|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00509 |
PRK00509 |
argininosuccinate synthase; Provisional |
1-396 |
0e+00 |
|
argininosuccinate synthase; Provisional
Pssm-ID: 234785 Cd Length: 399 Bit Score: 744.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 1 MKDKVVLAYSGGLDTSVAVKWLIEQ-GYDVIACCLDVGEGKDLDLVYQKALNMGAIESHVINATKEFAEDYVGYTIKGNL 79
Cdd:PRK00509 1 MKKKVVLAYSGGLDTSVIIKWLKETyGCEVIAFTADVGQGEELEPIREKALKSGASEIYVEDLREEFVRDYVFPAIRANA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 80 MYEQTYPLVSALSRPLISKKLVEIAHETNAVAIAHGCTGKGNDQVRFEVAIKALDPNLKVIAPVREWGW-SREEEIDYAK 158
Cdd:PRK00509 81 LYEGKYPLGTALARPLIAKKLVEIARKEGADAVAHGCTGKGNDQVRFELGIAALAPDLKVIAPWREWDLkSREELIAYAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 159 KHNIPVPIGKASPYSIDQNLWGRSNECGVLEDPYVAPPQDAYDLTSELEDTPDTADEILITFDQGIPTHINGEYYALDDL 238
Cdd:PRK00509 161 EHGIPIPVTKKSPYSIDANLWHRSIEGGILEDPWNEPPEDVYEWTVSPEDAPDEPEYVEIEFEKGVPVAINGEALSPAEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 239 ILYLNERAGKHGIGRIDHIENRLVGIKSREVYETPGAEVIIKAHQALETITLTKDVAHFKPIIEKQFAEQVYNGLWFSPL 318
Cdd:PRK00509 241 IEELNELAGKHGIGRIDIVENRLVGIKSRGVYETPGGTILIKAHRALESLTLDREVAHFKDELEPKYAELVYNGLWFSPL 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504427298 319 TDALKTFVDHTQKYVTGEVRVKLFKGHAIVNGRKSPYTLYNEKLATYTKEDAFNQQSAVGFIDIYGLPTQVNAMLHGG 396
Cdd:PRK00509 321 REALQAFIDETQEHVTGEVRLKLYKGNAIVVGRKSPNSLYDEDLATYEEDDVYDQKDAEGFIKLWGLPSKIAALVNKK 398
|
|
| ArgG |
COG0137 |
Argininosuccinate synthase [Amino acid transport and metabolism]; Argininosuccinate synthase ... |
3-396 |
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: 709.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 3 DKVVLAYSGGLDTSVAVKWLIEQ-GYDVIACCLDVGEGKDLDLVYQKALNMGAIESHVINATKEFAEDYVGYTIKGNLMY 81
Cdd:COG0137 1 KKVVLAYSGGLDTSVIIPWLKEKyGYEVIAVTADVGQGEDLEAIEEKALKLGASKAYVVDAREEFVEDYVFPAIKANALY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 82 EQTYPLVSALSRPLISKKLVEIAHETNAVAIAHGCTGKGNDQVRFEVAIKALDPNLKVIAPVREWGW-SREEEIDYAKKH 160
Cdd:COG0137 81 EGKYPLGTALARPLIAKKLVEIAREEGADAVAHGCTGKGNDQVRFELAIRALAPDLKIIAPWREWDLkSREEEIEYAEEH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 161 NIPVPIGKASPYSIDQNLWGRSNECGVLEDPYVAPPQDAYDLTSELEDTPDTADEILITFDQGIPTHINGEYYALDDLIL 240
Cdd:COG0137 161 GIPVPATKEKPYSIDENLWGRSIEGGELEDPWNEPPEDAYEWTVSPEDAPDEPEYVTITFEKGVPVALNGEKLSPVELIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 241 YLNERAGKHGIGRIDHIENRLVGIKSREVYETPGAEVIIKAHQALETITLTKDVAHFKPIIEKQFAEQVYNGLWFSPLTD 320
Cdd:COG0137 241 ELNEIGGKHGVGRIDIVENRLVGIKSRGVYEAPGATILITAHRALESLTLDRETLHFKDILDQKYAELVYNGLWFSPLRE 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504427298 321 ALKTFVDHTQKYVTGEVRVKLFKGHAIVNGRKSPYTLYNEKLATYTKEDAFNQQSAVGFIDIYGLPTQVNAMLHGG 396
Cdd:COG0137 321 ALDAFIDETQKRVTGTVRLKLYKGNATVVGRKSPYSLYDEDLATYEEDDVFDQKDAEGFIKLFGLPLRVAARVRKK 396
|
|
| ASS |
cd01999 |
argininosuccinate_synthase (ASS); Argininosuccinate synthase (ASS; EC 6.3.4.5) is a urea cycle ... |
3-386 |
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: 624.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 3 DKVVLAYSGGLDTSVAVKWLIEQ-GYDVIACCLDVGEGKDLDLVYQKALNMGAIESHVINATKEFAEDYVGYTIKGNLMY 81
Cdd:cd01999 1 KKVVLAYSGGLDTSVILKWLKEEyGYEVIAFTADLGQGDEEEEIEEKALKLGAVKVYVVDLREEFAEDYIFPAIKANAIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 82 EQTYPLVSALSRPLISKKLVEIAHETNAVAIAHGCTGKGNDQVRFEVAIKALDPNLKVIAPVREWG-WSREEEIDYAKKH 160
Cdd:cd01999 81 EGRYPLGTALARPLIAKKLVEVAREEGATAVAHGCTGKGNDQVRFELAIKALAPDLKVIAPWRDWNfLTRAEEIAYAKKH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 161 NIPVPIGKASPYSIDQNLWGRSNECGVLEDPYVAPPQDAYDLTSELEDTPDTADEILITFDQGIPTHINGEYYALDDLIL 240
Cdd:cd01999 161 GIPVPVTKKKPYSIDENLWGRSYEGGDLEDPWNEPPEDAFEWTVSPEKAPDEPEYVTIEFEKGVPVAVNGEKLDPVELIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 241 YLNERAGKHGIGRIDHIENRLVGIKSREVYETPGAEVIIKAHQALETITLTKDVAHFKPIIEKQFAEQVYNGLWFSPLTD 320
Cdd:cd01999 241 KLNEIAGRHGVGRIDIVENRLVGIKSRGVYEAPGATLLIKAHRDLEDLTLDREVLHFKDIVSRKYAELVYNGLWFDPLRE 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504427298 321 ALKTFVDHTQKYVTGEVRVKLFKGHAIVNGRKSPYTLYNEKLATYTKEDAFNQQSAVGFIDIYGLP 386
Cdd:cd01999 321 ALEAFIDKTQERVTGEVRLKLYKGNVIVVGRESPNSLYSEELATYEEGDGFDQKDAEGFIKIHGLQ 386
|
|
| Arginosuc_synth |
pfam00764 |
Arginosuccinate synthase; This family contains a PP-loop motif. |
6-389 |
0e+00 |
|
Arginosuccinate synthase; This family contains a PP-loop motif.
Pssm-ID: 279148 Cd Length: 386 Bit Score: 608.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 6 VLAYSGGLDTSVAVKWLIEQ-GYDVIACCLDVGEG-KDLDLVYQKALNMGAIESHVINATKEFAEDYVGYTIKGNLMYEQ 83
Cdd:pfam00764 1 VLAYSGGLDTSVCIPWLKEQgGYEVIAVAVDVGQGgEDIDEAREKALKLGAVKHYVIDAKEEFVEDYIFPAIQANALYED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 84 TYPLVSALSRPLISKKLVEIAHETNAVAIAHGCTGKGNDQVRFEVAIKALDPNLKVIAPVREWGWSREEEIDYAKKHNIP 163
Cdd:pfam00764 81 RYPLGTALARPLIAKKLVEAAKKEGASAVAHGCTGKGNDQVRFEVSFRSLAPDLKVIAPVRDPNLTREEEIEYAEEHGIP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 164 VPIGKASPYSIDQNLWGRSNECGVLEDPYVAPPQDAYDLTSELEDTPDTADEILITFDQGIPTHINGEYYALDDLILYLN 243
Cdd:pfam00764 161 IPVTKKSPYSIDENLWGRSIEAGILEDPWNAPPEDIYEWTKDPAKAPDEPDIVEIGFEKGVPVALDGEPVSPLELIEKLN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 244 ERAGKHGIGRIDHIENRLVGIKSREVYETPGAEVIIKAHQALETITLTKDVAHFKPIIEKQFAEQVYNGLWFSPLTDALK 323
Cdd:pfam00764 241 EIAGAHGVGRIDIVEDRLVGIKSREIYEAPAATVLITAHRDLENLTLTREVLRFKRIVDQKWAELVYDGLWFSPLKEALD 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504427298 324 TFVDHTQKYVTGEVRVKLFKGHAIVNGRKSPYTLYNEKLATYTKEDAFNQQSAVGFIDIYGLPTQV 389
Cdd:pfam00764 321 AFIDKTQERVTGTVRVKLHKGSAIVLGRRSPYSLYDEELVSYDEGDTFDQTDATGFIKIHGLQAKI 386
|
|
| argG |
TIGR00032 |
argininosuccinate synthase; argG in bacteria, ARG1 in Saccharomyces cerevisiae. There is a ... |
4-393 |
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: 552.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 4 KVVLAYSGGLDTSVAVKWLIEQGYDVIACCLDVGEG-KDLDLVYQKALNMGAIESHVINATKEFAEDYVGYTIKGNLMYE 82
Cdd:TIGR00032 1 KVVLAYSGGLDTSVCLKWLREKGYEVIAYTADVGQPeEDIDAIPEKALEYGAENHYTIDAREEFVKDYGFAAIQANAFYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 83 QTYPLVSALSRPLISKKLVEIAHETNAVAIAHGCTGKGNDQVRFEVAIKALDPNLKVIAPVREWGWSREEEIDYAKKHNI 162
Cdd:TIGR00032 81 GTYPLSTALARPLIAKKLVEAAKKEGANAVAHGCTGKGNDQERFERSIRLLNPDLKVIAPWRDLNFTREEEIEYAIQCGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 163 PVPIGKASPYSIDQNLWGRSNECGVLEDPYVAPPQDAYDLT-SELEDTPDTADEILITFDQGIPTHINGEYYALDDLILY 241
Cdd:TIGR00032 161 PYPMSKEKPYSIDENLWGRSIEAGILEDPSTEPPEDIYMWTkFPDEATPDEPEVVTIDFEQGVPVALNGVSLDPVELILE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 242 LNERAGKHGIGRIDHIENRLVGIKSREVYETPGAEVIIKAHQALETITLTKDVAHFKPIIEKQFAEQVYNGLWFSPLTDA 321
Cdd:TIGR00032 241 ANEIAGKHGVGRIDIIENRIIGLKSREIYEAPGAALLIIAHRDLETLTLTRDVLEFKDIVEEQYSELIYQGLWFDPLAEA 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504427298 322 LKTFVDHTQKYVTGEVRVKLFKGHAIVNGRKSPYTLYNEKLATYTKEDAFNQQSAVGFIDIYGLPTQVNAML 393
Cdd:TIGR00032 321 LDAFIRKTQERVTGTVRVKLFKGNAIVIGRTSPYSLYDEELVSMEKDDVFDPRDAIGFITMRGLQIKDYREK 392
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00509 |
PRK00509 |
argininosuccinate synthase; Provisional |
1-396 |
0e+00 |
|
argininosuccinate synthase; Provisional
Pssm-ID: 234785 Cd Length: 399 Bit Score: 744.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 1 MKDKVVLAYSGGLDTSVAVKWLIEQ-GYDVIACCLDVGEGKDLDLVYQKALNMGAIESHVINATKEFAEDYVGYTIKGNL 79
Cdd:PRK00509 1 MKKKVVLAYSGGLDTSVIIKWLKETyGCEVIAFTADVGQGEELEPIREKALKSGASEIYVEDLREEFVRDYVFPAIRANA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 80 MYEQTYPLVSALSRPLISKKLVEIAHETNAVAIAHGCTGKGNDQVRFEVAIKALDPNLKVIAPVREWGW-SREEEIDYAK 158
Cdd:PRK00509 81 LYEGKYPLGTALARPLIAKKLVEIARKEGADAVAHGCTGKGNDQVRFELGIAALAPDLKVIAPWREWDLkSREELIAYAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 159 KHNIPVPIGKASPYSIDQNLWGRSNECGVLEDPYVAPPQDAYDLTSELEDTPDTADEILITFDQGIPTHINGEYYALDDL 238
Cdd:PRK00509 161 EHGIPIPVTKKSPYSIDANLWHRSIEGGILEDPWNEPPEDVYEWTVSPEDAPDEPEYVEIEFEKGVPVAINGEALSPAEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 239 ILYLNERAGKHGIGRIDHIENRLVGIKSREVYETPGAEVIIKAHQALETITLTKDVAHFKPIIEKQFAEQVYNGLWFSPL 318
Cdd:PRK00509 241 IEELNELAGKHGIGRIDIVENRLVGIKSRGVYETPGGTILIKAHRALESLTLDREVAHFKDELEPKYAELVYNGLWFSPL 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504427298 319 TDALKTFVDHTQKYVTGEVRVKLFKGHAIVNGRKSPYTLYNEKLATYTKEDAFNQQSAVGFIDIYGLPTQVNAMLHGG 396
Cdd:PRK00509 321 REALQAFIDETQEHVTGEVRLKLYKGNAIVVGRKSPNSLYDEDLATYEEDDVYDQKDAEGFIKLWGLPSKIAALVNKK 398
|
|
| ArgG |
COG0137 |
Argininosuccinate synthase [Amino acid transport and metabolism]; Argininosuccinate synthase ... |
3-396 |
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: 709.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 3 DKVVLAYSGGLDTSVAVKWLIEQ-GYDVIACCLDVGEGKDLDLVYQKALNMGAIESHVINATKEFAEDYVGYTIKGNLMY 81
Cdd:COG0137 1 KKVVLAYSGGLDTSVIIPWLKEKyGYEVIAVTADVGQGEDLEAIEEKALKLGASKAYVVDAREEFVEDYVFPAIKANALY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 82 EQTYPLVSALSRPLISKKLVEIAHETNAVAIAHGCTGKGNDQVRFEVAIKALDPNLKVIAPVREWGW-SREEEIDYAKKH 160
Cdd:COG0137 81 EGKYPLGTALARPLIAKKLVEIAREEGADAVAHGCTGKGNDQVRFELAIRALAPDLKIIAPWREWDLkSREEEIEYAEEH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 161 NIPVPIGKASPYSIDQNLWGRSNECGVLEDPYVAPPQDAYDLTSELEDTPDTADEILITFDQGIPTHINGEYYALDDLIL 240
Cdd:COG0137 161 GIPVPATKEKPYSIDENLWGRSIEGGELEDPWNEPPEDAYEWTVSPEDAPDEPEYVTITFEKGVPVALNGEKLSPVELIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 241 YLNERAGKHGIGRIDHIENRLVGIKSREVYETPGAEVIIKAHQALETITLTKDVAHFKPIIEKQFAEQVYNGLWFSPLTD 320
Cdd:COG0137 241 ELNEIGGKHGVGRIDIVENRLVGIKSRGVYEAPGATILITAHRALESLTLDRETLHFKDILDQKYAELVYNGLWFSPLRE 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504427298 321 ALKTFVDHTQKYVTGEVRVKLFKGHAIVNGRKSPYTLYNEKLATYTKEDAFNQQSAVGFIDIYGLPTQVNAMLHGG 396
Cdd:COG0137 321 ALDAFIDETQKRVTGTVRLKLYKGNATVVGRKSPYSLYDEDLATYEEDDVFDQKDAEGFIKLFGLPLRVAARVRKK 396
|
|
| ASS |
cd01999 |
argininosuccinate_synthase (ASS); Argininosuccinate synthase (ASS; EC 6.3.4.5) is a urea cycle ... |
3-386 |
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: 624.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 3 DKVVLAYSGGLDTSVAVKWLIEQ-GYDVIACCLDVGEGKDLDLVYQKALNMGAIESHVINATKEFAEDYVGYTIKGNLMY 81
Cdd:cd01999 1 KKVVLAYSGGLDTSVILKWLKEEyGYEVIAFTADLGQGDEEEEIEEKALKLGAVKVYVVDLREEFAEDYIFPAIKANAIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 82 EQTYPLVSALSRPLISKKLVEIAHETNAVAIAHGCTGKGNDQVRFEVAIKALDPNLKVIAPVREWG-WSREEEIDYAKKH 160
Cdd:cd01999 81 EGRYPLGTALARPLIAKKLVEVAREEGATAVAHGCTGKGNDQVRFELAIKALAPDLKVIAPWRDWNfLTRAEEIAYAKKH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 161 NIPVPIGKASPYSIDQNLWGRSNECGVLEDPYVAPPQDAYDLTSELEDTPDTADEILITFDQGIPTHINGEYYALDDLIL 240
Cdd:cd01999 161 GIPVPVTKKKPYSIDENLWGRSYEGGDLEDPWNEPPEDAFEWTVSPEKAPDEPEYVTIEFEKGVPVAVNGEKLDPVELIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 241 YLNERAGKHGIGRIDHIENRLVGIKSREVYETPGAEVIIKAHQALETITLTKDVAHFKPIIEKQFAEQVYNGLWFSPLTD 320
Cdd:cd01999 241 KLNEIAGRHGVGRIDIVENRLVGIKSRGVYEAPGATLLIKAHRDLEDLTLDREVLHFKDIVSRKYAELVYNGLWFDPLRE 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504427298 321 ALKTFVDHTQKYVTGEVRVKLFKGHAIVNGRKSPYTLYNEKLATYTKEDAFNQQSAVGFIDIYGLP 386
Cdd:cd01999 321 ALEAFIDKTQERVTGEVRLKLYKGNVIVVGRESPNSLYSEELATYEEGDGFDQKDAEGFIKIHGLQ 386
|
|
| Arginosuc_synth |
pfam00764 |
Arginosuccinate synthase; This family contains a PP-loop motif. |
6-389 |
0e+00 |
|
Arginosuccinate synthase; This family contains a PP-loop motif.
Pssm-ID: 279148 Cd Length: 386 Bit Score: 608.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 6 VLAYSGGLDTSVAVKWLIEQ-GYDVIACCLDVGEG-KDLDLVYQKALNMGAIESHVINATKEFAEDYVGYTIKGNLMYEQ 83
Cdd:pfam00764 1 VLAYSGGLDTSVCIPWLKEQgGYEVIAVAVDVGQGgEDIDEAREKALKLGAVKHYVIDAKEEFVEDYIFPAIQANALYED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 84 TYPLVSALSRPLISKKLVEIAHETNAVAIAHGCTGKGNDQVRFEVAIKALDPNLKVIAPVREWGWSREEEIDYAKKHNIP 163
Cdd:pfam00764 81 RYPLGTALARPLIAKKLVEAAKKEGASAVAHGCTGKGNDQVRFEVSFRSLAPDLKVIAPVRDPNLTREEEIEYAEEHGIP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 164 VPIGKASPYSIDQNLWGRSNECGVLEDPYVAPPQDAYDLTSELEDTPDTADEILITFDQGIPTHINGEYYALDDLILYLN 243
Cdd:pfam00764 161 IPVTKKSPYSIDENLWGRSIEAGILEDPWNAPPEDIYEWTKDPAKAPDEPDIVEIGFEKGVPVALDGEPVSPLELIEKLN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 244 ERAGKHGIGRIDHIENRLVGIKSREVYETPGAEVIIKAHQALETITLTKDVAHFKPIIEKQFAEQVYNGLWFSPLTDALK 323
Cdd:pfam00764 241 EIAGAHGVGRIDIVEDRLVGIKSREIYEAPAATVLITAHRDLENLTLTREVLRFKRIVDQKWAELVYDGLWFSPLKEALD 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504427298 324 TFVDHTQKYVTGEVRVKLFKGHAIVNGRKSPYTLYNEKLATYTKEDAFNQQSAVGFIDIYGLPTQV 389
Cdd:pfam00764 321 AFIDKTQERVTGTVRVKLHKGSAIVLGRRSPYSLYDEELVSYDEGDTFDQTDATGFIKIHGLQAKI 386
|
|
| argG |
TIGR00032 |
argininosuccinate synthase; argG in bacteria, ARG1 in Saccharomyces cerevisiae. There is a ... |
4-393 |
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: 552.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 4 KVVLAYSGGLDTSVAVKWLIEQGYDVIACCLDVGEG-KDLDLVYQKALNMGAIESHVINATKEFAEDYVGYTIKGNLMYE 82
Cdd:TIGR00032 1 KVVLAYSGGLDTSVCLKWLREKGYEVIAYTADVGQPeEDIDAIPEKALEYGAENHYTIDAREEFVKDYGFAAIQANAFYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 83 QTYPLVSALSRPLISKKLVEIAHETNAVAIAHGCTGKGNDQVRFEVAIKALDPNLKVIAPVREWGWSREEEIDYAKKHNI 162
Cdd:TIGR00032 81 GTYPLSTALARPLIAKKLVEAAKKEGANAVAHGCTGKGNDQERFERSIRLLNPDLKVIAPWRDLNFTREEEIEYAIQCGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 163 PVPIGKASPYSIDQNLWGRSNECGVLEDPYVAPPQDAYDLT-SELEDTPDTADEILITFDQGIPTHINGEYYALDDLILY 241
Cdd:TIGR00032 161 PYPMSKEKPYSIDENLWGRSIEAGILEDPSTEPPEDIYMWTkFPDEATPDEPEVVTIDFEQGVPVALNGVSLDPVELILE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 242 LNERAGKHGIGRIDHIENRLVGIKSREVYETPGAEVIIKAHQALETITLTKDVAHFKPIIEKQFAEQVYNGLWFSPLTDA 321
Cdd:TIGR00032 241 ANEIAGKHGVGRIDIIENRIIGLKSREIYEAPGAALLIIAHRDLETLTLTRDVLEFKDIVEEQYSELIYQGLWFDPLAEA 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504427298 322 LKTFVDHTQKYVTGEVRVKLFKGHAIVNGRKSPYTLYNEKLATYTKEDAFNQQSAVGFIDIYGLPTQVNAML 393
Cdd:TIGR00032 321 LDAFIRKTQERVTGTVRVKLFKGNAIVIGRTSPYSLYDEELVSMEKDDVFDPRDAIGFITMRGLQIKDYREK 392
|
|
| PRK13820 |
PRK13820 |
argininosuccinate synthase; Provisional |
1-385 |
4.85e-169 |
|
argininosuccinate synthase; Provisional
Pssm-ID: 237521 Cd Length: 394 Bit Score: 478.27 E-value: 4.85e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 1 MKDKVVLAYSGGLDTSVAVKWLIEQ-GYD-VIACCLDVGEGK-DLDLVYQKALNMGaIESHVINATKEFAEDYVGYTIKG 77
Cdd:PRK13820 1 MMKKVVLAYSGGLDTSVCVPLLKEKyGYDeVITVTVDVGQPEeEIKEAEEKAKKLG-DKHYTIDAKEEFAKDYIFPAIKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 78 NLMYEqTYPLVSALSRPLISKKLVEIAHETNAVAIAHGCTGKGNDQVRFEVAIKALDpnLKVIAPVREWGWSREEEIDYA 157
Cdd:PRK13820 80 NALYE-GYPLGTALARPLIAEKIVEVAEKEGASAIAHGCTGKGNDQLRFEAVFRASD--LEVIAPIRELNLTREWEIEYA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 158 KKHNIPVPIGKASPYSIDQNLWGRSNECGVLEDPYVAPPQDAYDLTSELEDTPDTADEILITFDQGIPTHINGEYYALDD 237
Cdd:PRK13820 157 KEKGIPVPVGKEKPWSIDENLWSRSIEGGKLEDPAFEPPEEIYAWTVSPEDAPDEPEIVEIEFEEGVPVAINGEKMDGVE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 238 LILYLNERAGKHGIGRIDHIENRLVGIKSREVYETPGAEVIIKAHQALETITLTKDVAHFKPIIEKQFAEQVYNGLWFSP 317
Cdd:PRK13820 237 LIRKLNEIAGKHGVGRTDMMEDRVLGLKSRENYEHPAATVLLTAHKALEQLVLTREELKFKEIVDSKWAELAYEGLVDEP 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504427298 318 LTDALKTFVDHTQKYVTGEVRVKLFKGHAIVNGRKSPYTLYNEKLATYTKEDaFNQQSAVGFIDIYGL 385
Cdd:PRK13820 317 LREDLNAFIDKTQERVTGTVTVKLYKGSARVVGRESPYALYSEELVSFDSKT-IDQRDAEGMAKYHGL 383
|
|
| PLN00200 |
PLN00200 |
argininosuccinate synthase; Provisional |
1-396 |
5.49e-169 |
|
argininosuccinate synthase; Provisional
Pssm-ID: 177791 Cd Length: 404 Bit Score: 478.47 E-value: 5.49e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 1 MKDKVVLAYSGGLDTSVAVKWLIEQ-GYDVIACCLDVGEG-KDLDLVYQKALNMGAIESHVINATKEFAEDYVGYTIKGN 78
Cdd:PLN00200 4 KLNKVVLAYSGGLDTSVILKWLRENyGCEVVCFTADVGQGiEELEGLEAKAKASGAKQLVVKDLREEFVRDYIFPCLRAN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 79 LMYEQTYPLVSALSRPLISKKLVEIAHETNAVAIAHGCTGKGNDQVRFEVAIKALDPNLKVIAPVREWGW-SREEEIDYA 157
Cdd:PLN00200 84 AIYEGKYLLGTSMARPLIAKAMVDIAKEVGADAVAHGATGKGNDQVRFELTFFALNPELKVVAPWREWDIkGREDLIEYA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 158 KKHNIPVPIGKASPYSIDQNLWGRSNECGVLEDPYVAPPQDAYDLTSELEDTPDTADEILITFDQGIPTHINGEYYALDD 237
Cdd:PLN00200 164 KKHNIPVPVTKKSIYSRDRNLWHISYEGDILEDPANEPKEDMFMMSVSPEAAPDQPEYIEIEFEKGLPVAINGKTLSPAT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 238 LILYLNERAGKHGIGRIDHIENRLVGIKSREVYETPGAEVIIKAHQALETITLTKDVAHFKPIIEKQFAEQVYNGLWFSP 317
Cdd:PLN00200 244 LLTKLNEIGGKHGIGRIDMVENRFVGMKSRGVYETPGGTILFAAHRELESLTLDRETMQVKDSLALKYAELVYNGFWFDP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 318 LTDALKTFVDHTQKYVTGEVRVKLFKGHAIVNGRKSPYTLYNEKLATYTKED-AFNQQSAVGFIDIYGLPTQVNAMLHGG 396
Cdd:PLN00200 324 ERESMDAFMEKITETTTGSVRLKLYKGNVSVAGRKSPYSLYRQDISSFEEGGgIYNQADAAGFIRLYALRLRTRAMLRKK 403
|
|
| PRK04527 |
PRK04527 |
argininosuccinate synthase; Provisional |
1-395 |
2.76e-82 |
|
argininosuccinate synthase; Provisional
Pssm-ID: 235305 Cd Length: 400 Bit Score: 257.46 E-value: 2.76e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 1 MKDKVVLAYSGGLDTSVAVKWLIEQGYDVIACCLDVG--EGKDLDLVYQKALNMGAIESHVINATKEFAEDYVGYTIKGN 78
Cdd:PRK04527 1 SSKDIVLAFSGGLDTSFCIPYLQERGYAVHTVFADTGgvDAEERDFIEKRAAELGAASHVTVDGGPAIWEGFVKPLVWAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 79 LMYEQTYPLVSAlSRPLISKKLVEIAHETNAVAIAHGCTGKGNDQVRFEVAIKALDpNLKVIAPVRE----WGWSREEEI 154
Cdd:PRK04527 81 EGYQGQYPLLVS-DRYLIVDAALKRAEELGTRIIAHGCTGMGNDQVRFDLAVKALG-DYQIVAPIREiqkeHTQTRAYEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 155 DYAKKHNIPVPiGKASPYSIDQNLWGRSNECGVLeDPYVAPPQDAYDLTSELEDTPDTADEILITFDQGIPTHINGEYYA 234
Cdd:PRK04527 159 KYLEERGFGVR-AKQKAYTINENLLGVTMSGGEI-DRWEAPGEGARGWCAPRSAWPTEALTVTIKFVEGEAVALDGKPLP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 235 LDDLILYLNERAGKHGIGRIDHIENRLVGIKSREVYETPGAEVIIKAHQALETITLTKDVAHFKPIIEKQFAEQVYNGLW 314
Cdd:PRK04527 237 GAQILAKLNKLFAQYGVGRGVYTGDTVIGLKGRIVFEAPGLVSLLTAHRALEDAVLTKQQNRFKPDVARKWVELVYEGFY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 315 FSPLTDALKTFVDHTQKYVTGEVRVKLFKGHAIVNGRKSPYTLyNEKLATYTKEDAFNQQSAVGFIDIYGLPT----QVN 390
Cdd:PRK04527 317 HDPLKTDIEAFLKSSQAKVNGEVTLETRGGRVDAVAVRSPHLL-NSKGATYAQSADWGVEEAEGFIKLFGMSStlyaQVN 395
|
....*
gi 504427298 391 AMLHG 395
Cdd:PRK04527 396 RSLRS 400
|
|
| PRK05370 |
PRK05370 |
argininosuccinate synthase; Validated |
4-370 |
4.77e-35 |
|
argininosuccinate synthase; Validated
Pssm-ID: 235434 Cd Length: 447 Bit Score: 134.33 E-value: 4.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 4 KVVLAYSGGLDTSVAVKWLIEQGYDVIACCLDVGE--GKDLDLVYQKALNMGAIESHVINATKEFAEDYV------GYTI 75
Cdd:PRK05370 13 RVGIAFSGGLDTSAALLWMRQKGAVPYAYTANLGQpdEDDYDAIPRRAMEYGAENARLIDCRAQLVAEGIaaiqcgAFHI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 76 K-GNLMYEQTYPLVSALSRPLiskkLVEIAHETNAVAIAHGCTGKGNDQVRFEVAIKALDPNLKVIAP------VREWGw 148
Cdd:PRK05370 93 StGGVTYFNTTPLGRAVTGTM----LVAAMKEDGVNIWGDGSTYKGNDIERFYRYGLLTNPELKIYKPwldqdfIDELG- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 149 SREEEIDYAKKHNIPVPIGKASPYSIDQNLWGRSNECGVLE---------DPY--VAPPQDAYDLTSEledtpdtadEIL 217
Cdd:PRK05370 168 GRAEMSEFLIAHGFDYKMSVEKAYSTDSNMLGATHEAKDLEhlnsgikivNPImgVAFWDEDVEIKAE---------EVT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 218 ITFDQGIPTHINGEYYALD-DLILYLNERAGKHGIGRIDHIENRLVGIKSREVYETPGAEVIIKAHQALETitltkdVAH 296
Cdd:PRK05370 239 VRFEQGRPVALNGKTFSDPvELMLEANRIGGRHGLGMSDQIENRIIEAKSRGIYEAPGMALLHIAYERLVT------GIH 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 297 FKPIIEKQFAEQ------VYNGLWFSP----LTDALKTFVdhtQKYVTGEVRVKLFKG--HAIVNGRkSPYTLYN-EKLA 363
Cdd:PRK05370 313 NEDTIEQYRINGrrlgrlLYQGRWFDPqalmLRESLQRWV---ASAITGEVTLELRRGndYSILNTV-SPNLTYKpERLS 388
|
....*..
gi 504427298 364 TYTKEDA 370
Cdd:PRK05370 389 MEKVESA 395
|
|
| MnmA_TRMU-like |
cd01998 |
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ... |
4-83 |
5.29e-07 |
|
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: 50.97 E-value: 5.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 4 KVVLAYSGGLDTSVAVKWLIEQGYDVIA---------------CCldvgEGKDLDLVYQKALNMGaIESHVINATKEFAE 68
Cdd:cd01998 1 KVAVAMSGGVDSSVAAALLKEQGYDVIGvfmknwddednekggCC----SEEDIEDARRVADQLG-IPLYVVDFSEEYWE 75
|
90
....*....|....*
gi 504427298 69 DYVGYTIKGnlmYEQ 83
Cdd:cd01998 76 RVFDPFLEE---YKA 87
|
|
| tRNA_Me_trans |
pfam03054 |
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ... |
3-136 |
3.14e-06 |
|
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: 47.63 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 3 DKVVLAYSGGLDTSVAVKWLIEQGYDVIA---------CCLDvGEGK---DLDLVY-QKALNMGAIESHVINATKEFAED 69
Cdd:pfam03054 1 MKVVVAMSGGVDSSVAAYLLKEQGHNVIGvfmknwdeeQSLD-EEGKccsEEDLADaQRVCEQLGIPLYVVNFEKEYWED 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504427298 70 YVGYTIKGnlmYE--QTyPLVSALSRPLIS-KKLVEIAHET---NAVAIAHGCTGKGNDQVRFEVAIkALDPN 136
Cdd:pfam03054 80 VFEPFLDE---YKngRT-PNPDVLCNKEIKfGALLDYALENlgaDYVATGHYARVSLNKDGGSELLR-ALDKN 147
|
|
| mnmA |
PRK00143 |
tRNA-specific 2-thiouridylase MnmA; Reviewed |
4-77 |
2.78e-05 |
|
tRNA-specific 2-thiouridylase MnmA; Reviewed
Pssm-ID: 234664 [Multi-domain] Cd Length: 346 Bit Score: 45.83 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 4 KVVLAYSGGLDTSVAVKWLIEQGYDVI----------------ACCldvgEGKDLDLVYQKALNMGaIESHVINATKEFA 67
Cdd:PRK00143 2 RVVVGMSGGVDSSVAAALLKEQGYEVIgvfmklwddddetgkgGCC----AEEDIADARRVADKLG-IPHYVVDFEKEFW 76
|
90
....*....|
gi 504427298 68 EDYVGYTIKG 77
Cdd:PRK00143 77 DRVIDYFLDE 86
|
|
| QueC |
COG0603 |
7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and ... |
1-61 |
6.48e-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: 44.00 E-value: 6.48e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504427298 1 MKDKVVLAYSGGLDTSVAVKWLIEQGYDVIACCLDVG--EGKDLDLVYQKALNMGAIESHVIN 61
Cdd:COG0603 1 MMKKAVVLLSGGLDSTTCLAWALARGYEVYALSFDYGqrHRKELEAARRIAKALGVGEHKVID 63
|
|
| PRK14664 |
PRK14664 |
tRNA-specific 2-thiouridylase MnmA; Provisional |
2-115 |
1.22e-04 |
|
tRNA-specific 2-thiouridylase MnmA; Provisional
Pssm-ID: 173127 [Multi-domain] Cd Length: 362 Bit Score: 43.79 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 2 KDKVVLAYSGGLDTSVAVKWLIEQGYDVIACCLDVGeGKDLDLVYQKALNMGaIESHVINATKEFAEDYVGYTIKGNLMY 81
Cdd:PRK14664 5 KKRVLVGMSGGIDSTATCLMLQEQGYEIVGVTMRVW-GDEPQDARELAARMG-IEHYVADERVPFKDTIVKNFIDEYRQG 82
|
90 100 110
....*....|....*....|....*....|....*
gi 504427298 82 EQTYPLVsaLSRPLISKK-LVEIAHETNAVAIAHG 115
Cdd:PRK14664 83 RTPNPCV--MCNPLFKFRmLIEWADKLGCAWIATG 115
|
|
| MnmA |
COG0482 |
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ... |
4-77 |
1.76e-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: 43.12 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427298 4 KVVLAYSGGLDTSVAVKWLIEQGYDVI----------------ACCldvgEGKDLDLVYQKALNMGaIESHVINATKEFA 67
Cdd:COG0482 2 RVVVGMSGGVDSSVAAALLKEQGYEVIgvtmklwddddasgsgGCC----SLEDIEDARRVADKLG-IPHYVVDFEEEFK 76
|
90
....*....|
gi 504427298 68 EDYVGYTIKG 77
Cdd:COG0482 77 DRVIDYFLDE 86
|
|
| |
