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Conserved domains on  [gi|19075895|ref|NP_588395|]
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riboflavin kinase Fmn1 [Schizosaccharomyces pombe]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02940 super family cl31957
riboflavin kinase
 28-162 1.14e-50

riboflavin kinase


The actual alignment was detected with superfamily member PLN02940:

Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 166.16  E-value: 1.14e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075895   28 GKVVHGFGRGSKELGIPTANISEDAIQELLRYRDSGVYFGYAMVQKR-VFPMVMSVGWNPYYKNKLRSAEVHLIERQGED 106
Cdd:PLN02940 243 GPVIKGFGRGSKVLGIPTANLSTENYSDVLSEHPSGVYFGWAGLSTRgVYKMVMSIGWNPYFNNTEKTIEPWLLHDFGED 322

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 19075895  107 FYEEIMRVIVLGYIRPELNYAGLDKLIEDIHTDIRVALNSMDRPSYSSYKKDPFFK 162
Cdd:PLN02940 323 FYGEELRLVIVGYIRPEANFPSLESLIAKIHEDRRIAEKALDLPLYAKYKDDPYLT 378
 
Name Accession Description Interval E-value
PLN02940 PLN02940
riboflavin kinase
 28-162 1.14e-50

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 166.16  E-value: 1.14e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075895   28 GKVVHGFGRGSKELGIPTANISEDAIQELLRYRDSGVYFGYAMVQKR-VFPMVMSVGWNPYYKNKLRSAEVHLIERQGED 106
Cdd:PLN02940 243 GPVIKGFGRGSKVLGIPTANLSTENYSDVLSEHPSGVYFGWAGLSTRgVYKMVMSIGWNPYFNNTEKTIEPWLLHDFGED 322

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 19075895  107 FYEEIMRVIVLGYIRPELNYAGLDKLIEDIHTDIRVALNSMDRPSYSSYKKDPFFK 162
Cdd:PLN02940 323 FYGEELRLVIVGYIRPEANFPSLESLIAKIHEDRRIAEKALDLPLYAKYKDDPYLT 378
Flavokinase pfam01687
Riboflavin kinase; This family represents the C-terminal region of the bifunctional riboflavin ...
 21-146 5.84e-47

Riboflavin kinase; This family represents the C-terminal region of the bifunctional riboflavin biosynthesis protein known as RibC in Bacillus subtilis. The RibC protein from Bacillus subtilis has both flavokinase and flavin adenine dinucleotide synthetase (FAD-synthetase) activities. RibC plays an essential role in the flavin metabolism. This domain is thought to have kinase activity.


Pssm-ID: 460295 [Multi-domain]  Cd Length: 123  Bit Score: 148.68  E-value: 5.84e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075895    21 PYPIRFEGKVVHGFGRGsKELGIPTANISEDaiqELLRYRDsGVYFGYAMV-QKRVFPMVMSVGWNPYYKNKLRSAEVHL 99
Cdd:pfam01687   2 GRPYSISGKVVHGDGRG-RTLGFPTANLPLP---EKLLPAN-GVYAVWVRVdGGKVYPGVANIGTNPTFGNGKLTVEVHI 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 19075895   100 IERQGeDFYEEIMRVIVLGYIRPELNYAGLDKLIEDIHTDIRVALNS 146
Cdd:pfam01687  77 LDFDG-DLYGKEIRVEFLGFLRPEKKFDSLEALKAQIKKDIEQARAI 122
Flavokinase smart00904
Riboflavin kinase; Riboflavin is converted into catalytically active cofactors (FAD and FMN) ...
 22-145 3.84e-39

Riboflavin kinase; Riboflavin is converted into catalytically active cofactors (FAD and FMN) by the actions of riboflavin kinase, which converts it into FMN, and FAD synthetase, which adenylates FMN to FAD. Eukaryotes usually have two separate enzymes, while most prokaryotes have a single bifunctional protein that can carry out both catalyses, although exceptions occur in both cases. While eukaryotic monofunctional riboflavin kinase is orthologous to the bifunctional prokaryotic enzyme. the monofunctional FAD synthetase differs from its prokaryotic counterpart, and is instead related to the PAPS-reductase family. The bacterial FAD synthetase that is part of the bifunctional enzyme has remote similarity to nucleotidyl transferases and, hence, it may be involved in the adenylylation reaction of FAD synthetases. This entry represents riboflavin kinase, which occurs as part of a bifunctional enzyme or a stand-alone enzyme.


Pssm-ID: 214901 [Multi-domain]  Cd Length: 124  Bit Score: 129.10  E-value: 3.84e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075895     22 YPIRFEGKVVHGFGRGSKeLGIPTANISEDAIQELLRYrdsGVYFGYAMVQKRVFPMVMSVGWNPYYKNKlRSAEVHLIE 101
Cdd:smart00904   4 RPYSISGRVVHGDKRGRT-LGFPTANLPLDDRLLLPKN---GVYAVRVRVDGKIYPGVANIGTRPTFGGD-RSVEVHILD 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 19075895    102 RQGeDFYEEIMRVIVLGYIRPELNYAGLDKLIEDIHTDIRVALN 145
Cdd:smart00904  79 FSG-DLYGEEIEVEFLKFIRDEQKFDSLDELKAQISRDIEEARE 121
RibF COG0196
FAD synthase [Coenzyme transport and metabolism]; FAD synthase is part of the Pathway ...
 22-145 2.55e-28

FAD synthase [Coenzyme transport and metabolism]; FAD synthase is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis


Pssm-ID: 439966 [Multi-domain]  Cd Length: 310  Bit Score: 106.28  E-value: 2.55e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075895  22 YPIRFEGKVVHGFGRGsKELGIPTANISEDAIQELLRYrdsGVYFGYAMVQKRVFPMVMSVGWNPYYKNKLRSAEVHLIE 101
Cdd:COG0196 186 RPYSISGRVVHGDKRG-RTLGFPTANLALPEEKLLPAD---GVYAVRVRIDGRRYPGVANIGTRPTFDGGEPTLEVHLLD 261

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 19075895 102 RQGeDFYEEIMRVIVLGYIRPELNYAGLDKLIEDIHTDIRVALN 145
Cdd:COG0196 262 FDG-DLYGKEIEVEFLKRLRDEKKFDSLEALKAQIAKDVEQARA 304
 
Name Accession Description Interval E-value
PLN02940 PLN02940
riboflavin kinase
 28-162 1.14e-50

riboflavin kinase


Pssm-ID: 178528 [Multi-domain]  Cd Length: 382  Bit Score: 166.16  E-value: 1.14e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075895   28 GKVVHGFGRGSKELGIPTANISEDAIQELLRYRDSGVYFGYAMVQKR-VFPMVMSVGWNPYYKNKLRSAEVHLIERQGED 106
Cdd:PLN02940 243 GPVIKGFGRGSKVLGIPTANLSTENYSDVLSEHPSGVYFGWAGLSTRgVYKMVMSIGWNPYFNNTEKTIEPWLLHDFGED 322

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 19075895  107 FYEEIMRVIVLGYIRPELNYAGLDKLIEDIHTDIRVALNSMDRPSYSSYKKDPFFK 162
Cdd:PLN02940 323 FYGEELRLVIVGYIRPEANFPSLESLIAKIHEDRRIAEKALDLPLYAKYKDDPYLT 378
Flavokinase pfam01687
Riboflavin kinase; This family represents the C-terminal region of the bifunctional riboflavin ...
 21-146 5.84e-47

Riboflavin kinase; This family represents the C-terminal region of the bifunctional riboflavin biosynthesis protein known as RibC in Bacillus subtilis. The RibC protein from Bacillus subtilis has both flavokinase and flavin adenine dinucleotide synthetase (FAD-synthetase) activities. RibC plays an essential role in the flavin metabolism. This domain is thought to have kinase activity.


Pssm-ID: 460295 [Multi-domain]  Cd Length: 123  Bit Score: 148.68  E-value: 5.84e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075895    21 PYPIRFEGKVVHGFGRGsKELGIPTANISEDaiqELLRYRDsGVYFGYAMV-QKRVFPMVMSVGWNPYYKNKLRSAEVHL 99
Cdd:pfam01687   2 GRPYSISGKVVHGDGRG-RTLGFPTANLPLP---EKLLPAN-GVYAVWVRVdGGKVYPGVANIGTNPTFGNGKLTVEVHI 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 19075895   100 IERQGeDFYEEIMRVIVLGYIRPELNYAGLDKLIEDIHTDIRVALNS 146
Cdd:pfam01687  77 LDFDG-DLYGKEIRVEFLGFLRPEKKFDSLEALKAQIKKDIEQARAI 122
Flavokinase smart00904
Riboflavin kinase; Riboflavin is converted into catalytically active cofactors (FAD and FMN) ...
 22-145 3.84e-39

Riboflavin kinase; Riboflavin is converted into catalytically active cofactors (FAD and FMN) by the actions of riboflavin kinase, which converts it into FMN, and FAD synthetase, which adenylates FMN to FAD. Eukaryotes usually have two separate enzymes, while most prokaryotes have a single bifunctional protein that can carry out both catalyses, although exceptions occur in both cases. While eukaryotic monofunctional riboflavin kinase is orthologous to the bifunctional prokaryotic enzyme. the monofunctional FAD synthetase differs from its prokaryotic counterpart, and is instead related to the PAPS-reductase family. The bacterial FAD synthetase that is part of the bifunctional enzyme has remote similarity to nucleotidyl transferases and, hence, it may be involved in the adenylylation reaction of FAD synthetases. This entry represents riboflavin kinase, which occurs as part of a bifunctional enzyme or a stand-alone enzyme.


Pssm-ID: 214901 [Multi-domain]  Cd Length: 124  Bit Score: 129.10  E-value: 3.84e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075895     22 YPIRFEGKVVHGFGRGSKeLGIPTANISEDAIQELLRYrdsGVYFGYAMVQKRVFPMVMSVGWNPYYKNKlRSAEVHLIE 101
Cdd:smart00904   4 RPYSISGRVVHGDKRGRT-LGFPTANLPLDDRLLLPKN---GVYAVRVRVDGKIYPGVANIGTRPTFGGD-RSVEVHILD 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 19075895    102 RQGeDFYEEIMRVIVLGYIRPELNYAGLDKLIEDIHTDIRVALN 145
Cdd:smart00904  79 FSG-DLYGEEIEVEFLKFIRDEQKFDSLDELKAQISRDIEEARE 121
RibF COG0196
FAD synthase [Coenzyme transport and metabolism]; FAD synthase is part of the Pathway ...
 22-145 2.55e-28

FAD synthase [Coenzyme transport and metabolism]; FAD synthase is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis


Pssm-ID: 439966 [Multi-domain]  Cd Length: 310  Bit Score: 106.28  E-value: 2.55e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075895  22 YPIRFEGKVVHGFGRGsKELGIPTANISEDAIQELLRYrdsGVYFGYAMVQKRVFPMVMSVGWNPYYKNKLRSAEVHLIE 101
Cdd:COG0196 186 RPYSISGRVVHGDKRG-RTLGFPTANLALPEEKLLPAD---GVYAVRVRIDGRRYPGVANIGTRPTFDGGEPTLEVHLLD 261

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 19075895 102 RQGeDFYEEIMRVIVLGYIRPELNYAGLDKLIEDIHTDIRVALN 145
Cdd:COG0196 262 FDG-DLYGKEIEVEFLKRLRDEKKFDSLEALKAQIAKDVEQARA 304
PRK05627 PRK05627
bifunctional riboflavin kinase/FAD synthetase;
21-143 1.40e-24

bifunctional riboflavin kinase/FAD synthetase;


Pssm-ID: 235536 [Multi-domain]  Cd Length: 305  Bit Score: 96.37  E-value: 1.40e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19075895   21 PYPIrfEGKVVHGFGRGsKELGIPTANIsedaiqELLRYRD--SGVYFGYAMVQKRVFPMVMSVGWNPYYKNKLRSAEVH 98
Cdd:PRK05627 185 PYSI--SGRVVHGQKLG-RTLGFPTANL------PLPDRVLpaDGVYAVRVKVDGKPYPGVANIGTRPTVDGGRQLLEVH 255

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 19075895   99 LIERQGeDFYEEIMRVIVLGYIRPELNYAGLDKLIEDIHTDIRVA 143
Cdd:PRK05627 256 LLDFNG-DLYGEHITVEFLKKLRDEQKFDSLDELKAQIAKDIETA 299
 
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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