|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13820 |
PRK13820 |
argininosuccinate synthase; Provisional |
1-394 |
0e+00 |
|
argininosuccinate synthase; Provisional
Pssm-ID: 237521 Cd Length: 394 Bit Score: 805.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 1 MVKKVALAYSGGLDTSVCIPILKEKYGYDEVITISVDVGQPEEEIKKADAKAEKISNKHYTIDAKEEFVKDYIFPLIKAN 80
Cdd:PRK13820 1 MMKKVVLAYSGGLDTSVCVPLLKEKYGYDEVITVTVDVGQPEEEIKEAEEKAKKLGDKHYTIDAKEEFAKDYIFPAIKAN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 81 GDYEGYVMGTSVARPLIAKKVVEAAIKEGAVALAHGCTGKGNDQLRFEAVFRQTDMDVIAPMREMNLTREWEIDYAKEHG 160
Cdd:PRK13820 81 ALYEGYPLGTALARPLIAEKIVEVAEKEGASAIAHGCTGKGNDQLRFEAVFRASDLEVIAPIRELNLTREWEIEYAKEKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 161 IPVEVTKAKPWSVDENIWSRSIEGGKLEDPSFVPPEEIFEWTKSAEDAPNEPRIVDIDFEAGVPVALDGEKLGGYALVRK 240
Cdd:PRK13820 161 IPVPVGKEKPWSIDENLWSRSIEGGKLEDPAFEPPEEIYAWTVSPEDAPDEPEIVEIEFEEGVPVAINGEKMDGVELIRK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 241 LNEIAGENGVGRTDMIEDRVLGLKARENYEHPAATVLLAAHADLEKLVLTRGELKFKKIVDEQWSELAYYGLVDEPLYAD 320
Cdd:PRK13820 241 LNEIAGKHGVGRTDMMEDRVLGLKSRENYEHPAATVLLTAHKALEQLVLTREELKFKEIVDSKWAELAYEGLVDEPLRED 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499331636 321 LNAFIDKSQERVTGTVKVKLYKGALTILARSSPNALYSEDLVSFDSQTIDQKDAEGFAKYHGFQARMYRKVMEK 394
Cdd:PRK13820 321 LNAFIDKTQERVTGTVTVKLYKGSARVVGRESPYALYSEELVSFDSKTIDQRDAEGMAKYHGLQARLYNKVKRK 394
|
|
| Arginosuc_synth |
pfam00764 |
Arginosuccinate synthase; This family contains a PP-loop motif. |
7-387 |
0e+00 |
|
Arginosuccinate synthase; This family contains a PP-loop motif.
Pssm-ID: 279148 Cd Length: 386 Bit Score: 660.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 7 LAYSGGLDTSVCIPILKEKYGYdEVITISVDVGQPEEEIKKADAKAEKISN-KHYTIDAKEEFVKDYIFPLIKANGDYEG 85
Cdd:pfam00764 2 LAYSGGLDTSVCIPWLKEQGGY-EVIAVAVDVGQGGEDIDEAREKALKLGAvKHYVIDAKEEFVEDYIFPAIQANALYED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 86 -YVMGTSVARPLIAKKVVEAAIKEGAVALAHGCTGKGNDQLRFEAVFRQT--DMDVIAPMREMNLTREWEIDYAKEHGIP 162
Cdd:pfam00764 81 rYPLGTALARPLIAKKLVEAAKKEGASAVAHGCTGKGNDQVRFEVSFRSLapDLKVIAPVRDPNLTREEEIEYAEEHGIP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 163 VEVTKAKPWSVDENIWSRSIEGGKLEDPSFVPPEEIFEWTKSAEDAPNEPRIVDIDFEAGVPVALDGEKLGGYALVRKLN 242
Cdd:pfam00764 161 IPVTKKSPYSIDENLWGRSIEAGILEDPWNAPPEDIYEWTKDPAKAPDEPDIVEIGFEKGVPVALDGEPVSPLELIEKLN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 243 EIAGENGVGRTDMIEDRVLGLKARENYEHPAATVLLAAHADLEKLVLTRGELKFKKIVDEQWSELAYYGLVDEPLYADLN 322
Cdd:pfam00764 241 EIAGAHGVGRIDIVEDRLVGIKSREIYEAPAATVLITAHRDLENLTLTREVLRFKRIVDQKWAELVYDGLWFSPLKEALD 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499331636 323 AFIDKSQERVTGTVKVKLYKGALTILARSSPNALYSEDLVSFD-SQTIDQKDAEGFAKYHGFQARM 387
Cdd:pfam00764 321 AFIDKTQERVTGTVRVKLHKGSAIVLGRRSPYSLYDEELVSYDeGDTFDQTDATGFIKIHGLQAKI 386
|
|
| ArgG |
COG0137 |
Argininosuccinate synthase [Amino acid transport and metabolism]; Argininosuccinate synthase ... |
3-394 |
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: 656.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 3 KKVALAYSGGLDTSVCIPILKEKYGYdEVITISVDVGQpEEEIKKADAKAEKI-SNKHYTIDAKEEFVKDYIFPLIKANG 81
Cdd:COG0137 1 KKVVLAYSGGLDTSVIIPWLKEKYGY-EVIAVTADVGQ-GEDLEAIEEKALKLgASKAYVVDAREEFVEDYVFPAIKANA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 82 DYEG-YVMGTSVARPLIAKKVVEAAIKEGAVALAHGCTGKGNDQLRFEAVFRQT--DMDVIAPMREMNL-TREWEIDYAK 157
Cdd:COG0137 79 LYEGkYPLGTALARPLIAKKLVEIAREEGADAVAHGCTGKGNDQVRFELAIRALapDLKIIAPWREWDLkSREEEIEYAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 158 EHGIPVEVTKAKPWSVDENIWSRSIEGGKLEDPSFVPPEEIFEWTKSAEDAPNEPRIVDIDFEAGVPVALDGEKLGGYAL 237
Cdd:COG0137 159 EHGIPVPATKEKPYSIDENLWGRSIEGGELEDPWNEPPEDAYEWTVSPEDAPDEPEYVTITFEKGVPVALNGEKLSPVEL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 238 VRKLNEIAGENGVGRTDMIEDRVLGLKARENYEHPAATVLLAAHADLEKLVLTRGELKFKKIVDEQWSELAYYGLVDEPL 317
Cdd:COG0137 239 IEELNEIGGKHGVGRIDIVENRLVGIKSRGVYEAPGATILITAHRALESLTLDRETLHFKDILDQKYAELVYNGLWFSPL 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499331636 318 YADLNAFIDKSQERVTGTVKVKLYKGALTILARSSPNALYSEDLVSFD-SQTIDQKDAEGFAKYHGFQARMYRKVMEK 394
Cdd:COG0137 319 REALDAFIDETQKRVTGTVRLKLYKGNATVVGRKSPYSLYDEDLATYEeDDVFDQKDAEGFIKLFGLPLRVAARVRKK 396
|
|
| ASS |
cd01999 |
argininosuccinate_synthase (ASS); Argininosuccinate synthase (ASS; EC 6.3.4.5) is a urea cycle ... |
3-384 |
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: 596.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 3 KKVALAYSGGLDTSVCIPILKEKYGYdEVITISVDVGQPEEEIKkADAKAEKISN-KHYTIDAKEEFVKDYIFPLIKANG 81
Cdd:cd01999 1 KKVVLAYSGGLDTSVILKWLKEEYGY-EVIAFTADLGQGDEEEE-IEEKALKLGAvKVYVVDLREEFAEDYIFPAIKANA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 82 DYEG-YVMGTSVARPLIAKKVVEAAIKEGAVALAHGCTGKGNDQLRFEAVFR--QTDMDVIAPMREMNL-TREWEIDYAK 157
Cdd:cd01999 79 IYEGrYPLGTALARPLIAKKLVEVAREEGATAVAHGCTGKGNDQVRFELAIKalAPDLKVIAPWRDWNFlTRAEEIAYAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 158 EHGIPVEVTKAKPWSVDENIWSRSIEGGKLEDPSFVPPEEIFEWTKSAEDAPNEPRIVDIDFEAGVPVALDGEKLGGYAL 237
Cdd:cd01999 159 KHGIPVPVTKKKPYSIDENLWGRSYEGGDLEDPWNEPPEDAFEWTVSPEKAPDEPEYVTIEFEKGVPVAVNGEKLDPVEL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 238 VRKLNEIAGENGVGRTDMIEDRVLGLKARENYEHPAATVLLAAHADLEKLVLTRGELKFKKIVDEQWSELAYYGLVDEPL 317
Cdd:cd01999 239 IEKLNEIAGRHGVGRIDIVENRLVGIKSRGVYEAPGATLLIKAHRDLEDLTLDREVLHFKDIVSRKYAELVYNGLWFDPL 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499331636 318 YADLNAFIDKSQERVTGTVKVKLYKGALTILARSSPNALYSEDLVSFDS-QTIDQKDAEGFAKYHGFQ 384
Cdd:cd01999 319 REALEAFIDKTQERVTGEVRLKLYKGNVIVVGRESPNSLYSEELATYEEgDGFDQKDAEGFIKIHGLQ 386
|
|
| argG |
TIGR00032 |
argininosuccinate synthase; argG in bacteria, ARG1 in Saccharomyces cerevisiae. There is a ... |
4-392 |
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: 546.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 4 KVALAYSGGLDTSVCIPILKEKyGYdEVITISVDVGQPEEEIKKADAKAEKISN-KHYTIDAKEEFVKDYIFPLIKANGD 82
Cdd:TIGR00032 1 KVVLAYSGGLDTSVCLKWLREK-GY-EVIAYTADVGQPEEDIDAIPEKALEYGAeNHYTIDAREEFVKDYGFAAIQANAF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 83 YEG-YVMGTSVARPLIAKKVVEAAIKEGAVALAHGCTGKGNDQLRFEAVFR--QTDMDVIAPMREMNLTREWEIDYAKEH 159
Cdd:TIGR00032 79 YEGtYPLSTALARPLIAKKLVEAAKKEGANAVAHGCTGKGNDQERFERSIRllNPDLKVIAPWRDLNFTREEEIEYAIQC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 160 GIPVEVTKAKPWSVDENIWSRSIEGGKLEDPSFVPPEEIFEWTKSA-EDAPNEPRIVDIDFEAGVPVALDGEKLGGYALV 238
Cdd:TIGR00032 159 GIPYPMSKEKPYSIDENLWGRSIEAGILEDPSTEPPEDIYMWTKFPdEATPDEPEVVTIDFEQGVPVALNGVSLDPVELI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 239 RKLNEIAGENGVGRTDMIEDRVLGLKARENYEHPAATVLLAAHADLEKLVLTRGELKFKKIVDEQWSELAYYGLVDEPLY 318
Cdd:TIGR00032 239 LEANEIAGKHGVGRIDIIENRIIGLKSREIYEAPGAALLIIAHRDLETLTLTRDVLEFKDIVEEQYSELIYQGLWFDPLA 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499331636 319 ADLNAFIDKSQERVTGTVKVKLYKGALTILARSSPNALYSEDLVSFDSQT-IDQKDAEGFAKYHGFQARMYRKVM 392
Cdd:TIGR00032 319 EALDAFIRKTQERVTGTVRVKLFKGNAIVIGRTSPYSLYDEELVSMEKDDvFDPRDAIGFITMRGLQIKDYREKK 393
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13820 |
PRK13820 |
argininosuccinate synthase; Provisional |
1-394 |
0e+00 |
|
argininosuccinate synthase; Provisional
Pssm-ID: 237521 Cd Length: 394 Bit Score: 805.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 1 MVKKVALAYSGGLDTSVCIPILKEKYGYDEVITISVDVGQPEEEIKKADAKAEKISNKHYTIDAKEEFVKDYIFPLIKAN 80
Cdd:PRK13820 1 MMKKVVLAYSGGLDTSVCVPLLKEKYGYDEVITVTVDVGQPEEEIKEAEEKAKKLGDKHYTIDAKEEFAKDYIFPAIKAN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 81 GDYEGYVMGTSVARPLIAKKVVEAAIKEGAVALAHGCTGKGNDQLRFEAVFRQTDMDVIAPMREMNLTREWEIDYAKEHG 160
Cdd:PRK13820 81 ALYEGYPLGTALARPLIAEKIVEVAEKEGASAIAHGCTGKGNDQLRFEAVFRASDLEVIAPIRELNLTREWEIEYAKEKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 161 IPVEVTKAKPWSVDENIWSRSIEGGKLEDPSFVPPEEIFEWTKSAEDAPNEPRIVDIDFEAGVPVALDGEKLGGYALVRK 240
Cdd:PRK13820 161 IPVPVGKEKPWSIDENLWSRSIEGGKLEDPAFEPPEEIYAWTVSPEDAPDEPEIVEIEFEEGVPVAINGEKMDGVELIRK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 241 LNEIAGENGVGRTDMIEDRVLGLKARENYEHPAATVLLAAHADLEKLVLTRGELKFKKIVDEQWSELAYYGLVDEPLYAD 320
Cdd:PRK13820 241 LNEIAGKHGVGRTDMMEDRVLGLKSRENYEHPAATVLLTAHKALEQLVLTREELKFKEIVDSKWAELAYEGLVDEPLRED 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499331636 321 LNAFIDKSQERVTGTVKVKLYKGALTILARSSPNALYSEDLVSFDSQTIDQKDAEGFAKYHGFQARMYRKVMEK 394
Cdd:PRK13820 321 LNAFIDKTQERVTGTVTVKLYKGSARVVGRESPYALYSEELVSFDSKTIDQRDAEGMAKYHGLQARLYNKVKRK 394
|
|
| Arginosuc_synth |
pfam00764 |
Arginosuccinate synthase; This family contains a PP-loop motif. |
7-387 |
0e+00 |
|
Arginosuccinate synthase; This family contains a PP-loop motif.
Pssm-ID: 279148 Cd Length: 386 Bit Score: 660.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 7 LAYSGGLDTSVCIPILKEKYGYdEVITISVDVGQPEEEIKKADAKAEKISN-KHYTIDAKEEFVKDYIFPLIKANGDYEG 85
Cdd:pfam00764 2 LAYSGGLDTSVCIPWLKEQGGY-EVIAVAVDVGQGGEDIDEAREKALKLGAvKHYVIDAKEEFVEDYIFPAIQANALYED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 86 -YVMGTSVARPLIAKKVVEAAIKEGAVALAHGCTGKGNDQLRFEAVFRQT--DMDVIAPMREMNLTREWEIDYAKEHGIP 162
Cdd:pfam00764 81 rYPLGTALARPLIAKKLVEAAKKEGASAVAHGCTGKGNDQVRFEVSFRSLapDLKVIAPVRDPNLTREEEIEYAEEHGIP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 163 VEVTKAKPWSVDENIWSRSIEGGKLEDPSFVPPEEIFEWTKSAEDAPNEPRIVDIDFEAGVPVALDGEKLGGYALVRKLN 242
Cdd:pfam00764 161 IPVTKKSPYSIDENLWGRSIEAGILEDPWNAPPEDIYEWTKDPAKAPDEPDIVEIGFEKGVPVALDGEPVSPLELIEKLN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 243 EIAGENGVGRTDMIEDRVLGLKARENYEHPAATVLLAAHADLEKLVLTRGELKFKKIVDEQWSELAYYGLVDEPLYADLN 322
Cdd:pfam00764 241 EIAGAHGVGRIDIVEDRLVGIKSREIYEAPAATVLITAHRDLENLTLTREVLRFKRIVDQKWAELVYDGLWFSPLKEALD 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499331636 323 AFIDKSQERVTGTVKVKLYKGALTILARSSPNALYSEDLVSFD-SQTIDQKDAEGFAKYHGFQARM 387
Cdd:pfam00764 321 AFIDKTQERVTGTVRVKLHKGSAIVLGRRSPYSLYDEELVSYDeGDTFDQTDATGFIKIHGLQAKI 386
|
|
| ArgG |
COG0137 |
Argininosuccinate synthase [Amino acid transport and metabolism]; Argininosuccinate synthase ... |
3-394 |
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: 656.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 3 KKVALAYSGGLDTSVCIPILKEKYGYdEVITISVDVGQpEEEIKKADAKAEKI-SNKHYTIDAKEEFVKDYIFPLIKANG 81
Cdd:COG0137 1 KKVVLAYSGGLDTSVIIPWLKEKYGY-EVIAVTADVGQ-GEDLEAIEEKALKLgASKAYVVDAREEFVEDYVFPAIKANA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 82 DYEG-YVMGTSVARPLIAKKVVEAAIKEGAVALAHGCTGKGNDQLRFEAVFRQT--DMDVIAPMREMNL-TREWEIDYAK 157
Cdd:COG0137 79 LYEGkYPLGTALARPLIAKKLVEIAREEGADAVAHGCTGKGNDQVRFELAIRALapDLKIIAPWREWDLkSREEEIEYAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 158 EHGIPVEVTKAKPWSVDENIWSRSIEGGKLEDPSFVPPEEIFEWTKSAEDAPNEPRIVDIDFEAGVPVALDGEKLGGYAL 237
Cdd:COG0137 159 EHGIPVPATKEKPYSIDENLWGRSIEGGELEDPWNEPPEDAYEWTVSPEDAPDEPEYVTITFEKGVPVALNGEKLSPVEL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 238 VRKLNEIAGENGVGRTDMIEDRVLGLKARENYEHPAATVLLAAHADLEKLVLTRGELKFKKIVDEQWSELAYYGLVDEPL 317
Cdd:COG0137 239 IEELNEIGGKHGVGRIDIVENRLVGIKSRGVYEAPGATILITAHRALESLTLDRETLHFKDILDQKYAELVYNGLWFSPL 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499331636 318 YADLNAFIDKSQERVTGTVKVKLYKGALTILARSSPNALYSEDLVSFD-SQTIDQKDAEGFAKYHGFQARMYRKVMEK 394
Cdd:COG0137 319 REALDAFIDETQKRVTGTVRLKLYKGNATVVGRKSPYSLYDEDLATYEeDDVFDQKDAEGFIKLFGLPLRVAARVRKK 396
|
|
| ASS |
cd01999 |
argininosuccinate_synthase (ASS); Argininosuccinate synthase (ASS; EC 6.3.4.5) is a urea cycle ... |
3-384 |
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: 596.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 3 KKVALAYSGGLDTSVCIPILKEKYGYdEVITISVDVGQPEEEIKkADAKAEKISN-KHYTIDAKEEFVKDYIFPLIKANG 81
Cdd:cd01999 1 KKVVLAYSGGLDTSVILKWLKEEYGY-EVIAFTADLGQGDEEEE-IEEKALKLGAvKVYVVDLREEFAEDYIFPAIKANA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 82 DYEG-YVMGTSVARPLIAKKVVEAAIKEGAVALAHGCTGKGNDQLRFEAVFR--QTDMDVIAPMREMNL-TREWEIDYAK 157
Cdd:cd01999 79 IYEGrYPLGTALARPLIAKKLVEVAREEGATAVAHGCTGKGNDQVRFELAIKalAPDLKVIAPWRDWNFlTRAEEIAYAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 158 EHGIPVEVTKAKPWSVDENIWSRSIEGGKLEDPSFVPPEEIFEWTKSAEDAPNEPRIVDIDFEAGVPVALDGEKLGGYAL 237
Cdd:cd01999 159 KHGIPVPVTKKKPYSIDENLWGRSYEGGDLEDPWNEPPEDAFEWTVSPEKAPDEPEYVTIEFEKGVPVAVNGEKLDPVEL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 238 VRKLNEIAGENGVGRTDMIEDRVLGLKARENYEHPAATVLLAAHADLEKLVLTRGELKFKKIVDEQWSELAYYGLVDEPL 317
Cdd:cd01999 239 IEKLNEIAGRHGVGRIDIVENRLVGIKSRGVYEAPGATLLIKAHRDLEDLTLDREVLHFKDIVSRKYAELVYNGLWFDPL 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499331636 318 YADLNAFIDKSQERVTGTVKVKLYKGALTILARSSPNALYSEDLVSFDS-QTIDQKDAEGFAKYHGFQ 384
Cdd:cd01999 319 REALEAFIDKTQERVTGEVRLKLYKGNVIVVGRESPNSLYSEELATYEEgDGFDQKDAEGFIKIHGLQ 386
|
|
| PRK00509 |
PRK00509 |
argininosuccinate synthase; Provisional |
1-394 |
0e+00 |
|
argininosuccinate synthase; Provisional
Pssm-ID: 234785 Cd Length: 399 Bit Score: 575.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 1 MVKKVALAYSGGLDTSVCIPILKEKYGYdEVITISVDVGQpEEEIKKADAKAEKI-SNKHYTIDAKEEFVKDYIFPLIKA 79
Cdd:PRK00509 1 MKKKVVLAYSGGLDTSVIIKWLKETYGC-EVIAFTADVGQ-GEELEPIREKALKSgASEIYVEDLREEFVRDYVFPAIRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 80 NGDYEG-YVMGTSVARPLIAKKVVEAAIKEGAVALAHGCTGKGNDQLRFEAVFR--QTDMDVIAPMREMNL-TREWEIDY 155
Cdd:PRK00509 79 NALYEGkYPLGTALARPLIAKKLVEIARKEGADAVAHGCTGKGNDQVRFELGIAalAPDLKVIAPWREWDLkSREELIAY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 156 AKEHGIPVEVTKAKPWSVDENIWSRSIEGGKLEDPSFVPPEEIFEWTKSAEDAPNEPRIVDIDFEAGVPVALDGEKLGGY 235
Cdd:PRK00509 159 AEEHGIPIPVTKKSPYSIDANLWHRSIEGGILEDPWNEPPEDVYEWTVSPEDAPDEPEYVEIEFEKGVPVAINGEALSPA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 236 ALVRKLNEIAGENGVGRTDMIEDRVLGLKARENYEHPAATVLLAAHADLEKLVLTRGELKFKKIVDEQWSELAYYGLVDE 315
Cdd:PRK00509 239 ELIEELNELAGKHGIGRIDIVENRLVGIKSRGVYETPGGTILIKAHRALESLTLDREVAHFKDELEPKYAELVYNGLWFS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 316 PLYADLNAFIDKSQERVTGTVKVKLYKGALTILARSSPNALYSEDLVSFDS-QTIDQKDAEGFAKYHGFQARMYRKVMEK 394
Cdd:PRK00509 319 PLREALQAFIDETQEHVTGEVRLKLYKGNAIVVGRKSPNSLYDEDLATYEEdDVYDQKDAEGFIKLWGLPSKIAALVNKK 398
|
|
| argG |
TIGR00032 |
argininosuccinate synthase; argG in bacteria, ARG1 in Saccharomyces cerevisiae. There is a ... |
4-392 |
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: 546.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 4 KVALAYSGGLDTSVCIPILKEKyGYdEVITISVDVGQPEEEIKKADAKAEKISN-KHYTIDAKEEFVKDYIFPLIKANGD 82
Cdd:TIGR00032 1 KVVLAYSGGLDTSVCLKWLREK-GY-EVIAYTADVGQPEEDIDAIPEKALEYGAeNHYTIDAREEFVKDYGFAAIQANAF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 83 YEG-YVMGTSVARPLIAKKVVEAAIKEGAVALAHGCTGKGNDQLRFEAVFR--QTDMDVIAPMREMNLTREWEIDYAKEH 159
Cdd:TIGR00032 79 YEGtYPLSTALARPLIAKKLVEAAKKEGANAVAHGCTGKGNDQERFERSIRllNPDLKVIAPWRDLNFTREEEIEYAIQC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 160 GIPVEVTKAKPWSVDENIWSRSIEGGKLEDPSFVPPEEIFEWTKSA-EDAPNEPRIVDIDFEAGVPVALDGEKLGGYALV 238
Cdd:TIGR00032 159 GIPYPMSKEKPYSIDENLWGRSIEAGILEDPSTEPPEDIYMWTKFPdEATPDEPEVVTIDFEQGVPVALNGVSLDPVELI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 239 RKLNEIAGENGVGRTDMIEDRVLGLKARENYEHPAATVLLAAHADLEKLVLTRGELKFKKIVDEQWSELAYYGLVDEPLY 318
Cdd:TIGR00032 239 LEANEIAGKHGVGRIDIIENRIIGLKSREIYEAPGAALLIIAHRDLETLTLTRDVLEFKDIVEEQYSELIYQGLWFDPLA 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499331636 319 ADLNAFIDKSQERVTGTVKVKLYKGALTILARSSPNALYSEDLVSFDSQT-IDQKDAEGFAKYHGFQARMYRKVM 392
Cdd:TIGR00032 319 EALDAFIRKTQERVTGTVRVKLFKGNAIVIGRTSPYSLYDEELVSMEKDDvFDPRDAIGFITMRGLQIKDYREKK 393
|
|
| PLN00200 |
PLN00200 |
argininosuccinate synthase; Provisional |
1-388 |
2.85e-149 |
|
argininosuccinate synthase; Provisional
Pssm-ID: 177791 Cd Length: 404 Bit Score: 428.39 E-value: 2.85e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 1 MVKKVALAYSGGLDTSVCIPILKEKYGYdEVITISVDVGQPEEEIKKADAKAEKISNKHYTI-DAKEEFVKDYIFPLIKA 79
Cdd:PLN00200 4 KLNKVVLAYSGGLDTSVILKWLRENYGC-EVVCFTADVGQGIEELEGLEAKAKASGAKQLVVkDLREEFVRDYIFPCLRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 80 NGDYEG-YVMGTSVARPLIAKKVVEAAIKEGAVALAHGCTGKGNDQLRFEAVFR--QTDMDVIAPMREMNLT-REWEIDY 155
Cdd:PLN00200 83 NAIYEGkYLLGTSMARPLIAKAMVDIAKEVGADAVAHGATGKGNDQVRFELTFFalNPELKVVAPWREWDIKgREDLIEY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 156 AKEHGIPVEVTKAKPWSVDENIWSRSIEGGKLEDPSFVPPEEIFEWTKSAEDAPNEPRIVDIDFEAGVPVALDGEKLGGY 235
Cdd:PLN00200 163 AKKHNIPVPVTKKSIYSRDRNLWHISYEGDILEDPANEPKEDMFMMSVSPEAAPDQPEYIEIEFEKGLPVAINGKTLSPA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 236 ALVRKLNEIAGENGVGRTDMIEDRVLGLKARENYEHPAATVLLAAHADLEKLVLTRGELKFKKIVDEQWSELAYYGLVDE 315
Cdd:PLN00200 243 TLLTKLNEIGGKHGIGRIDMVENRFVGMKSRGVYETPGGTILFAAHRELESLTLDRETMQVKDSLALKYAELVYNGFWFD 322
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499331636 316 PLYADLNAFIDKSQERVTGTVKVKLYKGALTILARSSPNALYSEDLVSFDSQT--IDQKDAEGFAKYHGFQARMY 388
Cdd:PLN00200 323 PERESMDAFMEKITETTTGSVRLKLYKGNVSVAGRKSPYSLYRQDISSFEEGGgiYNQADAAGFIRLYALRLRTR 397
|
|
| PRK04527 |
PRK04527 |
argininosuccinate synthase; Provisional |
1-392 |
1.44e-85 |
|
argininosuccinate synthase; Provisional
Pssm-ID: 235305 Cd Length: 400 Bit Score: 265.54 E-value: 1.44e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 1 MVKKVALAYSGGLDTSVCIPILKEKyGYdEVITISVDVGQP-EEEIKKADAKAEKISNK-HYTIDAKEEFVKDYIFPLIK 78
Cdd:PRK04527 1 SSKDIVLAFSGGLDTSFCIPYLQER-GY-AVHTVFADTGGVdAEERDFIEKRAAELGAAsHVTVDGGPAIWEGFVKPLVW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 79 ANGDYEGYVMGTSVARPLIAKKVVEAAIKEGAVALAHGCTGKGNDQLRFE-AVFRQTDMDVIAPMREMNL----TREWEI 153
Cdd:PRK04527 79 AGEGYQGQYPLLVSDRYLIVDAALKRAEELGTRIIAHGCTGMGNDQVRFDlAVKALGDYQIVAPIREIQKehtqTRAYEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 154 DYAKEHGIPVEvTKAKPWSVDENIWSRSIEGGKLeDPSFVPPEEIFEWTKSAEDAPNEPRIVDIDFEAGVPVALDGEKLG 233
Cdd:PRK04527 159 KYLEERGFGVR-AKQKAYTINENLLGVTMSGGEI-DRWEAPGEGARGWCAPRSAWPTEALTVTIKFVEGEAVALDGKPLP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 234 GYALVRKLNEIAGENGVGRTDMIEDRVLGLKARENYEHPAATVLLAAHADLEKLVLTRGELKFKKIVDEQWSELAYYGLV 313
Cdd:PRK04527 237 GAQILAKLNKLFAQYGVGRGVYTGDTVIGLKGRIVFEAPGLVSLLTAHRALEDAVLTKQQNRFKPDVARKWVELVYEGFY 316
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499331636 314 DEPLYADLNAFIDKSQERVTGTVKVKLYKGALTILARSSPNALYSEDLVSFDSQTIDQKDAEGFAKYHGFQARMYRKVM 392
Cdd:PRK04527 317 HDPLKTDIEAFLKSSQAKVNGEVTLETRGGRVDAVAVRSPHLLNSKGATYAQSADWGVEEAEGFIKLFGMSSTLYAQVN 395
|
|
| PRK05370 |
PRK05370 |
argininosuccinate synthase; Validated |
3-288 |
2.25e-21 |
|
argininosuccinate synthase; Validated
Pssm-ID: 235434 Cd Length: 447 Bit Score: 95.43 E-value: 2.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 3 KKVALAYSGGLDTSVCIPILKEK----YGYdevitiSVDVGQPEE----EI-KKADA-KAEKISnkhyTIDAKEEFVKDY 72
Cdd:PRK05370 12 QRVGIAFSGGLDTSAALLWMRQKgavpYAY------TANLGQPDEddydAIpRRAMEyGAENAR----LIDCRAQLVAEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 73 IFPL------IKANGdyEGYVMGTSVARPLIAKKVVeAAIKEGAVAL-AHGCTGKGNDQLRFeavFR------------- 132
Cdd:PRK05370 82 IAAIqcgafhISTGG--VTYFNTTPLGRAVTGTMLV-AAMKEDGVNIwGDGSTYKGNDIERF---YRyglltnpelkiyk 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 133 ----QTDMDVIAPMREMNltrEWEIdyakEHGIPVEVTKAKPWSVDENIWSRSIEGGKLE--DPSFVPPEEIFE---WTK 203
Cdd:PRK05370 156 pwldQDFIDELGGRAEMS---EFLI----AHGFDYKMSVEKAYSTDSNMLGATHEAKDLEhlNSGIKIVNPIMGvafWDE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 204 SAEDAPNEpriVDIDFEAGVPVALDGEKLGG-YALVRKLNEIAGENGVGRTDMIEDRVLGLKARENYEHPAATVLLAAHa 282
Cdd:PRK05370 229 DVEIKAEE---VTVRFEQGRPVALNGKTFSDpVELMLEANRIGGRHGLGMSDQIENRIIEAKSRGIYEAPGMALLHIAY- 304
|
....*.
gi 499331636 283 dlEKLV 288
Cdd:PRK05370 305 --ERLV 308
|
|
| QueC |
pfam06508 |
Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis ... |
10-63 |
1.44e-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: 45.69 E-value: 1.44e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 499331636 10 SGGLDTSVCIPILKEkyGYDEVITISVDVGQPEE-EIKKADAKAEKISNKHYTID 63
Cdd:pfam06508 7 SGGLDSTTCLAWAKK--EGYEVYALSFDYGQRHRkELECAKKIAKALGVEHKILD 59
|
|
| QueC |
COG0603 |
7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and ... |
1-63 |
1.72e-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: 45.54 E-value: 1.72e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499331636 1 MVKKVALAYSGGLDTSVCIPILKEKygYDEVITISVDVGQPEE-EIKKADAKAEKI-SNKHYTID 63
Cdd:COG0603 1 MMKKAVVLLSGGLDSTTCLAWALAR--GYEVYALSFDYGQRHRkELEAARRIAKALgVGEHKVID 63
|
|
| QueC-like |
cd01995 |
7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC ... |
3-63 |
4.81e-05 |
|
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: 44.14 E-value: 4.81e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499331636 3 KKVALAYSGGLDTSVCIPILKEKygYDEVITISVDVGQ-PEEEIKKADAKAEKISN-KHYTID 63
Cdd:cd01995 1 MKAVVLLSGGLDSTTLLYWALKE--GYEVHALTFDYGQrHAKEELEAAKLIAKLLGiEHKVID 61
|
|
| mnmA |
PRK00143 |
tRNA-specific 2-thiouridylase MnmA; Reviewed |
3-74 |
2.00e-04 |
|
tRNA-specific 2-thiouridylase MnmA; Reviewed
Pssm-ID: 234664 [Multi-domain] Cd Length: 346 Bit Score: 43.14 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 3 KKVALAYSGGLDTSVCIPILKEKyGYdEVITISVDVGQPEEEIKK---------ADAK--AEKISNKHYTIDAKEEFvKD 71
Cdd:PRK00143 1 KRVVVGMSGGVDSSVAAALLKEQ-GY-EVIGVFMKLWDDDDETGKggccaeediADARrvADKLGIPHYVVDFEKEF-WD 77
|
...
gi 499331636 72 YIF 74
Cdd:PRK00143 78 RVI 80
|
|
| LarE-like |
cd01990 |
Lactate racemization operon protein LarE and similar proteins; This subfamily includes ... |
4-73 |
4.82e-04 |
|
Lactate racemization operon protein LarE and similar proteins; This subfamily includes Lactiplantibacillus plantarum LarE, a sacrificial sulfur insertase of the N-type ATP pyrophosphatase family. LarE is part of the lar operon, encoding five Lar proteins (LarA-E) that collaboratively synthesize and incorporate a niacin-derived Ni-containing cofactor into LarA, an Ni-dependent lactate racemase. It catalyzes successive thiolation reactions by donating the sulfur atom of their exclusive cysteine residues to the substrate. The LarE-like subfamily belongs to the nucleotide alpha hydrolase (AANH) superfamily that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. Proteins from this subfamily probably binds ATP. This domain is about 200 amino acids long with a strongly conserved motif SGGxDS at the N-terminus.
Pssm-ID: 467494 [Multi-domain] Cd Length: 222 Bit Score: 41.09 E-value: 4.82e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499331636 4 KVALAYSGGLDTSVCIPILKEKYGyDEVITISVDVG-QPEEEIKKADAKAEKISNKHYTIDAKEEFVKDYI 73
Cdd:cd01990 1 KVVVAFSGGVDSSLLAKLAKEVLG-DNVVAVTADSPlVPREELEEAKRIAEEIGIRHEIIKTDELDDEEYV 70
|
|
| MnmA |
COG0482 |
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ... |
3-74 |
1.20e-03 |
|
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: 40.42 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 3 KKVALAYSGGLDTSVCIPILKEKyGYDeVITISVDVGQPEEEIKK---------ADAK--AEKISNKHYTIDAKEEFvKD 71
Cdd:COG0482 1 KRVVVGMSGGVDSSVAAALLKEQ-GYE-VIGVTMKLWDDDDASGSggccslediEDARrvADKLGIPHYVVDFEEEF-KD 77
|
...
gi 499331636 72 YIF 74
Cdd:COG0482 78 RVI 80
|
|
| MnmA_TRMU-like |
cd01998 |
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ... |
4-74 |
1.95e-03 |
|
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: 39.80 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 4 KVALAYSGGLDTSVCIPILKEKyGYDeVI----------TISVDVGQPEEEIKKADAKAEKISNKHYTIDAKEEFvKDYI 73
Cdd:cd01998 1 KVAVAMSGGVDSSVAAALLKEQ-GYD-VIgvfmknwddeDNEKGGCCSEEDIEDARRVADQLGIPLYVVDFSEEY-WERV 77
|
.
gi 499331636 74 F 74
Cdd:cd01998 78 F 78
|
|
| tRNA_Me_trans |
pfam03054 |
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ... |
3-89 |
2.74e-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: 38.77 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499331636 3 KKVALAYSGGLDTSVCIPILKEKyGYdEVITI----------SVDVGQP--EEEIKKADAKAEKISNKHYTIDAKEEFVK 70
Cdd:pfam03054 1 MKVVVAMSGGVDSSVAAYLLKEQ-GH-NVIGVfmknwdeeqsLDEEGKCcsEEDLADAQRVCEQLGIPLYVVNFEKEYWE 78
|
90
....*....|....*....
gi 499331636 71 DYIFPLIkangdyEGYVMG 89
Cdd:pfam03054 79 DVFEPFL------DEYKNG 91
|
|
| |
