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Conserved domains on  [gi|17506045|ref|NP_491510|]
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Flavin-containing monooxygenase [Caenorhabditis elegans]

Protein Classification

flavin-containing monooxygenase( domain architecture ID 1750397)

flavin-containing monooxygenase (FMO) may act as an xenobiotic-metabolising enzyme that catalyzes the oxygenation of nucleophilic nitrogen, sulphur, phosphorus and selenium atoms in a range of structurally diverse compounds by using an NADPH cofactor and FAD prosthetic group

EC:  1.14.13.8
Gene Ontology:  GO:0004499|GO:0050661|GO:0050660
PubMed:  9538688

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02172 super family cl40780
flavin-containing monooxygenase FMO GS-OX
 3-359 1.06e-54

flavin-containing monooxygenase FMO GS-OX


The actual alignment was detected with superfamily member PLN02172:

Pssm-ID: 215116 [Multi-domain]  Cd Length: 461  Bit Score: 187.76  E-value: 1.06e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506045    3 KRVCVIGAGAAGLAAAKHSLAQGLEVEVFEQTGNVGGTWVYSKQTGS------------HSSMYQNMTTNLPKEVMQFRG 70
Cdd:PLN02172  11 QHVAVIGAGAAGLVAARELRREGHTVVVFEREKQVGGLWVYTPKSESdplsldptrsivHSSVYESLRTNLPRECMGYRD 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506045   71 VPF--RNELPS-----FLTHENVREYLQEFSQGMPI----HFNQTVENVERIDDKWKVTTHHGAGIDEH-FFDIVFVCNG 138
Cdd:PLN02172  91 FPFvpRFDDESrdsrrYPSHREVLAYLQDFAREFKIeemvRFETEVVRVEPVDGKWRVQSKNSGGFSKDeIFDAVVVCNG 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506045  139 HYFAPNN---PYEESaFEGSFIHSHDYRHSKDYIDKEVIVIGAGPSGIDISLQLSETAKKITLISKKA---TYPTL--PD 210
Cdd:PLN02172 171 HYTEPNVahiPGIKS-WPGKQIHSHNYRVPDPFKNEVVVVIGNFASGADISRDIAKVAKEVHIASRASesdTYEKLpvPQ 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506045  211 NITQISQHVKQVVPEGCET-DDGTLITADAIIVCTGYFYKYPFLSDN-ILRVKENNqlVSPIFEHVVHAEYPNSLYFIGL 288
Cdd:PLN02172 250 NNLWMHSEIDTAHEDGSIVfKNGKVVYADTIVHCTGYKYHFPFLETNgYMRIDENR--VEPLYKHVFPPALAPGLSFIGL 327

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17506045  289 NLVTITFPLFEYQVKMALSFATGRAPIPDRKMLIDYEKNQIEHQKSRGLAVRFYHLLQSEQWEYLARIAKL 359
Cdd:PLN02172 328 PAMGIQFVMFEIQSKWVAAVLSGRVTLPSEDKMMEDINAWYASLEALGIPKRYTHKLGKIQSEYLNWIAEE 398
 
Name Accession Description Interval E-value
PLN02172 PLN02172
flavin-containing monooxygenase FMO GS-OX
 3-359 1.06e-54

flavin-containing monooxygenase FMO GS-OX


Pssm-ID: 215116 [Multi-domain]  Cd Length: 461  Bit Score: 187.76  E-value: 1.06e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506045    3 KRVCVIGAGAAGLAAAKHSLAQGLEVEVFEQTGNVGGTWVYSKQTGS------------HSSMYQNMTTNLPKEVMQFRG 70
Cdd:PLN02172  11 QHVAVIGAGAAGLVAARELRREGHTVVVFEREKQVGGLWVYTPKSESdplsldptrsivHSSVYESLRTNLPRECMGYRD 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506045   71 VPF--RNELPS-----FLTHENVREYLQEFSQGMPI----HFNQTVENVERIDDKWKVTTHHGAGIDEH-FFDIVFVCNG 138
Cdd:PLN02172  91 FPFvpRFDDESrdsrrYPSHREVLAYLQDFAREFKIeemvRFETEVVRVEPVDGKWRVQSKNSGGFSKDeIFDAVVVCNG 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506045  139 HYFAPNN---PYEESaFEGSFIHSHDYRHSKDYIDKEVIVIGAGPSGIDISLQLSETAKKITLISKKA---TYPTL--PD 210
Cdd:PLN02172 171 HYTEPNVahiPGIKS-WPGKQIHSHNYRVPDPFKNEVVVVIGNFASGADISRDIAKVAKEVHIASRASesdTYEKLpvPQ 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506045  211 NITQISQHVKQVVPEGCET-DDGTLITADAIIVCTGYFYKYPFLSDN-ILRVKENNqlVSPIFEHVVHAEYPNSLYFIGL 288
Cdd:PLN02172 250 NNLWMHSEIDTAHEDGSIVfKNGKVVYADTIVHCTGYKYHFPFLETNgYMRIDENR--VEPLYKHVFPPALAPGLSFIGL 327

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17506045  289 NLVTITFPLFEYQVKMALSFATGRAPIPDRKMLIDYEKNQIEHQKSRGLAVRFYHLLQSEQWEYLARIAKL 359
Cdd:PLN02172 328 PAMGIQFVMFEIQSKWVAAVLSGRVTLPSEDKMMEDINAWYASLEALGIPKRYTHKLGKIQSEYLNWIAEE 398
FMO-like pfam00743
Flavin-binding monooxygenase-like; This family includes FMO proteins, cyclohexanone ...
 3-357 1.56e-38

Flavin-binding monooxygenase-like; This family includes FMO proteins, cyclohexanone mono-oxygenase and a number of different mono-oxygenases.


Pssm-ID: 395602 [Multi-domain]  Cd Length: 531  Bit Score: 145.31  E-value: 1.56e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506045     3 KRVCVIGAGAAGLAAAKHSLAQGLEVEVFEQTGNVGGTWVYSKQT-GSHSSMYQNMTTNLPKEVMQFRGVPFRNELPSFL 81
Cdd:pfam00743   2 KKVAVIGAGVSGLASIKCCLEEGLEPTCFERSDDIGGLWRFTENVeEGRASIYKSVITNTSKEMSCFSDFPFPEDYPNFM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506045    82 THENVREYLQEFSQGMP----IHFNQTVENVERIDD-----KWKVTTHHGAGIDEHFFDIVFVCNGHYFAPNNPYEE--- 149
Cdd:pfam00743  82 HNSKFLEYFRMFAKEFDllkyIQFKTTVCSVKKRPDfstsgQWEVVTEHEGKQESAVFDAVMVCTGHHTNPHLPLESfpg 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506045   150 -SAFEGSFIHSHDYRHSKDYIDKEVIVIGAGPSGIDISLQLSETAKKITLISKKAT----------YPT----------- 207
Cdd:pfam00743 162 iEKFKGQYFHSRDYKHPEGFTGKRVLVIGIGNSGGDIAVELSHTAAQVFLSTRRGSwvlsrvsdhgYPWdmlfstrftsf 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506045   208 ---------------------------------------------LPDNITQISQHVKQVVPEGCET----DDGTLITA- 237
Cdd:pfam00743 242 lrnilptsisnwlmekqmnrrfnhenyglkpknralskepvvnddLPNRILCGAVKVKPNVKEFTETsaifEDGTVEEDi 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506045   238 DAIIVCTGYFYKYPFLSDNILRVkENNQLVspIFEHVV--HAEYPnSLYFIGL-NLVTITFPLFEYQVKMALSFATGRAP 314
Cdd:pfam00743 322 DVVIFATGYTFAFPFLEESLVKV-ENNKVS--LYKYVFppNLEKP-TLAIIGLiQPLGSIIPTVELQARWATRVFKGLCT 397

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 17506045   315 IP-DRKMLIDYEKNQIEHQKSRGLAVRfyHLLQSEQWEYLARIA 357
Cdd:pfam00743 398 LPsQSEMMAEINKRQEKKIKRFGDSQS--HTIQTDYIDYMDELA 439
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 24-289 3.67e-38

Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];


Pssm-ID: 441675 [Multi-domain]  Cd Length: 414  Bit Score: 142.31  E-value: 3.67e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506045  24 QGLEVEVFEQTGNVGGTWvyskqtgsHSSMYQNMTTNLPKEVMQFRGVPFRNELPSFLTHENVREYLQEFSQ----GMPI 99
Cdd:COG2072  28 AGIDFVVLEKADDVGGTW--------RDNRYPGLRLDTPSHLYSLPFFPNWSDDPDFPTGDEILAYLEAYADkfglRRPI 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506045 100 HFNQTVENVE--RIDDKWKVTTHHGagiDEHFFDIVFVCNGHYFAPNNPY--EESAFEGSFIHSHDYRHSKDYIDKEVIV 175
Cdd:COG2072 100 RFGTEVTSARwdEADGRWTVTTDDG---ETLTARFVVVATGPLSRPKIPDipGLEDFAGEQLHSADWRNPVDLAGKRVLV 176

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506045 176 IGAGPSGIDISLQLSETAKKITLISKKATY---------------------------------------------PTL-- 208
Cdd:COG2072 177 VGTGASAVQIAPELARVAAHVTVFQRTPPWvlprpnydpergrpanylgleappalnrrdarawlrrllraqvkdPELgl 256

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506045 209 --PD---------------------NITQISQHVKQVVPEGCETDDGTLITADAIIVCTGYFYKYPFLSdnILRVKENNQ 265
Cdd:COG2072 257 ltPDyppgckrpllstdyyealrrgNVELVTGGIERITEDGVVFADGTEHEVDVIVWATGFRADLPWLA--PLDVRGRDG 334

                       330       340
                ....*....|....*....|....*
gi 17506045 266 LVSPI-FEHVVHAEYPNsLYFIGLN 289
Cdd:COG2072 335 RSGPRaYLGVVVPGFPN-LFFLGPN 358
MnmC_Cterm TIGR03197
tRNA U-34 5-methylaminomethyl-2-thiouridine biosynthesis protein MnmC, C-terminal domain; In ...
 86-143 3.45e-03

tRNA U-34 5-methylaminomethyl-2-thiouridine biosynthesis protein MnmC, C-terminal domain; In Escherichia coli, the protein previously designated YfcK is now identified as the bifunctional enzyme MnmC. It acts, following the action of the heterotetramer of GidA and MnmE, in the modification of U-34 of certain tRNA to 5-methylaminomethyl-2-thiouridine (mnm5s2U). In other bacterial, the corresponding proteins are usually but always found as a single polypeptide chain, but occasionally as the product of tandem genes. This model represents the C-terminal region of the multifunctional protein. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274478 [Multi-domain]  Cd Length: 381  Bit Score: 39.17  E-value: 3.45e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17506045    86 VREYLQEFSQGMPIHFNQTVENVERIDDKWKVTTHHGAGIDehfFDIVFVCNGH---YFAP 143
Cdd:TIGR03197 138 CRALLAHAGIRLTLHFNTEITSLERDGEGWQLLDANGEVIA---ASVVVLANGAqapQLAQ 195
 
Name Accession Description Interval E-value
PLN02172 PLN02172
flavin-containing monooxygenase FMO GS-OX
 3-359 1.06e-54

flavin-containing monooxygenase FMO GS-OX


Pssm-ID: 215116 [Multi-domain]  Cd Length: 461  Bit Score: 187.76  E-value: 1.06e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506045    3 KRVCVIGAGAAGLAAAKHSLAQGLEVEVFEQTGNVGGTWVYSKQTGS------------HSSMYQNMTTNLPKEVMQFRG 70
Cdd:PLN02172  11 QHVAVIGAGAAGLVAARELRREGHTVVVFEREKQVGGLWVYTPKSESdplsldptrsivHSSVYESLRTNLPRECMGYRD 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506045   71 VPF--RNELPS-----FLTHENVREYLQEFSQGMPI----HFNQTVENVERIDDKWKVTTHHGAGIDEH-FFDIVFVCNG 138
Cdd:PLN02172  91 FPFvpRFDDESrdsrrYPSHREVLAYLQDFAREFKIeemvRFETEVVRVEPVDGKWRVQSKNSGGFSKDeIFDAVVVCNG 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506045  139 HYFAPNN---PYEESaFEGSFIHSHDYRHSKDYIDKEVIVIGAGPSGIDISLQLSETAKKITLISKKA---TYPTL--PD 210
Cdd:PLN02172 171 HYTEPNVahiPGIKS-WPGKQIHSHNYRVPDPFKNEVVVVIGNFASGADISRDIAKVAKEVHIASRASesdTYEKLpvPQ 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506045  211 NITQISQHVKQVVPEGCET-DDGTLITADAIIVCTGYFYKYPFLSDN-ILRVKENNqlVSPIFEHVVHAEYPNSLYFIGL 288
Cdd:PLN02172 250 NNLWMHSEIDTAHEDGSIVfKNGKVVYADTIVHCTGYKYHFPFLETNgYMRIDENR--VEPLYKHVFPPALAPGLSFIGL 327

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17506045  289 NLVTITFPLFEYQVKMALSFATGRAPIPDRKMLIDYEKNQIEHQKSRGLAVRFYHLLQSEQWEYLARIAKL 359
Cdd:PLN02172 328 PAMGIQFVMFEIQSKWVAAVLSGRVTLPSEDKMMEDINAWYASLEALGIPKRYTHKLGKIQSEYLNWIAEE 398
FMO-like pfam00743
Flavin-binding monooxygenase-like; This family includes FMO proteins, cyclohexanone ...
 3-357 1.56e-38

Flavin-binding monooxygenase-like; This family includes FMO proteins, cyclohexanone mono-oxygenase and a number of different mono-oxygenases.


Pssm-ID: 395602 [Multi-domain]  Cd Length: 531  Bit Score: 145.31  E-value: 1.56e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506045     3 KRVCVIGAGAAGLAAAKHSLAQGLEVEVFEQTGNVGGTWVYSKQT-GSHSSMYQNMTTNLPKEVMQFRGVPFRNELPSFL 81
Cdd:pfam00743   2 KKVAVIGAGVSGLASIKCCLEEGLEPTCFERSDDIGGLWRFTENVeEGRASIYKSVITNTSKEMSCFSDFPFPEDYPNFM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506045    82 THENVREYLQEFSQGMP----IHFNQTVENVERIDD-----KWKVTTHHGAGIDEHFFDIVFVCNGHYFAPNNPYEE--- 149
Cdd:pfam00743  82 HNSKFLEYFRMFAKEFDllkyIQFKTTVCSVKKRPDfstsgQWEVVTEHEGKQESAVFDAVMVCTGHHTNPHLPLESfpg 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506045   150 -SAFEGSFIHSHDYRHSKDYIDKEVIVIGAGPSGIDISLQLSETAKKITLISKKAT----------YPT----------- 207
Cdd:pfam00743 162 iEKFKGQYFHSRDYKHPEGFTGKRVLVIGIGNSGGDIAVELSHTAAQVFLSTRRGSwvlsrvsdhgYPWdmlfstrftsf 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506045   208 ---------------------------------------------LPDNITQISQHVKQVVPEGCET----DDGTLITA- 237
Cdd:pfam00743 242 lrnilptsisnwlmekqmnrrfnhenyglkpknralskepvvnddLPNRILCGAVKVKPNVKEFTETsaifEDGTVEEDi 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506045   238 DAIIVCTGYFYKYPFLSDNILRVkENNQLVspIFEHVV--HAEYPnSLYFIGL-NLVTITFPLFEYQVKMALSFATGRAP 314
Cdd:pfam00743 322 DVVIFATGYTFAFPFLEESLVKV-ENNKVS--LYKYVFppNLEKP-TLAIIGLiQPLGSIIPTVELQARWATRVFKGLCT 397

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 17506045   315 IP-DRKMLIDYEKNQIEHQKSRGLAVRfyHLLQSEQWEYLARIA 357
Cdd:pfam00743 398 LPsQSEMMAEINKRQEKKIKRFGDSQS--HTIQTDYIDYMDELA 439
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 24-289 3.67e-38

Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];


Pssm-ID: 441675 [Multi-domain]  Cd Length: 414  Bit Score: 142.31  E-value: 3.67e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506045  24 QGLEVEVFEQTGNVGGTWvyskqtgsHSSMYQNMTTNLPKEVMQFRGVPFRNELPSFLTHENVREYLQEFSQ----GMPI 99
Cdd:COG2072  28 AGIDFVVLEKADDVGGTW--------RDNRYPGLRLDTPSHLYSLPFFPNWSDDPDFPTGDEILAYLEAYADkfglRRPI 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506045 100 HFNQTVENVE--RIDDKWKVTTHHGagiDEHFFDIVFVCNGHYFAPNNPY--EESAFEGSFIHSHDYRHSKDYIDKEVIV 175
Cdd:COG2072 100 RFGTEVTSARwdEADGRWTVTTDDG---ETLTARFVVVATGPLSRPKIPDipGLEDFAGEQLHSADWRNPVDLAGKRVLV 176

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506045 176 IGAGPSGIDISLQLSETAKKITLISKKATY---------------------------------------------PTL-- 208
Cdd:COG2072 177 VGTGASAVQIAPELARVAAHVTVFQRTPPWvlprpnydpergrpanylgleappalnrrdarawlrrllraqvkdPELgl 256

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506045 209 --PD---------------------NITQISQHVKQVVPEGCETDDGTLITADAIIVCTGYFYKYPFLSdnILRVKENNQ 265
Cdd:COG2072 257 ltPDyppgckrpllstdyyealrrgNVELVTGGIERITEDGVVFADGTEHEVDVIVWATGFRADLPWLA--PLDVRGRDG 334

                       330       340
                ....*....|....*....|....*
gi 17506045 266 LVSPI-FEHVVHAEYPNsLYFIGLN 289
Cdd:COG2072 335 RSGPRaYLGVVVPGFPN-LFFLGPN 358
Pyr_redox_3 pfam13738
Pyridine nucleotide-disulphide oxidoreductase;
88-287 3.84e-13

Pyridine nucleotide-disulphide oxidoreductase;


Pssm-ID: 404603 [Multi-domain]  Cd Length: 296  Bit Score: 69.56  E-value: 3.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506045    88 EYLQE--FSQGMPIHFNQTVENVERIDDKWKVTTHHGagidEHFFDIVFVCNGHYFAPNNPyeesAFEGSFIHSHDYRHS 165
Cdd:pfam13738  79 EYLRRvaDHFELPINLFEEVTSVKKEDDGFVVTTSKG----TYQARYVIIATGEFDFPNKL----GVPELPKHYSYVKDF 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506045   166 KDYIDKEVIVIGAGPSGIDISLQLSETAKKITLISKKATYPTL---------PDN--------------------ITQIS 216
Cdd:pfam13738 151 HPYAGQKVVVIGGYNSAVDAALELVRKGARVTVLYRGSEWEDRdsdpsyslsPDTlnrleelvkngkikahfnaeVKEIT 230

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17506045   217 QHVKQVVpegCETDDGT-LITADAIIVCTGYFYKYPFLSDNILRVKENNqlvspifEHVVHAE-----YPNsLYFIG 287
Cdd:pfam13738 231 EVDVSYK---VHTEDGRkVTSNDDPILATGYHPDLSFLKKGLFELDEDG-------RPVLTEEtestnVPG-LFLAG 296
YdhS COG4529
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];
14-200 3.40e-06

Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];


Pssm-ID: 443597 [Multi-domain]  Cd Length: 466  Bit Score: 48.80  E-value: 3.40e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506045  14 GLAAAKH---SLAQGLEVEVFEQTGNVGGTWVYSKQTGSHSsmyqnmtTNLPKEVMQfrgvPFRNELPSFLT--HEN--- 85
Cdd:COG4529  17 GTALAIHllrRAPEPLRITLFEPRPELGRGVAYSTDSPEHL-------LNVPAGRMS----AFPDDPDHFLRwlRENgar 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506045  86 -------------------VREYLQEFSQGMP-----IHFNQTVENVERIDDKWKVTTHHGAgidEHFFDIVFVCNGHyF 141
Cdd:COG4529  86 aapaidpdafvprrlfgeyLRERLAEALARAPagvrlRHIRAEVVDLERDDGGYRVTLADGE---TLRADAVVLATGH-P 161

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17506045 142 APNNPYEESAFEGSFIHShDYRHSK-DYIDKE--VIVIGAGPSGIDI--SLQLSETAKKITLIS 200
Cdd:COG4529 162 PPAPPPGLAAGSPRYIAD-PWPPGAlARIPPDarVLIIGTGLTAIDVvlSLAARGHRGPITALS 224
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
172-251 2.92e-05

Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 45.50  E-value: 2.92e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506045 172 EVIVIGAGPSGIDISLQLSETAKKITLISKKAT------------YPTLPDNIT----------Q--------ISQHVKQ 221
Cdd:COG0492   2 DVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEPggqlattkeienYPGFPEGISgpelaerlreQaerfgaeiLLEEVTS 81

                        90       100       110
                ....*....|....*....|....*....|....
gi 17506045 222 VVPEG----CETDDGTLITADAIIVCTGYFYKYP 251
Cdd:COG0492  82 VDKDDgpfrVTTDDGTEYEAKAVIIATGAGPRKL 115
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
21-199 7.33e-05

Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 44.34  E-value: 7.33e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506045  21 SLA-------QGLEVEVFEQtGNVGGtwvyskqtgshssmyQNMTTnlpKEVMQFRGVPfrnelpsflthENVR--EYLQ 91
Cdd:COG0492  12 GLTaaiyaarAGLKTLVIEG-GEPGG---------------QLATT---KEIENYPGFP-----------EGISgpELAE 61

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506045  92 EFSQ-----GMPIHFnQTVENVERIDDKWKVTTHHGagiDEHFFDIVFVCNG-HYFAPNNPYEEsAFEGSFIHS------ 159
Cdd:COG0492  62 RLREqaerfGAEILL-EEVTSVDKDDGPFRVTTDDG---TEYEAKAVIIATGaGPRKLGLPGEE-EFEGRGVSYcatcdg 136

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 17506045 160 HDYRhskdyiDKEVIVIGAGPSGIDISLQLSETAKKITLI 199
Cdd:COG0492 137 FFFR------GKDVVVVGGGDSALEEALYLTKFASKVTLI 170
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 3-246 2.58e-04

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 42.69  E-value: 2.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506045     3 KRVCVIGAGAAGLAAAKHSLAQGLEVEVFEqtgnVGGTWVYSKqtgshssmyqnmtTNLPKEVMQFRGVPF-RNELPSFL 81
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIE----DEGTCPYGG-------------CVLSKALLGAAEAPEiASLWADLY 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506045    82 THenVREYLQEFSQGMPIHFNqtvENVERIDDKWK--VTTHHGAGIDEHF-FDIVFVCNG-HYFAPNNP-YEESAFEGSF 156
Cdd:pfam07992  64 KR--KEEVVKKLNNGIEVLLG---TEVVSIDPGAKkvVLEELVDGDGETItYDRLVIATGaRPRLPPIPgVELNVGFLVR 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506045   157 IHSHDYRHSKDYIDKEVIVIGAGPSGIDISLQLSETAKKITLI--SKKATyPTLPDNITQISQH--------------VK 220
Cdd:pfam07992 139 TLDSAEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIeaLDRLL-RAFDEEISAALEKalekngvevrlgtsVK 217

                         250       260       270
                  ....*....|....*....|....*....|
gi 17506045   221 QVVPEG----CETDDGTLITADAIIVCTGY 246
Cdd:pfam07992 218 EIIGDGdgveVILKDGTEIDADLVVVAIGR 247
Lys_Orn_oxgnase pfam13434
L-lysine 6-monooxygenase/L-ornithine 5-monooxygenase; This is a family of Rossmann fold ...
 74-201 7.34e-04

L-lysine 6-monooxygenase/L-ornithine 5-monooxygenase; This is a family of Rossmann fold oxidoreductases that catalyze NADPH-dependent hydroxylation and are involved in siderophore biosynthesis. This family includes L-ornithine 5-monooxygenase, which catalyzes the hydroxylation of L-ornithine at the N5 position, and L-lysine 6-monooxygenase, which catalyzes the hydroxylation of lysine at the N6 position (EC:1.14.13.59).


Pssm-ID: 433204 [Multi-domain]  Cd Length: 338  Bit Score: 41.42  E-value: 7.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506045    74 RNELPSFLTHENVR-------EYLQEFSQGMP--IHFNQTVENVEriddkwkvttHHGAGIDEHFfdIVFVCN-----GH 139
Cdd:pfam13434  78 HGRLYSFYNLETFFpsrrefnDYLQWAASHLPnrLRFGQEVESVE----------PDAERGEPLL--RVRVRDadgeeTT 145

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17506045   140 YFAPN-------NPYEESAFEGS--FIHSHDY--RHSKDYIDKEVIVIGAGPSGIDISLQL--SETAKKITLISK 201
Cdd:pfam13434 146 FLARNlvlgtggEPYIPECARGGerVFHSSEYleRIDRLAAKKRIAVVGSGQSAAEIFRDLlrRGPAYELTWVTR 220
LhgO COG0579
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
88-140 8.07e-04

L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];


Pssm-ID: 440344 [Multi-domain]  Cd Length: 418  Bit Score: 41.28  E-value: 8.07e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 17506045  88 EYLQEfsQGMPIHFNQTVENVERIDDKWKVTTHHGagidEHFFDIVFVCNGHY 140
Cdd:COG0579 161 ENAEA--NGVELLLNTEVTGIEREGDGWEVTTNGG----TIRARFVINAAGLY 207
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 151-245 1.83e-03

Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440335 [Multi-domain]  Cd Length: 296  Bit Score: 40.05  E-value: 1.83e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506045 151 AFEGSFIHSHDYRHSKDYIDKE---VIVIGAGPSGIDISLQLSETAKKITLISKKatyptlPDNITQISQHVKQVVpEGC 227
Cdd:COG0569  73 VLFGGLLEALRRRRMERGIKKLkmhVIIIGAGRVGRSLARELEEEGHDVVVIDKD------PERVERLAEEDVLVI-VGD 145

                        90       100
                ....*....|....*....|...
gi 17506045 228 ETDDGTLI-----TADAIIVCTG 245
Cdd:COG0569 146 ATDEEVLEeagieDADAVIAATG 168
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
169-246 2.18e-03

Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 40.23  E-value: 2.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506045 169 IDKEVIVIGAGPSGIDISLQLSETAKKITLISKKA-----------TYPT-------LPDNITQISQH----------VK 220
Cdd:COG1148 139 VNKRALVIGGGIAGMTAALELAEQGYEVYLVEKEPelggraaqlhkTFPGldcpqciLEPLIAEVEANpnitvytgaeVE 218

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 17506045 221 QVvpEGC--------ETDDGTLIT--ADAIIVCTGY 246
Cdd:COG1148 219 EV--SGYvgnftvtiKKGPREEIEieVGAIVLATGF 252
MnmC_Cterm TIGR03197
tRNA U-34 5-methylaminomethyl-2-thiouridine biosynthesis protein MnmC, C-terminal domain; In ...
 86-143 3.45e-03

tRNA U-34 5-methylaminomethyl-2-thiouridine biosynthesis protein MnmC, C-terminal domain; In Escherichia coli, the protein previously designated YfcK is now identified as the bifunctional enzyme MnmC. It acts, following the action of the heterotetramer of GidA and MnmE, in the modification of U-34 of certain tRNA to 5-methylaminomethyl-2-thiouridine (mnm5s2U). In other bacterial, the corresponding proteins are usually but always found as a single polypeptide chain, but occasionally as the product of tandem genes. This model represents the C-terminal region of the multifunctional protein. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274478 [Multi-domain]  Cd Length: 381  Bit Score: 39.17  E-value: 3.45e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17506045    86 VREYLQEFSQGMPIHFNQTVENVERIDDKWKVTTHHGAGIDehfFDIVFVCNGH---YFAP 143
Cdd:TIGR03197 138 CRALLAHAGIRLTLHFNTEITSLERDGEGWQLLDANGEVIA---ASVVVLANGAqapQLAQ 195
mnmC PRK01747
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ...
 86-139 7.25e-03

bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent 5-carboxymethylaminomethyl-2-thiouridine(34) oxidoreductase MnmC;


Pssm-ID: 234978 [Multi-domain]  Cd Length: 662  Bit Score: 38.67  E-value: 7.25e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 17506045   86 VREYLQEFSQGMPIHFNQTVENVERIDDKWKVtTHHGAGIDEHffDIVFVCNGH 139
Cdd:PRK01747 411 CRALLALAGQQLTIHFGHEVARLEREDDGWQL-DFAGGTLASA--PVVVLANGH 461
 
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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