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Conserved domains on  [gi|1237951797|gb|PAK19188|]
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FAD:protein FMN transferase [Megasphaera elsdenii]

Protein Classification

FAD:protein FMN transferase( domain architecture ID 10003878)

FAD:protein FMN-transferase catalyzes the attachment of an FMN moiety to a threonine residue of a protein via a phosphoester bond in bacterial flavoproteins

CATH:  3.10.520.20
EC:  2.7.1.180
PubMed:  23558683
SCOP:  4003899

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ApbE COG1477
FAD:protein FMN transferase ApbE [Coenzyme transport and metabolism, Posttranslational ...
1-298 3.89e-120

FAD:protein FMN transferase ApbE [Coenzyme transport and metabolism, Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 441086 [Multi-domain]  Cd Length: 294  Bit Score: 346.75  E-value: 3.89e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237951797   1 MDTTVSLRASGK---EAKEAVDEGFDRLDQLDKLAGQN-EDSDVSRINAAAGREYVQVDPAVYEMIEYAKDYSAKSQGEW 76
Cdd:COG1477     1 MGTTVSITLYGPdeaQAEAALAAAFAELDRLEALLSTYrPDSELSRLNRAAGGEPVKVSPELAELLERALEISELSDGAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237951797  77 DITVGVMTNLWRIGNDDQHVPSADEISRALMKVNYKDILLRPEDHSVMLAKAGMAIDLGGVAKGYAVDEIRKIYEKHHIE 156
Cdd:COG1477    81 DPTVGPLVNLWGFGPDKARVPSAAEIAAALALVGYRKVELDEEGGTVRLARPGMQLDLGGIAKGYAVDRAAELLRAAGVT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237951797 157 SGLINLGaSSMYAVGKTSKGKPWRIGIKHPRSDDdkAFLGIVSIENQALSTSGDYERYFIQDGVRYHHIFDPRTGYPARS 236
Cdd:COG1477   161 NALVNLG-GDIRALGTKPDGRPWRVGIEDPRDPG--AVLAVLELSDGAVATSGDYERYFEIDGKRYSHIIDPRTGYPVEH 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1237951797 237 GVMSDSIIIDgsvphAGMLSDMMTTIVFVLGPQKGMELVNSMEGVDCEITGTDNAVYMTQGF 298
Cdd:COG1477   238 GLASVTVIAP-----DAMLADALATALFVLGPEKGLALAERLPGLEALLIDRDGKVFASPGF 294
 
Name Accession Description Interval E-value
ApbE COG1477
FAD:protein FMN transferase ApbE [Coenzyme transport and metabolism, Posttranslational ...
1-298 3.89e-120

FAD:protein FMN transferase ApbE [Coenzyme transport and metabolism, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441086 [Multi-domain]  Cd Length: 294  Bit Score: 346.75  E-value: 3.89e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237951797   1 MDTTVSLRASGK---EAKEAVDEGFDRLDQLDKLAGQN-EDSDVSRINAAAGREYVQVDPAVYEMIEYAKDYSAKSQGEW 76
Cdd:COG1477     1 MGTTVSITLYGPdeaQAEAALAAAFAELDRLEALLSTYrPDSELSRLNRAAGGEPVKVSPELAELLERALEISELSDGAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237951797  77 DITVGVMTNLWRIGNDDQHVPSADEISRALMKVNYKDILLRPEDHSVMLAKAGMAIDLGGVAKGYAVDEIRKIYEKHHIE 156
Cdd:COG1477    81 DPTVGPLVNLWGFGPDKARVPSAAEIAAALALVGYRKVELDEEGGTVRLARPGMQLDLGGIAKGYAVDRAAELLRAAGVT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237951797 157 SGLINLGaSSMYAVGKTSKGKPWRIGIKHPRSDDdkAFLGIVSIENQALSTSGDYERYFIQDGVRYHHIFDPRTGYPARS 236
Cdd:COG1477   161 NALVNLG-GDIRALGTKPDGRPWRVGIEDPRDPG--AVLAVLELSDGAVATSGDYERYFEIDGKRYSHIIDPRTGYPVEH 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1237951797 237 GVMSDSIIIDgsvphAGMLSDMMTTIVFVLGPQKGMELVNSMEGVDCEITGTDNAVYMTQGF 298
Cdd:COG1477   238 GLASVTVIAP-----DAMLADALATALFVLGPEKGLALAERLPGLEALLIDRDGKVFASPGF 294
ApbE pfam02424
ApbE family; This prokaryotic family of lipoproteins are related to ApbE from Salmonella ...
2-283 2.23e-80

ApbE family; This prokaryotic family of lipoproteins are related to ApbE from Salmonella typhimurium. ApbE is involved in thiamine synthesis. It acts as an FAD:protein FMN-transferase, catalysing the attachment of an FMN residue to a threonine residue of a protein via a phosphoester bond in such bacterial flavoproteins.


Pssm-ID: 460554 [Multi-domain]  Cd Length: 227  Bit Score: 243.12  E-value: 2.23e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237951797   2 DTTVSLR--ASGKEAKEAVDEGFD-RLDQLDKLAGQ-NEDSDVSRINAAaGREYVQVDPAVYEMIEYAKDYSAKSQGEWD 77
Cdd:pfam02424   1 GTTVSITvyGPDEAAAEALEAAIDaELDRLEALLSTyRPDSELSRLNRA-GAGPVKVSPELFELLERALEISELSGGAFD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237951797  78 ITVGvmtnlwrignddqhvpsadeisrALMkvnykdillrpedhsvmlakagmaIDLGGVAKGYAVDEIRKIYEKHHIES 157
Cdd:pfam02424  80 ITVG-----------------------PLV------------------------LDLGGIAKGYAVDRAAELLKAKGVTS 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237951797 158 GLINLGaSSMYAVGKTSKGKPWRIGIKHPRSDDDkafLGIVSIENQALSTSGDYERYFIqDGVRYHHIFDPRTGYPARSG 237
Cdd:pfam02424 113 ALVNLG-GDIRALGTKPDGSPWRVGIQDPRDPDS---LAVLELSDKAVATSGDYERYFE-DGKRYHHIIDPRTGYPVANG 187
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1237951797 238 VMSDSIIidgsvpHAGMLSDMMTTIVFVLGPQKGMELVNSMEGVDC 283
Cdd:pfam02424 188 LASVTVI------ADAMLADALATALFVLGPEKGLALLEKLPGLEA 227
PRK10461 PRK10461
thiamine biosynthesis lipoprotein ApbE; Provisional
7-299 4.32e-41

thiamine biosynthesis lipoprotein ApbE; Provisional


Pssm-ID: 182478  Cd Length: 350  Bit Score: 146.05  E-value: 4.32e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237951797   7 LRASGKEAKEAVDEGFDRLDQLdkLAGQNEDSDVSRINAAAGREYVQVDPAVYEMIEYAKDYSAKSQGEWDITVGVMTNL 86
Cdd:PRK10461   54 DAKRSAELQEKIQTQLDADDQL--LSTYKKDSALMRFNDSQSLSPWPVSEAMADIVTTSLRIGAKTDGAMDITVGPLVNL 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237951797  87 WRIGNDDQ--HVPSADEISRALMKVNYKDILLRPEDHSVMLAK--AGMAIDLGGVAKGYAVDEIRKIYEKHHIESGLINL 162
Cdd:PRK10461  132 WGFGPEKQpvQIPSQEQIDAAKAKTGLQHLTVINQSHQQYLQKdlPDLYVDLSTVGEGYAADHLARLMEQEGISRYLVSV 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237951797 163 GASsMYAVGKTSKGKPWRIGIKHPrSDDDKAFLGIVSIENQALSTSGDYERYFIQDGVRYHHIFDPRTGYPARSGVMSDS 242
Cdd:PRK10461  212 GGA-LSSRGMNGEGQPWRVAIQKP-TDKENAVQAVVDINGHGISTSGSYRNYYELDGKRLSHVIDPQTGRPIEHNLVSVT 289
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1237951797 243 IIidgsVPHAgMLSDMMTTIVFVLGPQKGMELVNSmEGVdceitgtdnAVYMT----QGFK 299
Cdd:PRK10461  290 VI----APTA-LEADGWDTGLMVLGPEKAKEVVRR-EGL---------AVYMItkegDGFK 335
 
Name Accession Description Interval E-value
ApbE COG1477
FAD:protein FMN transferase ApbE [Coenzyme transport and metabolism, Posttranslational ...
1-298 3.89e-120

FAD:protein FMN transferase ApbE [Coenzyme transport and metabolism, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441086 [Multi-domain]  Cd Length: 294  Bit Score: 346.75  E-value: 3.89e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237951797   1 MDTTVSLRASGK---EAKEAVDEGFDRLDQLDKLAGQN-EDSDVSRINAAAGREYVQVDPAVYEMIEYAKDYSAKSQGEW 76
Cdd:COG1477     1 MGTTVSITLYGPdeaQAEAALAAAFAELDRLEALLSTYrPDSELSRLNRAAGGEPVKVSPELAELLERALEISELSDGAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237951797  77 DITVGVMTNLWRIGNDDQHVPSADEISRALMKVNYKDILLRPEDHSVMLAKAGMAIDLGGVAKGYAVDEIRKIYEKHHIE 156
Cdd:COG1477    81 DPTVGPLVNLWGFGPDKARVPSAAEIAAALALVGYRKVELDEEGGTVRLARPGMQLDLGGIAKGYAVDRAAELLRAAGVT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237951797 157 SGLINLGaSSMYAVGKTSKGKPWRIGIKHPRSDDdkAFLGIVSIENQALSTSGDYERYFIQDGVRYHHIFDPRTGYPARS 236
Cdd:COG1477   161 NALVNLG-GDIRALGTKPDGRPWRVGIEDPRDPG--AVLAVLELSDGAVATSGDYERYFEIDGKRYSHIIDPRTGYPVEH 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1237951797 237 GVMSDSIIIDgsvphAGMLSDMMTTIVFVLGPQKGMELVNSMEGVDCEITGTDNAVYMTQGF 298
Cdd:COG1477   238 GLASVTVIAP-----DAMLADALATALFVLGPEKGLALAERLPGLEALLIDRDGKVFASPGF 294
ApbE pfam02424
ApbE family; This prokaryotic family of lipoproteins are related to ApbE from Salmonella ...
2-283 2.23e-80

ApbE family; This prokaryotic family of lipoproteins are related to ApbE from Salmonella typhimurium. ApbE is involved in thiamine synthesis. It acts as an FAD:protein FMN-transferase, catalysing the attachment of an FMN residue to a threonine residue of a protein via a phosphoester bond in such bacterial flavoproteins.


Pssm-ID: 460554 [Multi-domain]  Cd Length: 227  Bit Score: 243.12  E-value: 2.23e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237951797   2 DTTVSLR--ASGKEAKEAVDEGFD-RLDQLDKLAGQ-NEDSDVSRINAAaGREYVQVDPAVYEMIEYAKDYSAKSQGEWD 77
Cdd:pfam02424   1 GTTVSITvyGPDEAAAEALEAAIDaELDRLEALLSTyRPDSELSRLNRA-GAGPVKVSPELFELLERALEISELSGGAFD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237951797  78 ITVGvmtnlwrignddqhvpsadeisrALMkvnykdillrpedhsvmlakagmaIDLGGVAKGYAVDEIRKIYEKHHIES 157
Cdd:pfam02424  80 ITVG-----------------------PLV------------------------LDLGGIAKGYAVDRAAELLKAKGVTS 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237951797 158 GLINLGaSSMYAVGKTSKGKPWRIGIKHPRSDDDkafLGIVSIENQALSTSGDYERYFIqDGVRYHHIFDPRTGYPARSG 237
Cdd:pfam02424 113 ALVNLG-GDIRALGTKPDGSPWRVGIQDPRDPDS---LAVLELSDKAVATSGDYERYFE-DGKRYHHIIDPRTGYPVANG 187
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1237951797 238 VMSDSIIidgsvpHAGMLSDMMTTIVFVLGPQKGMELVNSMEGVDC 283
Cdd:pfam02424 188 LASVTVI------ADAMLADALATALFVLGPEKGLALLEKLPGLEA 227
PRK10461 PRK10461
thiamine biosynthesis lipoprotein ApbE; Provisional
7-299 4.32e-41

thiamine biosynthesis lipoprotein ApbE; Provisional


Pssm-ID: 182478  Cd Length: 350  Bit Score: 146.05  E-value: 4.32e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237951797   7 LRASGKEAKEAVDEGFDRLDQLdkLAGQNEDSDVSRINAAAGREYVQVDPAVYEMIEYAKDYSAKSQGEWDITVGVMTNL 86
Cdd:PRK10461   54 DAKRSAELQEKIQTQLDADDQL--LSTYKKDSALMRFNDSQSLSPWPVSEAMADIVTTSLRIGAKTDGAMDITVGPLVNL 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237951797  87 WRIGNDDQ--HVPSADEISRALMKVNYKDILLRPEDHSVMLAK--AGMAIDLGGVAKGYAVDEIRKIYEKHHIESGLINL 162
Cdd:PRK10461  132 WGFGPEKQpvQIPSQEQIDAAKAKTGLQHLTVINQSHQQYLQKdlPDLYVDLSTVGEGYAADHLARLMEQEGISRYLVSV 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237951797 163 GASsMYAVGKTSKGKPWRIGIKHPrSDDDKAFLGIVSIENQALSTSGDYERYFIQDGVRYHHIFDPRTGYPARSGVMSDS 242
Cdd:PRK10461  212 GGA-LSSRGMNGEGQPWRVAIQKP-TDKENAVQAVVDINGHGISTSGSYRNYYELDGKRLSHVIDPQTGRPIEHNLVSVT 289
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1237951797 243 IIidgsVPHAgMLSDMMTTIVFVLGPQKGMELVNSmEGVdceitgtdnAVYMT----QGFK 299
Cdd:PRK10461  290 VI----APTA-LEADGWDTGLMVLGPEKAKEVVRR-EGL---------AVYMItkegDGFK 335
PTZ00306 PTZ00306
NADH-dependent fumarate reductase; Provisional
14-227 5.07e-14

NADH-dependent fumarate reductase; Provisional


Pssm-ID: 140327 [Multi-domain]  Cd Length: 1167  Bit Score: 72.50  E-value: 5.07e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237951797   14 AKEAVDEGFDRLDQLdkLAGQNEDSDVSRINAAAGREYVQVDPAVYEMIEYAKDYSAKSQGEWDITVGVMTNLWRIGNDD 93
Cdd:PTZ00306    88 AKEVLRSAFQMVDTH--LNSFNPNSEVSRVNRMPVGEKHQMSAHLKRVMACCQRVYNSSGGCFDPAAGPLVHELREAARR 165
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237951797   94 QHVPSADEISRALMKV----NYKDILLrpEDHSVMLAKAGMAIDLGGVAKGYAVDeirkiyekhHIESGLINLGASSMY- 168
Cdd:PTZ00306   166 QKSVEAEFVIEELAGRftltNSFAIDL--EEGTIARKHEDAMLDLGGVNKGYTVD---------YVVDRLNAAGFDDVLf 234
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237951797  169 -------AVGKTSKGKPWRIGIKHPRS---------------DDDKAFLGIVSIENQALSTSGDYERY-FIQDGVRYHHI 225
Cdd:PTZ00306   235 ewggdcrASGVNVQRQPWAVGIVRPPSvdevraaaksgksapPDHKSLLRVMSLNNEALCTSGDYENVlEGPASKVYSST 314

                   ..
gi 1237951797  226 FD 227
Cdd:PTZ00306   315 FD 316
 
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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