLTGGKVHVTDYTNASRTMLFNIHTLDWDDELLELLDIPRS 213

                        170
                 ....*....|....
gi 311350624 161 MLPEVKNSSEIYGY 174
Cdd:PRK00047 214 MLPEVRPSSEVYGK 227
 
Name Accession Description Interval E-value
glpK PRK00047
glycerol kinase GlpK;
1-174 1.30e-133

glycerol kinase GlpK;


Pssm-ID: 234594 [Multi-domain]  Cd Length: 498  Bit Score: 382.25  E-value: 1.30e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624   1 ATQYSVLQEVMAKCNITQENIAAIGITNQRETTIVWDKNTGVPIYNAIVWQCRRTADICDELKeRDGLVDYIRENTGLVL 80
Cdd:PRK00047  55 ASQLSVIAEALAKAGISPDQIAAIGITNQRETTVVWDKETGRPIYNAIVWQDRRTADICEELK-RDGYEDYIREKTGLVI 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624  81 DAYFSGTKIKWILDNVEGAREKAEKGELLFGTVDSWLVWKLTNGKVHVTDYTNASRTMIFNIKNLEWDERMLKELDIPRS 160
Cdd:PRK00047 134 DPYFSGTKIKWILDNVEGARERAEKGELLFGTIDTWLVWKLTGGKVHVTDYTNASRTMLFNIHTLDWDDELLELLDIPRS 213

                        170
                 ....*....|....
gi 311350624 161 MLPEVKNSSEIYGY 174
Cdd:PRK00047 214 MLPEVRPSSEVYGK 227
GlpK COG0554
Glycerol kinase [Energy production and conversion];
1-174 1.30e-132

Glycerol kinase [Energy production and conversion];


Pssm-ID: 440320 [Multi-domain]  Cd Length: 496  Bit Score: 379.79  E-value: 1.30e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624   1 ATQYSVLQEVMAKCNITQENIAAIGITNQRETTIVWDKNTGVPIYNAIVWQCRRTADICDELKErDGLVDYIRENTGLVL 80
Cdd:COG0554   53 ESVLAVIREALAKAGISAEDIAAIGITNQRETTVVWDRKTGKPLYNAIVWQDRRTADICEELKA-DGLEDLIREKTGLVL 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624  81 DAYFSGTKIKWILDNVEGAREKAEKGELLFGTVDSWLVWKLTNGKVHVTDYTNASRTMIFNIKNLEWDERMLKELDIPRS 160
Cdd:COG0554  132 DPYFSATKIKWILDNVPGARERAEAGELLFGTIDSWLIWKLTGGKVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPRS 211

                        170
                 ....*....|....
gi 311350624 161 MLPEVKNSSEIYGY 174
Cdd:COG0554  212 MLPEVRPSSEVFGE 225
FGGY_EcGK_like cd07786
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ...
 1-174 9.28e-127

Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate kinases; This subgroup is composed of mostly bacterial and archaeal glycerol kinases (GK), including the well characterized proteins from Escherichia coli (EcGK), Thermococcus kodakaraensis (TkGK), and Enterococcus casseliflavus (EnGK). GKs contain two large domains separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The high affinity ATP binding site of EcGK is created only by a substrate-induced conformational change, which is initiated by protein-protein interactions through complex formation with enzyme IIAGlc (also known as IIIGlc), the glucose-specific phosphocarrier protein of the phosphotransferase system (PTS). EcGK exists in a dimer-tetramer equilibrium. IIAGlc binds to both EcGK dimer and tetramer, and inhibits the uptake and subsequent metabolism of glycerol and maltose. Another well-known allosteric regulator of EcGK is fructose 1,6-bisphosphate (FBP), which binds to the EcGK tetramer and plays an essential role in the stabilization of the inactive tetrameric form. EcGK requires Mg2+ for its enzymatic activity. Members in this subgroup belong to the FGGY family of carbohydrate kinases


Pssm-ID: 198361 [Multi-domain]  Cd Length: 486  Bit Score: 364.50  E-value: 9.28e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624   1 ATQYSVLQEVMAKCNITQENIAAIGITNQRETTIVWDKNTGVPIYNAIVWQCRRTADICDELKErDGLVDYIRENTGLVL 80
Cdd:cd07786   50 ESQLAVAREALAKAGIRASDIAAIGITNQRETTVVWDRETGKPVYNAIVWQDRRTADICEELKA-EGHEEMIREKTGLVL 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624  81 DAYFSGTKIKWILDNVEGAREKAEKGELLFGTVDSWLVWKLTNGKVHVTDYTNASRTMIFNIKNLEWDERMLKELDIPRS 160
Cdd:cd07786  129 DPYFSATKIRWILDNVPGARERAERGELAFGTIDSWLIWKLTGGKVHATDVTNASRTMLFNIHTLEWDDELLELFGIPAS 208

                        170
                 ....*....|....
gi 311350624 161 MLPEVKNSSEIYGY 174
Cdd:cd07786  209 MLPEVKPSSEVFGY 222
glycerol_kin TIGR01311
glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of ...
 1-174 4.92e-110

glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of carbohydrate kinases. [Energy metabolism, Other]


Pssm-ID: 273549 [Multi-domain]  Cd Length: 493  Bit Score: 322.27  E-value: 4.92e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624    1 ATQYSVLQEVMAKCNITQENIAAIGITNQRETTIVWDKNTGVPIYNAIVWQCRRTADICDELKErDGLVDYIRENTGLVL 80
Cdd:TIGR01311  51 ESVLSCIAEALAKAGIKPDDIAAIGITNQRETTVVWDKATGKPLYNAIVWQDRRTASICEELKA-EGYGEFIREKTGLPL 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624   81 DAYFSGTKIKWILDNVEGAREKAEKGELLFGTVDSWLVWKLTNGKVHVTDYTNASRTMIFNIKNLEWDERMLKELDIPRS 160
Cdd:TIGR01311 130 DPYFSATKLRWLLDNVPGVREAAERGELLFGTIDTWLIWNLTGGKVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPRE 209

                         170
                  ....*....|....
gi 311350624  161 MLPEVKNSSEIYGY 174
Cdd:TIGR01311 210 ILPEVRSSSEVYGY 223
FGGY_N pfam00370
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ...
 1-174 4.50e-72

FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the C-terminal domain.


Pssm-ID: 395295 [Multi-domain]  Cd Length: 245  Bit Score: 217.21  E-value: 4.50e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624    1 ATQYSVLQEVMAKCNITQENIAAIGITNQRETTIVWDKNTGvPIYNAIVWQCRRTADICDELKErDGLVDYIRENTGLVL 80
Cdd:pfam00370  50 QAVAQCIAKTLSQLGISLKQIKGIGISNQGHGTVLLDKNDK-PLYNAILWKDRRTAEIVENLKE-EGNNQKLYEITGLPI 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624   81 DAYFSGTKIKWILDNVEGAREKAEKgellFGTVDSWLVWKLTNgkVHVTDYTNASRTMIFNIKNLEWDERMLKELDIPRS 160
Cdd:pfam00370 128 WPGFTLSKLRWIKENEPEVFEKIHK----FLTIHDYLRWRLTG--VFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRD 201

                         170
                  ....*....|....
gi 311350624  161 MLPEVKNSSEIYGY 174
Cdd:pfam00370 202 HLPPLVESSEIYGE 215
 
Name Accession Description Interval E-value
glpK PRK00047
glycerol kinase GlpK;
1-174 1.30e-133

glycerol kinase GlpK;


Pssm-ID: 234594 [Multi-domain]  Cd Length: 498  Bit Score: 382.25  E-value: 1.30e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624   1 ATQYSVLQEVMAKCNITQENIAAIGITNQRETTIVWDKNTGVPIYNAIVWQCRRTADICDELKeRDGLVDYIRENTGLVL 80
Cdd:PRK00047  55 ASQLSVIAEALAKAGISPDQIAAIGITNQRETTVVWDKETGRPIYNAIVWQDRRTADICEELK-RDGYEDYIREKTGLVI 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624  81 DAYFSGTKIKWILDNVEGAREKAEKGELLFGTVDSWLVWKLTNGKVHVTDYTNASRTMIFNIKNLEWDERMLKELDIPRS 160
Cdd:PRK00047 134 DPYFSGTKIKWILDNVEGARERAEKGELLFGTIDTWLVWKLTGGKVHVTDYTNASRTMLFNIHTLDWDDELLELLDIPRS 213

                        170
                 ....*....|....
gi 311350624 161 MLPEVKNSSEIYGY 174
Cdd:PRK00047 214 MLPEVRPSSEVYGK 227
GlpK COG0554
Glycerol kinase [Energy production and conversion];
1-174 1.30e-132

Glycerol kinase [Energy production and conversion];


Pssm-ID: 440320 [Multi-domain]  Cd Length: 496  Bit Score: 379.79  E-value: 1.30e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624   1 ATQYSVLQEVMAKCNITQENIAAIGITNQRETTIVWDKNTGVPIYNAIVWQCRRTADICDELKErDGLVDYIRENTGLVL 80
Cdd:COG0554   53 ESVLAVIREALAKAGISAEDIAAIGITNQRETTVVWDRKTGKPLYNAIVWQDRRTADICEELKA-DGLEDLIREKTGLVL 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624  81 DAYFSGTKIKWILDNVEGAREKAEKGELLFGTVDSWLVWKLTNGKVHVTDYTNASRTMIFNIKNLEWDERMLKELDIPRS 160
Cdd:COG0554  132 DPYFSATKIKWILDNVPGARERAEAGELLFGTIDSWLIWKLTGGKVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPRS 211

                        170
                 ....*....|....
gi 311350624 161 MLPEVKNSSEIYGY 174
Cdd:COG0554  212 MLPEVRPSSEVFGE 225
FGGY_EcGK_like cd07786
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ...
 1-174 9.28e-127

Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate kinases; This subgroup is composed of mostly bacterial and archaeal glycerol kinases (GK), including the well characterized proteins from Escherichia coli (EcGK), Thermococcus kodakaraensis (TkGK), and Enterococcus casseliflavus (EnGK). GKs contain two large domains separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The high affinity ATP binding site of EcGK is created only by a substrate-induced conformational change, which is initiated by protein-protein interactions through complex formation with enzyme IIAGlc (also known as IIIGlc), the glucose-specific phosphocarrier protein of the phosphotransferase system (PTS). EcGK exists in a dimer-tetramer equilibrium. IIAGlc binds to both EcGK dimer and tetramer, and inhibits the uptake and subsequent metabolism of glycerol and maltose. Another well-known allosteric regulator of EcGK is fructose 1,6-bisphosphate (FBP), which binds to the EcGK tetramer and plays an essential role in the stabilization of the inactive tetrameric form. EcGK requires Mg2+ for its enzymatic activity. Members in this subgroup belong to the FGGY family of carbohydrate kinases


Pssm-ID: 198361 [Multi-domain]  Cd Length: 486  Bit Score: 364.50  E-value: 9.28e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624   1 ATQYSVLQEVMAKCNITQENIAAIGITNQRETTIVWDKNTGVPIYNAIVWQCRRTADICDELKErDGLVDYIRENTGLVL 80
Cdd:cd07786   50 ESQLAVAREALAKAGIRASDIAAIGITNQRETTVVWDRETGKPVYNAIVWQDRRTADICEELKA-EGHEEMIREKTGLVL 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624  81 DAYFSGTKIKWILDNVEGAREKAEKGELLFGTVDSWLVWKLTNGKVHVTDYTNASRTMIFNIKNLEWDERMLKELDIPRS 160
Cdd:cd07786  129 DPYFSATKIRWILDNVPGARERAERGELAFGTIDSWLIWKLTGGKVHATDVTNASRTMLFNIHTLEWDDELLELFGIPAS 208

                        170
                 ....*....|....
gi 311350624 161 MLPEVKNSSEIYGY 174
Cdd:cd07786  209 MLPEVKPSSEVFGY 222
ASKHA_NBD_FGGY_GK cd07769
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ...
 1-174 1.97e-124

nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), also called ATP:glycerol 3-phosphotransferase, or glycerokinase, is a key enzyme in the regulation of glycerol uptake and metabolism. It catalyzes the Mg-ATP-dependent phosphorylation of glycerol to yield sn-glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone, L-glyceraldehyde and D-glyceraldehyde. The subfamily includes GKs and GK-like proteins from all three kingdoms of living organisms. Metazoan GKs, coded by X chromosome-linked GK genes, and GK-like proteins, coded by autosomal testis-specific GK-like genes GK2, GK3 and Gykl1 (in mouse) are closely related to the bacterial GKs. The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Under different conditions, GKs from different species may exist in different oligomeric states. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466789 [Multi-domain]  Cd Length: 486  Bit Score: 358.70  E-value: 1.97e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624   1 ATQYSVLQEVMAKCNITQENIAAIGITNQRETTIVWDKNTGVPIYNAIVWQCRRTADICDELKErDGLVDYIRENTGLVL 80
Cdd:cd07769   50 ENTLEVIREALAKAGISASDIAAIGITNQRETTVVWDKKTGKPLYNAIVWQDRRTADICEELKA-KGLEERIREKTGLPL 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624  81 DAYFSGTKIKWILDNVEGAREKAEKGELLFGTVDSWLVWKLTNGKVHVTDYTNASRTMIFNIKNLEWDERMLKELDIPRS 160
Cdd:cd07769  129 DPYFSATKIKWILDNVPGARERAERGELLFGTIDTWLIWKLTGGKVHVTDVTNASRTMLFNIHTLEWDDELLELFGIPRS 208

                        170
                 ....*....|....
gi 311350624 161 MLPEVKNSSEIYGY 174
Cdd:cd07769  209 MLPEVRPSSEVFGY 222
glycerol_kin TIGR01311
glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of ...
 1-174 4.92e-110

glycerol kinase; This model describes glycerol kinase, a member of the FGGY family of carbohydrate kinases. [Energy metabolism, Other]


Pssm-ID: 273549 [Multi-domain]  Cd Length: 493  Bit Score: 322.27  E-value: 4.92e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624    1 ATQYSVLQEVMAKCNITQENIAAIGITNQRETTIVWDKNTGVPIYNAIVWQCRRTADICDELKErDGLVDYIRENTGLVL 80
Cdd:TIGR01311  51 ESVLSCIAEALAKAGIKPDDIAAIGITNQRETTVVWDKATGKPLYNAIVWQDRRTASICEELKA-EGYGEFIREKTGLPL 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624   81 DAYFSGTKIKWILDNVEGAREKAEKGELLFGTVDSWLVWKLTNGKVHVTDYTNASRTMIFNIKNLEWDERMLKELDIPRS 160
Cdd:TIGR01311 130 DPYFSATKLRWLLDNVPGVREAAERGELLFGTIDTWLIWNLTGGKVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPRE 209

                         170
                  ....*....|....
gi 311350624  161 MLPEVKNSSEIYGY 174
Cdd:TIGR01311 210 ILPEVRSSSEVYGY 223
ASKHA_NBD_FGGY_GK1-3-like cd07792
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ...
 4-174 9.44e-86

nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; This subfamily contains metazoan glycerol kinases (GKs), coded by X chromosome-linked GK genes, and glycerol kinase (GK)-like proteins, coded by autosomal testis-specific GK-like genes (GK-like genes, GK2 and GK3). Sequence comparison shows that metazoan GKs and GK-like proteins in this family are closely related to the bacterial GKs (EC 2.7.1.30), which catalyze the Mg-ATP dependent phosphorylation of glycerol to yield glycerol 3-phosphate (G3P). The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466802 [Multi-domain]  Cd Length: 499  Bit Score: 260.15  E-value: 9.44e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624   4 YSVLQEVMAKC---NITQENIAAIGITNQRETTIVWDKNTGVPIYNAIVWQCRRTADICDELKERDGL-VDYIRENTGLV 79
Cdd:cd07792   54 YECIEEAVEKLkalGISPSDIKAIGITNQRETTVVWDKSTGKPLYNAIVWLDTRTSDTVEELSAKTPGgKDHFRKKTGLP 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624  80 LDAYFSGTKIKWILDNVEGAREKAEKGELLFGTVDSWLVWKLTNGK---VHVTDYTNASRTMIFNIKNLEWDERMLKELD 156
Cdd:cd07792  134 ISTYFSAVKLRWLLDNVPEVKKAVDDGRLLFGTVDSWLIWNLTGGKnggVHVTDVTNASRTMLMNLRTLQWDPELCEFFG 213

                        170
                 ....*....|....*...
gi 311350624 157 IPRSMLPEVKNSSEIYGY 174
Cdd:cd07792  214 IPMSILPEIRSSSEVYGK 231
PTZ00294 PTZ00294
glycerol kinase-like protein; Provisional
 4-174 7.73e-77

glycerol kinase-like protein; Provisional


Pssm-ID: 240348 [Multi-domain]  Cd Length: 504  Bit Score: 237.56  E-value: 7.73e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624   4 YSVLQEVMAKC--NITQENIAAIGITNQRETTIVWDKNTGVPIYNAIVWQCRRTADICDELKERDGLVDYIRENTGLVLD 81
Cdd:PTZ00294  55 YKCMNEAIKKLreKGPSFKIKAIGITNQRETVVAWDKVTGKPLYNAIVWLDTRTYDIVNELTKKYGGSNFFQKITGLPIS 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624  82 AYFSGTKIKWILDNVEGAREKAEKGELLFGTVDSWLVWKLTNGKVHVTDYTNASRTMIFNIKNLEWDERMLKELDIPRSM 161
Cdd:PTZ00294 135 TYFSAFKIRWMLENVPAVKDAVKEGTLLFGTIDTWLIWNLTGGKSHVTDVTNASRTFLMNIKTLKWDEELLNKFGIPKET 214

                        170
                 ....*....|...
gi 311350624 162 LPEVKNSSEIYGY 174
Cdd:PTZ00294 215 LPEIKSSSENFGT 227
PLN02295 PLN02295
glycerol kinase
 20-173 3.04e-73

glycerol kinase


Pssm-ID: 215166 [Multi-domain]  Cd Length: 512  Bit Score: 228.43  E-value: 3.04e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624  20 NIAAIGITNQRETTIVWDKNTGVPIYNAIVWQCRRTADICDEL-KERDGLVDYIRENTGLVLDAYFSGTKIKWILDNVEG 98
Cdd:PLN02295  73 GLKAIGITNQRETTVAWSKSTGRPLYNAIVWMDSRTSSICRRLeKELSGGRKHFVETCGLPISTYFSATKLLWLLENVDA 152

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 311350624  99 AREKAEKGELLFGTVDSWLVWKLTNGK---VHVTDYTNASRTMIFNIKNLEWDERMLKELDIPRSMLPEVKNSSEIYG 173
Cdd:PLN02295 153 VKEAVKSGDALFGTIDSWLIWNLTGGAsggVHVTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIVSNSEVIG 230
FGGY_N pfam00370
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ...
 1-174 4.50e-72

FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the C-terminal domain.


Pssm-ID: 395295 [Multi-domain]  Cd Length: 245  Bit Score: 217.21  E-value: 4.50e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624    1 ATQYSVLQEVMAKCNITQENIAAIGITNQRETTIVWDKNTGvPIYNAIVWQCRRTADICDELKErDGLVDYIRENTGLVL 80
Cdd:pfam00370  50 QAVAQCIAKTLSQLGISLKQIKGIGISNQGHGTVLLDKNDK-PLYNAILWKDRRTAEIVENLKE-EGNNQKLYEITGLPI 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624   81 DAYFSGTKIKWILDNVEGAREKAEKgellFGTVDSWLVWKLTNgkVHVTDYTNASRTMIFNIKNLEWDERMLKELDIPRS 160
Cdd:pfam00370 128 WPGFTLSKLRWIKENEPEVFEKIHK----FLTIHDYLRWRLTG--VFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRD 201

                         170
                  ....*....|....
gi 311350624  161 MLPEVKNSSEIYGY 174
Cdd:pfam00370 202 HLPPLVESSEIYGE 215
ASKHA_NBD_FGGY_GK5-like cd07793
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ...
 4-174 2.53e-58

nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The subfamily corresponds to a group of metazoan putative glycerol kinases (GK), which may be coded by the GK-like gene, GK5. Sequence comparison shows members of this group are homologs of bacterial GKs, and they retain all functionally important residues. However, GK-like proteins in this family do not have detectable GK activity. The reason remains unclear. It has been suggested that the conserved catalytic residues might facilitate them performing a distinct function. GK5 is a skin-specific kinase expressed predominantly in sebaceous glands. It can form a complex with the sterol regulatory element-binding proteins (SREBPs) through their C-terminal regulatory domains, inhibiting SREBP processing and activation. GK5 also promotes gefitinib resistance by inhibiting apoptosis and cell cycle arrest. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466803 [Multi-domain]  Cd Length: 501  Bit Score: 189.31  E-value: 2.53e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624   4 YSVLQEVMAKCNITQENIAAIGITNQRETTIVWDKNTGVPIYNAIVWQCRRTADICDELKER---------DGLVDYIRE 74
Cdd:cd07793   53 VKVIKEALKNAGLTPEDIAAIGISTQRNTFLTWDKKTGKPLHNFITWQDLRAAELCESWNRSlllkalrggSKFLHFLTR 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624  75 NTGLVLDAYFSGT------KIKWILDNVEGAREKAEKGELLFGTVDSWLVWKLTNGKVHVTDYTNASRTMIFNIKNLEWD 148
Cdd:cd07793  133 NKRFLAASVLKFStahvsiRLLWILQNNPELKEAAEKGELLFGTIDTWLLWKLTGGKVHATDYSNASATGLFDPFTLEWS 212

                        170       180
                 ....*....|....*....|....*.
gi 311350624 149 ERMLKELDIPRSMLPEVKNSSEIYGY 174
Cdd:cd07793  213 PILLSLFGIPSSILPEVKDTSGDFGS 238
XylB COG1070
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ...
 5-174 4.77e-43

Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose or hexulose) kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 440688 [Multi-domain]  Cd Length: 494  Bit Score: 149.21  E-value: 4.77e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624   5 SVLQEVMAKCNITQENIAAIGITNQRETTIVWDKNtGVPIYNAIVWQCRRTADICDELKERDGLvDYIRENTGLVLDAYF 84
Cdd:COG1070   55 EAIRELLAKAGVDPEEIAAIGVSGQMHGLVLLDAD-GEPLRPAILWNDTRAAAEAAELREELGE-EALYEITGNPLHPGF 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624  85 SGTKIKWILDNVEGAREKAEKgellFGTVDSWLVWKLTnGKvHVTDYTNASRTMIFNIKNLEWDERMLKELDIPRSMLPE 164
Cdd:COG1070  133 TAPKLLWLKENEPEIFARIAK----VLLPKDYLRYRLT-GE-FVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPE 206

                        170
                 ....*....|
gi 311350624 165 VKNSSEIYGY 174
Cdd:COG1070  207 LVPPGEVAGT 216
ASKHA_NBD_FGGY_FK cd07773
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ...
 5-174 4.87e-38

nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), also called L-fuculose kinase, catalyzes the ATP-dependent phosphorylation of L-fuculose to produce L-fuculose-1-phosphate and ADP. It can also phosphorylate, with lower efficiency, D-ribulose, D-xylulose and D-fructose. The presence of Mg2+ or Mn2+ is required for enzymatic activity. FKs belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466793 [Multi-domain]  Cd Length: 443  Bit Score: 135.02  E-value: 4.87e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624   5 SVLQEVMAKCNitQENIAAIGITNQRETTIVWDKNtGVPIYNAIVWQCRRTADICDELKERDGLvDYIRENTGLVLDAYF 84
Cdd:cd07773   54 EAIREAAAQAG--PDPIAAISVSSQGESGVPVDRD-GEPLGPAIVWFDPRGKEEAEELAERIGA-EELYRITGLPPSPMY 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624  85 SGTKIKWILDNVEGAREKAEKgellFGTVDSWLVWKLTnGKvHVTDYTNASRTMIFNIKNLEWDERMLKELDIPRSMLPE 164
Cdd:cd07773  130 SLAKLLWLREHEPEIFAKAAK----WLSVADYIAYRLT-GE-PVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPE 203

                        170
                 ....*....|
gi 311350624 165 VKNSSEIYGY 174
Cdd:cd07773  204 LVPSGTVIGT 213
ASKHA_NBD_FGGY_EcXK-like cd07808
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ...
 6-174 1.52e-32

nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli xylulose kinase (EcXK). XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. EcXK, also known as 1-deoxy-D-xylulokinase, can also catalyze the phosphorylation of 1-deoxy-D-xylulose to 1-deoxy-D-xylulose 5-phosphate, with lower efficiency. It can also use D-ribulose, xylitol and D-arabitol, but D-xylulose is preferred over the other substrates. EcXK has a weak substrate-independent Mg-ATP-hydrolyzing activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466808 [Multi-domain]  Cd Length: 482  Bit Score: 120.72  E-value: 1.52e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624   6 VLQEVMAKCNITQENIAAIGITNQRETTIVWDKNtGVPIYNAIVWQCRRTADICDELKERDGlvDYIRENTGLVLDAYFS 85
Cdd:cd07808   55 ALRELLAKAGISPSDIAAIGLTGQMHGLVLLDKN-GRPLRPAILWNDQRSAAECEELEARLG--DEILIITGNPPLPGFT 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624  86 GTKIKWILDNVEGAREKAEKgeLLFgTVDsWLVWKLTNgkVHVTDYTNASRTMIFNIKNLEWDERMLKELDIPRSMLPEV 165
Cdd:cd07808  132 LPKLLWLKENEPEIFARIRK--ILL-PKD-YLRYRLTG--ELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPI 205


                 ....*....
gi 311350624 166 KNSSEIYGY 174
Cdd:cd07808  206 VESTEIVGT 214
ASKHA_NBD_FGGY_RrXK-like cd07804
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ...
 4-174 1.38e-30

nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Rhodospirillum rubrum xylulose kinase (RrXK). Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466806 [Multi-domain]  Cd Length: 451  Bit Score: 114.93  E-value: 1.38e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624   4 YSVLQEVMAKCNITQENIAAIGITNQRETTIVWDKNtGVPIYNAIVWQCRRTADICDELKERDGLvDYIRENTGLVLDAY 83
Cdd:cd07804   53 CEIIRELLAKAGISPKEIAAIGVSGLVPALVPVDEN-GKPLRPAILYGDRRATEEIEWLNENIGE-DRIFEITGNPLDSQ 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624  84 FSGTKIKWILDNVEGAREKAEKgellFGTVDSWLVWKLTNgkVHVTDYTNASRTM-IFNIKNLEWDERMLKELDIPRSML 162
Cdd:cd07804  131 SVGPKLLWIKRNEPEVFKKTRK----FLGAYDYIVYKLTG--EYVIDYSSAGNEGgLFDIRKRTWDEELLEALGIDPDLL 204

                        170
                 ....*....|..
gi 311350624 163 PEVKNSSEIYGY 174
Cdd:cd07804  205 PELVPSTEIVGE 216
ASKHA_NBD_FGGY_CvXK-like cd07805
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ...
 8-174 3.07e-30

nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Chromobacterium violaceum xylulose kinase (CvXK). Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466807 [Multi-domain]  Cd Length: 485  Bit Score: 114.54  E-value: 3.07e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624   8 QEVMAKCNITQENIAAIGITNQRETTIVWDKNtGVPIYNAIVWQCRRTADICDELKERDGLVDYIRENTGLVLDAYFSGT 87
Cdd:cd07805   57 RALLEKSGIDPSDIAAIAFSGQMQGVVPVDKD-GNPLRNAIIWSDTRAAEEAEEIAGGLGGIEGYRLGGGNPPSGKDPLA 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624  88 KIKWILDNvegAREKAEKGELLFGTVDsWLVWKLTnGKVhVTDYTNASRTMIFNIKNLEWDERMLKELDIPRSMLPEVKN 167
Cdd:cd07805  136 KILWLKEN---EPEIYAKTHKFLDAKD-YLNFRLT-GRA-ATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVP 209


                 ....*..
gi 311350624 168 SSEIYGY 174
Cdd:cd07805  210 STEVVGE 216
ASKHA_NBD_FGGY_YgcE-like cd07779
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ...
 4-174 4.47e-30

nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli sugar kinase YgcE. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466798 [Multi-domain]  Cd Length: 433  Bit Score: 113.38  E-value: 4.47e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624   4 YSVLQEVMAKCNITQENIAAIGITNQRETTIVWDKNtGVPIYNAIVWQCRRTADICdelkerdglvdyirentglvlday 83
Cdd:cd07779   53 CEALKEAVAKAGVDPEDIAAIGLTSQRSTFVPVDED-GRPLRPAISWQDKRTAKFL------------------------ 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624  84 fsgtkikwildnvegarekaekgellfgTVDSWLVWKLTNgkVHVTDYTNASRTMIFNIKNLEWDERMLKELDIPRSMLP 163
Cdd:cd07779  108 ----------------------------TVQDYLLYRLTG--EFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLP 157

                        170
                 ....*....|.
gi 311350624 164 EVKNSSEIYGY 174
Cdd:cd07779  158 ELVPPGTVIGT 168
ASKHA_NBD_FGGY cd00366
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ...
 5-174 4.46e-29

nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is predominantly composed of glycerol kinase (GK) and similar carbohydrate kinases including rhamnulokinase (RhuK), xylulokinase (XK), gluconokinase (GntK), ribulokinase (RBK), and fuculokinase (FK). These enzymes catalyze the transfer of a phosphate group, usually from ATP, to their carbohydrate substrates. The monomer of FGGY proteins contains two large domains, which are separated by a deep cleft that forms the active site. One domain is primarily involved in sugar substrate binding, and the other is mainly responsible for ATP binding. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. Substrate-induced conformational changes and a divalent cation may be required for the catalytic activity. The FGGY family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466787 [Multi-domain]  Cd Length: 392  Bit Score: 110.35  E-value: 4.46e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624   5 SVLQEVMAKCNITQENIAAIGITNQRETTIVWDKNtGVPIYNAIVWQCRRTAdicdelkerdglvdyirentglvldayf 84
Cdd:cd00366   54 EAIREVLAKAGIDPSDIAAIGISGQMPGVVLVDAD-GNPLRPAIIWLDRRAK---------------------------- 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624  85 sgtkikwildnvegarekaekgellFGTVDSWLVWKLTNgkVHVTDYTNASRTMIFNIKNLEWDERMLKELDIPRSMLPE 164
Cdd:cd00366  105 -------------------------FLQPNDYIVFRLTG--EFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPP 157

                        170
                 ....*....|
gi 311350624 165 VKNSSEIYGY 174
Cdd:cd00366  158 IVESGEVVGR 167
ASKHA_NBD_FGGY_EcLyxK-like cd07802
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ...
 5-174 6.14e-27

nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK; EC 2.7.1.-/EC 2.7.1.53), Pasteurella multocida L-xylulose kinase (PmLyX, also known as L-xylulokinase; EC 2.7.1.53), and Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). EcLyxK catalyzes the phosphorylation of L-xylulose and 3-keto-L-gulonate. It is involved in L-lyxose utilization via xylulose and may also be involved in the utilization of 2,3-diketo-L-gulonate. PmLyX catalyzes the phosphorylation of L-xylulose only. BaEryA catalyzes the phosphorylation of erythritol to D-erythritol-1-phosphate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466805 [Multi-domain]  Cd Length: 444  Bit Score: 104.94  E-value: 6.14e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624   5 SVLQEVMAKCNITQENIAAIGITNQRETTIVWDKNtGVPIYNAIVWQCRRTADICDELKErDGLVDYIRENTGLVLDAYF 84
Cdd:cd07802   54 EAIRELLEKSGVDPSDIAGVGVTGHGNGLYLVDKD-GKPVRNAILSNDSRAADIVDRWEE-DGTLEKVYPLTGQPLWPGQ 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624  85 SGTKIKWILDNvegAREKAEKGELLFGTVDsWLVWKLTnGKVHvTDYTNASrTMIFNIKNLEWDERMLKELDIP--RSML 162
Cdd:cd07802  132 PVALLRWLKEN---EPERYDRIRTVLFCKD-WIRYRLT-GEIS-TDYTDAG-SSLLDLDTGEYDDELLDLLGIEelKDKL 204

                        170
                 ....*....|..
gi 311350624 163 PEVKNSSEIYGY 174
Cdd:cd07802  205 PPLVPSTEIAGR 216
ASKHA_NBD_FGGY_SePSK_AtXK1-like cd07783
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ...
 5-173 6.86e-24

nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), Arabidopsis thaliana xylulose kinase-1 (AtXK-1) and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to Synechococcus elongatus putative sugar kinase (also known as SePSK; D-ribulose kinase; D-ribulokinase) and Arabidopsis thaliana xylulose kinase-1 (also known as AtXK-1; D-ribulose kinase; D-ribulokinase; inactive xylulose kinase 1). Both kinases exhibit ATP hydrolysis without substrate and can phosphorylate D-ribulose. They belong to the ribulokinase-like carbohydrate kinases, a subfamily of FGGY family carbohydrate kinases. Ribulokinase-like carbohydrate kinases are responsible for the phosphorylation of sugars such as L-ribulose and D-ribulose. Their monomers contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466801 [Multi-domain]  Cd Length: 429  Bit Score: 96.52  E-value: 6.86e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624   5 SVLQEVMAKCNITQenIAAIGITNQRETTIVWDKNtGVPIYNAIVWQCRRTADICDELKERDGlvdYIRENTGLVLDAYF 84
Cdd:cd07783   54 SLLRELPAELRPRR--VVAIAVDGTSGTLVLVDRE-GEPLRPAIMYNDARAVAEAEELAEAAG---AVAPRTGLAVSPSS 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624  85 SGTKIKWILDNVEGAREKAEKgeLLFGTvDsWLVWKLTnGKVHVTDYTNASRTMiFNIKNLEWDERMLKELDIPRSMLPE 164
Cdd:cd07783  128 SLAKLLWLKRHEPEVLAKTAK--FLHQA-D-WLAGRLT-GDRGVTDYNNALKLG-YDPETGRWPSWLLALLGIPPDLLPR 201


                 ....*....
gi 311350624 165 VKNSSEIYG 173
Cdd:cd07783  202 VVAPGTVIG 210
ASKHA_NBD_FGGY_YoaC-like cd07798
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ...
 5-173 3.36e-22

nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to Bacillus subtilis sugar kinase YoaC. It is part of the yoaDCB operon and induced by sulfate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466804 [Multi-domain]  Cd Length: 448  Bit Score: 91.90  E-value: 3.36e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624   5 SVLQEVMAKCNITQENIAAIGITNQRETTIVWDKNT----GVP-IYNaivwqcrRTADICDELKERDGLVDYIRenTGLV 79
Cdd:cd07798   56 EAIREALKKAGISPEDISAVSSTSQREGIVFLDKDGrelyAGPnIDA-------RGVEEAAEIDDEFGEEIYTT--TGHW 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624  80 LDAYFSGTKIKWILDNVEGAREKAEKgellFGTVDSWLVWKLTnGKVhVTDYTNASRTMIFNIKNLEWDERMLKELDIPR 159
Cdd:cd07798  127 PTELFPAARLLWFKENRPEIFERIAT----VLSISDWIGYRLT-GEL-VSEPSQASETQLFDIKKREWSQELLEALGLPP 200

                        170
                 ....*....|....
gi 311350624 160 SMLPEVKNSSEIYG 173
Cdd:cd07798  201 EILPEIVPSGTVLG 214
ASKHA_NBD_FGGY_GntK cd07770
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ...
 6-173 4.84e-22

nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7.1.12), also known as gluconokinase, catalyzes the ATP-dependent phosphorylation of D-gluconate and produce 6-phospho-D-gluconate and ADP. The presence of Mg2+ might be required for catalytic activity. The prototypical member of this subfamily is GntK from Lactobacillus acidophilus. Unlike Escherichia coli GntK, which belongs to the superfamily of P-loop containing nucleoside triphosphate hydrolases, Members of this subfamily are homologous to glycerol kinase, xylulose kinase, and rhamnulokinase from Escherichia coli. They have been classified as members of the FGGY family of carbohydrate kinases, which contain two large domains separated by a deep cleft that forms the active site. This model spans both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466790 [Multi-domain]  Cd Length: 478  Bit Score: 91.46  E-value: 4.84e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624   6 VLQEVMAKCNITQenIAAIGITNQRETTIVWDKNtGVPIYNAIVWQCRRTADICDELKERDGLVDyIRENTGLVLDAYFS 85
Cdd:cd07770   55 ALKEVLAKLGGGE--VDAIGFSSAMHSLLGVDED-GEPLTPVITWADTRAAEEAERLRKEGDGSE-LYRRTGCPIHPMYP 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624  86 GTKIKWILDNVEGAREKAEKgellFGTVDSWLVWKLTnGKvHVTDYTNASRTMIFNIKNLEWDERMLKELDIPRSMLPEV 165
Cdd:cd07770  131 LAKLLWLKEERPELFAKAAK----FVSIKEYLLYRLT-GE-LVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPEL 204


                 ....*...
gi 311350624 166 KNSSEIYG 173
Cdd:cd07770  205 VDPTEVLP 212
ASKHA_NBD_FGGY_BaXK-like cd07809
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ...
 5-174 5.66e-19

nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to xylulose kinases (XKs) from Bifidobacterium adolescentis, Streptomyces coelicolor, Actinoplanes missouriensis and Haemophilus influenzae. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466809 [Multi-domain]  Cd Length: 443  Bit Score: 82.98  E-value: 5.66e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624   5 SVLQEVMAKCNITQENIAAIGITNQRETTIVWDKNtGVPIYNAIVWQCRRTADICDELKERDGLVDYIreNTGLVLDAYF 84
Cdd:cd07809   55 AAFAQLLKDAGAELRDVAAIGISGQMHGLVALDAD-GKVLRPAKLWCDTRTAPEAEELTEALGGKKCL--LVGLNIPARF 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624  85 SGTKIKWILDNVEGAREKAEKGELLFGtvdsWLVWKLTNGKVhvTDYTNASRTMIFNIKNLEWDERMLKELD---IPRSM 161
Cdd:cd07809  132 TASKLLWLKENEPEHYARIAKILLPHD----YLNWKLTGEKV--TGLGDASGTFPIDPRTRDYDAELLAAIDpsrDLRDL 205

                        170
                 ....*....|...
gi 311350624 162 LPEVKNSSEIYGY 174
Cdd:cd07809  206 LPEVLPAGEVAGR 218
ASKHA_NBD_FGGY_SHK cd07777
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ...
 4-174 9.86e-19

nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1.14), also called heptulokinase, or carbohydrate kinase-like protein (CARKL), is encoded by the carbohydrate kinase-like (CARKL/SHPK) gene. It acts as a modulator of macrophage activation through control of glucose metabolism. SHK catalyzes the ATP-dependent phosphorylation of sedoheptulose to produce sedoheptulose 7-phosphate and ADP. The presence of Mg2+ or Mn2+ might be required for catalytic activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466796 [Multi-domain]  Cd Length: 436  Bit Score: 82.27  E-value: 9.86e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624   4 YSVLQEVMAK-CNITQENIAAIGITNQRETTIVWDKNtGVPIYNAIVWQCRRtadiCDElKERDGLVDYIRE---NTGLV 79
Cdd:cd07777   52 LEAVRNLIDElPREYLSDVTGIGITGQMHGIVLWDED-GNPVSPLITWQDQR----CSE-EFLGGLSTYGEEllpKSGMR 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624  80 LDAYFSGTKIKWILDNvegarEKAEKGELLFGTVDSWLVWKLTNGKVHVTDYTNASRTMIFNIKNLEWDERMLKELDIPR 159
Cdd:cd07777  126 LKPGYGLATLFWLLRN-----GPLPSKADRAGTIGDYIVARLTGLPKPVMHPTNAASWGLFDLETGTWNKDLLEALGLPV 200

                        170
                 ....*....|....*
gi 311350624 160 SMLPEVKNSSEIYGY 174
Cdd:cd07777  201 ILLPEIVPSGEIVGT 215
ASKHA_NBD_FGGY_BaEryA-like cd24121
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ...
 6-174 5.26e-17

nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). It catalyzes the phosphorylation of erythritol to D-erythritol-1-phosphate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466971 [Multi-domain]  Cd Length: 452  Bit Score: 77.28  E-value: 5.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624   6 VLQEVMAKCNITQENIAAIGITNQRETTIVWDKNtGVPIYNAIVWQCRRTADICDELkERDGLVDYIRENTGLVLDAYFS 85
Cdd:cd24121   55 TIREVVAKLDVLPDRVAAIGVTGQGDGTWLVDED-GRPVRDAILWLDGRAADIVERW-QADGIAEAVFEITGTGLFPGSQ 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624  86 GTKIKWILDNvegAREKAEKGELLFGTVDsWLVWKLTnGKVhVTDYTNASRTMiFNIKNLEWDERMLKELDIP--RSMLP 163
Cdd:cd24121  133 AAQLAWLKEN---EPERLERARTALHCKD-WLFYKLT-GEI-ATDPSDASLTF-LDFRTRQYDDEVLDLLGLEelRHLLP 205

                        170
                 ....*....|.
gi 311350624 164 EVKNSSEIYGY 174
Cdd:cd24121  206 PIRPGTEVIGP 216
ASKHA_NBD_FGGY_AI-2K cd07775
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ...
 5-174 6.28e-14

nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; AI-2 kinase (EC 2.7.1.189), also known as LsrK, catalyzes the phosphorylation of autoinducer-2 (AI-2) to phospho-AI-2, which subsequently inactivates the transcriptional regulator LsrR and leads to the transcription of the lsr operon. It phosphorylates the ring-open form of (S)-4,5-dihydroxypentane-2,3-dione (DPD), which is the precursor to all AI-2 signaling molecules, at the C5 position. It is required for the regulation of the lsr operon and many other genes. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466794 [Multi-domain]  Cd Length: 492  Bit Score: 68.51  E-value: 6.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624   5 SVLQEVMAKCNITQENIAAIGITNQRETTIVWDKNtGVPIynaivWQCR----RTADICDELKE-RDGLVDYIRENTG-- 77
Cdd:cd07775   56 ECIREALKKAGIAPKSIAAISTTSMREGIVLYDNE-GEEI-----WACAnvdaRAAEEVSELKElYNTLEEEVYRISGqt 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624  78 LVLDAyfsGTKIKWILDNVEGAREKAEKgellFGTVDSWLVWKLTnGKVhVTDYTNASRTMIFNIKNLEWDERMLKELDI 157
Cdd:cd07775  130 FALGA---IPRLLWLKNNRPEIYRKAAK----ITMLSDWIAYKLS-GEL-AVEPSNGSTTGLFDLKTRDWDPEILEMAGL 200

                        170
                 ....*....|....*..
gi 311350624 158 PRSMLPEVKNSSEIYGY 174
Cdd:cd07775  201 KADILPPVVESGTVIGK 217
PRK10939 PRK10939
autoinducer-2 (AI-2) kinase; Provisional
 7-174 2.65e-11

autoinducer-2 (AI-2) kinase; Provisional


Pssm-ID: 182853 [Multi-domain]  Cd Length: 520  Bit Score: 60.79  E-value: 2.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624   7 LQEVMAKCNITQENIAAIGITNQRETTIVWDKNtGVPIynaivWQC----RRTADICDELKE-RDGLVDYIRENTG--LV 79
Cdd:PRK10939  61 IRQALQKAGIPASDIAAVSATSMREGIVLYDRN-GTEI-----WACanvdARASREVSELKElHNNFEEEVYRCSGqtLA 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624  80 LDAYfsgTKIKWILDNVEGAREKAEKgellFGTVDSWLVWKLTNgkVHVTDYTNASRTMIFNIKNLEWDERMLKELDIPR 159
Cdd:PRK10939 135 LGAL---PRLLWLAHHRPDIYRQAHT----ITMISDWIAYMLSG--ELAVDPSNAGTTGLLDLVTRDWDPALLEMAGLRA 205

                        170
                 ....*....|....*
gi 311350624 160 SMLPEVKNSSEIYGY 174
Cdd:PRK10939 206 DILPPVKETGTVLGH 220
ASKHA_NBD_FGGY_RhaB-like cd07771
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ...
 117-173 1.05e-10

nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase (EC 2.7.1.5), also known as L-rhamnulose kinase, ATP:L-rhamnulose phosphotransferase, L-rhamnulose 1-kinase, or rhamnulose kinase, is an enzyme involved in the second step in rhamnose catabolism. It catalyzes the ATP-dependent phosphorylation of L-rhamnulose to produce L-rhamnulose-1-phosphate and ADP. Rhamnulokinase exists as a monomer composed of two large domains. The ATP binding site is located in the cleft between the two domains. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The presence of divalent Mg2+ or Mn2+ is required for catalysis. The subfamily also includes Streptococcus pneumoniae L-fuculose k fuculose Kinase inase (FcsK) that uses ATP to phosphorylate fuculose creating fuculose-1-phosphate, and Alkalihalobacillus clausii bifunctional enzyme RhaA/RhaB. Members of this subfamily belong to the FGGY family of carbohydrate kinases.


Pssm-ID: 466791 [Multi-domain]  Cd Length: 460  Bit Score: 59.08  E-value: 1.05e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 311350624 117 LVWKLTnGKVhVTDYTNASRTMIFNIKNLEWDERMLKELDIPRSMLPEVKNSSEIYG 173
Cdd:cd07771  158 LNYLLT-GEK-VAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIVPPGTVLG 212
PRK15027 PRK15027
xylulokinase; Provisional
 19-173 2.58e-09

xylulokinase; Provisional


Pssm-ID: 184987 [Multi-domain]  Cd Length: 484  Bit Score: 54.97  E-value: 2.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624  19 ENIAAIGITNQRETTIVWDKNTGVpIYNAIVWQCRRTADICDELKERdglVDYIRENTGLVLDAYFSGTKIKWIldnveg 98
Cdd:PRK15027  66 QDVKALGIAGQMHGATLLDAQQRV-LRPAILWNDGRCAQECALLEAR---VPQSRVITGNLMMPGFTAPKLLWV------ 135

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 311350624  99 AREKAEkgelLFGTVDSWLVWK----LTNGKVHVTDYTNASRTMIFNIKNLEWDERMLKELDIPRSMLPEVKNSSEIYG 173
Cdd:PRK15027 136 QRHEPE----IFRQIDKVLLPKdylrLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEITG 210
PRK10331 PRK10331
L-fuculokinase; Provisional
 15-173 1.65e-07

L-fuculokinase; Provisional


Pssm-ID: 182383 [Multi-domain]  Cd Length: 470  Bit Score: 49.64  E-value: 1.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624  15 NITQENIAAIGITNQRETTIVWDKNtGVPIYNAIVWQCRRTADICDEL-KERDGLVDYIRENTGlvldAYFSGT--KIKW 91
Cdd:PRK10331  66 ELTECHIRGITVTTFGVDGALVDKQ-GNLLYPIISWKCPRTAAVMENIeRYISAQQLQQISGVG----AFSFNTlyKLVW 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624  92 ILDNVEGAREKAEKgeLLFgtVDSWLVWKLTNgkVHVTDYTNASRTMIFNIKNLEWDERMLKELDIPRSMLPEVKNSSEI 171
Cdd:PRK10331 141 LKENHPQLLEQAHA--WLF--ISSLINHRLTG--EFTTDITMAGTSQMLDIQQRDFSPEILQATGLSRRLFPRLVEAGEQ 214


                 ..
gi 311350624 172 YG 173
Cdd:PRK10331 215 IG 216
ASKHA_NBD_FGGY_L-RBK cd07781
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ...
 4-174 1.47e-03

nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466799 [Multi-domain]  Cd Length: 504  Bit Score: 38.29  E-value: 1.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624   4 YSVLQEVMAKCNITQENIAAIGITNQRETTIVWDKNtGVPIYNAIVW-------QCRRTADICDELKERDGlvdyirent 76
Cdd:cd07781   56 EEAVRGALAEAGVDPEDVVGIGVDTTSSTVVPVDED-GNPLAPAILWmdhraqeEAAEINETAHPALEYYL--------- 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 311350624  77 glvldAYFSGT--------KIKWILDNVEGAREKAEK-GELlfgtVDsWLVWKLTNGKVhvtdytnASRTM-----IFNI 142
Cdd:cd07781  126 -----AYYGGVyssewmwpKALWLKRNAPEVYDAAYTiVEA----CD-WINARLTGRWV-------RSRCAaghkwMYNE 188

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 311350624 143 KNLEWDERMLKELD-----IPRSMLPEVKNSSEIYGY 174
Cdd:cd07781  189 WGGGPPREFLAALDpgllkLREKLPGEVVPVGEPAGT 225
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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