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Conserved domains on  [gi|568956638|ref|XP_006530983|]
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L-fucose kinase isoform X2 [Mus musculus]

Protein Classification

LbetaH and fkp superfamily-containing protein( domain architecture ID 1008129)

LbetaH and fkp superfamily-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
fkp super family cl36248
bifunctional fucokinase/L-fucose-1-P-guanylyltransferase; Provisional
336-719 1.52e-55

bifunctional fucokinase/L-fucose-1-P-guanylyltransferase; Provisional


The actual alignment was detected with superfamily member PRK13412:

Pssm-ID: 237379 [Multi-domain]  Cd Length: 974  Bit Score: 206.22  E-value: 1.52e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956638 336 PALLVRAARHYEGAEQILIRQAVMTARHFVSTQPVELPAPGQWVVTECPARVDFSGGWSDTPPIAYELGGAVLGLAVRVD 415
Cdd:PRK13412 567 LKLSGARYREEEQAAFRLLRDGLLDGAYPRKQTPKLEVYSDQIVWGRSPVRIDLAGGWTDTPPYCLYSGGNVVNLAIELN 646
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956638 416 GRRPIGAKARRIPEPELWLavgpRQDEMTMRIVCRSLDDLRDYCQPHAPGALLKAAFICAGIVHLHSELPL--LEQLLHS 493
Cdd:PRK13412 647 GQPPLQVYVKPCSEPHIVL----RSIDLGAMEVVRTNEELRDYKKVGSPFSIPKAALCLAGFAPRFSAESYasLEEQLKA 722
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956638 494 FNGGFELHTWSELPHGSGLGTSSILAGAALAALQRAAGRAVGTEALIHAVLHLEQVLTTGGGWQDQVSGLMPGIKV---G 570
Cdd:PRK13412 723 FGSGIEITLLAAIPAGSGLGTSSILAATVLGAISDFCGLAWDKNEICNRTLVLEQLLTTGGGWQDQYGGVLPGVKLlqtG 802
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956638 571 RSRAQLPLkveveeitvpegfVQKINDHL----------LLVYTGKTRLARNLLQDVLRNWYARLPVVVQNARRLVRQTE 640
Cdd:PRK13412 803 AGFAQSPL-------------VRWLPDSLftqpeyrdchLLYYTGITRTAKGILAEIVRSMFLNSTAHLQLLHEMKAHAL 869
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568956638 641 KCAEAFRQGNLPLLGQYLTSYWEQKKLMAPGCEPLAVQRMMDVLAPYAYGQSLAGAGGGGFLYLLTKEPRQKETLEAVL 719
Cdd:PRK13412 870 DMYEAIQRGEFEEFGRLVGKTWEQNKALDSGTNPAAVEAIIELIKDYTLGYKLPGAGGGGYLYMVAKDPGAAERIRKIL 948
Fucokinase super family cl37763
L-fucokinase; In the salvage pathway of GDP-L-fucose, free cytosolic fucose is phosphorylated ...
22-168 4.14e-46

L-fucokinase; In the salvage pathway of GDP-L-fucose, free cytosolic fucose is phosphorylated by L-fucokinase to form L-fucose-L-phosphate, which is then further converted to GDP-L-fucose in the reaction catalyzed by GDP-L-fucose pyrophosphorylase.


The actual alignment was detected with superfamily member pfam07959:

Pssm-ID: 462323  Cd Length: 405  Bit Score: 169.75  E-value: 4.14e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956638   22 IVHSQVEEPQLLEATCSVVSCLLEGPVHLGPRSVLQHCHLRGPIRIGAGCFVSGLDTAHSEAlhGLELH-DVILQGHHVR 100
Cdd:pfam07959 258 TAFSVIANARQLKAGASVINSVLEPGVSVGPGSVIEYCHLGGPVSIGSGCILSGLDLSSSLA--RLELPdDTFLHTLPLK 335
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568956638  101 LHGSLSRVFTLAGRLDSWERQ---GAGMYLNMSWNEFFKKTGIRDWDLWDPDTPPsDRCLLTARLFPVLHP 168
Cdd:pfam07959 336 LGGGKLYVTVVFGIHDNLKSSvsdGNLTFLGKPLEDFLSLTGIQPEDLWFSGEPR-EKSLWNARLFPVCHD 405
 
Name Accession Description Interval E-value
fkp PRK13412
bifunctional fucokinase/L-fucose-1-P-guanylyltransferase; Provisional
336-719 1.52e-55

bifunctional fucokinase/L-fucose-1-P-guanylyltransferase; Provisional


Pssm-ID: 237379 [Multi-domain]  Cd Length: 974  Bit Score: 206.22  E-value: 1.52e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956638 336 PALLVRAARHYEGAEQILIRQAVMTARHFVSTQPVELPAPGQWVVTECPARVDFSGGWSDTPPIAYELGGAVLGLAVRVD 415
Cdd:PRK13412 567 LKLSGARYREEEQAAFRLLRDGLLDGAYPRKQTPKLEVYSDQIVWGRSPVRIDLAGGWTDTPPYCLYSGGNVVNLAIELN 646
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956638 416 GRRPIGAKARRIPEPELWLavgpRQDEMTMRIVCRSLDDLRDYCQPHAPGALLKAAFICAGIVHLHSELPL--LEQLLHS 493
Cdd:PRK13412 647 GQPPLQVYVKPCSEPHIVL----RSIDLGAMEVVRTNEELRDYKKVGSPFSIPKAALCLAGFAPRFSAESYasLEEQLKA 722
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956638 494 FNGGFELHTWSELPHGSGLGTSSILAGAALAALQRAAGRAVGTEALIHAVLHLEQVLTTGGGWQDQVSGLMPGIKV---G 570
Cdd:PRK13412 723 FGSGIEITLLAAIPAGSGLGTSSILAATVLGAISDFCGLAWDKNEICNRTLVLEQLLTTGGGWQDQYGGVLPGVKLlqtG 802
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956638 571 RSRAQLPLkveveeitvpegfVQKINDHL----------LLVYTGKTRLARNLLQDVLRNWYARLPVVVQNARRLVRQTE 640
Cdd:PRK13412 803 AGFAQSPL-------------VRWLPDSLftqpeyrdchLLYYTGITRTAKGILAEIVRSMFLNSTAHLQLLHEMKAHAL 869
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568956638 641 KCAEAFRQGNLPLLGQYLTSYWEQKKLMAPGCEPLAVQRMMDVLAPYAYGQSLAGAGGGGFLYLLTKEPRQKETLEAVL 719
Cdd:PRK13412 870 DMYEAIQRGEFEEFGRLVGKTWEQNKALDSGTNPAAVEAIIELIKDYTLGYKLPGAGGGGYLYMVAKDPGAAERIRKIL 948
Fucokinase pfam07959
L-fucokinase; In the salvage pathway of GDP-L-fucose, free cytosolic fucose is phosphorylated ...
22-168 4.14e-46

L-fucokinase; In the salvage pathway of GDP-L-fucose, free cytosolic fucose is phosphorylated by L-fucokinase to form L-fucose-L-phosphate, which is then further converted to GDP-L-fucose in the reaction catalyzed by GDP-L-fucose pyrophosphorylase.


Pssm-ID: 462323  Cd Length: 405  Bit Score: 169.75  E-value: 4.14e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956638   22 IVHSQVEEPQLLEATCSVVSCLLEGPVHLGPRSVLQHCHLRGPIRIGAGCFVSGLDTAHSEAlhGLELH-DVILQGHHVR 100
Cdd:pfam07959 258 TAFSVIANARQLKAGASVINSVLEPGVSVGPGSVIEYCHLGGPVSIGSGCILSGLDLSSSLA--RLELPdDTFLHTLPLK 335
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568956638  101 LHGSLSRVFTLAGRLDSWERQ---GAGMYLNMSWNEFFKKTGIRDWDLWDPDTPPsDRCLLTARLFPVLHP 168
Cdd:pfam07959 336 LGGGKLYVTVVFGIHDNLKSSvsdGNLTFLGKPLEDFLSLTGIQPEDLWFSGEPR-EKSLWNARLFPVCHD 405
COG2605 COG2605
Predicted kinase related to galactokinase and mevalonate kinase [General function prediction ...
379-740 3.49e-37

Predicted kinase related to galactokinase and mevalonate kinase [General function prediction only];


Pssm-ID: 442017 [Multi-domain]  Cd Length: 328  Bit Score: 142.24  E-value: 3.49e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956638 379 VVTECPARVDFSGGWSDTPPIAYELGGAVLGLAVrvdgrrpigakARRIpepelWLAVGPRQDEmtmRIVCRSLDdlrdy 458
Cdd:COG2605    1 IISRAPLRISFAGGGTDLPPYYLEHGGAVLNAAI-----------DKYA-----YVTLEPRFDG---KIRLSSSD----- 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956638 459 cqphapgaLLKAAFICAGIVHLHselPLLEQLLHSFN--GGFELHTWSELPHGSGLGTSSILAGAALAALQRAAGRAVGT 536
Cdd:COG2605   57 --------TERVETVDEDDDIPH---PVIREALKLFGigDGLEITTDSDAPAGSGLGSSSALTVALLNALHALLGLPLSP 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956638 537 EALIHAVLHLEQ-VLTTGGGWQDQVSGLMPGIKVGRSRAQlpLKVEVEEITVPEGFVQKINDHLLLVYTGKTRLARNLLQ 615
Cdd:COG2605  126 YDLARLAYEIERnDLGEPGGKQDQYAAAFGGFNFIEFGPD--GRVIVNPLRISPEILNELESNLLLFYTGITRESSDILK 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956638 616 DVLRNWYARLPVVVQNARRLVRQTEKCAEAFRQGNLPLLGQYLTSYWEQKKLMAPGCEPLAVQRMMDV-LAPYAYGQSLA 694
Cdd:COG2605  204 EQVKNVEDGDEATLEALHEMKELALEMKEALLKGDLDEFGELLNEGWELKKRLASGISNPAIDEIYELaRKAGALGGKLL 283
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 568956638 695 GAGGGGFLYLLTKEPRQKETLEAvLAKAEGLgnysVHLVEVDPQGL 740
Cdd:COG2605  284 GAGGGGFLLFYAPPERREAVREA-LSKAGLR----VVPFSFDKEGS 324
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
46-103 5.88e-03

Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), Ferripyochelin Binding Protein (FBP), E. coli paaY protein, and similar proteins. CAs are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Gamma CAs are trimeric enzymes with left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100051 [Multi-domain]  Cd Length: 153  Bit Score: 38.16  E-value: 5.88e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568956638  46 GPVHLGPR-SVLQHCHLRG---PIRIGAGCFVSGLDTAHSEALHGLELHDVILQGHHVRLHG 103
Cdd:cd04645   16 GDVTLGEGsSVWFGAVLRGdvnPIRIGERTNIQDGSVLHVDPGYPTIIGDNVTVGHGAVLHG 77
 
Name Accession Description Interval E-value
fkp PRK13412
bifunctional fucokinase/L-fucose-1-P-guanylyltransferase; Provisional
336-719 1.52e-55

bifunctional fucokinase/L-fucose-1-P-guanylyltransferase; Provisional


Pssm-ID: 237379 [Multi-domain]  Cd Length: 974  Bit Score: 206.22  E-value: 1.52e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956638 336 PALLVRAARHYEGAEQILIRQAVMTARHFVSTQPVELPAPGQWVVTECPARVDFSGGWSDTPPIAYELGGAVLGLAVRVD 415
Cdd:PRK13412 567 LKLSGARYREEEQAAFRLLRDGLLDGAYPRKQTPKLEVYSDQIVWGRSPVRIDLAGGWTDTPPYCLYSGGNVVNLAIELN 646
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956638 416 GRRPIGAKARRIPEPELWLavgpRQDEMTMRIVCRSLDDLRDYCQPHAPGALLKAAFICAGIVHLHSELPL--LEQLLHS 493
Cdd:PRK13412 647 GQPPLQVYVKPCSEPHIVL----RSIDLGAMEVVRTNEELRDYKKVGSPFSIPKAALCLAGFAPRFSAESYasLEEQLKA 722
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956638 494 FNGGFELHTWSELPHGSGLGTSSILAGAALAALQRAAGRAVGTEALIHAVLHLEQVLTTGGGWQDQVSGLMPGIKV---G 570
Cdd:PRK13412 723 FGSGIEITLLAAIPAGSGLGTSSILAATVLGAISDFCGLAWDKNEICNRTLVLEQLLTTGGGWQDQYGGVLPGVKLlqtG 802
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956638 571 RSRAQLPLkveveeitvpegfVQKINDHL----------LLVYTGKTRLARNLLQDVLRNWYARLPVVVQNARRLVRQTE 640
Cdd:PRK13412 803 AGFAQSPL-------------VRWLPDSLftqpeyrdchLLYYTGITRTAKGILAEIVRSMFLNSTAHLQLLHEMKAHAL 869
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568956638 641 KCAEAFRQGNLPLLGQYLTSYWEQKKLMAPGCEPLAVQRMMDVLAPYAYGQSLAGAGGGGFLYLLTKEPRQKETLEAVL 719
Cdd:PRK13412 870 DMYEAIQRGEFEEFGRLVGKTWEQNKALDSGTNPAAVEAIIELIKDYTLGYKLPGAGGGGYLYMVAKDPGAAERIRKIL 948
Fucokinase pfam07959
L-fucokinase; In the salvage pathway of GDP-L-fucose, free cytosolic fucose is phosphorylated ...
22-168 4.14e-46

L-fucokinase; In the salvage pathway of GDP-L-fucose, free cytosolic fucose is phosphorylated by L-fucokinase to form L-fucose-L-phosphate, which is then further converted to GDP-L-fucose in the reaction catalyzed by GDP-L-fucose pyrophosphorylase.


Pssm-ID: 462323  Cd Length: 405  Bit Score: 169.75  E-value: 4.14e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956638   22 IVHSQVEEPQLLEATCSVVSCLLEGPVHLGPRSVLQHCHLRGPIRIGAGCFVSGLDTAHSEAlhGLELH-DVILQGHHVR 100
Cdd:pfam07959 258 TAFSVIANARQLKAGASVINSVLEPGVSVGPGSVIEYCHLGGPVSIGSGCILSGLDLSSSLA--RLELPdDTFLHTLPLK 335
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568956638  101 LHGSLSRVFTLAGRLDSWERQ---GAGMYLNMSWNEFFKKTGIRDWDLWDPDTPPsDRCLLTARLFPVLHP 168
Cdd:pfam07959 336 LGGGKLYVTVVFGIHDNLKSSvsdGNLTFLGKPLEDFLSLTGIQPEDLWFSGEPR-EKSLWNARLFPVCHD 405
COG2605 COG2605
Predicted kinase related to galactokinase and mevalonate kinase [General function prediction ...
379-740 3.49e-37

Predicted kinase related to galactokinase and mevalonate kinase [General function prediction only];


Pssm-ID: 442017 [Multi-domain]  Cd Length: 328  Bit Score: 142.24  E-value: 3.49e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956638 379 VVTECPARVDFSGGWSDTPPIAYELGGAVLGLAVrvdgrrpigakARRIpepelWLAVGPRQDEmtmRIVCRSLDdlrdy 458
Cdd:COG2605    1 IISRAPLRISFAGGGTDLPPYYLEHGGAVLNAAI-----------DKYA-----YVTLEPRFDG---KIRLSSSD----- 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956638 459 cqphapgaLLKAAFICAGIVHLHselPLLEQLLHSFN--GGFELHTWSELPHGSGLGTSSILAGAALAALQRAAGRAVGT 536
Cdd:COG2605   57 --------TERVETVDEDDDIPH---PVIREALKLFGigDGLEITTDSDAPAGSGLGSSSALTVALLNALHALLGLPLSP 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956638 537 EALIHAVLHLEQ-VLTTGGGWQDQVSGLMPGIKVGRSRAQlpLKVEVEEITVPEGFVQKINDHLLLVYTGKTRLARNLLQ 615
Cdd:COG2605  126 YDLARLAYEIERnDLGEPGGKQDQYAAAFGGFNFIEFGPD--GRVIVNPLRISPEILNELESNLLLFYTGITRESSDILK 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568956638 616 DVLRNWYARLPVVVQNARRLVRQTEKCAEAFRQGNLPLLGQYLTSYWEQKKLMAPGCEPLAVQRMMDV-LAPYAYGQSLA 694
Cdd:COG2605  204 EQVKNVEDGDEATLEALHEMKELALEMKEALLKGDLDEFGELLNEGWELKKRLASGISNPAIDEIYELaRKAGALGGKLL 283
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 568956638 695 GAGGGGFLYLLTKEPRQKETLEAvLAKAEGLgnysVHLVEVDPQGL 740
Cdd:COG2605  284 GAGGGGFLLFYAPPERREAVREA-LSKAGLR----VVPFSFDKEGS 324
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
46-103 5.88e-03

Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), Ferripyochelin Binding Protein (FBP), E. coli paaY protein, and similar proteins. CAs are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Gamma CAs are trimeric enzymes with left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100051 [Multi-domain]  Cd Length: 153  Bit Score: 38.16  E-value: 5.88e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568956638  46 GPVHLGPR-SVLQHCHLRG---PIRIGAGCFVSGLDTAHSEALHGLELHDVILQGHHVRLHG 103
Cdd:cd04645   16 GDVTLGEGsSVWFGAVLRGdvnPIRIGERTNIQDGSVLHVDPGYPTIIGDNVTVGHGAVLHG 77
 
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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