|
Name |
Accession |
Description |
Interval |
E-value |
| ASS |
cd01999 |
argininosuccinate_synthase (ASS); Argininosuccinate synthase (ASS; EC 6.3.4.5) is a urea cycle ... |
6-399 |
0e+00 |
|
argininosuccinate_synthase (ASS); Argininosuccinate synthase (ASS; EC 6.3.4.5) is a urea cycle enzyme that catalyzes the penultimate step in arginine biosynthesis: the ATP-dependent ligation of citrulline to aspartate to form argininosuccinate, AMP and pyrophosphate. In humans, a defect in the ASS gene causes citrullinemia, a genetic disease characterized by severe vomiting spells and mental retardation. ASS is a homotetrameric enzyme of about 400 amino-acid residues. An arginine residue seems to be important for the enzyme's catalytic mechanism. The sequences of ASS from various prokaryotes, archaeabacteria and eukaryotes show significant similarity.
Pssm-ID: 467503 Cd Length: 386 Bit Score: 600.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 6 KRCVLAYSGGLDTSCILAWLIEE-GWEVICYMANVGQEEDWDAAREKALKVGAKKVYVEDLREEFINDTVIPAAQANAIY 84
Cdd:cd01999 1 KKVVLAYSGGLDTSVILKWLKEEyGYEVIAFTADLGQGDEEEEIEEKALKLGAVKVYVVDLREEFAEDYIFPAIKANAIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 85 ENVYLLGTSLARPIIARRQIQIAEKENCIAVSHGCTGKGNDQVRFELAYYALKPDVQVIAPWRLPvffeRFAGRKDLLEY 164
Cdd:cd01999 81 EGRYPLGTALARPLIAKKLVEVAREEGATAVAHGCTGKGNDQVRFELAIKALAPDLKVIAPWRDW----NFLTRAEEIAY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 165 AAAKGIPVTQTTKKPWSMDENIVHCSYEAGILEDPSMTPPKDMWKLTVDPKDAPDEVEELSIHFEKGAPTKLeckDGTFS 244
Cdd:cd01999 157 AKKHGIPVPVTKKKPYSIDENLWGRSYEGGDLEDPWNEPPEDAFEWTVSPEKAPDEPEYVTIEFEKGVPVAV---NGEKL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 245 GVVSIFYQLNAIARRNGVGRIDIVENRFSGLKSRGCYETPGLTILRTAHMDLEGLTMEREVRALRDqFVTFNLAKILYNG 324
Cdd:cd01999 234 DPVELIEKLNEIAGRHGVGRIDIVENRLVGIKSRGVYEAPGATLLIKAHRDLEDLTLDREVLHFKD-IVSRKYAELVYNG 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19111975 325 QFFSPCTRMLLAANNVSQEVVNGVVKLSVYKGNVTVLGRKSDTAhLYDEKLSSMDELGGFDPTWTSGFIQIESMR 399
Cdd:cd01999 313 LWFDPLREALEAFIDKTQERVTGEVRLKLYKGNVIVVGRESPNS-LYSEELATYEEGDGFDQKDAEGFIKIHGLQ 386
|
|
| ArgG |
COG0137 |
Argininosuccinate synthase [Amino acid transport and metabolism]; Argininosuccinate synthase ... |
6-401 |
0e+00 |
|
Argininosuccinate synthase [Amino acid transport and metabolism]; Argininosuccinate synthase is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 439907 Cd Length: 397 Bit Score: 588.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 6 KRCVLAYSGGLDTSCILAWLIEE-GWEVICYMANVGQEEDWDAAREKALKVGAKKVYVEDLREEFINDTVIPAAQANAIY 84
Cdd:COG0137 1 KKVVLAYSGGLDTSVIIPWLKEKyGYEVIAVTADVGQGEDLEAIEEKALKLGASKAYVVDAREEFVEDYVFPAIKANALY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 85 ENVYLLGTSLARPIIARRQIQIAEKENCIAVSHGCTGKGNDQVRFELAYYALKPDVQVIAPWRLPvffeRFAGRKDLLEY 164
Cdd:COG0137 81 EGKYPLGTALARPLIAKKLVEIAREEGADAVAHGCTGKGNDQVRFELAIRALAPDLKIIAPWREW----DLKSREEEIEY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 165 AAAKGIPVTQTTKKPWSMDENIVHCSYEAGILEDPSMTPPKDMWKLTVDPKDAPDEVEELSIHFEKGAPTKLeckDGTFS 244
Cdd:COG0137 157 AEEHGIPVPATKEKPYSIDENLWGRSIEGGELEDPWNEPPEDAYEWTVSPEDAPDEPEYVTITFEKGVPVAL---NGEKL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 245 GVVSIFYQLNAIARRNGVGRIDIVENRFSGLKSRGCYETPGLTILRTAHMDLEGLTMEREVRALRDQfVTFNLAKILYNG 324
Cdd:COG0137 234 SPVELIEELNEIGGKHGVGRIDIVENRLVGIKSRGVYEAPGATILITAHRALESLTLDRETLHFKDI-LDQKYAELVYNG 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19111975 325 QFFSPCTRMLLAANNVSQEVVNGVVKLSVYKGNVTVLGRKSDTAhLYDEKLSSMDELGGFDPTWTSGFIQIESMRLR 401
Cdd:COG0137 313 LWFSPLREALDAFIDETQKRVTGTVRLKLYKGNATVVGRKSPYS-LYDEDLATYEEDDVFDQKDAEGFIKLFGLPLR 388
|
|
| PRK00509 |
PRK00509 |
argininosuccinate synthase; Provisional |
5-401 |
0e+00 |
|
argininosuccinate synthase; Provisional
Pssm-ID: 234785 Cd Length: 399 Bit Score: 580.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 5 VKRCVLAYSGGLDTSCILAWLIEE-GWEVICYMANVGQEEDWDAAREKALKVGAKKVYVEDLREEFINDTVIPAAQANAI 83
Cdd:PRK00509 2 KKKVVLAYSGGLDTSVIIKWLKETyGCEVIAFTADVGQGEELEPIREKALKSGASEIYVEDLREEFVRDYVFPAIRANAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 84 YENVYLLGTSLARPIIARRQIQIAEKENCIAVSHGCTGKGNDQVRFELAYYALKPDVQVIAPWRlpvffE-RFAGRKDLL 162
Cdd:PRK00509 82 YEGKYPLGTALARPLIAKKLVEIARKEGADAVAHGCTGKGNDQVRFELGIAALAPDLKVIAPWR-----EwDLKSREELI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 163 EYAAAKGIPVTQTTKKPWSMDENIVHCSYEAGILEDPSMTPPKDMWKLTVDPKDAPDEVEELSIHFEKGAPTKLeckDGT 242
Cdd:PRK00509 157 AYAEEHGIPIPVTKKSPYSIDANLWHRSIEGGILEDPWNEPPEDVYEWTVSPEDAPDEPEYVEIEFEKGVPVAI---NGE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 243 FSGVVSIFYQLNAIARRNGVGRIDIVENRFSGLKSRGCYETPGLTILRTAHMDLEGLTMEREVRALRDQfVTFNLAKILY 322
Cdd:PRK00509 234 ALSPAELIEELNELAGKHGIGRIDIVENRLVGIKSRGVYETPGGTILIKAHRALESLTLDREVAHFKDE-LEPKYAELVY 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19111975 323 NGQFFSPCTRMLLAANNVSQEVVNGVVKLSVYKGNVTVLGRKSDTAhLYDEKLSSMDELGGFDPTWTSGFIQIESMRLR 401
Cdd:PRK00509 313 NGLWFSPLREALQAFIDETQEHVTGEVRLKLYKGNAIVVGRKSPNS-LYDEDLATYEEDDVYDQKDAEGFIKLWGLPSK 390
|
|
| Arginosuc_synth |
pfam00764 |
Arginosuccinate synthase; This family contains a PP-loop motif. |
9-401 |
0e+00 |
|
Arginosuccinate synthase; This family contains a PP-loop motif.
Pssm-ID: 279148 Cd Length: 386 Bit Score: 532.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 9 VLAYSGGLDTSCILAWLIEE-GWEVICYMANVGQ-EEDWDAAREKALKVGAKKVYVEDLREEFINDTVIPAAQANAIYEN 86
Cdd:pfam00764 1 VLAYSGGLDTSVCIPWLKEQgGYEVIAVAVDVGQgGEDIDEAREKALKLGAVKHYVIDAKEEFVEDYIFPAIQANALYED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 87 VYLLGTSLARPIIARRQIQIAEKENCIAVSHGCTGKGNDQVRFELAYYALKPDVQVIAPWRLPVFFerfagRKDLLEYAA 166
Cdd:pfam00764 81 RYPLGTALARPLIAKKLVEAAKKEGASAVAHGCTGKGNDQVRFEVSFRSLAPDLKVIAPVRDPNLT-----REEEIEYAE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 167 AKGIPVTQTTKKPWSMDENIVHCSYEAGILEDPSMTPPKDMWKLTVDPKDAPDEVEELSIHFEKGAPTKLeckDGTFSGV 246
Cdd:pfam00764 156 EHGIPIPVTKKSPYSIDENLWGRSIEAGILEDPWNAPPEDIYEWTKDPAKAPDEPDIVEIGFEKGVPVAL---DGEPVSP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 247 VSIFYQLNAIARRNGVGRIDIVENRFSGLKSRGCYETPGLTILRTAHMDLEGLTMEREVRALRDQFVTfNLAKILYNGQF 326
Cdd:pfam00764 233 LELIEKLNEIAGAHGVGRIDIVEDRLVGIKSREIYEAPAATVLITAHRDLENLTLTREVLRFKRIVDQ-KWAELVYDGLW 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19111975 327 FSPCTRMLLAANNVSQEVVNGVVKLSVYKGNVTVLGRKSDTAhLYDEKLSSMDELGGFDPTWTSGFIQIESMRLR 401
Cdd:pfam00764 312 FSPLKEALDAFIDKTQERVTGTVRVKLHKGSAIVLGRRSPYS-LYDEELVSYDEGDTFDQTDATGFIKIHGLQAK 385
|
|
| argG |
TIGR00032 |
argininosuccinate synthase; argG in bacteria, ARG1 in Saccharomyces cerevisiae. There is a ... |
7-401 |
2.14e-170 |
|
argininosuccinate synthase; argG in bacteria, ARG1 in Saccharomyces cerevisiae. There is a very unusual clustering in the alignment, with a deep split between one cohort of E. coli, H. influenzae, and Streptomyces, and the other cohort of eukaryotes, archaea, and the rest of the eubacteria. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 199987 Cd Length: 394 Bit Score: 482.29 E-value: 2.14e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 7 RCVLAYSGGLDTSCILAWLIEEGWEVICYMANVGQ-EEDWDAAREKALKVGAKKVYVEDLREEFINDTVIPAAQANAIYE 85
Cdd:TIGR00032 1 KVVLAYSGGLDTSVCLKWLREKGYEVIAYTADVGQpEEDIDAIPEKALEYGAENHYTIDAREEFVKDYGFAAIQANAFYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 86 NVYLLGTSLARPIIARRQIQIAEKENCIAVSHGCTGKGNDQVRFELAYYALKPDVQVIAPWRLPVFFerfagRKDLLEYA 165
Cdd:TIGR00032 81 GTYPLSTALARPLIAKKLVEAAKKEGANAVAHGCTGKGNDQERFERSIRLLNPDLKVIAPWRDLNFT-----REEEIEYA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 166 AAKGIPVTQTTKKPWSMDENIVHCSYEAGILEDPSMTPPKDMWKLTVDP-KDAPDEVEELSIHFEKGAPTKLeckDGTFS 244
Cdd:TIGR00032 156 IQCGIPYPMSKEKPYSIDENLWGRSIEAGILEDPSTEPPEDIYMWTKFPdEATPDEPEVVTIDFEQGVPVAL---NGVSL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 245 GVVSIFYQLNAIARRNGVGRIDIVENRFSGLKSRGCYETPGLTILRTAHMDLEGLTMEREVRALRDqFVTFNLAKILYNG 324
Cdd:TIGR00032 233 DPVELILEANEIAGKHGVGRIDIIENRIIGLKSREIYEAPGAALLIIAHRDLETLTLTRDVLEFKD-IVEEQYSELIYQG 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19111975 325 QFFSPCTRMLLAANNVSQEVVNGVVKLSVYKGNVTVLGRKSDTAhLYDEKLSSMDELGGFDPTWTSGFIQIESMRLR 401
Cdd:TIGR00032 312 LWFDPLAEALDAFIRKTQERVTGTVRVKLFKGNAIVIGRTSPYS-LYDEELVSMEKDDVFDPRDAIGFITMRGLQIK 387
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ASS |
cd01999 |
argininosuccinate_synthase (ASS); Argininosuccinate synthase (ASS; EC 6.3.4.5) is a urea cycle ... |
6-399 |
0e+00 |
|
argininosuccinate_synthase (ASS); Argininosuccinate synthase (ASS; EC 6.3.4.5) is a urea cycle enzyme that catalyzes the penultimate step in arginine biosynthesis: the ATP-dependent ligation of citrulline to aspartate to form argininosuccinate, AMP and pyrophosphate. In humans, a defect in the ASS gene causes citrullinemia, a genetic disease characterized by severe vomiting spells and mental retardation. ASS is a homotetrameric enzyme of about 400 amino-acid residues. An arginine residue seems to be important for the enzyme's catalytic mechanism. The sequences of ASS from various prokaryotes, archaeabacteria and eukaryotes show significant similarity.
Pssm-ID: 467503 Cd Length: 386 Bit Score: 600.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 6 KRCVLAYSGGLDTSCILAWLIEE-GWEVICYMANVGQEEDWDAAREKALKVGAKKVYVEDLREEFINDTVIPAAQANAIY 84
Cdd:cd01999 1 KKVVLAYSGGLDTSVILKWLKEEyGYEVIAFTADLGQGDEEEEIEEKALKLGAVKVYVVDLREEFAEDYIFPAIKANAIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 85 ENVYLLGTSLARPIIARRQIQIAEKENCIAVSHGCTGKGNDQVRFELAYYALKPDVQVIAPWRLPvffeRFAGRKDLLEY 164
Cdd:cd01999 81 EGRYPLGTALARPLIAKKLVEVAREEGATAVAHGCTGKGNDQVRFELAIKALAPDLKVIAPWRDW----NFLTRAEEIAY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 165 AAAKGIPVTQTTKKPWSMDENIVHCSYEAGILEDPSMTPPKDMWKLTVDPKDAPDEVEELSIHFEKGAPTKLeckDGTFS 244
Cdd:cd01999 157 AKKHGIPVPVTKKKPYSIDENLWGRSYEGGDLEDPWNEPPEDAFEWTVSPEKAPDEPEYVTIEFEKGVPVAV---NGEKL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 245 GVVSIFYQLNAIARRNGVGRIDIVENRFSGLKSRGCYETPGLTILRTAHMDLEGLTMEREVRALRDqFVTFNLAKILYNG 324
Cdd:cd01999 234 DPVELIEKLNEIAGRHGVGRIDIVENRLVGIKSRGVYEAPGATLLIKAHRDLEDLTLDREVLHFKD-IVSRKYAELVYNG 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19111975 325 QFFSPCTRMLLAANNVSQEVVNGVVKLSVYKGNVTVLGRKSDTAhLYDEKLSSMDELGGFDPTWTSGFIQIESMR 399
Cdd:cd01999 313 LWFDPLREALEAFIDKTQERVTGEVRLKLYKGNVIVVGRESPNS-LYSEELATYEEGDGFDQKDAEGFIKIHGLQ 386
|
|
| ArgG |
COG0137 |
Argininosuccinate synthase [Amino acid transport and metabolism]; Argininosuccinate synthase ... |
6-401 |
0e+00 |
|
Argininosuccinate synthase [Amino acid transport and metabolism]; Argininosuccinate synthase is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 439907 Cd Length: 397 Bit Score: 588.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 6 KRCVLAYSGGLDTSCILAWLIEE-GWEVICYMANVGQEEDWDAAREKALKVGAKKVYVEDLREEFINDTVIPAAQANAIY 84
Cdd:COG0137 1 KKVVLAYSGGLDTSVIIPWLKEKyGYEVIAVTADVGQGEDLEAIEEKALKLGASKAYVVDAREEFVEDYVFPAIKANALY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 85 ENVYLLGTSLARPIIARRQIQIAEKENCIAVSHGCTGKGNDQVRFELAYYALKPDVQVIAPWRLPvffeRFAGRKDLLEY 164
Cdd:COG0137 81 EGKYPLGTALARPLIAKKLVEIAREEGADAVAHGCTGKGNDQVRFELAIRALAPDLKIIAPWREW----DLKSREEEIEY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 165 AAAKGIPVTQTTKKPWSMDENIVHCSYEAGILEDPSMTPPKDMWKLTVDPKDAPDEVEELSIHFEKGAPTKLeckDGTFS 244
Cdd:COG0137 157 AEEHGIPVPATKEKPYSIDENLWGRSIEGGELEDPWNEPPEDAYEWTVSPEDAPDEPEYVTITFEKGVPVAL---NGEKL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 245 GVVSIFYQLNAIARRNGVGRIDIVENRFSGLKSRGCYETPGLTILRTAHMDLEGLTMEREVRALRDQfVTFNLAKILYNG 324
Cdd:COG0137 234 SPVELIEELNEIGGKHGVGRIDIVENRLVGIKSRGVYEAPGATILITAHRALESLTLDRETLHFKDI-LDQKYAELVYNG 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19111975 325 QFFSPCTRMLLAANNVSQEVVNGVVKLSVYKGNVTVLGRKSDTAhLYDEKLSSMDELGGFDPTWTSGFIQIESMRLR 401
Cdd:COG0137 313 LWFSPLREALDAFIDETQKRVTGTVRLKLYKGNATVVGRKSPYS-LYDEDLATYEEDDVFDQKDAEGFIKLFGLPLR 388
|
|
| PRK00509 |
PRK00509 |
argininosuccinate synthase; Provisional |
5-401 |
0e+00 |
|
argininosuccinate synthase; Provisional
Pssm-ID: 234785 Cd Length: 399 Bit Score: 580.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 5 VKRCVLAYSGGLDTSCILAWLIEE-GWEVICYMANVGQEEDWDAAREKALKVGAKKVYVEDLREEFINDTVIPAAQANAI 83
Cdd:PRK00509 2 KKKVVLAYSGGLDTSVIIKWLKETyGCEVIAFTADVGQGEELEPIREKALKSGASEIYVEDLREEFVRDYVFPAIRANAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 84 YENVYLLGTSLARPIIARRQIQIAEKENCIAVSHGCTGKGNDQVRFELAYYALKPDVQVIAPWRlpvffE-RFAGRKDLL 162
Cdd:PRK00509 82 YEGKYPLGTALARPLIAKKLVEIARKEGADAVAHGCTGKGNDQVRFELGIAALAPDLKVIAPWR-----EwDLKSREELI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 163 EYAAAKGIPVTQTTKKPWSMDENIVHCSYEAGILEDPSMTPPKDMWKLTVDPKDAPDEVEELSIHFEKGAPTKLeckDGT 242
Cdd:PRK00509 157 AYAEEHGIPIPVTKKSPYSIDANLWHRSIEGGILEDPWNEPPEDVYEWTVSPEDAPDEPEYVEIEFEKGVPVAI---NGE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 243 FSGVVSIFYQLNAIARRNGVGRIDIVENRFSGLKSRGCYETPGLTILRTAHMDLEGLTMEREVRALRDQfVTFNLAKILY 322
Cdd:PRK00509 234 ALSPAELIEELNELAGKHGIGRIDIVENRLVGIKSRGVYETPGGTILIKAHRALESLTLDREVAHFKDE-LEPKYAELVY 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19111975 323 NGQFFSPCTRMLLAANNVSQEVVNGVVKLSVYKGNVTVLGRKSDTAhLYDEKLSSMDELGGFDPTWTSGFIQIESMRLR 401
Cdd:PRK00509 313 NGLWFSPLREALQAFIDETQEHVTGEVRLKLYKGNAIVVGRKSPNS-LYDEDLATYEEDDVYDQKDAEGFIKLWGLPSK 390
|
|
| Arginosuc_synth |
pfam00764 |
Arginosuccinate synthase; This family contains a PP-loop motif. |
9-401 |
0e+00 |
|
Arginosuccinate synthase; This family contains a PP-loop motif.
Pssm-ID: 279148 Cd Length: 386 Bit Score: 532.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 9 VLAYSGGLDTSCILAWLIEE-GWEVICYMANVGQ-EEDWDAAREKALKVGAKKVYVEDLREEFINDTVIPAAQANAIYEN 86
Cdd:pfam00764 1 VLAYSGGLDTSVCIPWLKEQgGYEVIAVAVDVGQgGEDIDEAREKALKLGAVKHYVIDAKEEFVEDYIFPAIQANALYED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 87 VYLLGTSLARPIIARRQIQIAEKENCIAVSHGCTGKGNDQVRFELAYYALKPDVQVIAPWRLPVFFerfagRKDLLEYAA 166
Cdd:pfam00764 81 RYPLGTALARPLIAKKLVEAAKKEGASAVAHGCTGKGNDQVRFEVSFRSLAPDLKVIAPVRDPNLT-----REEEIEYAE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 167 AKGIPVTQTTKKPWSMDENIVHCSYEAGILEDPSMTPPKDMWKLTVDPKDAPDEVEELSIHFEKGAPTKLeckDGTFSGV 246
Cdd:pfam00764 156 EHGIPIPVTKKSPYSIDENLWGRSIEAGILEDPWNAPPEDIYEWTKDPAKAPDEPDIVEIGFEKGVPVAL---DGEPVSP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 247 VSIFYQLNAIARRNGVGRIDIVENRFSGLKSRGCYETPGLTILRTAHMDLEGLTMEREVRALRDQFVTfNLAKILYNGQF 326
Cdd:pfam00764 233 LELIEKLNEIAGAHGVGRIDIVEDRLVGIKSREIYEAPAATVLITAHRDLENLTLTREVLRFKRIVDQ-KWAELVYDGLW 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19111975 327 FSPCTRMLLAANNVSQEVVNGVVKLSVYKGNVTVLGRKSDTAhLYDEKLSSMDELGGFDPTWTSGFIQIESMRLR 401
Cdd:pfam00764 312 FSPLKEALDAFIDKTQERVTGTVRVKLHKGSAIVLGRRSPYS-LYDEELVSYDEGDTFDQTDATGFIKIHGLQAK 385
|
|
| PLN00200 |
PLN00200 |
argininosuccinate synthase; Provisional |
1-401 |
2.29e-174 |
|
argininosuccinate synthase; Provisional
Pssm-ID: 177791 Cd Length: 404 Bit Score: 492.72 E-value: 2.29e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 1 MPQEVKRCVLAYSGGLDTSCILAWLIEE-GWEVICYMANVGQ-EEDWDAAREKALKVGAKKVYVEDLREEFINDTVIPAA 78
Cdd:PLN00200 1 LRGKLNKVVLAYSGGLDTSVILKWLRENyGCEVVCFTADVGQgIEELEGLEAKAKASGAKQLVVKDLREEFVRDYIFPCL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 79 QANAIYENVYLLGTSLARPIIARRQIQIAEKENCIAVSHGCTGKGNDQVRFELAYYALKPDVQVIAPWRlpvffE-RFAG 157
Cdd:PLN00200 81 RANAIYEGKYLLGTSMARPLIAKAMVDIAKEVGADAVAHGATGKGNDQVRFELTFFALNPELKVVAPWR-----EwDIKG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 158 RKDLLEYAAAKGIPVTQTTKKPWSMDENIVHCSYEAGILEDPSMTPPKDMWKLTVDPKDAPDEVEELSIHFEKGAPTKLe 237
Cdd:PLN00200 156 REDLIEYAKKHNIPVPVTKKSIYSRDRNLWHISYEGDILEDPANEPKEDMFMMSVSPEAAPDQPEYIEIEFEKGLPVAI- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 238 ckDGTFSGVVSIFYQLNAIARRNGVGRIDIVENRFSGLKSRGCYETPGLTILRTAHMDLEGLTMEREVRALRDQfVTFNL 317
Cdd:PLN00200 235 --NGKTLSPATLLTKLNEIGGKHGIGRIDMVENRFVGMKSRGVYETPGGTILFAAHRELESLTLDRETMQVKDS-LALKY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 318 AKILYNGQFFSPCTRMLLAANNVSQEVVNGVVKLSVYKGNVTVLGRKSDTAhLYDEKLSSMDELGG-FDPTWTSGFIQIE 396
Cdd:PLN00200 312 AELVYNGFWFDPERESMDAFMEKITETTTGSVRLKLYKGNVSVAGRKSPYS-LYRQDISSFEEGGGiYNQADAAGFIRLY 390
|
....*
gi 19111975 397 SMRLR 401
Cdd:PLN00200 391 ALRLR 395
|
|
| argG |
TIGR00032 |
argininosuccinate synthase; argG in bacteria, ARG1 in Saccharomyces cerevisiae. There is a ... |
7-401 |
2.14e-170 |
|
argininosuccinate synthase; argG in bacteria, ARG1 in Saccharomyces cerevisiae. There is a very unusual clustering in the alignment, with a deep split between one cohort of E. coli, H. influenzae, and Streptomyces, and the other cohort of eukaryotes, archaea, and the rest of the eubacteria. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 199987 Cd Length: 394 Bit Score: 482.29 E-value: 2.14e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 7 RCVLAYSGGLDTSCILAWLIEEGWEVICYMANVGQ-EEDWDAAREKALKVGAKKVYVEDLREEFINDTVIPAAQANAIYE 85
Cdd:TIGR00032 1 KVVLAYSGGLDTSVCLKWLREKGYEVIAYTADVGQpEEDIDAIPEKALEYGAENHYTIDAREEFVKDYGFAAIQANAFYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 86 NVYLLGTSLARPIIARRQIQIAEKENCIAVSHGCTGKGNDQVRFELAYYALKPDVQVIAPWRLPVFFerfagRKDLLEYA 165
Cdd:TIGR00032 81 GTYPLSTALARPLIAKKLVEAAKKEGANAVAHGCTGKGNDQERFERSIRLLNPDLKVIAPWRDLNFT-----REEEIEYA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 166 AAKGIPVTQTTKKPWSMDENIVHCSYEAGILEDPSMTPPKDMWKLTVDP-KDAPDEVEELSIHFEKGAPTKLeckDGTFS 244
Cdd:TIGR00032 156 IQCGIPYPMSKEKPYSIDENLWGRSIEAGILEDPSTEPPEDIYMWTKFPdEATPDEPEVVTIDFEQGVPVAL---NGVSL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 245 GVVSIFYQLNAIARRNGVGRIDIVENRFSGLKSRGCYETPGLTILRTAHMDLEGLTMEREVRALRDqFVTFNLAKILYNG 324
Cdd:TIGR00032 233 DPVELILEANEIAGKHGVGRIDIIENRIIGLKSREIYEAPGAALLIIAHRDLETLTLTRDVLEFKD-IVEEQYSELIYQG 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19111975 325 QFFSPCTRMLLAANNVSQEVVNGVVKLSVYKGNVTVLGRKSDTAhLYDEKLSSMDELGGFDPTWTSGFIQIESMRLR 401
Cdd:TIGR00032 312 LWFDPLAEALDAFIRKTQERVTGTVRVKLFKGNAIVIGRTSPYS-LYDEELVSMEKDDVFDPRDAIGFITMRGLQIK 387
|
|
| PRK13820 |
PRK13820 |
argininosuccinate synthase; Provisional |
4-380 |
4.27e-126 |
|
argininosuccinate synthase; Provisional
Pssm-ID: 237521 Cd Length: 394 Bit Score: 369.64 E-value: 4.27e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 4 EVKRCVLAYSGGLDTSCILAWLIEE-GW-EVICYMANVGQ-EEDWDAAREKALKVGAKKvYVEDLREEFINDTVIPAAQA 80
Cdd:PRK13820 1 MMKKVVLAYSGGLDTSVCVPLLKEKyGYdEVITVTVDVGQpEEEIKEAEEKAKKLGDKH-YTIDAKEEFAKDYIFPAIKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 81 NAIYENvYLLGTSLARPIIARRQIQIAEKENCIAVSHGCTGKGNDQVRFELAYYAlkPDVQVIAPWRlpvffERFAGRKD 160
Cdd:PRK13820 80 NALYEG-YPLGTALARPLIAEKIVEVAEKEGASAIAHGCTGKGNDQLRFEAVFRA--SDLEVIAPIR-----ELNLTREW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 161 LLEYAAAKGIPVTQTTKKPWSMDENIVHCSYEAGILEDPSMTPPKDMWKLTVDPKDAPDEVEELSIHFEKGAPTKLeckD 240
Cdd:PRK13820 152 EIEYAKEKGIPVPVGKEKPWSIDENLWSRSIEGGKLEDPAFEPPEEIYAWTVSPEDAPDEPEIVEIEFEEGVPVAI---N 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 241 GTFSGVVSIFYQLNAIARRNGVGRIDIVENRFSGLKSRGCYETPGLTILRTAHMDLEGLTMEREVRALRdQFVTFNLAKI 320
Cdd:PRK13820 229 GEKMDGVELIRKLNEIAGKHGVGRTDMMEDRVLGLKSRENYEHPAATVLLTAHKALEQLVLTREELKFK-EIVDSKWAEL 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 321 LYNGQFFSPCTRMLLAANNVSQEVVNGVVKLSVYKGNVTVLGRKSDTAhLYDEKLSSMDE 380
Cdd:PRK13820 308 AYEGLVDEPLREDLNAFIDKTQERVTGTVTVKLYKGSARVVGRESPYA-LYSEELVSFDS 366
|
|
| PRK04527 |
PRK04527 |
argininosuccinate synthase; Provisional |
6-398 |
2.73e-47 |
|
argininosuccinate synthase; Provisional
Pssm-ID: 235305 Cd Length: 400 Bit Score: 166.55 E-value: 2.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 6 KRCVLAYSGGLDTSCILAWLIEEGWEVICYMANVG--QEEDWDAAREKALKVGAKKVYVEDLREEFINDTVIPAAQANAI 83
Cdd:PRK04527 3 KDIVLAFSGGLDTSFCIPYLQERGYAVHTVFADTGgvDAEERDFIEKRAAELGAASHVTVDGGPAIWEGFVKPLVWAGEG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 84 YENVYLLGTSlARPIIARRQIQIAEKENCIAVSHGCTGKGNDQVRFELAYYALKpDVQVIAPWRlPVFFERFAGRKDLLE 163
Cdd:PRK04527 83 YQGQYPLLVS-DRYLIVDAALKRAEELGTRIIAHGCTGMGNDQVRFDLAVKALG-DYQIVAPIR-EIQKEHTQTRAYEQK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 164 YAAAKGIPVtQTTKKPWSMDENIVHCSYEAGILeDPSMTPPKDMWKLTVDPKDAPDEVEELSIHFEKGAPTKLeckDGTF 243
Cdd:PRK04527 160 YLEERGFGV-RAKQKAYTINENLLGVTMSGGEI-DRWEAPGEGARGWCAPRSAWPTEALTVTIKFVEGEAVAL---DGKP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 244 SGVVSIFYQLNAIARRNGVGRIDIVENRFSGLKSRGCYETPGLTILRTAHMDLEGLTMEREVRALRDQfVTFNLAKILYN 323
Cdd:PRK04527 235 LPGAQILAKLNKLFAQYGVGRGVYTGDTVIGLKGRIVFEAPGLVSLLTAHRALEDAVLTKQQNRFKPD-VARKWVELVYE 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19111975 324 GQFFSPCTRMLLAANNVSQEVVNGVVKLSVYKGNVTVLGRKSdtAHLYDEKLSSMDELGGFDPTWTSGFIQIESM 398
Cdd:PRK04527 314 GFYHDPLKTDIEAFLKSSQAKVNGEVTLETRGGRVDAVAVRS--PHLLNSKGATYAQSADWGVEEAEGFIKLFGM 386
|
|
| PRK05370 |
PRK05370 |
argininosuccinate synthase; Validated |
10-404 |
3.31e-43 |
|
argininosuccinate synthase; Validated
Pssm-ID: 235434 Cd Length: 447 Bit Score: 156.67 E-value: 3.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 10 LAYSGGLDTSCILAWLIEEGWEVICYMANVGQ--EEDWDAAREKALKVGAKKVYVEDLREEFINDTvIPAAQANA----- 82
Cdd:PRK05370 16 IAFSGGLDTSAALLWMRQKGAVPYAYTANLGQpdEDDYDAIPRRAMEYGAENARLIDCRAQLVAEG-IAAIQCGAfhist 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 83 ---IYENVYLLGTSLARPIIARrqiqiAEKENCIAV-SHGCTGKGNDQVRFelaY-YAL--KPDVQVIAPWRLPVFFERF 155
Cdd:PRK05370 95 ggvTYFNTTPLGRAVTGTMLVA-----AMKEDGVNIwGDGSTYKGNDIERF---YrYGLltNPELKIYKPWLDQDFIDEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 156 AGRKDLLEYAAAKGIPVTQTTKKPWSMDENIVHCSYEAGILE---------DPSMTPPkdMWKLTVDPKdapdeVEELSI 226
Cdd:PRK05370 167 GGRAEMSEFLIAHGFDYKMSVEKAYSTDSNMLGATHEAKDLEhlnsgikivNPIMGVA--FWDEDVEIK-----AEEVTV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 227 HFEKGAPTKLECKdgTFSGVVSIFYQLNAIARRNGVGRIDIVENRFSGLKSRGCYETPGLTILRTAHmdlegltmEREVR 306
Cdd:PRK05370 240 RFEQGRPVALNGK--TFSDPVELMLEANRIGGRHGLGMSDQIENRIIEAKSRGIYEAPGMALLHIAY--------ERLVT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 307 ALR-----DQFVT--FNLAKILYNGQFFSPCTRMLL-AANNVSQEVVNGVVKLSVYKGN-VTVLGRKSDTAHLYDEKLsS 377
Cdd:PRK05370 310 GIHnedtiEQYRIngRRLGRLLYQGRWFDPQALMLReSLQRWVASAITGEVTLELRRGNdYSILNTVSPNLTYKPERL-S 388
|
410 420
....*....|....*....|....*....
gi 19111975 378 MD--ELGGFDPTwtsgfIQIESMRLRNSD 404
Cdd:PRK05370 389 MEkvESAAFSPD-----DRIGQLTMRNLD 412
|
|
| PRK14664 |
PRK14664 |
tRNA-specific 2-thiouridylase MnmA; Provisional |
1-119 |
5.79e-05 |
|
tRNA-specific 2-thiouridylase MnmA; Provisional
Pssm-ID: 173127 [Multi-domain] Cd Length: 362 Bit Score: 44.94 E-value: 5.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 1 MPQEVKRCVLAYSGGLDTSCILAWLIEEGWEVICYMANVGQEEDWDaAREKALKVGAKKvYVEDLREEFiNDTVIpaaqA 80
Cdd:PRK14664 1 MKESKKRVLVGMSGGIDSTATCLMLQEQGYEIVGVTMRVWGDEPQD-ARELAARMGIEH-YVADERVPF-KDTIV----K 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 19111975 81 NAIYEnvYLLGTS-----LARPIIARRQ-IQIAEKENC--IAVSHGC 119
Cdd:PRK14664 74 NFIDE--YRQGRTpnpcvMCNPLFKFRMlIEWADKLGCawIATGHYS 118
|
|
| QueC-like |
cd01995 |
7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC ... |
6-66 |
1.26e-04 |
|
7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC 6.3.4.20) is also called 7-cyano-7-carbaguanine synthase, preQ(0) synthase, or queuosine biosynthesis protein QueC. It catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)), as part of the biosynthesis pathway of queuosine (Q). Q is one of the most complex modifications occurring at the wobble position of tRNAs with GUN anticodons, and is implicated in a number of biological activities, including accuracy of decoding, virulence, and cellular differentiation. This subfamily belongs to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.
Pssm-ID: 467499 [Multi-domain] Cd Length: 208 Bit Score: 42.99 E-value: 1.26e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19111975 6 KRCVLAYSGGLDTSCILAWLIEEGWEVICYMANVGQ----EEdwDAAREKALKVGAKKVYVEDLR 66
Cdd:cd01995 1 MKAVVLLSGGLDSTTLLYWALKEGYEVHALTFDYGQrhakEE--LEAAKLIAKLLGIEHKVIDLS 63
|
|
| QueC |
COG0603 |
7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and ... |
6-65 |
5.69e-04 |
|
7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and biogenesis]; 7-cyano-7-deazaguanine synthase (queuosine biosynthesis) is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440368 [Multi-domain] Cd Length: 223 Bit Score: 40.92 E-value: 5.69e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19111975 6 KRCVLAYSGGLDTSCILAWLIEEGWEVIC----YmanvGQEED--WDAAREKALKVGAKKVYVEDL 65
Cdd:COG0603 3 KKAVVLLSGGLDSTTCLAWALARGYEVYAlsfdY----GQRHRkeLEAARRIAKALGVGEHKVIDL 64
|
|
| mnmA |
PRK00143 |
tRNA-specific 2-thiouridylase MnmA; Reviewed |
6-75 |
9.91e-04 |
|
tRNA-specific 2-thiouridylase MnmA; Reviewed
Pssm-ID: 234664 [Multi-domain] Cd Length: 346 Bit Score: 40.82 E-value: 9.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 6 KRCVLAYSGGLDTSCILAWLIEEGWEVIC-YMAN------VG-----QEEDWDAAREKALKVGAkKVYVEDLREEFiNDT 73
Cdd:PRK00143 1 KRVVVGMSGGVDSSVAAALLKEQGYEVIGvFMKLwddddeTGkggccAEEDIADARRVADKLGI-PHYVVDFEKEF-WDR 78
|
..
gi 19111975 74 VI 75
Cdd:PRK00143 79 VI 80
|
|
| TilS |
COG0037 |
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ... |
1-172 |
1.19e-03 |
|
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA(Ile)-lysidine synthase TilS/MesJ is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 439807 [Multi-domain] Cd Length: 235 Bit Score: 40.20 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 1 MPQEVKRCVLAYSGGLDTSCILAWLIEE----GWEVICYMANVGQ----EEDWDAARE--KALKVgakKVYVEDLREEFI 70
Cdd:COG0037 11 LLEPGDRILVAVSGGKDSLALLHLLAKLrrrlGFELVAVHVDHGLreesDEDAEFVAElcEELGI---PLHVVRVDVPAI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111975 71 ndtVIPAAqanaiyENVYllgtSLARpiIARRQI--QIAEKENC--IAVSHgcTgkGNDQVrfE-----LAY----YALK 137
Cdd:COG0037 88 ---AKKEG------KSPE----AAAR--RARYGAlyELARELGAdkIATGH--H--LDDQA--EtfllnLLRgsglAGLA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 19111975 138 P-------DVQVIAPWrlpvffeRFAGRKDLLEYAAAKGIPV 172
Cdd:COG0037 147 GmppsrggGVRLIRPL-------LYVSRKEIEAYAKENGLPW 181
|
|
| QueC |
pfam06508 |
Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis ... |
7-58 |
1.67e-03 |
|
Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis of 7-carboxy-7-deazaguanine. They catalyze the conversion of 7-deaza-7-carboxyguanine to preQ0.
Pssm-ID: 428982 [Multi-domain] Cd Length: 210 Bit Score: 39.52 E-value: 1.67e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 19111975 7 RCVLAYSGGLDTSCILAWLIEEGWEVICYMANVGQEED--WDAAREKALKVGAK 58
Cdd:pfam06508 1 KAVVLLSGGLDSTTCLAWAKKEGYEVYALSFDYGQRHRkeLECAKKIAKALGVE 54
|
|
| |
