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Conserved domains on  [gi|493290588|ref|WP_006248291|]
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tRNA uridine-5-carboxymethylaminomethyl(34) synthesis enzyme MnmG [Mannheimia haemolytica]

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 ...
 1-628 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: 1235.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588   1 MIYNQIYDVIVVGGGHAGTEAALAPARMGLKTLILTHNVDTLGQMSCNPAIGGIGKGHLVKEIDAMGGLMAKATDVAGIQ 80
Cdd:COG0445    1 MYYPKEYDVIVVGGGHAGCEAALAAARMGAKTLLLTHNLDTIGQMSCNPAIGGIAKGHLVREIDALGGEMGRAADKTGIQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588  81 FRTLNNSKGPAVRATRAQADRVLYRNAVRTALENQPNLDIFQQEVVDILVENNRAVGAVTKMGLTFKARAVVLTAGTFLA 160
Cdd:COG0445   81 FRMLNTSKGPAVRAPRAQADRKLYRAAMRETLENQPNLDLIQGEVEDLIVEDGRVTGVVTADGIEFRAKAVVLTTGTFLN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588 161 GKIHIGLDNYAGGRAGDPAATMLADRLRDLNLRVDRLKTGTPPRLDARTINFDVLAKQHGDEVLPVFSFMGDVsQHPRQI 240
Cdd:COG0445  161 GLIHIGEKSYPGGRAGEPPSVGLSESLRELGFELGRLKTGTPPRIDGRSIDFSKLEEQPGDEPPPPFSFLTEK-IHPPQI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588 241 PCYITHTNDQTHDLIRNSLDRSPMYTGIIEGVGPRYCPSIEDKVMRFADRNSHQIYLEPEGLNTIEVYPNGISTSLPFDV 320
Cdd:COG0445  240 PCWITYTNEETHEIIRENLHRSPMYSGVIEGVGPRYCPSIEDKIVRFADKDRHQIFLEPEGLDTNEVYPNGISTSLPEDV 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588 321 QMGIVNSMKGLENTRIIKPGYAIEYDYFDPRDLKPTLETKAIDGLFFAGQINGTTGYEEAGAQGLLAGINAALQVQGKEA 400
Cdd:COG0445  320 QLAMLRSIPGLENAEILRPGYAIEYDYVDPTQLKPTLETKKIEGLFFAGQINGTTGYEEAAAQGLMAGINAALKAQGKEP 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588 401 WYPTRDQAYTGVLVDDLCTLGTKEPYRVFTSRAEYRLLLREDNADIRLTPKAHELGLIDEARWVRFNQKMEAIEQERARL 480
Cdd:COG0445  400 FILDRSEAYIGVLIDDLVTKGTDEPYRMFTSRAEYRLLLRQDNADLRLTEKGYELGLVSDERYERFEEKKEAIEEEIERL 479

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588 481 KSTWAHLQMPNLDELNALLANPLAREASGEDLIRRPEMSYEKLTQIALFAPAIeDKQVAEQVEIAIKYQGYIEHQYNEIE 560
Cdd:COG0445  480 KSTRVTPNEEVNEGLEELGSSPLKRGVSLFDLLRRPEITYEDLAELDPELPDL-DPEVAEQVEIEIKYEGYIERQEEEIE 558

                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493290588 561 RHKRHENTLIPVEFDYDKVESLSNEVRAKLMQHRPVSIGQASRISGITPAAISILLVNLKKQGMLKRG 628
Cdd:COG0445  559 KLKRLENLKIPEDFDYDAIPGLSNEAREKLKKIRPETLGQASRISGVTPADISLLLVYLKRRRRRKKA 626
 
Name Accession Description Interval E-value
MnmG COG0445
tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal ...
 1-628 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: 1235.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588   1 MIYNQIYDVIVVGGGHAGTEAALAPARMGLKTLILTHNVDTLGQMSCNPAIGGIGKGHLVKEIDAMGGLMAKATDVAGIQ 80
Cdd:COG0445    1 MYYPKEYDVIVVGGGHAGCEAALAAARMGAKTLLLTHNLDTIGQMSCNPAIGGIAKGHLVREIDALGGEMGRAADKTGIQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588  81 FRTLNNSKGPAVRATRAQADRVLYRNAVRTALENQPNLDIFQQEVVDILVENNRAVGAVTKMGLTFKARAVVLTAGTFLA 160
Cdd:COG0445   81 FRMLNTSKGPAVRAPRAQADRKLYRAAMRETLENQPNLDLIQGEVEDLIVEDGRVTGVVTADGIEFRAKAVVLTTGTFLN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588 161 GKIHIGLDNYAGGRAGDPAATMLADRLRDLNLRVDRLKTGTPPRLDARTINFDVLAKQHGDEVLPVFSFMGDVsQHPRQI 240
Cdd:COG0445  161 GLIHIGEKSYPGGRAGEPPSVGLSESLRELGFELGRLKTGTPPRIDGRSIDFSKLEEQPGDEPPPPFSFLTEK-IHPPQI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588 241 PCYITHTNDQTHDLIRNSLDRSPMYTGIIEGVGPRYCPSIEDKVMRFADRNSHQIYLEPEGLNTIEVYPNGISTSLPFDV 320
Cdd:COG0445  240 PCWITYTNEETHEIIRENLHRSPMYSGVIEGVGPRYCPSIEDKIVRFADKDRHQIFLEPEGLDTNEVYPNGISTSLPEDV 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588 321 QMGIVNSMKGLENTRIIKPGYAIEYDYFDPRDLKPTLETKAIDGLFFAGQINGTTGYEEAGAQGLLAGINAALQVQGKEA 400
Cdd:COG0445  320 QLAMLRSIPGLENAEILRPGYAIEYDYVDPTQLKPTLETKKIEGLFFAGQINGTTGYEEAAAQGLMAGINAALKAQGKEP 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588 401 WYPTRDQAYTGVLVDDLCTLGTKEPYRVFTSRAEYRLLLREDNADIRLTPKAHELGLIDEARWVRFNQKMEAIEQERARL 480
Cdd:COG0445  400 FILDRSEAYIGVLIDDLVTKGTDEPYRMFTSRAEYRLLLRQDNADLRLTEKGYELGLVSDERYERFEEKKEAIEEEIERL 479

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588 481 KSTWAHLQMPNLDELNALLANPLAREASGEDLIRRPEMSYEKLTQIALFAPAIeDKQVAEQVEIAIKYQGYIEHQYNEIE 560
Cdd:COG0445  480 KSTRVTPNEEVNEGLEELGSSPLKRGVSLFDLLRRPEITYEDLAELDPELPDL-DPEVAEQVEIEIKYEGYIERQEEEIE 558

                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493290588 561 RHKRHENTLIPVEFDYDKVESLSNEVRAKLMQHRPVSIGQASRISGITPAAISILLVNLKKQGMLKRG 628
Cdd:COG0445  559 KLKRLENLKIPEDFDYDAIPGLSNEAREKLKKIRPETLGQASRISGVTPADISLLLVYLKRRRRRKKA 626
gidA TIGR00136
glucose-inhibited division protein A; GidA, the longer of two forms of GidA-related proteins, ...
 7-623 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: 1081.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588    7 YDVIVVGGGHAGTEAALAPARMGLKTLILTHNVDTLGQMSCNPAIGGIGKGHLVKEIDAMGGLMAKATDVAGIQFRTLNN 86
Cdd:TIGR00136   1 FDVIVIGGGHAGCEAALAAARLGAKTLLLTLNLDTIGKCSCNPAIGGPAKGILVKEIDALGGEMGKAADKTGLQFRVLNS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588   87 SKGPAVRATRAQADRVLYRNAVRTALENQPNLDIFQQEVVDILVE-NNRAVGAVTKMGLTFKARAVVLTAGTFLAGKIHI 165
Cdd:TIGR00136  81 SKGPAVRATRAQIDKILYQKWMRNQLENQPNLSLFQGEVEDLILEdNDEIKGVVTKDGNEFRAKAVIITTGTFLRGKIHI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588  166 GLDNYAGGRAGDPAATMLADRLRDLNLRVDRLKTGTPPRLDARTINFDVLAKQHGDEVLPVFSFMGDVSQhPRQIPCYIT 245
Cdd:TIGR00136 161 GDKSYEAGRAGEQASYGLSTTLRELGFKTGRLKTGTPPRIDKRSIDFSKLEVQFGDTQPPAFSFTNKNFL-PQQLPCYLT 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588  246 HTNDQTHDLIRNSLDRSPMYTGIIEGVGPRYCPSIEDKVMRFADRNSHQIYLEPEGLNTIEVYPNGISTSLPFDVQMGIV 325
Cdd:TIGR00136 240 HTNPKTHQIIRDNLHRSPMYSGSIEGNGPRYCPSIEDKVVRFADKERHQIFLEPEGLNSDEIYLNGLSTSLPEDVQLKII 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588  326 NSMKGLENTRIIKPGYAIEYDYFDPRDLKPTLETKAIDGLFFAGQINGTTGYEEAGAQGLLAGINAALQVQGKEAWYPTR 405
Cdd:TIGR00136 320 RSIPGLENAEILRPGYAIEYDYFDPTQLKPTLETKLIKGLFFAGQINGTTGYEEAAAQGLMAGINAALKLQNKEPFILKR 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588  406 DQAYTGVLVDDLCTLGTKEPYRVFTSRAEYRLLLREDNADIRLTPKAHELGLIDEARWVRFNQKMEAIEQERARLKSTWA 485
Cdd:TIGR00136 400 NEAYIGVLIDDLVTKGTKEPYRMFTSRAEYRLLLREDNADFRLTEIGRELGLIDEDRYARFLKKKQNIEEEIERLKSTRL 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588  486 HLQMPNLDELNALLANPLAREASGEDLIRRPEMSYEKLTQIALFAPAIeDKQVAEQVEIAIKYQGYIEHQYNEIERHKRH 565
Cdd:TIGR00136 480 SPSKEVKEELKNLAQSPLKDEVSGYDLLKRPEMNLDKLTKLLPFLPPL-DEEVLEQVEIEIKYEGYIKKQQQYIKKLDRL 558

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 493290588  566 ENTLIPVEFDYDKVESLSNEVRAKLMQHRPVSIGQASRISGITPAAISILLVNLKKQG 623
Cdd:TIGR00136 559 ENVKIPADFDYRKIPGLSTEAREKLSKFRPLSLGQASRISGINPADISALLVYLKKQK 616
GIDA pfam01134
Glucose inhibited division protein A;
8-399 0e+00

Glucose inhibited division protein A;


Pssm-ID: 250388 [Multi-domain]  Cd Length: 391  Bit Score: 670.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588    8 DVIVVGGGHAGTEAALAPARMGLKTLILTHNVDTLGQMSCNPAIGGIGKGHLVKEIDAMGGLMAKATDVAGIQFRTLNNS 87
Cdd:pfam01134   1 DVIVIGGGHAGCEAALAAARMGAKVLLITHNTDTIAELSCNPSIGGIAKGHLVREIDALGGLMGKAADKTGIQFRMLNTS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588   88 KGPAVRATRAQADRVLYRNAVRTALENQPNLDIFQQEVVDILVENNRAVGAVTKMGLTFKARAVVLTAGTFLAGKIHIGL 167
Cdd:pfam01134  81 KGPAVRALRAQVDRDLYSKEMTETLENHPNLTLIQGEVTDLIPENGKVKGVVTEDGEEYKAKAVVLATGTFLNGKIHIGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588  168 DNYAGGRAGDPAATMLADRLRDLNLRVDRLKTGTPPRLDARTINFDVLAKQHGDEVLPVFSFMGDVSqHPRQIPCYITHT 247
Cdd:pfam01134 161 KCYPAGRLGELTSEGLSESLKELGFELGRFKTGTPPRIDKDSIDFSKLEEQPGDKPGPPFSYLNCPM-NKEQYPCFLTYT 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588  248 NDQTHDLIRNSLDRSPMYTGIIEGVGPRYCPSIEDKVMRFADRNSHQIYLEPEGLNTIEVYPNGISTSLPFDVQMGIVNS 327
Cdd:pfam01134 240 NEATHEIIRDNLHRSPMFEGCIEGIGPRYCPSIEDKPVRFADKPYHQVFLEPEGLDTDEYYLVGFSTSLPEDVQKRVLRT 319

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493290588  328 MKGLENTRIIKPGYAIEYDYFDPRDLKPTLETKAIDGLFFAGQINGTTGYEEAGAQGLLAGINAALQVQGKE 399
Cdd:pfam01134 320 IPGLENAEIVRPGYAIEYDYIDPPQLLPTLETKKIPGLFFAGQINGTEGYEEAAAQGLLAGINAARKALGKE 391
PRK05335 PRK05335
tRNA (uracil-5-)-methyltransferase Gid; Reviewed
 330-399 8.49e-13

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


Pssm-ID: 235416  Cd Length: 436  Bit Score: 70.56  E-value: 8.49e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493290588 330 GLENTRIIKPGYAIEYDYFD-PRDLKPTLETKAIDGLFFAGQINGTTGYEEAGAQGLLAGINAALQVQGKE 399
Cdd:PRK05335 297 GLENAEFVRYGVMHRNTFINsPKLLDPTLQLKKRPNLFFAGQITGVEGYVESAASGLLAGINAARLALGKE 367
 
Name Accession Description Interval E-value
MnmG COG0445
tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal ...
 1-628 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: 1235.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588   1 MIYNQIYDVIVVGGGHAGTEAALAPARMGLKTLILTHNVDTLGQMSCNPAIGGIGKGHLVKEIDAMGGLMAKATDVAGIQ 80
Cdd:COG0445    1 MYYPKEYDVIVVGGGHAGCEAALAAARMGAKTLLLTHNLDTIGQMSCNPAIGGIAKGHLVREIDALGGEMGRAADKTGIQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588  81 FRTLNNSKGPAVRATRAQADRVLYRNAVRTALENQPNLDIFQQEVVDILVENNRAVGAVTKMGLTFKARAVVLTAGTFLA 160
Cdd:COG0445   81 FRMLNTSKGPAVRAPRAQADRKLYRAAMRETLENQPNLDLIQGEVEDLIVEDGRVTGVVTADGIEFRAKAVVLTTGTFLN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588 161 GKIHIGLDNYAGGRAGDPAATMLADRLRDLNLRVDRLKTGTPPRLDARTINFDVLAKQHGDEVLPVFSFMGDVsQHPRQI 240
Cdd:COG0445  161 GLIHIGEKSYPGGRAGEPPSVGLSESLRELGFELGRLKTGTPPRIDGRSIDFSKLEEQPGDEPPPPFSFLTEK-IHPPQI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588 241 PCYITHTNDQTHDLIRNSLDRSPMYTGIIEGVGPRYCPSIEDKVMRFADRNSHQIYLEPEGLNTIEVYPNGISTSLPFDV 320
Cdd:COG0445  240 PCWITYTNEETHEIIRENLHRSPMYSGVIEGVGPRYCPSIEDKIVRFADKDRHQIFLEPEGLDTNEVYPNGISTSLPEDV 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588 321 QMGIVNSMKGLENTRIIKPGYAIEYDYFDPRDLKPTLETKAIDGLFFAGQINGTTGYEEAGAQGLLAGINAALQVQGKEA 400
Cdd:COG0445  320 QLAMLRSIPGLENAEILRPGYAIEYDYVDPTQLKPTLETKKIEGLFFAGQINGTTGYEEAAAQGLMAGINAALKAQGKEP 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588 401 WYPTRDQAYTGVLVDDLCTLGTKEPYRVFTSRAEYRLLLREDNADIRLTPKAHELGLIDEARWVRFNQKMEAIEQERARL 480
Cdd:COG0445  400 FILDRSEAYIGVLIDDLVTKGTDEPYRMFTSRAEYRLLLRQDNADLRLTEKGYELGLVSDERYERFEEKKEAIEEEIERL 479

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588 481 KSTWAHLQMPNLDELNALLANPLAREASGEDLIRRPEMSYEKLTQIALFAPAIeDKQVAEQVEIAIKYQGYIEHQYNEIE 560
Cdd:COG0445  480 KSTRVTPNEEVNEGLEELGSSPLKRGVSLFDLLRRPEITYEDLAELDPELPDL-DPEVAEQVEIEIKYEGYIERQEEEIE 558

                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493290588 561 RHKRHENTLIPVEFDYDKVESLSNEVRAKLMQHRPVSIGQASRISGITPAAISILLVNLKKQGMLKRG 628
Cdd:COG0445  559 KLKRLENLKIPEDFDYDAIPGLSNEAREKLKKIRPETLGQASRISGVTPADISLLLVYLKRRRRRKKA 626
gidA TIGR00136
glucose-inhibited division protein A; GidA, the longer of two forms of GidA-related proteins, ...
 7-623 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: 1081.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588    7 YDVIVVGGGHAGTEAALAPARMGLKTLILTHNVDTLGQMSCNPAIGGIGKGHLVKEIDAMGGLMAKATDVAGIQFRTLNN 86
Cdd:TIGR00136   1 FDVIVIGGGHAGCEAALAAARLGAKTLLLTLNLDTIGKCSCNPAIGGPAKGILVKEIDALGGEMGKAADKTGLQFRVLNS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588   87 SKGPAVRATRAQADRVLYRNAVRTALENQPNLDIFQQEVVDILVE-NNRAVGAVTKMGLTFKARAVVLTAGTFLAGKIHI 165
Cdd:TIGR00136  81 SKGPAVRATRAQIDKILYQKWMRNQLENQPNLSLFQGEVEDLILEdNDEIKGVVTKDGNEFRAKAVIITTGTFLRGKIHI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588  166 GLDNYAGGRAGDPAATMLADRLRDLNLRVDRLKTGTPPRLDARTINFDVLAKQHGDEVLPVFSFMGDVSQhPRQIPCYIT 245
Cdd:TIGR00136 161 GDKSYEAGRAGEQASYGLSTTLRELGFKTGRLKTGTPPRIDKRSIDFSKLEVQFGDTQPPAFSFTNKNFL-PQQLPCYLT 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588  246 HTNDQTHDLIRNSLDRSPMYTGIIEGVGPRYCPSIEDKVMRFADRNSHQIYLEPEGLNTIEVYPNGISTSLPFDVQMGIV 325
Cdd:TIGR00136 240 HTNPKTHQIIRDNLHRSPMYSGSIEGNGPRYCPSIEDKVVRFADKERHQIFLEPEGLNSDEIYLNGLSTSLPEDVQLKII 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588  326 NSMKGLENTRIIKPGYAIEYDYFDPRDLKPTLETKAIDGLFFAGQINGTTGYEEAGAQGLLAGINAALQVQGKEAWYPTR 405
Cdd:TIGR00136 320 RSIPGLENAEILRPGYAIEYDYFDPTQLKPTLETKLIKGLFFAGQINGTTGYEEAAAQGLMAGINAALKLQNKEPFILKR 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588  406 DQAYTGVLVDDLCTLGTKEPYRVFTSRAEYRLLLREDNADIRLTPKAHELGLIDEARWVRFNQKMEAIEQERARLKSTWA 485
Cdd:TIGR00136 400 NEAYIGVLIDDLVTKGTKEPYRMFTSRAEYRLLLREDNADFRLTEIGRELGLIDEDRYARFLKKKQNIEEEIERLKSTRL 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588  486 HLQMPNLDELNALLANPLAREASGEDLIRRPEMSYEKLTQIALFAPAIeDKQVAEQVEIAIKYQGYIEHQYNEIERHKRH 565
Cdd:TIGR00136 480 SPSKEVKEELKNLAQSPLKDEVSGYDLLKRPEMNLDKLTKLLPFLPPL-DEEVLEQVEIEIKYEGYIKKQQQYIKKLDRL 558

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 493290588  566 ENTLIPVEFDYDKVESLSNEVRAKLMQHRPVSIGQASRISGITPAAISILLVNLKKQG 623
Cdd:TIGR00136 559 ENVKIPADFDYRKIPGLSTEAREKLSKFRPLSLGQASRISGINPADISALLVYLKKQK 616
GIDA pfam01134
Glucose inhibited division protein A;
8-399 0e+00

Glucose inhibited division protein A;


Pssm-ID: 250388 [Multi-domain]  Cd Length: 391  Bit Score: 670.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588    8 DVIVVGGGHAGTEAALAPARMGLKTLILTHNVDTLGQMSCNPAIGGIGKGHLVKEIDAMGGLMAKATDVAGIQFRTLNNS 87
Cdd:pfam01134   1 DVIVIGGGHAGCEAALAAARMGAKVLLITHNTDTIAELSCNPSIGGIAKGHLVREIDALGGLMGKAADKTGIQFRMLNTS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588   88 KGPAVRATRAQADRVLYRNAVRTALENQPNLDIFQQEVVDILVENNRAVGAVTKMGLTFKARAVVLTAGTFLAGKIHIGL 167
Cdd:pfam01134  81 KGPAVRALRAQVDRDLYSKEMTETLENHPNLTLIQGEVTDLIPENGKVKGVVTEDGEEYKAKAVVLATGTFLNGKIHIGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588  168 DNYAGGRAGDPAATMLADRLRDLNLRVDRLKTGTPPRLDARTINFDVLAKQHGDEVLPVFSFMGDVSqHPRQIPCYITHT 247
Cdd:pfam01134 161 KCYPAGRLGELTSEGLSESLKELGFELGRFKTGTPPRIDKDSIDFSKLEEQPGDKPGPPFSYLNCPM-NKEQYPCFLTYT 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588  248 NDQTHDLIRNSLDRSPMYTGIIEGVGPRYCPSIEDKVMRFADRNSHQIYLEPEGLNTIEVYPNGISTSLPFDVQMGIVNS 327
Cdd:pfam01134 240 NEATHEIIRDNLHRSPMFEGCIEGIGPRYCPSIEDKPVRFADKPYHQVFLEPEGLDTDEYYLVGFSTSLPEDVQKRVLRT 319

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493290588  328 MKGLENTRIIKPGYAIEYDYFDPRDLKPTLETKAIDGLFFAGQINGTTGYEEAGAQGLLAGINAALQVQGKE 399
Cdd:pfam01134 320 IPGLENAEIVRPGYAIEYDYIDPPQLLPTLETKKIPGLFFAGQINGTEGYEEAAAQGLLAGINAARKALGKE 391
GIDA_C pfam13932
tRNA modifying enzyme MnmG/GidA C-terminal domain; The GidA associated domain is a domain that ...
 401-616 3.86e-116

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: 345.13  E-value: 3.86e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588  401 WYPTRDQAYTGVLVDDLCTLGTKEPYRVFTSRAEYRLLLREDNADIRLTPKAHELGLIDEARWVRFNQKMEAIEQERARL 480
Cdd:pfam13932   1 LILSRSEAYIGVLIDDLVTKGTSEPYRMFTSRAEYRLLLRQDNADLRLTEKGRELGLVSDERYERFEEKKEAIEEEIERL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588  481 KSTWAHLQMPNLDELNaLLANPLAREASGEDLIRRPEMSYEKLTQIALFAPAIeDKQVAEQVEIAIKYQGYIEHQYNEIE 560
Cdd:pfam13932  81 KSTRLSPSEWNNALLE-LGSAPLGTGRSAFDLLRRPEVTYEDLAALIPELAPL-DPEVLEQVEIEAKYEGYIERQEAEIE 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 493290588  561 RHKRHENTLIPVEFDYDKVESLSNEVRAKLMQHRPVSIGQASRISGITPAAISILL 616
Cdd:pfam13932 159 KFKRLENLKIPEDLDYDAIPGLSNEAREKLNKIRPETIGQASRISGVTPADISVLL 214
TrmFO COG1206
Folate-dependent tRNA-U54 methylase TrmFO/GidA [Translation, ribosomal structure and ...
 350-408 1.94e-13

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: 72.79  E-value: 1.94e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 493290588 350 PRDLKPTLETKAIDGLFFAGQINGTTGYEEAGAQGLLAGINAALQVQGKEAWYPTRDQA 408
Cdd:COG1206  318 PKLLDPTLQLKARPNLFFAGQITGVEGYVESAASGLLAGINAARLLLGKEPVPPPPTTA 376
PRK05335 PRK05335
tRNA (uracil-5-)-methyltransferase Gid; Reviewed
 330-399 8.49e-13

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


Pssm-ID: 235416  Cd Length: 436  Bit Score: 70.56  E-value: 8.49e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493290588 330 GLENTRIIKPGYAIEYDYFD-PRDLKPTLETKAIDGLFFAGQINGTTGYEEAGAQGLLAGINAALQVQGKE 399
Cdd:PRK05335 297 GLENAEFVRYGVMHRNTFINsPKLLDPTLQLKKRPNLFFAGQITGVEGYVESAASGLLAGINAARLALGKE 367
FAD_oxidored pfam12831
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ...
 8-152 3.30e-10

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


Pssm-ID: 432816 [Multi-domain]  Cd Length: 420  Bit Score: 62.63  E-value: 3.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588    8 DVIVVGGGHAGTEAALAPARMGLKTLiLTHNVDTLGQMSCN--------------PAIGGIGkGHLVKEIDAMGGLMAKA 73
Cdd:pfam12831   1 DVVVVGGGPAGVAAAIAAARAGAKVL-LVERRGFLGGMLTSglvgpdmgfylnkeQVVGGIA-REFRQRLRARGGLPGPY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588   74 TDvaGIQFRTLNNSKGPAVratraqADRVLyrnavrtaleNQPNLDI-FQQEVVDILVENNRAVGAVTKM---GLTFKAR 149
Cdd:pfam12831  79 GL--RGGWVPFDPEVAKAV------LDEML----------AEAGVTVlLHTRVVGVVKEGGRITGVTVETkggRITIRAK 140


                  ...
gi 493290588  150 AVV 152
Cdd:pfam12831 141 VFI 143
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
 7-156 6.17e-07

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: 52.14  E-value: 6.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588   7 YDVIVVGGGHAGTEAALAPARMGLKTLILTHnVDTLG----------QMSCNP---AIGGIGKGHLVKEIDAMGG----- 68
Cdd:COG1053    4 YDVVVVGSGGAGLRAALEAAEAGLKVLVLEK-VPPRGghtaaaqggiNAAGTNvqkAAGEDSPEEHFYDTVKGGDgladq 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588  69 ----LMAK-ATDVA------GIQFR-----TLNNSKGPAVRATRAQADRV-------LYRNAVRTalenqpNLDIFQQ-E 124
Cdd:COG1053   83 dlveALAEeAPEAIdwleaqGVPFSrtpdgRLPQFGGHSVGRTCYAGDGTghallatLYQAALRL------GVEIFTEtE 156

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 493290588 125 VVDILVENNRAVGAVTKMG----LTFKARAVVLTAG 156
Cdd:COG1053  157 VLDLIVDDGRVVGVVARDRtgeiVRIRAKAVVLATG 192
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
7-156 6.40e-07

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 51.66  E-value: 6.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588   7 YDVIVVGGGHAGTEAALAPARMGLKTLILthnvdtlgqmscnpaiggigkghlvkEIDAMGGLMAKATDV-------AGI 79
Cdd:COG0492    1 YDVVIIGAGPAGLTAAIYAARAGLKTLVI--------------------------EGGEPGGQLATTKEIenypgfpEGI 54

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493290588  80 QfrtlnnskGPA-VRATRAQADRVlyrnavrtalenqpNLDIFQQEVVDILVENNRAVgAVTKMGLTFKARAVVLTAG 156
Cdd:COG0492   55 S--------GPElAERLREQAERF--------------GAEILLEEVTSVDKDDGPFR-VTTDDGTEYEAKAVIIATG 109
PRK05329 PRK05329
glycerol-3-phosphate dehydrogenase subunit GlpB;
7-46 3.03e-04

glycerol-3-phosphate dehydrogenase subunit GlpB;


Pssm-ID: 235412  Cd Length: 422  Bit Score: 43.69  E-value: 3.03e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 493290588   7 YDVIVVGGGHAGTEAALAPARMGLKTLILTHNVDTLGQMS 46
Cdd:PRK05329   3 FDVLVIGGGLAGLTAALAAAEAGKRVALVAKGQGALHFSS 42
PRK07843 PRK07843
3-oxosteroid 1-dehydrogenase;
5-35 3.72e-04

3-oxosteroid 1-dehydrogenase;


Pssm-ID: 236111 [Multi-domain]  Cd Length: 557  Bit Score: 43.49  E-value: 3.72e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 493290588   5 QIYDVIVVGGGHAGTEAALAPARMGLKTLIL 35
Cdd:PRK07843   6 QEYDVVVVGSGAAGMVAALTAAHRGLSTVVV 36
PRK15317 PRK15317
alkyl hydroperoxide reductase subunit F; Provisional
 7-43 5.45e-04

alkyl hydroperoxide reductase subunit F; Provisional


Pssm-ID: 237942 [Multi-domain]  Cd Length: 517  Bit Score: 42.84  E-value: 5.45e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 493290588   7 YDVIVVGGGHAGTEAALAPARMGLKTLILTHNV-----DTLG 43
Cdd:PRK15317 212 YDVLVVGGGPAGAAAAIYAARKGIRTGIVAERFggqvlDTMG 253
GlpB COG3075
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];
7-42 9.49e-04

Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];


Pssm-ID: 442309  Cd Length: 415  Bit Score: 42.09  E-value: 9.49e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 493290588   7 YDVIVVGGGHAGTEAALAPARMGLKTLILTHNVDTL 42
Cdd:COG3075    3 FDVVVIGGGLAGLTAAIRAAEAGLRVAIVSAGQSAL 38
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 7-35 9.66e-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: 41.53  E-value: 9.66e-04
                          10        20
                  ....*....|....*....|....*....
gi 493290588    7 YDVIVVGGGHAGTEAALAPARMGLKTLIL 35
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLI 29
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
 8-158 1.38e-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: 41.50  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588    8 DVIVVGGGHAGTEAALAPARMGLKTLIlthnVDTLGQMSCNPAI--GGI---GKGHLVKE-------IDAMGGL------ 69
Cdd:pfam00890   1 DVLVIGGGLAGLAAALAAAEAGLKVAV----VEKGQPFGGATAWssGGIdalGNPPQGGIdspelhpTDTLKGLdeladh 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588   70 -----MAKATDVAGIQFRT----LNNSKGPAVRATR----AQADRVLYRNAVRT-----------ALENQ---PNLDI-F 121
Cdd:pfam00890  77 pyveaFVEAAPEAVDWLEAlgvpFSRTEDGHLDLRPlgglSATWRTPHDAADRRrglgtghallaRLLEGlrkAGVDFqP 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 493290588  122 QQEVVDILVENNRAVGAV----TKMGL-TFKAR-AVVLTAGTF 158
Cdd:pfam00890 157 RTAADDLIVEDGRVTGAVvenrRNGREvRIRAIaAVLLATGGF 199
GG-red-SF TIGR02032
geranylgeranyl reductase family; This model represents a subfamily which includes ...
 7-156 1.41e-03

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: 41.15  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493290588    7 YDVIVVGGGHAGTEAALAPARMGLKTLILTHNvDTLGQMSCnpaiGGIGKGHLVKEIDAMGGLMAKATDVAGI--QFRTL 84
Cdd:TIGR02032   1 YDVVVVGAGPAGASAAYRLADKGLRVLLLEKK-SFPRYKPC----GGALSPRALEELDLPGELIVNLVRGARFfsPNGDS 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493290588   85 NNSKGPAVRA---TRAQADRVLYRNAVRTALENQPNldifqQEVVDILVENNRAVGAVTKMGLTFKARAVVLTAG 156
Cdd:TIGR02032  76 VEIPIETELAyviDRDAFDEQLAERAQEAGAELRLG-----TRVLDVEIHDDRVVVIVRGSEGTVTAKIVIGADG 145
PRK12844 PRK12844
3-ketosteroid-delta-1-dehydrogenase; Reviewed
 1-35 1.48e-03

3-ketosteroid-delta-1-dehydrogenase; Reviewed


Pssm-ID: 183787 [Multi-domain]  Cd Length: 557  Bit Score: 41.66  E-value: 1.48e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 493290588   1 MIYNQIYDVIVVGGGHAGTEAALAPARMGLKTLIL 35
Cdd:PRK12844   1 ATWDETYDVVVVGSGGGGMCAALAAADSGLEPLIV 35
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 7-34 2.47e-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: 40.84  E-value: 2.47e-03
                         10        20
                 ....*....|....*....|....*...
gi 493290588   7 YDVIVVGGGHAGTEAALAPARMGLKTLI 34
Cdd:COG1249    4 YDLVVIGAGPGGYVAAIRAAQLGLKVAL 31
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 123-155 4.93e-03

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 39.83  E-value: 4.93e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 493290588 123 QEVVDILVENNRAVGAVTKMGLTFKARAVVLTA 155
Cdd:COG1233  243 AEVERILVEGGRATGVRLADGEEIRADAVVSNA 275
PRK08071 PRK08071
L-aspartate oxidase; Provisional
 105-156 7.30e-03

L-aspartate oxidase; Provisional


Pssm-ID: 236147 [Multi-domain]  Cd Length: 510  Bit Score: 39.20  E-value: 7.30e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 493290588 105 RNAVRTALENQ-PNLDIFQQE-VVDILVENNRAVGAVTKMGL----TFKARAVVLTAG 156
Cdd:PRK08071 130 KNLLEHLLQELvPHVTVVEQEmVIDLIIENGRCIGVLTKDSEgklkRYYADYVVLASG 187
HI0933_like pfam03486
HI0933-like protein;
7-38 9.07e-03

HI0933-like protein;


Pssm-ID: 427330 [Multi-domain]  Cd Length: 406  Bit Score: 38.72  E-value: 9.07e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 493290588    7 YDVIVVGGGHAGTEAALAPARMGLKTLILTHN 38
Cdd:pfam03486   1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKG 32
 
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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