|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11557 |
PRK11557 |
MurR/RpiR family transcriptional regulator; |
5-282 |
0e+00 |
|
MurR/RpiR family transcriptional regulator;
Pssm-ID: 183195 [Multi-domain] Cd Length: 278 Bit Score: 527.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 5 IRIRQRYAGFAQSDKKLADYLLSQPDRARHLSSQQLAGEAGVSQSSVVKFAQKIGYKGFPALKLAISEALVSNPNPQSMP 84
Cdd:PRK11557 1 LRIRQRYPGLAQSDRKLADYLLLQPDTARHLSSQQLANEAGVSQSSVVKFAQKLGYKGFPALKLALSEALASQPEPPSVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 85 VHNQIRGDDPMRLVGEKLIKENVAAMHATLDVNTEEKLLESVAMLRDARRIVLTGIGASGLVARNFGWKLTKIGYNAIVE 164
Cdd:PRK11557 81 VHNQIRGDDPLRLVGEKLIKENTAAMRATLDVNSEEKLHECVTMLRSARRIILTGIGASGLVAQNFAWKLMKIGINAVAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 165 QDMHALLATVQAMDPDDLLLAISYSGERREINMATDEALRVGGKILAITGFSPNALQQRATRCLYTIAEEQATRSAAISS 244
Cdd:PRK11557 161 RDMHALLATVQALSPDDLLLAISYSGERRELNLAADEALRVGAKVLAITGFTPNALQQRASHCLYTIAEEQATRSAAISS 240
|
250 260 270
....*....|....*....|....*....|....*...
gi 489957395 245 TSAQMMLTDLLFMALVQQDLERAPERIRHSEELVKKLV 282
Cdd:PRK11557 241 THAQGMLTDLLFMALIQQDLERAPERIRHSEALVKKLV 278
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
1-281 |
1.26e-79 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 242.14 E-value: 1.26e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 1 MNCLIRIRQRYAGFAQSDKKLADYLLSQPDRARHLSSQQLAGEAGVSQSSVVKFAQKIGYKGFPALKLAISEALVSNPNP 80
Cdd:COG1737 5 MSLLERIRARYPSLSPSERRIADYILDNPEEVAFMSIAELAEAAGVSEATVVRFCRKLGFSGFPELKLALAQELAEGLSS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 81 QSMpvHNQIRGDDPMRLVGEKLIKENVAAMHATLDVNTEEKLLESVAMLRDARRIVLTGIGASGLVARNFGWKLTKIGYN 160
Cdd:COG1737 85 YER--LRRLSPDDSLEDILAKVLEAEIANLEETLELLDEEALERAVDLLAKARRIYIFGVGASAPVAEDLAYKLLRLGKN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 161 AI-VEQDMHALLATVQAMDPDDLLLAISYSGERREINMATDEALRVGGKILAITGFSPNALQQRATRCLYTIAEEQATRS 239
Cdd:COG1737 163 VVlLDGDGHLQAESAALLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSEEPTLRS 242
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 489957395 240 AAISSTSAQMMLTDLLFMALVQQDLERAPERIRHSEELVKKL 281
Cdd:COG1737 243 SAFSSRVAQLALIDALAAAVAQRDGDKARERLERTEALLSEL 284
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
120-258 |
4.72e-33 |
|
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many phosphosugar isomerases and phosphosugar binding proteins. In E. coli, rpiR negatively regulates the expression of rpiB gene. Both rpiB and rpiA are ribose phosphate isomerases that catalyze the reversible reactions of ribose 5-phosphate into ribulose 5-phosphate.
Pssm-ID: 240144 [Multi-domain] Cd Length: 139 Bit Score: 118.10 E-value: 4.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 120 EKLLESVAMLRDARRIVLTGIGASGLVARNFGWKLTKIGYNAIVEQDMHALLATVQAMDPDDLLLAISYSGERREINMAT 199
Cdd:cd05013 1 EALEKAVDLLAKARRIYIFGVGSSGLVAEYLAYKLLRLGKPVVLLSDPHLQLMSAANLTPGDVVIAISFSGETKETVEAA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 489957395 200 DEALRVGGKILAITGFSPNALQQRATRCLYTIAEEQATRSAAISSTSAQMMLTDLLFMA 258
Cdd:cd05013 81 EIAKERGAKVIAITDSANSPLAKLADIVLLVSSEEGDFRSSAFSSRIAQLALIDALFLA 139
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
128-258 |
2.87e-29 |
|
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars. Presumably the SIS domains bind to the end-product of the pathway.
Pssm-ID: 426230 [Multi-domain] Cd Length: 131 Bit Score: 107.77 E-value: 2.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 128 MLRDARRIVLTGIGASGLVARNFGWKLTKIGYNAIVEQDMHALLATVQAM-DPDDLLLAISYSGERREINMATDEALRVG 206
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALvDEDDLVIAISYSGETKDLLAAAELAKARG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 489957395 207 GKILAITGFSPNALQQRATRCLYTIAEEQaTRSAAISSTSAQMMLTDLLFMA 258
Cdd:pfam01380 81 AKIIAITDSPGSPLAREADHVLYINAGPE-TGVASTKSITAQLAALDALAVA 131
|
|
| G6PI_arch |
TIGR02128 |
bifunctional phosphoglucose/phosphomannose isomerase; This bifunctional isomerase is a member ... |
129-282 |
1.20e-05 |
|
bifunctional phosphoglucose/phosphomannose isomerase; This bifunctional isomerase is a member of the larger PGI superfamily and only distantly related to other glucose-6-phosphate isomerases. The family is limited to the archaea.
Pssm-ID: 273988 [Multi-domain] Cd Length: 308 Bit Score: 45.89 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 129 LRDARRIVLTGIGASGLVARNFG-WKLTKIGYNAIVEQDMHALLATVqamDPDDLLLAISYSGERREINMATDEALRVGG 207
Cdd:TIGR02128 18 LKIYDEIVICGMGGSGIAGRIISiLLLEKSFQGPVFVVKDYRLPRFV---DGKTLLIAVSYSGNTEETLSAVEEAKKKGA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 208 KILAITgfSPNALQQRATRC---LYTIAEEQATRSA------AISSTSAQMMLTDLLFMALVQQDLERAPErirhsEELV 278
Cdd:TIGR02128 95 KVIAIT--SGGRLEEMAKERgldVIKIPKGLQPRAAfpylltPLILMLIKPLGIDIEEAELLEGGLDTPKL-----KALA 167
|
....
gi 489957395 279 KKLV 282
Cdd:TIGR02128 168 KRLA 171
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11557 |
PRK11557 |
MurR/RpiR family transcriptional regulator; |
5-282 |
0e+00 |
|
MurR/RpiR family transcriptional regulator;
Pssm-ID: 183195 [Multi-domain] Cd Length: 278 Bit Score: 527.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 5 IRIRQRYAGFAQSDKKLADYLLSQPDRARHLSSQQLAGEAGVSQSSVVKFAQKIGYKGFPALKLAISEALVSNPNPQSMP 84
Cdd:PRK11557 1 LRIRQRYPGLAQSDRKLADYLLLQPDTARHLSSQQLANEAGVSQSSVVKFAQKLGYKGFPALKLALSEALASQPEPPSVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 85 VHNQIRGDDPMRLVGEKLIKENVAAMHATLDVNTEEKLLESVAMLRDARRIVLTGIGASGLVARNFGWKLTKIGYNAIVE 164
Cdd:PRK11557 81 VHNQIRGDDPLRLVGEKLIKENTAAMRATLDVNSEEKLHECVTMLRSARRIILTGIGASGLVAQNFAWKLMKIGINAVAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 165 QDMHALLATVQAMDPDDLLLAISYSGERREINMATDEALRVGGKILAITGFSPNALQQRATRCLYTIAEEQATRSAAISS 244
Cdd:PRK11557 161 RDMHALLATVQALSPDDLLLAISYSGERRELNLAADEALRVGAKVLAITGFTPNALQQRASHCLYTIAEEQATRSAAISS 240
|
250 260 270
....*....|....*....|....*....|....*...
gi 489957395 245 TSAQMMLTDLLFMALVQQDLERAPERIRHSEELVKKLV 282
Cdd:PRK11557 241 THAQGMLTDLLFMALIQQDLERAPERIRHSEALVKKLV 278
|
|
| RpiR |
COG1737 |
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains ... |
1-281 |
1.26e-79 |
|
DNA-binding transcriptional regulator, MurR/RpiR family, contains HTH and SIS domains [Transcription];
Pssm-ID: 441343 [Multi-domain] Cd Length: 286 Bit Score: 242.14 E-value: 1.26e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 1 MNCLIRIRQRYAGFAQSDKKLADYLLSQPDRARHLSSQQLAGEAGVSQSSVVKFAQKIGYKGFPALKLAISEALVSNPNP 80
Cdd:COG1737 5 MSLLERIRARYPSLSPSERRIADYILDNPEEVAFMSIAELAEAAGVSEATVVRFCRKLGFSGFPELKLALAQELAEGLSS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 81 QSMpvHNQIRGDDPMRLVGEKLIKENVAAMHATLDVNTEEKLLESVAMLRDARRIVLTGIGASGLVARNFGWKLTKIGYN 160
Cdd:COG1737 85 YER--LRRLSPDDSLEDILAKVLEAEIANLEETLELLDEEALERAVDLLAKARRIYIFGVGASAPVAEDLAYKLLRLGKN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 161 AI-VEQDMHALLATVQAMDPDDLLLAISYSGERREINMATDEALRVGGKILAITGFSPNALQQRATRCLYTIAEEQATRS 239
Cdd:COG1737 163 VVlLDGDGHLQAESAALLGPGDVVIAISFSGYTRETLEAARLAKERGAKVIAITDSPLSPLAKLADVVLYVPSEEPTLRS 242
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 489957395 240 AAISSTSAQMMLTDLLFMALVQQDLERAPERIRHSEELVKKL 281
Cdd:COG1737 243 SAFSSRVAQLALIDALAAAVAQRDGDKARERLERTEALLSEL 284
|
|
| PRK15482 |
PRK15482 |
HTH-type transcriptional regulator MurR; |
1-281 |
3.41e-57 |
|
HTH-type transcriptional regulator MurR;
Pssm-ID: 185379 [Multi-domain] Cd Length: 285 Bit Score: 184.90 E-value: 3.41e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 1 MNCLIRIRQRYAGFAQSDKKLADYLLSQPDRARHLSSQQLAGEAGVSQSSVVKFAQKIGYKGFPALKLA-ISEALVS--N 77
Cdd:PRK15482 1 MLYLTKIRNAESEFTENEQKIADFLRANVSELKSVSSRKMAKQLGISQSSIVKFAQKLGAQGFTELRMAlIGEYSASreK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 78 PNPQSMPVHNQIRGDDPMRLVGEKLIKENVAAMHATLDVNTEEKLLESVAMLRDARRIVLTGIGASGLVARNFGWKLTKI 157
Cdd:PRK15482 81 TNATALHLHSSITSDDSLEVIARKLNREKELALEQTCALFDYARLQKIIEVISKAPFIQITGLGGSALVGRDLSFKLMKI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 158 GYNAIVEQDMHALLATVQAMDPDDLLLAISYSGERREINMATDEALRVGGKILAITGFSPNALQQRATRCLYTIAEEQAT 237
Cdd:PRK15482 161 GYRVACEADTHVQATVSQALKKGDVQIAISYSGSKKEIVLCAEAARKQGATVIAITSLADSPLRRLAHFTLDTVSGETEW 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 489957395 238 RSAAISSTSAQMMLTDLLFMALVQQDLERAPERIRHSEELVKKL 281
Cdd:PRK15482 241 RSSSMSTRTAQNSVTDLLFVGLVQLNDVESLKMIQRSSELTQRL 284
|
|
| SIS_RpiR |
cd05013 |
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many ... |
120-258 |
4.72e-33 |
|
RpiR-like protein. RpiR contains a SIS (Sugar ISomerase) domain, which is found in many phosphosugar isomerases and phosphosugar binding proteins. In E. coli, rpiR negatively regulates the expression of rpiB gene. Both rpiB and rpiA are ribose phosphate isomerases that catalyze the reversible reactions of ribose 5-phosphate into ribulose 5-phosphate.
Pssm-ID: 240144 [Multi-domain] Cd Length: 139 Bit Score: 118.10 E-value: 4.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 120 EKLLESVAMLRDARRIVLTGIGASGLVARNFGWKLTKIGYNAIVEQDMHALLATVQAMDPDDLLLAISYSGERREINMAT 199
Cdd:cd05013 1 EALEKAVDLLAKARRIYIFGVGSSGLVAEYLAYKLLRLGKPVVLLSDPHLQLMSAANLTPGDVVIAISFSGETKETVEAA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 489957395 200 DEALRVGGKILAITGFSPNALQQRATRCLYTIAEEQATRSAAISSTSAQMMLTDLLFMA 258
Cdd:cd05013 81 EIAKERGAKVIAITDSANSPLAKLADIVLLVSSEEGDFRSSAFSSRIAQLALIDALFLA 139
|
|
| PRK11337 |
PRK11337 |
MurR/RpiR family transcriptional regulator; |
6-279 |
2.87e-32 |
|
MurR/RpiR family transcriptional regulator;
Pssm-ID: 183089 [Multi-domain] Cd Length: 292 Bit Score: 120.25 E-value: 2.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 6 RIRQRYAGFAQSDKKLADYLLSQPDRARHLSSQQLAGEAGVSQSSVVKFAQKIGYKGFPALKLAIseALVSNPNPQSMpv 85
Cdd:PRK11337 18 YIRMKQEGLTPLESRVVEWLLKPGDLSEATALKDIAEALAVSEAMIVKVAKKLGFSGFRNLRSAL--EDYFSQSEQVL-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 86 HNQIRGDDPMRLVGEKLIKENVAAMHATLDVNTEEKLLESVAMLRDARRIVLTGIGASGLVARNFGWKLTKIGYNAIVEQ 165
Cdd:PRK11337 94 HSELSFDDAPQDVVNKVFNTSLQAIEETQSILDVDEFHRAARFFYQARQRDLYGAGGSAAIARDVQHKFLRIGVRCQAYD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 166 DMHALLATVQAMDPDDLLLAISYSGERREINMATDEALRVGGKILAITGFSPNALQQRATRCLYTIAEEQATRSAAISST 245
Cdd:PRK11337 174 DAHIMLMSAALLQEGDVVLVVSHSGRTSDVIEAVELAKKNGAKIICITNSYHSPIAKLADYVICSTAQGSPLLGENAAAR 253
|
250 260 270
....*....|....*....|....*....|....
gi 489957395 246 SAQMMLTDLLFMALVQQDLERAPERIRHSEELVK 279
Cdd:PRK11337 254 IAQLNILDAFFVSVAQLNIEQAEINLQKTGAAVD 287
|
|
| SIS |
pfam01380 |
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
128-258 |
2.87e-29 |
|
SIS domain; SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars. Presumably the SIS domains bind to the end-product of the pathway.
Pssm-ID: 426230 [Multi-domain] Cd Length: 131 Bit Score: 107.77 E-value: 2.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 128 MLRDARRIVLTGIGASGLVARNFGWKLTKIGYNAIVEQDMHALLATVQAM-DPDDLLLAISYSGERREINMATDEALRVG 206
Cdd:pfam01380 1 LLAKAKRIFVIGRGTSYAIALELALKFEEIGYKVVEVELASELRHGVLALvDEDDLVIAISYSGETKDLLAAAELAKARG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 489957395 207 GKILAITGFSPNALQQRATRCLYTIAEEQaTRSAAISSTSAQMMLTDLLFMA 258
Cdd:pfam01380 81 AKIIAITDSPGSPLAREADHVLYINAGPE-TGVASTKSITAQLAALDALAVA 131
|
|
| PRK14101 |
PRK14101 |
bifunctional transcriptional regulator/glucokinase; |
6-279 |
1.60e-26 |
|
bifunctional transcriptional regulator/glucokinase;
Pssm-ID: 184507 [Multi-domain] Cd Length: 638 Bit Score: 108.46 E-value: 1.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 6 RIRQRYAGFAQSDKKLADYLLSQPDRARHLSSQQLAGEAGVSQSSVVKFAQKIGYKGFPALKLAISEALVSnpnpqSMPV 85
Cdd:PRK14101 346 RIRQMRDALTPAERRVADLALNHPRSIINDPIVDIARKADVSQPTVIRFCRSLGCQGLSDFKLKLATGLTG-----TIPM 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 86 -HNQIRGDDPMRLVGEKLIKENVAAMHATLDVNTEEKLLESVAMLRDARRIVLTGIGASGLVARNFGWKLTKIGYNAIVE 164
Cdd:PRK14101 421 sHSQVHLGDTATDFGAKVLDNTVSAILQLREHLNFEHVEQAIDILNNARRIEFYGLGNSNIVAQDAHYKFFRFGIPTIAY 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 165 QDMHALLATVQAMDPDDLLLAISYSGERREINMATDEALRVGGKILAITGfSPNALQQRATRCLYTIAEEQATRSAAISS 244
Cdd:PRK14101 501 GDLYMQAASAALLGKGDVIVAVSKSGRAPELLRVLDVAMQAGAKVIAITS-SNTPLAKRATVALETDHIEMRESQLSMIS 579
|
250 260 270
....*....|....*....|....*....|....*
gi 489957395 245 TSAQMMLTDLLFMALVqqdLERAPERIRHSEELVK 279
Cdd:PRK14101 580 RILHLVMIDILAVGVA---IRRAAPNAELAEAVAR 611
|
|
| HTH_6 |
pfam01418 |
Helix-turn-helix domain, rpiR family; This domain contains a helix-turn-helix motif. The best ... |
1-74 |
2.40e-26 |
|
Helix-turn-helix domain, rpiR family; This domain contains a helix-turn-helix motif. The best characterized member of this family is Swiss:P39266. RpiR is a regulator of the expression of rpiB gene.
Pssm-ID: 334531 [Multi-domain] Cd Length: 77 Bit Score: 98.56 E-value: 2.40e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489957395 1 MNCLIRIRQRYAGFAQSDKKLADYLLSQPDRARHLSSQQLAGEAGVSQSSVVKFAQKIGYKGFPALKLAISEAL 74
Cdd:pfam01418 1 MGLLEKIQSRYSKLTKSERKIADYILAHPDLAIHLSISAIAKAAGVSEATIVRFCQKLGFSGFPELKLALAGEL 74
|
|
| PRK11302 |
PRK11302 |
DNA-binding transcriptional regulator HexR; Provisional |
1-255 |
6.38e-20 |
|
DNA-binding transcriptional regulator HexR; Provisional
Pssm-ID: 183082 [Multi-domain] Cd Length: 284 Bit Score: 86.97 E-value: 6.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 1 MNCLIRIRQRYAGFAQSDKKLADYLLSQPDRARHLSSQQLAGEAGVSQSSVVKFAQKIGYKGFPALKLAISEALVSNPNp 80
Cdd:PRK11302 1 MNMLEKIQSRLEHLSKSERKVAEVILASPQTAIHSSIATLAKMANVSEPTVNRFCRSLDTKGFPDFKLHLAQSLANGTP- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 81 qsmPVHNQIRGDDPMRLVGEKLIKENVAAM---HATLDVNTEEKlleSVAMLRDARRIVLTGIGASGLVARN-----FGW 152
Cdd:PRK11302 80 ---YVNRNVEEDDSVEAYTGKIFESAMASLdhaRQSLDPSAINR---AVDLLTQAKKISFFGLGASAAVAHDaqnkfFRF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 153 KLTKIGYNAIVEQDMHALLATVqamdpDDLLLAISYSGERREINMATDEALRVGGKILAITgfSPNA-LQQRATRCLYTI 231
Cdd:PRK11302 154 NVPVVYFDDIVMQRMSCMNSSD-----GDVVVLISHTGRTKSLVELAQLARENGATVIAIT--SAGSpLAREATLALTLD 226
|
250 260
....*....|....*....|....
gi 489957395 232 AEEQATRSAAISSTSAQMMLTDLL 255
Cdd:PRK11302 227 VPEDTDIYMPMVSRIAQLTVIDVL 250
|
|
| SIS_PHI |
cd05005 |
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) ... |
110-262 |
1.82e-16 |
|
Hexulose-6-phosphate isomerase (PHI). PHI is a member of the SIS (Sugar ISomerase domain) superfamily. In the ribulose monophosphate pathway of formaldehyde fixation, hexulose-6-phosphate synthase catalyzes the condensation of ribulose-5-phosphate with formadelhyde to become hexulose-6-phosphate, which is then isomerized to fructose-6-phosphate by PHI.
Pssm-ID: 240138 [Multi-domain] Cd Length: 179 Bit Score: 75.30 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 110 MHATLDVNTEEKLLESVAMLRDARRIVLTGIGASGLVARNFGWKLTKIGYNAIVEQDMhallaTVQAMDPDDLLLAISYS 189
Cdd:cd05005 11 IENVADKIDEEELDKLISAILNAKRIFVYGAGRSGLVAKAFAMRLMHLGLNVYVVGET-----TTPAIGPGDLLIAISGS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 190 GERREINMATDEALRVGGKILAITGFSPNALQQRATRCLYTIAEEQATRSAAISSTS--------AQMMLTDLLFMALVQ 261
Cdd:cd05005 86 GETSSVVNAAEKAKKAGAKVVLITSNPDSPLAKLADVVVVIPAATKDDHGGEHKSIQplgtlfeqSALVFLDAVIAKLME 165
|
.
gi 489957395 262 Q 262
Cdd:cd05005 166 E 166
|
|
| SIS_Kpsf |
cd05014 |
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ... |
133-258 |
1.59e-12 |
|
KpsF-like protein. KpsF is an arabinose-5-phosphate isomerase which contains SIS (Sugar ISomerase) domains. SIS domains are found in many phosphosugar isomerases and phosphosugar binding proteins. KpsF catalyzes the reversible reaction of ribulose 5-phosphate to arabinose 5-phosphate. This is the second step in the CMP-Kdo biosynthesis pathway.
Pssm-ID: 240145 [Multi-domain] Cd Length: 128 Bit Score: 63.33 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 133 RRIVLTGIGASGLVARNFGWKLTKIGYNAIVeqdMHAllatVQAM-------DPDDLLLAISYSGERREINMATDEALRV 205
Cdd:cd05014 1 GKVVVTGVGKSGHIARKIAATLSSTGTPAFF---LHP----TEALhgdlgmvTPGDVVIAISNSGETDELLNLLPHLKRR 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 489957395 206 GGKILAITGFSPNALQQRATRCL-YTIAEEQATRS-AAISSTSAQMMLTDLLFMA 258
Cdd:cd05014 74 GAPIIAITGNPNSTLAKLSDVVLdLPVEEEACPLGlAPTTSTTAMLALGDALAVA 128
|
|
| GutQ |
COG0794 |
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall ... |
105-259 |
3.07e-11 |
|
D-arabinose 5-phosphate isomerase GutQ [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440557 [Multi-domain] Cd Length: 317 Bit Score: 62.69 E-value: 3.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 105 ENVAAMHATLDvnteEKLLESVAMLRDAR-RIVLTGIGASGLVARNFGWKLTKIGYNAIVeqdMHAL------LATVQam 177
Cdd:COG0794 20 EALAALAERLD----ESFEKAVELILNCKgRVVVTGMGKSGHIARKIAATLASTGTPAFF---LHPAeashgdLGMIT-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 178 dPDDLLLAISYSGERREINMATDEALRVGGKILAITGFSPNALQQRATRCLYTIAEEQATRS--AAISSTSAQMMLTDLL 255
Cdd:COG0794 91 -PGDVVIAISNSGETEELLALLPLLKRLGVPLIAITGNPDSTLARAADVVLDLPVEREACPLnlAPTTSTTATLALGDAL 169
|
....
gi 489957395 256 FMAL 259
Cdd:COG0794 170 AVAL 173
|
|
| PRK08674 |
PRK08674 |
bifunctional phosphoglucose/phosphomannose isomerase; Validated |
128-213 |
9.92e-08 |
|
bifunctional phosphoglucose/phosphomannose isomerase; Validated
Pssm-ID: 181536 [Multi-domain] Cd Length: 337 Bit Score: 52.29 E-value: 9.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 128 MLRDARRIVLTGIGASGLV---ARNFGWKLTKIGYnaIVEQDMHaLLATVqamDPDDLLLAISYSGERREINMATDEALR 204
Cdd:PRK08674 30 DLEKIDNIVISGMGGSGIGgdlLRILLFDELKVPV--FVNRDYT-LPAFV---DEKTLVIAVSYSGNTEETLSAVEQALK 103
|
....*....
gi 489957395 205 VGGKILAIT 213
Cdd:PRK08674 104 RGAKIIAIT 112
|
|
| SIS_PGI_PMI_1 |
cd05017 |
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the ... |
134-226 |
1.18e-07 |
|
The members of this protein family contain the SIS (Sugar ISomerase) domain and have both the phosphoglucose isomerase (PGI) and the phosphomannose isomerase (PMI) functions. These functions catalyze the reversible reactions of glucose 6-phosphate to fructose 6-phosphate, and mannose 6-phosphate to fructose 6-phosphate, respectively at an equal rate. This protein contains two SIS domains. This alignment is based on the first SIS domain.
Pssm-ID: 240148 [Multi-domain] Cd Length: 119 Bit Score: 49.19 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 134 RIVLTGIGASGLVARNF-GWKLTKIGYNAIVEQDMHaLLATVqamDPDDLLLAISYSGERREINMATDEALRVGGKILAI 212
Cdd:cd05017 1 NIVILGMGGSGIGGDLLeSLLLDEAKIPVYVVKDYT-LPAFV---DRKTLVIAVSYSGNTEETLSAVEQAKERGAKIVAI 76
|
90
....*....|....
gi 489957395 213 TgfSPNALQQRATR 226
Cdd:cd05017 77 T--SGGKLLEMARE 88
|
|
| SIS |
cd04795 |
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and ... |
135-213 |
2.63e-07 |
|
SIS domain. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars.
Pssm-ID: 240112 [Multi-domain] Cd Length: 87 Bit Score: 47.37 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 135 IVLTGIGASGLVARNFGWKLTKIGY-NAIVEQDMHALLA-TVQAMDPDDLLLAISYSGERREINMATDEALRVGGKILAI 212
Cdd:cd04795 1 IFVIGIGGSGAIAAYFALELLELTGiEVVALIATELEHAsLLSLLRKGDVVIALSYSGRTEELLAALEIAKELGIPVIAI 80
|
.
gi 489957395 213 T 213
Cdd:cd04795 81 T 81
|
|
| gutQ |
PRK11543 |
arabinose-5-phosphate isomerase GutQ; |
134-262 |
4.52e-07 |
|
arabinose-5-phosphate isomerase GutQ;
Pssm-ID: 183186 [Multi-domain] Cd Length: 321 Bit Score: 50.15 E-value: 4.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 134 RIVLTGIGASGLVARNFGWKLTKIGYNAIVEQDMHALLATVQAMDPDDLLLAISYSGERREINMATDEALRVGGKILAIT 213
Cdd:PRK11543 44 KVVVSGIGKSGHIGKKIAATLASTGTPAFFVHPAEALHGDLGMIESRDVMLFISYSGGAKELDLIIPRLEDKSIALLAMT 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 489957395 214 GFSPNALQQRATRCLYTIAEEQA--TRSAAISSTSAQMMLTDLLFMALVQQ 262
Cdd:PRK11543 124 GKPTSPLGLAAKAVLDISVEREAcpMHLAPTSSTVNTLMMGDALAMAVMQA 174
|
|
| AgaS |
COG2222 |
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain ... |
108-273 |
1.57e-06 |
|
Fructoselysine-6-P-deglycase FrlB or related protein, duplicated sugar isomerase (SIS) domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441824 [Multi-domain] Cd Length: 336 Bit Score: 48.74 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 108 AAMHATLDVNTE--EKLLESVAMLRDaRRIVLTGIGASGLVARnFGWKLTKIGYNAIVEqdmhALLATVQAMDP------ 179
Cdd:COG2222 9 EAWRRALAALAAaiAALLARLRAKPP-RRVVLVGAGSSDHAAQ-AAAYLLERLLGIPVA----ALAPSELVVYPaylkle 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 180 DDLLLAISYSGERREINMATDEALRVGGKILAITGFSPNALQQRATRCLYT-IAEEQ---ATRSaAISSTSAQMMLTDLL 255
Cdd:COG2222 83 GTLVVAISRSGNSPEVVAALELAKARGARTLAITNNPDSPLAEAADRVLPLpAGPEKsvaATKS-FTTMLLALLALLAAW 161
|
170
....*....|....*....
gi 489957395 256 FM-ALVQQDLERAPERIRH 273
Cdd:COG2222 162 GGdDALLAALDALPAALEA 180
|
|
| SIS_GlmS_GlmD_1 |
cd05008 |
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and ... |
134-259 |
2.95e-06 |
|
SIS (Sugar ISomerase) domain repeat 1 found in Glucosamine 6-phosphate synthase (GlmS) and Glucosamine-6-phosphate deaminase (GlmD). The SIS domain is found in many phosphosugar isomerases and phosphosugar binding proteins. GlmS contains a N-terminal glutaminase domain and two C-terminal SIS domains and catalyzes the first step in hexosamine metabolism, converting fructose 6-phosphate into glucosamine 6-phosphate using glutamine as nitrogen source. The glutaminase domain hydrolyzes glutamine to glutamate and ammonia. Ammonia is transferred through a channel to the isomerase domain for glucosamine 6-phosphate synthesis. The end product of the pathway is N-acetylglucosamine, which plays multiple roles in eukaryotic cells including being a building block of bacterial and fungal cell walls. In the absence of glutamine, GlmS catalyzes the isomerization of fructose 6-phosphate into glucose 6- phosphate (PGI-like activity). Glucosamine-6-phosphate deaminase (GlmD) contains two SIS domains and catalyzes the deamination and isomerization of glucosamine-6-phosphate into fructose-6-phosphate with the release of ammonia; in presence of high ammonia concentration, GlmD can catalyze the reverse reaction.
Pssm-ID: 240141 [Multi-domain] Cd Length: 126 Bit Score: 45.57 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 134 RIVLTGIGAS---GLVARNFGWKLTKIgynaiveqDMHALLATV-----QAMDPDDLLLAISYSGERREINMATDEALRV 205
Cdd:cd05008 1 RILIVGCGTSyhaALVAKYLLERLAGI--------PVEVEAASEfryrrPLLDEDTLVIAISQSGETADTLAALRLAKEK 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 489957395 206 GGKILAITGFSPNALQQRATRCLYTIA-EEQAtrSAAISSTSAQMMLtdLLFMAL 259
Cdd:cd05008 73 GAKTVAITNVVGSTLAREADYVLYLRAgPEIS--VAATKAFTSQLLA--LLLLAL 123
|
|
| G6PI_arch |
TIGR02128 |
bifunctional phosphoglucose/phosphomannose isomerase; This bifunctional isomerase is a member ... |
129-282 |
1.20e-05 |
|
bifunctional phosphoglucose/phosphomannose isomerase; This bifunctional isomerase is a member of the larger PGI superfamily and only distantly related to other glucose-6-phosphate isomerases. The family is limited to the archaea.
Pssm-ID: 273988 [Multi-domain] Cd Length: 308 Bit Score: 45.89 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 129 LRDARRIVLTGIGASGLVARNFG-WKLTKIGYNAIVEQDMHALLATVqamDPDDLLLAISYSGERREINMATDEALRVGG 207
Cdd:TIGR02128 18 LKIYDEIVICGMGGSGIAGRIISiLLLEKSFQGPVFVVKDYRLPRFV---DGKTLLIAVSYSGNTEETLSAVEEAKKKGA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 208 KILAITgfSPNALQQRATRC---LYTIAEEQATRSA------AISSTSAQMMLTDLLFMALVQQDLERAPErirhsEELV 278
Cdd:TIGR02128 95 KVIAIT--SGGRLEEMAKERgldVIKIPKGLQPRAAfpylltPLILMLIKPLGIDIEEAELLEGGLDTPKL-----KALA 167
|
....
gi 489957395 279 KKLV 282
Cdd:TIGR02128 168 KRLA 171
|
|
| PRK00331 |
PRK00331 |
isomerizing glutamine--fructose-6-phosphate transaminase; |
100-281 |
9.47e-04 |
|
isomerizing glutamine--fructose-6-phosphate transaminase;
Pssm-ID: 234729 [Multi-domain] Cd Length: 604 Bit Score: 40.41 E-value: 9.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 100 EKLIKENVAAMHATLD--VNTEEKLLESVAMLRDARRIVLTGIGAS---GLVARNFGWKLTKI----------GYNAIVe 164
Cdd:PRK00331 255 LKEIYEQPEAIRDTLEgrLDELGEGELADEDLKKIDRIYIVACGTSyhaGLVAKYLIESLAGIpveveiasefRYRDPV- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 165 qdmhallatvqaMDPDDLLLAISYSGErreiNMATDEALRV----GGKILAITgfspNALQQRATR----CLYTIA--Ee 234
Cdd:PRK00331 334 ------------LSPKTLVIAISQSGE----TADTLAALRLakelGAKTLAIC----NVPGSTIAResdaVLYTHAgpE- 392
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489957395 235 qatrsaaIS--ST---SAQMMLTDLLFMALVQ--------------QDLERAPERIRH---SEELVKKL 281
Cdd:PRK00331 393 -------IGvaSTkafTAQLAVLYLLALALAKargtlsaeeeadlvHELRELPALIEQvldLKEQIEEL 454
|
|
| GlmS |
COG0449 |
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ... |
122-282 |
2.82e-03 |
|
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase domains [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440218 [Multi-domain] Cd Length: 610 Bit Score: 38.84 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 122 LLESVAMLRDARRIVLTGIGAS---GLVARNFGWKLTKI----------GYNAIVeqdmhallatvqaMDPDDLLLAISY 188
Cdd:COG0449 284 LNLAAEDLRNIDRIYIVACGTSyhaGLVGKYLIEELARIpveveiasefRYRDPV-------------VDPGTLVIAISQ 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489957395 189 SGErreinmaT-D--EALRV----GGKILAITgfspNALQQRATR----CLYTIA--EeqatrsaaIS--ST---SAQMM 250
Cdd:COG0449 351 SGE-------TaDtlAALREakekGAKVLAIC----NVVGSTIAResdaVLYTHAgpE--------IGvaSTkafTTQLA 411
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489957395 251 LTDLLFMALVQ--------------QDLERAPERIRH---SEELVKKLV 282
Cdd:COG0449 412 ALYLLALYLARargtlsaeeeaellEELRKLPEKIEEvldLEEQIEELA 460
|
|
| SIS_GmhA |
cd05006 |
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose ... |
179-229 |
7.16e-03 |
|
Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose isomerase catalyzes the isomerization of sedoheptulose 7-phosphate into D-glycero-D-mannoheptose 7-phosphate. This is the first step of the biosynthesis of gram-negative bacteria inner core lipopolysaccharide precursor, L-glycero-D-mannoheptose (Gmh).
Pssm-ID: 240139 [Multi-domain] Cd Length: 177 Bit Score: 36.72 E-value: 7.16e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 489957395 179 PDDLLLAISYSGERREINMATDEALRVGGKILAITGFSPNALQQRATRCLY 229
Cdd:cd05006 101 PGDVLIGISTSGNSPNVLKALEAAKERGMKTIALTGRDGGKLLELADIEIH 151
|
|
| |
