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Conserved domains on  [gi|218562880|ref|YP_002344659|]
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bifunctional tRNA (mnm(5)s(2)U34)-methyltransferase/FAD-dependent cmnm(5)s(2)U34 oxidoreductase [Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819]

Protein Classification

bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent 5-carboxymethylaminomethyl-2-thiouridine(34) oxidoreductase MnmC( domain architecture ID 11479706)

bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent 5-carboxymethylaminomethyl-2-thiouridine(34) oxidoreductase MnmC catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA: the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, and the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34

CATH:  3.50.50.60|3.30.9.10|2.20.25.110
EC:  2.1.1.61|1.5.-.-
Gene Ontology:  GO:0004808|GO:0032259|GO:1904047|GO:0016645|GO:0002097
PubMed:  23617613|12504684|12826405
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
mnmC PRK01747
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ...
 1-613 0e+00

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: 747.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880   1 MKKAKLIFK-DNTPFSLDFDDFYFNFKDGLNESKFVYTHS------FEWKNQENFIIAESGFGIGLNFFLTLKRFLE--- 70
Cdd:PRK01747   5 IQPATLEFNeDGTPVSRQFDDVYFSNDNGLEETRYVFLGGnglperWAEHPRRRFVIAETGFGTGLNFLATWQAFDQfrq 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880  71 TTPSKRPKKLFYISVEAFYIEKEQLREIYQKlefYEEFKELLEQFLKFYPKAKEGIYRFYFED--CFLDLVFEDIA-VLK 147
Cdd:PRK01747  85 RHPPARLKRLHFISFEKFPLTRADLARAHQH---WPELAPLAEQLQAQWPLLLPGCHRLLFDDgrVTLDLWFGDANeLLP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880 148 ELDFKADVWYLDGFSPNKNSQMFDENLIFEVARLSKKNTQICTFSSASFLQKNLKKYGFRVEKTKGF-RKREMIKAYLEN 226
Cdd:PRK01747 162 QLDARADAWFLDGFAPAKNPDMWSPNLFNALARLARPGATLATFTSAGFVRRGLQEAGFTVRKVKGFgRKREMLVGELEQ 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880 227 ELEFKDKEAYFSRTfSSLKNKKVAIIGAGISSAVLAYELSLRGFEIDIFEKHLELGKGASGNESGILSSLILKPKVNLGE 306
Cdd:PRK01747 242 TLPAPLAAPWFARP-GSPKARDAAIIGGGIAGAALALALARRGWQVTLYEADEAPAQGASGNRQGALYPLLSKDDNALSR 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880 307 FSELSFIEASRFYRQI------LDLEFKGVVEFAHNDLMQERF------------------DTQRENVLFKISKNQAFLE 362
Cdd:PRK01747 321 FFRAAFLFARRFYDALpaagvaFDHDWCGVLQLAWDEKSAEKIakmlalglpaelaraldaEEAEELAGLPVPCGGIFYP 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880 363 EGGVIFPKKLVKNLFEKSKA--CIYFNHEFQAYKFENGCFSLKFKNDVVKSdYAVLIYAMGADAKDFVFYDEMKLSKVRG 440
Cdd:PRK01747 401 QGGWLCPAELCRALLALAGQqlTIHFGHEVARLEREDDGWQLDFAGGTLAS-APVVVLANGHDAARFAQTAHLPLYSVRG 479

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880 441 QVTHLKPFLDTPFP---LSSKAYICPV-KDDLQVIGASYDRLNASLESKEEDDKQNIENIADFMD-----KNTKLEIIGS 511
Cdd:PRK01747 480 QVSHLPTTPALSALkqvLCYDGYLTPQpANGTHCIGASYDRDDTDTAFREADHQENLERLAECLPqalwaKEVDVSALQG 559

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880 512 KVGFRSYSSDRFMIVGNAYDEAFYKEEYKALLWTKNkeQKPAKMSCNLYFNFAHGSRGFSTSVLAARYLCALINNEPLCL 591
Cdd:PRK01747 560 RVGFRCASRDRLPMVGNVPDEAATLAEYAALANQQP--ARDAPRLPGLYVAGALGSRGLCSAPLGAELLASQIEGEPLPL 637

                        650       660
                 ....*....|....*....|..
gi 218562880 592 EKKYIHAIHPARFLIRKLKKGL 613
Cdd:PRK01747 638 ERDLLAALHPNRFWVRKLLKGK 659
 
Name Accession Description Interval E-value
mnmC PRK01747
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ...
 1-613 0e+00

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: 747.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880   1 MKKAKLIFK-DNTPFSLDFDDFYFNFKDGLNESKFVYTHS------FEWKNQENFIIAESGFGIGLNFFLTLKRFLE--- 70
Cdd:PRK01747   5 IQPATLEFNeDGTPVSRQFDDVYFSNDNGLEETRYVFLGGnglperWAEHPRRRFVIAETGFGTGLNFLATWQAFDQfrq 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880  71 TTPSKRPKKLFYISVEAFYIEKEQLREIYQKlefYEEFKELLEQFLKFYPKAKEGIYRFYFED--CFLDLVFEDIA-VLK 147
Cdd:PRK01747  85 RHPPARLKRLHFISFEKFPLTRADLARAHQH---WPELAPLAEQLQAQWPLLLPGCHRLLFDDgrVTLDLWFGDANeLLP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880 148 ELDFKADVWYLDGFSPNKNSQMFDENLIFEVARLSKKNTQICTFSSASFLQKNLKKYGFRVEKTKGF-RKREMIKAYLEN 226
Cdd:PRK01747 162 QLDARADAWFLDGFAPAKNPDMWSPNLFNALARLARPGATLATFTSAGFVRRGLQEAGFTVRKVKGFgRKREMLVGELEQ 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880 227 ELEFKDKEAYFSRTfSSLKNKKVAIIGAGISSAVLAYELSLRGFEIDIFEKHLELGKGASGNESGILSSLILKPKVNLGE 306
Cdd:PRK01747 242 TLPAPLAAPWFARP-GSPKARDAAIIGGGIAGAALALALARRGWQVTLYEADEAPAQGASGNRQGALYPLLSKDDNALSR 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880 307 FSELSFIEASRFYRQI------LDLEFKGVVEFAHNDLMQERF------------------DTQRENVLFKISKNQAFLE 362
Cdd:PRK01747 321 FFRAAFLFARRFYDALpaagvaFDHDWCGVLQLAWDEKSAEKIakmlalglpaelaraldaEEAEELAGLPVPCGGIFYP 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880 363 EGGVIFPKKLVKNLFEKSKA--CIYFNHEFQAYKFENGCFSLKFKNDVVKSdYAVLIYAMGADAKDFVFYDEMKLSKVRG 440
Cdd:PRK01747 401 QGGWLCPAELCRALLALAGQqlTIHFGHEVARLEREDDGWQLDFAGGTLAS-APVVVLANGHDAARFAQTAHLPLYSVRG 479

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880 441 QVTHLKPFLDTPFP---LSSKAYICPV-KDDLQVIGASYDRLNASLESKEEDDKQNIENIADFMD-----KNTKLEIIGS 511
Cdd:PRK01747 480 QVSHLPTTPALSALkqvLCYDGYLTPQpANGTHCIGASYDRDDTDTAFREADHQENLERLAECLPqalwaKEVDVSALQG 559

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880 512 KVGFRSYSSDRFMIVGNAYDEAFYKEEYKALLWTKNkeQKPAKMSCNLYFNFAHGSRGFSTSVLAARYLCALINNEPLCL 591
Cdd:PRK01747 560 RVGFRCASRDRLPMVGNVPDEAATLAEYAALANQQP--ARDAPRLPGLYVAGALGSRGLCSAPLGAELLASQIEGEPLPL 637

                        650       660
                 ....*....|....*....|..
gi 218562880 592 EKKYIHAIHPARFLIRKLKKGL 613
Cdd:PRK01747 638 ERDLLAALHPNRFWVRKLLKGK 659
MnmC_Cterm TIGR03197
tRNA U-34 5-methylaminomethyl-2-thiouridine biosynthesis protein MnmC, C-terminal domain; In ...
 261-606 2.65e-116

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: 351.57  E-value: 2.65e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880  261 LAYELSLRGFEIDIFEKHLELGKGASGNESGILSSLILKPKVNLGEFSELSFIEASRFYRQIL------DLEFKGVVEFA 334
Cdd:TIGR03197   1 TAYSLARRGWQVTLYEQDEAPAQGASGNPQGALYPLLSADDNPLSRFFLAAFLYARRFYRQLAeagfpfDHEWCGVLQLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880  335 HNDLMQERFDTQ------RENVLFKISKNQA-------------FLEEGGVIFPKKLVKNLFEKSKA--CIYFNHEFQAY 393
Cdd:TIGR03197  81 YDEKEAERLQKLleqlgfPEELARWVDAEQAsqlagiplpygglFFPQGGWLSPPQLCRALLAHAGIrlTLHFNTEITSL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880  394 KFENGCFSLKFKNDVVKSdYAVLIYAMGADAKDFVFYDEMKLSKVRGQVTHLKP---FLDTPFPLSSKAYICPVKDDLQV 470
Cdd:TIGR03197 161 ERDGEGWQLLDANGEVIA-ASVVVLANGAQAPQLAQTAHLPLRPVRGQVSHLPAteaLSALKTVLCYDGYLTPANNGEHC 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880  471 IGASYDRLNASLESKEEDDKQNIENIADFMDKNTKL-----EIIGSKVGFRSYSSDRFMIVGNAYDEAFYKEEYKALLWT 545
Cdd:TIGR03197 240 IGASYDRNDDDLALREADHAENLERLAECLPALAWAsevdiSALQGRVGVRCASPDHLPLVGAVPDFEAIKEAYAELAKD 319

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 218562880  546 KNKEQK-PAKMSCNLYFNFAHGSRGFSTSVLAARYLCALINNEPLCLEKKYIHAIHPARFLI 606
Cdd:TIGR03197 320 KNRPIAePAPYYPGLYVLGGLGSRGLTSAPLAAEILAAQICGEPLPLERDLLHALHPARFLI 381
MnmC COG4121
tRNA U34 5-methylaminomethyl-2-thiouridine-forming methyltransferase MnmC [Translation, ...
 4-224 5.14e-63

tRNA U34 5-methylaminomethyl-2-thiouridine-forming methyltransferase MnmC [Translation, ribosomal structure and biogenesis]; tRNA U34 5-methylaminomethyl-2-thiouridine-forming methyltransferase MnmC is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443297  Cd Length: 245  Bit Score: 208.13  E-value: 5.14e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880   4 AKLIFKD--NTPFSLDFDDFYFNFKDGLNESKFVYTH----SFEWKNQENFIIAESGFGIGLNFFLTLKRFLETTPskRP 77
Cdd:COG4121    8 ATLTTADgsGTPYSPEFDDVYHSKHGALQESRHVFLEgnllPERWQGRSPFVILETGFGTGLNFLATWQAWREDAP--RN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880  78 KKLFYISVEAFYIEKEQLREIyqkLEFYEEFKELLEQFLKFYPKAKEGIYRFYFED--CFLDLVFEDIA-VLKELD--FK 152
Cdd:COG4121   86 ARLHFISVEKYPLTPEDLARA---LAAWPELAPLAEQLHAQWPPLVPGCHRLELDGgrVTLTLLFGDAReLLPQLDqnGR 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 218562880 153 ADVWYLDGFSPNKNSQMFDENLIFEVARLSKKNTQICTFSSASFLQKNLKKYGFRVEKTKGF-RKREMIKAYL 224
Cdd:COG4121  163 ADAWFLDGFAPAKNPEMWTEELFAKLARLLKPGGTLATYTAAGAVRRALQAAGFEVEKLPGFgGKREMLRARK 235
tRNA_MNMC2 NF033855
tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD; This HMM describes either ...
 13-222 3.30e-51

tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD; This HMM describes either the N-terminal region, called MNMC2, of the tRNA modification bifunctional enzyme MnmC, or a free-standing protein that performs the same methyltransferase function, in partnership with an FAD-dependent protein, or C-terminal region, called MNMC1 (see TIGR03197).


Pssm-ID: 468209  Cd Length: 205  Bit Score: 175.35  E-value: 3.30e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880  13 PFSLDFDDFYFNFKDGLNESKFVY------THSFewknQENFIIAESGFGIGLNFFLTLKRFLEttpskRPKKLFYISVE 86
Cdd:NF033855   1 PVSPRFDDHYFSKHGGLAETRHVFlegnglPERF----APGFTILELGFGTGLNFLATLAAWEE-----SGAPLHYTSFE 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880  87 AFYIEKEQLREIyqkLEFYEEFKELLEQFLKFYPkakEGIYRFyFEDCFLDLVFEDI-AVLKELDFKADVWYLDGFSPNK 165
Cdd:NF033855  72 AFPLSAEDLARA---LYAFPELAPLAEALLAAWP---EEPLKL-TGDFTLTVIFGDArETLPQLDGRADAWYLDGFSPAK 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 218562880 166 NSQMFDENLIFEVARLSKKNTQICTFSSASFLQKNLKKYGFRVEKTKGF-RKREMIKA 222
Cdd:NF033855 145 NPEMWSPELFAELARLTAPGGTLATYTAAGFVRRALQAAGFTVERLPGFgGKREMLRG 202
Methyltransf_30 pfam05430
S-adenosyl-L-methionine-dependent methyltransferase; This family is a S-adenosyl-L-methionine ...
 106-225 2.88e-49

S-adenosyl-L-methionine-dependent methyltransferase; This family is a S-adenosyl-L-methionine (SAM)-dependent methyltransferase. It is often found in association with pfam01266, where it is responsible for catalysing the transfer of a methyl group from S-adenosyl-L-methionine to 5-aminomethyl-2-thiouridine to form 5-methylaminomethyl-2-thiouridine.


Pssm-ID: 398864 [Multi-domain]  Cd Length: 124  Bit Score: 167.08  E-value: 2.88e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880  106 EEFKELLEQFLKFYPKAKEGIYRFYF--EDCFLDLVFEDI-AVLKELDFKADVWYLDGFSPNKNSQMFDENLIFEVARLS 182
Cdd:pfam05430   1 PELAEIAEQLLKQWPLPLAGCHRIEFagGRVTLDLWFGDArAALPELDFKADAWFLDGFSPAKNPEMWTEEFFALLARRS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 218562880  183 KKNTQICTFSSASFLQKNLKKYGFRVEKTKGF-RKREMIKAYLE 225
Cdd:pfam05430  81 KPGGTLATYSSAGFVRRGLIAAGFHVGKRPGFgRKREMLVASKP 124
 
Name Accession Description Interval E-value
mnmC PRK01747
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ...
 1-613 0e+00

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: 747.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880   1 MKKAKLIFK-DNTPFSLDFDDFYFNFKDGLNESKFVYTHS------FEWKNQENFIIAESGFGIGLNFFLTLKRFLE--- 70
Cdd:PRK01747   5 IQPATLEFNeDGTPVSRQFDDVYFSNDNGLEETRYVFLGGnglperWAEHPRRRFVIAETGFGTGLNFLATWQAFDQfrq 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880  71 TTPSKRPKKLFYISVEAFYIEKEQLREIYQKlefYEEFKELLEQFLKFYPKAKEGIYRFYFED--CFLDLVFEDIA-VLK 147
Cdd:PRK01747  85 RHPPARLKRLHFISFEKFPLTRADLARAHQH---WPELAPLAEQLQAQWPLLLPGCHRLLFDDgrVTLDLWFGDANeLLP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880 148 ELDFKADVWYLDGFSPNKNSQMFDENLIFEVARLSKKNTQICTFSSASFLQKNLKKYGFRVEKTKGF-RKREMIKAYLEN 226
Cdd:PRK01747 162 QLDARADAWFLDGFAPAKNPDMWSPNLFNALARLARPGATLATFTSAGFVRRGLQEAGFTVRKVKGFgRKREMLVGELEQ 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880 227 ELEFKDKEAYFSRTfSSLKNKKVAIIGAGISSAVLAYELSLRGFEIDIFEKHLELGKGASGNESGILSSLILKPKVNLGE 306
Cdd:PRK01747 242 TLPAPLAAPWFARP-GSPKARDAAIIGGGIAGAALALALARRGWQVTLYEADEAPAQGASGNRQGALYPLLSKDDNALSR 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880 307 FSELSFIEASRFYRQI------LDLEFKGVVEFAHNDLMQERF------------------DTQRENVLFKISKNQAFLE 362
Cdd:PRK01747 321 FFRAAFLFARRFYDALpaagvaFDHDWCGVLQLAWDEKSAEKIakmlalglpaelaraldaEEAEELAGLPVPCGGIFYP 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880 363 EGGVIFPKKLVKNLFEKSKA--CIYFNHEFQAYKFENGCFSLKFKNDVVKSdYAVLIYAMGADAKDFVFYDEMKLSKVRG 440
Cdd:PRK01747 401 QGGWLCPAELCRALLALAGQqlTIHFGHEVARLEREDDGWQLDFAGGTLAS-APVVVLANGHDAARFAQTAHLPLYSVRG 479

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880 441 QVTHLKPFLDTPFP---LSSKAYICPV-KDDLQVIGASYDRLNASLESKEEDDKQNIENIADFMD-----KNTKLEIIGS 511
Cdd:PRK01747 480 QVSHLPTTPALSALkqvLCYDGYLTPQpANGTHCIGASYDRDDTDTAFREADHQENLERLAECLPqalwaKEVDVSALQG 559

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880 512 KVGFRSYSSDRFMIVGNAYDEAFYKEEYKALLWTKNkeQKPAKMSCNLYFNFAHGSRGFSTSVLAARYLCALINNEPLCL 591
Cdd:PRK01747 560 RVGFRCASRDRLPMVGNVPDEAATLAEYAALANQQP--ARDAPRLPGLYVAGALGSRGLCSAPLGAELLASQIEGEPLPL 637

                        650       660
                 ....*....|....*....|..
gi 218562880 592 EKKYIHAIHPARFLIRKLKKGL 613
Cdd:PRK01747 638 ERDLLAALHPNRFWVRKLLKGK 659
MnmC_Cterm TIGR03197
tRNA U-34 5-methylaminomethyl-2-thiouridine biosynthesis protein MnmC, C-terminal domain; In ...
 261-606 2.65e-116

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: 351.57  E-value: 2.65e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880  261 LAYELSLRGFEIDIFEKHLELGKGASGNESGILSSLILKPKVNLGEFSELSFIEASRFYRQIL------DLEFKGVVEFA 334
Cdd:TIGR03197   1 TAYSLARRGWQVTLYEQDEAPAQGASGNPQGALYPLLSADDNPLSRFFLAAFLYARRFYRQLAeagfpfDHEWCGVLQLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880  335 HNDLMQERFDTQ------RENVLFKISKNQA-------------FLEEGGVIFPKKLVKNLFEKSKA--CIYFNHEFQAY 393
Cdd:TIGR03197  81 YDEKEAERLQKLleqlgfPEELARWVDAEQAsqlagiplpygglFFPQGGWLSPPQLCRALLAHAGIrlTLHFNTEITSL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880  394 KFENGCFSLKFKNDVVKSdYAVLIYAMGADAKDFVFYDEMKLSKVRGQVTHLKP---FLDTPFPLSSKAYICPVKDDLQV 470
Cdd:TIGR03197 161 ERDGEGWQLLDANGEVIA-ASVVVLANGAQAPQLAQTAHLPLRPVRGQVSHLPAteaLSALKTVLCYDGYLTPANNGEHC 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880  471 IGASYDRLNASLESKEEDDKQNIENIADFMDKNTKL-----EIIGSKVGFRSYSSDRFMIVGNAYDEAFYKEEYKALLWT 545
Cdd:TIGR03197 240 IGASYDRNDDDLALREADHAENLERLAECLPALAWAsevdiSALQGRVGVRCASPDHLPLVGAVPDFEAIKEAYAELAKD 319

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 218562880  546 KNKEQK-PAKMSCNLYFNFAHGSRGFSTSVLAARYLCALINNEPLCLEKKYIHAIHPARFLI 606
Cdd:TIGR03197 320 KNRPIAePAPYYPGLYVLGGLGSRGLTSAPLAAEILAAQICGEPLPLERDLLHALHPARFLI 381
MnmC COG4121
tRNA U34 5-methylaminomethyl-2-thiouridine-forming methyltransferase MnmC [Translation, ...
 4-224 5.14e-63

tRNA U34 5-methylaminomethyl-2-thiouridine-forming methyltransferase MnmC [Translation, ribosomal structure and biogenesis]; tRNA U34 5-methylaminomethyl-2-thiouridine-forming methyltransferase MnmC is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443297  Cd Length: 245  Bit Score: 208.13  E-value: 5.14e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880   4 AKLIFKD--NTPFSLDFDDFYFNFKDGLNESKFVYTH----SFEWKNQENFIIAESGFGIGLNFFLTLKRFLETTPskRP 77
Cdd:COG4121    8 ATLTTADgsGTPYSPEFDDVYHSKHGALQESRHVFLEgnllPERWQGRSPFVILETGFGTGLNFLATWQAWREDAP--RN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880  78 KKLFYISVEAFYIEKEQLREIyqkLEFYEEFKELLEQFLKFYPKAKEGIYRFYFED--CFLDLVFEDIA-VLKELD--FK 152
Cdd:COG4121   86 ARLHFISVEKYPLTPEDLARA---LAAWPELAPLAEQLHAQWPPLVPGCHRLELDGgrVTLTLLFGDAReLLPQLDqnGR 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 218562880 153 ADVWYLDGFSPNKNSQMFDENLIFEVARLSKKNTQICTFSSASFLQKNLKKYGFRVEKTKGF-RKREMIKAYL 224
Cdd:COG4121  163 ADAWFLDGFAPAKNPEMWTEELFAKLARLLKPGGTLATYTAAGAVRRALQAAGFEVEKLPGFgGKREMLRARK 235
tRNA_MNMC2 NF033855
tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD; This HMM describes either ...
 13-222 3.30e-51

tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD; This HMM describes either the N-terminal region, called MNMC2, of the tRNA modification bifunctional enzyme MnmC, or a free-standing protein that performs the same methyltransferase function, in partnership with an FAD-dependent protein, or C-terminal region, called MNMC1 (see TIGR03197).


Pssm-ID: 468209  Cd Length: 205  Bit Score: 175.35  E-value: 3.30e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880  13 PFSLDFDDFYFNFKDGLNESKFVY------THSFewknQENFIIAESGFGIGLNFFLTLKRFLEttpskRPKKLFYISVE 86
Cdd:NF033855   1 PVSPRFDDHYFSKHGGLAETRHVFlegnglPERF----APGFTILELGFGTGLNFLATLAAWEE-----SGAPLHYTSFE 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880  87 AFYIEKEQLREIyqkLEFYEEFKELLEQFLKFYPkakEGIYRFyFEDCFLDLVFEDI-AVLKELDFKADVWYLDGFSPNK 165
Cdd:NF033855  72 AFPLSAEDLARA---LYAFPELAPLAEALLAAWP---EEPLKL-TGDFTLTVIFGDArETLPQLDGRADAWYLDGFSPAK 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 218562880 166 NSQMFDENLIFEVARLSKKNTQICTFSSASFLQKNLKKYGFRVEKTKGF-RKREMIKA 222
Cdd:NF033855 145 NPEMWSPELFAELARLTAPGGTLATYTAAGFVRRALQAAGFTVERLPGFgGKREMLRG 202
Methyltransf_30 pfam05430
S-adenosyl-L-methionine-dependent methyltransferase; This family is a S-adenosyl-L-methionine ...
 106-225 2.88e-49

S-adenosyl-L-methionine-dependent methyltransferase; This family is a S-adenosyl-L-methionine (SAM)-dependent methyltransferase. It is often found in association with pfam01266, where it is responsible for catalysing the transfer of a methyl group from S-adenosyl-L-methionine to 5-aminomethyl-2-thiouridine to form 5-methylaminomethyl-2-thiouridine.


Pssm-ID: 398864 [Multi-domain]  Cd Length: 124  Bit Score: 167.08  E-value: 2.88e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880  106 EEFKELLEQFLKFYPKAKEGIYRFYF--EDCFLDLVFEDI-AVLKELDFKADVWYLDGFSPNKNSQMFDENLIFEVARLS 182
Cdd:pfam05430   1 PELAEIAEQLLKQWPLPLAGCHRIEFagGRVTLDLWFGDArAALPELDFKADAWFLDGFSPAKNPEMWTEEFFALLARRS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 218562880  183 KKNTQICTFSSASFLQKNLKKYGFRVEKTKGF-RKREMIKAYLE 225
Cdd:pfam05430  81 KPGGTLATYSSAGFVRRGLIAAGFHVGKRPGFgRKREMLVASKP 124
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
248-603 2.02e-33

Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 131.18  E-value: 2.02e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880 248 KVAIIGAGISSAVLAYELSLRGFEIDIFEKHlELGKGASGNESGILSSLILKP-KVNLGEFSELSFieasRFYRQI---- 322
Cdd:COG0665    4 DVVVIGGGIAGLSTAYHLARRGLDVTVLERG-RPGSGASGRNAGQLRPGLAALaDRALVRLAREAL----DLWRELaael 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880 323 -LDLEFK--GVVEFAHN----DLMQERFDTQREN--VLFKISKNQA----------------FLEEGGVIFPKKLVKNL- 376
Cdd:COG0665   79 gIDCDFRrtGVLYLARTeaelAALRAEAEALRALglPVELLDAAELrerepglgspdyagglYDPDDGHVDPAKLVRALa 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880 377 --FEKSKACIYFNHEFQAYKFENG-CFSLKFKNDVVKSDYAVLiyAMGADAKDFV--FYDEMKLSKVRGQVTHLKPFLDT 451
Cdd:COG0665  159 raARAAGVRIREGTPVTGLEREGGrVTGVRTERGTVRADAVVL--AAGAWSARLLpmLGLRLPLRPVRGYVLVTEPLPDL 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880 452 PFP---LSSKAYICPVKDDLQVIGASYDRLNASLESKEEDDKQNIENIADFMDKNTKLEIIGSKVGFRSYSSDRFMIVGN 528
Cdd:COG0665  237 PLRpvlDDTGVYLRPTADGRLLVGGTAEPAGFDRAPTPERLEALLRRLRRLFPALADAEIVRAWAGLRPMTPDGLPIIGR 316

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 218562880 529 AYDEAfykeeykallwtknkeqkpakmscNLYFNFAHGSRGFSTSVLAARYLCALINNEPLCLEkkyIHAIHPAR 603
Cdd:COG0665  317 LPGAP------------------------GLYVATGHGGHGVTLAPAAGRLLADLILGGEPPLD---LAPFSPDR 364
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 248-583 1.13e-26

FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.


Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 111.34  E-value: 1.13e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880  248 KVAIIGAGISSAVLAYELSLRGFEIDIFEKHLELGKGASGNESGILSSLILKPKvnLGEFSELSfIEASRFYRQI----- 322
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGSGASGRNAGLIHPGLRYLE--PSELARLA-LEALDLWEELeeelg 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880  323 --LDLEFKGVVEFAHNDL---MQERFDTQREN--VLFKISKNQA--------------FLEEGGVIFPKKLVKNL---FE 378
Cdd:pfam01266  78 idCGFRRCGVLVLARDEEeeaLEKLLAALRRLgvPAELLDAEELrelepllpglrgglFYPDGGHVDPARLLRALaraAE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880  379 KSKACIYFNHEFQAYKFENGCFSLKFKNDVvksDYAVLiyAMGADAKDFVFYD-EMKLSKVRGQVTHLKP----FLDTPF 453
Cdd:pfam01266 158 ALGVRIIEGTEVTGIEEEGGVWGVVTTGEA---DAVVN--AAGAWADLLALPGlRLPVRPVRGQVLVLEPlpeaLLILPV 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880  454 PLSSKA----YICPVKDDLQVIGASYDRLNASLESKEEDDKQNI-ENIADFMDKNTklEIIGSKVGFRSYsSDRFMIVGN 528
Cdd:pfam01266 233 PITVDPgrgvYLRPRADGRLLLGGTDEEDGFDDPTPDPEEIEELlEAARRLFPALA--DIERAWAGLRPL-PDGLPIIGR 309

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 218562880  529 AYDEafykeeykallwtknkeqkpakmscNLYFNFAHGSRGFSTSVLAARYLCAL 583
Cdd:pfam01266 310 PGSP-------------------------GLYLATGHGGHGLTLAPGIGKLLAEL 339
LhgO COG0579
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
249-415 7.56e-13

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


Pssm-ID: 440344 [Multi-domain]  Cd Length: 418  Bit Score: 70.56  E-value: 7.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880 249 VAIIGAGISSAVLAYELS-LRGFEIDIFEKHLELGKGASGNESGIL-SSLILKP------KVNLG--EFSELSfieasrf 318
Cdd:COG0579    7 VVIIGAGIVGLALARELSrYEDLKVLVLEKEDDVAQESSGNNSGVIhAGLYYTPgslkarLCVEGneLFYELC------- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880 319 yRQiLDLEFK--GVVEFAHND----LMQERFDTQRENV---LFKISKNQA---------------FLEEGGVIFPKKLVK 374
Cdd:COG0579   80 -RE-LGIPFKrcGKLVVATGEeevaFLEKLYERGKANGvpgLEILDREELrelepllsdegvaalYSPSTGIVDPGALTR 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 218562880 375 NLFE---KSKACIYFNHEFQAYKFENGCFSLKFKNDVVKSDYAV 415
Cdd:COG0579  158 ALAEnaeANGVELLLNTEVTGIEREGDGWEVTTNGGTIRARFVI 201
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
251-282 3.62e-07

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 47.53  E-value: 3.62e-07
                          10        20        30
                  ....*....|....*....|....*....|..
gi 218562880  251 IIGAGISSAVLAYELSLRGFEIDIFEKHLELG 282
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLG 32
YdhS COG4529
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];
247-284 7.24e-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: 7.24e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 218562880 247 KKVAIIGAGISSAVLAYEL---SLRGFEIDIFEKHLELGKG 284
Cdd:COG4529    6 KRIAIIGGGASGTALAIHLlrrAPEPLRITLFEPRPELGRG 46
PRK07233 PRK07233
hypothetical protein; Provisional
 248-325 9.20e-06

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 48.34  E-value: 9.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880 248 KVAIIGAGISSAVLAYELSLRGFEIDIFEKHLELGkgasgnesGILSSLilkpkvnlgEFSELSfIEasRFY-------R 320
Cdd:PRK07233   1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLG--------GLAASF---------EFGGLP-IE--RFYhhifksdE 60


                 ....*
gi 218562880 321 QILDL 325
Cdd:PRK07233  61 ALLEL 65
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 247-282 2.90e-05

Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440845 [Multi-domain]  Cd Length: 443  Bit Score: 46.75  E-value: 2.90e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 218562880 247 KKVAIIGAGISSAVLAYELSLRGFEIDIFEKHLELG 282
Cdd:COG1232    2 KRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVG 37
PRK12409 PRK12409
D-amino acid dehydrogenase small subunit; Provisional
 247-279 3.50e-05

D-amino acid dehydrogenase small subunit; Provisional


Pssm-ID: 237093 [Multi-domain]  Cd Length: 410  Bit Score: 46.55  E-value: 3.50e-05
                         10        20        30
                 ....*....|....*....|....*....|...
gi 218562880 247 KKVAIIGAGISSAVLAYELSLRGFEIDIFEKHL 279
Cdd:PRK12409   2 SHIAVIGAGITGVTTAYALAQRGYQVTVFDRHR 34
COG3380 COG3380
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
247-287 5.17e-05

Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];


Pssm-ID: 442607 [Multi-domain]  Cd Length: 331  Bit Score: 45.64  E-value: 5.17e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 218562880 247 KKVAIIGAGISSAVLAYELSLRGFEIDIFEKhlelGKGASG 287
Cdd:COG3380    4 PDIAIIGAGIAGLAAARALQDAGHEVTVFEK----SRGVGG 40
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 246-282 1.01e-04

NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 440259 [Multi-domain]  Cd Length: 434  Bit Score: 45.13  E-value: 1.01e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 218562880 246 NKKVAIIGAGISSAVLAYELSLRGFEIDIFEKHLELG 282
Cdd:COG0493  121 GKKVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPG 157
PRK13984 PRK13984
putative oxidoreductase; Provisional
 245-276 2.50e-04

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 43.99  E-value: 2.50e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 218562880 245 KNKKVAIIGAGISSAVLAYELSLRGFEIDIFE 276
Cdd:PRK13984 282 KNKKVAIVGSGPAGLSAAYFLATMGYEVTVYE 313
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 245-278 4.39e-04

2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 440419 [Multi-domain]  Cd Length: 326  Bit Score: 42.62  E-value: 4.39e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 218562880 245 KNKKVAIIGAGISSAVLAYELSLRGFEIDIFEKH 278
Cdd:COG0654    2 MRTDVLIVGGGPAGLALALALARAGIRVTVVERA 35
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 247-282 6.49e-04

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 42.47  E-value: 6.49e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 218562880 247 KKVAIIGAGISSAVLAYELSLRGFEIDIFEKHLELG 282
Cdd:PRK11749 141 KKVAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAG 176
PRK12831 PRK12831
putative oxidoreductase; Provisional
 223-282 6.83e-04

putative oxidoreductase; Provisional


Pssm-ID: 183780 [Multi-domain]  Cd Length: 464  Bit Score: 42.31  E-value: 6.83e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 218562880 223 YLENELEFKDKEAyfsrtfssLKNKKVAIIGAGISSAVLAYELSLRGFEIDIFEKHLELG 282
Cdd:PRK12831 125 ARENGIDLSETEE--------KKGKKVAVIGSGPAGLTCAGDLAKMGYDVTIFEALHEPG 176
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 247-282 8.44e-04

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 42.17  E-value: 8.44e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 218562880 247 KKVAIIGAGIS--SAvlAYELSLRGFEIDIFEKHLELG 282
Cdd:PRK12771 138 KRVAVIGGGPAglSA--AYHLRRMGHAVTIFEAGPKLG 173
PRK07588 PRK07588
FAD-binding domain;
247-284 4.86e-03

FAD-binding domain;


Pssm-ID: 169028 [Multi-domain]  Cd Length: 391  Bit Score: 39.72  E-value: 4.86e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 218562880 247 KKVAIIGAGISSAVLAYELSLRGFEIDIFEKHLELGKG 284
Cdd:PRK07588   1 MKVAISGAGIAGPTLAYWLRRYGHEPTLIERAPELRTG 38
PRK11883 PRK11883
protoporphyrinogen oxidase; Reviewed
 247-277 5.99e-03

protoporphyrinogen oxidase; Reviewed


Pssm-ID: 237009 [Multi-domain]  Cd Length: 451  Bit Score: 39.45  E-value: 5.99e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 218562880 247 KKVAIIGAGISSAVLAYELSLRG--FEIDIFEK 277
Cdd:PRK11883   1 KKVAIIGGGITGLSAAYRLHKKGpdADITLLEA 33
Ppro0129 COG2907
Predicted flavin-containing amine oxidase [General function prediction only];
247-282 7.43e-03

Predicted flavin-containing amine oxidase [General function prediction only];


Pssm-ID: 442151 [Multi-domain]  Cd Length: 423  Bit Score: 38.94  E-value: 7.43e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 218562880 247 KKVAIIGAGISSAVLAYELSlRGFEIDIFEKHLELG 282
Cdd:COG2907    4 MRIAVIGSGISGLTAAWLLS-RRHDVTLFEANDRLG 38
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 249-282 8.86e-03

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: 38.69  E-value: 8.86e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 218562880 249 VAIIGAGISSAVLAYELSLRGFEIDIFEKHLELG 282
Cdd:COG2072    9 VVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVG 42
 
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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