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Conserved domains on  [gi|1051014064|gb|AOA03436|]
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tRNA uridine(34) 5-carboxymethylaminomethyl synthesis enzyme MnmG [Carnobacterium maltaromaticum]

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 ...
 4-631 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: 1195.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064   4 FEAGTFDVIVVGAGHAGSEAALASARMGQKTLLLTINLDMVAFMPCNPSVGGPAKGVVVREIDALGGEMGRNIDKTYIQM 83
Cdd:COG0445     2 YYPKEYDVIVVGGGHAGCEAALAAARMGAKTLLLTHNLDTIGQMSCNPAIGGIAKGHLVREIDALGGEMGRAADKTGIQF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064  84 RMLNTGKGPAVRALRAQADKFLYANEMKHTIEREDNIILRQGIAEDLIIEDGVCLGIVTNTGAVYRSKSVILTAGTSSRG 163
Cdd:COG0445    82 RMLNTSKGPAVRAPRAQADRKLYRAAMRETLENQPNLDLIQGEVEDLIVEDGRVTGVVTADGIEFRAKAVVLTTGTFLNG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064 164 QIIIGELKYSSGPNNSQPSIKLSESLLRNGFELARFKTGTPPRVKASTIDYSVTEEQPGDEKANHFSYETPDSayVKDQL 243
Cdd:COG0445   162 LIHIGEKSYPGGRAGEPPSVGLSESLRELGFELGRLKTGTPPRIDGRSIDFSKLEEQPGDEPPPPFSFLTEKI--HPPQI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064 244 SCWLTYSNEKTHDIIKANLHRAPMFTGIVEGVGARYCPSIEDKIVRFSDKPRHQMFLEPEGRNTEEVYVQGLSTSMPEDV 323
Cdd:COG0445   240 PCWITYTNEETHEIIRENLHRSPMYSGVIEGVGPRYCPSIEDKIVRFADKDRHQIFLEPEGLDTNEVYPNGISTSLPEDV 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064 324 QLDMIRSVAGLEKAEMMRTGYAIEYDVVVPYQLRPSLETKIVENLFTAGQMNGTSGYEEAASQGLMAGINAALKNQGKEP 403
Cdd:COG0445   320 QLAMLRSIPGLENAEILRPGYAIEYDYVDPTQLKPTLETKKIEGLFFAGQINGTTGYEEAAAQGLMAGINAALKAQGKEP 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064 404 FVMKRSEGYIGVMVDDLVTKGTMEPYRLLTSRAEYRLLLRHDNADFRLTEIGHEIGLVSDERYETFLAKKALVEDEIKRL 483
Cdd:COG0445   400 FILDRSEAYIGVLIDDLVTKGTDEPYRMFTSRAEYRLLLRQDNADLRLTEKGYELGLVSDERYERFEEKKEAIEEEIERL 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064 484 MKTRLKPTAELQAFLvDVKGASPLKDGILAADFLRRPEMTYEEVVSFAPATIELPLAVKEQVEIQIKYEGYIQKAIEKVE 563
Cdd:COG0445   480 KSTRVTPNEEVNEGL-EELGSSPLKRGVSLFDLLRRPEITYEDLAELDPELPDLDPEVAEQVEIEIKYEGYIERQEEEIE 558

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1051014064 564 KMKRMESKRIPERIDYEAINGLATEARQKLVKIQPETIAQASRISGVNPADISILMVYVEQGKIAKVA 631
Cdd:COG0445   559 KLKRLENLKIPEDFDYDAIPGLSNEAREKLKKIRPETLGQASRISGVTPADISLLLVYLKRRRRRKKA 626
 
Name Accession Description Interval E-value
MnmG COG0445
tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal ...
 4-631 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: 1195.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064   4 FEAGTFDVIVVGAGHAGSEAALASARMGQKTLLLTINLDMVAFMPCNPSVGGPAKGVVVREIDALGGEMGRNIDKTYIQM 83
Cdd:COG0445     2 YYPKEYDVIVVGGGHAGCEAALAAARMGAKTLLLTHNLDTIGQMSCNPAIGGIAKGHLVREIDALGGEMGRAADKTGIQF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064  84 RMLNTGKGPAVRALRAQADKFLYANEMKHTIEREDNIILRQGIAEDLIIEDGVCLGIVTNTGAVYRSKSVILTAGTSSRG 163
Cdd:COG0445    82 RMLNTSKGPAVRAPRAQADRKLYRAAMRETLENQPNLDLIQGEVEDLIVEDGRVTGVVTADGIEFRAKAVVLTTGTFLNG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064 164 QIIIGELKYSSGPNNSQPSIKLSESLLRNGFELARFKTGTPPRVKASTIDYSVTEEQPGDEKANHFSYETPDSayVKDQL 243
Cdd:COG0445   162 LIHIGEKSYPGGRAGEPPSVGLSESLRELGFELGRLKTGTPPRIDGRSIDFSKLEEQPGDEPPPPFSFLTEKI--HPPQI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064 244 SCWLTYSNEKTHDIIKANLHRAPMFTGIVEGVGARYCPSIEDKIVRFSDKPRHQMFLEPEGRNTEEVYVQGLSTSMPEDV 323
Cdd:COG0445   240 PCWITYTNEETHEIIRENLHRSPMYSGVIEGVGPRYCPSIEDKIVRFADKDRHQIFLEPEGLDTNEVYPNGISTSLPEDV 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064 324 QLDMIRSVAGLEKAEMMRTGYAIEYDVVVPYQLRPSLETKIVENLFTAGQMNGTSGYEEAASQGLMAGINAALKNQGKEP 403
Cdd:COG0445   320 QLAMLRSIPGLENAEILRPGYAIEYDYVDPTQLKPTLETKKIEGLFFAGQINGTTGYEEAAAQGLMAGINAALKAQGKEP 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064 404 FVMKRSEGYIGVMVDDLVTKGTMEPYRLLTSRAEYRLLLRHDNADFRLTEIGHEIGLVSDERYETFLAKKALVEDEIKRL 483
Cdd:COG0445   400 FILDRSEAYIGVLIDDLVTKGTDEPYRMFTSRAEYRLLLRQDNADLRLTEKGYELGLVSDERYERFEEKKEAIEEEIERL 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064 484 MKTRLKPTAELQAFLvDVKGASPLKDGILAADFLRRPEMTYEEVVSFAPATIELPLAVKEQVEIQIKYEGYIQKAIEKVE 563
Cdd:COG0445   480 KSTRVTPNEEVNEGL-EELGSSPLKRGVSLFDLLRRPEITYEDLAELDPELPDLDPEVAEQVEIEIKYEGYIERQEEEIE 558

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1051014064 564 KMKRMESKRIPERIDYEAINGLATEARQKLVKIQPETIAQASRISGVNPADISILMVYVEQGKIAKVA 631
Cdd:COG0445   559 KLKRLENLKIPEDFDYDAIPGLSNEAREKLKKIRPETLGQASRISGVTPADISLLLVYLKRRRRRKKA 626
gidA TIGR00136
glucose-inhibited division protein A; GidA, the longer of two forms of GidA-related proteins, ...
 9-626 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: 998.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064   9 FDVIVVGAGHAGSEAALASARMGQKTLLLTINLDMVAFMPCNPSVGGPAKGVVVREIDALGGEMGRNIDKTYIQMRMLNT 88
Cdd:TIGR00136   1 FDVIVIGGGHAGCEAALAAARLGAKTLLLTLNLDTIGKCSCNPAIGGPAKGILVKEIDALGGEMGKAADKTGLQFRVLNS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064  89 GKGPAVRALRAQADKFLYANEMKHTIEREDNIILRQGIAEDLIIED-GVCLGIVTNTGAVYRSKSVILTAGTSSRGQIII 167
Cdd:TIGR00136  81 SKGPAVRATRAQIDKILYQKWMRNQLENQPNLSLFQGEVEDLILEDnDEIKGVVTKDGNEFRAKAVIITTGTFLRGKIHI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064 168 GELKYSSGPNNSQPSIKLSESLLRNGFELARFKTGTPPRVKASTIDYSVTEEQPGDEKANHFSYETpdSAYVKDQLSCWL 247
Cdd:TIGR00136 161 GDKSYEAGRAGEQASYGLSTTLRELGFKTGRLKTGTPPRIDKRSIDFSKLEVQFGDTQPPAFSFTN--KNFLPQQLPCYL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064 248 TYSNEKTHDIIKANLHRAPMFTGIVEGVGARYCPSIEDKIVRFSDKPRHQMFLEPEGRNTEEVYVQGLSTSMPEDVQLDM 327
Cdd:TIGR00136 239 THTNPKTHQIIRDNLHRSPMYSGSIEGNGPRYCPSIEDKVVRFADKERHQIFLEPEGLNSDEIYLNGLSTSLPEDVQLKI 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064 328 IRSVAGLEKAEMMRTGYAIEYDVVVPYQLRPSLETKIVENLFTAGQMNGTSGYEEAASQGLMAGINAALKNQGKEPFVMK 407
Cdd:TIGR00136 319 IRSIPGLENAEILRPGYAIEYDYFDPTQLKPTLETKLIKGLFFAGQINGTTGYEEAAAQGLMAGINAALKLQNKEPFILK 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064 408 RSEGYIGVMVDDLVTKGTMEPYRLLTSRAEYRLLLRHDNADFRLTEIGHEIGLVSDERYETFLAKKALVEDEIKRLMKTR 487
Cdd:TIGR00136 399 RNEAYIGVLIDDLVTKGTKEPYRMFTSRAEYRLLLREDNADFRLTEIGRELGLIDEDRYARFLKKKQNIEEEIERLKSTR 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064 488 LKPTAELQAFLVDVKGaSPLKDGILAADFLRRPEMTYEEVVSFAPATIELPLAVKEQVEIQIKYEGYIQKAIEKVEKMKR 567
Cdd:TIGR00136 479 LSPSKEVKEELKNLAQ-SPLKDEVSGYDLLKRPEMNLDKLTKLLPFLPPLDEEVLEQVEIEIKYEGYIKKQQQYIKKLDR 557

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1051014064 568 MESKRIPERIDYEAINGLATEARQKLVKIQPETIAQASRISGVNPADISILMVYVEQGK 626
Cdd:TIGR00136 558 LENVKIPADFDYRKIPGLSTEAREKLSKFRPLSLGQASRISGINPADISALLVYLKKQK 616
GIDA pfam01134
Glucose inhibited division protein A;
10-402 0e+00

Glucose inhibited division protein A;


Pssm-ID: 250388 [Multi-domain]  Cd Length: 391  Bit Score: 654.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064  10 DVIVVGAGHAGSEAALASARMGQKTLLLTINLDMVAFMPCNPSVGGPAKGVVVREIDALGGEMGRNIDKTYIQMRMLNTG 89
Cdd:pfam01134   1 DVIVIGGGHAGCEAALAAARMGAKVLLITHNTDTIAELSCNPSIGGIAKGHLVREIDALGGLMGKAADKTGIQFRMLNTS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064  90 KGPAVRALRAQADKFLYANEMKHTIEREDNIILRQGIAEDLIIEDGVCLGIVTNTGAVYRSKSVILTAGTSSRGQIIIGE 169
Cdd:pfam01134  81 KGPAVRALRAQVDRDLYSKEMTETLENHPNLTLIQGEVTDLIPENGKVKGVVTEDGEEYKAKAVVLATGTFLNGKIHIGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064 170 LKYSSGPNNSQPSIKLSESLLRNGFELARFKTGTPPRVKASTIDYSVTEEQPGDEKANHFSYETPDsaYVKDQLSCWLTY 249
Cdd:pfam01134 161 KCYPAGRLGELTSEGLSESLKELGFELGRFKTGTPPRIDKDSIDFSKLEEQPGDKPGPPFSYLNCP--MNKEQYPCFLTY 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064 250 SNEKTHDIIKANLHRAPMFTGIVEGVGARYCPSIEDKIVRFSDKPRHQMFLEPEGRNTEEVYVQGLSTSMPEDVQLDMIR 329
Cdd:pfam01134 239 TNEATHEIIRDNLHRSPMFEGCIEGIGPRYCPSIEDKPVRFADKPYHQVFLEPEGLDTDEYYLVGFSTSLPEDVQKRVLR 318

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1051014064 330 SVAGLEKAEMMRTGYAIEYDVVVPYQLRPSLETKIVENLFTAGQMNGTSGYEEAASQGLMAGINAALKNQGKE 402
Cdd:pfam01134 319 TIPGLENAEIVRPGYAIEYDYIDPPQLLPTLETKKIPGLFFAGQINGTEGYEEAAAQGLLAGINAARKALGKE 391
PRK05335 PRK05335
tRNA (uracil-5-)-methyltransferase Gid; Reviewed
 324-405 3.71e-12

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


Pssm-ID: 235416  Cd Length: 436  Bit Score: 68.63  E-value: 3.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064 324 QLDMIRSVAGLEKAEMMRTGyaieydvVV--------PYQLRPSLETKIVENLFTAGQMNGTSGYEEAASQGLMAGINAA 395
Cdd:PRK05335  288 QKRVFRMIPGLENAEFVRYG-------VMhrntfinsPKLLDPTLQLKKRPNLFFAGQITGVEGYVESAASGLLAGINAA 360

                          90
                  ....*....|
gi 1051014064 396 LKNQGKEPFV 405
Cdd:PRK05335  361 RLALGKEPVI 370
 
Name Accession Description Interval E-value
MnmG COG0445
tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal ...
 4-631 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: 1195.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064   4 FEAGTFDVIVVGAGHAGSEAALASARMGQKTLLLTINLDMVAFMPCNPSVGGPAKGVVVREIDALGGEMGRNIDKTYIQM 83
Cdd:COG0445     2 YYPKEYDVIVVGGGHAGCEAALAAARMGAKTLLLTHNLDTIGQMSCNPAIGGIAKGHLVREIDALGGEMGRAADKTGIQF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064  84 RMLNTGKGPAVRALRAQADKFLYANEMKHTIEREDNIILRQGIAEDLIIEDGVCLGIVTNTGAVYRSKSVILTAGTSSRG 163
Cdd:COG0445    82 RMLNTSKGPAVRAPRAQADRKLYRAAMRETLENQPNLDLIQGEVEDLIVEDGRVTGVVTADGIEFRAKAVVLTTGTFLNG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064 164 QIIIGELKYSSGPNNSQPSIKLSESLLRNGFELARFKTGTPPRVKASTIDYSVTEEQPGDEKANHFSYETPDSayVKDQL 243
Cdd:COG0445   162 LIHIGEKSYPGGRAGEPPSVGLSESLRELGFELGRLKTGTPPRIDGRSIDFSKLEEQPGDEPPPPFSFLTEKI--HPPQI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064 244 SCWLTYSNEKTHDIIKANLHRAPMFTGIVEGVGARYCPSIEDKIVRFSDKPRHQMFLEPEGRNTEEVYVQGLSTSMPEDV 323
Cdd:COG0445   240 PCWITYTNEETHEIIRENLHRSPMYSGVIEGVGPRYCPSIEDKIVRFADKDRHQIFLEPEGLDTNEVYPNGISTSLPEDV 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064 324 QLDMIRSVAGLEKAEMMRTGYAIEYDVVVPYQLRPSLETKIVENLFTAGQMNGTSGYEEAASQGLMAGINAALKNQGKEP 403
Cdd:COG0445   320 QLAMLRSIPGLENAEILRPGYAIEYDYVDPTQLKPTLETKKIEGLFFAGQINGTTGYEEAAAQGLMAGINAALKAQGKEP 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064 404 FVMKRSEGYIGVMVDDLVTKGTMEPYRLLTSRAEYRLLLRHDNADFRLTEIGHEIGLVSDERYETFLAKKALVEDEIKRL 483
Cdd:COG0445   400 FILDRSEAYIGVLIDDLVTKGTDEPYRMFTSRAEYRLLLRQDNADLRLTEKGYELGLVSDERYERFEEKKEAIEEEIERL 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064 484 MKTRLKPTAELQAFLvDVKGASPLKDGILAADFLRRPEMTYEEVVSFAPATIELPLAVKEQVEIQIKYEGYIQKAIEKVE 563
Cdd:COG0445   480 KSTRVTPNEEVNEGL-EELGSSPLKRGVSLFDLLRRPEITYEDLAELDPELPDLDPEVAEQVEIEIKYEGYIERQEEEIE 558

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1051014064 564 KMKRMESKRIPERIDYEAINGLATEARQKLVKIQPETIAQASRISGVNPADISILMVYVEQGKIAKVA 631
Cdd:COG0445   559 KLKRLENLKIPEDFDYDAIPGLSNEAREKLKKIRPETLGQASRISGVTPADISLLLVYLKRRRRRKKA 626
gidA TIGR00136
glucose-inhibited division protein A; GidA, the longer of two forms of GidA-related proteins, ...
 9-626 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: 998.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064   9 FDVIVVGAGHAGSEAALASARMGQKTLLLTINLDMVAFMPCNPSVGGPAKGVVVREIDALGGEMGRNIDKTYIQMRMLNT 88
Cdd:TIGR00136   1 FDVIVIGGGHAGCEAALAAARLGAKTLLLTLNLDTIGKCSCNPAIGGPAKGILVKEIDALGGEMGKAADKTGLQFRVLNS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064  89 GKGPAVRALRAQADKFLYANEMKHTIEREDNIILRQGIAEDLIIED-GVCLGIVTNTGAVYRSKSVILTAGTSSRGQIII 167
Cdd:TIGR00136  81 SKGPAVRATRAQIDKILYQKWMRNQLENQPNLSLFQGEVEDLILEDnDEIKGVVTKDGNEFRAKAVIITTGTFLRGKIHI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064 168 GELKYSSGPNNSQPSIKLSESLLRNGFELARFKTGTPPRVKASTIDYSVTEEQPGDEKANHFSYETpdSAYVKDQLSCWL 247
Cdd:TIGR00136 161 GDKSYEAGRAGEQASYGLSTTLRELGFKTGRLKTGTPPRIDKRSIDFSKLEVQFGDTQPPAFSFTN--KNFLPQQLPCYL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064 248 TYSNEKTHDIIKANLHRAPMFTGIVEGVGARYCPSIEDKIVRFSDKPRHQMFLEPEGRNTEEVYVQGLSTSMPEDVQLDM 327
Cdd:TIGR00136 239 THTNPKTHQIIRDNLHRSPMYSGSIEGNGPRYCPSIEDKVVRFADKERHQIFLEPEGLNSDEIYLNGLSTSLPEDVQLKI 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064 328 IRSVAGLEKAEMMRTGYAIEYDVVVPYQLRPSLETKIVENLFTAGQMNGTSGYEEAASQGLMAGINAALKNQGKEPFVMK 407
Cdd:TIGR00136 319 IRSIPGLENAEILRPGYAIEYDYFDPTQLKPTLETKLIKGLFFAGQINGTTGYEEAAAQGLMAGINAALKLQNKEPFILK 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064 408 RSEGYIGVMVDDLVTKGTMEPYRLLTSRAEYRLLLRHDNADFRLTEIGHEIGLVSDERYETFLAKKALVEDEIKRLMKTR 487
Cdd:TIGR00136 399 RNEAYIGVLIDDLVTKGTKEPYRMFTSRAEYRLLLREDNADFRLTEIGRELGLIDEDRYARFLKKKQNIEEEIERLKSTR 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064 488 LKPTAELQAFLVDVKGaSPLKDGILAADFLRRPEMTYEEVVSFAPATIELPLAVKEQVEIQIKYEGYIQKAIEKVEKMKR 567
Cdd:TIGR00136 479 LSPSKEVKEELKNLAQ-SPLKDEVSGYDLLKRPEMNLDKLTKLLPFLPPLDEEVLEQVEIEIKYEGYIKKQQQYIKKLDR 557

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1051014064 568 MESKRIPERIDYEAINGLATEARQKLVKIQPETIAQASRISGVNPADISILMVYVEQGK 626
Cdd:TIGR00136 558 LENVKIPADFDYRKIPGLSTEAREKLSKFRPLSLGQASRISGINPADISALLVYLKKQK 616
GIDA pfam01134
Glucose inhibited division protein A;
10-402 0e+00

Glucose inhibited division protein A;


Pssm-ID: 250388 [Multi-domain]  Cd Length: 391  Bit Score: 654.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064  10 DVIVVGAGHAGSEAALASARMGQKTLLLTINLDMVAFMPCNPSVGGPAKGVVVREIDALGGEMGRNIDKTYIQMRMLNTG 89
Cdd:pfam01134   1 DVIVIGGGHAGCEAALAAARMGAKVLLITHNTDTIAELSCNPSIGGIAKGHLVREIDALGGLMGKAADKTGIQFRMLNTS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064  90 KGPAVRALRAQADKFLYANEMKHTIEREDNIILRQGIAEDLIIEDGVCLGIVTNTGAVYRSKSVILTAGTSSRGQIIIGE 169
Cdd:pfam01134  81 KGPAVRALRAQVDRDLYSKEMTETLENHPNLTLIQGEVTDLIPENGKVKGVVTEDGEEYKAKAVVLATGTFLNGKIHIGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064 170 LKYSSGPNNSQPSIKLSESLLRNGFELARFKTGTPPRVKASTIDYSVTEEQPGDEKANHFSYETPDsaYVKDQLSCWLTY 249
Cdd:pfam01134 161 KCYPAGRLGELTSEGLSESLKELGFELGRFKTGTPPRIDKDSIDFSKLEEQPGDKPGPPFSYLNCP--MNKEQYPCFLTY 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064 250 SNEKTHDIIKANLHRAPMFTGIVEGVGARYCPSIEDKIVRFSDKPRHQMFLEPEGRNTEEVYVQGLSTSMPEDVQLDMIR 329
Cdd:pfam01134 239 TNEATHEIIRDNLHRSPMFEGCIEGIGPRYCPSIEDKPVRFADKPYHQVFLEPEGLDTDEYYLVGFSTSLPEDVQKRVLR 318

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1051014064 330 SVAGLEKAEMMRTGYAIEYDVVVPYQLRPSLETKIVENLFTAGQMNGTSGYEEAASQGLMAGINAALKNQGKE 402
Cdd:pfam01134 319 TIPGLENAEIVRPGYAIEYDYIDPPQLLPTLETKKIPGLFFAGQINGTEGYEEAAAQGLLAGINAARKALGKE 391
GIDA_C pfam13932
tRNA modifying enzyme MnmG/GidA C-terminal domain; The GidA associated domain is a domain that ...
 404-619 7.92e-125

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: 367.48  E-value: 7.92e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064 404 FVMKRSEGYIGVMVDDLVTKGTMEPYRLLTSRAEYRLLLRHDNADFRLTEIGHEIGLVSDERYETFLAKKALVEDEIKRL 483
Cdd:pfam13932   1 LILSRSEAYIGVLIDDLVTKGTSEPYRMFTSRAEYRLLLRQDNADLRLTEKGRELGLVSDERYERFEEKKEAIEEEIERL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064 484 MKTRLKPTAELQAFLvdVKGASPLKDGILAADFLRRPEMTYEEVVSFAPATIELPLAVKEQVEIQIKYEGYIQKAIEKVE 563
Cdd:pfam13932  81 KSTRLSPSEWNNALL--ELGSAPLGTGRSAFDLLRRPEVTYEDLAALIPELAPLDPEVLEQVEIEAKYEGYIERQEAEIE 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1051014064 564 KMKRMESKRIPERIDYEAINGLATEARQKLVKIQPETIAQASRISGVNPADISILM 619
Cdd:pfam13932 159 KFKRLENLKIPEDLDYDAIPGLSNEAREKLNKIRPETIGQASRISGVTPADISVLL 214
PRK05335 PRK05335
tRNA (uracil-5-)-methyltransferase Gid; Reviewed
 324-405 3.71e-12

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


Pssm-ID: 235416  Cd Length: 436  Bit Score: 68.63  E-value: 3.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064 324 QLDMIRSVAGLEKAEMMRTGyaieydvVV--------PYQLRPSLETKIVENLFTAGQMNGTSGYEEAASQGLMAGINAA 395
Cdd:PRK05335  288 QKRVFRMIPGLENAEFVRYG-------VMhrntfinsPKLLDPTLQLKKRPNLFFAGQITGVEGYVESAASGLLAGINAA 360

                          90
                  ....*....|
gi 1051014064 396 LKNQGKEPFV 405
Cdd:PRK05335  361 RLALGKEPVI 370
TrmFO COG1206
Folate-dependent tRNA-U54 methylase TrmFO/GidA [Translation, ribosomal structure and ...
 324-405 9.76e-12

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: 67.39  E-value: 9.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064 324 QLDMIRSVAGLEKAEMMRTGyaieydvVV--------PYQLRPSLETKIVENLFTAGQMNGTSGYEEAASQGLMAGINAA 395
Cdd:COG1206   288 QKRVFRMIPGLENAEFVRYG-------VMhrntfinsPKLLDPTLQLKARPNLFFAGQITGVEGYVESAASGLLAGINAA 360

                          90
                  ....*....|
gi 1051014064 396 LKNQGKEPFV 405
Cdd:COG1206   361 RLLLGKEPVP 370
FAD_oxidored pfam12831
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ...
 10-37 7.58e-06

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


Pssm-ID: 432816 [Multi-domain]  Cd Length: 420  Bit Score: 48.76  E-value: 7.58e-06
                          10        20
                  ....*....|....*....|....*...
gi 1051014064  10 DVIVVGAGHAGSEAALASARMGQKTLLL 37
Cdd:pfam12831   1 DVVVVGGGPAGVAAAIAAARAGAKVLLV 28
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
 8-158 1.69e-05

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: 47.52  E-value: 1.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064   8 TFDVIVVGAGHAGSEAALASARMGQKTLLLT---------------INL-------------------DMVAFM--PCNP 51
Cdd:COG1053     3 EYDVVVVGSGGAGLRAALEAAEAGLKVLVLEkvpprgghtaaaqggINAagtnvqkaagedspeehfyDTVKGGdgLADQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064  52 SV------GGPAkgvVVREIDALGGEMGRNIDKTYIQM------RMLNTGK--GPA-VRALRAQAdkflyanemkhtier 116
Cdd:COG1053    83 DLvealaeEAPE---AIDWLEAQGVPFSRTPDGRLPQFgghsvgRTCYAGDgtGHAlLATLYQAA--------------- 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1051014064 117 edniiLRQGI-------AEDLIIEDGVCLGIV--TNTGA--VYRSKSVILTAG 158
Cdd:COG1053   145 -----LRLGVeifteteVLDLIVDDGRVVGVVarDRTGEivRIRAKAVVLATG 192
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
9-162 3.47e-05

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 46.27  E-value: 3.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064   9 FDVIVVGAGHAGSEAALASARMGQKTLLLtinldmvafmpcnpsvggpakgvvvrEIDALGGEMGrNIDKTY-------- 80
Cdd:COG0492     1 YDVVIIGAGPAGLTAAIYAARAGLKTLVI--------------------------EGGEPGGQLA-TTKEIEnypgfpeg 53

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064  81 IQmrmlntgkGPA-VRALRAQADKF--LYANEMKHTIEREDNIILrqgiaedliiedgvclgIVTNTGAVYRSKSVILTA 157
Cdd:COG0492    54 IS--------GPElAERLREQAERFgaEILLEEVTSVDKDDGPFR-----------------VTTDDGTEYEAKAVIIAT 108


                  ....*
gi 1051014064 158 GTSSR 162
Cdd:COG0492   109 GAGPR 113
GG-red-SF TIGR02032
geranylgeranyl reductase family; This model represents a subfamily which includes ...
 9-162 2.84e-04

geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 273936 [Multi-domain]  Cd Length: 295  Bit Score: 43.08  E-value: 2.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064   9 FDVIVVGAGHAGSEAALASARMGQKTLLLTINlDMVAFMPCnpsvGGPAKGVVVREIDALGGEMGRNIDKTYIQM---RM 85
Cdd:TIGR02032   1 YDVVVVGAGPAGASAAYRLADKGLRVLLLEKK-SFPRYKPC----GGALSPRALEELDLPGELIVNLVRGARFFSpngDS 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064  86 LN----TGKGPAVRalRAQADKFLYANEMKHTIE-REDNIILrqgiaeDLIIEDGVCLGIVTNTGAVYRSKSVILTAGTS 160
Cdd:TIGR02032  76 VEipieTELAYVID--RDAFDEQLAERAQEAGAElRLGTRVL------DVEIHDDRVVVIVRGSEGTVTAKIVIGADGSR 147


                  ..
gi 1051014064 161 SR 162
Cdd:TIGR02032 148 SI 149
PRK07843 PRK07843
3-oxosteroid 1-dehydrogenase;
5-37 1.24e-03

3-oxosteroid 1-dehydrogenase;


Pssm-ID: 236111 [Multi-domain]  Cd Length: 557  Bit Score: 41.94  E-value: 1.24e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1051014064   5 EAGTFDVIVVGAGHAGSEAALASARMGQKTLLL 37
Cdd:PRK07843    4 TVQEYDVVVVGSGAAGMVAALTAAHRGLSTVVV 36
soxA_mon TIGR01377
sarcosine oxidase, monomeric form; Sarcosine oxidase catalyzes the oxidative demethylation of ...
 9-37 2.09e-03

sarcosine oxidase, monomeric form; Sarcosine oxidase catalyzes the oxidative demethylation of sarcosine to glycine. The reaction converts tetrahydrofolate to 5,10-methylene-tetrahydrofolate. The enzyme is known in monomeric and heterotetrameric (alpha,beta,gamma,delta) forms [Energy metabolism, Amino acids and amines]


Pssm-ID: 130444 [Multi-domain]  Cd Length: 380  Bit Score: 40.97  E-value: 2.09e-03
                          10        20
                  ....*....|....*....|....*....
gi 1051014064   9 FDVIVVGAGHAGSEAALASARMGQKTLLL 37
Cdd:TIGR01377   1 FDVIVVGAGIMGCFAAYHLAKHGKKTLLL 29
PRK12843 PRK12843
FAD-dependent oxidoreductase;
5-37 2.45e-03

FAD-dependent oxidoreductase;


Pssm-ID: 237225 [Multi-domain]  Cd Length: 578  Bit Score: 40.88  E-value: 2.45e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1051014064   5 EAGTFDVIVVGAGHAGSEAALASARMGQKTLLL 37
Cdd:PRK12843   13 WDAEFDVIVIGAGAAGMSAALFAAIAGLKVLLV 45
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 8-36 3.33e-03

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: 40.46  E-value: 3.33e-03
                          10        20
                  ....*....|....*....|....*....
gi 1051014064   8 TFDVIVVGAGHAGSEAALASARMGQKTLL 36
Cdd:COG1249     3 DYDLVVIGAGPGGYVAAIRAAQLGLKVAL 31
PRK05329 PRK05329
glycerol-3-phosphate dehydrogenase subunit GlpB;
9-38 3.65e-03

glycerol-3-phosphate dehydrogenase subunit GlpB;


Pssm-ID: 235412  Cd Length: 422  Bit Score: 40.22  E-value: 3.65e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1051014064   9 FDVIVVGAGHAGSEAALASARMGQKTLLLT 38
Cdd:PRK05329    3 FDVLVIGGGLAGLTAALAAAEAGKRVALVA 32
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
 10-162 6.52e-03

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: 39.19  E-value: 6.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064  10 DVIVVGAGHAGSEAALASARMGQKTLLLT------INLDM---VAFMPCNPSVGGPAKGVVVREiDALGG---------- 70
Cdd:pfam00890   1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEkgqpfgGATAWssgGIDALGNPPQGGIDSPELHPT-DTLKGldeladhpyv 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051014064  71 EMG-RNIDKTYIQ-----MRMLNTGKGP-AVRALRAQADKFLYANEM----------KHTIEREDNIILRQGI------- 126
Cdd:pfam00890  80 EAFvEAAPEAVDWlealgVPFSRTEDGHlDLRPLGGLSATWRTPHDAadrrrglgtgHALLARLLEGLRKAGVdfqprta 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1051014064 127 AEDLIIEDGVCLGIV---TNTGAVYRSKS---VILTAGTSSR 162
Cdd:pfam00890 160 ADDLIVEDGRVTGAVvenRRNGREVRIRAiaaVLLATGGFGR 201
 
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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