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Conserved domains on  [gi|1514766286|dbj|BBH25336|]
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tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG [Intestinibaculum porci]

Protein Classification

tRNA uridine-5-carboxymethylaminomethyl modification enzyme MnmG/GidA( domain architecture ID 11418560)

tRNA uridine-5-carboxymethylaminomethyl modification enzyme MnmG/GidA such as tRNA uridine-5-carboxymethylaminomethyl(34) synthesis enzyme MnmG, which is involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34

CATH:  1.10.10.1800
EC:  2.1.1.-
Gene Ontology:  GO:0050660|GO:0002098|GO:0030488|GO:0008033
PubMed:  18565343|19801413|19767610|11544186
SCOP:  4006485

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MnmG COG0445
tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal ...
 2-614 0e+00

tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA is part of the Pathway/BioSystem: tRNA modification


:

Pssm-ID: 440214 [Multi-domain]  Cd Length: 626  Bit Score: 1096.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286   2 YDVIVVGAGHAGIEACLAPARIGKKTLLVTSHFANAGQMPCNTAIGGPAKGIIVREVDALGGQMGKSADANYTQMKMLNT 81
Cdd:COG0445     7 YDVIVVGGGHAGCEAALAAARMGAKTLLLTHNLDTIGQMSCNPAIGGIAKGHLVREIDALGGEMGRAADKTGIQFRMLNT 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286  82 AKGPGVWALRAQEDKKTYPRYMQKVLKEQENLDIIEAMVEDLIVEENTCKGVILEDGQRIEGKTVILTTGTYLKAEILVG 161
Cdd:COG0445    87 SKGPAVRAPRAQADRKLYRAAMRETLENQPNLDLIQGEVEDLIVEDGRVTGVVTADGIEFRAKAVVLTTGTFLNGLIHIG 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286 162 DQKTPSGPDQERYSKFLSDKLRDYGFRIQRLKTGTPPRIKAESIDFSKTSVQPGTDAKLSFSYSTKTFTPlaEQDVCYLT 241
Cdd:COG0445   167 EKSYPGGRAGEPPSVGLSESLRELGFELGRLKTGTPPRIDGRSIDFSKLEEQPGDEPPPPFSFLTEKIHP--PQIPCWIT 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286 242 YTTAKTHQLIRDNLSKSSMYSGIVKGVGPRYCPSIEDKVVKFADKERHQLFLEPESRETNSIYLQGFSTSMPHDIQEQMV 321
Cdd:COG0445   245 YTNEETHEIIRENLHRSPMYSGVIEGVGPRYCPSIEDKIVRFADKDRHQIFLEPEGLDTNEVYPNGISTSLPEDVQLAML 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286 322 HSLPGLEHAEFLKYAYAIEYDAIDPLQLWPSLETKVIKNLYTAGQINGTSGYEEAAGQGLIAGINAAKKVDGIAPLILKR 401
Cdd:COG0445   325 RSIPGLENAEILRPGYAIEYDYVDPTQLKPTLETKKIEGLFFAGQINGTTGYEEAAAQGLMAGINAALKAQGKEPFILDR 404

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286 402 NEAYIGVLIDDLVTKGTKEPYRMLTSRAEYRLLLRHDNADERLMKYGYEAGLVKEETYQEYLTKMDHIDQEITRLSTLRF 481
Cdd:COG0445   405 SEAYIGVLIDDLVTKGTDEPYRMFTSRAEYRLLLRQDNADLRLTEKGYELGLVSDERYERFEEKKEAIEEEIERLKSTRV 484

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286 482 TPKSEINERIEELGSTKLKEGISAKVLLQRPELTYDKIKDYLGNV-DLTDEERLRVTINIKYKGYIDKALRQVEKVKAME 560
Cdd:COG0445   485 TPNEEVNEGLEELGSSPLKRGVSLFDLLRRPEITYEDLAELDPELpDLDPEVAEQVEIEIKYEGYIERQEEEIEKLKRLE 564

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1514766286 561 EKHIPEDIDYDQVINLALEAKQKLKEVRPLTVGQASRISGINPADISVLLIYLK 614
Cdd:COG0445   565 NLKIPEDFDYDAIPGLSNEAREKLKKIRPETLGQASRISGVTPADISLLLVYLK 618
 
Name Accession Description Interval E-value
MnmG COG0445
tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal ...
 2-614 0e+00

tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440214 [Multi-domain]  Cd Length: 626  Bit Score: 1096.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286   2 YDVIVVGAGHAGIEACLAPARIGKKTLLVTSHFANAGQMPCNTAIGGPAKGIIVREVDALGGQMGKSADANYTQMKMLNT 81
Cdd:COG0445     7 YDVIVVGGGHAGCEAALAAARMGAKTLLLTHNLDTIGQMSCNPAIGGIAKGHLVREIDALGGEMGRAADKTGIQFRMLNT 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286  82 AKGPGVWALRAQEDKKTYPRYMQKVLKEQENLDIIEAMVEDLIVEENTCKGVILEDGQRIEGKTVILTTGTYLKAEILVG 161
Cdd:COG0445    87 SKGPAVRAPRAQADRKLYRAAMRETLENQPNLDLIQGEVEDLIVEDGRVTGVVTADGIEFRAKAVVLTTGTFLNGLIHIG 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286 162 DQKTPSGPDQERYSKFLSDKLRDYGFRIQRLKTGTPPRIKAESIDFSKTSVQPGTDAKLSFSYSTKTFTPlaEQDVCYLT 241
Cdd:COG0445   167 EKSYPGGRAGEPPSVGLSESLRELGFELGRLKTGTPPRIDGRSIDFSKLEEQPGDEPPPPFSFLTEKIHP--PQIPCWIT 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286 242 YTTAKTHQLIRDNLSKSSMYSGIVKGVGPRYCPSIEDKVVKFADKERHQLFLEPESRETNSIYLQGFSTSMPHDIQEQMV 321
Cdd:COG0445   245 YTNEETHEIIRENLHRSPMYSGVIEGVGPRYCPSIEDKIVRFADKDRHQIFLEPEGLDTNEVYPNGISTSLPEDVQLAML 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286 322 HSLPGLEHAEFLKYAYAIEYDAIDPLQLWPSLETKVIKNLYTAGQINGTSGYEEAAGQGLIAGINAAKKVDGIAPLILKR 401
Cdd:COG0445   325 RSIPGLENAEILRPGYAIEYDYVDPTQLKPTLETKKIEGLFFAGQINGTTGYEEAAAQGLMAGINAALKAQGKEPFILDR 404

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286 402 NEAYIGVLIDDLVTKGTKEPYRMLTSRAEYRLLLRHDNADERLMKYGYEAGLVKEETYQEYLTKMDHIDQEITRLSTLRF 481
Cdd:COG0445   405 SEAYIGVLIDDLVTKGTDEPYRMFTSRAEYRLLLRQDNADLRLTEKGYELGLVSDERYERFEEKKEAIEEEIERLKSTRV 484

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286 482 TPKSEINERIEELGSTKLKEGISAKVLLQRPELTYDKIKDYLGNV-DLTDEERLRVTINIKYKGYIDKALRQVEKVKAME 560
Cdd:COG0445   485 TPNEEVNEGLEELGSSPLKRGVSLFDLLRRPEITYEDLAELDPELpDLDPEVAEQVEIEIKYEGYIERQEEEIEKLKRLE 564

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1514766286 561 EKHIPEDIDYDQVINLALEAKQKLKEVRPLTVGQASRISGINPADISVLLIYLK 614
Cdd:COG0445   565 NLKIPEDFDYDAIPGLSNEAREKLKKIRPETLGQASRISGVTPADISLLLVYLK 618
gidA TIGR00136
glucose-inhibited division protein A; GidA, the longer of two forms of GidA-related proteins, ...
 2-614 0e+00

glucose-inhibited division protein A; GidA, the longer of two forms of GidA-related proteins, appears to be present in all complete eubacterial genomes so far, as well as Saccharomyces cerevisiae. A subset of these organisms have a closely related protein. GidA is absent in the Archaea. It appears to act with MnmE, in an alpha2/beta2 heterotetramer, in the 5-carboxymethylaminomethyl modification of uridine 34 in certain tRNAs. The shorter, related protein, previously called gid or gidA(S), is now called TrmFO (see model TIGR00137). [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 272927 [Multi-domain]  Cd Length: 616  Bit Score: 911.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286   2 YDVIVVGAGHAGIEACLAPARIGKKTLLVTSHFANAGQMPCNTAIGGPAKGIIVREVDALGGQMGKSADANYTQMKMLNT 81
Cdd:TIGR00136   1 FDVIVIGGGHAGCEAALAAARLGAKTLLLTLNLDTIGKCSCNPAIGGPAKGILVKEIDALGGEMGKAADKTGLQFRVLNS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286  82 AKGPGVWALRAQEDKKTYPRYMQKVLKEQENLDIIEAMVEDLIVEENT-CKGVILEDGQRIEGKTVILTTGTYLKAEILV 160
Cdd:TIGR00136  81 SKGPAVRATRAQIDKILYQKWMRNQLENQPNLSLFQGEVEDLILEDNDeIKGVVTKDGNEFRAKAVIITTGTFLRGKIHI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286 161 GDQKTPSGPDQERYSKFLSDKLRDYGFRIQRLKTGTPPRIKAESIDFSKTSVQPGTDAKLSFSYSTKTFTPlaEQDVCYL 240
Cdd:TIGR00136 161 GDKSYEAGRAGEQASYGLSTTLRELGFKTGRLKTGTPPRIDKRSIDFSKLEVQFGDTQPPAFSFTNKNFLP--QQLPCYL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286 241 TYTTAKTHQLIRDNLSKSSMYSGIVKGVGPRYCPSIEDKVVKFADKERHQLFLEPESRETNSIYLQGFSTSMPHDIQEQM 320
Cdd:TIGR00136 239 THTNPKTHQIIRDNLHRSPMYSGSIEGNGPRYCPSIEDKVVRFADKERHQIFLEPEGLNSDEIYLNGLSTSLPEDVQLKI 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286 321 VHSLPGLEHAEFLKYAYAIEYDAIDPLQLWPSLETKVIKNLYTAGQINGTSGYEEAAGQGLIAGINAAKKVDGIAPLILK 400
Cdd:TIGR00136 319 IRSIPGLENAEILRPGYAIEYDYFDPTQLKPTLETKLIKGLFFAGQINGTTGYEEAAAQGLMAGINAALKLQNKEPFILK 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286 401 RNEAYIGVLIDDLVTKGTKEPYRMLTSRAEYRLLLRHDNADERLMKYGYEAGLVKEETYQEYLTKMDHIDQEITRLSTLR 480
Cdd:TIGR00136 399 RNEAYIGVLIDDLVTKGTKEPYRMFTSRAEYRLLLREDNADFRLTEIGRELGLIDEDRYARFLKKKQNIEEEIERLKSTR 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286 481 FTPKSEINERIEELGSTKLKEGISAKVLLQRPELTYDK-IKDYLGNVDLTDEERLRVTINIKYKGYIDKALRQVEKVKAM 559
Cdd:TIGR00136 479 LSPSKEVKEELKNLAQSPLKDEVSGYDLLKRPEMNLDKlTKLLPFLPPLDEEVLEQVEIEIKYEGYIKKQQQYIKKLDRL 558

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1514766286 560 EEKHIPEDIDYDQVINLALEAKQKLKEVRPLTVGQASRISGINPADISVLLIYLK 614
Cdd:TIGR00136 559 ENVKIPADFDYRKIPGLSTEAREKLSKFRPLSLGQASRISGINPADISALLVYLK 613
GIDA pfam01134
Glucose inhibited division protein A;
3-394 0e+00

Glucose inhibited division protein A;


Pssm-ID: 250388 [Multi-domain]  Cd Length: 391  Bit Score: 616.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286   3 DVIVVGAGHAGIEACLAPARIGKKTLLVTSHFANAGQMPCNTAIGGPAKGIIVREVDALGGQMGKSADANYTQMKMLNTA 82
Cdd:pfam01134   1 DVIVIGGGHAGCEAALAAARMGAKVLLITHNTDTIAELSCNPSIGGIAKGHLVREIDALGGLMGKAADKTGIQFRMLNTS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286  83 KGPGVWALRAQEDKKTYPRYMQKVLKEQENLDIIEAMVEDLIVEENTCKGVILEDGQRIEGKTVILTTGTYLKAEILVGD 162
Cdd:pfam01134  81 KGPAVRALRAQVDRDLYSKEMTETLENHPNLTLIQGEVTDLIPENGKVKGVVTEDGEEYKAKAVVLATGTFLNGKIHIGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286 163 QKTPSGPDQERYSKFLSDKLRDYGFRIQRLKTGTPPRIKAESIDFSKTSVQPGTDAKLSFSYSTKTFTPlaEQDVCYLTY 242
Cdd:pfam01134 161 KCYPAGRLGELTSEGLSESLKELGFELGRFKTGTPPRIDKDSIDFSKLEEQPGDKPGPPFSYLNCPMNK--EQYPCFLTY 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286 243 TTAKTHQLIRDNLSKSSMYSGIVKGVGPRYCPSIEDKVVKFADKERHQLFLEPESRETNSIYLQGFSTSMPHDIQEQMVH 322
Cdd:pfam01134 239 TNEATHEIIRDNLHRSPMFEGCIEGIGPRYCPSIEDKPVRFADKPYHQVFLEPEGLDTDEYYLVGFSTSLPEDVQKRVLR 318

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1514766286 323 SLPGLEHAEFLKYAYAIEYDAIDPLQLWPSLETKVIKNLYTAGQINGTSGYEEAAGQGLIAGINAAKKVDGI 394
Cdd:pfam01134 319 TIPGLENAEIVRPGYAIEYDYIDPPQLLPTLETKKIPGLFFAGQINGTEGYEEAAAQGLLAGINAARKALGK 390
PRK05335 PRK05335
tRNA (uracil-5-)-methyltransferase Gid; Reviewed
 307-410 3.36e-15

tRNA (uracil-5-)-methyltransferase Gid; Reviewed


Pssm-ID: 235416  Cd Length: 436  Bit Score: 78.26  E-value: 3.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286 307 GFSTSMPHDIQEQMVHSLPGLEHAEFLKYA------YaieydaID-PLQLWPSLETKVIKNLYTAGQINGTSGYEEAAGQ 379
Cdd:PRK05335  278 GFQTKLKWGEQKRVFRMIPGLENAEFVRYGvmhrntF------INsPKLLDPTLQLKKRPNLFFAGQITGVEGYVESAAS 351

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1514766286 380 GLIAGINAAKKVDGIAPLILKRNEAyIGVLI 410
Cdd:PRK05335  352 GLLAGINAARLALGKEPVIPPPTTA-LGALL 381
 
Name Accession Description Interval E-value
MnmG COG0445
tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal ...
 2-614 0e+00

tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440214 [Multi-domain]  Cd Length: 626  Bit Score: 1096.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286   2 YDVIVVGAGHAGIEACLAPARIGKKTLLVTSHFANAGQMPCNTAIGGPAKGIIVREVDALGGQMGKSADANYTQMKMLNT 81
Cdd:COG0445     7 YDVIVVGGGHAGCEAALAAARMGAKTLLLTHNLDTIGQMSCNPAIGGIAKGHLVREIDALGGEMGRAADKTGIQFRMLNT 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286  82 AKGPGVWALRAQEDKKTYPRYMQKVLKEQENLDIIEAMVEDLIVEENTCKGVILEDGQRIEGKTVILTTGTYLKAEILVG 161
Cdd:COG0445    87 SKGPAVRAPRAQADRKLYRAAMRETLENQPNLDLIQGEVEDLIVEDGRVTGVVTADGIEFRAKAVVLTTGTFLNGLIHIG 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286 162 DQKTPSGPDQERYSKFLSDKLRDYGFRIQRLKTGTPPRIKAESIDFSKTSVQPGTDAKLSFSYSTKTFTPlaEQDVCYLT 241
Cdd:COG0445   167 EKSYPGGRAGEPPSVGLSESLRELGFELGRLKTGTPPRIDGRSIDFSKLEEQPGDEPPPPFSFLTEKIHP--PQIPCWIT 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286 242 YTTAKTHQLIRDNLSKSSMYSGIVKGVGPRYCPSIEDKVVKFADKERHQLFLEPESRETNSIYLQGFSTSMPHDIQEQMV 321
Cdd:COG0445   245 YTNEETHEIIRENLHRSPMYSGVIEGVGPRYCPSIEDKIVRFADKDRHQIFLEPEGLDTNEVYPNGISTSLPEDVQLAML 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286 322 HSLPGLEHAEFLKYAYAIEYDAIDPLQLWPSLETKVIKNLYTAGQINGTSGYEEAAGQGLIAGINAAKKVDGIAPLILKR 401
Cdd:COG0445   325 RSIPGLENAEILRPGYAIEYDYVDPTQLKPTLETKKIEGLFFAGQINGTTGYEEAAAQGLMAGINAALKAQGKEPFILDR 404

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286 402 NEAYIGVLIDDLVTKGTKEPYRMLTSRAEYRLLLRHDNADERLMKYGYEAGLVKEETYQEYLTKMDHIDQEITRLSTLRF 481
Cdd:COG0445   405 SEAYIGVLIDDLVTKGTDEPYRMFTSRAEYRLLLRQDNADLRLTEKGYELGLVSDERYERFEEKKEAIEEEIERLKSTRV 484

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286 482 TPKSEINERIEELGSTKLKEGISAKVLLQRPELTYDKIKDYLGNV-DLTDEERLRVTINIKYKGYIDKALRQVEKVKAME 560
Cdd:COG0445   485 TPNEEVNEGLEELGSSPLKRGVSLFDLLRRPEITYEDLAELDPELpDLDPEVAEQVEIEIKYEGYIERQEEEIEKLKRLE 564

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1514766286 561 EKHIPEDIDYDQVINLALEAKQKLKEVRPLTVGQASRISGINPADISVLLIYLK 614
Cdd:COG0445   565 NLKIPEDFDYDAIPGLSNEAREKLKKIRPETLGQASRISGVTPADISLLLVYLK 618
gidA TIGR00136
glucose-inhibited division protein A; GidA, the longer of two forms of GidA-related proteins, ...
 2-614 0e+00

glucose-inhibited division protein A; GidA, the longer of two forms of GidA-related proteins, appears to be present in all complete eubacterial genomes so far, as well as Saccharomyces cerevisiae. A subset of these organisms have a closely related protein. GidA is absent in the Archaea. It appears to act with MnmE, in an alpha2/beta2 heterotetramer, in the 5-carboxymethylaminomethyl modification of uridine 34 in certain tRNAs. The shorter, related protein, previously called gid or gidA(S), is now called TrmFO (see model TIGR00137). [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 272927 [Multi-domain]  Cd Length: 616  Bit Score: 911.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286   2 YDVIVVGAGHAGIEACLAPARIGKKTLLVTSHFANAGQMPCNTAIGGPAKGIIVREVDALGGQMGKSADANYTQMKMLNT 81
Cdd:TIGR00136   1 FDVIVIGGGHAGCEAALAAARLGAKTLLLTLNLDTIGKCSCNPAIGGPAKGILVKEIDALGGEMGKAADKTGLQFRVLNS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286  82 AKGPGVWALRAQEDKKTYPRYMQKVLKEQENLDIIEAMVEDLIVEENT-CKGVILEDGQRIEGKTVILTTGTYLKAEILV 160
Cdd:TIGR00136  81 SKGPAVRATRAQIDKILYQKWMRNQLENQPNLSLFQGEVEDLILEDNDeIKGVVTKDGNEFRAKAVIITTGTFLRGKIHI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286 161 GDQKTPSGPDQERYSKFLSDKLRDYGFRIQRLKTGTPPRIKAESIDFSKTSVQPGTDAKLSFSYSTKTFTPlaEQDVCYL 240
Cdd:TIGR00136 161 GDKSYEAGRAGEQASYGLSTTLRELGFKTGRLKTGTPPRIDKRSIDFSKLEVQFGDTQPPAFSFTNKNFLP--QQLPCYL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286 241 TYTTAKTHQLIRDNLSKSSMYSGIVKGVGPRYCPSIEDKVVKFADKERHQLFLEPESRETNSIYLQGFSTSMPHDIQEQM 320
Cdd:TIGR00136 239 THTNPKTHQIIRDNLHRSPMYSGSIEGNGPRYCPSIEDKVVRFADKERHQIFLEPEGLNSDEIYLNGLSTSLPEDVQLKI 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286 321 VHSLPGLEHAEFLKYAYAIEYDAIDPLQLWPSLETKVIKNLYTAGQINGTSGYEEAAGQGLIAGINAAKKVDGIAPLILK 400
Cdd:TIGR00136 319 IRSIPGLENAEILRPGYAIEYDYFDPTQLKPTLETKLIKGLFFAGQINGTTGYEEAAAQGLMAGINAALKLQNKEPFILK 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286 401 RNEAYIGVLIDDLVTKGTKEPYRMLTSRAEYRLLLRHDNADERLMKYGYEAGLVKEETYQEYLTKMDHIDQEITRLSTLR 480
Cdd:TIGR00136 399 RNEAYIGVLIDDLVTKGTKEPYRMFTSRAEYRLLLREDNADFRLTEIGRELGLIDEDRYARFLKKKQNIEEEIERLKSTR 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286 481 FTPKSEINERIEELGSTKLKEGISAKVLLQRPELTYDK-IKDYLGNVDLTDEERLRVTINIKYKGYIDKALRQVEKVKAM 559
Cdd:TIGR00136 479 LSPSKEVKEELKNLAQSPLKDEVSGYDLLKRPEMNLDKlTKLLPFLPPLDEEVLEQVEIEIKYEGYIKKQQQYIKKLDRL 558

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1514766286 560 EEKHIPEDIDYDQVINLALEAKQKLKEVRPLTVGQASRISGINPADISVLLIYLK 614
Cdd:TIGR00136 559 ENVKIPADFDYRKIPGLSTEAREKLSKFRPLSLGQASRISGINPADISALLVYLK 613
GIDA pfam01134
Glucose inhibited division protein A;
3-394 0e+00

Glucose inhibited division protein A;


Pssm-ID: 250388 [Multi-domain]  Cd Length: 391  Bit Score: 616.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286   3 DVIVVGAGHAGIEACLAPARIGKKTLLVTSHFANAGQMPCNTAIGGPAKGIIVREVDALGGQMGKSADANYTQMKMLNTA 82
Cdd:pfam01134   1 DVIVIGGGHAGCEAALAAARMGAKVLLITHNTDTIAELSCNPSIGGIAKGHLVREIDALGGLMGKAADKTGIQFRMLNTS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286  83 KGPGVWALRAQEDKKTYPRYMQKVLKEQENLDIIEAMVEDLIVEENTCKGVILEDGQRIEGKTVILTTGTYLKAEILVGD 162
Cdd:pfam01134  81 KGPAVRALRAQVDRDLYSKEMTETLENHPNLTLIQGEVTDLIPENGKVKGVVTEDGEEYKAKAVVLATGTFLNGKIHIGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286 163 QKTPSGPDQERYSKFLSDKLRDYGFRIQRLKTGTPPRIKAESIDFSKTSVQPGTDAKLSFSYSTKTFTPlaEQDVCYLTY 242
Cdd:pfam01134 161 KCYPAGRLGELTSEGLSESLKELGFELGRFKTGTPPRIDKDSIDFSKLEEQPGDKPGPPFSYLNCPMNK--EQYPCFLTY 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286 243 TTAKTHQLIRDNLSKSSMYSGIVKGVGPRYCPSIEDKVVKFADKERHQLFLEPESRETNSIYLQGFSTSMPHDIQEQMVH 322
Cdd:pfam01134 239 TNEATHEIIRDNLHRSPMFEGCIEGIGPRYCPSIEDKPVRFADKPYHQVFLEPEGLDTDEYYLVGFSTSLPEDVQKRVLR 318

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1514766286 323 SLPGLEHAEFLKYAYAIEYDAIDPLQLWPSLETKVIKNLYTAGQINGTSGYEEAAGQGLIAGINAAKKVDGI 394
Cdd:pfam01134 319 TIPGLENAEIVRPGYAIEYDYIDPPQLLPTLETKKIPGLFFAGQINGTEGYEEAAAQGLLAGINAARKALGK 390
GIDA_C pfam13932
tRNA modifying enzyme MnmG/GidA C-terminal domain; The GidA associated domain is a domain that ...
 397-610 1.35e-115

tRNA modifying enzyme MnmG/GidA C-terminal domain; The GidA associated domain is a domain that has been identified at the C-terminus of protein GidA. It consists of several helices, the last three being rather short and forming small bundle. GidA is an tRNA modification enzyme found in bacteria and mitochondrial. Based on mutational analysis this domain has been suggested to be implicated in binding of the D-stem of tRNA and to be responsible for the interaction with protein MnmE. Structures of GidA in complex with either tRNA or MnmE are missing. Reported to bind to Pfam family MnmE, pfam12631.


Pssm-ID: 464049 [Multi-domain]  Cd Length: 214  Bit Score: 343.21  E-value: 1.35e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286 397 LILKRNEAYIGVLIDDLVTKGTKEPYRMLTSRAEYRLLLRHDNADERLMKYGYEAGLVKEETYQEYLTKMDHIDQEITRL 476
Cdd:pfam13932   1 LILSRSEAYIGVLIDDLVTKGTSEPYRMFTSRAEYRLLLRQDNADLRLTEKGRELGLVSDERYERFEEKKEAIEEEIERL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286 477 STLRFTPkSEINERIEELGSTKLKEGISAKVLLQRPELTYDKIKDYL-GNVDLTDEERLRVTINIKYKGYIDKALRQVEK 555
Cdd:pfam13932  81 KSTRLSP-SEWNNALLELGSAPLGTGRSAFDLLRRPEVTYEDLAALIpELAPLDPEVLEQVEIEAKYEGYIERQEAEIEK 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1514766286 556 VKAMEEKHIPEDIDYDQVINLALEAKQKLKEVRPLTVGQASRISGINPADISVLL 610
Cdd:pfam13932 160 FKRLENLKIPEDLDYDAIPGLSNEAREKLNKIRPETIGQASRISGVTPADISVLL 214
TrmFO COG1206
Folate-dependent tRNA-U54 methylase TrmFO/GidA [Translation, ribosomal structure and ...
 307-419 3.65e-16

Folate-dependent tRNA-U54 methylase TrmFO/GidA [Translation, ribosomal structure and biogenesis]; Folate-dependent tRNA-U54 methylase TrmFO/GidA is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440819  Cd Length: 436  Bit Score: 81.26  E-value: 3.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286 307 GFSTSMPHDIQEQMVHSLPGLEHAEFLKYA------YaieydaID-PLQLWPSLETKVIKNLYTAGQINGTSGYEEAAGQ 379
Cdd:COG1206   278 GFQTKLKWGEQKRVFRMIPGLENAEFVRYGvmhrntF------INsPKLLDPTLQLKARPNLFFAGQITGVEGYVESAAS 351

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1514766286 380 GLIAGINAAKKVDGIAPLILKRNEAyIGVLIDDLVTKGTK 419
Cdd:COG1206   352 GLLAGINAARLLLGKEPVPPPPTTA-LGALLNYITGADPK 390
PRK05335 PRK05335
tRNA (uracil-5-)-methyltransferase Gid; Reviewed
 307-410 3.36e-15

tRNA (uracil-5-)-methyltransferase Gid; Reviewed


Pssm-ID: 235416  Cd Length: 436  Bit Score: 78.26  E-value: 3.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286 307 GFSTSMPHDIQEQMVHSLPGLEHAEFLKYA------YaieydaID-PLQLWPSLETKVIKNLYTAGQINGTSGYEEAAGQ 379
Cdd:PRK05335  278 GFQTKLKWGEQKRVFRMIPGLENAEFVRYGvmhrntF------INsPKLLDPTLQLKKRPNLFFAGQITGVEGYVESAAS 351

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1514766286 380 GLIAGINAAKKVDGIAPLILKRNEAyIGVLI 410
Cdd:PRK05335  352 GLLAGINAARLALGKEPVIPPPTTA-LGALL 381
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
2-151 7.73e-09

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 57.44  E-value: 7.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286   2 YDVIVVGAGHAGIEACLAPARIGKKTLLVTShfanagqmpcntaiggpakgiivrevDALGGQMGKSAD-ANYtqmkmln 80
Cdd:COG0492     1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEG--------------------------GEPGGQLATTKEiENY------- 47

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1514766286  81 takgPGV-WALRAQEdkktyprYMQKVLK--EQENLDIIEAMVEDLIVEENTcKGVILEDGQRIEGKTVILTTG 151
Cdd:COG0492    48 ----PGFpEGISGPE-------LAERLREqaERFGAEILLEEVTSVDKDDGP-FRVTTDDGTEYEAKAVIIATG 109
FAD_oxidored pfam12831
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ...
 3-151 6.13e-08

FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.


Pssm-ID: 432816 [Multi-domain]  Cd Length: 420  Bit Score: 55.31  E-value: 6.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286   3 DVIVVGAGHAGIEACLAPARIGKKTLLV--TSHFanAGQMpcnT-AIGGPAKGIIVREVDALGGqmgkSADANYTQMKml 79
Cdd:pfam12831   1 DVVVVGGGPAGVAAAIAAARAGAKVLLVerRGFL--GGML---TsGLVGPDMGFYLNKEQVVGG----IAREFRQRLR-- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286  80 ntAKGPGVWALRAQEDKKTY-PRYMQKVLKE---QENLDII-EAMVEDLIVEENTCKGVILED---GQRIEGKTVILTTG 151
Cdd:pfam12831  70 --ARGGLPGPYGLRGGWVPFdPEVAKAVLDEmlaEAGVTVLlHTRVVGVVKEGGRITGVTVETkggRITIRAKVFIDATG 147
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
 3-153 7.18e-05

FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.


Pssm-ID: 395718 [Multi-domain]  Cd Length: 398  Bit Score: 45.36  E-value: 7.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286   3 DVIVVGAGHAGIEACLAPARIGKKTLLV--------TSHFANAGqmpCNTAIGGPAKGIIVRE------VDALGGQmgks 68
Cdd:pfam00890   1 DVLVIGGGLAGLAAALAAAEAGLKVAVVekgqpfggATAWSSGG---IDALGNPPQGGIDSPElhptdtLKGLDEL---- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286  69 ADANYTQMkMLNTAK----------------GPGVWALR-----------------AQEDKKTYPRyMQKVLKEQ---EN 112
Cdd:pfam00890  74 ADHPYVEA-FVEAAPeavdwlealgvpfsrtEDGHLDLRplgglsatwrtphdaadRRRGLGTGHA-LLARLLEGlrkAG 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1514766286 113 LDI-IEAMVEDLIVEENTCKGVILEDGQ-----RIEGKT-VILTTGTY 153
Cdd:pfam00890 152 VDFqPRTAADDLIVEDGRVTGAVVENRRngrevRIRAIAaVLLATGGF 199
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
 1-151 1.34e-04

Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440673 [Multi-domain]  Cd Length: 443  Bit Score: 44.82  E-value: 1.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286   1 MYDVIVVGAGHAGIEACLAPARIGKKTLLVT------SHFA------NAGQMPCNTAIGG--PAKGI--IVREVDALGGQ 64
Cdd:COG1053     3 EYDVVVVGSGGAGLRAALEAAEAGLKVLVLEkvpprgGHTAaaqggiNAAGTNVQKAAGEdsPEEHFydTVKGGDGLADQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286  65 -----MGKSADANYTQMKmlntAKG----PGVWALRAQEDKKTYPR----------YMQKVLKEQ---ENLDII-EAMVE 121
Cdd:COG1053    83 dlveaLAEEAPEAIDWLE----AQGvpfsRTPDGRLPQFGGHSVGRtcyagdgtghALLATLYQAalrLGVEIFtETEVL 158

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1514766286 122 DLIVEENTCKGVILEDG----QRIEGKTVILTTG 151
Cdd:COG1053   159 DLIVDDGRVVGVVARDRtgeiVRIRAKAVVLATG 192
PRK05329 PRK05329
glycerol-3-phosphate dehydrogenase subunit GlpB;
1-35 4.82e-04

glycerol-3-phosphate dehydrogenase subunit GlpB;


Pssm-ID: 235412  Cd Length: 422  Bit Score: 42.92  E-value: 4.82e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1514766286   1 MYDVIVVGAGHAGIEACLAPARIGKKTLLVTS-----HFA 35
Cdd:PRK05329    2 KFDVLVIGGGLAGLTAALAAAEAGKRVALVAKgqgalHFS 41
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 2-151 7.92e-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: 41.92  E-value: 7.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286   2 YDVIVVGAGHAGIEACLAPARIGKKTLLVTS--HFANAGQMPCNTAIGGPAKGiivrevdalggqmgksadanytqmkml 79
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDegTCPYGGCVLSKALLGAAEAP--------------------------- 53

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1514766286  80 NTAKGPGVWALRAQEDKKTYPRYMQKVLKEQ-ENLDIIEAMVedliveenTCKGVILEDGQRIEGKTVILTTG 151
Cdd:pfam07992  54 EIASLWADLYKRKEEVVKKLNNGIEVLLGTEvVSIDPGAKKV--------VLEELVDGDGETITYDRLVIATG 118
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 1-152 8.84e-04

Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation


Pssm-ID: 440861 [Multi-domain]  Cd Length: 456  Bit Score: 42.00  E-value: 8.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286   1 MYDVIVVGAGHAGIEACLAPARIGKKTLLVTSHfanagqmpcntAIGG--------PAKGIIvrevdalggqmgKSADAn 72
Cdd:COG1249     3 DYDLVVIGAGPGGYVAAIRAAQLGLKVALVEKG-----------RLGGtclnvgciPSKALL------------HAAEV- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1514766286  73 ytqMKMLNTAKGPGVwalRAQEDKKTYPRYMQKVLKEQENL-DIIEAMVEDL----------IVEENTckgVILEDGQRI 141
Cdd:COG1249    59 ---AHEARHAAEFGI---SAGAPSVDWAALMARKDKVVDRLrGGVEELLKKNgvdvirgrarFVDPHT---VEVTGGETL 129

                         170
                  ....*....|.
gi 1514766286 142 EGKTVILTTGT 152
Cdd:COG1249   130 TADHIVIATGS 140
 
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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