|
Name |
Accession |
Description |
Interval |
E-value |
| MnmG |
COG0445 |
tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal ... |
1-625 |
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: 1275.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 1 MDFPSRFEVIVIGGGHAGTEAALASARMGVKTLLLTHNVETLGQMSCNPAIGGIGKSHLVKEIDALGGAMAMATDKGGIQ 80
Cdd:COG0445 1 MYYPKEYDVIVVGGGHAGCEAALAAARMGAKTLLLTHNLDTIGQMSCNPAIGGIAKGHLVREIDALGGEMGRAADKTGIQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 81 FRVLNSRKGPAVRATRAQADRVLYKAAIRETLENQPNLWIFQQACDDLIVEQDQVRGVVTQMGMRIFADSVVLTTGTFLG 160
Cdd:COG0445 81 FRMLNTSKGPAVRAPRAQADRKLYRAAMRETLENQPNLDLIQGEVEDLIVEDGRVTGVVTADGIEFRAKAVVLTTGTFLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 161 GLIHIGMQNYSGGRAGDPPSIALAQRLRELPLRVGRLKTGTPPRIDGRSVDFSVMTEQPGDTPIPVMSFLgNKEQHPPQV 240
Cdd:COG0445 161 GLIHIGEKSYPGGRAGEPPSVGLSESLRELGFELGRLKTGTPPRIDGRSIDFSKLEEQPGDEPPPPFSFL-TEKIHPPQI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 241 SCWITHTNARTHEIIASNLDRSPMYSGVIEGIGPRYCPSIEDKIHRFADKESHQVFIEPEGLTTHELYPNGISTSLPFDV 320
Cdd:COG0445 240 PCWITYTNEETHEIIRENLHRSPMYSGVIEGVGPRYCPSIEDKIVRFADKDRHQIFLEPEGLDTNEVYPNGISTSLPEDV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 321 QLQIVQSIRGMENAHIVRPGYAIEYDYFDPRDLKYSLETKVIGGLFFAGQINGTTGYEEAGAQGLLAGTNAALRAQGRDS 400
Cdd:COG0445 320 QLAMLRSIPGLENAEILRPGYAIEYDYVDPTQLKPTLETKKIEGLFFAGQINGTTGYEEAAAQGLMAGINAALKAQGKEP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 401 WCPRRDEAYIGVLVDDLITLGTQEPYRMFTSRAEYRLILREDNADLRLTEKGRELGLVDDARWAAFCTKRESIELEEQRL 480
Cdd:COG0445 400 FILDRSEAYIGVLIDDLVTKGTDEPYRMFTSRAEYRLLLRQDNADLRLTEKGYELGLVSDERYERFEEKKEAIEEEIERL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 481 KSTWVRPGTEQGDAIAAHFGTPLTHEYNLLNLLTRPEIDYASLISITGQG-CIDPQVAEQVEIKTKYAGYIDRQQDEIAR 559
Cdd:COG0445 480 KSTRVTPNEEVNEGLEELGSSPLKRGVSLFDLLRRPEITYEDLAELDPELpDLDPEVAEQVEIEIKYEGYIERQEEEIEK 559
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489516690 560 LRASEDTGLPEDIDYAAISGLSKEIQSKLGITRPQTLGQASRIPGVTPAAISLLMIHLKKRGAGRQ 625
Cdd:COG0445 560 LKRLENLKIPEDFDYDAIPGLSNEAREKLKKIRPETLGQASRISGVTPADISLLLVYLKRRRRRKK 625
|
|
| gidA |
TIGR00136 |
glucose-inhibited division protein A; GidA, the longer of two forms of GidA-related proteins, ... |
7-621 |
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: 997.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 7 FEVIVIGGGHAGTEAALASARMGVKTLLLTHNVETLGQMSCNPAIGGIGKSHLVKEIDALGGAMAMATDKGGIQFRVLNS 86
Cdd:TIGR00136 1 FDVIVIGGGHAGCEAALAAARLGAKTLLLTLNLDTIGKCSCNPAIGGPAKGILVKEIDALGGEMGKAADKTGLQFRVLNS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 87 RKGPAVRATRAQADRVLYKAAIRETLENQPNLWIFQQACDDLIVEQ-DQVRGVVTQMGMRIFADSVVLTTGTFLGGLIHI 165
Cdd:TIGR00136 81 SKGPAVRATRAQIDKILYQKWMRNQLENQPNLSLFQGEVEDLILEDnDEIKGVVTKDGNEFRAKAVIITTGTFLRGKIHI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 166 GMQNYSGGRAGDPPSIALAQRLRELPLRVGRLKTGTPPRIDGRSVDFSVMTEQPGDTPIPVMSFLgNKEQHPPQVSCWIT 245
Cdd:TIGR00136 161 GDKSYEAGRAGEQASYGLSTTLRELGFKTGRLKTGTPPRIDKRSIDFSKLEVQFGDTQPPAFSFT-NKNFLPQQLPCYLT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 246 HTNARTHEIIASNLDRSPMYSGVIEGIGPRYCPSIEDKIHRFADKESHQVFIEPEGLTTHELYPNGISTSLPFDVQLQIV 325
Cdd:TIGR00136 240 HTNPKTHQIIRDNLHRSPMYSGSIEGNGPRYCPSIEDKVVRFADKERHQIFLEPEGLNSDEIYLNGLSTSLPEDVQLKII 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 326 QSIRGMENAHIVRPGYAIEYDYFDPRDLKYSLETKVIGGLFFAGQINGTTGYEEAGAQGLLAGTNAALRAQGRDSWCPRR 405
Cdd:TIGR00136 320 RSIPGLENAEILRPGYAIEYDYFDPTQLKPTLETKLIKGLFFAGQINGTTGYEEAAAQGLMAGINAALKLQNKEPFILKR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 406 DEAYIGVLVDDLITLGTQEPYRMFTSRAEYRLILREDNADLRLTEKGRELGLVDDARWAAFCTKRESIELEEQRLKSTWV 485
Cdd:TIGR00136 400 NEAYIGVLIDDLVTKGTKEPYRMFTSRAEYRLLLREDNADFRLTEIGRELGLIDEDRYARFLKKKQNIEEEIERLKSTRL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 486 RPGTEQGDAIAAHFGTPLTHEYNLLNLLTRPEIDYASLISIT-GQGCIDPQVAEQVEIKTKYAGYIDRQQDEIARLRASE 564
Cdd:TIGR00136 480 SPSKEVKEELKNLAQSPLKDEVSGYDLLKRPEMNLDKLTKLLpFLPPLDEEVLEQVEIEIKYEGYIKKQQQYIKKLDRLE 559
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 489516690 565 DTGLPEDIDYAAISGLSKEIQSKLGITRPQTLGQASRIPGVTPAAISLLMIHLKKRG 621
Cdd:TIGR00136 560 NVKIPADFDYRKIPGLSTEAREKLSKFRPLSLGQASRISGINPADISALLVYLKKQK 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: 693.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 9 VIVIGGGHAGTEAALASARMGVKTLLLTHNVETLGQMSCNPAIGGIGKSHLVKEIDALGGAMAMATDKGGIQFRVLNSRK 88
Cdd:pfam01134 2 VIVIGGGHAGCEAALAAARMGAKVLLITHNTDTIAELSCNPSIGGIAKGHLVREIDALGGLMGKAADKTGIQFRMLNTSK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 89 GPAVRATRAQADRVLYKAAIRETLENQPNLWIFQQACDDLIVEQDQVRGVVTQMGMRIFADSVVLTTGTFLGGLIHIGMQ 168
Cdd:pfam01134 82 GPAVRALRAQVDRDLYSKEMTETLENHPNLTLIQGEVTDLIPENGKVKGVVTEDGEEYKAKAVVLATGTFLNGKIHIGLK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 169 NYSGGRAGDPPSIALAQRLRELPLRVGRLKTGTPPRIDGRSVDFSVMTEQPGDTPIPVMSFLgNKEQHPPQVSCWITHTN 248
Cdd:pfam01134 162 CYPAGRLGELTSEGLSESLKELGFELGRFKTGTPPRIDKDSIDFSKLEEQPGDKPGPPFSYL-NCPMNKEQYPCFLTYTN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 249 ARTHEIIASNLDRSPMYSGVIEGIGPRYCPSIEDKIHRFADKESHQVFIEPEGLTTHELYPNGISTSLPFDVQLQIVQSI 328
Cdd:pfam01134 241 EATHEIIRDNLHRSPMFEGCIEGIGPRYCPSIEDKPVRFADKPYHQVFLEPEGLDTDEYYLVGFSTSLPEDVQKRVLRTI 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489516690 329 RGMENAHIVRPGYAIEYDYFDPRDLKYSLETKVIGGLFFAGQINGTTGYEEAGAQGLLAGTNAALRAQGRD 399
Cdd:pfam01134 321 PGLENAEIVRPGYAIEYDYIDPPQLLPTLETKKIPGLFFAGQINGTEGYEEAAAQGLLAGINAARKALGKE 391
|
|
| PRK05335 |
PRK05335 |
tRNA (uracil-5-)-methyltransferase Gid; Reviewed |
8-399 |
4.47e-14 |
|
tRNA (uracil-5-)-methyltransferase Gid; Reviewed
Pssm-ID: 235416 Cd Length: 436 Bit Score: 74.80 E-value: 4.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 8 EVIVIGGGHAGTEAALASARMGVKTLL-------LT--HNVETLGQMSCNPAIGGIGKSH----LVKEIDALGGA-MAMA 73
Cdd:PRK05335 4 PVNVIGAGLAGSEAAWQLAKRGVPVELyemrpvkKTpaHHTDGFAELVCSNSFRSDSLTNavglLKEEMRRLGSLiMEAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 74 tDKGgiqfrvlnsrkgpAVRATRAQA-DRVLYKAAIRETLENQPNLWIfqqacddliveqdqVRGVVTQmgmrIFADSVV 152
Cdd:PRK05335 84 -DAH-------------RVPAGGALAvDREGFSEYVTEALENHPLITV--------------IREEVTE----IPEDITI 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 153 LTTGtflgglihigmqnysggragdpP--SIALAQRLRELplrvgrlkTGTP---------PRIDGRSVDFSVmteqpgd 221
Cdd:PRK05335 132 IATG----------------------PltSDALAEAIKAL--------TGEDylyffdaaaPIVDKDSIDMDK------- 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 222 tpipvmsflgnkeqhppqvsCWIthtnartheiiASNLDRS-------PM----YSGVIEGIgprycpsIEDKIHRFADK 290
Cdd:PRK05335 175 --------------------VYL-----------ASRYDKGeadylncPMtkeeYEAFYEAL-------IAAEKAELKDF 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 291 ESHQVF-----IE----------------PEGLT---THE----------------LYpN--GISTSLPFDVQLQIVQSI 328
Cdd:PRK05335 217 EKEKYFegcmpIEvmaergretlrfgpmkPVGLTdprTGKrpyavvqlrqdnaagtLY-NivGFQTKLKWGEQKRVFRMI 295
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489516690 329 RGMENAHIVRPGYAIEYDYFD-PRDLKYSLETKVIGGLFFAGQINGTTGYEEAGAQGLLAGTNAALRAQGRD 399
Cdd:PRK05335 296 PGLENAEFVRYGVMHRNTFINsPKLLDPTLQLKKRPNLFFAGQITGVEGYVESAASGLLAGINAARLALGKE 367
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| MnmG |
COG0445 |
tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal ... |
1-625 |
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: 1275.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 1 MDFPSRFEVIVIGGGHAGTEAALASARMGVKTLLLTHNVETLGQMSCNPAIGGIGKSHLVKEIDALGGAMAMATDKGGIQ 80
Cdd:COG0445 1 MYYPKEYDVIVVGGGHAGCEAALAAARMGAKTLLLTHNLDTIGQMSCNPAIGGIAKGHLVREIDALGGEMGRAADKTGIQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 81 FRVLNSRKGPAVRATRAQADRVLYKAAIRETLENQPNLWIFQQACDDLIVEQDQVRGVVTQMGMRIFADSVVLTTGTFLG 160
Cdd:COG0445 81 FRMLNTSKGPAVRAPRAQADRKLYRAAMRETLENQPNLDLIQGEVEDLIVEDGRVTGVVTADGIEFRAKAVVLTTGTFLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 161 GLIHIGMQNYSGGRAGDPPSIALAQRLRELPLRVGRLKTGTPPRIDGRSVDFSVMTEQPGDTPIPVMSFLgNKEQHPPQV 240
Cdd:COG0445 161 GLIHIGEKSYPGGRAGEPPSVGLSESLRELGFELGRLKTGTPPRIDGRSIDFSKLEEQPGDEPPPPFSFL-TEKIHPPQI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 241 SCWITHTNARTHEIIASNLDRSPMYSGVIEGIGPRYCPSIEDKIHRFADKESHQVFIEPEGLTTHELYPNGISTSLPFDV 320
Cdd:COG0445 240 PCWITYTNEETHEIIRENLHRSPMYSGVIEGVGPRYCPSIEDKIVRFADKDRHQIFLEPEGLDTNEVYPNGISTSLPEDV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 321 QLQIVQSIRGMENAHIVRPGYAIEYDYFDPRDLKYSLETKVIGGLFFAGQINGTTGYEEAGAQGLLAGTNAALRAQGRDS 400
Cdd:COG0445 320 QLAMLRSIPGLENAEILRPGYAIEYDYVDPTQLKPTLETKKIEGLFFAGQINGTTGYEEAAAQGLMAGINAALKAQGKEP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 401 WCPRRDEAYIGVLVDDLITLGTQEPYRMFTSRAEYRLILREDNADLRLTEKGRELGLVDDARWAAFCTKRESIELEEQRL 480
Cdd:COG0445 400 FILDRSEAYIGVLIDDLVTKGTDEPYRMFTSRAEYRLLLRQDNADLRLTEKGYELGLVSDERYERFEEKKEAIEEEIERL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 481 KSTWVRPGTEQGDAIAAHFGTPLTHEYNLLNLLTRPEIDYASLISITGQG-CIDPQVAEQVEIKTKYAGYIDRQQDEIAR 559
Cdd:COG0445 480 KSTRVTPNEEVNEGLEELGSSPLKRGVSLFDLLRRPEITYEDLAELDPELpDLDPEVAEQVEIEIKYEGYIERQEEEIEK 559
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489516690 560 LRASEDTGLPEDIDYAAISGLSKEIQSKLGITRPQTLGQASRIPGVTPAAISLLMIHLKKRGAGRQ 625
Cdd:COG0445 560 LKRLENLKIPEDFDYDAIPGLSNEAREKLKKIRPETLGQASRISGVTPADISLLLVYLKRRRRRKK 625
|
|
| gidA |
TIGR00136 |
glucose-inhibited division protein A; GidA, the longer of two forms of GidA-related proteins, ... |
7-621 |
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: 997.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 7 FEVIVIGGGHAGTEAALASARMGVKTLLLTHNVETLGQMSCNPAIGGIGKSHLVKEIDALGGAMAMATDKGGIQFRVLNS 86
Cdd:TIGR00136 1 FDVIVIGGGHAGCEAALAAARLGAKTLLLTLNLDTIGKCSCNPAIGGPAKGILVKEIDALGGEMGKAADKTGLQFRVLNS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 87 RKGPAVRATRAQADRVLYKAAIRETLENQPNLWIFQQACDDLIVEQ-DQVRGVVTQMGMRIFADSVVLTTGTFLGGLIHI 165
Cdd:TIGR00136 81 SKGPAVRATRAQIDKILYQKWMRNQLENQPNLSLFQGEVEDLILEDnDEIKGVVTKDGNEFRAKAVIITTGTFLRGKIHI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 166 GMQNYSGGRAGDPPSIALAQRLRELPLRVGRLKTGTPPRIDGRSVDFSVMTEQPGDTPIPVMSFLgNKEQHPPQVSCWIT 245
Cdd:TIGR00136 161 GDKSYEAGRAGEQASYGLSTTLRELGFKTGRLKTGTPPRIDKRSIDFSKLEVQFGDTQPPAFSFT-NKNFLPQQLPCYLT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 246 HTNARTHEIIASNLDRSPMYSGVIEGIGPRYCPSIEDKIHRFADKESHQVFIEPEGLTTHELYPNGISTSLPFDVQLQIV 325
Cdd:TIGR00136 240 HTNPKTHQIIRDNLHRSPMYSGSIEGNGPRYCPSIEDKVVRFADKERHQIFLEPEGLNSDEIYLNGLSTSLPEDVQLKII 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 326 QSIRGMENAHIVRPGYAIEYDYFDPRDLKYSLETKVIGGLFFAGQINGTTGYEEAGAQGLLAGTNAALRAQGRDSWCPRR 405
Cdd:TIGR00136 320 RSIPGLENAEILRPGYAIEYDYFDPTQLKPTLETKLIKGLFFAGQINGTTGYEEAAAQGLMAGINAALKLQNKEPFILKR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 406 DEAYIGVLVDDLITLGTQEPYRMFTSRAEYRLILREDNADLRLTEKGRELGLVDDARWAAFCTKRESIELEEQRLKSTWV 485
Cdd:TIGR00136 400 NEAYIGVLIDDLVTKGTKEPYRMFTSRAEYRLLLREDNADFRLTEIGRELGLIDEDRYARFLKKKQNIEEEIERLKSTRL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 486 RPGTEQGDAIAAHFGTPLTHEYNLLNLLTRPEIDYASLISIT-GQGCIDPQVAEQVEIKTKYAGYIDRQQDEIARLRASE 564
Cdd:TIGR00136 480 SPSKEVKEELKNLAQSPLKDEVSGYDLLKRPEMNLDKLTKLLpFLPPLDEEVLEQVEIEIKYEGYIKKQQQYIKKLDRLE 559
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 489516690 565 DTGLPEDIDYAAISGLSKEIQSKLGITRPQTLGQASRIPGVTPAAISLLMIHLKKRG 621
Cdd:TIGR00136 560 NVKIPADFDYRKIPGLSTEAREKLSKFRPLSLGQASRISGINPADISALLVYLKKQK 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: 693.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 9 VIVIGGGHAGTEAALASARMGVKTLLLTHNVETLGQMSCNPAIGGIGKSHLVKEIDALGGAMAMATDKGGIQFRVLNSRK 88
Cdd:pfam01134 2 VIVIGGGHAGCEAALAAARMGAKVLLITHNTDTIAELSCNPSIGGIAKGHLVREIDALGGLMGKAADKTGIQFRMLNTSK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 89 GPAVRATRAQADRVLYKAAIRETLENQPNLWIFQQACDDLIVEQDQVRGVVTQMGMRIFADSVVLTTGTFLGGLIHIGMQ 168
Cdd:pfam01134 82 GPAVRALRAQVDRDLYSKEMTETLENHPNLTLIQGEVTDLIPENGKVKGVVTEDGEEYKAKAVVLATGTFLNGKIHIGLK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 169 NYSGGRAGDPPSIALAQRLRELPLRVGRLKTGTPPRIDGRSVDFSVMTEQPGDTPIPVMSFLgNKEQHPPQVSCWITHTN 248
Cdd:pfam01134 162 CYPAGRLGELTSEGLSESLKELGFELGRFKTGTPPRIDKDSIDFSKLEEQPGDKPGPPFSYL-NCPMNKEQYPCFLTYTN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 249 ARTHEIIASNLDRSPMYSGVIEGIGPRYCPSIEDKIHRFADKESHQVFIEPEGLTTHELYPNGISTSLPFDVQLQIVQSI 328
Cdd:pfam01134 241 EATHEIIRDNLHRSPMFEGCIEGIGPRYCPSIEDKPVRFADKPYHQVFLEPEGLDTDEYYLVGFSTSLPEDVQKRVLRTI 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489516690 329 RGMENAHIVRPGYAIEYDYFDPRDLKYSLETKVIGGLFFAGQINGTTGYEEAGAQGLLAGTNAALRAQGRD 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 ... |
401-614 |
1.99e-119 |
|
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: 353.61 E-value: 1.99e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 401 WCPRRDEAYIGVLVDDLITLGTQEPYRMFTSRAEYRLILREDNADLRLTEKGRELGLVDDARWAAFCTKRESIELEEQRL 480
Cdd:pfam13932 1 LILSRSEAYIGVLIDDLVTKGTSEPYRMFTSRAEYRLLLRQDNADLRLTEKGRELGLVSDERYERFEEKKEAIEEEIERL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 481 KSTWVRPGTEQGDAIAAHfGTPLTHEYNLLNLLTRPEIDYASLIS-ITGQGCIDPQVAEQVEIKTKYAGYIDRQQDEIAR 559
Cdd:pfam13932 81 KSTRLSPSEWNNALLELG-SAPLGTGRSAFDLLRRPEVTYEDLAAlIPELAPLDPEVLEQVEIEAKYEGYIERQEAEIEK 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489516690 560 LRASEDTGLPEDIDYAAISGLSKEIQSKLGITRPQTLGQASRIPGVTPAAISLLM 614
Cdd:pfam13932 160 FKRLENLKIPEDLDYDAIPGLSNEAREKLNKIRPETIGQASRISGVTPADISVLL 214
|
|
| PRK05335 |
PRK05335 |
tRNA (uracil-5-)-methyltransferase Gid; Reviewed |
8-399 |
4.47e-14 |
|
tRNA (uracil-5-)-methyltransferase Gid; Reviewed
Pssm-ID: 235416 Cd Length: 436 Bit Score: 74.80 E-value: 4.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 8 EVIVIGGGHAGTEAALASARMGVKTLL-------LT--HNVETLGQMSCNPAIGGIGKSH----LVKEIDALGGA-MAMA 73
Cdd:PRK05335 4 PVNVIGAGLAGSEAAWQLAKRGVPVELyemrpvkKTpaHHTDGFAELVCSNSFRSDSLTNavglLKEEMRRLGSLiMEAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 74 tDKGgiqfrvlnsrkgpAVRATRAQA-DRVLYKAAIRETLENQPNLWIfqqacddliveqdqVRGVVTQmgmrIFADSVV 152
Cdd:PRK05335 84 -DAH-------------RVPAGGALAvDREGFSEYVTEALENHPLITV--------------IREEVTE----IPEDITI 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 153 LTTGtflgglihigmqnysggragdpP--SIALAQRLRELplrvgrlkTGTP---------PRIDGRSVDFSVmteqpgd 221
Cdd:PRK05335 132 IATG----------------------PltSDALAEAIKAL--------TGEDylyffdaaaPIVDKDSIDMDK------- 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 222 tpipvmsflgnkeqhppqvsCWIthtnartheiiASNLDRS-------PM----YSGVIEGIgprycpsIEDKIHRFADK 290
Cdd:PRK05335 175 --------------------VYL-----------ASRYDKGeadylncPMtkeeYEAFYEAL-------IAAEKAELKDF 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 291 ESHQVF-----IE----------------PEGLT---THE----------------LYpN--GISTSLPFDVQLQIVQSI 328
Cdd:PRK05335 217 EKEKYFegcmpIEvmaergretlrfgpmkPVGLTdprTGKrpyavvqlrqdnaagtLY-NivGFQTKLKWGEQKRVFRMI 295
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489516690 329 RGMENAHIVRPGYAIEYDYFD-PRDLKYSLETKVIGGLFFAGQINGTTGYEEAGAQGLLAGTNAALRAQGRD 399
Cdd:PRK05335 296 PGLENAEFVRYGVMHRNTFINsPKLLDPTLQLKKRPNLFFAGQITGVEGYVESAASGLLAGINAARLALGKE 367
|
|
| TrmFO |
COG1206 |
Folate-dependent tRNA-U54 methylase TrmFO/GidA [Translation, ribosomal structure and ... |
8-399 |
1.43e-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: 70.09 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 8 EVIVIGGGHAGTEAALASARMGVKTLL-------LT--HNVETLGQMSC---------NPAIGgigkshLVK-EIDALGG 68
Cdd:COG1206 3 PVTVIGGGLAGSEAAWQLAERGVPVRLyemrpvkMTpaHKTDGFAELVCsnslrsddlTNAVG------LLKeEMRRLGS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 69 ---AMAMATdkggiqfrvlnsrkgpAVRATRAQA-DRVLYKAAIRETLENQPNLWIfqqacddliveqdqVRGVVTQmgm 144
Cdd:COG1206 77 limAAADAH----------------RVPAGGALAvDREGFSAAVTEKLENHPNITV--------------VREEVTE--- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 145 rIFAD-SVVLTTGtflgglihigmqnysggragdpP--SIALAQRLRELplrvgrlkTGTP---------PRIDGRSVDF 212
Cdd:COG1206 124 -IPEDgPVIIATG----------------------PltSDALAEAIQEL--------TGEEylyfydaiaPIVDADSIDM 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 213 SVmteqpgdtpipvmsflgnkeqhppqvsCWIthtnartheiiASnldrspmysgviegigpRY---------CPSIEDK 283
Cdd:COG1206 173 DK---------------------------AFR-----------AS-----------------RYdkgeadylnCPMTKEE 197
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 284 IHRF------ADK------ESHQVF-----IE----------------PEGLT---THE----------------LYpN- 310
Cdd:COG1206 198 YEAFyeallaAEKvelkdfEKEKYFegclpIEvmarrgrdtlrfgpmkPVGLTdprTGKrpyavvqlrqenaegtLY-Nl 276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 311 -GISTSLPFDVQLQIVQSIRGMENAHIVRPGyAIEYDYF--DPRDLKYSLETKVIGGLFFAGQINGTTGYEEAGAQGLLA 387
Cdd:COG1206 277 vGFQTKLKWGEQKRVFRMIPGLENAEFVRYG-VMHRNTFinSPKLLDPTLQLKARPNLFFAGQITGVEGYVESAASGLLA 355
|
490
....*....|..
gi 489516690 388 GTNAALRAQGRD 399
Cdd:COG1206 356 GINAARLLLGKE 367
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
9-156 |
6.52e-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: 55.31 E-value: 6.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 9 VIVIGGGHAGTEAALASARMGVKTLLlthnVETlgqmscNPAIGGIGKShlvkeidALGGAMAMATDK-----GGI--QF 81
Cdd:pfam12831 2 VVVVGGGPAGVAAAIAAARAGAKVLL----VER------RGFLGGMLTS-------GLVGPDMGFYLNkeqvvGGIarEF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 82 RVLNSRKGPAVRATRAQADRVLY-----KAAIRETLEnQPNL-WIFQQACDDLIVEQDQVRGVVTQM---GMRIFADSVV 152
Cdd:pfam12831 65 RQRLRARGGLPGPYGLRGGWVPFdpevaKAVLDEMLA-EAGVtVLLHTRVVGVVKEGGRITGVTVETkggRITIRAKVFI 143
|
....
gi 489516690 153 LTTG 156
Cdd:pfam12831 144 DATG 147
|
|
| PRK05329 |
PRK05329 |
glycerol-3-phosphate dehydrogenase subunit GlpB; |
6-46 |
7.11e-04 |
|
glycerol-3-phosphate dehydrogenase subunit GlpB;
Pssm-ID: 235412 Cd Length: 422 Bit Score: 42.53 E-value: 7.11e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 489516690 6 RFEVIVIGGGHAGTEAALASARMGVKTLLLTHNVETLGQMS 46
Cdd:PRK05329 2 KFDVLVIGGGLAGLTAALAAAEAGKRVALVAKGQGALHFSS 42
|
|
| GlpB |
COG3075 |
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism]; |
6-42 |
9.91e-04 |
|
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 442309 Cd Length: 415 Bit Score: 42.09 E-value: 9.91e-04
10 20 30
....*....|....*....|....*....|....*..
gi 489516690 6 RFEVIVIGGGHAGTEAALASARMGVKTLLLTHNVETL 42
Cdd:COG3075 2 KFDVVVIGGGLAGLTAAIRAAEAGLRVAIVSAGQSAL 38
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
7-156 |
9.93e-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: 42.13 E-value: 9.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 7 FEVIVIGGGHAGTEAALASARMGVKTLLLTHnVETLG----------QMSCNPAIGGIGK----SH---LVKEIDALG-- 67
Cdd:COG1053 4 YDVVVVGSGGAGLRAALEAAEAGLKVLVLEK-VPPRGghtaaaqggiNAAGTNVQKAAGEdspeEHfydTVKGGDGLAdq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 68 --------GAMAMA--TDKGGIQFRV-----LNSRKGPAVRATRAQADRV-------LYKAAIRETLEnqpnlwIFQQA- 124
Cdd:COG1053 83 dlvealaeEAPEAIdwLEAQGVPFSRtpdgrLPQFGGHSVGRTCYAGDGTghallatLYQAALRLGVE------IFTETe 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 489516690 125 CDDLIVEQDQVRGVVTQMG----MRIFADSVVLTTG 156
Cdd:COG1053 157 VLDLIVDDGRVVGVVARDRtgeiVRIRAKAVVLATG 192
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
7-35 |
2.26e-03 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 400379 [Multi-domain] Cd Length: 301 Bit Score: 40.38 E-value: 2.26e-03
10 20
....*....|....*....|....*....
gi 489516690 7 FEVIVIGGGHAGTEAALASARMGVKTLLL 35
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLI 29
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
9-53 |
2.90e-03 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 40.61 E-value: 2.90e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 489516690 9 VIVIGGGHAGTEAALASARMGVKTLLlthnVETlgqmscNPAIGG 53
Cdd:COG1148 143 ALVIGGGIAGMTAALELAEQGYEVYL----VEK------EPELGG 177
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
7-156 |
3.05e-03 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 40.10 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489516690 7 FEVIVIGGGHAGTEAALASARMGVKTLLLthnvetlgqmscnpaiggigkshlvkEIDALGGAMAMATD-------KGGI 79
Cdd:COG0492 1 YDVVIIGAGPAGLTAAIYAARAGLKTLVI--------------------------EGGEPGGQLATTKEienypgfPEGI 54
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489516690 80 QfrvlnsrkGPA-VRATRAQADRvlYKAAIR-ETLENqpnlwifqqacddlIVEQDQVRGVVTQMGMRIFADSVVLTTG 156
Cdd:COG0492 55 S--------GPElAERLREQAER--FGAEILlEEVTS--------------VDKDDGPFRVTTDDGTEYEAKAVIIATG 109
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
7-38 |
5.83e-03 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 39.49 E-value: 5.83e-03
10 20 30
....*....|....*....|....*....|..
gi 489516690 7 FEVIVIGGGHAGTEAALASARMGVKTLLLTHN 38
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKG 32
|
|
|