|
Name |
Accession |
Description |
Interval |
E-value |
| ArgG |
COG0137 |
Argininosuccinate synthase [Amino acid transport and metabolism]; Argininosuccinate synthase ... |
5-408 |
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: 593.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 5 KVCLAYSGGLDTSVILAWLLEQ-GYEVIAFMANIGQEEDFAAAEKKALAIGASKYVLVDVRKEFVEEVLFPAVQVNAVYE 83
Cdd:COG0137 2 KVVLAYSGGLDTSVIIPWLKEKyGYEVIAVTADVGQGEDLEAIEEKALKLGASKAYVVDAREEFVEDYVFPAIKANALYE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 84 NVYLLGTSLARPVIAKAQIEVAEKEGCFAVSHGCTGKGNDQVRFELSFYALKPDVKVIAPWRDPSfferFAGRKDLLDYA 163
Cdd:COG0137 82 GKYPLGTALARPLIAKKLVEIAREEGADAVAHGCTGKGNDQVRFELAIRALAPDLKIIAPWREWD----LKSREEEIEYA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 164 AQKGIPVTQTKAKPWSTDENMAHISFEAGILEDPDTTPPKDMWKLTVDPTDAPDEPEDFIVEFEKGIPKKLilsDGKEVT 243
Cdd:COG0137 158 EEHGIPVPATKEKPYSIDENLWGRSIEGGELEDPWNEPPEDAYEWTVSPEDAPDEPEYVTITFEKGVPVAL---NGEKLS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 244 ePVTLFITANAIGRRNGVGRIDIVENRFIGIKSRGCYETPGLTLLRSAHIDLEGLTLDREVRSIRDTfVTPTYSKLLYNG 323
Cdd:COG0137 235 -PVELIEELNEIGGKHGVGRIDIVENRLVGIKSRGVYEAPGATILITAHRALESLTLDRETLHFKDI-LDQKYAELVYNG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 324 MYFTPECEYVRSMIQPSQNTVNGLVRARCYKGSVIILGRSSSTEkLYDATESSMDELTGFQPQDASGFIAVQSIRIKKYG 403
Cdd:COG0137 313 LWFSPLREALDAFIDETQKRVTGTVRLKLYKGNATVVGRKSPYS-LYDEDLATYEEDDVFDQKDAEGFIKLFGLPLRVAA 391
|
....*
gi 2066107567 404 EKARE 408
Cdd:COG0137 392 RVRKK 396
|
|
| Arginosuc_synth |
pfam00764 |
Arginosuccinate synthase; This family contains a PP-loop motif. |
7-401 |
0e+00 |
|
Arginosuccinate synthase; This family contains a PP-loop motif.
Pssm-ID: 279148 Cd Length: 386 Bit Score: 587.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 7 CLAYSGGLDTSVILAWLLEQ-GYEVIAFMANIGQ-EEDFAAAEKKALAIGASKYVLVDVRKEFVEEVLFPAVQVNAVYEN 84
Cdd:pfam00764 1 VLAYSGGLDTSVCIPWLKEQgGYEVIAVAVDVGQgGEDIDEAREKALKLGAVKHYVIDAKEEFVEDYIFPAIQANALYED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 85 VYLLGTSLARPVIAKAQIEVAEKEGCFAVSHGCTGKGNDQVRFELSFYALKPDVKVIAPWRDPSFFerfagRKDLLDYAA 164
Cdd:pfam00764 81 RYPLGTALARPLIAKKLVEAAKKEGASAVAHGCTGKGNDQVRFEVSFRSLAPDLKVIAPVRDPNLT-----REEEIEYAE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 165 QKGIPVTQTKAKPWSTDENMAHISFEAGILEDPDTTPPKDMWKLTVDPTDAPDEPEDFIVEFEKGIPKKLilsDGKEVtE 244
Cdd:pfam00764 156 EHGIPIPVTKKSPYSIDENLWGRSIEAGILEDPWNAPPEDIYEWTKDPAKAPDEPDIVEIGFEKGVPVAL---DGEPV-S 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 245 PVTLFITANAIGRRNGVGRIDIVENRFIGIKSRGCYETPGLTLLRSAHIDLEGLTLDREVRSIRDTFVTPtYSKLLYNGM 324
Cdd:pfam00764 232 PLELIEKLNEIAGAHGVGRIDIVEDRLVGIKSREIYEAPAATVLITAHRDLENLTLTREVLRFKRIVDQK-WAELVYDGL 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2066107567 325 YFTPECEYVRSMIQPSQNTVNGLVRARCYKGSVIILGRSSSTEkLYDATESSMDELTGFQPQDASGFIAVQSIRIKK 401
Cdd:pfam00764 311 WFSPLKEALDAFIDKTQERVTGTVRVKLHKGSAIVLGRRSPYS-LYDEELVSYDEGDTFDQTDATGFIKIHGLQAKI 386
|
|
| ASS |
cd01999 |
argininosuccinate_synthase (ASS); Argininosuccinate synthase (ASS; EC 6.3.4.5) is a urea cycle ... |
4-398 |
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: 581.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 4 GKVCLAYSGGLDTSVILAWLLEQ-GYEVIAFMANIGQEEDFAAAEKKALAIGASKYVLVDVRKEFVEEVLFPAVQVNAVY 82
Cdd:cd01999 1 KKVVLAYSGGLDTSVILKWLKEEyGYEVIAFTADLGQGDEEEEIEEKALKLGAVKVYVVDLREEFAEDYIFPAIKANAIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 83 ENVYLLGTSLARPVIAKAQIEVAEKEGCFAVSHGCTGKGNDQVRFELSFYALKPDVKVIAPWRDPsffeRFAGRKDLLDY 162
Cdd:cd01999 81 EGRYPLGTALARPLIAKKLVEVAREEGATAVAHGCTGKGNDQVRFELAIKALAPDLKVIAPWRDW----NFLTRAEEIAY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 163 AAQKGIPVTQTKAKPWSTDENMAHISFEAGILEDPDTTPPKDMWKLTVDPTDAPDEPEDFIVEFEKGIPKKLilsDGkEV 242
Cdd:cd01999 157 AKKHGIPVPVTKKKPYSIDENLWGRSYEGGDLEDPWNEPPEDAFEWTVSPEKAPDEPEYVTIEFEKGVPVAV---NG-EK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 243 TEPVTLFITANAIGRRNGVGRIDIVENRFIGIKSRGCYETPGLTLLRSAHIDLEGLTLDREVRSIRDtFVTPTYSKLLYN 322
Cdd:cd01999 233 LDPVELIEKLNEIAGRHGVGRIDIVENRLVGIKSRGVYEAPGATLLIKAHRDLEDLTLDREVLHFKD-IVSRKYAELVYN 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2066107567 323 GMYFTPECEYVRSMIQPSQNTVNGLVRARCYKGSVIILGRSSSTeKLYDATESSMDELTGFQPQDASGFIAVQSIR 398
Cdd:cd01999 312 GLWFDPLREALEAFIDKTQERVTGEVRLKLYKGNVIVVGRESPN-SLYSEELATYEEGDGFDQKDAEGFIKIHGLQ 386
|
|
| argG |
TIGR00032 |
argininosuccinate synthase; argG in bacteria, ARG1 in Saccharomyces cerevisiae. There is a ... |
5-407 |
0e+00 |
|
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: 575.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 5 KVCLAYSGGLDTSVILAWLLEQGYEVIAFMANIGQ-EEDFAAAEKKALAIGASKYVLVDVRKEFVEEVLFPAVQVNAVYE 83
Cdd:TIGR00032 1 KVVLAYSGGLDTSVCLKWLREKGYEVIAYTADVGQpEEDIDAIPEKALEYGAENHYTIDAREEFVKDYGFAAIQANAFYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 84 NVYLLGTSLARPVIAKAQIEVAEKEGCFAVSHGCTGKGNDQVRFELSFYALKPDVKVIAPWRDPSFFerfagRKDLLDYA 163
Cdd:TIGR00032 81 GTYPLSTALARPLIAKKLVEAAKKEGANAVAHGCTGKGNDQERFERSIRLLNPDLKVIAPWRDLNFT-----REEEIEYA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 164 AQKGIPVTQTKAKPWSTDENMAHISFEAGILEDPDTTPPKDMWKLTVDPTDA-PDEPEDFIVEFEKGIPKKLilsDGKEV 242
Cdd:TIGR00032 156 IQCGIPYPMSKEKPYSIDENLWGRSIEAGILEDPSTEPPEDIYMWTKFPDEAtPDEPEVVTIDFEQGVPVAL---NGVSL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 243 tEPVTLFITANAIGRRNGVGRIDIVENRFIGIKSRGCYETPGLTLLRSAHIDLEGLTLDREVRSIRDtFVTPTYSKLLYN 322
Cdd:TIGR00032 233 -DPVELILEANEIAGKHGVGRIDIIENRIIGLKSREIYEAPGAALLIIAHRDLETLTLTRDVLEFKD-IVEEQYSELIYQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 323 GMYFTPECEYVRSMIQPSQNTVNGLVRARCYKGSVIILGRsSSTEKLYDATESSMDELTGFQPQDASGFIAVQSIRIKKY 402
Cdd:TIGR00032 311 GLWFDPLAEALDAFIRKTQERVTGTVRVKLFKGNAIVIGR-TSPYSLYDEELVSMEKDDVFDPRDAIGFITMRGLQIKDY 389
|
....*
gi 2066107567 403 GEKAR 407
Cdd:TIGR00032 390 REKKK 394
|
|
| PRK00509 |
PRK00509 |
argininosuccinate synthase; Provisional |
5-405 |
0e+00 |
|
argininosuccinate synthase; Provisional
Pssm-ID: 234785 Cd Length: 399 Bit Score: 568.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 5 KVCLAYSGGLDTSVILAWLLEQ-GYEVIAFMANIGQEEDFAAAEKKALAIGASKYVLVDVRKEFVEEVLFPAVQVNAVYE 83
Cdd:PRK00509 4 KVVLAYSGGLDTSVIIKWLKETyGCEVIAFTADVGQGEELEPIREKALKSGASEIYVEDLREEFVRDYVFPAIRANALYE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 84 NVYLLGTSLARPVIAKAQIEVAEKEGCFAVSHGCTGKGNDQVRFELSFYALKPDVKVIAPWRDpsffERFAGRKDLLDYA 163
Cdd:PRK00509 84 GKYPLGTALARPLIAKKLVEIARKEGADAVAHGCTGKGNDQVRFELGIAALAPDLKVIAPWRE----WDLKSREELIAYA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 164 AQKGIPVTQTKAKPWSTDENMAHISFEAGILEDPDTTPPKDMWKLTVDPTDAPDEPEDFIVEFEKGIPKKLilsDGKEVT 243
Cdd:PRK00509 160 EEHGIPIPVTKKSPYSIDANLWHRSIEGGILEDPWNEPPEDVYEWTVSPEDAPDEPEYVEIEFEKGVPVAI---NGEALS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 244 ePVTLFITANAIGRRNGVGRIDIVENRFIGIKSRGCYETPGLTLLRSAHIDLEGLTLDREVRSIRDTfVTPTYSKLLYNG 323
Cdd:PRK00509 237 -PAELIEELNELAGKHGIGRIDIVENRLVGIKSRGVYETPGGTILIKAHRALESLTLDREVAHFKDE-LEPKYAELVYNG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 324 MYFTPECEYVRSMIQPSQNTVNGLVRARCYKGSVIILGRsSSTEKLYDATESSMDELTGFQPQDASGFIAVQSIRIKKYG 403
Cdd:PRK00509 315 LWFSPLREALQAFIDETQEHVTGEVRLKLYKGNAIVVGR-KSPNSLYDEDLATYEEDDVYDQKDAEGFIKLWGLPSKIAA 393
|
..
gi 2066107567 404 EK 405
Cdd:PRK00509 394 LV 395
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ArgG |
COG0137 |
Argininosuccinate synthase [Amino acid transport and metabolism]; Argininosuccinate synthase ... |
5-408 |
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: 593.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 5 KVCLAYSGGLDTSVILAWLLEQ-GYEVIAFMANIGQEEDFAAAEKKALAIGASKYVLVDVRKEFVEEVLFPAVQVNAVYE 83
Cdd:COG0137 2 KVVLAYSGGLDTSVIIPWLKEKyGYEVIAVTADVGQGEDLEAIEEKALKLGASKAYVVDAREEFVEDYVFPAIKANALYE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 84 NVYLLGTSLARPVIAKAQIEVAEKEGCFAVSHGCTGKGNDQVRFELSFYALKPDVKVIAPWRDPSfferFAGRKDLLDYA 163
Cdd:COG0137 82 GKYPLGTALARPLIAKKLVEIAREEGADAVAHGCTGKGNDQVRFELAIRALAPDLKIIAPWREWD----LKSREEEIEYA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 164 AQKGIPVTQTKAKPWSTDENMAHISFEAGILEDPDTTPPKDMWKLTVDPTDAPDEPEDFIVEFEKGIPKKLilsDGKEVT 243
Cdd:COG0137 158 EEHGIPVPATKEKPYSIDENLWGRSIEGGELEDPWNEPPEDAYEWTVSPEDAPDEPEYVTITFEKGVPVAL---NGEKLS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 244 ePVTLFITANAIGRRNGVGRIDIVENRFIGIKSRGCYETPGLTLLRSAHIDLEGLTLDREVRSIRDTfVTPTYSKLLYNG 323
Cdd:COG0137 235 -PVELIEELNEIGGKHGVGRIDIVENRLVGIKSRGVYEAPGATILITAHRALESLTLDRETLHFKDI-LDQKYAELVYNG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 324 MYFTPECEYVRSMIQPSQNTVNGLVRARCYKGSVIILGRSSSTEkLYDATESSMDELTGFQPQDASGFIAVQSIRIKKYG 403
Cdd:COG0137 313 LWFSPLREALDAFIDETQKRVTGTVRLKLYKGNATVVGRKSPYS-LYDEDLATYEEDDVFDQKDAEGFIKLFGLPLRVAA 391
|
....*
gi 2066107567 404 EKARE 408
Cdd:COG0137 392 RVRKK 396
|
|
| Arginosuc_synth |
pfam00764 |
Arginosuccinate synthase; This family contains a PP-loop motif. |
7-401 |
0e+00 |
|
Arginosuccinate synthase; This family contains a PP-loop motif.
Pssm-ID: 279148 Cd Length: 386 Bit Score: 587.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 7 CLAYSGGLDTSVILAWLLEQ-GYEVIAFMANIGQ-EEDFAAAEKKALAIGASKYVLVDVRKEFVEEVLFPAVQVNAVYEN 84
Cdd:pfam00764 1 VLAYSGGLDTSVCIPWLKEQgGYEVIAVAVDVGQgGEDIDEAREKALKLGAVKHYVIDAKEEFVEDYIFPAIQANALYED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 85 VYLLGTSLARPVIAKAQIEVAEKEGCFAVSHGCTGKGNDQVRFELSFYALKPDVKVIAPWRDPSFFerfagRKDLLDYAA 164
Cdd:pfam00764 81 RYPLGTALARPLIAKKLVEAAKKEGASAVAHGCTGKGNDQVRFEVSFRSLAPDLKVIAPVRDPNLT-----REEEIEYAE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 165 QKGIPVTQTKAKPWSTDENMAHISFEAGILEDPDTTPPKDMWKLTVDPTDAPDEPEDFIVEFEKGIPKKLilsDGKEVtE 244
Cdd:pfam00764 156 EHGIPIPVTKKSPYSIDENLWGRSIEAGILEDPWNAPPEDIYEWTKDPAKAPDEPDIVEIGFEKGVPVAL---DGEPV-S 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 245 PVTLFITANAIGRRNGVGRIDIVENRFIGIKSRGCYETPGLTLLRSAHIDLEGLTLDREVRSIRDTFVTPtYSKLLYNGM 324
Cdd:pfam00764 232 PLELIEKLNEIAGAHGVGRIDIVEDRLVGIKSREIYEAPAATVLITAHRDLENLTLTREVLRFKRIVDQK-WAELVYDGL 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2066107567 325 YFTPECEYVRSMIQPSQNTVNGLVRARCYKGSVIILGRSSSTEkLYDATESSMDELTGFQPQDASGFIAVQSIRIKK 401
Cdd:pfam00764 311 WFSPLKEALDAFIDKTQERVTGTVRVKLHKGSAIVLGRRSPYS-LYDEELVSYDEGDTFDQTDATGFIKIHGLQAKI 386
|
|
| ASS |
cd01999 |
argininosuccinate_synthase (ASS); Argininosuccinate synthase (ASS; EC 6.3.4.5) is a urea cycle ... |
4-398 |
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: 581.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 4 GKVCLAYSGGLDTSVILAWLLEQ-GYEVIAFMANIGQEEDFAAAEKKALAIGASKYVLVDVRKEFVEEVLFPAVQVNAVY 82
Cdd:cd01999 1 KKVVLAYSGGLDTSVILKWLKEEyGYEVIAFTADLGQGDEEEEIEEKALKLGAVKVYVVDLREEFAEDYIFPAIKANAIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 83 ENVYLLGTSLARPVIAKAQIEVAEKEGCFAVSHGCTGKGNDQVRFELSFYALKPDVKVIAPWRDPsffeRFAGRKDLLDY 162
Cdd:cd01999 81 EGRYPLGTALARPLIAKKLVEVAREEGATAVAHGCTGKGNDQVRFELAIKALAPDLKVIAPWRDW----NFLTRAEEIAY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 163 AAQKGIPVTQTKAKPWSTDENMAHISFEAGILEDPDTTPPKDMWKLTVDPTDAPDEPEDFIVEFEKGIPKKLilsDGkEV 242
Cdd:cd01999 157 AKKHGIPVPVTKKKPYSIDENLWGRSYEGGDLEDPWNEPPEDAFEWTVSPEKAPDEPEYVTIEFEKGVPVAV---NG-EK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 243 TEPVTLFITANAIGRRNGVGRIDIVENRFIGIKSRGCYETPGLTLLRSAHIDLEGLTLDREVRSIRDtFVTPTYSKLLYN 322
Cdd:cd01999 233 LDPVELIEKLNEIAGRHGVGRIDIVENRLVGIKSRGVYEAPGATLLIKAHRDLEDLTLDREVLHFKD-IVSRKYAELVYN 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2066107567 323 GMYFTPECEYVRSMIQPSQNTVNGLVRARCYKGSVIILGRSSSTeKLYDATESSMDELTGFQPQDASGFIAVQSIR 398
Cdd:cd01999 312 GLWFDPLREALEAFIDKTQERVTGEVRLKLYKGNVIVVGRESPN-SLYSEELATYEEGDGFDQKDAEGFIKIHGLQ 386
|
|
| argG |
TIGR00032 |
argininosuccinate synthase; argG in bacteria, ARG1 in Saccharomyces cerevisiae. There is a ... |
5-407 |
0e+00 |
|
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: 575.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 5 KVCLAYSGGLDTSVILAWLLEQGYEVIAFMANIGQ-EEDFAAAEKKALAIGASKYVLVDVRKEFVEEVLFPAVQVNAVYE 83
Cdd:TIGR00032 1 KVVLAYSGGLDTSVCLKWLREKGYEVIAYTADVGQpEEDIDAIPEKALEYGAENHYTIDAREEFVKDYGFAAIQANAFYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 84 NVYLLGTSLARPVIAKAQIEVAEKEGCFAVSHGCTGKGNDQVRFELSFYALKPDVKVIAPWRDPSFFerfagRKDLLDYA 163
Cdd:TIGR00032 81 GTYPLSTALARPLIAKKLVEAAKKEGANAVAHGCTGKGNDQERFERSIRLLNPDLKVIAPWRDLNFT-----REEEIEYA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 164 AQKGIPVTQTKAKPWSTDENMAHISFEAGILEDPDTTPPKDMWKLTVDPTDA-PDEPEDFIVEFEKGIPKKLilsDGKEV 242
Cdd:TIGR00032 156 IQCGIPYPMSKEKPYSIDENLWGRSIEAGILEDPSTEPPEDIYMWTKFPDEAtPDEPEVVTIDFEQGVPVAL---NGVSL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 243 tEPVTLFITANAIGRRNGVGRIDIVENRFIGIKSRGCYETPGLTLLRSAHIDLEGLTLDREVRSIRDtFVTPTYSKLLYN 322
Cdd:TIGR00032 233 -DPVELILEANEIAGKHGVGRIDIIENRIIGLKSREIYEAPGAALLIIAHRDLETLTLTRDVLEFKD-IVEEQYSELIYQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 323 GMYFTPECEYVRSMIQPSQNTVNGLVRARCYKGSVIILGRsSSTEKLYDATESSMDELTGFQPQDASGFIAVQSIRIKKY 402
Cdd:TIGR00032 311 GLWFDPLAEALDAFIRKTQERVTGTVRVKLFKGNAIVIGR-TSPYSLYDEELVSMEKDDVFDPRDAIGFITMRGLQIKDY 389
|
....*
gi 2066107567 403 GEKAR 407
Cdd:TIGR00032 390 REKKK 394
|
|
| PRK00509 |
PRK00509 |
argininosuccinate synthase; Provisional |
5-405 |
0e+00 |
|
argininosuccinate synthase; Provisional
Pssm-ID: 234785 Cd Length: 399 Bit Score: 568.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 5 KVCLAYSGGLDTSVILAWLLEQ-GYEVIAFMANIGQEEDFAAAEKKALAIGASKYVLVDVRKEFVEEVLFPAVQVNAVYE 83
Cdd:PRK00509 4 KVVLAYSGGLDTSVIIKWLKETyGCEVIAFTADVGQGEELEPIREKALKSGASEIYVEDLREEFVRDYVFPAIRANALYE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 84 NVYLLGTSLARPVIAKAQIEVAEKEGCFAVSHGCTGKGNDQVRFELSFYALKPDVKVIAPWRDpsffERFAGRKDLLDYA 163
Cdd:PRK00509 84 GKYPLGTALARPLIAKKLVEIARKEGADAVAHGCTGKGNDQVRFELGIAALAPDLKVIAPWRE----WDLKSREELIAYA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 164 AQKGIPVTQTKAKPWSTDENMAHISFEAGILEDPDTTPPKDMWKLTVDPTDAPDEPEDFIVEFEKGIPKKLilsDGKEVT 243
Cdd:PRK00509 160 EEHGIPIPVTKKSPYSIDANLWHRSIEGGILEDPWNEPPEDVYEWTVSPEDAPDEPEYVEIEFEKGVPVAI---NGEALS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 244 ePVTLFITANAIGRRNGVGRIDIVENRFIGIKSRGCYETPGLTLLRSAHIDLEGLTLDREVRSIRDTfVTPTYSKLLYNG 323
Cdd:PRK00509 237 -PAELIEELNELAGKHGIGRIDIVENRLVGIKSRGVYETPGGTILIKAHRALESLTLDREVAHFKDE-LEPKYAELVYNG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 324 MYFTPECEYVRSMIQPSQNTVNGLVRARCYKGSVIILGRsSSTEKLYDATESSMDELTGFQPQDASGFIAVQSIRIKKYG 403
Cdd:PRK00509 315 LWFSPLREALQAFIDETQEHVTGEVRLKLYKGNAIVVGR-KSPNSLYDEDLATYEEDDVYDQKDAEGFIKLWGLPSKIAA 393
|
..
gi 2066107567 404 EK 405
Cdd:PRK00509 394 LV 395
|
|
| PLN00200 |
PLN00200 |
argininosuccinate synthase; Provisional |
3-403 |
4.64e-179 |
|
argininosuccinate synthase; Provisional
Pssm-ID: 177791 Cd Length: 404 Bit Score: 504.66 E-value: 4.64e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 3 KGKVCLAYSGGLDTSVILAWLLEQ-GYEVIAFMANIGQ-EEDFAAAEKKALAIGASKYVLVDVRKEFVEEVLFPAVQVNA 80
Cdd:PLN00200 5 LNKVVLAYSGGLDTSVILKWLRENyGCEVVCFTADVGQgIEELEGLEAKAKASGAKQLVVKDLREEFVRDYIFPCLRANA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 81 VYENVYLLGTSLARPVIAKAQIEVAEKEGCFAVSHGCTGKGNDQVRFELSFYALKPDVKVIAPWRDPSfferFAGRKDLL 160
Cdd:PLN00200 85 IYEGKYLLGTSMARPLIAKAMVDIAKEVGADAVAHGATGKGNDQVRFELTFFALNPELKVVAPWREWD----IKGREDLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 161 DYAAQKGIPVTQTKAKPWSTDENMAHISFEAGILEDPDTTPPKDMWKLTVDPTDAPDEPEDFIVEFEKGIPKKLilsDGK 240
Cdd:PLN00200 161 EYAKKHNIPVPVTKKSIYSRDRNLWHISYEGDILEDPANEPKEDMFMMSVSPEAAPDQPEYIEIEFEKGLPVAI---NGK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 241 EvTEPVTLFITANAIGRRNGVGRIDIVENRFIGIKSRGCYETPGLTLLRSAHIDLEGLTLDREVRSIRDTfVTPTYSKLL 320
Cdd:PLN00200 238 T-LSPATLLTKLNEIGGKHGIGRIDMVENRFVGMKSRGVYETPGGTILFAAHRELESLTLDRETMQVKDS-LALKYAELV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 321 YNGMYFTPECEYVRSMIQPSQNTVNGLVRARCYKGSVIILGRSSStEKLYDATESSMDELTG-FQPQDASGFIAVQSIRI 399
Cdd:PLN00200 316 YNGFWFDPERESMDAFMEKITETTTGSVRLKLYKGNVSVAGRKSP-YSLYRQDISSFEEGGGiYNQADAAGFIRLYALRL 394
|
....
gi 2066107567 400 KKYG 403
Cdd:PLN00200 395 RTRA 398
|
|
| PRK13820 |
PRK13820 |
argininosuccinate synthase; Provisional |
3-407 |
5.79e-133 |
|
argininosuccinate synthase; Provisional
Pssm-ID: 237521 Cd Length: 394 Bit Score: 387.36 E-value: 5.79e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 3 KGKVCLAYSGGLDTSVILAwLLEQGY---EVIAFMANIGQ-EEDFAAAEKKALAIGASKYVlVDVRKEFVEEVLFPAVQV 78
Cdd:PRK13820 2 MKKVVLAYSGGLDTSVCVP-LLKEKYgydEVITVTVDVGQpEEEIKEAEEKAKKLGDKHYT-IDAKEEFAKDYIFPAIKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 79 NAVYENvYLLGTSLARPVIAKAQIEVAEKEGCFAVSHGCTGKGNDQVRFELSFYAlkPDVKVIAPWRDPSFferfaGRKD 158
Cdd:PRK13820 80 NALYEG-YPLGTALARPLIAEKIVEVAEKEGASAIAHGCTGKGNDQLRFEAVFRA--SDLEVIAPIRELNL-----TREW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 159 LLDYAAQKGIPVTQTKAKPWSTDENMAHISFEAGILEDPDTTPPKDMWKLTVDPTDAPDEPEDFIVEFEKGIPKKLilsD 238
Cdd:PRK13820 152 EIEYAKEKGIPVPVGKEKPWSIDENLWSRSIEGGKLEDPAFEPPEEIYAWTVSPEDAPDEPEIVEIEFEEGVPVAI---N 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 239 GKEVtEPVTLFITANAIGRRNGVGRIDIVENRFIGIKSRGCYETPGLTLLRSAHIDLEGLTLDREVRSIRDTfVTPTYSK 318
Cdd:PRK13820 229 GEKM-DGVELIRKLNEIAGKHGVGRTDMMEDRVLGLKSRENYEHPAATVLLTAHKALEQLVLTREELKFKEI-VDSKWAE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 319 LLYNGMYFTPECEYVRSMIQPSQNTVNGLVRARCYKGSVIILGRSSSTeKLYDATESSMDELTGFQpQDASGFiavqsir 398
Cdd:PRK13820 307 LAYEGLVDEPLREDLNAFIDKTQERVTGTVTVKLYKGSARVVGRESPY-ALYSEELVSFDSKTIDQ-RDAEGM------- 377
|
....*....
gi 2066107567 399 IKKYGEKAR 407
Cdd:PRK13820 378 AKYHGLQAR 386
|
|
| PRK05370 |
PRK05370 |
argininosuccinate synthase; Validated |
5-338 |
5.73e-55 |
|
argininosuccinate synthase; Validated
Pssm-ID: 235434 Cd Length: 447 Bit Score: 188.26 E-value: 5.73e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 5 KVCLAYSGGLDTSVILAWLLEQGYEVIAFMANIGQ--EEDFAAAEKKALAIGASKYVLVDVRKEFVEEVLfPAVQVNAVY 82
Cdd:PRK05370 13 RVGIAFSGGLDTSAALLWMRQKGAVPYAYTANLGQpdEDDYDAIPRRAMEYGAENARLIDCRAQLVAEGI-AAIQCGAFH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 83 EN----VYLLGTSLARPVIAKAQIEVAEKEGCFAVSHGCTGKGNDQVRFELsfYAL--KPDVKVIAPWRDPSFFERFAGR 156
Cdd:PRK05370 92 IStggvTYFNTTPLGRAVTGTMLVAAMKEDGVNIWGDGSTYKGNDIERFYR--YGLltNPELKIYKPWLDQDFIDELGGR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 157 KDLLDYAAQKGIPVTQTKAKPWSTDENMAHISFEAGILEDPDTTPPkdmwklTVDPT--------DAPDEPEDFIVEFEK 228
Cdd:PRK05370 170 AEMSEFLIAHGFDYKMSVEKAYSTDSNMLGATHEAKDLEHLNSGIK------IVNPImgvafwdeDVEIKAEEVTVRFEQ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 229 GIPKKLilsDGKEVTEPVTLFITANAIGRRNGVGRIDIVENRFIGIKSRGCYETPGLTLLrsaHIDLEgltldREVRSIR 308
Cdd:PRK05370 244 GRPVAL---NGKTFSDPVELMLEANRIGGRHGLGMSDQIENRIIEAKSRGIYEAPGMALL---HIAYE-----RLVTGIH 312
|
330 340 350
....*....|....*....|....*....|....*..
gi 2066107567 309 DTFVTPTY-------SKLLYNGMYFTPECEYVRSMIQ 338
Cdd:PRK05370 313 NEDTIEQYringrrlGRLLYQGRWFDPQALMLRESLQ 349
|
|
| PRK04527 |
PRK04527 |
argininosuccinate synthase; Provisional |
2-408 |
6.05e-53 |
|
argininosuccinate synthase; Provisional
Pssm-ID: 235305 Cd Length: 400 Bit Score: 181.57 E-value: 6.05e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 2 SKGKVCLAYSGGLDTSVILAWLLEQGYEVIAFMANIG----QEEDFAaaEKKALAIGASKYVLVDVRKEFVEEVLFPAVQ 77
Cdd:PRK04527 1 SSKDIVLAFSGGLDTSFCIPYLQERGYAVHTVFADTGgvdaEERDFI--EKRAAELGAASHVTVDGGPAIWEGFVKPLVW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 78 VNAVYENVYLLGTSlARPVIAKAQIEVAEKEGCFAVSHGCTGKGNDQVRFELSFYALKpDVKVIAPWRDPSfFERFAGRK 157
Cdd:PRK04527 79 AGEGYQGQYPLLVS-DRYLIVDAALKRAEELGTRIIAHGCTGMGNDQVRFDLAVKALG-DYQIVAPIREIQ-KEHTQTRA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 158 DLLDYAAQKGIPVtQTKAKPWSTDENMAHISFEAGILeDPDTTPPKDMWKLTVDPTDAPDEPEDFIVEFEKGipkKLILS 237
Cdd:PRK04527 156 YEQKYLEERGFGV-RAKQKAYTINENLLGVTMSGGEI-DRWEAPGEGARGWCAPRSAWPTEALTVTIKFVEG---EAVAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 238 DGKEVTEPvTLFITANAIGRRNGVGRIDIVENRFIGIKSRGCYETPGLTLLRSAHIDLEGLTLDREVRSIRDTfVTPTYS 317
Cdd:PRK04527 231 DGKPLPGA-QILAKLNKLFAQYGVGRGVYTGDTVIGLKGRIVFEAPGLVSLLTAHRALEDAVLTKQQNRFKPD-VARKWV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 318 KLLYNGMYFTPECEYVRSMIQPSQNTVNGLVRARCYKGSVIILGRSSSTekLYDATESSMDELTGFQPQDASGFIAVQSI 397
Cdd:PRK04527 309 ELVYEGFYHDPLKTDIEAFLKSSQAKVNGEVTLETRGGRVDAVAVRSPH--LLNSKGATYAQSADWGVEEAEGFIKLFGM 386
|
410
....*....|.
gi 2066107567 398 RIKKYGEKARE 408
Cdd:PRK04527 387 SSTLYAQVNRS 397
|
|
| tRNA_Me_trans |
pfam03054 |
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ... |
5-71 |
2.41e-07 |
|
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA(5-methylaminomethyl-2-thiouridine)-methyltransferase which is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine present in the wobble position of some tRNAs.
Pssm-ID: 460787 [Multi-domain] Cd Length: 202 Bit Score: 50.71 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 5 KVCLAYSGGLDTSVILAWLLEQGYEVIA-FMAN---------IGQ---EEDFAAAEKKALAIGASKYVlVDVRKEFVEEV 71
Cdd:pfam03054 2 KVVVAMSGGVDSSVAAYLLKEQGHNVIGvFMKNwdeeqsldeEGKccsEEDLADAQRVCEQLGIPLYV-VNFEKEYWEDV 80
|
|
| QueC-like |
cd01995 |
7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC ... |
11-117 |
6.41e-07 |
|
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: 49.53 E-value: 6.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 11 SGGLDTSVILAWLLEQGYEVIAFMANIGQ----EEDFAAAE-KKALAIgasKYVLVDVRkeFVEEvlfpavqvnavyenv 85
Cdd:cd01995 8 SGGLDSTTLLYWALKEGYEVHALTFDYGQrhakEELEAAKLiAKLLGI---EHKVIDLS--FLGE--------------- 67
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2066107567 86 yLLGTSLARPVIAKAQIEVAEKE-----------------GCFAVSHGC 117
Cdd:cd01995 68 -LGGSSLTDEGEEVPDGEYDEESipstwvpnrnliflsiaAAYAESLGA 115
|
|
| MnmA_TRMU-like |
cd01998 |
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ... |
5-71 |
1.90e-06 |
|
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial tRNA-specific 2-thiouridylase MnmA (EC 2.8.1.13) and mitochondrial tRNA-specific 2-thiouridylase 1 (TRMU or MTU1, EC 2.8.1.14). MnmA catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. TRMU/MTU1 catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln); this is required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. This family 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: 467502 [Multi-domain] Cd Length: 349 Bit Score: 49.43 E-value: 1.90e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2066107567 5 KVCLAYSGGLDTSVILAWLLEQGYEVIA-FMAN----------IGQEEDFAAAEKKALAIGASKYVlVDVRKEFVEEV 71
Cdd:cd01998 1 KVAVAMSGGVDSSVAAALLKEQGYDVIGvFMKNwddednekggCCSEEDIEDARRVADQLGIPLYV-VDFSEEYWERV 77
|
|
| QueC |
COG0603 |
7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and ... |
1-63 |
1.39e-05 |
|
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: 45.92 E-value: 1.39e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2066107567 1 MSKGKVCLaYSGGLDTSVILAWLLEQGYEVIAFMANIGQEEDF--AAAEKKALAIGASKYVLVDV 63
Cdd:COG0603 1 MMKKAVVL-LSGGLDSTTCLAWALARGYEVYALSFDYGQRHRKelEAARRIAKALGVGEHKVIDL 64
|
|
| mnmA |
PRK00143 |
tRNA-specific 2-thiouridylase MnmA; Reviewed |
5-71 |
2.39e-05 |
|
tRNA-specific 2-thiouridylase MnmA; Reviewed
Pssm-ID: 234664 [Multi-domain] Cd Length: 346 Bit Score: 45.83 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 5 KVCLAYSGGLDTSVIlAWLL-EQGYEVI-AFMAN--------IG---QEEDFAAAEKKALAIGASKYVlVDVRKEFVEEV 71
Cdd:PRK00143 2 RVVVGMSGGVDSSVA-AALLkEQGYEVIgVFMKLwddddetgKGgccAEEDIADARRVADKLGIPHYV-VDFEKEFWDRV 79
|
|
| TIGR00364 |
TIGR00364 |
queuosine biosynthesis protein QueC; Members of this protein family are QueC, involved in ... |
10-63 |
2.89e-05 |
|
queuosine biosynthesis protein QueC; Members of this protein family are QueC, involved in synthesizing pre-Q0 from GTP en route to tRNA modification with queuosine. This protein family is represented by a single member in nearly every completed large (> 1000 genes) prokaryotic genome. In Rhizobium meliloti, the gene was designated exsB, possibly because of polar effects on exsA expression in a shared polycistronic mRNA. In Arthrobacter viscosus, the homologous gene was designated ALU1 and was associated with an aluminum tolerance phenotype. [Unknown function, General]
Pssm-ID: 129461 [Multi-domain] Cd Length: 201 Bit Score: 44.69 E-value: 2.89e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2066107567 10 YSGGLDTSVILAWLLEQGYEVIAFMANIGQEED--FAAAEKKALAIGAsKYVLVDV 63
Cdd:TIGR00364 5 LSGGQDSTTCLLWAKDEGYEVHAVTFDYGQRHSreLESARKIAEALGI-EHHLLDL 59
|
|
| QueC |
pfam06508 |
Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis ... |
11-60 |
4.37e-05 |
|
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: 44.15 E-value: 4.37e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2066107567 11 SGGLDTSVILAWLLEQGYEVIAFMANIGQEED--FAAAEKKALAIGASKYVL 60
Cdd:pfam06508 7 SGGLDSTTCLAWAKKEGYEVYALSFDYGQRHRkeLECAKKIAKALGVEHKIL 58
|
|
| MnmA |
COG0482 |
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ... |
5-72 |
1.12e-04 |
|
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ribosomal structure and biogenesis]; tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440250 [Multi-domain] Cd Length: 353 Bit Score: 43.89 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 5 KVCLAYSGGLDTSVIlAWLL-EQGYEVI-AFMAN------IG-----QEEDFAAAEKKALAIGASKYVlVDVRKEFVEEV 71
Cdd:COG0482 2 RVVVGMSGGVDSSVA-AALLkEQGYEVIgVTMKLwddddaSGsggccSLEDIEDARRVADKLGIPHYV-VDFEEEFKDRV 79
|
.
gi 2066107567 72 L 72
Cdd:COG0482 80 I 80
|
|
| PRK14561 |
PRK14561 |
hypothetical protein; Provisional |
5-85 |
6.55e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 184745 Cd Length: 194 Bit Score: 40.58 E-value: 6.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066107567 5 KVCLAYSGGLDTSvILAWLLEQGYEVIAFMANIGQEEDFAAAEKKALAIGASKYVLV---DVRKEFVEEVL---FPAVQV 78
Cdd:PRK14561 2 KAGVLFSGGKDSS-LAAILLERFYDVELVTVNFGVLDSWKHAREAAKALGFPHRVLEldrEILEKAVDMIIedgYPNNAI 80
|
....*..
gi 2066107567 79 NAVYENV 85
Cdd:PRK14561 81 QYVHEHA 87
|
|
| PRK14664 |
PRK14664 |
tRNA-specific 2-thiouridylase MnmA; Provisional |
2-72 |
1.34e-03 |
|
tRNA-specific 2-thiouridylase MnmA; Provisional
Pssm-ID: 173127 [Multi-domain] Cd Length: 362 Bit Score: 40.71 E-value: 1.34e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2066107567 2 SKGKVCLAYSGGLDTSVILAWLLEQGYEVIAF-MANIGQEEDfaAAEKKALAIGASKYVlVDVRKEFVEEVL 72
Cdd:PRK14664 4 SKKRVLVGMSGGIDSTATCLMLQEQGYEIVGVtMRVWGDEPQ--DARELAARMGIEHYV-ADERVPFKDTIV 72
|
|
| |
