|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08099 |
PRK08099 |
multifunctional transcriptional regulator/nicotinamide-nucleotide adenylyltransferase ... |
13-409 |
0e+00 |
|
multifunctional transcriptional regulator/nicotinamide-nucleotide adenylyltransferase/ribosylnicotinamide kinase NadR;
Pssm-ID: 236151 [Multi-domain] Cd Length: 399 Bit Score: 827.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111746 13 QQGCTLQQVADASGMTKGYLSQLLNAKIKSPSAQKLEALHRFLGLEFPRQKKTIGVVFGKFYPLHTGHIYLIQRACSQVD 92
Cdd:PRK08099 1 QQGCTLQQVADASGMTKGYLSQLLNAKIKSPSAQKLEALHRFLGLEFPRQMKKIGVVFGKFYPLHTGHIYLIQRACSQVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111746 93 ELHIIMGFDDTRDRALFEDSAMSQQPTVPDRLRWLLQTFKYQKNIRIHAFNEEGMEPYPHGWDVWSNGIKKFMAEKGIQP 172
Cdd:PRK08099 81 ELHIIICYDDERDRKLFEDSAMSQQPTVSDRLRWLLQTFKYQKNIKIHAFNEEGMEPYPHGWDVWSNGIKAFMAEKGIQP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111746 173 DLIYTSEEADAPQYMEHLGIETVLVDPKRTFMSISGAQIRENPFRYWEYIPTEVKPFFVRTVAILGGESSGKSTLVNKLA 252
Cdd:PRK08099 161 DVIYTSEEQDAPQYEEHLGIETVLVDPKRTFMNISGTQIRENPFRYWEYIPTEVRPFFVRTVAILGGESSGKSTLVNKLA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111746 253 NIFNTTSAWEYGRDYVFSHLGGDEIALQYSDYDKIALGHAQYIDFAVKYANKVAFIDTDFVTTQAFCKKYEGREHPFVQA 332
Cdd:PRK08099 241 NIFNTTSAWEYGREYVFSHLGGDEMALQYSDYDKIALGHAQYIDFAVKYANKVAFIDTDFVTTQAFCKKYEGREHPFVQA 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90111746 333 LIDEYRFDLVILLENNTPWVADGLRSLGSSVDRKEFQNLLVEMLEENNIEFVRVEEEDYDSRFLRCVELVREMMGEQ 409
Cdd:PRK08099 321 LIDEYRFDLTILLENNTPWVADGLRSLGSSVDRKRFQNLLKEMLKENNIEYVHVESPDYDKRYLRCVELVDQMLGEQ 397
|
|
| nadR_NMN_Atrans |
TIGR01526 |
nicotinamide-nucleotide adenylyltransferase, NadR type; The NadR protein of E. coli and ... |
64-395 |
0e+00 |
|
nicotinamide-nucleotide adenylyltransferase, NadR type; The NadR protein of E. coli and closely related bacteria is both enzyme and regulatory protein. The first 60 or so amino acids, N-terminal to the region covered by this model, is a DNA-binding helix-turn-helix domain (pfam01381) responsible for repressing the nadAB genes of NAD de novo biosynthesis. The NadR homologs in Mycobacterium tuberculosis, Haemophilus influenzae, and others appear to lack the repressor domain. NadR has recently been shown to act as an enzyme of the salvage pathway of NAD biosynthesis, nicotinamide-nucleotide adenylyltransferase; members of this family are presumed to share this activity. E. coli NadR has also been found to regulate the import of its substrate, nicotinamide ribonucleotide, but it is not known if the other members of this model share that activity.
Pssm-ID: 273670 [Multi-domain] Cd Length: 325 Bit Score: 559.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111746 64 KTIGVVFGKFYPLHTGHIYLIQRACSQVDELHIIMGFddtrdraLFEDSAMSQQPTVPDRLRWLLQTFKYQKN-IRIHAF 142
Cdd:TIGR01526 1 KTIGVVFGKFYPLHTGHIYLIYEAFSKVDELHIVVGS-------LFYDSKAKRPPPVQDRLRWLREIFKYQKNqIFIHHL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111746 143 NEEGMEPYPHGWDVWSNGIKKFMAEKGIQPDLIYTSEEADAPQYMEHLGIETVLVDPKRTFMSISGAQIRENPFRYWEYI 222
Cdd:TIGR01526 74 NEDGIPEYPNGWDSWSNALKTLFHEKHFEPDIVFSSEPQYAAPYEKYLGLEVVLVDPDRTFFSVSATQIRENPFQHWKHI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111746 223 PTEVKPFFVRTVAILGGESSGKSTLVNKLANIFNTTSAWEYGRDYVFSHLGGDEiALQYSDYDKIALGHAQYIDFAVKYA 302
Cdd:TIGR01526 154 PREVRPFFVKTVAILGGESTGKSTLVNKLAAVFNTTSAWEYAREYVEEKLGGDE-ALQYSDYAQIALGQQRYIDYAVRHA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111746 303 NKVAFIDTDFVTTQAFCKKYEGREHPFVQALIDEYRFDLVILLENNTPWVADGLRSLGSSVDRKEFQNLLVEMLEENNIE 382
Cdd:TIGR01526 233 HKIAFIDTDFITTQVFAKQYEGREHPFLDSDIAEYPFDLTLLLKPNTEWVDDGLRSLGSQKQRQEFQQLLKKLLDEYGVP 312
|
330
....*....|...
gi 90111746 383 FVRVEEEDYDSRF 395
Cdd:TIGR01526 313 FVVIESPDYLDRY 325
|
|
| NMNAT_NadR |
cd02167 |
Nicotinamide/nicotinate mononucleotide adenylyltransferase of bifunctional NadR-like proteins; ... |
66-227 |
1.27e-84 |
|
Nicotinamide/nicotinate mononucleotide adenylyltransferase of bifunctional NadR-like proteins; NMNAT domain of NadR protein. The NadR protein (NadR) is a bifunctional enzyme possessing both NMN adenylytransferase (NMNAT) and ribosylnicotinamide kinase (RNK) activities. Its function is essential for the growth and survival of H. influenzae and thus may present a new highly specific anti-infectious drug target. The N-terminal domain that hosts the NMNAT activity is closely related to archaeal NMNAT. The bound NAD at the active site of the NMNAT domain reveals several critical interactions between NAD and the protein.The NMNAT domain of hiNadR defines yet another member of the pyridine nucleotide adenylyltransferase
Pssm-ID: 173918 Cd Length: 158 Bit Score: 255.11 E-value: 1.27e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111746 66 IGVVFGKFYPLHTGHIYLIQRACSQVDELHIIMGFDDTRDRAlfedsamSQQPTVPDRLRWLLQTFKYQKNIRIHAFNEE 145
Cdd:cd02167 1 IGIVFGKFAPLHTGHVYLIYKALSQVDELLIIVGSDDTRDDA-------RTGLPLEKRLRWLREIFPDQENIVVHTLNEP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111746 146 GMEPYPHGWDVWSNGIKKFMAEKG-IQPDLIYTSEEADAPQY--MEHLGIETVLVDPKRTFMSISGAQIRENPFRYWEYI 222
Cdd:cd02167 74 DIPEYPNGWDIWSNRVKTLIAENTrCRPDIVFTAEEYEAAFElvLAYLGAQVVLVDPDRTDISVSATQIRENPFRYWYHI 153
|
....*
gi 90111746 223 PTEVK 227
Cdd:cd02167 154 PREVR 158
|
|
| NadR3 |
COG3172 |
Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase ... |
224-408 |
9.56e-76 |
|
Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase is part of the Pathway/BioSystem: NAD biosynthesis
Pssm-ID: 442405 [Multi-domain] Cd Length: 178 Bit Score: 233.17 E-value: 9.56e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111746 224 TEVKPFFVRTVAILGGESSGKSTLVNKLANIFNTTSAWEYGRDYVFSHLGgdeiALQYSDYDKIALGHAQYIDFAVKYAN 303
Cdd:COG3172 1 PEVRPSFVKKIVLLGAESTGKTTLARALAAHYNTPWVPEYGREYLEEKGR----ALTYDDLLAIARGQLALEDAAAKRAN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111746 304 KVAFIDTDFVTTQAFCKKYEGREHPFVQALIDEYRFDLVILLENNTPWVADGLRSLGSsvDRKEFQNLLVEMLEENNIEF 383
Cdd:COG3172 77 KLLFCDTDALTTKVYSELYFGKCPPWLEALAAQRRYDLYLLLDPDIPWVADGLRDGPE--VREEFQQLLREELEERGIPY 154
|
170 180
....*....|....*....|....*
gi 90111746 384 VRVeEEDYDSRFLRCVELVREMMGE 408
Cdd:COG3172 155 VVI-SGDYEERLEQALAAIDELLAK 178
|
|
| AAA_28 |
pfam13521 |
AAA domain; |
234-394 |
1.82e-36 |
|
AAA domain;
Pssm-ID: 433278 [Multi-domain] Cd Length: 164 Bit Score: 130.85 E-value: 1.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111746 234 VAILGGESSGKSTLVNKLANIFNTTSAWEYGRDYVFSHLGGDEIALQYSdYDKIALGH----AQYIDFAVKYANKVAFID 309
Cdd:pfam13521 2 IVITGGPSTGKTTLAEALAARFGYPVVPEAAREILEELGADGGDALPWV-EDLLAFARgvleAQLEDEAAAAANDLLFFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111746 310 TDFVTTQAFCKKYEGREHPFVQALIDEYRFDLVILLENNTPWVADGLRsLGSSVDRKEFQNLLVEMLEENNIEFVRVEEE 389
Cdd:pfam13521 81 RGPLDTLAYSRAYGGPCPPELEAAARASRYDLVFLLPPDPEIVQDGER-REDPEERERFHERLREALRELGIPVIIVPRG 159
|
....*
gi 90111746 390 DYDSR 394
Cdd:pfam13521 160 SVEER 164
|
|
| HTH_XRE |
smart00530 |
Helix-turn-helix XRE-family like proteins; |
7-58 |
2.04e-07 |
|
Helix-turn-helix XRE-family like proteins;
Pssm-ID: 197775 [Multi-domain] Cd Length: 56 Bit Score: 47.51 E-value: 2.04e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 90111746 7 LKTAIKQQGCTLQQVADASGMTKGYLSQLLNAKIKsPSAQKLEALHRFLGLE 58
Cdd:smart00530 2 LKELREEKGLTQEELAEKLGVSRSTLSRIENGKRK-PSLETLKKLAKALGVS 52
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08099 |
PRK08099 |
multifunctional transcriptional regulator/nicotinamide-nucleotide adenylyltransferase ... |
13-409 |
0e+00 |
|
multifunctional transcriptional regulator/nicotinamide-nucleotide adenylyltransferase/ribosylnicotinamide kinase NadR;
Pssm-ID: 236151 [Multi-domain] Cd Length: 399 Bit Score: 827.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111746 13 QQGCTLQQVADASGMTKGYLSQLLNAKIKSPSAQKLEALHRFLGLEFPRQKKTIGVVFGKFYPLHTGHIYLIQRACSQVD 92
Cdd:PRK08099 1 QQGCTLQQVADASGMTKGYLSQLLNAKIKSPSAQKLEALHRFLGLEFPRQMKKIGVVFGKFYPLHTGHIYLIQRACSQVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111746 93 ELHIIMGFDDTRDRALFEDSAMSQQPTVPDRLRWLLQTFKYQKNIRIHAFNEEGMEPYPHGWDVWSNGIKKFMAEKGIQP 172
Cdd:PRK08099 81 ELHIIICYDDERDRKLFEDSAMSQQPTVSDRLRWLLQTFKYQKNIKIHAFNEEGMEPYPHGWDVWSNGIKAFMAEKGIQP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111746 173 DLIYTSEEADAPQYMEHLGIETVLVDPKRTFMSISGAQIRENPFRYWEYIPTEVKPFFVRTVAILGGESSGKSTLVNKLA 252
Cdd:PRK08099 161 DVIYTSEEQDAPQYEEHLGIETVLVDPKRTFMNISGTQIRENPFRYWEYIPTEVRPFFVRTVAILGGESSGKSTLVNKLA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111746 253 NIFNTTSAWEYGRDYVFSHLGGDEIALQYSDYDKIALGHAQYIDFAVKYANKVAFIDTDFVTTQAFCKKYEGREHPFVQA 332
Cdd:PRK08099 241 NIFNTTSAWEYGREYVFSHLGGDEMALQYSDYDKIALGHAQYIDFAVKYANKVAFIDTDFVTTQAFCKKYEGREHPFVQA 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90111746 333 LIDEYRFDLVILLENNTPWVADGLRSLGSSVDRKEFQNLLVEMLEENNIEFVRVEEEDYDSRFLRCVELVREMMGEQ 409
Cdd:PRK08099 321 LIDEYRFDLTILLENNTPWVADGLRSLGSSVDRKRFQNLLKEMLKENNIEYVHVESPDYDKRYLRCVELVDQMLGEQ 397
|
|
| nadR_NMN_Atrans |
TIGR01526 |
nicotinamide-nucleotide adenylyltransferase, NadR type; The NadR protein of E. coli and ... |
64-395 |
0e+00 |
|
nicotinamide-nucleotide adenylyltransferase, NadR type; The NadR protein of E. coli and closely related bacteria is both enzyme and regulatory protein. The first 60 or so amino acids, N-terminal to the region covered by this model, is a DNA-binding helix-turn-helix domain (pfam01381) responsible for repressing the nadAB genes of NAD de novo biosynthesis. The NadR homologs in Mycobacterium tuberculosis, Haemophilus influenzae, and others appear to lack the repressor domain. NadR has recently been shown to act as an enzyme of the salvage pathway of NAD biosynthesis, nicotinamide-nucleotide adenylyltransferase; members of this family are presumed to share this activity. E. coli NadR has also been found to regulate the import of its substrate, nicotinamide ribonucleotide, but it is not known if the other members of this model share that activity.
Pssm-ID: 273670 [Multi-domain] Cd Length: 325 Bit Score: 559.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111746 64 KTIGVVFGKFYPLHTGHIYLIQRACSQVDELHIIMGFddtrdraLFEDSAMSQQPTVPDRLRWLLQTFKYQKN-IRIHAF 142
Cdd:TIGR01526 1 KTIGVVFGKFYPLHTGHIYLIYEAFSKVDELHIVVGS-------LFYDSKAKRPPPVQDRLRWLREIFKYQKNqIFIHHL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111746 143 NEEGMEPYPHGWDVWSNGIKKFMAEKGIQPDLIYTSEEADAPQYMEHLGIETVLVDPKRTFMSISGAQIRENPFRYWEYI 222
Cdd:TIGR01526 74 NEDGIPEYPNGWDSWSNALKTLFHEKHFEPDIVFSSEPQYAAPYEKYLGLEVVLVDPDRTFFSVSATQIRENPFQHWKHI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111746 223 PTEVKPFFVRTVAILGGESSGKSTLVNKLANIFNTTSAWEYGRDYVFSHLGGDEiALQYSDYDKIALGHAQYIDFAVKYA 302
Cdd:TIGR01526 154 PREVRPFFVKTVAILGGESTGKSTLVNKLAAVFNTTSAWEYAREYVEEKLGGDE-ALQYSDYAQIALGQQRYIDYAVRHA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111746 303 NKVAFIDTDFVTTQAFCKKYEGREHPFVQALIDEYRFDLVILLENNTPWVADGLRSLGSSVDRKEFQNLLVEMLEENNIE 382
Cdd:TIGR01526 233 HKIAFIDTDFITTQVFAKQYEGREHPFLDSDIAEYPFDLTLLLKPNTEWVDDGLRSLGSQKQRQEFQQLLKKLLDEYGVP 312
|
330
....*....|...
gi 90111746 383 FVRVEEEDYDSRF 395
Cdd:TIGR01526 313 FVVIESPDYLDRY 325
|
|
| NMNAT_NadR |
cd02167 |
Nicotinamide/nicotinate mononucleotide adenylyltransferase of bifunctional NadR-like proteins; ... |
66-227 |
1.27e-84 |
|
Nicotinamide/nicotinate mononucleotide adenylyltransferase of bifunctional NadR-like proteins; NMNAT domain of NadR protein. The NadR protein (NadR) is a bifunctional enzyme possessing both NMN adenylytransferase (NMNAT) and ribosylnicotinamide kinase (RNK) activities. Its function is essential for the growth and survival of H. influenzae and thus may present a new highly specific anti-infectious drug target. The N-terminal domain that hosts the NMNAT activity is closely related to archaeal NMNAT. The bound NAD at the active site of the NMNAT domain reveals several critical interactions between NAD and the protein.The NMNAT domain of hiNadR defines yet another member of the pyridine nucleotide adenylyltransferase
Pssm-ID: 173918 Cd Length: 158 Bit Score: 255.11 E-value: 1.27e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111746 66 IGVVFGKFYPLHTGHIYLIQRACSQVDELHIIMGFDDTRDRAlfedsamSQQPTVPDRLRWLLQTFKYQKNIRIHAFNEE 145
Cdd:cd02167 1 IGIVFGKFAPLHTGHVYLIYKALSQVDELLIIVGSDDTRDDA-------RTGLPLEKRLRWLREIFPDQENIVVHTLNEP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111746 146 GMEPYPHGWDVWSNGIKKFMAEKG-IQPDLIYTSEEADAPQY--MEHLGIETVLVDPKRTFMSISGAQIRENPFRYWEYI 222
Cdd:cd02167 74 DIPEYPNGWDIWSNRVKTLIAENTrCRPDIVFTAEEYEAAFElvLAYLGAQVVLVDPDRTDISVSATQIRENPFRYWYHI 153
|
....*
gi 90111746 223 PTEVK 227
Cdd:cd02167 154 PREVR 158
|
|
| NadR3 |
COG3172 |
Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase ... |
224-408 |
9.56e-76 |
|
Nicotinamide riboside kinase [Coenzyme transport and metabolism]; Nicotinamide riboside kinase is part of the Pathway/BioSystem: NAD biosynthesis
Pssm-ID: 442405 [Multi-domain] Cd Length: 178 Bit Score: 233.17 E-value: 9.56e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111746 224 TEVKPFFVRTVAILGGESSGKSTLVNKLANIFNTTSAWEYGRDYVFSHLGgdeiALQYSDYDKIALGHAQYIDFAVKYAN 303
Cdd:COG3172 1 PEVRPSFVKKIVLLGAESTGKTTLARALAAHYNTPWVPEYGREYLEEKGR----ALTYDDLLAIARGQLALEDAAAKRAN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111746 304 KVAFIDTDFVTTQAFCKKYEGREHPFVQALIDEYRFDLVILLENNTPWVADGLRSLGSsvDRKEFQNLLVEMLEENNIEF 383
Cdd:COG3172 77 KLLFCDTDALTTKVYSELYFGKCPPWLEALAAQRRYDLYLLLDPDIPWVADGLRDGPE--VREEFQQLLREELEERGIPY 154
|
170 180
....*....|....*....|....*
gi 90111746 384 VRVeEEDYDSRFLRCVELVREMMGE 408
Cdd:COG3172 155 VVI-SGDYEERLEQALAAIDELLAK 178
|
|
| NadR |
COG1056 |
Nicotinamide mononucleotide adenylyltransferase [Coenzyme transport and metabolism]; ... |
63-229 |
2.65e-37 |
|
Nicotinamide mononucleotide adenylyltransferase [Coenzyme transport and metabolism]; Nicotinamide mononucleotide adenylyltransferase is part of the Pathway/BioSystem: NAD biosynthesis
Pssm-ID: 440676 [Multi-domain] Cd Length: 162 Bit Score: 133.01 E-value: 2.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111746 63 KKTIGVVFGKFYPLHTGHIYLIQRACSQVDELHIIMGFDDTRDRalfedsaMSQQPTVPDRLRWLLQTFKYQ--KNIRIH 140
Cdd:COG1056 1 MMKRGLFIGRFQPFHLGHLAVIKWALEEVDELIIGIGSAQESHT-------PRNPFTAGERIEMIRAALKEEglSRVYIV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111746 141 AFNEEgmepypHGWDVWSNGIKKFMAEkgiqPDLIYTSEEaDAPQYMEHLGIEtVLVDPKRTFMSISGAQIRENPFRY-- 218
Cdd:COG1056 74 PIPDI------NNNSLWVSHVKSLVPP----FDVVYSNNP-LVGRLFKEAGYE-VLLPPLFEREEYSGTEIRRLMLEGed 141
|
170
....*....|..
gi 90111746 219 WEYI-PTEVKPF 229
Cdd:COG1056 142 WESLvPPAVAEV 153
|
|
| AAA_28 |
pfam13521 |
AAA domain; |
234-394 |
1.82e-36 |
|
AAA domain;
Pssm-ID: 433278 [Multi-domain] Cd Length: 164 Bit Score: 130.85 E-value: 1.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111746 234 VAILGGESSGKSTLVNKLANIFNTTSAWEYGRDYVFSHLGGDEIALQYSdYDKIALGH----AQYIDFAVKYANKVAFID 309
Cdd:pfam13521 2 IVITGGPSTGKTTLAEALAARFGYPVVPEAAREILEELGADGGDALPWV-EDLLAFARgvleAQLEDEAAAAANDLLFFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111746 310 TDFVTTQAFCKKYEGREHPFVQALIDEYRFDLVILLENNTPWVADGLRsLGSSVDRKEFQNLLVEMLEENNIEFVRVEEE 389
Cdd:pfam13521 81 RGPLDTLAYSRAYGGPCPPELEAAARASRYDLVFLLPPDPEIVQDGER-REDPEERERFHERLREALRELGIPVIIVPRG 159
|
....*
gi 90111746 390 DYDSR 394
Cdd:pfam13521 160 SVEER 164
|
|
| cyt_tran_rel |
TIGR00125 |
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ... |
66-136 |
2.81e-13 |
|
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown. Many of these proteins are known to use CTP or ATP and release pyrophosphate.
Pssm-ID: 272920 [Multi-domain] Cd Length: 66 Bit Score: 64.25 E-value: 2.81e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90111746 66 IGVVFGKFYPLHTGHIYLIQRACSQVDELHIIMGFDDtrdralfEDSAMSQQP-TVPDRLRWLLQTFKYQKN 136
Cdd:TIGR00125 1 RVIFVGTFDPFHLGHLDLLERAKELFDELIVGVGSDQ-------FVNPLKGEPvFSLEERLEMLKALKYVDE 65
|
|
| cytidylyltransferase_like |
cd02039 |
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ... |
66-213 |
8.20e-13 |
|
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are known to use CTP or ATP and release pyrophosphate. Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown.
Pssm-ID: 185678 [Multi-domain] Cd Length: 143 Bit Score: 65.54 E-value: 8.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111746 66 IGVVFGKFYPLHTGHIYLIQRACSQVDELHIIMGFDDTRDRALFEDSAmsqqpTVPDRLRWLLQTFKYQKNIRIHAFNEE 145
Cdd:cd02039 1 VGIIIGRFEPFHLGHLKLIKEALEEALDEVIIIIVSNPPKKKRNKDPF-----SLHERVEMLKEILKDRLKVVPVDFPEV 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90111746 146 gmepyphGWDVWSNGIKKFMaeKGIQPDLIYTSEEADAPQYMEH--------LGIETVLVDPKRTFMSISGAQIRE 213
Cdd:cd02039 76 -------KILLAVVFILKIL--LKVGPDKVVVGEDFAFGKNASYnkdlkelfLDIEIVEVPRVRDGKKISSTLIRE 142
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|
| HTH_XRE |
cd00093 |
Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the ... |
7-59 |
1.81e-07 |
|
Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the xenobiotic response element family of transcriptional regulators.
Pssm-ID: 238045 [Multi-domain] Cd Length: 58 Bit Score: 47.55 E-value: 1.81e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 90111746 7 LKTAIKQQGCTLQQVADASGMTKGYLSQLLNAKIkSPSAQKLEALHRFLGLEF 59
Cdd:cd00093 4 LKELRKEKGLTQEELAEKLGVSRSTISRIENGKR-NPSLETLEKLAKALGVSL 55
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| HTH_XRE |
smart00530 |
Helix-turn-helix XRE-family like proteins; |
7-58 |
2.04e-07 |
|
Helix-turn-helix XRE-family like proteins;
Pssm-ID: 197775 [Multi-domain] Cd Length: 56 Bit Score: 47.51 E-value: 2.04e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 90111746 7 LKTAIKQQGCTLQQVADASGMTKGYLSQLLNAKIKsPSAQKLEALHRFLGLE 58
Cdd:smart00530 2 LKELREEKGLTQEELAEKLGVSRSTLSRIENGKRK-PSLETLKKLAKALGVS 52
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|
| HTH_3 |
pfam01381 |
Helix-turn-helix; This large family of DNA binding helix-turn helix proteins includes Cro and ... |
7-59 |
7.51e-07 |
|
Helix-turn-helix; This large family of DNA binding helix-turn helix proteins includes Cro and CI. Within the protein Swiss:Q5F9C2, the full protein fold incorporates a helix-turn-helix motif, but the function of this member is unlikely to be that of a DNA-binding regulator, the function of most other members, so is not necessarily characteriztic of the whole family.
Pssm-ID: 460181 [Multi-domain] Cd Length: 55 Bit Score: 45.61 E-value: 7.51e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 90111746 7 LKTAIKQQGCTLQQVADASGMTKGYLSQLLNAKiKSPSAQKLEALHRFLGLEF 59
Cdd:pfam01381 1 LKELREELGLSQEELAEKLGVSRSTISKIENGK-REPSLETLKKLAEALGVSL 52
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|
| HipB |
COG1396 |
Transcriptional regulator, contains XRE-family HTH domain [Transcription]; |
7-57 |
1.37e-06 |
|
Transcriptional regulator, contains XRE-family HTH domain [Transcription];
Pssm-ID: 441006 [Multi-domain] Cd Length: 83 Bit Score: 45.76 E-value: 1.37e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 90111746 7 LKTAIKQQGCTLQQVADASGMTKGYLSQLLNAKiKSPSAQKLEALHRFLGL 57
Cdd:COG1396 12 LRELRKARGLTQEELAERLGVSRSTISRIERGR-RNPSLETLLKLAKALGV 61
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|
| HTH_31 |
pfam13560 |
Helix-turn-helix domain; This domain is a helix-turn-helix domain that probably binds to DNA. |
5-57 |
2.74e-05 |
|
Helix-turn-helix domain; This domain is a helix-turn-helix domain that probably binds to DNA.
Pssm-ID: 433309 [Multi-domain] Cd Length: 64 Bit Score: 41.74 E-value: 2.74e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 90111746 5 DYLKTAIKQQGCTLQQVADASGMTKGYLSQLLNAKIKSPSAQKLEALHRFLGL 57
Cdd:pfam13560 4 ARLRRLRERAGLSQEALARRLGVSRSTLSRLETGRRGRPSPAVVERLARALGV 56
|
|
| NMNAT_Archaea |
cd02166 |
Nicotinamide/nicotinate mononucleotide adenylyltransferase, archaeal; This family of archaeal ... |
67-99 |
1.72e-04 |
|
Nicotinamide/nicotinate mononucleotide adenylyltransferase, archaeal; This family of archaeal proteins exhibits nicotinamide-nucleotide adenylyltransferase (NMNAT) activity utilizing the salvage pathway to synthesize NAD. In some cases, the enzyme was tested and found also to have the activity of nicotinate-nucleotide adenylyltransferase an enzyme of NAD de novo biosynthesis, although with a higher Km. In some archaeal species, a number of proteins which are uncharacterized with respect to activity, are also present.
Pssm-ID: 173917 Cd Length: 163 Bit Score: 41.90 E-value: 1.72e-04
10 20 30
....*....|....*....|....*....|...
gi 90111746 67 GVVFGKFYPLHTGHIYLIQRACSQVDELHIIMG 99
Cdd:cd02166 2 ALFIGRFQPFHLGHLKVIKWILEEVDELIIGIG 34
|
|
| PRK01153 |
PRK01153 |
nicotinamide-nucleotide adenylyltransferase; Provisional |
67-99 |
2.09e-04 |
|
nicotinamide-nucleotide adenylyltransferase; Provisional
Pssm-ID: 179235 Cd Length: 174 Bit Score: 41.78 E-value: 2.09e-04
10 20 30
....*....|....*....|....*....|...
gi 90111746 67 GVVFGKFYPLHTGHIYLIQRACSQVDELHIIMG 99
Cdd:PRK01153 3 ALFIGRFQPFHKGHLEVIKWILEEVDELIIGIG 35
|
|
| PPAT |
cd02163 |
Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is ... |
66-143 |
5.07e-04 |
|
Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is an essential enzyme in bacteria, responsible for catalyzing the rate-limiting step in coenzyme A (CoA) biosynthesis. The dinucleotide-binding fold of PPAT is homologous to class I aminoacyl-tRNA synthetases. CoA has been shown to inhibit PPAT and competes with ATP, PhP, and dPCoA. PPAT is a homohexamer in E. coli.
Pssm-ID: 173914 [Multi-domain] Cd Length: 153 Bit Score: 40.14 E-value: 5.07e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90111746 66 IGVVFGKFYPLHTGHIYLIQRACSQVDELHIIMgFDDTRDRALFedsamsqqpTVPDRLRWLLQTFKYQKNIRIHAFN 143
Cdd:cd02163 1 IAVYPGSFDPITNGHLDIIERASKLFDEVIVAV-AVNPSKKPLF---------SLEERVELIREATKHLPNVEVDGFD 68
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