|
Name |
Accession |
Description |
Interval |
E-value |
| MnmG |
COG0445 |
tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal ... |
3-627 |
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: 1251.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 3 YEAGQYDVIVVGAGHAGVEAALASARQGAKTLVLTINLDMVAFMPCNPSVGGPAKGIVVREIDALGGEMARNIDKTHIQM 82
Cdd:COG0445 2 YYPKEYDVIVVGGGHAGCEAALAAARMGAKTLLLTHNLDTIGQMSCNPAIGGIAKGHLVREIDALGGEMGRAADKTGIQF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 83 RMLNTGKGPAVRALRAQADKFQYQHEMKKTMENEPNLTMLQGMVDHLIVEDDECKGVVTQTGANYRAKSVVLTTGTFLKG 162
Cdd:COG0445 82 RMLNTSKGPAVRAPRAQADRKLYRAAMRETLENQPNLDLIQGEVEDLIVEDGRVTGVVTADGIEFRAKAVVLTTGTFLNG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 163 RIILGDLSYSSGPNNQQPSIKLSDHLAELGFDLVRFKTGTPPRVNSHSIDYSKTEIQPGDDVPRAFSYETVEYITDQLPC 242
Cdd:COG0445 162 LIHIGEKSYPGGRAGEPPSVGLSESLRELGFELGRLKTGTPPRIDGRSIDFSKLEEQPGDEPPPPFSFLTEKIHPPQIPC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 243 WLTYTSLETHQIIDENLHRSPMYSGMIKGTGPRYCPSIEDKVVRFNDKPRHQIFLEPEGRNTQEVYVQGLSTSLPEDVQQ 322
Cdd:COG0445 242 WITYTNEETHEIIRENLHRSPMYSGVIEGVGPRYCPSIEDKIVRFADKDRHQIFLEPEGLDTNEVYPNGISTSLPEDVQL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 323 RMLSTIPGLENVQMMRAGYAIEYDAIVPTQLWPTLETKKISGLYTAGQINGTSGYEEAAGQGIMAGINAGRKALGKEEVI 402
Cdd:COG0445 322 AMLRSIPGLENAEILRPGYAIEYDYVDPTQLKPTLETKKIEGLFFAGQINGTTGYEEAAAQGLMAGINAALKAQGKEPFI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 403 LSRSDAYIGVLIDDLVTKGTNEPYRLLTSRAEYRLLLRHDNADLRLTELGYNIGLISEERFQAFTQKKEAIEAEKKRLYS 482
Cdd:COG0445 402 LDRSEAYIGVLIDDLVTKGTDEPYRMFTSRAEYRLLLRQDNADLRLTEKGYELGLVSDERYERFEEKKEAIEEEIERLKS 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 483 VIIKPTAETQEYIRSLGGSELKDGIRASDLMKRPEMNYESVVKLAPADTQLPADVCEQVEIQIKYEGYIEKSLQQVEKLK 562
Cdd:COG0445 482 TRVTPNEEVNEGLEELGSSPLKRGVSLFDLLRRPEITYEDLAELDPELPDLDPEVAEQVEIEIKYEGYIERQEEEIEKLK 561
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515929286 563 KMENKKIPDRIDYDAIKGIATEAKQKLKEVRPLSVAQASRISGVNPADISILLVYLEQGRIAKIA 627
Cdd:COG0445 562 RLENLKIPEDFDYDAIPGLSNEAREKLKKIRPETLGQASRISGVTPADISLLLVYLKRRRRRKKA 626
|
|
| gidA |
TIGR00136 |
glucose-inhibited division protein A; GidA, the longer of two forms of GidA-related proteins, ... |
8-622 |
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: 1091.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 8 YDVIVVGAGHAGVEAALASARQGAKTLVLTINLDMVAFMPCNPSVGGPAKGIVVREIDALGGEMARNIDKTHIQMRMLNT 87
Cdd:TIGR00136 1 FDVIVIGGGHAGCEAALAAARLGAKTLLLTLNLDTIGKCSCNPAIGGPAKGILVKEIDALGGEMGKAADKTGLQFRVLNS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 88 GKGPAVRALRAQADKFQYQHEMKKTMENEPNLTMLQGMVDHLIVED-DECKGVVTQTGANYRAKSVVLTTGTFLKGRIIL 166
Cdd:TIGR00136 81 SKGPAVRATRAQIDKILYQKWMRNQLENQPNLSLFQGEVEDLILEDnDEIKGVVTKDGNEFRAKAVIITTGTFLRGKIHI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 167 GDLSYSSGPNNQQPSIKLSDHLAELGFDLVRFKTGTPPRVNSHSIDYSKTEIQPGDDVPRAFSYETVEYITDQLPCWLTY 246
Cdd:TIGR00136 161 GDKSYEAGRAGEQASYGLSTTLRELGFKTGRLKTGTPPRIDKRSIDFSKLEVQFGDTQPPAFSFTNKNFLPQQLPCYLTH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 247 TSLETHQIIDENLHRSPMYSGMIKGTGPRYCPSIEDKVVRFNDKPRHQIFLEPEGRNTQEVYVQGLSTSLPEDVQQRMLS 326
Cdd:TIGR00136 241 TNPKTHQIIRDNLHRSPMYSGSIEGNGPRYCPSIEDKVVRFADKERHQIFLEPEGLNSDEIYLNGLSTSLPEDVQLKIIR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 327 TIPGLENVQMMRAGYAIEYDAIVPTQLWPTLETKKISGLYTAGQINGTSGYEEAAGQGIMAGINAGRKALGKEEVILSRS 406
Cdd:TIGR00136 321 SIPGLENAEILRPGYAIEYDYFDPTQLKPTLETKLIKGLFFAGQINGTTGYEEAAAQGLMAGINAALKLQNKEPFILKRN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 407 DAYIGVLIDDLVTKGTNEPYRLLTSRAEYRLLLRHDNADLRLTELGYNIGLISEERFQAFTQKKEAIEAEKKRLYSVIIK 486
Cdd:TIGR00136 401 EAYIGVLIDDLVTKGTKEPYRMFTSRAEYRLLLREDNADFRLTEIGRELGLIDEDRYARFLKKKQNIEEEIERLKSTRLS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 487 PTAETQEYIRSLGGSELKDGIRASDLMKRPEMNYESVVKLAPADTQLPADVCEQVEIQIKYEGYIEKSLQQVEKLKKMEN 566
Cdd:TIGR00136 481 PSKEVKEELKNLAQSPLKDEVSGYDLLKRPEMNLDKLTKLLPFLPPLDEEVLEQVEIEIKYEGYIKKQQQYIKKLDRLEN 560
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 515929286 567 KKIPDRIDYDAIKGIATEAKQKLKEVRPLSVAQASRISGVNPADISILLVYLEQGR 622
Cdd:TIGR00136 561 VKIPADFDYRKIPGLSTEAREKLSKFRPLSLGQASRISGINPADISALLVYLKKQK 616
|
|
| GIDA |
pfam01134 |
Glucose inhibited division protein A; |
9-399 |
0e+00 |
|
Glucose inhibited division protein A;
Pssm-ID: 250388 [Multi-domain] Cd Length: 391 Bit Score: 689.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 9 DVIVVGAGHAGVEAALASARQGAKTLVLTINLDMVAFMPCNPSVGGPAKGIVVREIDALGGEMARNIDKTHIQMRMLNTG 88
Cdd:pfam01134 1 DVIVIGGGHAGCEAALAAARMGAKVLLITHNTDTIAELSCNPSIGGIAKGHLVREIDALGGLMGKAADKTGIQFRMLNTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 89 KGPAVRALRAQADKFQYQHEMKKTMENEPNLTMLQGMVDHLIVEDDECKGVVTQTGANYRAKSVVLTTGTFLKGRIILGD 168
Cdd:pfam01134 81 KGPAVRALRAQVDRDLYSKEMTETLENHPNLTLIQGEVTDLIPENGKVKGVVTEDGEEYKAKAVVLATGTFLNGKIHIGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 169 LSYSSGPNNQQPSIKLSDHLAELGFDLVRFKTGTPPRVNSHSIDYSKTEIQPGDDVPRAFSYETVEYITDQLPCWLTYTS 248
Cdd:pfam01134 161 KCYPAGRLGELTSEGLSESLKELGFELGRFKTGTPPRIDKDSIDFSKLEEQPGDKPGPPFSYLNCPMNKEQYPCFLTYTN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 249 LETHQIIDENLHRSPMYSGMIKGTGPRYCPSIEDKVVRFNDKPRHQIFLEPEGRNTQEVYVQGLSTSLPEDVQQRMLSTI 328
Cdd:pfam01134 241 EATHEIIRDNLHRSPMFEGCIEGIGPRYCPSIEDKPVRFADKPYHQVFLEPEGLDTDEYYLVGFSTSLPEDVQKRVLRTI 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515929286 329 PGLENVQMMRAGYAIEYDAIVPTQLWPTLETKKISGLYTAGQINGTSGYEEAAGQGIMAGINAGRKALGKE 399
Cdd:pfam01134 321 PGLENAEIVRPGYAIEYDYIDPPQLLPTLETKKIPGLFFAGQINGTEGYEEAAAQGLLAGINAARKALGKE 391
|
|
| PRK05335 |
PRK05335 |
tRNA (uracil-5-)-methyltransferase Gid; Reviewed |
311-414 |
6.35e-18 |
|
tRNA (uracil-5-)-methyltransferase Gid; Reviewed
Pssm-ID: 235416 Cd Length: 436 Bit Score: 86.74 E-value: 6.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 311 GLSTSL--PEdvQQRMLSTIPGLENVQMMRAGyaieydaiV---------PTQLWPTLETKKISGLYTAGQINGTSGYEE 379
Cdd:PRK05335 278 GFQTKLkwGE--QKRVFRMIPGLENAEFVRYG--------VmhrntfinsPKLLDPTLQLKKRPNLFFAGQITGVEGYVE 347
|
90 100 110
....*....|....*....|....*....|....*
gi 515929286 380 AAGQGIMAGINAGRKALGKEEVILSRSDAyIGVLI 414
Cdd:PRK05335 348 SAASGLLAGINAARLALGKEPVIPPPTTA-LGALL 381
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| MnmG |
COG0445 |
tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal ... |
3-627 |
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: 1251.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 3 YEAGQYDVIVVGAGHAGVEAALASARQGAKTLVLTINLDMVAFMPCNPSVGGPAKGIVVREIDALGGEMARNIDKTHIQM 82
Cdd:COG0445 2 YYPKEYDVIVVGGGHAGCEAALAAARMGAKTLLLTHNLDTIGQMSCNPAIGGIAKGHLVREIDALGGEMGRAADKTGIQF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 83 RMLNTGKGPAVRALRAQADKFQYQHEMKKTMENEPNLTMLQGMVDHLIVEDDECKGVVTQTGANYRAKSVVLTTGTFLKG 162
Cdd:COG0445 82 RMLNTSKGPAVRAPRAQADRKLYRAAMRETLENQPNLDLIQGEVEDLIVEDGRVTGVVTADGIEFRAKAVVLTTGTFLNG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 163 RIILGDLSYSSGPNNQQPSIKLSDHLAELGFDLVRFKTGTPPRVNSHSIDYSKTEIQPGDDVPRAFSYETVEYITDQLPC 242
Cdd:COG0445 162 LIHIGEKSYPGGRAGEPPSVGLSESLRELGFELGRLKTGTPPRIDGRSIDFSKLEEQPGDEPPPPFSFLTEKIHPPQIPC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 243 WLTYTSLETHQIIDENLHRSPMYSGMIKGTGPRYCPSIEDKVVRFNDKPRHQIFLEPEGRNTQEVYVQGLSTSLPEDVQQ 322
Cdd:COG0445 242 WITYTNEETHEIIRENLHRSPMYSGVIEGVGPRYCPSIEDKIVRFADKDRHQIFLEPEGLDTNEVYPNGISTSLPEDVQL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 323 RMLSTIPGLENVQMMRAGYAIEYDAIVPTQLWPTLETKKISGLYTAGQINGTSGYEEAAGQGIMAGINAGRKALGKEEVI 402
Cdd:COG0445 322 AMLRSIPGLENAEILRPGYAIEYDYVDPTQLKPTLETKKIEGLFFAGQINGTTGYEEAAAQGLMAGINAALKAQGKEPFI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 403 LSRSDAYIGVLIDDLVTKGTNEPYRLLTSRAEYRLLLRHDNADLRLTELGYNIGLISEERFQAFTQKKEAIEAEKKRLYS 482
Cdd:COG0445 402 LDRSEAYIGVLIDDLVTKGTDEPYRMFTSRAEYRLLLRQDNADLRLTEKGYELGLVSDERYERFEEKKEAIEEEIERLKS 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 483 VIIKPTAETQEYIRSLGGSELKDGIRASDLMKRPEMNYESVVKLAPADTQLPADVCEQVEIQIKYEGYIEKSLQQVEKLK 562
Cdd:COG0445 482 TRVTPNEEVNEGLEELGSSPLKRGVSLFDLLRRPEITYEDLAELDPELPDLDPEVAEQVEIEIKYEGYIERQEEEIEKLK 561
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515929286 563 KMENKKIPDRIDYDAIKGIATEAKQKLKEVRPLSVAQASRISGVNPADISILLVYLEQGRIAKIA 627
Cdd:COG0445 562 RLENLKIPEDFDYDAIPGLSNEAREKLKKIRPETLGQASRISGVTPADISLLLVYLKRRRRRKKA 626
|
|
| gidA |
TIGR00136 |
glucose-inhibited division protein A; GidA, the longer of two forms of GidA-related proteins, ... |
8-622 |
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: 1091.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 8 YDVIVVGAGHAGVEAALASARQGAKTLVLTINLDMVAFMPCNPSVGGPAKGIVVREIDALGGEMARNIDKTHIQMRMLNT 87
Cdd:TIGR00136 1 FDVIVIGGGHAGCEAALAAARLGAKTLLLTLNLDTIGKCSCNPAIGGPAKGILVKEIDALGGEMGKAADKTGLQFRVLNS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 88 GKGPAVRALRAQADKFQYQHEMKKTMENEPNLTMLQGMVDHLIVED-DECKGVVTQTGANYRAKSVVLTTGTFLKGRIIL 166
Cdd:TIGR00136 81 SKGPAVRATRAQIDKILYQKWMRNQLENQPNLSLFQGEVEDLILEDnDEIKGVVTKDGNEFRAKAVIITTGTFLRGKIHI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 167 GDLSYSSGPNNQQPSIKLSDHLAELGFDLVRFKTGTPPRVNSHSIDYSKTEIQPGDDVPRAFSYETVEYITDQLPCWLTY 246
Cdd:TIGR00136 161 GDKSYEAGRAGEQASYGLSTTLRELGFKTGRLKTGTPPRIDKRSIDFSKLEVQFGDTQPPAFSFTNKNFLPQQLPCYLTH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 247 TSLETHQIIDENLHRSPMYSGMIKGTGPRYCPSIEDKVVRFNDKPRHQIFLEPEGRNTQEVYVQGLSTSLPEDVQQRMLS 326
Cdd:TIGR00136 241 TNPKTHQIIRDNLHRSPMYSGSIEGNGPRYCPSIEDKVVRFADKERHQIFLEPEGLNSDEIYLNGLSTSLPEDVQLKIIR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 327 TIPGLENVQMMRAGYAIEYDAIVPTQLWPTLETKKISGLYTAGQINGTSGYEEAAGQGIMAGINAGRKALGKEEVILSRS 406
Cdd:TIGR00136 321 SIPGLENAEILRPGYAIEYDYFDPTQLKPTLETKLIKGLFFAGQINGTTGYEEAAAQGLMAGINAALKLQNKEPFILKRN 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 407 DAYIGVLIDDLVTKGTNEPYRLLTSRAEYRLLLRHDNADLRLTELGYNIGLISEERFQAFTQKKEAIEAEKKRLYSVIIK 486
Cdd:TIGR00136 401 EAYIGVLIDDLVTKGTKEPYRMFTSRAEYRLLLREDNADFRLTEIGRELGLIDEDRYARFLKKKQNIEEEIERLKSTRLS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 487 PTAETQEYIRSLGGSELKDGIRASDLMKRPEMNYESVVKLAPADTQLPADVCEQVEIQIKYEGYIEKSLQQVEKLKKMEN 566
Cdd:TIGR00136 481 PSKEVKEELKNLAQSPLKDEVSGYDLLKRPEMNLDKLTKLLPFLPPLDEEVLEQVEIEIKYEGYIKKQQQYIKKLDRLEN 560
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 515929286 567 KKIPDRIDYDAIKGIATEAKQKLKEVRPLSVAQASRISGVNPADISILLVYLEQGR 622
Cdd:TIGR00136 561 VKIPADFDYRKIPGLSTEAREKLSKFRPLSLGQASRISGINPADISALLVYLKKQK 616
|
|
| GIDA |
pfam01134 |
Glucose inhibited division protein A; |
9-399 |
0e+00 |
|
Glucose inhibited division protein A;
Pssm-ID: 250388 [Multi-domain] Cd Length: 391 Bit Score: 689.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 9 DVIVVGAGHAGVEAALASARQGAKTLVLTINLDMVAFMPCNPSVGGPAKGIVVREIDALGGEMARNIDKTHIQMRMLNTG 88
Cdd:pfam01134 1 DVIVIGGGHAGCEAALAAARMGAKVLLITHNTDTIAELSCNPSIGGIAKGHLVREIDALGGLMGKAADKTGIQFRMLNTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 89 KGPAVRALRAQADKFQYQHEMKKTMENEPNLTMLQGMVDHLIVEDDECKGVVTQTGANYRAKSVVLTTGTFLKGRIILGD 168
Cdd:pfam01134 81 KGPAVRALRAQVDRDLYSKEMTETLENHPNLTLIQGEVTDLIPENGKVKGVVTEDGEEYKAKAVVLATGTFLNGKIHIGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 169 LSYSSGPNNQQPSIKLSDHLAELGFDLVRFKTGTPPRVNSHSIDYSKTEIQPGDDVPRAFSYETVEYITDQLPCWLTYTS 248
Cdd:pfam01134 161 KCYPAGRLGELTSEGLSESLKELGFELGRFKTGTPPRIDKDSIDFSKLEEQPGDKPGPPFSYLNCPMNKEQYPCFLTYTN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 249 LETHQIIDENLHRSPMYSGMIKGTGPRYCPSIEDKVVRFNDKPRHQIFLEPEGRNTQEVYVQGLSTSLPEDVQQRMLSTI 328
Cdd:pfam01134 241 EATHEIIRDNLHRSPMFEGCIEGIGPRYCPSIEDKPVRFADKPYHQVFLEPEGLDTDEYYLVGFSTSLPEDVQKRVLRTI 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515929286 329 PGLENVQMMRAGYAIEYDAIVPTQLWPTLETKKISGLYTAGQINGTSGYEEAAGQGIMAGINAGRKALGKE 399
Cdd:pfam01134 321 PGLENAEIVRPGYAIEYDYIDPPQLLPTLETKKIPGLFFAGQINGTEGYEEAAAQGLLAGINAARKALGKE 391
|
|
| GIDA_C |
pfam13932 |
tRNA modifying enzyme MnmG/GidA C-terminal domain; The GidA associated domain is a domain that ... |
401-615 |
3.69e-128 |
|
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: 375.95 E-value: 3.69e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 401 VILSRSDAYIGVLIDDLVTKGTNEPYRLLTSRAEYRLLLRHDNADLRLTELGYNIGLISEERFQAFTQKKEAIEAEKKRL 480
Cdd:pfam13932 1 LILSRSEAYIGVLIDDLVTKGTSEPYRMFTSRAEYRLLLRQDNADLRLTEKGRELGLVSDERYERFEEKKEAIEEEIERL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 481 YSVIIKPTAETQEYIrSLGGSELKDGIRASDLMKRPEMNYESVVKLAPADTQLPADVCEQVEIQIKYEGYIEKSLQQVEK 560
Cdd:pfam13932 81 KSTRLSPSEWNNALL-ELGSAPLGTGRSAFDLLRRPEVTYEDLAALIPELAPLDPEVLEQVEIEAKYEGYIERQEAEIEK 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 515929286 561 LKKMENKKIPDRIDYDAIKGIATEAKQKLKEVRPLSVAQASRISGVNPADISILL 615
Cdd:pfam13932 160 FKRLENLKIPEDLDYDAIPGLSNEAREKLNKIRPETIGQASRISGVTPADISVLL 214
|
|
| PRK05335 |
PRK05335 |
tRNA (uracil-5-)-methyltransferase Gid; Reviewed |
311-414 |
6.35e-18 |
|
tRNA (uracil-5-)-methyltransferase Gid; Reviewed
Pssm-ID: 235416 Cd Length: 436 Bit Score: 86.74 E-value: 6.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 311 GLSTSL--PEdvQQRMLSTIPGLENVQMMRAGyaieydaiV---------PTQLWPTLETKKISGLYTAGQINGTSGYEE 379
Cdd:PRK05335 278 GFQTKLkwGE--QKRVFRMIPGLENAEFVRYG--------VmhrntfinsPKLLDPTLQLKKRPNLFFAGQITGVEGYVE 347
|
90 100 110
....*....|....*....|....*....|....*
gi 515929286 380 AAGQGIMAGINAGRKALGKEEVILSRSDAyIGVLI 414
Cdd:PRK05335 348 SAASGLLAGINAARLALGKEPVIPPPTTA-LGALL 381
|
|
| TrmFO |
COG1206 |
Folate-dependent tRNA-U54 methylase TrmFO/GidA [Translation, ribosomal structure and ... |
321-414 |
3.58e-17 |
|
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: 84.34 E-value: 3.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 321 QQRMLSTIPGLENVQMMRAGyaieydaiV---------PTQLWPTLETKKISGLYTAGQINGTSGYEEAAGQGIMAGINA 391
Cdd:COG1206 288 QKRVFRMIPGLENAEFVRYG--------VmhrntfinsPKLLDPTLQLKARPNLFFAGQITGVEGYVESAASGLLAGINA 359
|
90 100
....*....|....*....|...
gi 515929286 392 GRKALGKEEVILSRSDAyIGVLI 414
Cdd:COG1206 360 ARLLLGKEPVPPPPTTA-LGALL 381
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
8-157 |
3.69e-10 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 61.29 E-value: 3.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 8 YDVIVVGAGHAGVEAALASARQGAKTLVLtinldmvafmpcnpsvggpakgivvrEIDALGGEMAR-----NI--DKTHI 80
Cdd:COG0492 1 YDVVIIGAGPAGLTAAIYAARAGLKTLVI--------------------------EGGEPGGQLATtkeieNYpgFPEGI 54
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515929286 81 QmrmlntgkGPA-VRALRAQADKFqyqhemkktmenepNLTMLQGMVDHlIVEDDECKGVVTQTGANYRAKSVVLTTG 157
Cdd:COG0492 55 S--------GPElAERLREQAERF--------------GAEILLEEVTS-VDKDDGPFRVTTDDGTEYEAKAVIIATG 109
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
7-157 |
6.55e-09 |
|
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: 58.31 E-value: 6.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 7 QYDVIVVGAGHAGVEAALASARQGAKTLVLT---------------INL-------------------DMVAFM--PCNP 50
Cdd:COG1053 3 EYDVVVVGSGGAGLRAALEAAEAGLKVLVLEkvpprgghtaaaqggINAagtnvqkaagedspeehfyDTVKGGdgLADQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 51 SV------GGPAkgiVVREIDALGGEMARNIDKTHIQM------RMLNTGK--GPA-VRALRAQADK----FQYQHEMKK 111
Cdd:COG1053 83 DLvealaeEAPE---AIDWLEAQGVPFSRTPDGRLPQFgghsvgRTCYAGDgtGHAlLATLYQAALRlgveIFTETEVLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 515929286 112 tmenepnltmlqgmvdhLIVEDDECKGVV--TQTGA--NYRAKSVVLTTG 157
Cdd:COG1053 160 -----------------LIVDDGRVVGVVarDRTGEivRIRAKAVVLATG 192
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
9-174 |
2.43e-08 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 56.46 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 9 DVIVVGAGHAGVEAALASARQGAKTLV----------LT---INLDMVAFMPCNPSVGGpakgiVVREIdalggeMARNI 75
Cdd:pfam12831 1 DVVVVGGGPAGVAAAIAAARAGAKVLLverrgflggmLTsglVGPDMGFYLNKEQVVGG-----IAREF------RQRLR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 76 DKTHIQMRMLNTGKGPAvralraqadkfqYQHE-MKKTMEN---EPNLTMLQG-MVDHLIVEDDECKGVVTQT---GANY 147
Cdd:pfam12831 70 ARGGLPGPYGLRGGWVP------------FDPEvAKAVLDEmlaEAGVTVLLHtRVVGVVKEGGRITGVTVETkggRITI 137
|
170 180
....*....|....*....|....*..
gi 515929286 148 RAKSVVLTTGtflkgriiLGDLSYSSG 174
Cdd:pfam12831 138 RAKVFIDATG--------DGDLAALAG 156
|
|
| PRK07843 |
PRK07843 |
3-oxosteroid 1-dehydrogenase; |
1-36 |
5.80e-06 |
|
3-oxosteroid 1-dehydrogenase;
Pssm-ID: 236111 [Multi-domain] Cd Length: 557 Bit Score: 49.26 E-value: 5.80e-06
10 20 30
....*....|....*....|....*....|....*.
gi 515929286 1 MGYEAGQYDVIVVGAGHAGVEAALASARQGAKTLVL 36
Cdd:PRK07843 1 MAMTVQEYDVVVVGSGAAGMVAALTAAHRGLSTVVV 36
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
9-159 |
6.99e-06 |
|
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: 48.82 E-value: 6.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 9 DVIVVGAGHAGVEAALASARQGAKTLVLT------INLDM---VAFMPCNPSVGGPAKGIVVRE--------------ID 65
Cdd:pfam00890 1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEkgqpfgGATAWssgGIDALGNPPQGGIDSPELHPTdtlkgldeladhpyVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515929286 66 AL---GGEMARNIDKTHiqMRMLNTGKGP-AVRALRAQADKFQYQHEMKKTMENEPN-----LTMLQG------------ 124
Cdd:pfam00890 81 AFveaAPEAVDWLEALG--VPFSRTEDGHlDLRPLGGLSATWRTPHDAADRRRGLGTghallARLLEGlrkagvdfqprt 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 515929286 125 MVDHLIVEDDECKGVVTQTGAN-----YRAKS-VVLTTGTF 159
Cdd:pfam00890 159 AADDLIVEDGRVTGAVVENRRNgrevrIRAIAaVLLATGGF 199
|
|
| sdhA |
PRK07803 |
succinate dehydrogenase flavoprotein subunit; Reviewed |
1-40 |
2.39e-05 |
|
succinate dehydrogenase flavoprotein subunit; Reviewed
Pssm-ID: 236101 [Multi-domain] Cd Length: 626 Bit Score: 47.34 E-value: 2.39e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 515929286 1 MGYEAGQYDVIVVGAGHAGVEAALASARQGAKTLVLTINL 40
Cdd:PRK07803 2 TEVERHSYDVVVIGAGGAGLRAAIEARERGLRVAVVCKSL 41
|
|
| PRK05329 |
PRK05329 |
glycerol-3-phosphate dehydrogenase subunit GlpB; |
8-37 |
1.07e-04 |
|
glycerol-3-phosphate dehydrogenase subunit GlpB;
Pssm-ID: 235412 Cd Length: 422 Bit Score: 44.84 E-value: 1.07e-04
10 20 30
....*....|....*....|....*....|
gi 515929286 8 YDVIVVGAGHAGVEAALASARQGAKTLVLT 37
Cdd:PRK05329 3 FDVLVIGGGLAGLTAALAAAEAGKRVALVA 32
|
|
| PRK08274 |
PRK08274 |
FAD-dependent tricarballylate dehydrogenase TcuA; |
8-36 |
1.26e-04 |
|
FAD-dependent tricarballylate dehydrogenase TcuA;
Pssm-ID: 236214 [Multi-domain] Cd Length: 466 Bit Score: 44.87 E-value: 1.26e-04
10 20
....*....|....*....|....*....
gi 515929286 8 YDVIVVGAGHAGVEAALASARQGAKTLVL 36
Cdd:PRK08274 5 VDVLVIGGGNAALCAALAAREAGASVLLL 33
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
7-36 |
1.65e-04 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 44.46 E-value: 1.65e-04
10 20 30
....*....|....*....|....*....|
gi 515929286 7 QYDVIVVGAGHAGVEAALASARQGAKTLVL 36
Cdd:COG1233 3 MYDVVVIGAGIGGLAAAALLARAGYRVTVL 32
|
|
| PRK07121 |
PRK07121 |
FAD-binding protein; |
8-36 |
2.17e-04 |
|
FAD-binding protein;
Pssm-ID: 180854 [Multi-domain] Cd Length: 492 Bit Score: 44.11 E-value: 2.17e-04
10 20
....*....|....*....|....*....
gi 515929286 8 YDVIVVGAGHAGVEAALASARQGAKTLVL 36
Cdd:PRK07121 21 ADVVVVGFGAAGACAAIEAAAAGARVLVL 49
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
8-39 |
2.23e-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: 43.46 E-value: 2.23e-04
10 20 30
....*....|....*....|....*....|..
gi 515929286 8 YDVIVVGAGHAGVEAALASARQGAKTLVLTIN 39
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDE 32
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
8-80 |
2.90e-04 |
|
geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
Pssm-ID: 273936 [Multi-domain] Cd Length: 295 Bit Score: 43.08 E-value: 2.90e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515929286 8 YDVIVVGAGHAGVEAALASARQGAKTLVLTINlDMVAFMPCnpsvGGPAKGIVVREIDALGGEMARNIDKTHI 80
Cdd:TIGR02032 1 YDVVVVGAGPAGASAAYRLADKGLRVLLLEKK-SFPRYKPC----GGALSPRALEELDLPGELIVNLVRGARF 68
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
7-35 |
3.11e-04 |
|
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation
Pssm-ID: 440861 [Multi-domain] Cd Length: 456 Bit Score: 43.54 E-value: 3.11e-04
10 20
....*....|....*....|....*....
gi 515929286 7 QYDVIVVGAGHAGVEAALASARQGAKTLV 35
Cdd:COG1249 3 DYDLVVIGAGPGGYVAAIRAAQLGLKVAL 31
|
|
| PRK07791 |
PRK07791 |
short chain dehydrogenase; Provisional |
10-76 |
6.75e-04 |
|
short chain dehydrogenase; Provisional
Pssm-ID: 236099 [Multi-domain] Cd Length: 286 Bit Score: 41.97 E-value: 6.75e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515929286 10 VIVVGAGHA-GVEAALASARQGAKTLVltiNlDMVAFMPCNPSVGGPAKGiVVREIDALGGEMARNID 76
Cdd:PRK07791 9 VIVTGAGGGiGRAHALAFAAEGARVVV---N-DIGVGLDGSASGGSAAQA-VVDEIVAAGGEAVANGD 71
|
|
| PRK07804 |
PRK07804 |
L-aspartate oxidase; Provisional |
9-37 |
2.09e-03 |
|
L-aspartate oxidase; Provisional
Pssm-ID: 236102 [Multi-domain] Cd Length: 541 Bit Score: 41.11 E-value: 2.09e-03
10 20
....*....|....*....|....*....
gi 515929286 9 DVIVVGAGHAGVEAALASARQGAKTLVLT 37
Cdd:PRK07804 18 DVVVVGSGVAGLTAALAARRAGRRVLVVT 46
|
|
| PRK12839 |
PRK12839 |
FAD-dependent oxidoreductase; |
7-36 |
2.31e-03 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237223 [Multi-domain] Cd Length: 572 Bit Score: 40.97 E-value: 2.31e-03
10 20 30
....*....|....*....|....*....|
gi 515929286 7 QYDVIVVGAGHAGVEAALASARQGAKTLVL 36
Cdd:PRK12839 8 TYDVVVVGSGAGGLSAAVAAAYGGAKVLVV 37
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
8-36 |
2.61e-03 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 40.64 E-value: 2.61e-03
10 20
....*....|....*....|....*....
gi 515929286 8 YDVIVVGAGHAGVEAALASARQGAKTLVL 36
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLI 29
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
4-36 |
2.86e-03 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 40.49 E-value: 2.86e-03
10 20 30
....*....|....*....|....*....|...
gi 515929286 4 EAGQYDVIVVGAGHAGVEAALASARQGAKTLVL 36
Cdd:PRK12843 13 WDAEFDVIVIGAGAAGMSAALFAAIAGLKVLLV 45
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
4-33 |
3.88e-03 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 40.14 E-value: 3.88e-03
10 20 30
....*....|....*....|....*....|
gi 515929286 4 EAGQYDVIVVGAGHAGVEAALASARQGAKT 33
Cdd:PRK15317 208 AKDPYDVLVVGGGPAGAAAAIYAARKGIRT 237
|
|
|