|
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: 1213.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 1 MVQEYDVIVIGAGHAGIEAGLASARRGAKTLMLTINLDNIAFMPCNPSVGGPAKGIVVREIDALGGQMAKTIDKTHIQMR 80
Cdd:COG0445 3 YPKEYDVIVVGGGHAGCEAALAAARMGAKTLLLTHNLDTIGQMSCNPAIGGIAKGHLVREIDALGGEMGRAADKTGIQFR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 81 MLNTGKGPAVRALRAQADKVLYQQEMKNVIEDEDNLDIMQGMVDELIIEDDEVKGVRTNIGTEYRSKAVVITTGTFLRGE 160
Cdd:COG0445 83 MLNTSKGPAVRAPRAQADRKLYRAAMRETLENQPNLDLIQGEVEDLIVEDGRVTGVVTADGIEFRAKAVVLTTGTFLNGL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 161 IILGNMKYSSGPNHQLPSVTLADNLRGLGFEVVRFKTGTPPRVNSKTIDYSKTEIQPGDDVGRAFSYETTEYILDQLPCW 240
Cdd:COG0445 163 IHIGEKSYPGGRAGEPPSVGLSESLRELGFELGRLKTGTPPRIDGRSIDFSKLEEQPGDEPPPPFSFLTEKIHPPQIPCW 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 241 LTYTNDKTHQVIDDNLHLSAMYSGMIKGTGPRYCPSIEDKFVRFNDKPRHQLFLEPEGRNTNEVYVQGLSTSLPEHVQRQ 320
Cdd:COG0445 243 ITYTNEETHEIIRENLHRSPMYSGVIEGVGPRYCPSIEDKIVRFADKDRHQIFLEPEGLDTNEVYPNGISTSLPEDVQLA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 321 MLETIPGLEKADMMRAGYAIEYDAIVPTQLWPTLETKMIKNLYTAGQINGTSGYEEAAGQGIMAGINAAGKVLGKEEKIL 400
Cdd:COG0445 323 MLRSIPGLENAEILRPGYAIEYDYVDPTQLKPTLETKKIEGLFFAGQINGTTGYEEAAAQGLMAGINAALKAQGKEPFIL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 401 SRSDAYIGVLIDDLVTKGTNEPYRLLTSRAEYRLLLRHDNADLRLTDLGHELGLISDERYAQFNHKRQQIKDEIQRLTDI 480
Cdd:COG0445 403 DRSEAYIGVLIDDLVTKGTDEPYRMFTSRAEYRLLLRQDNADLRLTEKGYELGLVSDERYERFEEKKEAIEEEIERLKST 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 481 RIKPNDHTQSVIEANGGSKLKDGILAIDLLRRPEMTYDTILEILEEDHQLPSEVEEQVEIQTKYEGYINKSLQQVEKVKR 560
Cdd:COG0445 483 RVTPNEEVNEGLEELGSSPLKRGVSLFDLLRRPEITYEDLAELDPELPDLDPEVAEQVEIEIKYEGYIERQEEEIEKLKR 562
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1325404581 561 MEQKKIPEDLDYSKVDSLASEAREKLAEVKPLNIAQASRISGVNPADISILLVYLEQGKLQRVN 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: 1030.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 5 YDVIVIGAGHAGIEAGLASARRGAKTLMLTINLDNIAFMPCNPSVGGPAKGIVVREIDALGGQMAKTIDKTHIQMRMLNT 84
Cdd:TIGR00136 1 FDVIVIGGGHAGCEAALAAARLGAKTLLLTLNLDTIGKCSCNPAIGGPAKGILVKEIDALGGEMGKAADKTGLQFRVLNS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 85 GKGPAVRALRAQADKVLYQQEMKNVIEDEDNLDIMQGMVDELIIED-DEVKGVRTNIGTEYRSKAVVITTGTFLRGEIIL 163
Cdd:TIGR00136 81 SKGPAVRATRAQIDKILYQKWMRNQLENQPNLSLFQGEVEDLILEDnDEIKGVVTKDGNEFRAKAVIITTGTFLRGKIHI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 164 GNMKYSSGPNHQLPSVTLADNLRGLGFEVVRFKTGTPPRVNSKTIDYSKTEIQPGDDVGRAFSYETTEYILDQLPCWLTY 243
Cdd:TIGR00136 161 GDKSYEAGRAGEQASYGLSTTLRELGFKTGRLKTGTPPRIDKRSIDFSKLEVQFGDTQPPAFSFTNKNFLPQQLPCYLTH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 244 TNDKTHQVIDDNLHLSAMYSGMIKGTGPRYCPSIEDKFVRFNDKPRHQLFLEPEGRNTNEVYVQGLSTSLPEHVQRQMLE 323
Cdd:TIGR00136 241 TNPKTHQIIRDNLHRSPMYSGSIEGNGPRYCPSIEDKVVRFADKERHQIFLEPEGLNSDEIYLNGLSTSLPEDVQLKIIR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 324 TIPGLEKADMMRAGYAIEYDAIVPTQLWPTLETKMIKNLYTAGQINGTSGYEEAAGQGIMAGINAAGKVLGKEEKILSRS 403
Cdd:TIGR00136 321 SIPGLENAEILRPGYAIEYDYFDPTQLKPTLETKLIKGLFFAGQINGTTGYEEAAAQGLMAGINAALKLQNKEPFILKRN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 404 DAYIGVLIDDLVTKGTNEPYRLLTSRAEYRLLLRHDNADLRLTDLGHELGLISDERYAQFNHKRQQIKDEIQRLTDIRIK 483
Cdd:TIGR00136 401 EAYIGVLIDDLVTKGTKEPYRMFTSRAEYRLLLREDNADFRLTEIGRELGLIDEDRYARFLKKKQNIEEEIERLKSTRLS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 484 PNDHTQSVIEANGGSKLKDGILAIDLLRRPEMTYDTILEILEEDHQLPSEVEEQVEIQTKYEGYINKSLQQVEKVKRMEQ 563
Cdd:TIGR00136 481 PSKEVKEELKNLAQSPLKDEVSGYDLLKRPEMNLDKLTKLLPFLPPLDEEVLEQVEIEIKYEGYIKKQQQYIKKLDRLEN 560
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1325404581 564 KKIPEDLDYSKVDSLASEAREKLAEVKPLNIAQASRISGVNPADISILLVYLEQGK 619
Cdd:TIGR00136 561 VKIPADFDYRKIPGLSTEAREKLSKFRPLSLGQASRISGINPADISALLVYLKKQK 616
|
|
| GIDA |
pfam01134 |
Glucose inhibited division protein A; |
6-396 |
0e+00 |
|
Glucose inhibited division protein A;
Pssm-ID: 250388 [Multi-domain] Cd Length: 391 Bit Score: 683.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 6 DVIVIGAGHAGIEAGLASARRGAKTLMLTINLDNIAFMPCNPSVGGPAKGIVVREIDALGGQMAKTIDKTHIQMRMLNTG 85
Cdd:pfam01134 1 DVIVIGGGHAGCEAALAAARMGAKVLLITHNTDTIAELSCNPSIGGIAKGHLVREIDALGGLMGKAADKTGIQFRMLNTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 86 KGPAVRALRAQADKVLYQQEMKNVIEDEDNLDIMQGMVDELIIEDDEVKGVRTNIGTEYRSKAVVITTGTFLRGEIILGN 165
Cdd:pfam01134 81 KGPAVRALRAQVDRDLYSKEMTETLENHPNLTLIQGEVTDLIPENGKVKGVVTEDGEEYKAKAVVLATGTFLNGKIHIGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 166 MKYSSGPNHQLPSVTLADNLRGLGFEVVRFKTGTPPRVNSKTIDYSKTEIQPGDDVGRAFSYETTEYILDQLPCWLTYTN 245
Cdd:pfam01134 161 KCYPAGRLGELTSEGLSESLKELGFELGRFKTGTPPRIDKDSIDFSKLEEQPGDKPGPPFSYLNCPMNKEQYPCFLTYTN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 246 DKTHQVIDDNLHLSAMYSGMIKGTGPRYCPSIEDKFVRFNDKPRHQLFLEPEGRNTNEVYVQGLSTSLPEHVQRQMLETI 325
Cdd:pfam01134 241 EATHEIIRDNLHRSPMFEGCIEGIGPRYCPSIEDKPVRFADKPYHQVFLEPEGLDTDEYYLVGFSTSLPEDVQKRVLRTI 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1325404581 326 PGLEKADMMRAGYAIEYDAIVPTQLWPTLETKMIKNLYTAGQINGTSGYEEAAGQGIMAGINAAGKVLGKE 396
Cdd:pfam01134 321 PGLENAEIVRPGYAIEYDYIDPPQLLPTLETKKIPGLFFAGQINGTEGYEEAAAQGLLAGINAARKALGKE 391
|
|
| PRK05335 |
PRK05335 |
tRNA (uracil-5-)-methyltransferase Gid; Reviewed |
7-411 |
1.15e-15 |
|
tRNA (uracil-5-)-methyltransferase Gid; Reviewed
Pssm-ID: 235416 Cd Length: 436 Bit Score: 79.42 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 7 VIVIGAGHAGIEAGLASARRGAK-TL--MLTI------NLDNIAFMPCNPSVGGP----AKGIVVREIDALGGQMAKTID 73
Cdd:PRK05335 5 VNVIGAGLAGSEAAWQLAKRGVPvELyeMRPVkktpahHTDGFAELVCSNSFRSDsltnAVGLLKEEMRRLGSLIMEAAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 74 KTHIqmrmlntgkgPAVRALraqA-DKVLYQQEMKNVIEDEDNLDIMQGMVDELiieDDEVkgvrtnigteyrskaVVIT 152
Cdd:PRK05335 85 AHRV----------PAGGAL---AvDREGFSEYVTEALENHPLITVIREEVTEI---PEDI---------------TIIA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 153 TGtflrgeiilgnmkyssgPnhqLPSVTLADNLRGL-GFEVVRFKTGTPPRVNSKTIDYSKTEIQPGDDVGRAfsyette 231
Cdd:PRK05335 134 TG-----------------P---LTSDALAEAIKALtGEDYLYFFDAAAPIVDKDSIDMDKVYLASRYDKGEA------- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 232 yilDQLPCWLT---YTndkthqviddnlhlsAMYSGMIKG--------TGPRY---CPSIE------DKFVRFndKPrhq 291
Cdd:PRK05335 187 ---DYLNCPMTkeeYE---------------AFYEALIAAekaelkdfEKEKYfegCMPIEvmaergRETLRF--GP--- 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 292 lfLEPEG----RNTNEVY--VQ--------------GLSTSL--PEhvQRQMLETIPGLEKADMMRAGyaieydaiV--- 346
Cdd:PRK05335 244 --MKPVGltdpRTGKRPYavVQlrqdnaagtlynivGFQTKLkwGE--QKRVFRMIPGLENAEFVRYG--------Vmhr 311
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1325404581 347 ------PTQLWPTLETKMIKNLYTAGQINGTSGYEEAAGQGIMAGINAAGKVLGKEEKILSRSDAyIGVLI 411
Cdd:PRK05335 312 ntfinsPKLLDPTLQLKKRPNLFFAGQITGVEGYVESAASGLLAGINAARLALGKEPVIPPPTTA-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: 1213.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 1 MVQEYDVIVIGAGHAGIEAGLASARRGAKTLMLTINLDNIAFMPCNPSVGGPAKGIVVREIDALGGQMAKTIDKTHIQMR 80
Cdd:COG0445 3 YPKEYDVIVVGGGHAGCEAALAAARMGAKTLLLTHNLDTIGQMSCNPAIGGIAKGHLVREIDALGGEMGRAADKTGIQFR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 81 MLNTGKGPAVRALRAQADKVLYQQEMKNVIEDEDNLDIMQGMVDELIIEDDEVKGVRTNIGTEYRSKAVVITTGTFLRGE 160
Cdd:COG0445 83 MLNTSKGPAVRAPRAQADRKLYRAAMRETLENQPNLDLIQGEVEDLIVEDGRVTGVVTADGIEFRAKAVVLTTGTFLNGL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 161 IILGNMKYSSGPNHQLPSVTLADNLRGLGFEVVRFKTGTPPRVNSKTIDYSKTEIQPGDDVGRAFSYETTEYILDQLPCW 240
Cdd:COG0445 163 IHIGEKSYPGGRAGEPPSVGLSESLRELGFELGRLKTGTPPRIDGRSIDFSKLEEQPGDEPPPPFSFLTEKIHPPQIPCW 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 241 LTYTNDKTHQVIDDNLHLSAMYSGMIKGTGPRYCPSIEDKFVRFNDKPRHQLFLEPEGRNTNEVYVQGLSTSLPEHVQRQ 320
Cdd:COG0445 243 ITYTNEETHEIIRENLHRSPMYSGVIEGVGPRYCPSIEDKIVRFADKDRHQIFLEPEGLDTNEVYPNGISTSLPEDVQLA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 321 MLETIPGLEKADMMRAGYAIEYDAIVPTQLWPTLETKMIKNLYTAGQINGTSGYEEAAGQGIMAGINAAGKVLGKEEKIL 400
Cdd:COG0445 323 MLRSIPGLENAEILRPGYAIEYDYVDPTQLKPTLETKKIEGLFFAGQINGTTGYEEAAAQGLMAGINAALKAQGKEPFIL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 401 SRSDAYIGVLIDDLVTKGTNEPYRLLTSRAEYRLLLRHDNADLRLTDLGHELGLISDERYAQFNHKRQQIKDEIQRLTDI 480
Cdd:COG0445 403 DRSEAYIGVLIDDLVTKGTDEPYRMFTSRAEYRLLLRQDNADLRLTEKGYELGLVSDERYERFEEKKEAIEEEIERLKST 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 481 RIKPNDHTQSVIEANGGSKLKDGILAIDLLRRPEMTYDTILEILEEDHQLPSEVEEQVEIQTKYEGYINKSLQQVEKVKR 560
Cdd:COG0445 483 RVTPNEEVNEGLEELGSSPLKRGVSLFDLLRRPEITYEDLAELDPELPDLDPEVAEQVEIEIKYEGYIERQEEEIEKLKR 562
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1325404581 561 MEQKKIPEDLDYSKVDSLASEAREKLAEVKPLNIAQASRISGVNPADISILLVYLEQGKLQRVN 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: 1030.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 5 YDVIVIGAGHAGIEAGLASARRGAKTLMLTINLDNIAFMPCNPSVGGPAKGIVVREIDALGGQMAKTIDKTHIQMRMLNT 84
Cdd:TIGR00136 1 FDVIVIGGGHAGCEAALAAARLGAKTLLLTLNLDTIGKCSCNPAIGGPAKGILVKEIDALGGEMGKAADKTGLQFRVLNS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 85 GKGPAVRALRAQADKVLYQQEMKNVIEDEDNLDIMQGMVDELIIED-DEVKGVRTNIGTEYRSKAVVITTGTFLRGEIIL 163
Cdd:TIGR00136 81 SKGPAVRATRAQIDKILYQKWMRNQLENQPNLSLFQGEVEDLILEDnDEIKGVVTKDGNEFRAKAVIITTGTFLRGKIHI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 164 GNMKYSSGPNHQLPSVTLADNLRGLGFEVVRFKTGTPPRVNSKTIDYSKTEIQPGDDVGRAFSYETTEYILDQLPCWLTY 243
Cdd:TIGR00136 161 GDKSYEAGRAGEQASYGLSTTLRELGFKTGRLKTGTPPRIDKRSIDFSKLEVQFGDTQPPAFSFTNKNFLPQQLPCYLTH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 244 TNDKTHQVIDDNLHLSAMYSGMIKGTGPRYCPSIEDKFVRFNDKPRHQLFLEPEGRNTNEVYVQGLSTSLPEHVQRQMLE 323
Cdd:TIGR00136 241 TNPKTHQIIRDNLHRSPMYSGSIEGNGPRYCPSIEDKVVRFADKERHQIFLEPEGLNSDEIYLNGLSTSLPEDVQLKIIR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 324 TIPGLEKADMMRAGYAIEYDAIVPTQLWPTLETKMIKNLYTAGQINGTSGYEEAAGQGIMAGINAAGKVLGKEEKILSRS 403
Cdd:TIGR00136 321 SIPGLENAEILRPGYAIEYDYFDPTQLKPTLETKLIKGLFFAGQINGTTGYEEAAAQGLMAGINAALKLQNKEPFILKRN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 404 DAYIGVLIDDLVTKGTNEPYRLLTSRAEYRLLLRHDNADLRLTDLGHELGLISDERYAQFNHKRQQIKDEIQRLTDIRIK 483
Cdd:TIGR00136 401 EAYIGVLIDDLVTKGTKEPYRMFTSRAEYRLLLREDNADFRLTEIGRELGLIDEDRYARFLKKKQNIEEEIERLKSTRLS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 484 PNDHTQSVIEANGGSKLKDGILAIDLLRRPEMTYDTILEILEEDHQLPSEVEEQVEIQTKYEGYINKSLQQVEKVKRMEQ 563
Cdd:TIGR00136 481 PSKEVKEELKNLAQSPLKDEVSGYDLLKRPEMNLDKLTKLLPFLPPLDEEVLEQVEIEIKYEGYIKKQQQYIKKLDRLEN 560
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1325404581 564 KKIPEDLDYSKVDSLASEAREKLAEVKPLNIAQASRISGVNPADISILLVYLEQGK 619
Cdd:TIGR00136 561 VKIPADFDYRKIPGLSTEAREKLSKFRPLSLGQASRISGINPADISALLVYLKKQK 616
|
|
| GIDA |
pfam01134 |
Glucose inhibited division protein A; |
6-396 |
0e+00 |
|
Glucose inhibited division protein A;
Pssm-ID: 250388 [Multi-domain] Cd Length: 391 Bit Score: 683.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 6 DVIVIGAGHAGIEAGLASARRGAKTLMLTINLDNIAFMPCNPSVGGPAKGIVVREIDALGGQMAKTIDKTHIQMRMLNTG 85
Cdd:pfam01134 1 DVIVIGGGHAGCEAALAAARMGAKVLLITHNTDTIAELSCNPSIGGIAKGHLVREIDALGGLMGKAADKTGIQFRMLNTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 86 KGPAVRALRAQADKVLYQQEMKNVIEDEDNLDIMQGMVDELIIEDDEVKGVRTNIGTEYRSKAVVITTGTFLRGEIILGN 165
Cdd:pfam01134 81 KGPAVRALRAQVDRDLYSKEMTETLENHPNLTLIQGEVTDLIPENGKVKGVVTEDGEEYKAKAVVLATGTFLNGKIHIGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 166 MKYSSGPNHQLPSVTLADNLRGLGFEVVRFKTGTPPRVNSKTIDYSKTEIQPGDDVGRAFSYETTEYILDQLPCWLTYTN 245
Cdd:pfam01134 161 KCYPAGRLGELTSEGLSESLKELGFELGRFKTGTPPRIDKDSIDFSKLEEQPGDKPGPPFSYLNCPMNKEQYPCFLTYTN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 246 DKTHQVIDDNLHLSAMYSGMIKGTGPRYCPSIEDKFVRFNDKPRHQLFLEPEGRNTNEVYVQGLSTSLPEHVQRQMLETI 325
Cdd:pfam01134 241 EATHEIIRDNLHRSPMFEGCIEGIGPRYCPSIEDKPVRFADKPYHQVFLEPEGLDTDEYYLVGFSTSLPEDVQKRVLRTI 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1325404581 326 PGLEKADMMRAGYAIEYDAIVPTQLWPTLETKMIKNLYTAGQINGTSGYEEAAGQGIMAGINAAGKVLGKE 396
Cdd:pfam01134 321 PGLENAEIVRPGYAIEYDYIDPPQLLPTLETKKIPGLFFAGQINGTEGYEEAAAQGLLAGINAARKALGKE 391
|
|
| GIDA_C |
pfam13932 |
tRNA modifying enzyme MnmG/GidA C-terminal domain; The GidA associated domain is a domain that ... |
399-612 |
7.94e-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: 369.79 E-value: 7.94e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 399 ILSRSDAYIGVLIDDLVTKGTNEPYRLLTSRAEYRLLLRHDNADLRLTDLGHELGLISDERYAQFNHKRQQIKDEIQRLT 478
Cdd:pfam13932 2 ILSRSEAYIGVLIDDLVTKGTSEPYRMFTSRAEYRLLLRQDNADLRLTEKGRELGLVSDERYERFEEKKEAIEEEIERLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 479 DIRIKPNDHTQSVIEaNGGSKLKDGILAIDLLRRPEMTYDTILEILEEDHQLPSEVEEQVEIQTKYEGYINKSLQQVEKV 558
Cdd:pfam13932 82 STRLSPSEWNNALLE-LGSAPLGTGRSAFDLLRRPEVTYEDLAALIPELAPLDPEVLEQVEIEAKYEGYIERQEAEIEKF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1325404581 559 KRMEQKKIPEDLDYSKVDSLASEAREKLAEVKPLNIAQASRISGVNPADISILL 612
Cdd:pfam13932 161 KRLENLKIPEDLDYDAIPGLSNEAREKLNKIRPETIGQASRISGVTPADISVLL 214
|
|
| PRK05335 |
PRK05335 |
tRNA (uracil-5-)-methyltransferase Gid; Reviewed |
7-411 |
1.15e-15 |
|
tRNA (uracil-5-)-methyltransferase Gid; Reviewed
Pssm-ID: 235416 Cd Length: 436 Bit Score: 79.42 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 7 VIVIGAGHAGIEAGLASARRGAK-TL--MLTI------NLDNIAFMPCNPSVGGP----AKGIVVREIDALGGQMAKTID 73
Cdd:PRK05335 5 VNVIGAGLAGSEAAWQLAKRGVPvELyeMRPVkktpahHTDGFAELVCSNSFRSDsltnAVGLLKEEMRRLGSLIMEAAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 74 KTHIqmrmlntgkgPAVRALraqA-DKVLYQQEMKNVIEDEDNLDIMQGMVDELiieDDEVkgvrtnigteyrskaVVIT 152
Cdd:PRK05335 85 AHRV----------PAGGAL---AvDREGFSEYVTEALENHPLITVIREEVTEI---PEDI---------------TIIA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 153 TGtflrgeiilgnmkyssgPnhqLPSVTLADNLRGL-GFEVVRFKTGTPPRVNSKTIDYSKTEIQPGDDVGRAfsyette 231
Cdd:PRK05335 134 TG-----------------P---LTSDALAEAIKALtGEDYLYFFDAAAPIVDKDSIDMDKVYLASRYDKGEA------- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 232 yilDQLPCWLT---YTndkthqviddnlhlsAMYSGMIKG--------TGPRY---CPSIE------DKFVRFndKPrhq 291
Cdd:PRK05335 187 ---DYLNCPMTkeeYE---------------AFYEALIAAekaelkdfEKEKYfegCMPIEvmaergRETLRF--GP--- 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 292 lfLEPEG----RNTNEVY--VQ--------------GLSTSL--PEhvQRQMLETIPGLEKADMMRAGyaieydaiV--- 346
Cdd:PRK05335 244 --MKPVGltdpRTGKRPYavVQlrqdnaagtlynivGFQTKLkwGE--QKRVFRMIPGLENAEFVRYG--------Vmhr 311
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1325404581 347 ------PTQLWPTLETKMIKNLYTAGQINGTSGYEEAAGQGIMAGINAAGKVLGKEEKILSRSDAyIGVLI 411
Cdd:PRK05335 312 ntfinsPKLLDPTLQLKKRPNLFFAGQITGVEGYVESAASGLLAGINAARLALGKEPVIPPPTTA-LGALL 381
|
|
| TrmFO |
COG1206 |
Folate-dependent tRNA-U54 methylase TrmFO/GidA [Translation, ribosomal structure and ... |
318-411 |
1.25e-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: 73.17 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 318 QRQMLETIPGLEKADMMRAGyaieydaiV---------PTQLWPTLETKMIKNLYTAGQINGTSGYEEAAGQGIMAGINA 388
Cdd:COG1206 288 QKRVFRMIPGLENAEFVRYG--------VmhrntfinsPKLLDPTLQLKARPNLFFAGQITGVEGYVESAASGLLAGINA 359
|
90 100
....*....|....*....|...
gi 1325404581 389 AGKVLGKEEKILSRSDAyIGVLI 411
Cdd:COG1206 360 ARLLLGKEPVPPPPTTA-LGALL 381
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
5-154 |
3.48e-13 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 70.53 E-value: 3.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 5 YDVIVIGAGHAGIEAGLASARRGAKTLMLtinldniafmpcnpsvggpakgivvrEIDALGGQMAKTID-------KTHI 77
Cdd:COG0492 1 YDVVIIGAGPAGLTAAIYAARAGLKTLVI--------------------------EGGEPGGQLATTKEienypgfPEGI 54
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1325404581 78 QmrmlntgkGPA-VRALRAQADKVlyqqemknviededNLDIMQGMVDElIIEDDEVKGVRTNIGTEYRSKAVVITTG 154
Cdd:COG0492 55 S--------GPElAERLREQAERF--------------GAEILLEEVTS-VDKDDGPFRVTTDDGTEYEAKAVIIATG 109
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
4-154 |
1.55e-05 |
|
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440673 [Multi-domain] Cd Length: 443 Bit Score: 47.91 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 4 EYDVIVIGAGHAGIEAGLASARRGAKTLMLT---------------INL-----------DNIAFM----------PCNP 47
Cdd:COG1053 3 EYDVVVVGSGGAGLRAALEAAEAGLKVLVLEkvpprgghtaaaqggINAagtnvqkaageDSPEEHfydtvkggdgLADQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 48 SV------GGPAkgiVVREIDALGGQMAKTIDKTHIQM------RMLNTGK--GPA-VRALRAQADKvlyqqemKNVied 112
Cdd:COG1053 83 DLvealaeEAPE---AIDWLEAQGVPFSRTPDGRLPQFgghsvgRTCYAGDgtGHAlLATLYQAALR-------LGV--- 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1325404581 113 ednlDIMQG-MVDELIIEDDEVKGVRTNIGT----EYRSKAVVITTG 154
Cdd:COG1053 150 ----EIFTEtEVLDLIVDDGRVVGVVARDRTgeivRIRAKAVVLATG 192
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
6-154 |
3.55e-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: 46.45 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 6 DVIVIGAGHAGIEAGLASARRGAKTLMltinLDNiafmpcNPSVGGpakgivvreidALGGQMAKTIDKTHIQMRMLNTG 85
Cdd:pfam12831 1 DVVVVGGGPAGVAAAIAAARAGAKVLL----VER------RGFLGG-----------MLTSGLVGPDMGFYLNKEQVVGG 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 86 -----------KGPAVRALRAQADKVLYQQE-MKNVIED---EDNLDIMQG-MVDELIIEDDEVKGVRTNI---GTEYRS 146
Cdd:pfam12831 60 iarefrqrlraRGGLPGPYGLRGGWVPFDPEvAKAVLDEmlaEAGVTVLLHtRVVGVVKEGGRITGVTVETkggRITIRA 139
|
....*...
gi 1325404581 147 KAVVITTG 154
Cdd:pfam12831 140 KVFIDATG 147
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
5-154 |
8.37e-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: 45.00 E-value: 8.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 5 YDVIVIGAGHAGIEAGLASARRGAKTLMLTINlDNIAFMPCnpsvGGPAKGIVVREIDALGGQMAKTIDKTHIQM---RM 81
Cdd:TIGR02032 1 YDVVVVGAGPAGASAAYRLADKGLRVLLLEKK-SFPRYKPC----GGALSPRALEELDLPGELIVNLVRGARFFSpngDS 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1325404581 82 LN----TGKGPAVRalRAQADKVLYQQEMKNVIEDEDNLDImqgmVDELIIEDDEVKGVRTNIGTeYRSKAVVITTG 154
Cdd:TIGR02032 76 VEipieTELAYVID--RDAFDEQLAERAQEAGAELRLGTRV----LDVEIHDDRVVVIVRGSEGT-VTAKIVIGADG 145
|
|
| PRK05329 |
PRK05329 |
glycerol-3-phosphate dehydrogenase subunit GlpB; |
4-34 |
8.51e-05 |
|
glycerol-3-phosphate dehydrogenase subunit GlpB;
Pssm-ID: 235412 Cd Length: 422 Bit Score: 45.23 E-value: 8.51e-05
10 20 30
....*....|....*....|....*....|.
gi 1325404581 4 EYDVIVIGAGHAGIEAGLASARRGAKTLMLT 34
Cdd:PRK05329 2 KFDVLVIGGGLAGLTAALAAAEAGKRVALVA 32
|
|
| PRK07843 |
PRK07843 |
3-oxosteroid 1-dehydrogenase; |
1-33 |
2.31e-04 |
|
3-oxosteroid 1-dehydrogenase;
Pssm-ID: 236111 [Multi-domain] Cd Length: 557 Bit Score: 44.26 E-value: 2.31e-04
10 20 30
....*....|....*....|....*....|...
gi 1325404581 1 MVQEYDVIVIGAGHAGIEAGLASARRGAKTLML 33
Cdd:PRK07843 4 TVQEYDVVVVGSGAAGMVAALTAAHRGLSTVVV 36
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
5-154 |
2.78e-04 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 43.72 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 5 YDVIVIGAGHAGIEAGLASARRGAKTLMLT----------------INLDNIAFMPCNPSVGGPAKGIVVRE-------- 60
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEkgkklgrkilisgggrCNVTNLSEEPDNFLSRYPGNPKFLKSalsrftpw 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 61 --IDALGGQMAKTIDKTHIQMRMLNTGKGPAVRALRAQADKvlyqqemKNV-IEdednldiMQGMVDELIIEDDEVKGVR 137
Cdd:pfam03486 81 dfIAFFESLGVPLKEEDHGRLFPDSDKASDIVDALLNELKE-------LGVkIR-------LRTRVLSVEKDDDGRFRVK 146
|
170
....*....|....*..
gi 1325404581 138 TNiGTEYRSKAVVITTG 154
Cdd:pfam03486 147 TG-GEELEADSLVLATG 162
|
|
| PRK08274 |
PRK08274 |
FAD-dependent tricarballylate dehydrogenase TcuA; |
1-33 |
2.94e-04 |
|
FAD-dependent tricarballylate dehydrogenase TcuA;
Pssm-ID: 236214 [Multi-domain] Cd Length: 466 Bit Score: 43.71 E-value: 2.94e-04
10 20 30
....*....|....*....|....*....|...
gi 1325404581 1 MVQEYDVIVIGAGHAGIEAGLASARRGAKTLML 33
Cdd:PRK08274 1 MASMVDVLVIGGGNAALCAALAAREAGASVLLL 33
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
5-74 |
3.55e-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: 43.08 E-value: 3.55e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325404581 5 YDVIVIGAGHAGIEAGLASARRGAKTLMLTINlDNIAFMPCNPSVGGPAKGIvVREIDALGGQMAKTIDK 74
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDE-GTCPYGGCVLSKALLGAAE-APEIASLWADLYKRKEE 68
|
|
| GlpB |
COG3075 |
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism]; |
4-30 |
3.58e-04 |
|
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 442309 Cd Length: 415 Bit Score: 43.24 E-value: 3.58e-04
10 20
....*....|....*....|....*..
gi 1325404581 4 EYDVIVIGAGHAGIEAGLASARRGAKT 30
Cdd:COG3075 2 KFDVVVIGGGLAGLTAAIRAAEAGLRV 28
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
3-33 |
4.35e-04 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 43.30 E-value: 4.35e-04
10 20 30
....*....|....*....|....*....|.
gi 1325404581 3 QEYDVIVIGAGHAGIEAGLASARRGAKTLML 33
Cdd:COG1233 2 MMYDVVVIGAGIGGLAAAALLARAGYRVTVL 32
|
|
| sdhA |
PRK07803 |
succinate dehydrogenase flavoprotein subunit; Reviewed |
2-37 |
5.23e-04 |
|
succinate dehydrogenase flavoprotein subunit; Reviewed
Pssm-ID: 236101 [Multi-domain] Cd Length: 626 Bit Score: 43.10 E-value: 5.23e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1325404581 2 VQEYDVIVIGAGHAGIEAGLASARRGAKTLMLTINL 37
Cdd:PRK07803 6 RHSYDVVVIGAGGAGLRAAIEARERGLRVAVVCKSL 41
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
3-32 |
5.86e-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: 5.86e-04
10 20 30
....*....|....*....|....*....|
gi 1325404581 3 QEYDVIVIGAGHAGIEAGLASARRGAKTLM 32
Cdd:COG1249 2 KDYDLVVIGAGPGGYVAAIRAAQLGLKVAL 31
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
6-34 |
1.52e-03 |
|
FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.
Pssm-ID: 395718 [Multi-domain] Cd Length: 398 Bit Score: 41.12 E-value: 1.52e-03
10 20
....*....|....*....|....*....
gi 1325404581 6 DVIVIGAGHAGIEAGLASARRGAKTLMLT 34
Cdd:pfam00890 1 DVLVIGGGLAGLAAALAAAEAGLKVAVVE 29
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
4-33 |
4.15e-03 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 40.10 E-value: 4.15e-03
10 20 30
....*....|....*....|....*....|
gi 1325404581 4 EYDVIVIGAGHAGIEAGLASARRGAKTLML 33
Cdd:PRK12843 16 EFDVIVIGAGAAGMSAALFAAIAGLKVLLV 45
|
|
| solA |
PRK11259 |
N-methyl-L-tryptophan oxidase; |
3-33 |
5.53e-03 |
|
N-methyl-L-tryptophan oxidase;
Pssm-ID: 236887 [Multi-domain] Cd Length: 376 Bit Score: 39.43 E-value: 5.53e-03
10 20 30
....*....|....*....|....*....|.
gi 1325404581 3 QEYDVIVIGAGHAGIEAGLASARRGAKTLML 33
Cdd:PRK11259 2 MRYDVIVIGLGSMGSAAGYYLARRGLRVLGL 32
|
|
| PRK07121 |
PRK07121 |
FAD-binding protein; |
4-33 |
8.48e-03 |
|
FAD-binding protein;
Pssm-ID: 180854 [Multi-domain] Cd Length: 492 Bit Score: 39.10 E-value: 8.48e-03
10 20 30
....*....|....*....|....*....|
gi 1325404581 4 EYDVIVIGAGHAGIEAGLASARRGAKTLML 33
Cdd:PRK07121 20 EADVVVVGFGAAGACAAIEAAAAGARVLVL 49
|
|
| |
