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Conserved domains on  [gi|2796056213|ref|WP_372816237|]
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glutamine-hydrolyzing GMP synthase [Pyrococcus kukulkanii]

Protein Classification

similar to GMP synthase [glutamine-hydrolyzing] subunit B( domain architecture ID 11424848)

protein similar to GMP synthase [glutamine-hydrolyzing] subunit B

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GuaA2 COG0519
GMP synthase, PP-ATPase domain/subunit [Nucleotide transport and metabolism]; GMP synthase, ...
 3-307 0e+00

GMP synthase, PP-ATPase domain/subunit [Nucleotide transport and metabolism]; GMP synthase, PP-ATPase domain/subunit is part of the Pathway/BioSystem: Purine biosynthesis


:

Pssm-ID: 440285 [Multi-domain]  Cd Length: 512  Bit Score: 567.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213   3 EKFIEEKVREIRETVGDAKAIIALSGGVDSSTAAVLAHKAIGDRLHAVFVNTGFLRKGEPEFVVKTFRDEFGMNLHYVDA 82
Cdd:COG0519   199 ENFIEEAIEEIREQVGDGKVICALSGGVDSSVAAALLHKAIGDQLTCVFVDHGLLRKGEAEQVEETFKEHFGLNLIYVDA 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  83 QDRFFEALKGVTDPEEKRKIIGRVFIEVFEEVAKEIG-AEYLIQGTIAPDWIESKG------KIKSHHNVGGLPERLNLK 155
Cdd:COG0519   279 SERFLSALKGVTDPEEKRKIIGEEFIEVFEEEAKKLGgAKFLAQGTLYPDVIESGSvkgpaaTIKSHHNVGGLPEDMKFK 358

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213 156 LIEPLRDLYKDEVRQLAKELGLPEKIYNRMPFPGPGLAVRVIGEVTPEKIAIVREANAIVEEEVEKAGL--RPWQAFAVL 233
Cdd:COG0519   359 LVEPLRELFKDEVRALGRELGLPEEIVYRHPFPGPGLAIRILGEVTKEKLEILREADAIFIEELRKAGLydKVWQAFAVL 438

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2796056213 234 LGVKTVGVQGDIRAYKETIAVRIVESVDGMTANAMNVPWEVLQRIAFRITSEIPQVGRVLYDITNKPPATIEFE 307
Cdd:COG0519   439 LPVKSVGVMGDERTYEYVVALRAVTSVDGMTADWARLPYEVLERISNRIINEVKGVNRVVYDITSKPPATIEWE 512
 
Name Accession Description Interval E-value
GuaA2 COG0519
GMP synthase, PP-ATPase domain/subunit [Nucleotide transport and metabolism]; GMP synthase, ...
 3-307 0e+00

GMP synthase, PP-ATPase domain/subunit [Nucleotide transport and metabolism]; GMP synthase, PP-ATPase domain/subunit is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440285 [Multi-domain]  Cd Length: 512  Bit Score: 567.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213   3 EKFIEEKVREIRETVGDAKAIIALSGGVDSSTAAVLAHKAIGDRLHAVFVNTGFLRKGEPEFVVKTFRDEFGMNLHYVDA 82
Cdd:COG0519   199 ENFIEEAIEEIREQVGDGKVICALSGGVDSSVAAALLHKAIGDQLTCVFVDHGLLRKGEAEQVEETFKEHFGLNLIYVDA 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  83 QDRFFEALKGVTDPEEKRKIIGRVFIEVFEEVAKEIG-AEYLIQGTIAPDWIESKG------KIKSHHNVGGLPERLNLK 155
Cdd:COG0519   279 SERFLSALKGVTDPEEKRKIIGEEFIEVFEEEAKKLGgAKFLAQGTLYPDVIESGSvkgpaaTIKSHHNVGGLPEDMKFK 358

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213 156 LIEPLRDLYKDEVRQLAKELGLPEKIYNRMPFPGPGLAVRVIGEVTPEKIAIVREANAIVEEEVEKAGL--RPWQAFAVL 233
Cdd:COG0519   359 LVEPLRELFKDEVRALGRELGLPEEIVYRHPFPGPGLAIRILGEVTKEKLEILREADAIFIEELRKAGLydKVWQAFAVL 438

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2796056213 234 LGVKTVGVQGDIRAYKETIAVRIVESVDGMTANAMNVPWEVLQRIAFRITSEIPQVGRVLYDITNKPPATIEFE 307
Cdd:COG0519   439 LPVKSVGVMGDERTYEYVVALRAVTSVDGMTADWARLPYEVLERISNRIINEVKGVNRVVYDITSKPPATIEWE 512
guaA PRK00074
GMP synthase; Reviewed
 3-307 0e+00

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 556.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213   3 EKFIEEKVREIRETVGDAKAIIALSGGVDSSTAAVLAHKAIGDRLHAVFVNTGFLRKGEPEFVVKTFRDEFGMNLHYVDA 82
Cdd:PRK00074  199 ENFIEEAIEEIREQVGDKKVILGLSGGVDSSVAAVLLHKAIGDQLTCVFVDHGLLRKNEAEQVMEMFREHFGLNLIHVDA 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  83 QDRFFEALKGVTDPEEKRKIIGRVFIEVFEEVAKEI-GAEYLIQGTIAPDWIESKG-----KIKSHHNVGGLPERLNLKL 156
Cdd:PRK00074  279 SDRFLSALAGVTDPEEKRKIIGREFIEVFEEEAKKLgGVKFLAQGTLYPDVIESGGtkkaaTIKSHHNVGGLPEDMKLKL 358

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213 157 IEPLRDLYKDEVRQLAKELGLPEKIYNRMPFPGPGLAVRVIGEVTPEKIAIVREANAIVEEEVEKAGL--RPWQAFAVLL 234
Cdd:PRK00074  359 VEPLRELFKDEVRKLGLELGLPEEIVYRHPFPGPGLAIRILGEVTKEKLDILREADAIFIEELRKAGLydKIWQAFAVLL 438

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2796056213 235 GVKTVGVQGDIRAYKETIAVRIVESVDGMTANAMNVPWEVLQRIAFRITSEIPQVGRVLYDITNKPPATIEFE 307
Cdd:PRK00074  439 PVKSVGVMGDGRTYDYVVALRAVTSIDGMTADWARLPYDFLEKISNRIINEVKGVNRVVYDITSKPPATIEWE 511
guaA_Cterm TIGR00884
GMP synthase (glutamine-hydrolyzing), C-terminal domain or B subunit; This protein of purine ...
 4-307 0e+00

GMP synthase (glutamine-hydrolyzing), C-terminal domain or B subunit; This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This C-terminal region would be the larger subunit [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273321 [Multi-domain]  Cd Length: 311  Bit Score: 532.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213   4 KFIEEKVREIRETVGDAKAIIALSGGVDSSTAAVLAHKAIGDRLHAVFVNTGFLRKGEPEFVVKTFRDEFGMNLHYVDAQ 83
Cdd:TIGR00884   1 NFIEEAVEEIREQVGDAKVIIALSGGVDSSVAAVLAHRAIGDRLTCVFVDHGLLRKGEAEQVVKTFGDRLGLNLVYVDAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  84 DRFFEALKGVTDPEEKRKIIGRVFIEVFEEVAKEIG-AEYLIQGTIAPDWIESKG----KIKSHHNVGGLPERLNLKLIE 158
Cdd:TIGR00884  81 ERFLSALKGVTDPEEKRKIIGRVFIEVFEREAKKIGdAEYLAQGTIYPDVIESAAgtahVIKSHHNVGGLPEDMKLKLVE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213 159 PLRDLYKDEVRQLAKELGLPEKIYNRMPFPGPGLAVRVIGEVTPEKIAIVREANAIVEEEVEKAGL--RPWQAFAVLLGV 236
Cdd:TIGR00884 161 PLRELFKDEVRKLGKELGLPEEIVWRHPFPGPGLAVRVLGEVTKEKLEILRRADAIVIEELKKAGLydKVWQAFAVLLPV 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2796056213 237 KTVGVQGDIRAYKETIAVRIVESVDGMTANAMNVPWEVLQRIAFRITSEIPQVGRVLYDITNKPPATIEFE 307
Cdd:TIGR00884 241 KSVGVMGDGRTYGYVIALRAVESIDGMTADWARLPYDFLERISNRITNEVPGVNRVVYDITSKPPATIEWE 311
GMP_synthase_C cd01997
C-terminal domain of GMP synthetase (glutamine-hydrolyzing); The C-terminal domain of GMP ...
 13-307 6.66e-176

C-terminal domain of GMP synthetase (glutamine-hydrolyzing); The C-terminal domain of GMP synthetase (glutamine-hydrolyzing, EC 6.3.5.2) contains two subdomains: the ATP pyrophosphatase domain at the N-terminal and the dimerization domain at the C-terminal end. The ATP-PPase domain is a twisted, five-stranded parallel beta-sheet sandwiched between helical layers. It has a signature nucleotide-binding motif, or PP-loop, at the end of the first-beta strand. GMP synthetase is a homodimer, but in some archaea, it is a heterodimer made up of ATP pyrophosphatase (ATP-PPase) and a GATase subunit. In eukaryotes and bacteria, the two catalytic units are encoded by a single gene producing a two-domain-type GMP with a GATase domain in the N-terminus and an ATP-PPase domain in the C-terminus.


Pssm-ID: 467501 [Multi-domain]  Cd Length: 311  Bit Score: 488.59  E-value: 6.66e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  13 IRETVGDAKAIIALSGGVDSSTAAVLAHKAIGD-RLHAVFVNTGFLRKGEPEFVVKTFRDEFGMNLHYVDAQDRFFEALK 91
Cdd:cd01997     1 IKRTVGDKKVLCLVSGGVDSTVCAALLHKALGDeRVIAVHIDNGLMRKNESEQVEEALKKLGVINLAKVDASKRFLKKLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  92 GVTDPEEKRKIIGRVFIEVFEEVAKEIGA----EYLIQGTIAPDWIESKGK--------IKSHHNVGGLPERL-NLKLIE 158
Cdd:cd01997    81 GVTDPEEKRKIIGDTFIEVFDEVAKELNLdpddVYLAQGTLYPDLIESASSlasskadtIKTHHNVGGLPRELlKGKLVE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213 159 PLRDLYKDEVRQLAKELGLPEKIYNRMPFPGPGLAVRVIGEVTPEKIAIVREANAIVEEEVEKAGL--RPWQAFAVLLGV 236
Cdd:cd01997   161 PLRDLFKDEVRELGRELGLPEELVWRHPFPGPGLAIRVLGEVTPEKLEILREADAIVEEELREAGLydKISQAFAVLLPI 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2796056213 237 KTVGVQGDIRAYKETIAVRIVESVDGMTANAMNVPWEVLQRIAFRITSEIPQVGRVLYDITNKPPATIEFE 307
Cdd:cd01997   241 KSVGVQGDGRTYGYVVALRAVETEDFMTAEWARPPYEVLDKISNRITNEVPGVNRVVYDITSKPPATIEWE 311
GMP_synt_C pfam00958
GMP synthase C terminal domain; GMP synthetase is a glutamine amidotransferase from the de ...
 217-306 6.81e-47

GMP synthase C terminal domain; GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. This family is the C-terminal domain specific to the GMP synthases EC:6.3.5.2. In prokaryotes this domain mediates dimerization. Eukaryotic GMP synthases are monomers. This domain in eukaryotes includes several large insertions that may form globular domains.


Pssm-ID: 425963 [Multi-domain]  Cd Length: 92  Bit Score: 152.57  E-value: 6.81e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213 217 EEVEKAGL--RPWQAFAVLLGVKTVGVQGDIRAYKETIAVRIVESVDGMTANAMNVPWEVLQRIAFRITSEIPQVGRVLY 294
Cdd:pfam00958   1 EEIKKAGLyrKIWQAFAVLLPVKSVGVMGDERTYEYVVALRAVTSTDGMTADWARLPYEVLEKISNRIVNEVPGVNRVVY 80

                          90
                  ....*....|..
gi 2796056213 295 DITNKPPATIEF 306
Cdd:pfam00958  81 DITSKPPATIEW 92
 
Name Accession Description Interval E-value
GuaA2 COG0519
GMP synthase, PP-ATPase domain/subunit [Nucleotide transport and metabolism]; GMP synthase, ...
 3-307 0e+00

GMP synthase, PP-ATPase domain/subunit [Nucleotide transport and metabolism]; GMP synthase, PP-ATPase domain/subunit is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440285 [Multi-domain]  Cd Length: 512  Bit Score: 567.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213   3 EKFIEEKVREIRETVGDAKAIIALSGGVDSSTAAVLAHKAIGDRLHAVFVNTGFLRKGEPEFVVKTFRDEFGMNLHYVDA 82
Cdd:COG0519   199 ENFIEEAIEEIREQVGDGKVICALSGGVDSSVAAALLHKAIGDQLTCVFVDHGLLRKGEAEQVEETFKEHFGLNLIYVDA 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  83 QDRFFEALKGVTDPEEKRKIIGRVFIEVFEEVAKEIG-AEYLIQGTIAPDWIESKG------KIKSHHNVGGLPERLNLK 155
Cdd:COG0519   279 SERFLSALKGVTDPEEKRKIIGEEFIEVFEEEAKKLGgAKFLAQGTLYPDVIESGSvkgpaaTIKSHHNVGGLPEDMKFK 358

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213 156 LIEPLRDLYKDEVRQLAKELGLPEKIYNRMPFPGPGLAVRVIGEVTPEKIAIVREANAIVEEEVEKAGL--RPWQAFAVL 233
Cdd:COG0519   359 LVEPLRELFKDEVRALGRELGLPEEIVYRHPFPGPGLAIRILGEVTKEKLEILREADAIFIEELRKAGLydKVWQAFAVL 438

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2796056213 234 LGVKTVGVQGDIRAYKETIAVRIVESVDGMTANAMNVPWEVLQRIAFRITSEIPQVGRVLYDITNKPPATIEFE 307
Cdd:COG0519   439 LPVKSVGVMGDERTYEYVVALRAVTSVDGMTADWARLPYEVLERISNRIINEVKGVNRVVYDITSKPPATIEWE 512
guaA PRK00074
GMP synthase; Reviewed
 3-307 0e+00

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 556.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213   3 EKFIEEKVREIRETVGDAKAIIALSGGVDSSTAAVLAHKAIGDRLHAVFVNTGFLRKGEPEFVVKTFRDEFGMNLHYVDA 82
Cdd:PRK00074  199 ENFIEEAIEEIREQVGDKKVILGLSGGVDSSVAAVLLHKAIGDQLTCVFVDHGLLRKNEAEQVMEMFREHFGLNLIHVDA 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  83 QDRFFEALKGVTDPEEKRKIIGRVFIEVFEEVAKEI-GAEYLIQGTIAPDWIESKG-----KIKSHHNVGGLPERLNLKL 156
Cdd:PRK00074  279 SDRFLSALAGVTDPEEKRKIIGREFIEVFEEEAKKLgGVKFLAQGTLYPDVIESGGtkkaaTIKSHHNVGGLPEDMKLKL 358

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213 157 IEPLRDLYKDEVRQLAKELGLPEKIYNRMPFPGPGLAVRVIGEVTPEKIAIVREANAIVEEEVEKAGL--RPWQAFAVLL 234
Cdd:PRK00074  359 VEPLRELFKDEVRKLGLELGLPEEIVYRHPFPGPGLAIRILGEVTKEKLDILREADAIFIEELRKAGLydKIWQAFAVLL 438

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2796056213 235 GVKTVGVQGDIRAYKETIAVRIVESVDGMTANAMNVPWEVLQRIAFRITSEIPQVGRVLYDITNKPPATIEFE 307
Cdd:PRK00074  439 PVKSVGVMGDGRTYDYVVALRAVTSIDGMTADWARLPYDFLEKISNRIINEVKGVNRVVYDITSKPPATIEWE 511
guaA_Cterm TIGR00884
GMP synthase (glutamine-hydrolyzing), C-terminal domain or B subunit; This protein of purine ...
 4-307 0e+00

GMP synthase (glutamine-hydrolyzing), C-terminal domain or B subunit; This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This C-terminal region would be the larger subunit [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273321 [Multi-domain]  Cd Length: 311  Bit Score: 532.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213   4 KFIEEKVREIRETVGDAKAIIALSGGVDSSTAAVLAHKAIGDRLHAVFVNTGFLRKGEPEFVVKTFRDEFGMNLHYVDAQ 83
Cdd:TIGR00884   1 NFIEEAVEEIREQVGDAKVIIALSGGVDSSVAAVLAHRAIGDRLTCVFVDHGLLRKGEAEQVVKTFGDRLGLNLVYVDAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  84 DRFFEALKGVTDPEEKRKIIGRVFIEVFEEVAKEIG-AEYLIQGTIAPDWIESKG----KIKSHHNVGGLPERLNLKLIE 158
Cdd:TIGR00884  81 ERFLSALKGVTDPEEKRKIIGRVFIEVFEREAKKIGdAEYLAQGTIYPDVIESAAgtahVIKSHHNVGGLPEDMKLKLVE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213 159 PLRDLYKDEVRQLAKELGLPEKIYNRMPFPGPGLAVRVIGEVTPEKIAIVREANAIVEEEVEKAGL--RPWQAFAVLLGV 236
Cdd:TIGR00884 161 PLRELFKDEVRKLGKELGLPEEIVWRHPFPGPGLAVRVLGEVTKEKLEILRRADAIVIEELKKAGLydKVWQAFAVLLPV 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2796056213 237 KTVGVQGDIRAYKETIAVRIVESVDGMTANAMNVPWEVLQRIAFRITSEIPQVGRVLYDITNKPPATIEFE 307
Cdd:TIGR00884 241 KSVGVMGDGRTYGYVIALRAVESIDGMTADWARLPYDFLERISNRITNEVPGVNRVVYDITSKPPATIEWE 311
GMP_synthase_C cd01997
C-terminal domain of GMP synthetase (glutamine-hydrolyzing); The C-terminal domain of GMP ...
 13-307 6.66e-176

C-terminal domain of GMP synthetase (glutamine-hydrolyzing); The C-terminal domain of GMP synthetase (glutamine-hydrolyzing, EC 6.3.5.2) contains two subdomains: the ATP pyrophosphatase domain at the N-terminal and the dimerization domain at the C-terminal end. The ATP-PPase domain is a twisted, five-stranded parallel beta-sheet sandwiched between helical layers. It has a signature nucleotide-binding motif, or PP-loop, at the end of the first-beta strand. GMP synthetase is a homodimer, but in some archaea, it is a heterodimer made up of ATP pyrophosphatase (ATP-PPase) and a GATase subunit. In eukaryotes and bacteria, the two catalytic units are encoded by a single gene producing a two-domain-type GMP with a GATase domain in the N-terminus and an ATP-PPase domain in the C-terminus.


Pssm-ID: 467501 [Multi-domain]  Cd Length: 311  Bit Score: 488.59  E-value: 6.66e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  13 IRETVGDAKAIIALSGGVDSSTAAVLAHKAIGD-RLHAVFVNTGFLRKGEPEFVVKTFRDEFGMNLHYVDAQDRFFEALK 91
Cdd:cd01997     1 IKRTVGDKKVLCLVSGGVDSTVCAALLHKALGDeRVIAVHIDNGLMRKNESEQVEEALKKLGVINLAKVDASKRFLKKLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  92 GVTDPEEKRKIIGRVFIEVFEEVAKEIGA----EYLIQGTIAPDWIESKGK--------IKSHHNVGGLPERL-NLKLIE 158
Cdd:cd01997    81 GVTDPEEKRKIIGDTFIEVFDEVAKELNLdpddVYLAQGTLYPDLIESASSlasskadtIKTHHNVGGLPRELlKGKLVE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213 159 PLRDLYKDEVRQLAKELGLPEKIYNRMPFPGPGLAVRVIGEVTPEKIAIVREANAIVEEEVEKAGL--RPWQAFAVLLGV 236
Cdd:cd01997   161 PLRDLFKDEVRELGRELGLPEELVWRHPFPGPGLAIRVLGEVTPEKLEILREADAIVEEELREAGLydKISQAFAVLLPI 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2796056213 237 KTVGVQGDIRAYKETIAVRIVESVDGMTANAMNVPWEVLQRIAFRITSEIPQVGRVLYDITNKPPATIEFE 307
Cdd:cd01997   241 KSVGVQGDGRTYGYVVALRAVETEDFMTAEWARPPYEVLDKISNRITNEVPGVNRVVYDITSKPPATIEWE 311
PLN02347 PLN02347
GMP synthetase
 3-307 1.29e-136

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 397.13  E-value: 1.29e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213   3 EKFIEEKVREIRETVG-DAKAIIALSGGVDSSTAAVLAHKAIGDRLHAVFVNTGFLRKGEPEFVVKTFRDEFGMNLHYVD 81
Cdd:PLN02347  212 QDVLEEQIELIKATVGpDEHVICALSGGVDSTVAATLVHKAIGDRLHCVFVDNGLLRYKEQERVMETFKRDLHLPVTCVD 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  82 AQDRFFEALKGVTDPEEKRKIIGRVFIEVFEEVAKEIGAE------YLIQGTIAPDWIES---KGK-------IKSHHNV 145
Cdd:PLN02347  292 ASERFLSKLKGVTDPEKKRKIIGAEFIEVFDEFAHKLEQKlgkkpaFLVQGTLYPDVIEScppPGSgrthshtIKSHHNV 371

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213 146 GGLPERLNLKLIEPLRDLYKDEVRQLAKELGLPEKIYNRMPFPGPGLAVRVIGEVTPE-KIAIVREANAIVEEEVEKAGL 224
Cdd:PLN02347  372 GGLPKDMKLKLIEPLKLLFKDEVRKLGRLLGVPEAFLKRHPFPGPGLAVRVLGDVTEGnALDILRQVDEIFINSIKDAGL 451

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213 225 --RPWQAFAVLLGVKTVGVQGDIRAYKETIAVRIVESVDGMTANAMNVPWEVLQRIAFRITSEIPQVGRVLYDITNKPPA 302
Cdd:PLN02347  452 ydEIWQAFAVFLPVKSVGVQGDQRTHSHVVALRAVTSEDGMTADWYHFEHKFLDDVSRKICNEVRGVNRVVYDITSKPPS 531


                  ....*
gi 2796056213 303 TIEFE 307
Cdd:PLN02347  532 TIEWE 536
GMP_synt_C pfam00958
GMP synthase C terminal domain; GMP synthetase is a glutamine amidotransferase from the de ...
 217-306 6.81e-47

GMP synthase C terminal domain; GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. This family is the C-terminal domain specific to the GMP synthases EC:6.3.5.2. In prokaryotes this domain mediates dimerization. Eukaryotic GMP synthases are monomers. This domain in eukaryotes includes several large insertions that may form globular domains.


Pssm-ID: 425963 [Multi-domain]  Cd Length: 92  Bit Score: 152.57  E-value: 6.81e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213 217 EEVEKAGL--RPWQAFAVLLGVKTVGVQGDIRAYKETIAVRIVESVDGMTANAMNVPWEVLQRIAFRITSEIPQVGRVLY 294
Cdd:pfam00958   1 EEIKKAGLyrKIWQAFAVLLPVKSVGVMGDERTYEYVVALRAVTSTDGMTADWARLPYEVLEKISNRIVNEVPGVNRVVY 80

                          90
                  ....*....|..
gi 2796056213 295 DITNKPPATIEF 306
Cdd:pfam00958  81 DITSKPPATIEW 92
COG1606 COG1606
ATP-utilizing enzyme, PP-loop superfamily [General function prediction only];
6-225 8.20e-18

ATP-utilizing enzyme, PP-loop superfamily [General function prediction only];


Pssm-ID: 441214 [Multi-domain]  Cd Length: 265  Bit Score: 81.31  E-value: 8.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213   6 IEEKVREIRETVGD-AKAIIALSGGVDSSTAAVLAHKAIGDRLHAVFVNTGFLRKGEPEFVVKtFRDEFGMNLHYVD--- 81
Cdd:COG1606     1 LEEKLERLKAILKElGSVLVAFSGGVDSTLLAKVAHDVLGDRVLAVTADSPSLPERELEEAKE-LAKEIGIRHEVIEtde 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  82 -AQDRFfealkgVTDPEE-----KRKIIGRVfievfEEVAKEIGAEYLIQGTIAPDWIE--------SKGKIKShhnvgg 147
Cdd:COG1606    80 lEDPEF------VANPPDrcyhcKKELFSKL-----KELAKELGYAVVADGTNADDLGDyrpglraaKELGVRS------ 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213 148 lperlnlkliePLRD--LYKDEVRQLAKELGLPekIYNRMPFpgPGLAVRV-IGE-VTPEKIAIVREAnaivEEEVEKAG 223
Cdd:COG1606   143 -----------PLAEagLTKAEIRELARELGLP--TWDKPSS--ACLASRIpYGEeITPEKLRRVERA----EAFLRSLG 203


                  ..
gi 2796056213 224 LR 225
Cdd:COG1606   204 FR 205
NAD_synthase pfam02540
NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is ...
 3-189 4.53e-13

NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is induced by stress factors such as heat shock and glucose limitation.


Pssm-ID: 396888 [Multi-domain]  Cd Length: 241  Bit Score: 67.41  E-value: 4.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213   3 EKFIEEKVREiretVGDAKAIIALSGGVDSSTAAVLAHKAIG-DRLHAVFVNTGFLRKGEPEfVVKTFRDEFGMNLHYVD 81
Cdd:pfam02540   6 VDFLRDYVQK----AGFKGVVLGLSGGIDSSLVAYLAVKALGkENVLALIMPSSQSSEEDVQ-DALALAENLGIEYKTID 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  82 AQDrffealkgvtdpeekrkiIGRVFIEVFEEVAKEIGAEYL-------IQGTIAPdwieskgkiKSHHNVGGLPERLNL 154
Cdd:pfam02540  81 IKP------------------IVRAFSQLFQDASEDFAKGNLkarirmaILYYIAN---------KFNYLVLGTGNKSEL 133

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2796056213 155 KL------------IEPLRDLYKDEVRQLAKELGLPEKIYNRMP----FPG 189
Cdd:pfam02540 134 AVgyftkygdgacdIAPIGDLYKTQVYELARYLNVPERIIKKPPsadlWPG 184
LarE-like cd01990
Lactate racemization operon protein LarE and similar proteins; This subfamily includes ...
 21-226 4.98e-13

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: 66.90  E-value: 4.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  21 KAIIALSGGVDSSTAAVLAHKAIGDRLHAVFVNTGFLRKGEPEFvVKTFRDEFGMNLhyvdaqdrFFEALKGVTDPEEKR 100
Cdd:cd01990     1 KVVVAFSGGVDSSLLAKLAKEVLGDNVVAVTADSPLVPREELEE-AKRIAEEIGIRH--------EIIKTDELDDEEYVA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213 101 KIIGRVFI---EVFE---EVAKEIGAEYLIQGTIAPDWIEskgkikshHNVGGLPER-LNLKLIEPLRDLYKDEVRQLAK 173
Cdd:cd01990    72 NDPDRCYHckkALYStlkEIAKERGYDVVLDGTNADDLKD--------YRPGLLAAAeLGIRSPLPELGLTKSEIRELAR 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2796056213 174 ELGLPekiyNRMPFPGPGLAVRV-IGE-VTPEKIAIVREAnaiVEEEVEKAGLRP 226
Cdd:cd01990   144 ELGLP----NWDKPASACLASRIpYGEeITPERLKRIEKA---EELYLRLLGFRQ 191
NAD_synthase cd00553
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de ...
 2-186 2.24e-11

NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de novo nicotinamide adenine dinucleotide (NAD(+)) biosynthesis, an amide transfer from either ammonia or glutamine to nicotinic acid adenine dinucleotide (NaAD). The conversion of NaAD to NAD(+) occurs via a NAD-adenylate intermediate and requires ATP and Mg(2+). The intermediate is subsequently cleaved into NAD(+) and AMP. In many prokaryotes, such as Escherichia coli, NAD synthase consists of a single domain and is strictly ammonia dependent. In contrast, eukaryotes and other prokaryotes have an additional N-terminal amidohydrolase domain that prefer glutamine. Interestingly, NAD(+) synthases in these prokaryotes, can also utilize ammonia as an amide source.


Pssm-ID: 467484 [Multi-domain]  Cd Length: 248  Bit Score: 62.57  E-value: 2.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213   2 WEKFIEEKVREIRETV---GDAKAIIALSGGVDSSTAAVLAHKAIG-DRLHAVFVNTGFLRKGEPEFvVKTFRDEFGMNL 77
Cdd:cd00553     3 PEEIIEALVCFLRDYLrksGAKGFVLGLSGGIDSAVVAALAVRALGaENVLALIMPSRYSSKETRDD-AKALAENLGIEY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  78 HYVD---AQDRFFEALKGVTDPEEKRKIIG------RVFIEVFeeVAKEIGA---------EYLI-QGTIAPDwieskgk 138
Cdd:cd00553    82 RTIDidpIVDAFLKALEHAGGSEAEDLALGniqarlRMVLLYA--LANLLGGlvlgtgnksELLLgYFTKYGD------- 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2796056213 139 ikshHNVGglperlnlklIEPLRDLYKDEVRQLAKELGLPEKIYNRMP 186
Cdd:cd00553   153 ----GAAD----------INPIGDLYKTQVRELARYLGVPEEIIEKPP 186
PRK13980 PRK13980
NAD synthetase; Provisional
 8-189 3.71e-11

NAD synthetase; Provisional


Pssm-ID: 184435 [Multi-domain]  Cd Length: 265  Bit Score: 62.15  E-value: 3.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213   8 EKVRE-----IRETVGDA---KAIIALSGGVDSSTAAVLAHKAIG-DRLHAVFVNTgflRKGEPEFVVKTFR--DEFGMN 76
Cdd:PRK13980   11 EKVREiivdfIREEVEKAgakGVVLGLSGGIDSAVVAYLAVKALGkENVLALLMPS---SVSPPEDLEDAELvaEDLGIE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  77 LHYVDAQ---DRFFEALkgvtdPEEKRKIIG----RVFIEVFEEVAKEIGaeYLIQGTiapdwieskgkikshhnvGGLP 149
Cdd:PRK13980   88 YKVIEITpivDAFFSAI-----PDADRLRVGnimaRTRMVLLYDYANREN--RLVLGT------------------GNKS 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2796056213 150 ERLnlkL------------IEPLRDLYKDEVRQLAKELGLPEKIYNRMPFPG 189
Cdd:PRK13980  143 ELL---LgyftkygdgavdLNPIGDLYKTQVRELARHLGVPEDIIEKPPSAD 191
nadE TIGR00552
NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the ...
 3-189 1.39e-10

NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the biosynthesis of the essensial cofactor NAD. The member of this family from Bacillus subtilis is a strictly NH(3)-dependent NAD(+) synthetase of 272 amino acids. Proteins consisting only of the domain modeled here may be named as NH3-dependent NAD+ synthetase. Amidotransferase activity may reside in a separate protein, or not be present. Some other members of the family, such as from Mycobacterium tuberculosis, are considerably longer, contain an apparent amidotransferase domain, and show glutamine-dependent as well as NH(3)-dependent activity. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]


Pssm-ID: 273132 [Multi-domain]  Cd Length: 250  Bit Score: 60.48  E-value: 1.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213   3 EKFIEEKVreirETVGDAKAIIALSGGVDSSTAAVLAHKAIGDRLHAVFVNTGflrKGEPEFVVK---TFRDEFGMNLHY 79
Cdd:TIGR00552  10 EDFLRGYV----QKSGAKGVVLGLSGGIDSAVVAALCVEALGEQNHALLLPHS---VQTPEQDVQdalALAEPLGINYKN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  80 VDAQDRFFEALKGVTDPEEKRKIIGRVFIEVFEEVAkeigAEYLIQGtiapdwieskgkiKSHHNVGGLPERLNLKL--- 156
Cdd:TIGR00552  83 IDIAPIAASFQAQTETGDELSDFLAKGNLKARLRMA----ALYAIAN-------------KHNLLVLGTGNKSELMLgyf 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2796056213 157 ---------IEPLRDLYKDEVRQLAKELGLPEKIYNRMP----FPG 189
Cdd:TIGR00552 146 tkygdggcdIAPIGDLFKTQVYELAKRLNVPERIIEKPPtadlFDG 191
TilS COG0037
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ...
 23-178 8.78e-10

tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA(Ile)-lysidine synthase TilS/MesJ is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439807 [Multi-domain]  Cd Length: 235  Bit Score: 57.92  E-value: 8.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  23 IIALSGGVDSST-AAVLAH--KAIGDRLHAVFVNTGfLRK--GEPEFVVKTFRDEFGMNLHYVDAQDRFFEALKGVTdPE 97
Cdd:COG0037    19 LVAVSGGKDSLAlLHLLAKlrRRLGFELVAVHVDHG-LREesDEDAEFVAELCEELGIPLHVVRVDVPAIAKKEGKS-PE 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  98 E-----KRKIigrvfievFEEVAKEIGAEYLIQGtiapdwieskgkiksHH----------------NVGGLP-----ER 151
Cdd:COG0037    97 AaarraRYGA--------LYELARELGADKIATG---------------HHlddqaetfllnllrgsGLAGLAgmppsRG 153

                         170       180
                  ....*....|....*....|....*..
gi 2796056213 152 LNLKLIEPLRDLYKDEVRQLAKELGLP 178
Cdd:COG0037   154 GGVRLIRPLLYVSRKEIEAYAKENGLP 180
TilS_N cd01992
N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine ...
 23-178 7.65e-09

N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine synthase (EC 6.3.4.19), also called tRNA(Ile)-2-lysyl-cytidine synthase or tRNA(Ile)-lysidine synthetase, catalyzes the ligation of lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. This subfamily belongs to the adenine nucleotide alpha hydrolase superfamily that also includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to adenosine group. This domain has a strongly conserved motif SGGXD at the N-terminus.


Pssm-ID: 467496 [Multi-domain]  Cd Length: 185  Bit Score: 54.52  E-value: 7.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  23 IIALSGGVDSSTAAVLAHKAI---GDRLHAVFVNTGfLRKG---EPEFVVKTFRDeFGMNLHYVdaqdRFFEALKGVTDP 96
Cdd:cd01992     3 LVAVSGGPDSMALLHLLKELRpklGLKLVAVHVDHG-LREEsaeEAQFVAKLCKK-LGIPLHIL----TVTEAPKSGGNL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  97 EEK-RKIigRvfIEVFEEVAKEIGAEYLIQGTIAPDWIE------SKGkikSH-HNVGGLPERL---NLKLIEPLRDLYK 165
Cdd:cd01992    77 EAAaREA--R--YAFLERAAKEHGIDVLLTAHHLDDQAEtvlmrlLRG---SGlSGLAGMAARSkagGIRLIRPLLGISK 149

                         170
                  ....*....|...
gi 2796056213 166 DEVRQLAKELGLP 178
Cdd:cd01992   150 AELLAYCRENGLP 162
QueC pfam06508
Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis ...
 21-178 2.42e-08

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: 53.39  E-value: 2.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  21 KAIIALSGGVDSSTAAVLAHKAiGDRLHAVFVNTGFLRKGEPEfVVKTFRDEFGMNLHYVDAQdrFFEALKG-------- 92
Cdd:pfam06508   1 KAVVLLSGGLDSTTCLAWAKKE-GYEVYALSFDYGQRHRKELE-CAKKIAKALGVEHKILDLD--FLKQIGGsaltddsi 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  93 -VTDPEEKRKII------GR--VFIEVFEEVAKEIGAEYLIQGTIA----------PDWIESkgkikshhnvggLPERLN 153
Cdd:pfam06508  77 eVPKAELESEEIpntyvpGRnlIFLSIAASLAEALGAEAIFIGVNEedysgypdcrPEFVKA------------FNVALN 144

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2796056213 154 L-------KLIEPLRDLYKDEVRQLAKELGLP 178
Cdd:pfam06508 145 LgtmgkpiEIHTPLMDLSKAEIVKLGDELGVP 176
tRNA_Me_trans pfam03054
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ...
 21-178 4.63e-08

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: 52.25  E-value: 4.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  21 KAIIALSGGVDSSTAAVLAHKAiGDRLHAVF----VNTGFLRKGEPEFVVKTFRD------EFGMNLHYVDAQDRFFEAl 90
Cdd:pfam03054   2 KVVVAMSGGVDSSVAAYLLKEQ-GHNVIGVFmknwDEEQSLDEEGKCCSEEDLADaqrvceQLGIPLYVVNFEKEYWED- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  91 kgVTDP--EEKRKiiGRV------------FIEVFEEVAKEIGAEYLIQGTIAPDWIESKGKIKSHHNV----------G 146
Cdd:pfam03054  80 --VFEPflDEYKN--GRTpnpdvlcnkeikFGALLDYALENLGADYVATGHYARVSLNKDGGSELLRALdknkdqsyflS 155

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2796056213 147 GLPERLNLKLIEPLRDLYKDEVRQLAKELGLP 178
Cdd:pfam03054 156 TLSQEQLEKLLFPLGELTKEEVRKIAKEAGLA 187
mnmA PRK00143
tRNA-specific 2-thiouridylase MnmA; Reviewed
 21-178 7.34e-08

tRNA-specific 2-thiouridylase MnmA; Reviewed


Pssm-ID: 234664 [Multi-domain]  Cd Length: 346  Bit Score: 53.15  E-value: 7.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  21 KAIIALSGGVDSSTAAVLAHKA----IGdrLH-AVFVNTGFLRKGE---PEFVVKTFR--DEFGMNLHYVDAQDRFfeal 90
Cdd:PRK00143    2 RVVVGMSGGVDSSVAAALLKEQgyevIG--VFmKLWDDDDETGKGGccaEEDIADARRvaDKLGIPHYVVDFEKEF---- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  91 kgvtdpeeKRKIIGRvFIE---------------------VFEEVAKEIGAEYLIQG---TIAPDWIESKGKIKSH---- 142
Cdd:PRK00143   76 --------WDRVIDY-FLDeykagrtpnpcvlcnkeikfkAFLEYARELGADYIATGhyaRIRDGRELLRGVDPNKdqsy 146

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2796056213 143 --HNVGglPERLNlKLIEPLRDLYKDEVRQLAKELGLP 178
Cdd:PRK00143  147 flYQLT--QEQLA-KLLFPLGELTKPEVREIAEEAGLP 181
MnmA COG0482
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ...
 21-178 1.78e-07

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: 51.98  E-value: 1.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  21 KAIIALSGGVDSSTAAVLAHKAiGDRLHAVFV----NTGFLRKGE---PEFVVKTFR--DEFGMNLHYVDAQDRFFEAlk 91
Cdd:COG0482     2 RVVVGMSGGVDSSVAAALLKEQ-GYEVIGVTMklwdDDDASGSGGccsLEDIEDARRvaDKLGIPHYVVDFEEEFKDR-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  92 gVTDP--EEKRKiiGR-----------VFIEVFEEVAKEIGAEYLIQGTIApdwieskgKIKSHHNVGGL---------- 148
Cdd:COG0482    79 -VIDYflDEYLA--GRtpnpcvlcnreIKFGALLEKALELGADYIATGHYA--------RVEEKDGRYELlrgvdpnkdq 147

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2796056213 149 --------PERLNlKLIEPLRDLYKDEVRQLAKELGLP 178
Cdd:COG0482   148 syflyrltQEQLS-KTLFPLGELTKPEVREIAEELGLP 184
QueC-like cd01995
7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC ...
 21-178 2.05e-07

7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC 6.3.4.20) is also called 7-cyano-7-carbaguanine synthase, preQ(0) synthase, or queuosine biosynthesis protein QueC. It catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)), as part of the biosynthesis pathway of queuosine (Q). Q is one of the most complex modifications occurring at the wobble position of tRNAs with GUN anticodons, and is implicated in a number of biological activities, including accuracy of decoding, virulence, and cellular differentiation. This subfamily belongs to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.


Pssm-ID: 467499 [Multi-domain]  Cd Length: 208  Bit Score: 50.69  E-value: 2.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  21 KAIIALSGGVDSSTAAVLAhKAIGDRLHAVFVNTGFLRKGEPEFVVKTFRDEFGMNLHYVDAqdRFFEALKG-------- 92
Cdd:cd01995     2 KAVVLLSGGLDSTTLLYWA-LKEGYEVHALTFDYGQRHAKEELEAAKLIAKLLGIEHKVIDL--SFLGELGGssltdege 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  93 -VTDPEEKRKII------GR--VFIEVFEEVAKEIGAEYLIQGTIAPD----WIESKGKIKSHHNVGGLPERLNLKLIEP 159
Cdd:cd01995    79 eVPDGEYDEESIpstwvpNRnlIFLSIAAAYAESLGASAIVIGVNAEDasgyPDCRPEFVEAMNSALNLGTATGVKVVAP 158

                         170
                  ....*....|....*....
gi 2796056213 160 LRDLYKDEVRQLAKELGLP 178
Cdd:cd01995   159 LIGLSKAEIVKLGVELGVP 177
NadE COG0171
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ...
 2-51 6.16e-07

NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ synthetase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 439941 [Multi-domain]  Cd Length: 542  Bit Score: 50.62  E-value: 6.16e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2796056213   2 WEKFIEEKVREIRETVGDA---KAIIALSGGVDSSTAAVLAHKAIG-DRLHAVF 51
Cdd:COG0171   266 LEEVYDALVLGLRDYVRKNgfkGVVLGLSGGIDSALVAALAVDALGpENVLGVT 319
PRK13795 PRK13795
hypothetical protein; Provisional
 3-91 6.94e-07

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 50.38  E-value: 6.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213   3 EKFIEEKVREIRETVG--DAKAIIALSGGVDSSTAAVLAHKAiGDRLHAVFVNTG--FlrkgePEFV--VKTFRDEFGMN 76
Cdd:PRK13795  225 EEKEKEAVNFIRGVAEkyNLPVSVSFSGGKDSLVVLDLAREA-LKDFKAFFNNTGleF-----PETVenVKEVAEEYGIE 298

                          90
                  ....*....|....*
gi 2796056213  77 LHYVDAQDRFFEALK 91
Cdd:PRK13795  299 LIEADAGDAFWRAVE 313
CTU1-like cd01713
cytoplasmic tRNA 2-thiolation protein 1 and similar proteins; This subfamily includes human ...
 6-178 8.62e-07

cytoplasmic tRNA 2-thiolation protein 1 and similar proteins; This subfamily includes human cytoplasmic tRNA 2-thiolation protein 1, also called cytosolic thiouridylase subunit 1 (CTU1), ATP-binding domain-containing protein 3 (ATPBD3), cancer-associated gene protein, or cytoplasmic tRNA adenylyltransferase 1. CTU1 plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). It directly binds tRNAs and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation. The CTU1-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.


Pssm-ID: 467486  Cd Length: 208  Bit Score: 48.74  E-value: 8.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213   6 IEEKV-REIRETV----GDaKAIIALSGGVDSSTAAVLAHKAIGD-----RLHAVFVNTG--FLRKGEPEfVVKTFRDEF 73
Cdd:cd01713     1 IERRVhRTIRKYRlikpGD-RVAVGLSGGKDSTVLLYVLKELNKRhdygvELIAVTIDEGikGYRDDSLE-AARKLAEEY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  74 GMNLHYVDAQDRFfealkGVTDPEEKRKIIGRV----FIEVF-----EEVAKEIGAEYLIQGTIAPDWIES------KGK 138
Cdd:cd01713    79 GIPLEIVSFEDEF-----GFTLDELIVGKGGKKnactYCGVFrrralNRGARELGADKLATGHNLDDEAETilmnllRGD 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2796056213 139 IKSHHNVGGLPERLNLKL---IEPLRDLYKDEVRQLAKELGLP 178
Cdd:cd01713   154 VARLLRTGPEPRSEGEGLvprIKPLRYIPEKEIVLYAHLNGLP 196
COG1365 COG1365
Predicted ATPase, PP-loop superfamily [General function prediction only];
20-126 3.03e-06

Predicted ATPase, PP-loop superfamily [General function prediction only];


Pssm-ID: 440976  Cd Length: 256  Bit Score: 47.74  E-value: 3.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  20 AKAIIALSGGVDSSTAAVLAhKAIGDRLHAVFVNTGFLRKGEPEFVVKTFRDEFGMNLHYVDAQ--DRFFEALKGvtdpe 97
Cdd:COG1365    61 PKVVVAFSGGVDSSASLIIA-KWIGFDVEAVTVKSTIILPQMFKKNIKELCKKLNVKHEFIEIDlgEIIEDALKG----- 134

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2796056213  98 eKRKIIGR---VFIEVFEEVAKEIGAEYLIQG 126
Cdd:COG1365   135 -KFHPCGRchsLIEEAVEDYAKKNGIKIVIFG 165
lysidine_TilS_N TIGR02432
tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble ...
 21-184 3.84e-06

tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble position of a tRNA must discriminate between G and A of mRNA are AUA (Ile) vs. AUG (Met) and UGA (stop) vs. UGG (Trp). In all bacteria, the wobble position of the tRNA(Ile) recognizing AUA is lysidine, a lysine derivative of cytidine. This family describes a protein domain found, apparently, in all bacteria in a single copy. Eukaryotic sequences appear to be organellar. The domain archictecture of this protein family is variable; some, including characterized proteins of E. coli and B. subtilis known to be tRNA(Ile)-lysidine synthetase, include a conserved 50-residue domain that many other members lack. This protein belongs to the ATP-binding PP-loop family ( pfam01171). It appears in the literature and protein databases as TilS, YacA, and putative cell cycle protein MesJ (a misnomer). [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274129 [Multi-domain]  Cd Length: 189  Bit Score: 46.47  E-value: 3.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  21 KAIIALSGGVDSStaaVLAH------KAIGDRLHAVFVNTGfLRKG---EPEFVVKtFRDEFGMNLHYVDAQDRFFEALK 91
Cdd:TIGR02432   1 RILVAVSGGVDSM---ALLHlllklqPKIKIKLIAAHVDHG-LRPEsdeEAEFVQQ-FCRKLNIPLEIKKVDVKALAKGK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  92 GVTDPEEKRKIigRvfIEVFEEVAKEIGAEYLIQGTIAPDWIE-----------SKGkIKSHHNVGGLPERLNlkLIEPL 160
Cdd:TIGR02432  76 KKNLEEAAREA--R--YDFFEEIAKKHGADYILTAHHADDQAEtilmrllrgsgLRG-LSGMKPIRILGSGIQ--IIRPL 148

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2796056213 161 RDLYKDEVRQLAKELGLP--------EKIYNR 184
Cdd:TIGR02432 149 LGISKSEIEEYLKENGLPwfedetnqDDKYLR 180
MnmA_TRMU-like cd01998
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ...
 21-178 5.96e-06

MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial tRNA-specific 2-thiouridylase MnmA (EC 2.8.1.13) and mitochondrial tRNA-specific 2-thiouridylase 1 (TRMU or MTU1, EC 2.8.1.14). MnmA catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. TRMU/MTU1 catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln); this is required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. This family belongs to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.


Pssm-ID: 467502 [Multi-domain]  Cd Length: 349  Bit Score: 47.12  E-value: 5.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  21 KAIIALSGGVDSSTAAVLAHKAiGDRLHAVFVNTGFLRKGEP---------EFVVKTfRDEFGMNLHYVDAQDRFFEalk 91
Cdd:cd01998     1 KVAVAMSGGVDSSVAAALLKEQ-GYDVIGVFMKNWDDEDNEKggccseediEDARRV-ADQLGIPLYVVDFSEEYWE--- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  92 GVTDP--EEKRKiiGRV---------FI--EVFEEVAKEIGAEYLIQGTIApdwieskgKIKSHHNVGGL---------- 148
Cdd:cd01998    76 RVFDPflEEYKA--GRTpnpdvlcnrEIkfGALLDAAKKLGADYIATGHYA--------RIEEDNRGRYRllravdpnkd 145

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2796056213 149 ---------PERLNlKLIEPLRDLYKDEVRQLAKELGLP 178
Cdd:cd01998   146 qsyflsrlsQEQLS-RTLFPLGHLTKSEVREIAREAGLP 183
nadE PRK00876
NAD(+) synthase;
6-186 1.26e-05

NAD(+) synthase;


Pssm-ID: 179150 [Multi-domain]  Cd Length: 326  Bit Score: 46.10  E-value: 1.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213   6 IEEKVRE-IRETVGDAKAIIALSGGVDSSTAAVLAHKAIG-DRLHAVF---------------------------VNTG- 55
Cdd:PRK00876   19 IRAAIREqVRGTLRRRGVVLGLSGGIDSSVTAALCVRALGkERVYGLLmperdsspeslrlgrevaehlgveyvvEDITp 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  56 -------------FLRKGEPEF--------VVKTFRDEFGMNLHYVDAQDRFFEALKGVTDPEEKRKIIG--------RV 106
Cdd:PRK00876   99 alealgcyrrrdeAIRRVVPEYgpgwkskiVLPNLLDGDGLNVFSLVVQDPDGEVTRKRLPANAYLQIVAatnfkqrtRK 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213 107 FIEVFEevakeigAEYLiqgtiapdwieskgkiksHHNVGGLPERLNLKL------------IEPLRDLYKDEVRQLAKE 174
Cdd:PRK00876  179 MVEYYH-------ADRL------------------NYAVAGTPNRLEYDQgffvkngdgaadLKPIAHLYKTQVYALAEH 233

                         250
                  ....*....|..
gi 2796056213 175 LGLPEKIYNRMP 186
Cdd:PRK00876  234 LGVPEEIRRRPP 245
AANH-like cd01986
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ...
 22-73 5.71e-05

adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide alpha hydrolase (AANH)-like proteins includes N-type ATP PPases and ATP sulfurylases. The domain forms an alpha/beta/alpha fold which binds to adenosine nucleotide.


Pssm-ID: 467490 [Multi-domain]  Cd Length: 74  Bit Score: 40.51  E-value: 5.71e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2796056213  22 AIIALSGGVDSSTAAVLAHKAIGDRLH-AVFVNTGFLRKGEPEFVVKTFRDEF 73
Cdd:cd01986     1 VVVGYSGGKDSSVALHLASRLGRKAEVaVVHIDHGIGFKEEAESVASIARRSI 53
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 7-101 6.32e-05

3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or related enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; 3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or related enzyme is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 439945 [Multi-domain]  Cd Length: 232  Bit Score: 43.30  E-value: 6.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213   7 EEKVREIRETVGDaKAIIALSGGVDSSTAAVLAHKaIGDRLHAVFVNTGFlrkgepEF-----VVKTFRDEFGMNLHYVD 81
Cdd:COG0175    22 IEILREAAAEFGG-RVVVSSSGGKDSTVLLHLAAK-FKPPIPVLFLDTGY------EFpetyeFRDRLAERLGLDLIVVR 93

                          90       100
                  ....*....|....*....|..
gi 2796056213  82 AQDRFFEAL--KGVTDPEEKRK 101
Cdd:COG0175    94 PEDAFAEQLaeFGPPLFYRDPR 115
ATP_bind_3 pfam01171
PP-loop family; This family of proteins belongs to the PP-loop superfamily.
 24-178 6.50e-05

PP-loop family; This family of proteins belongs to the PP-loop superfamily.


Pssm-ID: 426097 [Multi-domain]  Cd Length: 178  Bit Score: 42.61  E-value: 6.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  24 IALSGGVDSSTAAVLAHKAIGDRLH---AVFVNTGfLR---KGEPEFvVKTFRDEFGMNLHYVDAQDrffEALKGVTDPE 97
Cdd:pfam01171   1 VAVSGGPDSMALLYLLAKLKIKLGIeltAAHVNHG-LReesDREAEH-VQALCRQLGIPLEILRVDV---AKKSGENLEA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  98 EKRKIigRVfiEVFEEVAKEIGAEYLIQGTIAPDWIE------SKGKIKShhNVGGLP---ERLNLKLIEPLRDLYKDEV 168
Cdd:pfam01171  76 AAREA--RY--DFFEEALKKHGADVLLTAHHLDDQLEtflmrlKRGSGLA--GLAGIPpvrEFAGGRIIRPLLKVSKAEI 149

                         170
                  ....*....|
gi 2796056213 169 RQLAKELGLP 178
Cdd:pfam01171 150 EAYAKEHKIP 159
TtcA-like cd24138
tRNA-cytidine(32) 2-sulfurtransferase and similar proteins; tRNA-cytidine(32) ...
 13-178 1.00e-04

tRNA-cytidine(32) 2-sulfurtransferase and similar proteins; tRNA-cytidine(32) 2-sulfurtransferase, also called two-thiocytidine biosynthesis protein A or tRNA 2-thiocytidine biosynthesis protein TtcA, catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). TtcA belongs to the adenine nucleotide alpha hydrolase superfamily (AANH) that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. This domain has a strongly conserved motif SGGKD at the N-terminus.


Pssm-ID: 467514 [Multi-domain]  Cd Length: 187  Bit Score: 42.26  E-value: 1.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  13 IREtvGDaKAIIALSGGVDSSTAA----VLAHKA-IGDRLHAVFVNTGFLRKGEPEFVVKTFRDEFGMNLHYVDAQDRFf 87
Cdd:cd24138     5 IEP--GD-RILVGLSGGKDSLTLLhlleELKRRApIKFELVAVTVDPGYPGYRPPREELAEILEELGEILEDEESEIII- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  88 ealKGVTDPEE---------KRKIIGRvfievfeeVAKEIGAEYLIQGTIAPDWIES-------KGKIKshhnvgGLP-- 149
Cdd:cd24138    81 ---IEKEREEKspcslcsrlRRGILYS--------LAKELGCNKLALGHHLDDAVETllmnllyGGRLK------TMPpk 143

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2796056213 150 ---ERLNLKLIEPLRDLYKDEVRQLAKELGLP 178
Cdd:cd24138   144 vtmDRGGLTVIRPLIYVREKDIRAFAEENGLP 175
QueC COG0603
7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and ...
 21-55 1.21e-04

7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and biogenesis]; 7-cyano-7-deazaguanine synthase (queuosine biosynthesis) is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440368 [Multi-domain]  Cd Length: 223  Bit Score: 42.46  E-value: 1.21e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2796056213  21 KAIIALSGGVDSSTAAVLAhKAIGDRLHAVFVNTG 55
Cdd:COG0603     4 KAVVLLSGGLDSTTCLAWA-LARGYEVYALSFDYG 37
PRK08557 PRK08557
hypothetical protein; Provisional
 25-90 1.40e-04

hypothetical protein; Provisional


Pssm-ID: 181465 [Multi-domain]  Cd Length: 417  Bit Score: 43.20  E-value: 1.40e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2796056213  25 ALSGGVDSSTAAVLAHKAIGDrLHAVFVNTGFLRKGEPEFvVKTFRDEFGMNLHYVDAQDrFFEAL 90
Cdd:PRK08557  187 SFSGGKDSSVSTLLAKEVIPD-LEVIFIDTGLEYPETINY-VKDFAKKYDLNLDTLDGDN-FWENL 249
ASS cd01999
argininosuccinate_synthase (ASS); Argininosuccinate synthase (ASS; EC 6.3.4.5) is a urea cycle ...
 21-126 6.94e-04

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: 40.98  E-value: 6.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  21 KAIIALSGGVDSSTAAVLAHKAIGDRLHAVFVNTGflRKGEPEFVVKTFRDEFGMNLHYVDAQDRF-----FEALKGVTD 95
Cdd:cd01999     2 KVVLAYSGGLDTSVILKWLKEEYGYEVIAFTADLG--QGDEEEEIEEKALKLGAVKVYVVDLREEFaedyiFPAIKANAI 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2796056213  96 PEEK--------RKIIGRVFIevfeEVAKEIGAEYLIQG 126
Cdd:cd01999    80 YEGRyplgtalaRPLIAKKLV----EVAREEGATAVAHG 114
ThiI pfam02568
Thiamine biosynthesis protein (ThiI); ThiI is required for thiazole synthesis, required for ...
 21-176 1.56e-03

Thiamine biosynthesis protein (ThiI); ThiI is required for thiazole synthesis, required for thiamine biosynthesis.


Pssm-ID: 280691 [Multi-domain]  Cd Length: 197  Bit Score: 38.95  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  21 KAIIALSGGVDSSTAAVLAHKAiGDRLHAVFVntgFLRKGEPEFVVKTFRD------EFG----MNLHYVDAQDRFFEAL 90
Cdd:pfam02568   5 KVLALISGGIDSPVAAYMMMRR-GCRVVALHF---INNPGTSAEAIGKVQKlaellaRYGtsheVRLVVFDFTDVQKEIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  91 KGVtdPEEKRKII-GRVFIEVFEEVAKEIGAEYLIQGtiapdwiESKGKIKSH--HNVGGLPERLNLKLIEPLRDLYKDE 167
Cdd:pfam02568  81 EKA--PEGYRCVLlKRCMYRIAEKVAEEEGADALVTG-------ESLGQVASQtlDNLRVISAVSNTPILRPLIGLDKED 151


                  ....*....
gi 2796056213 168 VRQLAKELG 176
Cdd:pfam02568 152 IINLAKEIG 160
Asn_synthase_B_C cd01991
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or ...
 19-84 2.24e-03

C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or synthetase) B is always associated with an N-terminal amidotransferase domain. Family members that contain this domain catalyze the conversion of aspartate to asparagine. Asparagine synthase B catalyzes the synthesis of asparagine from aspartate, Mg(2+)ATP, and glutamine. The three-dimensional architecture of the N-terminal domain of asparagine synthetase B is similar to that observed for glutamine phosphoribosylpyrophosphate amidotransferase while the molecular motif of the C-domain is reminiscent to that observed for GMP synthetase.


Pssm-ID: 467495 [Multi-domain]  Cd Length: 224  Bit Score: 38.79  E-value: 2.24e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2796056213  19 DAKAIIALSGGVDSSTAAVLAHKAIGD-RLHAvfVNTGFLRKGEPE--FVVKTFrDEFGMNLH--YVDAQD 84
Cdd:cd01991     2 DVPVGVLLSGGLDSSLIAALAARLLPEtPIDL--FTVGFEGSPTPDraAARRVA-EELGTEHHevEVTIEE 69
TtuA-like cd01993
tRNA-5-methyluridine(54) 2-sulfurtransferase and similar proteins; tRNA-5-methyluridine(54) ...
 19-101 3.87e-03

tRNA-5-methyluridine(54) 2-sulfurtransferase and similar proteins; tRNA-5-methyluridine(54) 2-sulfurtransferase, also called tRNA thiouridine synthetase TtuA, catalyzes the ATP-dependent 2-thiolation of 5-methyluridine residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2-thiouridine (m(5)s(2)U or s(2)T). TtuA belongs to the adenine nucleotide alpha hydrolase superfamily (AANH) that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. This domain has a strongly conserved motif SGGKD at the N-terminus.


Pssm-ID: 467497 [Multi-domain]  Cd Length: 190  Bit Score: 37.69  E-value: 3.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  19 DAKAIIALSGGVDSSTAAVLAHKaIGDRLHAVFVNTGFLRKGE-PEFVVKTFRDEFGMNLHYVDAQDrffEALKGVTDPE 97
Cdd:cd01993     8 DDKILVAVSGGKDSLALLAVLKK-LGYNVEALYINLGIGEYSEkSEEVVKKLAEKLNLPLHVVDLKE---EYGLGIPELA 83


                  ....
gi 2796056213  98 EKRK 101
Cdd:cd01993    84 KKSR 87
AANH_WbpG-like cd01996
Rhizobium leguminosarum WbpG protein and similar proteins; This subfamily includes Rhizobium ...
 22-79 6.76e-03

Rhizobium leguminosarum WbpG protein and similar proteins; This subfamily includes Rhizobium leguminosarum WbpG and Campylobacter jejuni PseA proteins. They belong to the of adenine nucleotide alpha hydrolase (AANH) superfamily that also includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to adenosine group. This subfamily of proteins is predicted to bind ATP. This domain has a strongly conserved motif SGGKD at the N-terminus.


Pssm-ID: 467500 [Multi-domain]  Cd Length: 158  Bit Score: 36.58  E-value: 6.76e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213  22 AIIALSGGVDSSTAAVLAHKAIGDRLHAVFVNTGFLRkgePEFV--VKTFRDEFGMNLHY 79
Cdd:cd01996     8 CIIGVSGGKDSTYAAHKAKEKYGLRPLLVTVDAGWNS---PEAVknIEKLVRALGVDLIT 64
AsnB COG0367
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ...
 7-93 6.87e-03

Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; Asparagine synthetase B (glutamine-hydrolyzing) is part of the Pathway/BioSystem: Asparagine biosynthesis


Pssm-ID: 440136 [Multi-domain]  Cd Length: 558  Bit Score: 37.89  E-value: 6.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796056213   7 EEKVREIRETVGDA--KAIIA-------LSGGVDSSTAAVLAHKAIGDRLHAvFvNTGFLRKGEPEF-VVKTFRDEFGMN 76
Cdd:COG0367   235 EEAVEELRELLEDAvrRRLRAdvpvgafLSGGLDSSAIAALAARLSKGPLKT-F-SIGFEDSAYDESpYARAVAEHLGTE 312

                          90
                  ....*....|....*....
gi 2796056213  77 LH--YVDAQDrFFEALKGV 93
Cdd:COG0367   313 HHevTVTPED-LLDALPDL 330
PRK04527 PRK04527
argininosuccinate synthase; Provisional
 21-88 9.32e-03

argininosuccinate synthase; Provisional


Pssm-ID: 235305  Cd Length: 400  Bit Score: 37.51  E-value: 9.32e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2796056213  21 KAIIALSGGVDSSTAaVLAHKAIGDRLHAVFVNTGFLRKGEPEFVVKTFRdEFGMNLHY-VDAQDRFFE 88
Cdd:PRK04527    4 DIVLAFSGGLDTSFC-IPYLQERGYAVHTVFADTGGVDAEERDFIEKRAA-ELGAASHVtVDGGPAIWE 70
PRK13981 PRK13981
NAD synthetase; Provisional
 21-51 9.78e-03

NAD synthetase; Provisional


Pssm-ID: 237577 [Multi-domain]  Cd Length: 540  Bit Score: 37.44  E-value: 9.78e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2796056213  21 KAIIALSGGVDSSTAAVLAHKAIG-DRLHAVF 51
Cdd:PRK13981  282 GVVLGLSGGIDSALVAAIAVDALGaERVRAVM 313
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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