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Conserved domains on  [gi|616684526|gb|KAE82235|]
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tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG [Staphylococcus aureus VET0402R]

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 ...
 1-624 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: 1205.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526   1 MVQEYDVIVIGAGHAGVEAGLASARRGAKTLMLTINLDNIAFMPCNPSVGGPAKGIVVREIDALGGQMAKTIDKTHIQMR 80
Cdd:COG0445    3 YPKEYDVIVVGGGHAGCEAALAAARMGAKTLLLTHNLDTIGQMSCNPAIGGIAKGHLVREIDALGGEMGRAADKTGIQFR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526  81 MLNTGKGPAVRALRAQADKVLYQQEMKRVIEDEENLHIMQGMVDELIIEDNEVKGVRTNIGTEYLSKAVIITTGTFLRGE 160
Cdd:COG0445   83 MLNTSKGPAVRAPRAQADRKLYRAAMRETLENQPNLDLIQGEVEDLIVEDGRVTGVVTADGIEFRAKAVVLTTGTFLNGL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526 161 IILGNMKYSSGPNHQLPSITLSDNLRELGFEIVRFKTGTPPRVNSKTIDYSKTEIQPGDDVGRAFSFETTEYILDQLPCW 240
Cdd:COG0445  163 IHIGEKSYPGGRAGEPPSVGLSESLRELGFELGRLKTGTPPRIDGRSIDFSKLEEQPGDEPPPPFSFLTEKIHPPQIPCW 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526 241 LTYTNAETHKVIDDNLHLSAMYSGMIKGTGPRYCPSIEDKFVRFNDKPRHQLFLEPEGRNTNEVYVQGLSTSLPEHVQRQ 320
Cdd:COG0445  243 ITYTNEETHEIIRENLHRSPMYSGVIEGVGPRYCPSIEDKIVRFADKDRHQIFLEPEGLDTNEVYPNGISTSLPEDVQLA 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526 321 MLETIPGLEKADMMRAGYAIEYDAIVPTQLWPTLETKMIKNLYTAGQINGTSGYEEAAGQGLMAGINAAGKVLNTGEKIL 400
Cdd:COG0445  323 MLRSIPGLENAEILRPGYAIEYDYVDPTQLKPTLETKKIEGLFFAGQINGTTGYEEAAAQGLMAGINAALKAQGKEPFIL 402

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526 401 SRSDAYIGVLIDDLVTKGTNEPYRLLTSRAEYRLLLRHDNADLRLTDMGYELGMISEERYARFNEKRQQIDAEIKRLSDI 480
Cdd:COG0445  403 DRSEAYIGVLIDDLVTKGTDEPYRMFTSRAEYRLLLRQDNADLRLTEKGYELGLVSDERYERFEEKKEAIEEEIERLKST 482

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526 481 RIKPNEHTQAIIEQHGGSRLKDGILAIDLLRRPEMTYDIILEILEEEHQLNADVEEQVEIQTKYEGYINKSLQQVEKVKR 560
Cdd:COG0445  483 RVTPNEEVNEGLEELGSSPLKRGVSLFDLLRRPEITYEDLAELDPELPDLDPEVAEQVEIEIKYEGYIERQEEEIEKLKR 562

                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616684526 561 MEEKKIPEDLDYSKIDSLATEAREKLSEVKPLNIAQASRISGVNPADISILLIYLEQGKLQRVS 624
Cdd:COG0445  563 LENLKIPEDFDYDAIPGLSNEAREKLKKIRPETLGQASRISGVTPADISLLLVYLKRRRRRKKA 626
 
Name Accession Description Interval E-value
MnmG COG0445
tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal ...
 1-624 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: 1205.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526   1 MVQEYDVIVIGAGHAGVEAGLASARRGAKTLMLTINLDNIAFMPCNPSVGGPAKGIVVREIDALGGQMAKTIDKTHIQMR 80
Cdd:COG0445    3 YPKEYDVIVVGGGHAGCEAALAAARMGAKTLLLTHNLDTIGQMSCNPAIGGIAKGHLVREIDALGGEMGRAADKTGIQFR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526  81 MLNTGKGPAVRALRAQADKVLYQQEMKRVIEDEENLHIMQGMVDELIIEDNEVKGVRTNIGTEYLSKAVIITTGTFLRGE 160
Cdd:COG0445   83 MLNTSKGPAVRAPRAQADRKLYRAAMRETLENQPNLDLIQGEVEDLIVEDGRVTGVVTADGIEFRAKAVVLTTGTFLNGL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526 161 IILGNMKYSSGPNHQLPSITLSDNLRELGFEIVRFKTGTPPRVNSKTIDYSKTEIQPGDDVGRAFSFETTEYILDQLPCW 240
Cdd:COG0445  163 IHIGEKSYPGGRAGEPPSVGLSESLRELGFELGRLKTGTPPRIDGRSIDFSKLEEQPGDEPPPPFSFLTEKIHPPQIPCW 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526 241 LTYTNAETHKVIDDNLHLSAMYSGMIKGTGPRYCPSIEDKFVRFNDKPRHQLFLEPEGRNTNEVYVQGLSTSLPEHVQRQ 320
Cdd:COG0445  243 ITYTNEETHEIIRENLHRSPMYSGVIEGVGPRYCPSIEDKIVRFADKDRHQIFLEPEGLDTNEVYPNGISTSLPEDVQLA 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526 321 MLETIPGLEKADMMRAGYAIEYDAIVPTQLWPTLETKMIKNLYTAGQINGTSGYEEAAGQGLMAGINAAGKVLNTGEKIL 400
Cdd:COG0445  323 MLRSIPGLENAEILRPGYAIEYDYVDPTQLKPTLETKKIEGLFFAGQINGTTGYEEAAAQGLMAGINAALKAQGKEPFIL 402

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526 401 SRSDAYIGVLIDDLVTKGTNEPYRLLTSRAEYRLLLRHDNADLRLTDMGYELGMISEERYARFNEKRQQIDAEIKRLSDI 480
Cdd:COG0445  403 DRSEAYIGVLIDDLVTKGTDEPYRMFTSRAEYRLLLRQDNADLRLTEKGYELGLVSDERYERFEEKKEAIEEEIERLKST 482

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526 481 RIKPNEHTQAIIEQHGGSRLKDGILAIDLLRRPEMTYDIILEILEEEHQLNADVEEQVEIQTKYEGYINKSLQQVEKVKR 560
Cdd:COG0445  483 RVTPNEEVNEGLEELGSSPLKRGVSLFDLLRRPEITYEDLAELDPELPDLDPEVAEQVEIEIKYEGYIERQEEEIEKLKR 562

                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616684526 561 MEEKKIPEDLDYSKIDSLATEAREKLSEVKPLNIAQASRISGVNPADISILLIYLEQGKLQRVS 624
Cdd:COG0445  563 LENLKIPEDFDYDAIPGLSNEAREKLKKIRPETLGQASRISGVTPADISLLLVYLKRRRRRKKA 626
gidA TIGR00136
glucose-inhibited division protein A; GidA, the longer of two forms of GidA-related proteins, ...
 5-619 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: 1017.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526    5 YDVIVIGAGHAGVEAGLASARRGAKTLMLTINLDNIAFMPCNPSVGGPAKGIVVREIDALGGQMAKTIDKTHIQMRMLNT 84
Cdd:TIGR00136   1 FDVIVIGGGHAGCEAALAAARLGAKTLLLTLNLDTIGKCSCNPAIGGPAKGILVKEIDALGGEMGKAADKTGLQFRVLNS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526   85 GKGPAVRALRAQADKVLYQQEMKRVIEDEENLHIMQGMVDELIIEDN-EVKGVRTNIGTEYLSKAVIITTGTFLRGEIIL 163
Cdd:TIGR00136  81 SKGPAVRATRAQIDKILYQKWMRNQLENQPNLSLFQGEVEDLILEDNdEIKGVVTKDGNEFRAKAVIITTGTFLRGKIHI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526  164 GNMKYSSGPNHQLPSITLSDNLRELGFEIVRFKTGTPPRVNSKTIDYSKTEIQPGDDVGRAFSFETTEYILDQLPCWLTY 243
Cdd:TIGR00136 161 GDKSYEAGRAGEQASYGLSTTLRELGFKTGRLKTGTPPRIDKRSIDFSKLEVQFGDTQPPAFSFTNKNFLPQQLPCYLTH 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526  244 TNAETHKVIDDNLHLSAMYSGMIKGTGPRYCPSIEDKFVRFNDKPRHQLFLEPEGRNTNEVYVQGLSTSLPEHVQRQMLE 323
Cdd:TIGR00136 241 TNPKTHQIIRDNLHRSPMYSGSIEGNGPRYCPSIEDKVVRFADKERHQIFLEPEGLNSDEIYLNGLSTSLPEDVQLKIIR 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526  324 TIPGLEKADMMRAGYAIEYDAIVPTQLWPTLETKMIKNLYTAGQINGTSGYEEAAGQGLMAGINAAGKVLNTGEKILSRS 403
Cdd:TIGR00136 321 SIPGLENAEILRPGYAIEYDYFDPTQLKPTLETKLIKGLFFAGQINGTTGYEEAAAQGLMAGINAALKLQNKEPFILKRN 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526  404 DAYIGVLIDDLVTKGTNEPYRLLTSRAEYRLLLRHDNADLRLTDMGYELGMISEERYARFNEKRQQIDAEIKRLSDIRIK 483
Cdd:TIGR00136 401 EAYIGVLIDDLVTKGTKEPYRMFTSRAEYRLLLREDNADFRLTEIGRELGLIDEDRYARFLKKKQNIEEEIERLKSTRLS 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526  484 PNEHTQAIIEQHGGSRLKDGILAIDLLRRPEMTYDIILEILEEEHQLNADVEEQVEIQTKYEGYINKSLQQVEKVKRMEE 563
Cdd:TIGR00136 481 PSKEVKEELKNLAQSPLKDEVSGYDLLKRPEMNLDKLTKLLPFLPPLDEEVLEQVEIEIKYEGYIKKQQQYIKKLDRLEN 560

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 616684526  564 KKIPEDLDYSKIDSLATEAREKLSEVKPLNIAQASRISGVNPADISILLIYLEQGK 619
Cdd:TIGR00136 561 VKIPADFDYRKIPGLSTEAREKLSKFRPLSLGQASRISGINPADISALLVYLKKQK 616
GIDA pfam01134
Glucose inhibited division protein A;
6-394 0e+00

Glucose inhibited division protein A;


Pssm-ID: 250388 [Multi-domain]  Cd Length: 391  Bit Score: 680.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526    6 DVIVIGAGHAGVEAGLASARRGAKTLMLTINLDNIAFMPCNPSVGGPAKGIVVREIDALGGQMAKTIDKTHIQMRMLNTG 85
Cdd:pfam01134   1 DVIVIGGGHAGCEAALAAARMGAKVLLITHNTDTIAELSCNPSIGGIAKGHLVREIDALGGLMGKAADKTGIQFRMLNTS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526   86 KGPAVRALRAQADKVLYQQEMKRVIEDEENLHIMQGMVDELIIEDNEVKGVRTNIGTEYLSKAVIITTGTFLRGEIILGN 165
Cdd:pfam01134  81 KGPAVRALRAQVDRDLYSKEMTETLENHPNLTLIQGEVTDLIPENGKVKGVVTEDGEEYKAKAVVLATGTFLNGKIHIGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526  166 MKYSSGPNHQLPSITLSDNLRELGFEIVRFKTGTPPRVNSKTIDYSKTEIQPGDDVGRAFSFETTEYILDQLPCWLTYTN 245
Cdd:pfam01134 161 KCYPAGRLGELTSEGLSESLKELGFELGRFKTGTPPRIDKDSIDFSKLEEQPGDKPGPPFSYLNCPMNKEQYPCFLTYTN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526  246 AETHKVIDDNLHLSAMYSGMIKGTGPRYCPSIEDKFVRFNDKPRHQLFLEPEGRNTNEVYVQGLSTSLPEHVQRQMLETI 325
Cdd:pfam01134 241 EATHEIIRDNLHRSPMFEGCIEGIGPRYCPSIEDKPVRFADKPYHQVFLEPEGLDTDEYYLVGFSTSLPEDVQKRVLRTI 320

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616684526  326 PGLEKADMMRAGYAIEYDAIVPTQLWPTLETKMIKNLYTAGQINGTSGYEEAAGQGLMAGINAAGKVLN 394
Cdd:pfam01134 321 PGLENAEIVRPGYAIEYDYIDPPQLLPTLETKKIPGLFFAGQINGTEGYEEAAAQGLLAGINAARKALG 389
PRK05335 PRK05335
tRNA (uracil-5-)-methyltransferase Gid; Reviewed
 7-411 2.71e-15

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


Pssm-ID: 235416  Cd Length: 436  Bit Score: 78.26  E-value: 2.71e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526   7 VIVIGAGHAGVEAGLASARRGAK-TL--MLTI------NLDNIAFMPCNPSVGGP----AKGIVVREIDALGGQMAKTID 73
Cdd:PRK05335   5 VNVIGAGLAGSEAAWQLAKRGVPvELyeMRPVkktpahHTDGFAELVCSNSFRSDsltnAVGLLKEEMRRLGSLIMEAAD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526  74 KTHIqmrmlntgkgPAVRALraqA-DKVLYQQEMKRVIEDEENLHIMQGMVDElIIEDNevkgvrtnigteylskaVIIT 152
Cdd:PRK05335  85 AHRV----------PAGGAL---AvDREGFSEYVTEALENHPLITVIREEVTE-IPEDI-----------------TIIA 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526 153 TGtflrgeiilgnmkyssgPnhqLPSITLSDNLREL-GFEIVRFKTGTPPRVNSKTIDYSKTEIQPGDDVGRAfsfette 231
Cdd:PRK05335 134 TG-----------------P---LTSDALAEAIKALtGEDYLYFFDAAAPIVDKDSIDMDKVYLASRYDKGEA------- 186

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526 232 yilDQLPCWLT---Y-------TNAETH--KVIDDNLHLSAmysgmikgtgpryCPSIE------DKFVRFndKPrhqlf 293
Cdd:PRK05335 187 ---DYLNCPMTkeeYeafyealIAAEKAelKDFEKEKYFEG-------------CMPIEvmaergRETLRF--GP----- 243

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526 294 LEPEG----RNTNEVY--VQ--------------GLSTSL--PEhvQRQMLETIPGLEKADMMRAGyaieydaiV----- 346
Cdd:PRK05335 244 MKPVGltdpRTGKRPYavVQlrqdnaagtlynivGFQTKLkwGE--QKRVFRMIPGLENAEFVRYG--------Vmhrnt 313

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616684526 347 ----PTQLWPTLETKMIKNLYTAGQINGTSGYEEAAGQGLMAGINAAGKVLNTGEKILSRSDAyIGVLI 411
Cdd:PRK05335 314 finsPKLLDPTLQLKKRPNLFFAGQITGVEGYVESAASGLLAGINAARLALGKEPVIPPPTTA-LGALL 381
 
Name Accession Description Interval E-value
MnmG COG0445
tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal ...
 1-624 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: 1205.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526   1 MVQEYDVIVIGAGHAGVEAGLASARRGAKTLMLTINLDNIAFMPCNPSVGGPAKGIVVREIDALGGQMAKTIDKTHIQMR 80
Cdd:COG0445    3 YPKEYDVIVVGGGHAGCEAALAAARMGAKTLLLTHNLDTIGQMSCNPAIGGIAKGHLVREIDALGGEMGRAADKTGIQFR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526  81 MLNTGKGPAVRALRAQADKVLYQQEMKRVIEDEENLHIMQGMVDELIIEDNEVKGVRTNIGTEYLSKAVIITTGTFLRGE 160
Cdd:COG0445   83 MLNTSKGPAVRAPRAQADRKLYRAAMRETLENQPNLDLIQGEVEDLIVEDGRVTGVVTADGIEFRAKAVVLTTGTFLNGL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526 161 IILGNMKYSSGPNHQLPSITLSDNLRELGFEIVRFKTGTPPRVNSKTIDYSKTEIQPGDDVGRAFSFETTEYILDQLPCW 240
Cdd:COG0445  163 IHIGEKSYPGGRAGEPPSVGLSESLRELGFELGRLKTGTPPRIDGRSIDFSKLEEQPGDEPPPPFSFLTEKIHPPQIPCW 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526 241 LTYTNAETHKVIDDNLHLSAMYSGMIKGTGPRYCPSIEDKFVRFNDKPRHQLFLEPEGRNTNEVYVQGLSTSLPEHVQRQ 320
Cdd:COG0445  243 ITYTNEETHEIIRENLHRSPMYSGVIEGVGPRYCPSIEDKIVRFADKDRHQIFLEPEGLDTNEVYPNGISTSLPEDVQLA 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526 321 MLETIPGLEKADMMRAGYAIEYDAIVPTQLWPTLETKMIKNLYTAGQINGTSGYEEAAGQGLMAGINAAGKVLNTGEKIL 400
Cdd:COG0445  323 MLRSIPGLENAEILRPGYAIEYDYVDPTQLKPTLETKKIEGLFFAGQINGTTGYEEAAAQGLMAGINAALKAQGKEPFIL 402

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526 401 SRSDAYIGVLIDDLVTKGTNEPYRLLTSRAEYRLLLRHDNADLRLTDMGYELGMISEERYARFNEKRQQIDAEIKRLSDI 480
Cdd:COG0445  403 DRSEAYIGVLIDDLVTKGTDEPYRMFTSRAEYRLLLRQDNADLRLTEKGYELGLVSDERYERFEEKKEAIEEEIERLKST 482

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526 481 RIKPNEHTQAIIEQHGGSRLKDGILAIDLLRRPEMTYDIILEILEEEHQLNADVEEQVEIQTKYEGYINKSLQQVEKVKR 560
Cdd:COG0445  483 RVTPNEEVNEGLEELGSSPLKRGVSLFDLLRRPEITYEDLAELDPELPDLDPEVAEQVEIEIKYEGYIERQEEEIEKLKR 562

                        570       580       590       600       610       620
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616684526 561 MEEKKIPEDLDYSKIDSLATEAREKLSEVKPLNIAQASRISGVNPADISILLIYLEQGKLQRVS 624
Cdd:COG0445  563 LENLKIPEDFDYDAIPGLSNEAREKLKKIRPETLGQASRISGVTPADISLLLVYLKRRRRRKKA 626
gidA TIGR00136
glucose-inhibited division protein A; GidA, the longer of two forms of GidA-related proteins, ...
 5-619 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: 1017.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526    5 YDVIVIGAGHAGVEAGLASARRGAKTLMLTINLDNIAFMPCNPSVGGPAKGIVVREIDALGGQMAKTIDKTHIQMRMLNT 84
Cdd:TIGR00136   1 FDVIVIGGGHAGCEAALAAARLGAKTLLLTLNLDTIGKCSCNPAIGGPAKGILVKEIDALGGEMGKAADKTGLQFRVLNS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526   85 GKGPAVRALRAQADKVLYQQEMKRVIEDEENLHIMQGMVDELIIEDN-EVKGVRTNIGTEYLSKAVIITTGTFLRGEIIL 163
Cdd:TIGR00136  81 SKGPAVRATRAQIDKILYQKWMRNQLENQPNLSLFQGEVEDLILEDNdEIKGVVTKDGNEFRAKAVIITTGTFLRGKIHI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526  164 GNMKYSSGPNHQLPSITLSDNLRELGFEIVRFKTGTPPRVNSKTIDYSKTEIQPGDDVGRAFSFETTEYILDQLPCWLTY 243
Cdd:TIGR00136 161 GDKSYEAGRAGEQASYGLSTTLRELGFKTGRLKTGTPPRIDKRSIDFSKLEVQFGDTQPPAFSFTNKNFLPQQLPCYLTH 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526  244 TNAETHKVIDDNLHLSAMYSGMIKGTGPRYCPSIEDKFVRFNDKPRHQLFLEPEGRNTNEVYVQGLSTSLPEHVQRQMLE 323
Cdd:TIGR00136 241 TNPKTHQIIRDNLHRSPMYSGSIEGNGPRYCPSIEDKVVRFADKERHQIFLEPEGLNSDEIYLNGLSTSLPEDVQLKIIR 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526  324 TIPGLEKADMMRAGYAIEYDAIVPTQLWPTLETKMIKNLYTAGQINGTSGYEEAAGQGLMAGINAAGKVLNTGEKILSRS 403
Cdd:TIGR00136 321 SIPGLENAEILRPGYAIEYDYFDPTQLKPTLETKLIKGLFFAGQINGTTGYEEAAAQGLMAGINAALKLQNKEPFILKRN 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526  404 DAYIGVLIDDLVTKGTNEPYRLLTSRAEYRLLLRHDNADLRLTDMGYELGMISEERYARFNEKRQQIDAEIKRLSDIRIK 483
Cdd:TIGR00136 401 EAYIGVLIDDLVTKGTKEPYRMFTSRAEYRLLLREDNADFRLTEIGRELGLIDEDRYARFLKKKQNIEEEIERLKSTRLS 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526  484 PNEHTQAIIEQHGGSRLKDGILAIDLLRRPEMTYDIILEILEEEHQLNADVEEQVEIQTKYEGYINKSLQQVEKVKRMEE 563
Cdd:TIGR00136 481 PSKEVKEELKNLAQSPLKDEVSGYDLLKRPEMNLDKLTKLLPFLPPLDEEVLEQVEIEIKYEGYIKKQQQYIKKLDRLEN 560

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 616684526  564 KKIPEDLDYSKIDSLATEAREKLSEVKPLNIAQASRISGVNPADISILLIYLEQGK 619
Cdd:TIGR00136 561 VKIPADFDYRKIPGLSTEAREKLSKFRPLSLGQASRISGINPADISALLVYLKKQK 616
GIDA pfam01134
Glucose inhibited division protein A;
6-394 0e+00

Glucose inhibited division protein A;


Pssm-ID: 250388 [Multi-domain]  Cd Length: 391  Bit Score: 680.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526    6 DVIVIGAGHAGVEAGLASARRGAKTLMLTINLDNIAFMPCNPSVGGPAKGIVVREIDALGGQMAKTIDKTHIQMRMLNTG 85
Cdd:pfam01134   1 DVIVIGGGHAGCEAALAAARMGAKVLLITHNTDTIAELSCNPSIGGIAKGHLVREIDALGGLMGKAADKTGIQFRMLNTS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526   86 KGPAVRALRAQADKVLYQQEMKRVIEDEENLHIMQGMVDELIIEDNEVKGVRTNIGTEYLSKAVIITTGTFLRGEIILGN 165
Cdd:pfam01134  81 KGPAVRALRAQVDRDLYSKEMTETLENHPNLTLIQGEVTDLIPENGKVKGVVTEDGEEYKAKAVVLATGTFLNGKIHIGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526  166 MKYSSGPNHQLPSITLSDNLRELGFEIVRFKTGTPPRVNSKTIDYSKTEIQPGDDVGRAFSFETTEYILDQLPCWLTYTN 245
Cdd:pfam01134 161 KCYPAGRLGELTSEGLSESLKELGFELGRFKTGTPPRIDKDSIDFSKLEEQPGDKPGPPFSYLNCPMNKEQYPCFLTYTN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526  246 AETHKVIDDNLHLSAMYSGMIKGTGPRYCPSIEDKFVRFNDKPRHQLFLEPEGRNTNEVYVQGLSTSLPEHVQRQMLETI 325
Cdd:pfam01134 241 EATHEIIRDNLHRSPMFEGCIEGIGPRYCPSIEDKPVRFADKPYHQVFLEPEGLDTDEYYLVGFSTSLPEDVQKRVLRTI 320

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616684526  326 PGLEKADMMRAGYAIEYDAIVPTQLWPTLETKMIKNLYTAGQINGTSGYEEAAGQGLMAGINAAGKVLN 394
Cdd:pfam01134 321 PGLENAEIVRPGYAIEYDYIDPPQLLPTLETKKIPGLFFAGQINGTEGYEEAAAQGLLAGINAARKALG 389
GIDA_C pfam13932
tRNA modifying enzyme MnmG/GidA C-terminal domain; The GidA associated domain is a domain that ...
 399-612 6.26e-126

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: 370.17  E-value: 6.26e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526  399 ILSRSDAYIGVLIDDLVTKGTNEPYRLLTSRAEYRLLLRHDNADLRLTDMGYELGMISEERYARFNEKRQQIDAEIKRLS 478
Cdd:pfam13932   2 ILSRSEAYIGVLIDDLVTKGTSEPYRMFTSRAEYRLLLRQDNADLRLTEKGRELGLVSDERYERFEEKKEAIEEEIERLK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526  479 DIRIKPNEHTQAIIEqHGGSRLKDGILAIDLLRRPEMTYDIILEILEEEHQLNADVEEQVEIQTKYEGYINKSLQQVEKV 558
Cdd:pfam13932  82 STRLSPSEWNNALLE-LGSAPLGTGRSAFDLLRRPEVTYEDLAALIPELAPLDPEVLEQVEIEAKYEGYIERQEAEIEKF 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 616684526  559 KRMEEKKIPEDLDYSKIDSLATEAREKLSEVKPLNIAQASRISGVNPADISILL 612
Cdd:pfam13932 161 KRLENLKIPEDLDYDAIPGLSNEAREKLNKIRPETIGQASRISGVTPADISVLL 214
PRK05335 PRK05335
tRNA (uracil-5-)-methyltransferase Gid; Reviewed
 7-411 2.71e-15

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


Pssm-ID: 235416  Cd Length: 436  Bit Score: 78.26  E-value: 2.71e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526   7 VIVIGAGHAGVEAGLASARRGAK-TL--MLTI------NLDNIAFMPCNPSVGGP----AKGIVVREIDALGGQMAKTID 73
Cdd:PRK05335   5 VNVIGAGLAGSEAAWQLAKRGVPvELyeMRPVkktpahHTDGFAELVCSNSFRSDsltnAVGLLKEEMRRLGSLIMEAAD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526  74 KTHIqmrmlntgkgPAVRALraqA-DKVLYQQEMKRVIEDEENLHIMQGMVDElIIEDNevkgvrtnigteylskaVIIT 152
Cdd:PRK05335  85 AHRV----------PAGGAL---AvDREGFSEYVTEALENHPLITVIREEVTE-IPEDI-----------------TIIA 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526 153 TGtflrgeiilgnmkyssgPnhqLPSITLSDNLREL-GFEIVRFKTGTPPRVNSKTIDYSKTEIQPGDDVGRAfsfette 231
Cdd:PRK05335 134 TG-----------------P---LTSDALAEAIKALtGEDYLYFFDAAAPIVDKDSIDMDKVYLASRYDKGEA------- 186

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526 232 yilDQLPCWLT---Y-------TNAETH--KVIDDNLHLSAmysgmikgtgpryCPSIE------DKFVRFndKPrhqlf 293
Cdd:PRK05335 187 ---DYLNCPMTkeeYeafyealIAAEKAelKDFEKEKYFEG-------------CMPIEvmaergRETLRF--GP----- 243

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526 294 LEPEG----RNTNEVY--VQ--------------GLSTSL--PEhvQRQMLETIPGLEKADMMRAGyaieydaiV----- 346
Cdd:PRK05335 244 MKPVGltdpRTGKRPYavVQlrqdnaagtlynivGFQTKLkwGE--QKRVFRMIPGLENAEFVRYG--------Vmhrnt 313

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616684526 347 ----PTQLWPTLETKMIKNLYTAGQINGTSGYEEAAGQGLMAGINAAGKVLNTGEKILSRSDAyIGVLI 411
Cdd:PRK05335 314 finsPKLLDPTLQLKKRPNLFFAGQITGVEGYVESAASGLLAGINAARLALGKEPVIPPPTTA-LGALL 381
TrmFO COG1206
Folate-dependent tRNA-U54 methylase TrmFO/GidA [Translation, ribosomal structure and ...
 318-394 8.55e-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: 8.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526 318 QRQMLETIPGLEKADMMRAGyaieydaiV---------PTQLWPTLETKMIKNLYTAGQINGTSGYEEAAGQGLMAGINA 388
Cdd:COG1206  288 QKRVFRMIPGLENAEFVRYG--------VmhrntfinsPKLLDPTLQLKARPNLFFAGQITGVEGYVESAASGLLAGINA 359


                 ....*.
gi 616684526 389 AGKVLN 394
Cdd:COG1206  360 ARLLLG 365
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
5-154 1.34e-11

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 65.91  E-value: 1.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526   5 YDVIVIGAGHAGVEAGLASARRGAKTLMLtinldniafmpcnpsvggpakgivvrEIDALGGQMAKTID-------KTHI 77
Cdd:COG0492    1 YDVVIIGAGPAGLTAAIYAARAGLKTLVI--------------------------EGGEPGGQLATTKEienypgfPEGI 54

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616684526  78 QmrmlntgkGPA-VRALRAQADKVlyqqemkrviedeeNLHIMQGMVDElIIEDNEVKGVRTNIGTEYLSKAVIITTG 154
Cdd:COG0492   55 S--------GPElAERLREQAERF--------------GAEILLEEVTS-VDKDDGPFRVTTDDGTEYEAKAVIIATG 109
GG-red-SF TIGR02032
geranylgeranyl reductase family; This model represents a subfamily which includes ...
 5-154 1.02e-05

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: 47.70  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526    5 YDVIVIGAGHAGVEAGLASARRGAKTLMLTINlDNIAFMPCnpsvGGPAKGIVVREIDALGGQMAKTIDKTHIQM---RM 81
Cdd:TIGR02032   1 YDVVVVGAGPAGASAAYRLADKGLRVLLLEKK-SFPRYKPC----GGALSPRALEELDLPGELIVNLVRGARFFSpngDS 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616684526   82 LN----TGKGPAVRalRAQADKVLYQQEMKRVIEDEENLHImqgmVDELIIEDNEVKGVRTNIGTeYLSKAVIITTG 154
Cdd:TIGR02032  76 VEipieTELAYVID--RDAFDEQLAERAQEAGAELRLGTRV----LDVEIHDDRVVVIVRGSEGT-VTAKIVIGADG 145
FAD_oxidored pfam12831
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ...
 6-154 5.16e-05

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


Pssm-ID: 432816 [Multi-domain]  Cd Length: 420  Bit Score: 46.06  E-value: 5.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526    6 DVIVIGAGHAGVEAGLASARRGAKTL----------MLTINLDNiAFMPCNPSVGGPAKGI---VVREIDALGGQMAKTI 72
Cdd:pfam12831   1 DVVVVGGGPAGVAAAIAAARAGAKVLlverrgflggMLTSGLVG-PDMGFYLNKEQVVGGIareFRQRLRARGGLPGPYG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526   73 DKTHIQMRmlntgkGPAVralraqadkvlyqqeMKRVIED---EENLHIMQG-MVDELIIEDNEVKGVRTNI---GTEYL 145
Cdd:pfam12831  80 LRGGWVPF------DPEV---------------AKAVLDEmlaEAGVTVLLHtRVVGVVKEGGRITGVTVETkggRITIR 138


                  ....*....
gi 616684526  146 SKAVIITTG 154
Cdd:pfam12831 139 AKVFIDATG 147
PRK05329 PRK05329
glycerol-3-phosphate dehydrogenase subunit GlpB;
4-34 1.37e-04

glycerol-3-phosphate dehydrogenase subunit GlpB;


Pssm-ID: 235412  Cd Length: 422  Bit Score: 44.84  E-value: 1.37e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 616684526   4 EYDVIVIGAGHAGVEAGLASARRGAKTLMLT 34
Cdd:PRK05329   2 KFDVLVIGGGLAGLTAALAAAEAGKRVALVA 32
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
 4-154 1.84e-04

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


Pssm-ID: 440673 [Multi-domain]  Cd Length: 443  Bit Score: 44.44  E-value: 1.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526   4 EYDVIVIGAGHAGVEAGLASARRGAKTLMLT---------------INL-----------DNIAFM----------PCNP 47
Cdd:COG1053    3 EYDVVVVGSGGAGLRAALEAAEAGLKVLVLEkvpprgghtaaaqggINAagtnvqkaageDSPEEHfydtvkggdgLADQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526  48 SV------GGPAkgiVVREIDALGGQMAKTIDKTHIQM------RMLNTGK--GPA-VRALRAQADKvlyqqemkrvied 112
Cdd:COG1053   83 DLvealaeEAPE---AIDWLEAQGVPFSRTPDGRLPQFgghsvgRTCYAGDgtGHAlLATLYQAALR------------- 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 616684526 113 eENLHIMQG-MVDELIIEDNEVKGVRTNIGT----EYLSKAVIITTG 154
Cdd:COG1053  147 -LGVEIFTEtEVLDLIVDDGRVVGVVARDRTgeivRIRAKAVVLATG 192
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 5-154 2.07e-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: 43.85  E-value: 2.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526    5 YDVIVIGAGHAGVEAGLASARRGAKTLMLTINlDNIAFMPCNPSVGGPAKGIvVREIDALGGQMAKTIDKtHIQMRMLNT 84
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDE-GTCPYGGCVLSKALLGAAE-APEIASLWADLYKRKEE-VVKKLNNGI 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526   85 gkgpavralraqadKVLYQQEMKRVIEDEENLHimqgmvdeliiedneVKGVRTNIGTEYLSKAVIITTG 154
Cdd:pfam07992  78 --------------EVLLGTEVVSIDPGAKKVV---------------LEELVDGDGETITYDRLVIATG 118
PRK07843 PRK07843
3-oxosteroid 1-dehydrogenase;
1-33 2.65e-04

3-oxosteroid 1-dehydrogenase;


Pssm-ID: 236111 [Multi-domain]  Cd Length: 557  Bit Score: 43.87  E-value: 2.65e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 616684526   1 MVQEYDVIVIGAGHAGVEAGLASARRGAKTLML 33
Cdd:PRK07843   4 TVQEYDVVVVGSGAAGMVAALTAAHRGLSTVVV 36
PRK08274 PRK08274
FAD-dependent tricarballylate dehydrogenase TcuA;
1-33 3.59e-04

FAD-dependent tricarballylate dehydrogenase TcuA;


Pssm-ID: 236214 [Multi-domain]  Cd Length: 466  Bit Score: 43.33  E-value: 3.59e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 616684526   1 MVQEYDVIVIGAGHAGVEAGLASARRGAKTLML 33
Cdd:PRK08274   1 MASMVDVLVIGGGNAALCAALAAREAGASVLLL 33
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 3-32 5.47e-04

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


Pssm-ID: 440861 [Multi-domain]  Cd Length: 456  Bit Score: 42.77  E-value: 5.47e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 616684526   3 QEYDVIVIGAGHAGVEAGLASARRGAKTLM 32
Cdd:COG1249    2 KDYDLVVIGAGPGGYVAAIRAAQLGLKVAL 31
GlpB COG3075
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];
4-30 6.41e-04

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


Pssm-ID: 442309  Cd Length: 415  Bit Score: 42.47  E-value: 6.41e-04
                         10        20
                 ....*....|....*....|....*..
gi 616684526   4 EYDVIVIGAGHAGVEAGLASARRGAKT 30
Cdd:COG3075    2 KFDVVVIGGGLAGLTAAIRAAEAGLRV 28
sdhA PRK07803
succinate dehydrogenase flavoprotein subunit; Reviewed
 2-37 7.01e-04

succinate dehydrogenase flavoprotein subunit; Reviewed


Pssm-ID: 236101 [Multi-domain]  Cd Length: 626  Bit Score: 42.72  E-value: 7.01e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 616684526   2 VQEYDVIVIGAGHAGVEAGLASARRGAKTLMLTINL 37
Cdd:PRK07803   6 RHSYDVVVIGAGGAGLRAAIEARERGLRVAVVCKSL 41
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 3-33 2.06e-03

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 40.99  E-value: 2.06e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 616684526   3 QEYDVIVIGAGHAGVEAGLASARRGAKTLML 33
Cdd:COG1233    2 MMYDVVVIGAGIGGLAAAALLARAGYRVTVL 32
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
 6-34 3.02e-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: 40.35  E-value: 3.02e-03
                          10        20
                  ....*....|....*....|....*....
gi 616684526    6 DVIVIGAGHAGVEAGLASARRGAKTLMLT 34
Cdd:pfam00890   1 DVLVIGGGLAGLAAALAAAEAGLKVAVVE 29
solA PRK11259
N-methyl-L-tryptophan oxidase;
3-33 4.45e-03

N-methyl-L-tryptophan oxidase;


Pssm-ID: 236887 [Multi-domain]  Cd Length: 376  Bit Score: 39.82  E-value: 4.45e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 616684526   3 QEYDVIVIGAGHAGVEAGLASARRGAKTLML 33
Cdd:PRK11259   2 MRYDVIVIGLGSMGSAAGYYLARRGLRVLGL 32
PRK12843 PRK12843
FAD-dependent oxidoreductase;
4-33 4.80e-03

FAD-dependent oxidoreductase;


Pssm-ID: 237225 [Multi-domain]  Cd Length: 578  Bit Score: 40.10  E-value: 4.80e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 616684526   4 EYDVIVIGAGHAGVEAGLASARRGAKTLML 33
Cdd:PRK12843  16 EFDVIVIGAGAAGMSAALFAAIAGLKVLLV 45
PRK07121 PRK07121
FAD-binding protein;
4-33 4.88e-03

FAD-binding protein;


Pssm-ID: 180854 [Multi-domain]  Cd Length: 492  Bit Score: 39.87  E-value: 4.88e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 616684526   4 EYDVIVIGAGHAGVEAGLASARRGAKTLML 33
Cdd:PRK07121  20 EADVVVVGFGAAGACAAIEAAAAGARVLVL 49
HI0933_like pfam03486
HI0933-like protein;
5-154 5.72e-03

HI0933-like protein;


Pssm-ID: 427330 [Multi-domain]  Cd Length: 406  Bit Score: 39.49  E-value: 5.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526    5 YDVIVIGAGHAGVEAGLASARRGAKTLMLT----------------INLDNIAFMPCNPSVGGPAKGIVVRE-------- 60
Cdd:pfam03486   1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEkgkklgrkilisgggrCNVTNLSEEPDNFLSRYPGNPKFLKSalsrftpw 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616684526   61 --IDALGGQMAKTIDKTHIQMRMLNTGKGPAVRALRAQAD----KVLYQQEmkrviedeenlhimqgmVDELIIEDNEVK 134
Cdd:pfam03486  81 dfIAFFESLGVPLKEEDHGRLFPDSDKASDIVDALLNELKelgvKIRLRTR-----------------VLSVEKDDDGRF 143

                         170       180
                  ....*....|....*....|
gi 616684526  135 GVRTNiGTEYLSKAVIITTG 154
Cdd:pfam03486 144 RVKTG-GEELEADSLVLATG 162
 
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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