|
Name |
Accession |
Description |
Interval |
E-value |
| Arginosuc_synth |
pfam00764 |
Arginosuccinate synthase; This family contains a PP-loop motif. |
8-401 |
0e+00 |
|
Arginosuccinate synthase; This family contains a PP-loop motif.
Pssm-ID: 279148 Cd Length: 386 Bit Score: 629.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 8 VLAYSGGLDTSCILVWLKEQ-GYDVIAYLANIGQK-EDFEEARKKALKLGAKKVFIEDVSKEFVEEFIWPAVQSSALYED 85
Cdd:pfam00764 1 VLAYSGGLDTSVCIPWLKEQgGYEVIAVAVDVGQGgEDIDEAREKALKLGAVKHYVIDAKEEFVEDYIFPAIQANALYED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 86 RYLLGTSLARPCIARRQVEIAQREGAKYVSHGATGKGNDQVRFELTCYSLAPQIKVIAPWRMPEFYnrfkgRNDLMEYAK 165
Cdd:pfam00764 81 RYPLGTALARPLIAKKLVEAAKKEGASAVAHGCTGKGNDQVRFEVSFRSLAPDLKVIAPVRDPNLT-----REEEIEYAE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 166 QHGIPIPVTPKSPWSMDENLMHISYEAGILENPKNQAPPGLYTKTQDPAKAPNSPDVLEIEFKKGVPVKVtnikDGTTRT 245
Cdd:pfam00764 156 EHGIPIPVTKKSPYSIDENLWGRSIEAGILEDPWNAPPEDIYEWTKDPAKAPDEPDIVEIGFEKGVPVAL----DGEPVS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 246 TsLELFMYLNEVAGKHGVGRIDIVENRFIGMKSRGIYETPAGTILYHAHLDIEAFTMDREVRKIKQGLGLKFAELVYTGF 325
Cdd:pfam00764 232 P-LELIEKLNEIAGAHGVGRIDIVEDRLVGIKSREIYEAPAATVLITAHRDLENLTLTREVLRFKRIVDQKWAELVYDGL 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6996911 326 WHSPECEFVRHCIQKSQERVEGKVQVSVFKGQVYILGRESPLSLYNEELVSMNVQGDYEPIDATGFININSLRLKE 401
Cdd:pfam00764 311 WFSPLKEALDAFIDKTQERVTGTVRVKLHKGSAIVLGRRSPYSLYDEELVSYDEGDTFDQTDATGFIKIHGLQAKI 386
|
|
| ASS |
cd01999 |
argininosuccinate_synthase (ASS); Argininosuccinate synthase (ASS; EC 6.3.4.5) is a urea cycle ... |
7-398 |
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: 623.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 7 VVLAYSGGLDTSCILVWLKEQ-GYDVIAYLANIGQKEDFEEARKKALKLGAKKVFIEDVSKEFVEEFIWPAVQSSALYED 85
Cdd:cd01999 3 VVLAYSGGLDTSVILKWLKEEyGYEVIAFTADLGQGDEEEEIEEKALKLGAVKVYVVDLREEFAEDYIFPAIKANAIYEG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 86 RYLLGTSLARPCIARRQVEIAQREGAKYVSHGATGKGNDQVRFELTCYSLAPQIKVIAPWRMPefynRFKGRNDLMEYAK 165
Cdd:cd01999 83 RYPLGTALARPLIAKKLVEVAREEGATAVAHGCTGKGNDQVRFELAIKALAPDLKVIAPWRDW----NFLTRAEEIAYAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 166 QHGIPIPVTPKSPWSMDENLMHISYEAGILENPKNQAPPGLYTKTQDPAKAPNSPDVLEIEFKKGVPVKVTNIKdgttrT 245
Cdd:cd01999 159 KHGIPVPVTKKKPYSIDENLWGRSYEGGDLEDPWNEPPEDAFEWTVSPEKAPDEPEYVTIEFEKGVPVAVNGEK-----L 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 246 TSLELFMYLNEVAGKHGVGRIDIVENRFIGMKSRGIYETPAGTILYHAHLDIEAFTMDREVRKIKQGLGLKFAELVYTGF 325
Cdd:cd01999 234 DPVELIEKLNEIAGRHGVGRIDIVENRLVGIKSRGVYEAPGATLLIKAHRDLEDLTLDREVLHFKDIVSRKYAELVYNGL 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6996911 326 WHSPECEFVRHCIQKSQERVEGKVQVSVFKGQVYILGRESPLSLYNEELVSMNVQGDYEPIDATGFININSLR 398
Cdd:cd01999 314 WFDPLREALEAFIDKTQERVTGEVRLKLYKGNVIVVGRESPNSLYSEELATYEEGDGFDQKDAEGFIKIHGLQ 386
|
|
| ArgG |
COG0137 |
Argininosuccinate synthase [Amino acid transport and metabolism]; Argininosuccinate synthase ... |
7-409 |
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: 609.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 7 VVLAYSGGLDTSCILVWLKEQ-GYDVIAYLANIGQKEDFEEARKKALKLGAKKVFIEDVSKEFVEEFIWPAVQSSALYED 85
Cdd:COG0137 3 VVLAYSGGLDTSVIIPWLKEKyGYEVIAVTADVGQGEDLEAIEEKALKLGASKAYVVDAREEFVEDYVFPAIKANALYEG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 86 RYLLGTSLARPCIARRQVEIAQREGAKYVSHGATGKGNDQVRFELTCYSLAPQIKVIAPWRMPEFynrfKGRNDLMEYAK 165
Cdd:COG0137 83 KYPLGTALARPLIAKKLVEIAREEGADAVAHGCTGKGNDQVRFELAIRALAPDLKIIAPWREWDL----KSREEEIEYAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 166 QHGIPIPVTPKSPWSMDENLMHISYEAGILENPKNQAPPGLYTKTQDPAKAPNSPDVLEIEFKKGVPVKVtnikDGTtRT 245
Cdd:COG0137 159 EHGIPVPATKEKPYSIDENLWGRSIEGGELEDPWNEPPEDAYEWTVSPEDAPDEPEYVTITFEKGVPVAL----NGE-KL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 246 TSLELFMYLNEVAGKHGVGRIDIVENRFIGMKSRGIYETPAGTILYHAHLDIEAFTMDREVRKIKQGLGLKFAELVYTGF 325
Cdd:COG0137 234 SPVELIEELNEIGGKHGVGRIDIVENRLVGIKSRGVYEAPGATILITAHRALESLTLDRETLHFKDILDQKYAELVYNGL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 326 WHSPECEFVRHCIQKSQERVEGKVQVSVFKGQVYILGRESPLSLYNEELVSMNVQGDYEPIDATGFININSLRLKEYHRL 405
Cdd:COG0137 314 WFSPLREALDAFIDETQKRVTGTVRLKLYKGNATVVGRKSPYSLYDEDLATYEEDDVFDQKDAEGFIKLFGLPLRVAARV 393
|
....
gi 6996911 406 QSKV 409
Cdd:COG0137 394 RKKK 397
|
|
| PRK00509 |
PRK00509 |
argininosuccinate synthase; Provisional |
7-408 |
0e+00 |
|
argininosuccinate synthase; Provisional
Pssm-ID: 234785 Cd Length: 399 Bit Score: 602.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 7 VVLAYSGGLDTSCILVWLKEQ-GYDVIAYLANIGQKEDFEEARKKALKLGAKKVFIEDVSKEFVEEFIWPAVQSSALYED 85
Cdd:PRK00509 5 VVLAYSGGLDTSVIIKWLKETyGCEVIAFTADVGQGEELEPIREKALKSGASEIYVEDLREEFVRDYVFPAIRANALYEG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 86 RYLLGTSLARPCIARRQVEIAQREGAKYVSHGATGKGNDQVRFELTCYSLAPQIKVIAPWRmpEFynRFKGRNDLMEYAK 165
Cdd:PRK00509 85 KYPLGTALARPLIAKKLVEIARKEGADAVAHGCTGKGNDQVRFELGIAALAPDLKVIAPWR--EW--DLKSREELIAYAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 166 QHGIPIPVTPKSPWSMDENLMHISYEAGILENPKNQAPPGLYTKTQDPAKAPNSPDVLEIEFKKGVPVKVtnikDGtTRT 245
Cdd:PRK00509 161 EHGIPIPVTKKSPYSIDANLWHRSIEGGILEDPWNEPPEDVYEWTVSPEDAPDEPEYVEIEFEKGVPVAI----NG-EAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 246 TSLELFMYLNEVAGKHGVGRIDIVENRFIGMKSRGIYETPAGTILYHAHLDIEAFTMDREVRKIKQGLGLKFAELVYTGF 325
Cdd:PRK00509 236 SPAELIEELNELAGKHGIGRIDIVENRLVGIKSRGVYETPGGTILIKAHRALESLTLDREVAHFKDELEPKYAELVYNGL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 326 WHSPECEFVRHCIQKSQERVEGKVQVSVFKGQVYILGRESPLSLYNEELVSMNVQGDYEPIDATGFININSLRLKEYHRL 405
Cdd:PRK00509 316 WFSPLREALQAFIDETQEHVTGEVRLKLYKGNAIVVGRKSPNSLYDEDLATYEEDDVYDQKDAEGFIKLWGLPSKIAALV 395
|
...
gi 6996911 406 QSK 408
Cdd:PRK00509 396 NKK 398
|
|
| argG |
TIGR00032 |
argininosuccinate synthase; argG in bacteria, ARG1 in Saccharomyces cerevisiae. There is a ... |
7-405 |
4.03e-160 |
|
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: 456.10 E-value: 4.03e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 7 VVLAYSGGLDTSCILVWLKEQGYDVIAYLANIGQ-KEDFEEARKKALKLGAKKVFIEDVSKEFVEEFIWPAVQSSALYED 85
Cdd:TIGR00032 2 VVLAYSGGLDTSVCLKWLREKGYEVIAYTADVGQpEEDIDAIPEKALEYGAENHYTIDAREEFVKDYGFAAIQANAFYEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 86 RYLLGTSLARPCIARRQVEIAQREGAKYVSHGATGKGNDQVRFELTCYSLAPQIKVIAPWRMPEFYnrfkgRNDLMEYAK 165
Cdd:TIGR00032 82 TYPLSTALARPLIAKKLVEAAKKEGANAVAHGCTGKGNDQERFERSIRLLNPDLKVIAPWRDLNFT-----REEEIEYAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 166 QHGIPIPVTPKSPWSMDENLMHISYEAGILENPKNQAPPGLYTKTQDP-AKAPNSPDVLEIEFKKGVPVKVTNIkdgttR 244
Cdd:TIGR00032 157 QCGIPYPMSKEKPYSIDENLWGRSIEAGILEDPSTEPPEDIYMWTKFPdEATPDEPEVVTIDFEQGVPVALNGV-----S 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 245 TTSLELFMYLNEVAGKHGVGRIDIVENRFIGMKSRGIYETPAGTILYHAHLDIEAFTMDREVRKIKQGLGLKFAELVYTG 324
Cdd:TIGR00032 232 LDPVELILEANEIAGKHGVGRIDIIENRIIGLKSREIYEAPGAALLIIAHRDLETLTLTRDVLEFKDIVEEQYSELIYQG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 325 FWHSPECEFVRHCIQKSQERVEGKVQVSVFKGQVYILGRESPLSLYNEELVSMNVQGDYEPIDATGFININSLRLKEYHR 404
Cdd:TIGR00032 312 LWFDPLAEALDAFIRKTQERVTGTVRVKLFKGNAIVIGRTSPYSLYDEELVSMEKDDVFDPRDAIGFITMRGLQIKDYRE 391
|
.
gi 6996911 405 L 405
Cdd:TIGR00032 392 K 392
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Arginosuc_synth |
pfam00764 |
Arginosuccinate synthase; This family contains a PP-loop motif. |
8-401 |
0e+00 |
|
Arginosuccinate synthase; This family contains a PP-loop motif.
Pssm-ID: 279148 Cd Length: 386 Bit Score: 629.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 8 VLAYSGGLDTSCILVWLKEQ-GYDVIAYLANIGQK-EDFEEARKKALKLGAKKVFIEDVSKEFVEEFIWPAVQSSALYED 85
Cdd:pfam00764 1 VLAYSGGLDTSVCIPWLKEQgGYEVIAVAVDVGQGgEDIDEAREKALKLGAVKHYVIDAKEEFVEDYIFPAIQANALYED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 86 RYLLGTSLARPCIARRQVEIAQREGAKYVSHGATGKGNDQVRFELTCYSLAPQIKVIAPWRMPEFYnrfkgRNDLMEYAK 165
Cdd:pfam00764 81 RYPLGTALARPLIAKKLVEAAKKEGASAVAHGCTGKGNDQVRFEVSFRSLAPDLKVIAPVRDPNLT-----REEEIEYAE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 166 QHGIPIPVTPKSPWSMDENLMHISYEAGILENPKNQAPPGLYTKTQDPAKAPNSPDVLEIEFKKGVPVKVtnikDGTTRT 245
Cdd:pfam00764 156 EHGIPIPVTKKSPYSIDENLWGRSIEAGILEDPWNAPPEDIYEWTKDPAKAPDEPDIVEIGFEKGVPVAL----DGEPVS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 246 TsLELFMYLNEVAGKHGVGRIDIVENRFIGMKSRGIYETPAGTILYHAHLDIEAFTMDREVRKIKQGLGLKFAELVYTGF 325
Cdd:pfam00764 232 P-LELIEKLNEIAGAHGVGRIDIVEDRLVGIKSREIYEAPAATVLITAHRDLENLTLTREVLRFKRIVDQKWAELVYDGL 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6996911 326 WHSPECEFVRHCIQKSQERVEGKVQVSVFKGQVYILGRESPLSLYNEELVSMNVQGDYEPIDATGFININSLRLKE 401
Cdd:pfam00764 311 WFSPLKEALDAFIDKTQERVTGTVRVKLHKGSAIVLGRRSPYSLYDEELVSYDEGDTFDQTDATGFIKIHGLQAKI 386
|
|
| ASS |
cd01999 |
argininosuccinate_synthase (ASS); Argininosuccinate synthase (ASS; EC 6.3.4.5) is a urea cycle ... |
7-398 |
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: 623.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 7 VVLAYSGGLDTSCILVWLKEQ-GYDVIAYLANIGQKEDFEEARKKALKLGAKKVFIEDVSKEFVEEFIWPAVQSSALYED 85
Cdd:cd01999 3 VVLAYSGGLDTSVILKWLKEEyGYEVIAFTADLGQGDEEEEIEEKALKLGAVKVYVVDLREEFAEDYIFPAIKANAIYEG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 86 RYLLGTSLARPCIARRQVEIAQREGAKYVSHGATGKGNDQVRFELTCYSLAPQIKVIAPWRMPefynRFKGRNDLMEYAK 165
Cdd:cd01999 83 RYPLGTALARPLIAKKLVEVAREEGATAVAHGCTGKGNDQVRFELAIKALAPDLKVIAPWRDW----NFLTRAEEIAYAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 166 QHGIPIPVTPKSPWSMDENLMHISYEAGILENPKNQAPPGLYTKTQDPAKAPNSPDVLEIEFKKGVPVKVTNIKdgttrT 245
Cdd:cd01999 159 KHGIPVPVTKKKPYSIDENLWGRSYEGGDLEDPWNEPPEDAFEWTVSPEKAPDEPEYVTIEFEKGVPVAVNGEK-----L 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 246 TSLELFMYLNEVAGKHGVGRIDIVENRFIGMKSRGIYETPAGTILYHAHLDIEAFTMDREVRKIKQGLGLKFAELVYTGF 325
Cdd:cd01999 234 DPVELIEKLNEIAGRHGVGRIDIVENRLVGIKSRGVYEAPGATLLIKAHRDLEDLTLDREVLHFKDIVSRKYAELVYNGL 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6996911 326 WHSPECEFVRHCIQKSQERVEGKVQVSVFKGQVYILGRESPLSLYNEELVSMNVQGDYEPIDATGFININSLR 398
Cdd:cd01999 314 WFDPLREALEAFIDKTQERVTGEVRLKLYKGNVIVVGRESPNSLYSEELATYEEGDGFDQKDAEGFIKIHGLQ 386
|
|
| ArgG |
COG0137 |
Argininosuccinate synthase [Amino acid transport and metabolism]; Argininosuccinate synthase ... |
7-409 |
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: 609.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 7 VVLAYSGGLDTSCILVWLKEQ-GYDVIAYLANIGQKEDFEEARKKALKLGAKKVFIEDVSKEFVEEFIWPAVQSSALYED 85
Cdd:COG0137 3 VVLAYSGGLDTSVIIPWLKEKyGYEVIAVTADVGQGEDLEAIEEKALKLGASKAYVVDAREEFVEDYVFPAIKANALYEG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 86 RYLLGTSLARPCIARRQVEIAQREGAKYVSHGATGKGNDQVRFELTCYSLAPQIKVIAPWRMPEFynrfKGRNDLMEYAK 165
Cdd:COG0137 83 KYPLGTALARPLIAKKLVEIAREEGADAVAHGCTGKGNDQVRFELAIRALAPDLKIIAPWREWDL----KSREEEIEYAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 166 QHGIPIPVTPKSPWSMDENLMHISYEAGILENPKNQAPPGLYTKTQDPAKAPNSPDVLEIEFKKGVPVKVtnikDGTtRT 245
Cdd:COG0137 159 EHGIPVPATKEKPYSIDENLWGRSIEGGELEDPWNEPPEDAYEWTVSPEDAPDEPEYVTITFEKGVPVAL----NGE-KL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 246 TSLELFMYLNEVAGKHGVGRIDIVENRFIGMKSRGIYETPAGTILYHAHLDIEAFTMDREVRKIKQGLGLKFAELVYTGF 325
Cdd:COG0137 234 SPVELIEELNEIGGKHGVGRIDIVENRLVGIKSRGVYEAPGATILITAHRALESLTLDRETLHFKDILDQKYAELVYNGL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 326 WHSPECEFVRHCIQKSQERVEGKVQVSVFKGQVYILGRESPLSLYNEELVSMNVQGDYEPIDATGFININSLRLKEYHRL 405
Cdd:COG0137 314 WFSPLREALDAFIDETQKRVTGTVRLKLYKGNATVVGRKSPYSLYDEDLATYEEDDVFDQKDAEGFIKLFGLPLRVAARV 393
|
....
gi 6996911 406 QSKV 409
Cdd:COG0137 394 RKKK 397
|
|
| PRK00509 |
PRK00509 |
argininosuccinate synthase; Provisional |
7-408 |
0e+00 |
|
argininosuccinate synthase; Provisional
Pssm-ID: 234785 Cd Length: 399 Bit Score: 602.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 7 VVLAYSGGLDTSCILVWLKEQ-GYDVIAYLANIGQKEDFEEARKKALKLGAKKVFIEDVSKEFVEEFIWPAVQSSALYED 85
Cdd:PRK00509 5 VVLAYSGGLDTSVIIKWLKETyGCEVIAFTADVGQGEELEPIREKALKSGASEIYVEDLREEFVRDYVFPAIRANALYEG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 86 RYLLGTSLARPCIARRQVEIAQREGAKYVSHGATGKGNDQVRFELTCYSLAPQIKVIAPWRmpEFynRFKGRNDLMEYAK 165
Cdd:PRK00509 85 KYPLGTALARPLIAKKLVEIARKEGADAVAHGCTGKGNDQVRFELGIAALAPDLKVIAPWR--EW--DLKSREELIAYAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 166 QHGIPIPVTPKSPWSMDENLMHISYEAGILENPKNQAPPGLYTKTQDPAKAPNSPDVLEIEFKKGVPVKVtnikDGtTRT 245
Cdd:PRK00509 161 EHGIPIPVTKKSPYSIDANLWHRSIEGGILEDPWNEPPEDVYEWTVSPEDAPDEPEYVEIEFEKGVPVAI----NG-EAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 246 TSLELFMYLNEVAGKHGVGRIDIVENRFIGMKSRGIYETPAGTILYHAHLDIEAFTMDREVRKIKQGLGLKFAELVYTGF 325
Cdd:PRK00509 236 SPAELIEELNELAGKHGIGRIDIVENRLVGIKSRGVYETPGGTILIKAHRALESLTLDREVAHFKDELEPKYAELVYNGL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 326 WHSPECEFVRHCIQKSQERVEGKVQVSVFKGQVYILGRESPLSLYNEELVSMNVQGDYEPIDATGFININSLRLKEYHRL 405
Cdd:PRK00509 316 WFSPLREALQAFIDETQEHVTGEVRLKLYKGNAIVVGRKSPNSLYDEDLATYEEDDVYDQKDAEGFIKLWGLPSKIAALV 395
|
...
gi 6996911 406 QSK 408
Cdd:PRK00509 396 NKK 398
|
|
| PLN00200 |
PLN00200 |
argininosuccinate synthase; Provisional |
7-408 |
0e+00 |
|
argininosuccinate synthase; Provisional
Pssm-ID: 177791 Cd Length: 404 Bit Score: 541.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 7 VVLAYSGGLDTSCILVWLKEQ-GYDVIAYLANIGQ-KEDFEEARKKALKLGAKKVFIEDVSKEFVEEFIWPAVQSSALYE 84
Cdd:PLN00200 8 VVLAYSGGLDTSVILKWLRENyGCEVVCFTADVGQgIEELEGLEAKAKASGAKQLVVKDLREEFVRDYIFPCLRANAIYE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 85 DRYLLGTSLARPCIARRQVEIAQREGAKYVSHGATGKGNDQVRFELTCYSLAPQIKVIAPWRMPEFynrfKGRNDLMEYA 164
Cdd:PLN00200 88 GKYLLGTSMARPLIAKAMVDIAKEVGADAVAHGATGKGNDQVRFELTFFALNPELKVVAPWREWDI----KGREDLIEYA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 165 KQHGIPIPVTPKSPWSMDENLMHISYEAGILENPKNQAPPGLYTKTQDPAKAPNSPDVLEIEFKKGVPVKVTNIkdgttR 244
Cdd:PLN00200 164 KKHNIPVPVTKKSIYSRDRNLWHISYEGDILEDPANEPKEDMFMMSVSPEAAPDQPEYIEIEFEKGLPVAINGK-----T 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 245 TTSLELFMYLNEVAGKHGVGRIDIVENRFIGMKSRGIYETPAGTILYHAHLDIEAFTMDREVRKIKQGLGLKFAELVYTG 324
Cdd:PLN00200 239 LSPATLLTKLNEIGGKHGIGRIDMVENRFVGMKSRGVYETPGGTILFAAHRELESLTLDRETMQVKDSLALKYAELVYNG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 325 FWHSPECEFVRHCIQKSQERVEGKVQVSVFKGQVYILGRESPLSLYNEELVSMNV-QGDYEPIDATGFININSLRLKEYH 403
Cdd:PLN00200 319 FWFDPERESMDAFMEKITETTTGSVRLKLYKGNVSVAGRKSPYSLYRQDISSFEEgGGIYNQADAAGFIRLYALRLRTRA 398
|
....*
gi 6996911 404 RLQSK 408
Cdd:PLN00200 399 MLRKK 403
|
|
| argG |
TIGR00032 |
argininosuccinate synthase; argG in bacteria, ARG1 in Saccharomyces cerevisiae. There is a ... |
7-405 |
4.03e-160 |
|
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: 456.10 E-value: 4.03e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 7 VVLAYSGGLDTSCILVWLKEQGYDVIAYLANIGQ-KEDFEEARKKALKLGAKKVFIEDVSKEFVEEFIWPAVQSSALYED 85
Cdd:TIGR00032 2 VVLAYSGGLDTSVCLKWLREKGYEVIAYTADVGQpEEDIDAIPEKALEYGAENHYTIDAREEFVKDYGFAAIQANAFYEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 86 RYLLGTSLARPCIARRQVEIAQREGAKYVSHGATGKGNDQVRFELTCYSLAPQIKVIAPWRMPEFYnrfkgRNDLMEYAK 165
Cdd:TIGR00032 82 TYPLSTALARPLIAKKLVEAAKKEGANAVAHGCTGKGNDQERFERSIRLLNPDLKVIAPWRDLNFT-----REEEIEYAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 166 QHGIPIPVTPKSPWSMDENLMHISYEAGILENPKNQAPPGLYTKTQDP-AKAPNSPDVLEIEFKKGVPVKVTNIkdgttR 244
Cdd:TIGR00032 157 QCGIPYPMSKEKPYSIDENLWGRSIEAGILEDPSTEPPEDIYMWTKFPdEATPDEPEVVTIDFEQGVPVALNGV-----S 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 245 TTSLELFMYLNEVAGKHGVGRIDIVENRFIGMKSRGIYETPAGTILYHAHLDIEAFTMDREVRKIKQGLGLKFAELVYTG 324
Cdd:TIGR00032 232 LDPVELILEANEIAGKHGVGRIDIIENRIIGLKSREIYEAPGAALLIIAHRDLETLTLTRDVLEFKDIVEEQYSELIYQG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 325 FWHSPECEFVRHCIQKSQERVEGKVQVSVFKGQVYILGRESPLSLYNEELVSMNVQGDYEPIDATGFININSLRLKEYHR 404
Cdd:TIGR00032 312 LWFDPLAEALDAFIRKTQERVTGTVRVKLFKGNAIVIGRTSPYSLYDEELVSMEKDDVFDPRDAIGFITMRGLQIKDYRE 391
|
.
gi 6996911 405 L 405
Cdd:TIGR00032 392 K 392
|
|
| PRK13820 |
PRK13820 |
argininosuccinate synthase; Provisional |
4-408 |
3.99e-132 |
|
argininosuccinate synthase; Provisional
Pssm-ID: 237521 Cd Length: 394 Bit Score: 385.05 E-value: 3.99e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 4 KGSVVLAYSGGLDTSCILVWLKEQ-GYD-VIAYLANIGQ-KEDFEEARKKALKLGAKKvFIEDVSKEFVEEFIWPAVQSS 80
Cdd:PRK13820 2 MKKVVLAYSGGLDTSVCVPLLKEKyGYDeVITVTVDVGQpEEEIKEAEEKAKKLGDKH-YTIDAKEEFAKDYIFPAIKAN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 81 ALYEDrYLLGTSLARPCIARRQVEIAQREGAKYVSHGATGKGNDQVRFELTCYslAPQIKVIAPWRmpefynrfkgrnDL 160
Cdd:PRK13820 81 ALYEG-YPLGTALARPLIAEKIVEVAEKEGASAIAHGCTGKGNDQLRFEAVFR--ASDLEVIAPIR------------EL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 161 -------MEYAKQHGIPIPVTPKSPWSMDENLMHISYEAGILENPKNQAPPGLYTKTQDPAKAPNSPDVLEIEFKKGVPV 233
Cdd:PRK13820 146 nltreweIEYAKEKGIPVPVGKEKPWSIDENLWSRSIEGGKLEDPAFEPPEEIYAWTVSPEDAPDEPEIVEIEFEEGVPV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 234 KVtnikDGTtRTTSLELFMYLNEVAGKHGVGRIDIVENRFIGMKSRGIYETPAGTILYHAHLDIEAFTMDREVRKIKQGL 313
Cdd:PRK13820 226 AI----NGE-KMDGVELIRKLNEIAGKHGVGRTDMMEDRVLGLKSRENYEHPAATVLLTAHKALEQLVLTREELKFKEIV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 314 GLKFAELVYTGFWHSPECEFVRHCIQKSQERVEGKVQVSVFKGQVYILGRESPLSLYNEELVSMNVQgDYEPIDATGFIN 393
Cdd:PRK13820 301 DSKWAELAYEGLVDEPLREDLNAFIDKTQERVTGTVTVKLYKGSARVVGRESPYALYSEELVSFDSK-TIDQRDAEGMAK 379
|
410
....*....|....*
gi 6996911 394 INSLRLKEYHRLQSK 408
Cdd:PRK13820 380 YHGLQARLYNKVKRK 394
|
|
| PRK04527 |
PRK04527 |
argininosuccinate synthase; Provisional |
3-394 |
2.00e-53 |
|
argininosuccinate synthase; Provisional
Pssm-ID: 235305 Cd Length: 400 Bit Score: 182.73 E-value: 2.00e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 3 SKGSVVLAYSGGLDTSCILVWLKEQGYDVIAYLANIG----QKEDFEEARKKALKLGAKKVFieDVSKEFVEEFIWPAVQ 78
Cdd:PRK04527 1 SSKDIVLAFSGGLDTSFCIPYLQERGYAVHTVFADTGgvdaEERDFIEKRAAELGAASHVTV--DGGPAIWEGFVKPLVW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 79 SSALYEDRYLLGTSlARPCIARRQVEIAQREGAKYVSHGATGKGNDQVRFELTCYSLApQIKVIAPWRmpEFYNRFKG-R 157
Cdd:PRK04527 79 AGEGYQGQYPLLVS-DRYLIVDAALKRAEELGTRIIAHGCTGMGNDQVRFDLAVKALG-DYQIVAPIR--EIQKEHTQtR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 158 NDLMEYAKQHGIPIPVTPKSpWSMDENLMHISYEAGilENPKNQAP-PGLYTKTQDPAKAPNSPDVLEIEFKKGVPVKVt 236
Cdd:PRK04527 155 AYEQKYLEERGFGVRAKQKA-YTINENLLGVTMSGG--EIDRWEAPgEGARGWCAPRSAWPTEALTVTIKFVEGEAVAL- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 237 nikDGTTRTtSLELFMYLNEVAGKHGVGRIDIVENRFIGMKSRGIYETPAGTILYHAHLDIEAFTMDREVRKIKQGLGLK 316
Cdd:PRK04527 231 ---DGKPLP-GAQILAKLNKLFAQYGVGRGVYTGDTVIGLKGRIVFEAPGLVSLLTAHRALEDAVLTKQQNRFKPDVARK 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6996911 317 FAELVYTGFWHSPECEFVRHCIQKSQERVEGKVQVSVFKGQVYILGRESPlSLYNEELVSMNVQGDYEPIDATGFINI 394
Cdd:PRK04527 307 WVELVYEGFYHDPLKTDIEAFLKSSQAKVNGEVTLETRGGRVDAVAVRSP-HLLNSKGATYAQSADWGVEEAEGFIKL 383
|
|
| PRK05370 |
PRK05370 |
argininosuccinate synthase; Validated |
7-390 |
1.92e-37 |
|
argininosuccinate synthase; Validated
Pssm-ID: 235434 Cd Length: 447 Bit Score: 140.88 E-value: 1.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 7 VVLAYSGGLDTSCILVWLKEQGYDVIAYLANIGQ--KEDFEEARKKALKLGAKKVFIEDVSKEFVEEFIwPAVQSSALYE 84
Cdd:PRK05370 14 VGIAFSGGLDTSAALLWMRQKGAVPYAYTANLGQpdEDDYDAIPRRAMEYGAENARLIDCRAQLVAEGI-AAIQCGAFHI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 85 D----RYLLGTSLARPCIARRQVEIAQREGAKYVSHGATGKGNDQVRFELtcYSLA--PQIKVIAPWRMPEFYNRFKGRN 158
Cdd:PRK05370 93 StggvTYFNTTPLGRAVTGTMLVAAMKEDGVNIWGDGSTYKGNDIERFYR--YGLLtnPELKIYKPWLDQDFIDELGGRA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 159 DLMEYAKQHGIPIPVTPKSPWSMDENLMHISYEAGILENpknqappgLYT--KTQDP--AKAPNSPDV------LEIEFK 228
Cdd:PRK05370 171 EMSEFLIAHGFDYKMSVEKAYSTDSNMLGATHEAKDLEH--------LNSgiKIVNPimGVAFWDEDVeikaeeVTVRFE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 229 KGVPVKVtnikDGTTRTTSLELFMYLNEVAGKHGVGRIDIVENRFIGMKSRGIYETPAGTILYHAHldieaftmDREVRK 308
Cdd:PRK05370 243 QGRPVAL----NGKTFSDPVELMLEANRIGGRHGLGMSDQIENRIIEAKSRGIYEAPGMALLHIAY--------ERLVTG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6996911 309 IK--------QGLGLKFAELVYTGFWHSPECEFVRHCIQKSQER-VEGKVQVSVFKGQVY-ILGRESPLSLYNEELVSMN 378
Cdd:PRK05370 311 IHnedtieqyRINGRRLGRLLYQGRWFDPQALMLRESLQRWVASaITGEVTLELRRGNDYsILNTVSPNLTYKPERLSME 390
|
410
....*....|....
gi 6996911 379 VQGD--YEPIDATG 390
Cdd:PRK05370 391 KVESaaFSPDDRIG 404
|
|
| QueC |
COG0603 |
7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and ... |
2-48 |
4.86e-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: 44.38 E-value: 4.86e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 6996911 2 SSKGSVVLaYSGGLDTSCILVWLKEQGYDVIA----YlaniGQKEDFE-EAR 48
Cdd:COG0603 1 MMKKAVVL-LSGGLDSTTCLAWALARGYEVYAlsfdY----GQRHRKElEAA 47
|
|
| QueC-like |
cd01995 |
7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC ... |
4-46 |
3.16e-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: 41.83 E-value: 3.16e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 6996911 4 KGSVVLAySGGLDTSCILVWLKEQGYDVIAYLANIGQKEDFEE 46
Cdd:cd01995 1 MKAVVLL-SGGLDSTTLLYWALKEGYEVHALTFDYGQRHAKEE 42
|
|
| QueC |
pfam06508 |
Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis ... |
7-45 |
6.23e-04 |
|
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: 40.68 E-value: 6.23e-04
10 20 30
....*....|....*....|....*....|....*....
gi 6996911 7 VVLAySGGLDTSCILVWLKEQGYDVIAYLANIGQKEDFE 45
Cdd:pfam06508 3 VVLL-SGGLDSTTCLAWAKKEGYEVYALSFDYGQRHRKE 40
|
|
| TIGR00364 |
TIGR00364 |
queuosine biosynthesis protein QueC; Members of this protein family are QueC, involved in ... |
8-45 |
1.61e-03 |
|
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: 39.30 E-value: 1.61e-03
10 20 30
....*....|....*....|....*....|....*...
gi 6996911 8 VLAYSGGLDTSCILVWLKEQGYDVIAYLANIGQKEDFE 45
Cdd:TIGR00364 2 IVVLSGGQDSTTCLLWAKDEGYEVHAVTFDYGQRHSRE 39
|
|
| tRNA_Me_trans |
pfam03054 |
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ... |
7-48 |
9.70e-03 |
|
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: 37.23 E-value: 9.70e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 6996911 7 VVLAYSGGLDTSCILVWLKEQGYDVIA-YLAN---------IGQ---KEDFEEAR 48
Cdd:pfam03054 3 VVVAMSGGVDSSVAAYLLKEQGHNVIGvFMKNwdeeqsldeEGKccsEEDLADAQ 57
|
|
| |
