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Conserved domains on  [gi|1277971089|gb|PIV64808|]
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tRNA uridine-5-carboxymethylaminomethyl(34) synthesis enzyme MnmG, partial [bacterium (Candidatus Ratteibacteria) CG01_land_8_20_14_3_00_40_19]

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 ...
 1-578 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: 1114.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089   1 PQKYDVIVVGAGHAGCEAALATAKMGLRTLLLTINLDTIAQMSCNPAIGGCAKGQLVKEIDALGGEMGKNIDKTGIQFRM 80
Cdd:COG0445     4 PKEYDVIVVGGGHAGCEAALAAARMGAKTLLLTHNLDTIGQMSCNPAIGGIAKGHLVREIDALGGEMGRAADKTGIQFRM 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089  81 LNTKKGPAVWGPRAQADKKSYQFGLKHTLEKEENLDLKQELVEEILVKEKKVIGVITHHQTLYYGKAIILTTGTFLKGLI 160
Cdd:COG0445    84 LNTSKGPAVRAPRAQADRKLYRAAMRETLENQPNLDLIQGEVEDLIVEDGRVTGVVTADGIEFRAKAVVLTTGTFLNGLI 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089 161 HIGELKIAAGRAGEFPAEKLSDNLKKLGFAIGRLKTGTPPRINRNSIDFSKTEIQNGDKKPTPFSFSTERIRQPQIPCYI 240
Cdd:COG0445   164 HIGEKSYPGGRAGEPPSVGLSESLRELGFELGRLKTGTPPRIDGRSIDFSKLEEQPGDEPPPPFSFLTEKIHPPQIPCWI 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089 241 TYTNEKCHKIIRKNLKRAPLYTGQIKGIGPRYCPSIEVKIVNFPQKERHQIFLEPEGINTEEIYLNGFATSIPVDVQLEA 320
Cdd:COG0445   244 TYTNEETHEIIRENLHRSPMYSGVIEGVGPRYCPSIEDKIVRFADKDRHQIFLEPEGLDTNEVYPNGISTSLPEDVQLAM 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089 321 LSAITGLQNVKMMRPGYAIEYDFIFPHQIKATLETKLIENLYLAGQINGTSGYEEAGAQGIMAGINATLKIKGKSPFILD 400
Cdd:COG0445   324 LRSIPGLENAEILRPGYAIEYDYVDPTQLKPTLETKKIEGLFFAGQINGTTGYEEAAAQGLMAGINAALKAQGKEPFILD 403

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089 401 RASAYIGVLIDDLITKDISEPYRMFTSRAEYRLLLRQDNADLRLMEYGYKFGLINEEQFEKLQEKRRKITEELDKLKHKK 480
Cdd:COG0445   404 RSEAYIGVLIDDLVTKGTDEPYRMFTSRAEYRLLLRQDNADLRLTEKGYELGLVSDERYERFEEKKEAIEEEIERLKSTR 483

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089 481 -------NYIINKN----------------------------------LNEDTRRQVEIQLKYEGYIKRELQSIKRFKKA 519
Cdd:COG0445   484 vtpneevNEGLEELgssplkrgvslfdllrrpeityedlaeldpelpdLDPEVAEQVEIEIKYEGYIERQEEEIEKLKRL 563

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1277971089 520 EKKRIPPNFDYSTLYGLSTEAREKLTRIKPFSFGQASRIDGLRQSDLSILLIHLEKSRK 578
Cdd:COG0445   564 ENLKIPEDFDYDAIPGLSNEAREKLKKIRPETLGQASRISGVTPADISLLLVYLKRRRR 622
 
Name Accession Description Interval E-value
MnmG COG0445
tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal ...
 1-578 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: 1114.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089   1 PQKYDVIVVGAGHAGCEAALATAKMGLRTLLLTINLDTIAQMSCNPAIGGCAKGQLVKEIDALGGEMGKNIDKTGIQFRM 80
Cdd:COG0445     4 PKEYDVIVVGGGHAGCEAALAAARMGAKTLLLTHNLDTIGQMSCNPAIGGIAKGHLVREIDALGGEMGRAADKTGIQFRM 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089  81 LNTKKGPAVWGPRAQADKKSYQFGLKHTLEKEENLDLKQELVEEILVKEKKVIGVITHHQTLYYGKAIILTTGTFLKGLI 160
Cdd:COG0445    84 LNTSKGPAVRAPRAQADRKLYRAAMRETLENQPNLDLIQGEVEDLIVEDGRVTGVVTADGIEFRAKAVVLTTGTFLNGLI 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089 161 HIGELKIAAGRAGEFPAEKLSDNLKKLGFAIGRLKTGTPPRINRNSIDFSKTEIQNGDKKPTPFSFSTERIRQPQIPCYI 240
Cdd:COG0445   164 HIGEKSYPGGRAGEPPSVGLSESLRELGFELGRLKTGTPPRIDGRSIDFSKLEEQPGDEPPPPFSFLTEKIHPPQIPCWI 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089 241 TYTNEKCHKIIRKNLKRAPLYTGQIKGIGPRYCPSIEVKIVNFPQKERHQIFLEPEGINTEEIYLNGFATSIPVDVQLEA 320
Cdd:COG0445   244 TYTNEETHEIIRENLHRSPMYSGVIEGVGPRYCPSIEDKIVRFADKDRHQIFLEPEGLDTNEVYPNGISTSLPEDVQLAM 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089 321 LSAITGLQNVKMMRPGYAIEYDFIFPHQIKATLETKLIENLYLAGQINGTSGYEEAGAQGIMAGINATLKIKGKSPFILD 400
Cdd:COG0445   324 LRSIPGLENAEILRPGYAIEYDYVDPTQLKPTLETKKIEGLFFAGQINGTTGYEEAAAQGLMAGINAALKAQGKEPFILD 403

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089 401 RASAYIGVLIDDLITKDISEPYRMFTSRAEYRLLLRQDNADLRLMEYGYKFGLINEEQFEKLQEKRRKITEELDKLKHKK 480
Cdd:COG0445   404 RSEAYIGVLIDDLVTKGTDEPYRMFTSRAEYRLLLRQDNADLRLTEKGYELGLVSDERYERFEEKKEAIEEEIERLKSTR 483

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089 481 -------NYIINKN----------------------------------LNEDTRRQVEIQLKYEGYIKRELQSIKRFKKA 519
Cdd:COG0445   484 vtpneevNEGLEELgssplkrgvslfdllrrpeityedlaeldpelpdLDPEVAEQVEIEIKYEGYIERQEEEIEKLKRL 563

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1277971089 520 EKKRIPPNFDYSTLYGLSTEAREKLTRIKPFSFGQASRIDGLRQSDLSILLIHLEKSRK 578
Cdd:COG0445   564 ENLKIPEDFDYDAIPGLSNEAREKLKKIRPETLGQASRISGVTPADISLLLVYLKRRRR 622
gidA TIGR00136
glucose-inhibited division protein A; GidA, the longer of two forms of GidA-related proteins, ...
 4-575 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: 874.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089   4 YDVIVVGAGHAGCEAALATAKMGLRTLLLTINLDTIAQMSCNPAIGGCAKGQLVKEIDALGGEMGKNIDKTGIQFRMLNT 83
Cdd:TIGR00136   1 FDVIVIGGGHAGCEAALAAARLGAKTLLLTLNLDTIGKCSCNPAIGGPAKGILVKEIDALGGEMGKAADKTGLQFRVLNS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089  84 KKGPAVWGPRAQADKKSYQFGLKHTLEKEENLDLKQELVEEILVKE-KKVIGVITHHQTLYYGKAIILTTGTFLKGLIHI 162
Cdd:TIGR00136  81 SKGPAVRATRAQIDKILYQKWMRNQLENQPNLSLFQGEVEDLILEDnDEIKGVVTKDGNEFRAKAVIITTGTFLRGKIHI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089 163 GELKIAAGRAGEFPAEKLSDNLKKLGFAIGRLKTGTPPRINRNSIDFSKTEIQNGDKKPTPFSFSTERIRQPQIPCYITY 242
Cdd:TIGR00136 161 GDKSYEAGRAGEQASYGLSTTLRELGFKTGRLKTGTPPRIDKRSIDFSKLEVQFGDTQPPAFSFTNKNFLPQQLPCYLTH 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089 243 TNEKCHKIIRKNLKRAPLYTGQIKGIGPRYCPSIEVKIVNFPQKERHQIFLEPEGINTEEIYLNGFATSIPVDVQLEALS 322
Cdd:TIGR00136 241 TNPKTHQIIRDNLHRSPMYSGSIEGNGPRYCPSIEDKVVRFADKERHQIFLEPEGLNSDEIYLNGLSTSLPEDVQLKIIR 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089 323 AITGLQNVKMMRPGYAIEYDFIFPHQIKATLETKLIENLYLAGQINGTSGYEEAGAQGIMAGINATLKIKGKSPFILDRA 402
Cdd:TIGR00136 321 SIPGLENAEILRPGYAIEYDYFDPTQLKPTLETKLIKGLFFAGQINGTTGYEEAAAQGLMAGINAALKLQNKEPFILKRN 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089 403 SAYIGVLIDDLITKDISEPYRMFTSRAEYRLLLRQDNADLRLMEYGYKFGLINEEQFEKLQEKRRKITEELDKLKHK--- 479
Cdd:TIGR00136 401 EAYIGVLIDDLVTKGTKEPYRMFTSRAEYRLLLREDNADFRLTEIGRELGLIDEDRYARFLKKKQNIEEEIERLKSTrls 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089 480 ---------KNYIINK-----------------------------NLNEDTRRQVEIQLKYEGYIKRELQSIKRFKKAEK 521
Cdd:TIGR00136 481 pskevkeelKNLAQSPlkdevsgydllkrpemnldkltkllpflpPLDEEVLEQVEIEIKYEGYIKKQQQYIKKLDRLEN 560

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1277971089 522 KRIPPNFDYSTLYGLSTEAREKLTRIKPFSFGQASRIDGLRQSDLSILLIHLEK 575
Cdd:TIGR00136 561 VKIPADFDYRKIPGLSTEAREKLSKFRPLSLGQASRISGINPADISALLVYLKK 614
GIDA pfam01134
Glucose inhibited division protein A;
5-395 0e+00

Glucose inhibited division protein A;


Pssm-ID: 250388 [Multi-domain]  Cd Length: 391  Bit Score: 656.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089   5 DVIVVGAGHAGCEAALATAKMGLRTLLLTINLDTIAQMSCNPAIGGCAKGQLVKEIDALGGEMGKNIDKTGIQFRMLNTK 84
Cdd:pfam01134   1 DVIVIGGGHAGCEAALAAARMGAKVLLITHNTDTIAELSCNPSIGGIAKGHLVREIDALGGLMGKAADKTGIQFRMLNTS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089  85 KGPAVWGPRAQADKKSYQFGLKHTLEKEENLDLKQELVEEILVKEKKVIGVITHHQTLYYGKAIILTTGTFLKGLIHIGE 164
Cdd:pfam01134  81 KGPAVRALRAQVDRDLYSKEMTETLENHPNLTLIQGEVTDLIPENGKVKGVVTEDGEEYKAKAVVLATGTFLNGKIHIGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089 165 LKIAAGRAGEFPAEKLSDNLKKLGFAIGRLKTGTPPRINRNSIDFSKTEIQNGDKKPTPFSFSTERIRQPQIPCYITYTN 244
Cdd:pfam01134 161 KCYPAGRLGELTSEGLSESLKELGFELGRFKTGTPPRIDKDSIDFSKLEEQPGDKPGPPFSYLNCPMNKEQYPCFLTYTN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089 245 EKCHKIIRKNLKRAPLYTGQIKGIGPRYCPSIEVKIVNFPQKERHQIFLEPEGINTEEIYLNGFATSIPVDVQLEALSAI 324
Cdd:pfam01134 241 EATHEIIRDNLHRSPMFEGCIEGIGPRYCPSIEDKPVRFADKPYHQVFLEPEGLDTDEYYLVGFSTSLPEDVQKRVLRTI 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1277971089 325 TGLQNVKMMRPGYAIEYDFIFPHQIKATLETKLIENLYLAGQINGTSGYEEAGAQGIMAGINATLKIKGKS 395
Cdd:pfam01134 321 PGLENAEIVRPGYAIEYDYIDPPQLLPTLETKKIPGLFFAGQINGTEGYEEAAAQGLLAGINAARKALGKE 391
PRK05335 PRK05335
tRNA (uracil-5-)-methyltransferase Gid; Reviewed
 307-418 2.07e-13

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


Pssm-ID: 235416  Cd Length: 436  Bit Score: 72.49  E-value: 2.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089 307 GFATSIPVDVQLEALSAITGLQNVKMMRPGYAIEYDFI-FPHQIKATLETKLIENLYLAGQINGTSGYEEAGAQGIMAGI 385
Cdd:PRK05335  278 GFQTKLKWGEQKRVFRMIPGLENAEFVRYGVMHRNTFInSPKLLDPTLQLKKRPNLFFAGQITGVEGYVESAASGLLAGI 357

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1277971089 386 NATLKIKGKSPFILDRASAyIGVLIDDLITKDI 418
Cdd:PRK05335  358 NAARLALGKEPVIPPPTTA-LGALLNYITGANP 389
 
Name Accession Description Interval E-value
MnmG COG0445
tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal ...
 1-578 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: 1114.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089   1 PQKYDVIVVGAGHAGCEAALATAKMGLRTLLLTINLDTIAQMSCNPAIGGCAKGQLVKEIDALGGEMGKNIDKTGIQFRM 80
Cdd:COG0445     4 PKEYDVIVVGGGHAGCEAALAAARMGAKTLLLTHNLDTIGQMSCNPAIGGIAKGHLVREIDALGGEMGRAADKTGIQFRM 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089  81 LNTKKGPAVWGPRAQADKKSYQFGLKHTLEKEENLDLKQELVEEILVKEKKVIGVITHHQTLYYGKAIILTTGTFLKGLI 160
Cdd:COG0445    84 LNTSKGPAVRAPRAQADRKLYRAAMRETLENQPNLDLIQGEVEDLIVEDGRVTGVVTADGIEFRAKAVVLTTGTFLNGLI 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089 161 HIGELKIAAGRAGEFPAEKLSDNLKKLGFAIGRLKTGTPPRINRNSIDFSKTEIQNGDKKPTPFSFSTERIRQPQIPCYI 240
Cdd:COG0445   164 HIGEKSYPGGRAGEPPSVGLSESLRELGFELGRLKTGTPPRIDGRSIDFSKLEEQPGDEPPPPFSFLTEKIHPPQIPCWI 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089 241 TYTNEKCHKIIRKNLKRAPLYTGQIKGIGPRYCPSIEVKIVNFPQKERHQIFLEPEGINTEEIYLNGFATSIPVDVQLEA 320
Cdd:COG0445   244 TYTNEETHEIIRENLHRSPMYSGVIEGVGPRYCPSIEDKIVRFADKDRHQIFLEPEGLDTNEVYPNGISTSLPEDVQLAM 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089 321 LSAITGLQNVKMMRPGYAIEYDFIFPHQIKATLETKLIENLYLAGQINGTSGYEEAGAQGIMAGINATLKIKGKSPFILD 400
Cdd:COG0445   324 LRSIPGLENAEILRPGYAIEYDYVDPTQLKPTLETKKIEGLFFAGQINGTTGYEEAAAQGLMAGINAALKAQGKEPFILD 403

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089 401 RASAYIGVLIDDLITKDISEPYRMFTSRAEYRLLLRQDNADLRLMEYGYKFGLINEEQFEKLQEKRRKITEELDKLKHKK 480
Cdd:COG0445   404 RSEAYIGVLIDDLVTKGTDEPYRMFTSRAEYRLLLRQDNADLRLTEKGYELGLVSDERYERFEEKKEAIEEEIERLKSTR 483

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089 481 -------NYIINKN----------------------------------LNEDTRRQVEIQLKYEGYIKRELQSIKRFKKA 519
Cdd:COG0445   484 vtpneevNEGLEELgssplkrgvslfdllrrpeityedlaeldpelpdLDPEVAEQVEIEIKYEGYIERQEEEIEKLKRL 563

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1277971089 520 EKKRIPPNFDYSTLYGLSTEAREKLTRIKPFSFGQASRIDGLRQSDLSILLIHLEKSRK 578
Cdd:COG0445   564 ENLKIPEDFDYDAIPGLSNEAREKLKKIRPETLGQASRISGVTPADISLLLVYLKRRRR 622
gidA TIGR00136
glucose-inhibited division protein A; GidA, the longer of two forms of GidA-related proteins, ...
 4-575 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: 874.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089   4 YDVIVVGAGHAGCEAALATAKMGLRTLLLTINLDTIAQMSCNPAIGGCAKGQLVKEIDALGGEMGKNIDKTGIQFRMLNT 83
Cdd:TIGR00136   1 FDVIVIGGGHAGCEAALAAARLGAKTLLLTLNLDTIGKCSCNPAIGGPAKGILVKEIDALGGEMGKAADKTGLQFRVLNS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089  84 KKGPAVWGPRAQADKKSYQFGLKHTLEKEENLDLKQELVEEILVKE-KKVIGVITHHQTLYYGKAIILTTGTFLKGLIHI 162
Cdd:TIGR00136  81 SKGPAVRATRAQIDKILYQKWMRNQLENQPNLSLFQGEVEDLILEDnDEIKGVVTKDGNEFRAKAVIITTGTFLRGKIHI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089 163 GELKIAAGRAGEFPAEKLSDNLKKLGFAIGRLKTGTPPRINRNSIDFSKTEIQNGDKKPTPFSFSTERIRQPQIPCYITY 242
Cdd:TIGR00136 161 GDKSYEAGRAGEQASYGLSTTLRELGFKTGRLKTGTPPRIDKRSIDFSKLEVQFGDTQPPAFSFTNKNFLPQQLPCYLTH 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089 243 TNEKCHKIIRKNLKRAPLYTGQIKGIGPRYCPSIEVKIVNFPQKERHQIFLEPEGINTEEIYLNGFATSIPVDVQLEALS 322
Cdd:TIGR00136 241 TNPKTHQIIRDNLHRSPMYSGSIEGNGPRYCPSIEDKVVRFADKERHQIFLEPEGLNSDEIYLNGLSTSLPEDVQLKIIR 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089 323 AITGLQNVKMMRPGYAIEYDFIFPHQIKATLETKLIENLYLAGQINGTSGYEEAGAQGIMAGINATLKIKGKSPFILDRA 402
Cdd:TIGR00136 321 SIPGLENAEILRPGYAIEYDYFDPTQLKPTLETKLIKGLFFAGQINGTTGYEEAAAQGLMAGINAALKLQNKEPFILKRN 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089 403 SAYIGVLIDDLITKDISEPYRMFTSRAEYRLLLRQDNADLRLMEYGYKFGLINEEQFEKLQEKRRKITEELDKLKHK--- 479
Cdd:TIGR00136 401 EAYIGVLIDDLVTKGTKEPYRMFTSRAEYRLLLREDNADFRLTEIGRELGLIDEDRYARFLKKKQNIEEEIERLKSTrls 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089 480 ---------KNYIINK-----------------------------NLNEDTRRQVEIQLKYEGYIKRELQSIKRFKKAEK 521
Cdd:TIGR00136 481 pskevkeelKNLAQSPlkdevsgydllkrpemnldkltkllpflpPLDEEVLEQVEIEIKYEGYIKKQQQYIKKLDRLEN 560

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1277971089 522 KRIPPNFDYSTLYGLSTEAREKLTRIKPFSFGQASRIDGLRQSDLSILLIHLEK 575
Cdd:TIGR00136 561 VKIPADFDYRKIPGLSTEAREKLSKFRPLSLGQASRISGINPADISALLVYLKK 614
GIDA pfam01134
Glucose inhibited division protein A;
5-395 0e+00

Glucose inhibited division protein A;


Pssm-ID: 250388 [Multi-domain]  Cd Length: 391  Bit Score: 656.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089   5 DVIVVGAGHAGCEAALATAKMGLRTLLLTINLDTIAQMSCNPAIGGCAKGQLVKEIDALGGEMGKNIDKTGIQFRMLNTK 84
Cdd:pfam01134   1 DVIVIGGGHAGCEAALAAARMGAKVLLITHNTDTIAELSCNPSIGGIAKGHLVREIDALGGLMGKAADKTGIQFRMLNTS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089  85 KGPAVWGPRAQADKKSYQFGLKHTLEKEENLDLKQELVEEILVKEKKVIGVITHHQTLYYGKAIILTTGTFLKGLIHIGE 164
Cdd:pfam01134  81 KGPAVRALRAQVDRDLYSKEMTETLENHPNLTLIQGEVTDLIPENGKVKGVVTEDGEEYKAKAVVLATGTFLNGKIHIGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089 165 LKIAAGRAGEFPAEKLSDNLKKLGFAIGRLKTGTPPRINRNSIDFSKTEIQNGDKKPTPFSFSTERIRQPQIPCYITYTN 244
Cdd:pfam01134 161 KCYPAGRLGELTSEGLSESLKELGFELGRFKTGTPPRIDKDSIDFSKLEEQPGDKPGPPFSYLNCPMNKEQYPCFLTYTN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089 245 EKCHKIIRKNLKRAPLYTGQIKGIGPRYCPSIEVKIVNFPQKERHQIFLEPEGINTEEIYLNGFATSIPVDVQLEALSAI 324
Cdd:pfam01134 241 EATHEIIRDNLHRSPMFEGCIEGIGPRYCPSIEDKPVRFADKPYHQVFLEPEGLDTDEYYLVGFSTSLPEDVQKRVLRTI 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1277971089 325 TGLQNVKMMRPGYAIEYDFIFPHQIKATLETKLIENLYLAGQINGTSGYEEAGAQGIMAGINATLKIKGKS 395
Cdd:pfam01134 321 PGLENAEIVRPGYAIEYDYIDPPQLLPTLETKKIPGLFFAGQINGTEGYEEAAAQGLLAGINAARKALGKE 391
GIDA_C pfam13932
tRNA modifying enzyme MnmG/GidA C-terminal domain; The GidA associated domain is a domain that ...
 397-570 2.79e-92

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: 282.35  E-value: 2.79e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089 397 FILDRASAYIGVLIDDLITKDISEPYRMFTSRAEYRLLLRQDNADLRLMEYGYKFGLINEEQFEKLQEKRRKITEELDKL 476
Cdd:pfam13932   1 LILSRSEAYIGVLIDDLVTKGTSEPYRMFTSRAEYRLLLRQDNADLRLTEKGRELGLVSDERYERFEEKKEAIEEEIERL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089 477 KHKK-------NYIINKNLNEDTRR---------------------------------QVEIQLKYEGYIKRELQSIKRF 516
Cdd:pfam13932  81 KSTRlspsewnNALLELGSAPLGTGrsafdllrrpevtyedlaalipelapldpevleQVEIEAKYEGYIERQEAEIEKF 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1277971089 517 KKAEKKRIPPNFDYSTLYGLSTEAREKLTRIKPFSFGQASRIDGLRQSDLSILL 570
Cdd:pfam13932 161 KRLENLKIPEDLDYDAIPGLSNEAREKLNKIRPETIGQASRISGVTPADISVLL 214
PRK05335 PRK05335
tRNA (uracil-5-)-methyltransferase Gid; Reviewed
 307-418 2.07e-13

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


Pssm-ID: 235416  Cd Length: 436  Bit Score: 72.49  E-value: 2.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089 307 GFATSIPVDVQLEALSAITGLQNVKMMRPGYAIEYDFI-FPHQIKATLETKLIENLYLAGQINGTSGYEEAGAQGIMAGI 385
Cdd:PRK05335  278 GFQTKLKWGEQKRVFRMIPGLENAEFVRYGVMHRNTFInSPKLLDPTLQLKKRPNLFFAGQITGVEGYVESAASGLLAGI 357

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1277971089 386 NATLKIKGKSPFILDRASAyIGVLIDDLITKDI 418
Cdd:PRK05335  358 NAARLALGKEPVIPPPTTA-LGALLNYITGANP 389
TrmFO COG1206
Folate-dependent tRNA-U54 methylase TrmFO/GidA [Translation, ribosomal structure and ...
 346-410 1.98e-11

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: 66.24  E-value: 1.98e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1277971089 346 PHQIKATLETKLIENLYLAGQINGTSGYEEAGAQGIMAGINATLKIKGKSPFILDRASAyIGVLI 410
Cdd:COG1206   318 PKLLDPTLQLKARPNLFFAGQITGVEGYVESAASGLLAGINAARLLLGKEPVPPPPTTA-LGALL 381
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
4-153 2.17e-07

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 52.81  E-value: 2.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089   4 YDVIVVGAGHAGCEAALATAKMGLRTLLLTInldtiaqmscnPAIGgcakGQLV--KEIDALGGemgkniDKTGIQfrml 81
Cdd:COG0492     1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEG-----------GEPG----GQLAttKEIENYPG------FPEGIS---- 55

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1277971089  82 ntkkgpavwGP------RAQADKksyqFGLKHTLEKeenldlkqelVEEIlVKEKKVIGVITHHQTLYYGKAIILTTG 153
Cdd:COG0492    56 ---------GPelaerlREQAER----FGAEILLEE----------VTSV-DKDDGPFRVTTDDGTEYEAKAVIIATG 109
GG-red-SF TIGR02032
geranylgeranyl reductase family; This model represents a subfamily which includes ...
 4-32 2.72e-06

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: 49.24  E-value: 2.72e-06
                          10        20
                  ....*....|....*....|....*....
gi 1277971089   4 YDVIVVGAGHAGCEAALATAKMGLRTLLL 32
Cdd:TIGR02032   1 YDVVVVGAGPAGASAAYRLADKGLRVLLL 29
FAD_oxidored pfam12831
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ...
 5-153 3.62e-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: 49.53  E-value: 3.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277971089   5 DVIVVGAGHAGCEAALATAKMGLRTLLLtinldtiaqmSCNPAIGGCAKGQLVKEIDalGGEMGKNIDKTGI--QFRMLN 82
Cdd:pfam12831   1 DVVVVGGGPAGVAAAIAAARAGAKVLLV----------ERRGFLGGMLTSGLVGPDM--GFYLNKEQVVGGIarEFRQRL 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1277971089  83 TKKGPAVWGPRAQADKKSYQ-FGLKHTLE---KEENLD-LKQELVEEILVKEKKVIGVITH---HQTLYYGKAIILTTG 153
Cdd:pfam12831  69 RARGGLPGPYGLRGGWVPFDpEVAKAVLDemlAEAGVTvLLHTRVVGVVKEGGRITGVTVEtkgGRITIRAKVFIDATG 147
PRK07843 PRK07843
3-oxosteroid 1-dehydrogenase;
1-32 1.01e-05

3-oxosteroid 1-dehydrogenase;


Pssm-ID: 236111 [Multi-domain]  Cd Length: 557  Bit Score: 48.49  E-value: 1.01e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1277971089   1 PQKYDVIVVGAGHAGCEAALATAKMGLRTLLL 32
Cdd:PRK07843    5 VQEYDVVVVGSGAAGMVAALTAAHRGLSTVVV 36
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
 3-33 3.02e-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: 46.75  E-value: 3.02e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1277971089   3 KYDVIVVGAGHAGCEAALATAKMGLRTLLLT 33
Cdd:COG1053     3 EYDVVVVGSGGAGLRAALEAAEAGLKVLVLE 33
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 2-31 3.03e-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: 43.54  E-value: 3.03e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1277971089   2 QKYDVIVVGAGHAGCEAALATAKMGLRTLL 31
Cdd:COG1249     2 KDYDLVVIGAGPGGYVAAIRAAQLGLKVAL 31
PRK05329 PRK05329
glycerol-3-phosphate dehydrogenase subunit GlpB;
3-33 3.05e-04

glycerol-3-phosphate dehydrogenase subunit GlpB;


Pssm-ID: 235412  Cd Length: 422  Bit Score: 43.30  E-value: 3.05e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1277971089   3 KYDVIVVGAGHAGCEAALATAKMGLRTLLLT 33
Cdd:PRK05329    2 KFDVLVIGGGLAGLTAALAAAEAGKRVALVA 32
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
 5-33 3.87e-04

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: 43.05  E-value: 3.87e-04
                          10        20
                  ....*....|....*....|....*....
gi 1277971089   5 DVIVVGAGHAGCEAALATAKMGLRTLLLT 33
Cdd:pfam00890   1 DVLVIGGGLAGLAAALAAAEAGLKVAVVE 29
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 2-32 6.52e-04

Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 42.53  E-value: 6.52e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1277971089   2 QKYDVIVVGAGHAGCEAALATAKMGLRTLLL 32
Cdd:COG1233     2 MMYDVVVIGAGIGGLAAAALLARAGYRVTVL 32
PRK12844 PRK12844
3-ketosteroid-delta-1-dehydrogenase; Reviewed
 4-32 1.52e-03

3-ketosteroid-delta-1-dehydrogenase; Reviewed


Pssm-ID: 183787 [Multi-domain]  Cd Length: 557  Bit Score: 41.28  E-value: 1.52e-03
                          10        20
                  ....*....|....*....|....*....
gi 1277971089   4 YDVIVVGAGHAGCEAALATAKMGLRTLLL 32
Cdd:PRK12844    7 YDVVVVGSGGGGMCAALAAADSGLEPLIV 35
soxA_mon TIGR01377
sarcosine oxidase, monomeric form; Sarcosine oxidase catalyzes the oxidative demethylation of ...
 4-32 1.78e-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: 1.78e-03
                          10        20
                  ....*....|....*....|....*....
gi 1277971089   4 YDVIVVGAGHAGCEAALATAKMGLRTLLL 32
Cdd:TIGR01377   1 FDVIVVGAGIMGCFAAYHLAKHGKKTLLL 29
sdhA PRK07803
succinate dehydrogenase flavoprotein subunit; Reviewed
 2-52 2.33e-03

succinate dehydrogenase flavoprotein subunit; Reviewed


Pssm-ID: 236101 [Multi-domain]  Cd Length: 626  Bit Score: 40.79  E-value: 2.33e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1277971089   2 QKYDVIVVGAGHAGCEAALATAKMGLRTLLLTINLDTIAQ--MscnpAIGGCA 52
Cdd:PRK07803    7 HSYDVVVIGAGGAGLRAAIEARERGLRVAVVCKSLFGKAHtvM----AEGGCA 55
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 4-35 2.48e-03

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: 40.38  E-value: 2.48e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1277971089   4 YDVIVVGAGHAGCEAALATAKMGLRTLLLTIN 35
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDE 32
PRK07608 PRK07608
UbiH/UbiF family hydroxylase;
1-32 2.62e-03

UbiH/UbiF family hydroxylase;


Pssm-ID: 181057 [Multi-domain]  Cd Length: 388  Bit Score: 40.32  E-value: 2.62e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1277971089   1 PQKYDVIVVGAGHAGCEAALATAKMGLRTLLL 32
Cdd:PRK07608    3 HMKFDVVVVGGGLVGASLALALAQSGLRVALL 34
PRK12843 PRK12843
FAD-dependent oxidoreductase;
4-32 3.47e-03

FAD-dependent oxidoreductase;


Pssm-ID: 237225 [Multi-domain]  Cd Length: 578  Bit Score: 40.10  E-value: 3.47e-03
                          10        20
                  ....*....|....*....|....*....
gi 1277971089   4 YDVIVVGAGHAGCEAALATAKMGLRTLLL 32
Cdd:PRK12843   17 FDVIVIGAGAAGMSAALFAAIAGLKVLLV 45
PRK10015 PRK10015
oxidoreductase; Provisional
 2-32 4.48e-03

oxidoreductase; Provisional


Pssm-ID: 182194 [Multi-domain]  Cd Length: 429  Bit Score: 39.57  E-value: 4.48e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1277971089   2 QKYDVIVVGAGHAGCEAALATAKMGLRTLLL 32
Cdd:PRK10015    4 DKFDAIVVGAGVAGSVAALVMARAGLDVLVI 34
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
2-32 6.67e-03

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 39.12  E-value: 6.67e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1277971089   2 QKYDVIVVGAGHAGCEAALATAKMGLRTLLL 32
Cdd:COG0665     1 ATADVVVIGGGIAGLSTAYHLARRGLDVTVL 31
PRK07804 PRK07804
L-aspartate oxidase; Provisional
 5-33 8.24e-03

L-aspartate oxidase; Provisional


Pssm-ID: 236102 [Multi-domain]  Cd Length: 541  Bit Score: 39.18  E-value: 8.24e-03
                          10        20
                  ....*....|....*....|....*....
gi 1277971089   5 DVIVVGAGHAGCEAALATAKMGLRTLLLT 33
Cdd:PRK07804   18 DVVVVGSGVAGLTAALAARRAGRRVLVVT 46
HI0933_like pfam03486
HI0933-like protein;
4-32 8.78e-03

HI0933-like protein;


Pssm-ID: 427330 [Multi-domain]  Cd Length: 406  Bit Score: 38.72  E-value: 8.78e-03
                          10        20
                  ....*....|....*....|....*....
gi 1277971089   4 YDVIVVGAGHAGCEAALATAKMGLRTLLL 32
Cdd:pfam03486   1 FDVIVIGGGAAGLMAAISAAKRGRRVLLI 29
TrmFO COG1206
Folate-dependent tRNA-U54 methylase TrmFO/GidA [Translation, ribosomal structure and ...
 5-28 9.67e-03

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: 38.50  E-value: 9.67e-03
                          10        20
                  ....*....|....*....|....
gi 1277971089   5 DVIVVGAGHAGCEAALATAKMGLR 28
Cdd:COG1206     3 PVTVIGGGLAGSEAAWQLAERGVP 26
 
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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