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Conserved domains on  [gi|1720427245|ref|XP_030099371|]
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L-fucose kinase isoform X3 [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
212-595 2.98e-56

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: 205.84  E-value: 2.98e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427245 212 PALLVRAARHYEGAEQILIRQAVMTARHFVSTQPVELPAPGQWVVTECPARVDFSGGWSDTPPIAYELGGAVLGLAVRVD 291
Cdd:PRK13412  567 LKLSGARYREEEQAAFRLLRDGLLDGAYPRKQTPKLEVYSDQIVWGRSPVRIDLAGGWTDTPPYCLYSGGNVVNLAIELN 646
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427245 292 GRRPIGAKARRIPEPELWLavgpRQDEMTMRIVCRSLDDLRDYCQPHAPGALLKAAFICAGIVHLHSELPL--LEQLLHS 369
Cdd:PRK13412  647 GQPPLQVYVKPCSEPHIVL----RSIDLGAMEVVRTNEELRDYKKVGSPFSIPKAALCLAGFAPRFSAESYasLEEQLKA 722
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427245 370 FNGGFELHTWSELPHGSGLGTSSILAGAALAALQRAAGRAVGTEALIHAVLHLEQVLTTGGGWQDQVSGLMPGIKV---G 446
Cdd:PRK13412  723 FGSGIEITLLAAIPAGSGLGTSSILAATVLGAISDFCGLAWDKNEICNRTLVLEQLLTTGGGWQDQYGGVLPGVKLlqtG 802
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427245 447 RSRAQLPLkveveeitvpegfVQKINDHL----------LLVYTGKTRLARNLLQDVLRNWYARLPVVVQNARRLVRQTE 516
Cdd:PRK13412  803 AGFAQSPL-------------VRWLPDSLftqpeyrdchLLYYTGITRTAKGILAEIVRSMFLNSTAHLQLLHEMKAHAL 869
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720427245 517 KCAEAFRQGNLPLLGQYLTSYWEQKKLMAPGCEPLAVQRMMDVLAPYAYGQSLAGAGGGGFLYLLTKEPRQKETLEAVL 595
Cdd:PRK13412  870 DMYEAIQRGEFEEFGRLVGKTWEQNKALDSGTNPAAVEAIIELIKDYTLGYKLPGAGGGGYLYMVAKDPGAAERIRKIL 948
Fucokinase super family cl37763
L-fucokinase; In the salvage pathway of GDP-L-fucose, free cytosolic fucose is phosphorylated ...
2-44 5.01e-13

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: 71.14  E-value: 5.01e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1720427245   2 YLNMSWNEFFKKTGIRDWDLWDPDTPPsDRCLLTARLFPVLHP 44
Cdd:pfam07959 364 FLGKPLEDFLSLTGIQPEDLWFSGEPR-EKSLWNARLFPVCHD 405
 
Name Accession Description Interval E-value
fkp PRK13412
bifunctional fucokinase/L-fucose-1-P-guanylyltransferase; Provisional
212-595 2.98e-56

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


Pssm-ID: 237379 [Multi-domain]  Cd Length: 974  Bit Score: 205.84  E-value: 2.98e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427245 212 PALLVRAARHYEGAEQILIRQAVMTARHFVSTQPVELPAPGQWVVTECPARVDFSGGWSDTPPIAYELGGAVLGLAVRVD 291
Cdd:PRK13412  567 LKLSGARYREEEQAAFRLLRDGLLDGAYPRKQTPKLEVYSDQIVWGRSPVRIDLAGGWTDTPPYCLYSGGNVVNLAIELN 646
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427245 292 GRRPIGAKARRIPEPELWLavgpRQDEMTMRIVCRSLDDLRDYCQPHAPGALLKAAFICAGIVHLHSELPL--LEQLLHS 369
Cdd:PRK13412  647 GQPPLQVYVKPCSEPHIVL----RSIDLGAMEVVRTNEELRDYKKVGSPFSIPKAALCLAGFAPRFSAESYasLEEQLKA 722
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427245 370 FNGGFELHTWSELPHGSGLGTSSILAGAALAALQRAAGRAVGTEALIHAVLHLEQVLTTGGGWQDQVSGLMPGIKV---G 446
Cdd:PRK13412  723 FGSGIEITLLAAIPAGSGLGTSSILAATVLGAISDFCGLAWDKNEICNRTLVLEQLLTTGGGWQDQYGGVLPGVKLlqtG 802
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427245 447 RSRAQLPLkveveeitvpegfVQKINDHL----------LLVYTGKTRLARNLLQDVLRNWYARLPVVVQNARRLVRQTE 516
Cdd:PRK13412  803 AGFAQSPL-------------VRWLPDSLftqpeyrdchLLYYTGITRTAKGILAEIVRSMFLNSTAHLQLLHEMKAHAL 869
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720427245 517 KCAEAFRQGNLPLLGQYLTSYWEQKKLMAPGCEPLAVQRMMDVLAPYAYGQSLAGAGGGGFLYLLTKEPRQKETLEAVL 595
Cdd:PRK13412  870 DMYEAIQRGEFEEFGRLVGKTWEQNKALDSGTNPAAVEAIIELIKDYTLGYKLPGAGGGGYLYMVAKDPGAAERIRKIL 948
COG2605 COG2605
Predicted kinase related to galactokinase and mevalonate kinase [General function prediction ...
255-616 1.45e-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: 1.45e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427245 255 VVTECPARVDFSGGWSDTPPIAYELGGAVLGLAVrvdgrrpigakARRIpepelWLAVGPRQDEmtmRIVCRSLDdlrdy 334
Cdd:COG2605     1 IISRAPLRISFAGGGTDLPPYYLEHGGAVLNAAI-----------DKYA-----YVTLEPRFDG---KIRLSSSD----- 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427245 335 cqphapgaLLKAAFICAGIVHLHselPLLEQLLHSFN--GGFELHTWSELPHGSGLGTSSILAGAALAALQRAAGRAVGT 412
Cdd:COG2605    57 --------TERVETVDEDDDIPH---PVIREALKLFGigDGLEITTDSDAPAGSGLGSSSALTVALLNALHALLGLPLSP 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427245 413 EALIHAVLHLEQ-VLTTGGGWQDQVSGLMPGIKVGRSRAQlpLKVEVEEITVPEGFVQKINDHLLLVYTGKTRLARNLLQ 491
Cdd:COG2605   126 YDLARLAYEIERnDLGEPGGKQDQYAAAFGGFNFIEFGPD--GRVIVNPLRISPEILNELESNLLLFYTGITRESSDILK 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427245 492 DVLRNWYARLPVVVQNARRLVRQTEKCAEAFRQGNLPLLGQYLTSYWEQKKLMAPGCEPLAVQRMMDV-LAPYAYGQSLA 570
Cdd:COG2605   204 EQVKNVEDGDEATLEALHEMKELALEMKEALLKGDLDEFGELLNEGWELKKRLASGISNPAIDEIYELaRKAGALGGKLL 283
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1720427245 571 GAGGGGFLYLLTKEPRQKETLEAvLAKAEGLgnysVHLVEVDPQGL 616
Cdd:COG2605   284 GAGGGGFLLFYAPPERREAVREA-LSKAGLR----VVPFSFDKEGS 324
Fucokinase pfam07959
L-fucokinase; In the salvage pathway of GDP-L-fucose, free cytosolic fucose is phosphorylated ...
2-44 5.01e-13

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: 71.14  E-value: 5.01e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1720427245   2 YLNMSWNEFFKKTGIRDWDLWDPDTPPsDRCLLTARLFPVLHP 44
Cdd:pfam07959 364 FLGKPLEDFLSLTGIQPEDLWFSGEPR-EKSLWNARLFPVCHD 405
 
Name Accession Description Interval E-value
fkp PRK13412
bifunctional fucokinase/L-fucose-1-P-guanylyltransferase; Provisional
212-595 2.98e-56

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


Pssm-ID: 237379 [Multi-domain]  Cd Length: 974  Bit Score: 205.84  E-value: 2.98e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427245 212 PALLVRAARHYEGAEQILIRQAVMTARHFVSTQPVELPAPGQWVVTECPARVDFSGGWSDTPPIAYELGGAVLGLAVRVD 291
Cdd:PRK13412  567 LKLSGARYREEEQAAFRLLRDGLLDGAYPRKQTPKLEVYSDQIVWGRSPVRIDLAGGWTDTPPYCLYSGGNVVNLAIELN 646
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427245 292 GRRPIGAKARRIPEPELWLavgpRQDEMTMRIVCRSLDDLRDYCQPHAPGALLKAAFICAGIVHLHSELPL--LEQLLHS 369
Cdd:PRK13412  647 GQPPLQVYVKPCSEPHIVL----RSIDLGAMEVVRTNEELRDYKKVGSPFSIPKAALCLAGFAPRFSAESYasLEEQLKA 722
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427245 370 FNGGFELHTWSELPHGSGLGTSSILAGAALAALQRAAGRAVGTEALIHAVLHLEQVLTTGGGWQDQVSGLMPGIKV---G 446
Cdd:PRK13412  723 FGSGIEITLLAAIPAGSGLGTSSILAATVLGAISDFCGLAWDKNEICNRTLVLEQLLTTGGGWQDQYGGVLPGVKLlqtG 802
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427245 447 RSRAQLPLkveveeitvpegfVQKINDHL----------LLVYTGKTRLARNLLQDVLRNWYARLPVVVQNARRLVRQTE 516
Cdd:PRK13412  803 AGFAQSPL-------------VRWLPDSLftqpeyrdchLLYYTGITRTAKGILAEIVRSMFLNSTAHLQLLHEMKAHAL 869
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720427245 517 KCAEAFRQGNLPLLGQYLTSYWEQKKLMAPGCEPLAVQRMMDVLAPYAYGQSLAGAGGGGFLYLLTKEPRQKETLEAVL 595
Cdd:PRK13412  870 DMYEAIQRGEFEEFGRLVGKTWEQNKALDSGTNPAAVEAIIELIKDYTLGYKLPGAGGGGYLYMVAKDPGAAERIRKIL 948
COG2605 COG2605
Predicted kinase related to galactokinase and mevalonate kinase [General function prediction ...
255-616 1.45e-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: 1.45e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427245 255 VVTECPARVDFSGGWSDTPPIAYELGGAVLGLAVrvdgrrpigakARRIpepelWLAVGPRQDEmtmRIVCRSLDdlrdy 334
Cdd:COG2605     1 IISRAPLRISFAGGGTDLPPYYLEHGGAVLNAAI-----------DKYA-----YVTLEPRFDG---KIRLSSSD----- 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427245 335 cqphapgaLLKAAFICAGIVHLHselPLLEQLLHSFN--GGFELHTWSELPHGSGLGTSSILAGAALAALQRAAGRAVGT 412
Cdd:COG2605    57 --------TERVETVDEDDDIPH---PVIREALKLFGigDGLEITTDSDAPAGSGLGSSSALTVALLNALHALLGLPLSP 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427245 413 EALIHAVLHLEQ-VLTTGGGWQDQVSGLMPGIKVGRSRAQlpLKVEVEEITVPEGFVQKINDHLLLVYTGKTRLARNLLQ 491
Cdd:COG2605   126 YDLARLAYEIERnDLGEPGGKQDQYAAAFGGFNFIEFGPD--GRVIVNPLRISPEILNELESNLLLFYTGITRESSDILK 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720427245 492 DVLRNWYARLPVVVQNARRLVRQTEKCAEAFRQGNLPLLGQYLTSYWEQKKLMAPGCEPLAVQRMMDV-LAPYAYGQSLA 570
Cdd:COG2605   204 EQVKNVEDGDEATLEALHEMKELALEMKEALLKGDLDEFGELLNEGWELKKRLASGISNPAIDEIYELaRKAGALGGKLL 283
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1720427245 571 GAGGGGFLYLLTKEPRQKETLEAvLAKAEGLgnysVHLVEVDPQGL 616
Cdd:COG2605   284 GAGGGGFLLFYAPPERREAVREA-LSKAGLR----VVPFSFDKEGS 324
Fucokinase pfam07959
L-fucokinase; In the salvage pathway of GDP-L-fucose, free cytosolic fucose is phosphorylated ...
2-44 5.01e-13

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: 71.14  E-value: 5.01e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1720427245   2 YLNMSWNEFFKKTGIRDWDLWDPDTPPsDRCLLTARLFPVLHP 44
Cdd:pfam07959 364 FLGKPLEDFLSLTGIQPEDLWFSGEPR-EKSLWNARLFPVCHD 405
 
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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