|
Name |
Accession |
Description |
Interval |
E-value |
| trkA |
PRK09496 |
Trk system potassium transporter TrkA; |
1-456 |
0e+00 |
|
Trk system potassium transporter TrkA;
Pssm-ID: 236541 [Multi-domain] Cd Length: 453 Bit Score: 730.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913485869 1 MKIIILGAGQVGGTLAENLVGENNDITIVDKNGDRLRELQDKYDLRVVNGHASHPDVLHEAGAQDADMLVAVTNTDETNM 80
Cdd:PRK09496 1 MKIIIVGAGQVGYTLAENLSGENNDVTVIDTDEERLRRLQDRLDVRTVVGNGSSPDVLREAGAEDADLLIAVTDSDETNM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913485869 81 AACQVAFTLFNTPNRVARIRSPEYLAEKEaLFKSGAIPVDHLIAPEELVTSYIERLIQYPGALQVVSFAEQKVSLVAVKA 160
Cdd:PRK09496 81 VACQIAKSLFGAPTTIARVRNPEYAEYDK-LFSKEALGIDLLISPELLVAREIARLIEYPGALDVEEFADGRVQLVEVKV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913485869 161 YYGGPLVGNALSALREHMPHIDTRVAAIFRQGRPIRPQGTTIIEADDEVFFVAASNHIRSVMSELQRLEKPYRRIMIVGG 240
Cdd:PRK09496 160 YEGSPLVGKPLSDLREHFPDIDVRVVAIFRGGRLIIPRGDTVIEAGDEVYFIGAREHIRAVMSEFGRLEKPVKRVMIVGG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913485869 241 GNIGASLAKRLEQT-YSVKLIERNYQRAEKLSEQLENTIVFCGDAADQELLTEENIDQVDVFIALTNEDETNIMSAMLAK 319
Cdd:PRK09496 240 GNIGYYLAKLLEKEgYSVKLIERDPERAEELAEELPNTLVLHGDGTDQELLEEEGIDEADAFIALTNDDEANILSSLLAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913485869 320 RMGAKKVMVLIQRGAYVDLVQGGVIDVAISPQQATISALLTHVRRADIVNVSSLRRGAAEAIEAVAHgdeTTSKVVGRAI 399
Cdd:PRK09496 320 RLGAKKVIALVNRPAYVDLVEGLGIDIAISPRQATASEILRHVRRGDIVAVHSLRRGAAEAIEAVAH---ETSKVVGKPL 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 913485869 400 GDIKLPPGTTIGAIVRGEEVLIAHDRTVIEQDDHVVMFLVDKKYVPDVEALFQPSPF 456
Cdd:PRK09496 397 KDLKLPKGVLIGAIVRGGEVIIPTGDTVIEPGDHVIVFVLDKKFVPDVEKLFQVSPF 453
|
|
| TrkA |
COG0569 |
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ... |
137-435 |
1.70e-72 |
|
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];
Pssm-ID: 440335 [Multi-domain] Cd Length: 296 Bit Score: 230.72 E-value: 1.70e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913485869 137 IQYPGALQVVSFAEQKVSLVAVKAYYGGPLVGNALSALREHMPHIDTRVAAIFRQGRPIRPQGTTIIEADDEVFFVAASN 216
Cdd:COG0569 1 LLILLLLLVLLFAMGIEGLVLLDALYGLLITLTTVTTLGGGLLDPVTLVAAIFLIGVVIIPLGYTLITFGDAVLFGGLLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913485869 217 HIRSVMSELQRLEKPyRRIMIVGGGNIGASLAKRLEQT-YSVKLIERNYQRAEKLSEqlENTIVFCGDAADQELLTEENI 295
Cdd:COG0569 81 ALRRRRMERGIKKLK-MHVIIIGAGRVGRSLARELEEEgHDVVVIDKDPERVERLAE--EDVLVIVGDATDEEVLEEAGI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913485869 296 DQVDVFIALTNEDETNIMSAMLAKRMGAKKVMVLIQRGAYVDLVQGGVIDVAISPQQATISALLTHVRRADIVNVSSLRR 375
Cdd:COG0569 158 EDADAVIAATGDDEANILACLLAKELGVPRIIARANDPEYADLLERLGADVVISPERLAARRIARLLLRPGVLDVLELAD 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 913485869 376 GAAEAIEAVAHGDettSKVVGRAIGDIKLPP--GTTIGAIVRGEEVLIAHDRTVIEQDDHVV 435
Cdd:COG0569 238 GDAEIVEVTVPEG---SPLVGKTLKELDLREryGVTVVAIKRGGEVIIPSGDTVLEAGDELI 296
|
|
| TrkA_N |
pfam02254 |
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include ... |
3-125 |
3.93e-26 |
|
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include potassium channels, phosphoesterases, and various other transporters. This domain binds to NAD.
Pssm-ID: 426679 [Multi-domain] Cd Length: 115 Bit Score: 102.22 E-value: 3.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913485869 3 IIILGAGQVGGTLAENLVgENNDITIVDKNGDRLRELQDKYdLRVVNGHASHPDVLHEAGAQDADMLVAVTNTDETNMAA 82
Cdd:pfam02254 1 IIIIGYGRVGRSLAEELS-EGGDVVVIDKDEERVEELREEG-VPVVVGDATDEEVLEEAGIEEADAVIAATGDDEANILI 78
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 913485869 83 CQVAFTLFNTPNRVARIRSPEYlaeKEALFKSGAipvDHLIAP 125
Cdd:pfam02254 79 VLLARELNPDKKIIARANDPEH---AELLRRLGA---DHVISP 115
|
|
| L-AlaDH |
cd05305 |
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ... |
2-72 |
3.23e-07 |
|
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyruvate to L-alanine via reductive amination. Like formate dehydrogenase and related enzymes, L-AlaDH is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. Ligand binding and active site residues are found in the cleft between the subdomains. L-AlaDH is typically hexameric and is critical in carbon and nitrogen metabolism in micro-organisms.
Pssm-ID: 240630 [Multi-domain] Cd Length: 359 Bit Score: 52.02 E-value: 3.23e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 913485869 2 KIIILGAGQVGGTLAENLVGENNDITIVDKNGDRLRELQDKYDLRVVNgHASHPDVLHEAgAQDADMLV-AV 72
Cdd:cd05305 170 KVVILGAGVVGENAARVALGLGAEVTVLDINLERLRYLDDIFGGRVTT-LYSNPANLEEA-LKEADLVIgAV 239
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
2-70 |
8.51e-03 |
|
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.
Pssm-ID: 214966 [Multi-domain] Cd Length: 149 Bit Score: 36.72 E-value: 8.51e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 913485869 2 KIIILGAGQVGGTLAENLVGENNDITIVDKNGDRLRELQDKYDLRVVnGHASHPDVLHEAgAQDADMLV 70
Cdd:smart01002 22 KVVVIGAGVVGLGAAATAKGLGAEVTVLDVRPARLRQLESLLGARFT-TLYSQAELLEEA-VKEADLVI 88
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| trkA |
PRK09496 |
Trk system potassium transporter TrkA; |
1-456 |
0e+00 |
|
Trk system potassium transporter TrkA;
Pssm-ID: 236541 [Multi-domain] Cd Length: 453 Bit Score: 730.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913485869 1 MKIIILGAGQVGGTLAENLVGENNDITIVDKNGDRLRELQDKYDLRVVNGHASHPDVLHEAGAQDADMLVAVTNTDETNM 80
Cdd:PRK09496 1 MKIIIVGAGQVGYTLAENLSGENNDVTVIDTDEERLRRLQDRLDVRTVVGNGSSPDVLREAGAEDADLLIAVTDSDETNM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913485869 81 AACQVAFTLFNTPNRVARIRSPEYLAEKEaLFKSGAIPVDHLIAPEELVTSYIERLIQYPGALQVVSFAEQKVSLVAVKA 160
Cdd:PRK09496 81 VACQIAKSLFGAPTTIARVRNPEYAEYDK-LFSKEALGIDLLISPELLVAREIARLIEYPGALDVEEFADGRVQLVEVKV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913485869 161 YYGGPLVGNALSALREHMPHIDTRVAAIFRQGRPIRPQGTTIIEADDEVFFVAASNHIRSVMSELQRLEKPYRRIMIVGG 240
Cdd:PRK09496 160 YEGSPLVGKPLSDLREHFPDIDVRVVAIFRGGRLIIPRGDTVIEAGDEVYFIGAREHIRAVMSEFGRLEKPVKRVMIVGG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913485869 241 GNIGASLAKRLEQT-YSVKLIERNYQRAEKLSEQLENTIVFCGDAADQELLTEENIDQVDVFIALTNEDETNIMSAMLAK 319
Cdd:PRK09496 240 GNIGYYLAKLLEKEgYSVKLIERDPERAEELAEELPNTLVLHGDGTDQELLEEEGIDEADAFIALTNDDEANILSSLLAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913485869 320 RMGAKKVMVLIQRGAYVDLVQGGVIDVAISPQQATISALLTHVRRADIVNVSSLRRGAAEAIEAVAHgdeTTSKVVGRAI 399
Cdd:PRK09496 320 RLGAKKVIALVNRPAYVDLVEGLGIDIAISPRQATASEILRHVRRGDIVAVHSLRRGAAEAIEAVAH---ETSKVVGKPL 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 913485869 400 GDIKLPPGTTIGAIVRGEEVLIAHDRTVIEQDDHVVMFLVDKKYVPDVEALFQPSPF 456
Cdd:PRK09496 397 KDLKLPKGVLIGAIVRGGEVIIPTGDTVIEPGDHVIVFVLDKKFVPDVEKLFQVSPF 453
|
|
| TrkA |
COG0569 |
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ... |
137-435 |
1.70e-72 |
|
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];
Pssm-ID: 440335 [Multi-domain] Cd Length: 296 Bit Score: 230.72 E-value: 1.70e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913485869 137 IQYPGALQVVSFAEQKVSLVAVKAYYGGPLVGNALSALREHMPHIDTRVAAIFRQGRPIRPQGTTIIEADDEVFFVAASN 216
Cdd:COG0569 1 LLILLLLLVLLFAMGIEGLVLLDALYGLLITLTTVTTLGGGLLDPVTLVAAIFLIGVVIIPLGYTLITFGDAVLFGGLLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913485869 217 HIRSVMSELQRLEKPyRRIMIVGGGNIGASLAKRLEQT-YSVKLIERNYQRAEKLSEqlENTIVFCGDAADQELLTEENI 295
Cdd:COG0569 81 ALRRRRMERGIKKLK-MHVIIIGAGRVGRSLARELEEEgHDVVVIDKDPERVERLAE--EDVLVIVGDATDEEVLEEAGI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913485869 296 DQVDVFIALTNEDETNIMSAMLAKRMGAKKVMVLIQRGAYVDLVQGGVIDVAISPQQATISALLTHVRRADIVNVSSLRR 375
Cdd:COG0569 158 EDADAVIAATGDDEANILACLLAKELGVPRIIARANDPEYADLLERLGADVVISPERLAARRIARLLLRPGVLDVLELAD 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 913485869 376 GAAEAIEAVAHGDettSKVVGRAIGDIKLPP--GTTIGAIVRGEEVLIAHDRTVIEQDDHVV 435
Cdd:COG0569 238 GDAEIVEVTVPEG---SPLVGKTLKELDLREryGVTVVAIKRGGEVIIPSGDTVLEAGDELI 296
|
|
| TrkA |
COG0569 |
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ... |
1-210 |
3.13e-55 |
|
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];
Pssm-ID: 440335 [Multi-domain] Cd Length: 296 Bit Score: 185.66 E-value: 3.13e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913485869 1 MKIIILGAGQVGGTLAENLVGENNDITIVDKNGDRLRELQDKyDLRVVNGHASHPDVLHEAGAQDADMLVAVTNTDETNM 80
Cdd:COG0569 96 MHVIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAEE-DVLVIVGDATDEEVLEEAGIEDADAVIAATGDDEANI 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913485869 81 AACQVAFTLfNTPNRVARIRSPEYLAEKEALfksgaiPVDHLIAPEELVTSYIERLIQYPGALQVVSFAEQKVSLVAVKA 160
Cdd:COG0569 175 LACLLAKEL-GVPRIIARANDPEYADLLERL------GADVVISPERLAARRIARLLLRPGVLDVLELADGDAEIVEVTV 247
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 913485869 161 YYGGPLVGNALSALREHMPHiDTRVAAIFRQGRPIRPQGTTIIEADDEVF 210
Cdd:COG0569 248 PEGSPLVGKTLKELDLRERY-GVTVVAIKRGGEVIIPSGDTVLEAGDELI 296
|
|
| TrkA_N |
pfam02254 |
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include ... |
3-125 |
3.93e-26 |
|
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include potassium channels, phosphoesterases, and various other transporters. This domain binds to NAD.
Pssm-ID: 426679 [Multi-domain] Cd Length: 115 Bit Score: 102.22 E-value: 3.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913485869 3 IIILGAGQVGGTLAENLVgENNDITIVDKNGDRLRELQDKYdLRVVNGHASHPDVLHEAGAQDADMLVAVTNTDETNMAA 82
Cdd:pfam02254 1 IIIIGYGRVGRSLAEELS-EGGDVVVIDKDEERVEELREEG-VPVVVGDATDEEVLEEAGIEEADAVIAATGDDEANILI 78
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 913485869 83 CQVAFTLFNTPNRVARIRSPEYlaeKEALFKSGAipvDHLIAP 125
Cdd:pfam02254 79 VLLARELNPDKKIIARANDPEH---AELLRRLGA---DHVISP 115
|
|
| TrkA_N |
pfam02254 |
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include ... |
235-350 |
3.72e-25 |
|
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include potassium channels, phosphoesterases, and various other transporters. This domain binds to NAD.
Pssm-ID: 426679 [Multi-domain] Cd Length: 115 Bit Score: 99.52 E-value: 3.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913485869 235 IMIVGGGNIGASLAKRLEQTYSVKLIERNYQRAEKLSEQLenTIVFCGDAADQELLTEENIDQVDVFIALTNEDETNIMS 314
Cdd:pfam02254 1 IIIIGYGRVGRSLAEELSEGGDVVVIDKDEERVEELREEG--VPVVVGDATDEEVLEEAGIEEADAVIAATGDDEANILI 78
|
90 100 110
....*....|....*....|....*....|....*..
gi 913485869 315 AMLAKRM-GAKKVMVLIQRGAYVDLVQGGVIDVAISP 350
Cdd:pfam02254 79 VLLARELnPDKKIIARANDPEHAELLRRLGADHVISP 115
|
|
| Kch |
COG1226 |
Voltage-gated potassium channel Kch [Inorganic ion transport and metabolism]; |
3-131 |
2.77e-12 |
|
Voltage-gated potassium channel Kch [Inorganic ion transport and metabolism];
Pssm-ID: 440839 [Multi-domain] Cd Length: 279 Bit Score: 67.06 E-value: 2.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913485869 3 IIILGAGQVGGTLAENLVGENNDITIVDKNGDRLRELQdKYDLRVVNGHASHPDVLHEAGAQDADMLVAVTNTDETNMAA 82
Cdd:COG1226 127 VIIAGFGRVGQIVARLLRAEGIPFVVIDLDPERVEELR-RFGIKVYYGDATRPDVLEAAGIERARALVVAIDDPEAALRI 205
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 913485869 83 CQVAFTLFNTPNRVARIRSPEylaEKEALFKSGAipvDHLIaPEELVTS 131
Cdd:COG1226 206 VELARELNPDLKIIARARDRE---HAEELRQAGA---DEVV-RETFESA 247
|
|
| NhaP2 |
COG3263 |
NhaP-type Na+/H+ and K+/H+ antiporter with C-terminal TrkAC and CorC domains [Energy ... |
392-455 |
7.43e-11 |
|
NhaP-type Na+/H+ and K+/H+ antiporter with C-terminal TrkAC and CorC domains [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 442494 [Multi-domain] Cd Length: 502 Bit Score: 63.98 E-value: 7.43e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 913485869 392 SKVVGRAIGDIKLPPGTTIGAIVRGEEVLIAHDRTVIEQDDHVVMfLVDKKYVPDVEALFQPSP 455
Cdd:COG3263 424 SPAVGKTLRELRLPEGALVVLIVRDGELLVPRGSTRLQAGDQLLV-LAPPEDLEALERLFAAVS 486
|
|
| PRK05326 |
PRK05326 |
potassium/proton antiporter; |
392-455 |
8.89e-09 |
|
potassium/proton antiporter;
Pssm-ID: 235410 [Multi-domain] Cd Length: 562 Bit Score: 57.52 E-value: 8.89e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 913485869 392 SKVVGRAIGDIKLPPGTTIGAIVRGEEVLIAHDRTVIEQDDHVVMfLVDKKYVPDVEALFQPSP 455
Cdd:PRK05326 425 SWLVGKALRDLRLPRGALIALIIRDGKLLVPTGSTRLKAGDVLLV-LGPERDLPALERLFSQSP 487
|
|
| TrkA_C |
pfam02080 |
TrkA-C domain; This domain is often found next to the pfam02254 domain. The exact function of ... |
155-225 |
8.96e-08 |
|
TrkA-C domain; This domain is often found next to the pfam02254 domain. The exact function of this domain is unknown. It has been suggested that it may bind an unidentified ligand. The domain is predicted to adopt an all beta structure.
Pssm-ID: 460440 [Multi-domain] Cd Length: 70 Bit Score: 49.14 E-value: 8.96e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 913485869 155 LVAVKAYYGGPLVGNALSALRehMPHI-DTRVAAIFRQGRPIRPQGTTIIEADDEVFFVAASNHIRSVMSEL 225
Cdd:pfam02080 1 LVEVTVPENSPLVGKTLKELN--LPERfGVRIVAIRRGGRLIIPSGDTVLEAGDRLLVIGTPDDLAALRELL 70
|
|
| L-AlaDH |
cd05305 |
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ... |
2-72 |
3.23e-07 |
|
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyruvate to L-alanine via reductive amination. Like formate dehydrogenase and related enzymes, L-AlaDH is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. Ligand binding and active site residues are found in the cleft between the subdomains. L-AlaDH is typically hexameric and is critical in carbon and nitrogen metabolism in micro-organisms.
Pssm-ID: 240630 [Multi-domain] Cd Length: 359 Bit Score: 52.02 E-value: 3.23e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 913485869 2 KIIILGAGQVGGTLAENLVGENNDITIVDKNGDRLRELQDKYDLRVVNgHASHPDVLHEAgAQDADMLV-AV 72
Cdd:cd05305 170 KVVILGAGVVGENAARVALGLGAEVTVLDINLERLRYLDDIFGGRVTT-LYSNPANLEEA-LKEADLVIgAV 239
|
|
| Ald |
COG0686 |
Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and ... |
2-72 |
5.98e-07 |
|
Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and metabolism]; Alanine dehydrogenase (includes sporulation protein SpoVN) is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440450 [Multi-domain] Cd Length: 372 Bit Score: 51.16 E-value: 5.98e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 913485869 2 KIIILGAGQVGGTLAENLVGENNDITIVDKNGDRLRELQDKYDLRvVNGHASHPDVLHEAgAQDADMLV-AV 72
Cdd:COG0686 170 KVVILGGGVVGTNAARMALGLGADVTVLDINLDRLRRLDDIFGGR-VTTLYSNPANIEEA-LKEADLVIgAV 239
|
|
| TrkA_C |
pfam02080 |
TrkA-C domain; This domain is often found next to the pfam02254 domain. The exact function of ... |
391-451 |
1.45e-06 |
|
TrkA-C domain; This domain is often found next to the pfam02254 domain. The exact function of this domain is unknown. It has been suggested that it may bind an unidentified ligand. The domain is predicted to adopt an all beta structure.
Pssm-ID: 460440 [Multi-domain] Cd Length: 70 Bit Score: 45.68 E-value: 1.45e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 913485869 391 TSKVVGRAIGDIKLP--PGTTIGAIVRGEEVLIAHDRTVIEQDDHVVmFLVDKKYVPDVEALF 451
Cdd:pfam02080 9 NSPLVGKTLKELNLPerFGVRIVAIRRGGRLIIPSGDTVLEAGDRLL-VIGTPDDLAALRELL 70
|
|
| PRK05326 |
PRK05326 |
potassium/proton antiporter; |
165-221 |
2.03e-06 |
|
potassium/proton antiporter;
Pssm-ID: 235410 [Multi-domain] Cd Length: 562 Bit Score: 50.20 E-value: 2.03e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 913485869 165 PLVGNALSALRehMPHiDTRVAAIFRQGRPIRPQGTTIIEADDEVFFVAASNHIRSV 221
Cdd:PRK05326 426 WLVGKALRDLR--LPR-GALIALIIRDGKLLVPTGSTRLKAGDVLLVLGPERDLPAL 479
|
|
| PRK06522 |
PRK06522 |
2-dehydropantoate 2-reductase; Reviewed |
1-65 |
1.18e-04 |
|
2-dehydropantoate 2-reductase; Reviewed
Pssm-ID: 235821 [Multi-domain] Cd Length: 304 Bit Score: 44.07 E-value: 1.18e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 913485869 1 MKIIILGAGQVGGTLAENLVGENNDITIVDKNGDRLRELQDKyDLRVVNGHAS----HPDVLHEAGAQD 65
Cdd:PRK06522 1 MKIAILGAGAIGGLFGAALAQAGHDVTLVARRGAHLDALNEN-GLRLEDGEITvpvlAADDPAELGPQD 68
|
|
| ProC |
COG0345 |
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ... |
1-72 |
3.07e-04 |
|
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis
Pssm-ID: 440114 [Multi-domain] Cd Length: 267 Bit Score: 42.36 E-value: 3.07e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 913485869 1 MKIIILGAGQVGGTLAENLVG---ENNDITIVDKNGDRLRELQDKYDLRVVNGHAshpdvlheAGAQDADMLV-AV 72
Cdd:COG0345 3 MKIGFIGAGNMGSAIIKGLLKsgvPPEDIIVSDRSPERLEALAERYGVRVTTDNA--------EAAAQADVVVlAV 70
|
|
| YbjL |
COG2985 |
Uncharacterized membrane protein YbjL, putative transporter [General function prediction only]; ... |
360-451 |
3.27e-04 |
|
Uncharacterized membrane protein YbjL, putative transporter [General function prediction only];
Pssm-ID: 442224 [Multi-domain] Cd Length: 543 Bit Score: 43.19 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913485869 360 THVRRADIVNVSslrrGAAEAIEAVAH--GDE------------------TTSKVVGRAIGDIKLPP--GTTIGAIVRGE 417
Cdd:COG2985 248 TVLQEGDIVLVV----GTREALEAAEAllGEEvddselldsdldvrrivvTNKEVAGKTLGELNLRNrfGVVITRVRRGG 323
|
90 100 110
....*....|....*....|....*....|....
gi 913485869 418 EVLIAHDRTVIEQDDhVVMFLVDKKYVPDVEALF 451
Cdd:COG2985 324 VELPATPDTVLQLGD-RLTVVGPKEDVERVAKLL 356
|
|
| AlaDh_PNT_C |
pfam01262 |
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ... |
2-70 |
9.02e-04 |
|
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine 2-oxoglutarate reductases.
Pssm-ID: 426165 [Multi-domain] Cd Length: 213 Bit Score: 40.56 E-value: 9.02e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 913485869 2 KIIILGAGQVGGTLAENLVGENNDITIVDKNGDRLRELQDKYDLRVVNGHASHPDVLHEAgAQDADMLV 70
Cdd:pfam01262 30 KVLVIGGGVAGLNAAATAKGLGAIVTILDVRPARLEQLESILGAKFVETLYSQAELIAEA-VKEADLVI 97
|
|
| NAD_bind_Leu_Phe_Val_DH |
cd01075 |
NAD(P) binding domain of leucine dehydrogenase, phenylalanine dehydrogenase, and valine ... |
1-70 |
9.97e-04 |
|
NAD(P) binding domain of leucine dehydrogenase, phenylalanine dehydrogenase, and valine dehydrogenase; Amino acid dehydrogenase (DH) is a widely distributed family of enzymes that catalyzes the oxidative deamination of an amino acid to its keto acid and ammonia with concomitant reduction of NADP+. For example, leucine DH catalyzes the reversible oxidative deamination of L-leucine and several other straight or branched chain amino acids to the corresponding 2-oxoacid derivative. Amino acid DH -like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.
Pssm-ID: 133444 Cd Length: 200 Bit Score: 40.27 E-value: 9.97e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913485869 1 MKIIILGAGQVGGTLAENLVGENNDITIVDKNGDRLRELQDKYDLRVVNghashPDVLHeagAQDADMLV 70
Cdd:cd01075 29 KTVAVQGLGKVGYKLAEHLLEEGAKLIVADINEEAVARAAELFGATVVA-----PEEIY---SVDADVFA 90
|
|
| NmrA |
pfam05368 |
NmrA-like family; NmrA is a negative transcriptional regulator involved in the ... |
235-324 |
1.32e-03 |
|
NmrA-like family; NmrA is a negative transcriptional regulator involved in the post-translational modification of the transcription factor AreA. NmrA is part of a system controlling nitrogen metabolite repression in fungi. This family only contains a few sequences as iteration results in significant matches to other Rossmann fold families.
Pssm-ID: 398829 [Multi-domain] Cd Length: 236 Bit Score: 40.40 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913485869 235 IMIVGG-GNIGASLAK-RLEQTYSVKLIERNYQ--RAEKLSEQlENTIVfCGDAADQELLtEENIDQVDVFIALTN---- 306
Cdd:pfam05368 1 ILVFGAtGQQGGSVVRaSLKAGHKVRALVRDPKseLAKSLKEA-GVELV-KGDLDDKESL-VEALKGVDVVFSVTGfwag 77
|
90 100
....*....|....*....|.
gi 913485869 307 ---EDETNIMSAmlAKRMGAK 324
Cdd:pfam05368 78 keiEDGKKLADA--AKEAGVK 96
|
|
| WcaG |
COG0451 |
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis]; |
2-70 |
1.33e-03 |
|
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440220 [Multi-domain] Cd Length: 295 Bit Score: 40.73 E-value: 1.33e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913485869 2 KIIILGA-GQVGGTLAENLVGENNDITIVDKNGDRLRELQDKYDLRVVNGHASHPDVLHEAgAQDADMLV 70
Cdd:COG0451 1 RILVTGGaGFIGSHLARRLLARGHEVVGLDRSPPGAANLAALPGVEFVRGDLRDPEALAAA-LAGVDAVV 69
|
|
| PRK03659 |
PRK03659 |
glutathione-regulated potassium-efflux system protein KefB; Provisional |
2-87 |
1.46e-03 |
|
glutathione-regulated potassium-efflux system protein KefB; Provisional
Pssm-ID: 179625 [Multi-domain] Cd Length: 601 Bit Score: 41.17 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913485869 2 KIIILGAGQVGGTLAENLVGENNDITIVDKNGDRLRELQdKYDLRVVNGHASHPDVLHEAGAQDADMLVAVTNTDETNMA 81
Cdd:PRK03659 402 QVIIVGFGRFGQVIGRLLMANKMRITVLERDISAVNLMR-KYGYKVYYGDATQLELLRAAGAEKAEAIVITCNEPEDTMK 480
|
....*....
gi 913485869 82 A---CQVAF 87
Cdd:PRK03659 481 IvelCQQHF 489
|
|
| PRK03562 |
PRK03562 |
glutathione-regulated potassium-efflux system protein KefC; Provisional |
3-100 |
7.18e-03 |
|
glutathione-regulated potassium-efflux system protein KefC; Provisional
Pssm-ID: 235131 [Multi-domain] Cd Length: 621 Bit Score: 38.82 E-value: 7.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913485869 3 IIILGAGQVGGTLAENLVGENNDITIVDKNGDRLRELQdKYDLRVVNGHASHPDVLHEAGAQDADMLVAVTNTDETNMAA 82
Cdd:PRK03562 403 VIIAGFGRFGQIVGRLLLSSGVKMTVLDHDPDHIETLR-KFGMKVFYGDATRMDLLESAGAAKAEVLINAIDDPQTSLQL 481
|
90
....*....|....*...
gi 913485869 83 CQVAFTLFNTPNRVARIR 100
Cdd:PRK03562 482 VELVKEHFPHLQIIARAR 499
|
|
| Kch |
COG1226 |
Voltage-gated potassium channel Kch [Inorganic ion transport and metabolism]; |
234-321 |
8.21e-03 |
|
Voltage-gated potassium channel Kch [Inorganic ion transport and metabolism];
Pssm-ID: 440839 [Multi-domain] Cd Length: 279 Bit Score: 38.17 E-value: 8.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913485869 234 RIMIVGGGNIGASLAKRLEQT-YSVKLIERNYQRAEKLSEQleNTIVFCGDAADQELLTEENIDQVDVFIALTNEDETNI 312
Cdd:COG1226 126 HVIIAGFGRVGQIVARLLRAEgIPFVVIDLDPERVEELRRF--GIKVYYGDATRPDVLEAAGIERARALVVAIDDPEAAL 203
|
....*....
gi 913485869 313 MSAMLAKRM 321
Cdd:COG1226 204 RIVELAREL 212
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
2-70 |
8.51e-03 |
|
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.
Pssm-ID: 214966 [Multi-domain] Cd Length: 149 Bit Score: 36.72 E-value: 8.51e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 913485869 2 KIIILGAGQVGGTLAENLVGENNDITIVDKNGDRLRELQDKYDLRVVnGHASHPDVLHEAgAQDADMLV 70
Cdd:smart01002 22 KVVVIGAGVVGLGAAATAKGLGAEVTVLDVRPARLRQLESLLGARFT-TLYSQAELLEEA-VKEADLVI 88
|
|
| PRK11880 |
PRK11880 |
pyrroline-5-carboxylate reductase; Reviewed |
1-72 |
9.05e-03 |
|
pyrroline-5-carboxylate reductase; Reviewed
Pssm-ID: 237008 [Multi-domain] Cd Length: 267 Bit Score: 37.82 E-value: 9.05e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 913485869 1 MKIIILGAGQVGGTLAENLVGEN---NDITIVDKNGDRLRELQDKYDLRVVNGHAshpdvlheAGAQDADMLV-AV 72
Cdd:PRK11880 3 KKIGFIGGGNMASAIIGGLLASGvpaKDIIVSDPSPEKRAALAEEYGVRAATDNQ--------EAAQEADVVVlAV 70
|
|
| |
