|
Name |
Accession |
Description |
Interval |
E-value |
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
1-374 |
5.07e-113 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 335.96 E-value: 5.07e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 1 MHPIVIIGSGMAGYTLAREFRKLNPEQELVMICADDAVNYAKPTLSNAFAGKKAPEQIPLGDAAkMSAQLNMRIEPFTWV 80
Cdd:COG1251 1 KMRIVIIGAGMAGVRAAEELRKLDPDGEITVIGAEPHPPYNRPPLSKVLAGETDEEDLLLRPAD-FYEENGIDLRLGTRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 81 KEILAERHELVLEKDGVIsqqPYSKLILAVGANPIRLAIAGDGSDDIHVVNSLIDYRSFRENLAQRKdkRVVILGAGLIG 160
Cdd:COG1251 80 TAIDRAARTVTLADGETL---PYDKLVLATGSRPRVPPIPGADLPGVFTLRTLDDADALRAALAPGK--RVVVIGGGLIG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 161 CEFANDLLHSEYDVTVIDLAPQPLGRLLPSHIASAFQQNLEEAGVKFALGTTVEKVSKINNGEdyAVTLANGQTLVADIV 240
Cdd:COG1251 155 LEAAAALRKRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVT--GVRLADGEELPADLV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 241 LSAIGLQPNISLAQSANIQTSRGVITNSLLETNQADIYAIGDCAEVNG-----TLLPYVMPIMQQARALAKTLSGQQTNV 315
Cdd:COG1251 233 VVAIGVRPNTELARAAGLAVDRGIVVDDYLRTSDPDIYAAGDCAEHPGpvygrRVLELVAPAYEQARVAAANLAGGPAAY 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 446475553 316 HYPAMPVAVKTPAAPLTVLPAPVDVDVNWETEEFDDGMLAKAIDNEGTLRGFVLLGATA 374
Cdd:COG1251 313 EGSVPSTKLKVFGVDVASAGDAEGDEEVVVRGDPARGVYKKLVLRDGRLVGAVLVGDTS 371
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
1-368 |
9.29e-110 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 326.49 E-value: 9.29e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 1 MHPIVIIGSGMAGYTLAREFRKLNPEQELVMICADDAVNYAKPTLSNAFAGKKAPEQIPLGDAAKMSAQLNMRIEPFTWV 80
Cdd:PRK04965 2 SNGIVIIGSGFAARQLVKNIRKQDAHIPITLITADSGDEYNKPDLSHVFSQGQRADDLTRQSAGEFAEQFNLRLFPHTWV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 81 KEILAERHeLVLEKDGVIsqqPYSKLILAVGANPIRLAIAGDGSddIHVVNSLIDYRSFRENLAQRKdkRVVILGAGLIG 160
Cdd:PRK04965 82 TDIDAEAQ-VVKSQGNQW---QYDKLVLATGASAFVPPIPGREL--MLTLNSQQEYRAAETQLRDAQ--RVLVVGGGLIG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 161 CEFANDLLHSEYDVTVIDLAPQPLGRLLPSHIASAFQQNLEEAGVKFALGTTVEKVSKINNGedYAVTLANGQTLVADIV 240
Cdd:PRK04965 154 TELAMDLCRAGKAVTLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSG--IRATLDSGRSIEVDAV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 241 LSAIGLQPNISLAQSANIQTSRGVITNSLLETNQADIYAIGDCAEVNGTLLPYVMPIMQQARALAKTLSGQQTNVHYPAM 320
Cdd:PRK04965 232 IAAAGLRPNTALARRAGLAVNRGIVVDSYLQTSAPDIYALGDCAEINGQVLPFLQPIQLSAMALAKNLLGQNTPLKLPAM 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 446475553 321 PVAVKTPAAPLTVLPAPVDVDVNWETEEFDDGMLAKAIDNEGTLRGFV 368
Cdd:PRK04965 312 LVKVKTPELPLQLAGETQRQDLRWQINAESQGMVAKGVDEAGQLRAFV 359
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
22-313 |
4.62e-59 |
|
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];
Pssm-ID: 440215 [Multi-domain] Cd Length: 322 Bit Score: 194.64 E-value: 4.62e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 22 KLNPEQELVMICADDAVNYAKPTLSNAFAG-KKAPEQIPLGDAAKMsAQLNMRIEPFTWVKEILAERHELVLEKDGVISq 100
Cdd:COG0446 1 RLGPDAEITVIEKGPHHSYQPCGLPYYVGGgIKDPEDLLVRTPESF-ERKGIDVRTGTEVTAIDPEAKTVTLRDGETLS- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 101 qpYSKLILAVGANPIRLAIAGDGSDDIHVVNSLIDYRSFRENLAQRKDKRVVILGAGLIGCEFANDLLHSEYDVTVIDLA 180
Cdd:COG0446 79 --YDKLVLATGARPRPPPIPGLDLPGVFTLRTLDDADALREALKEFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 181 PQPLGRLLPsHIASAFQQNLEEAGVKFALGTTVEkvsKINNGEDYAVTLANGQTLVADIVLSAIGLQPNISLAQSANIQT 260
Cdd:COG0446 157 PRLLGVLDP-EMAALLEEELREHGVELRLGETVV---AIDGDDKVAVTLTDGEEIPADLVVVAPGVRPNTELAKDAGLAL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446475553 261 --SRGVITNSLLETNQADIYAIGDCAEVNG------TLLPYVMPIMQQARALAKTLSGQQT 313
Cdd:COG0446 233 geRGWIKVDETLQTSDPDVYAAGDCAEVPHpvtgktVYIPLASAANKQGRVAAENILGGPA 293
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
4-379 |
7.78e-49 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 176.56 E-value: 7.78e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 4 IVIIGSGMAGYTLAREFRKLNPEQ-ELVMICADDAVNYAKPTLSNAFAGKKAPEQIPLGDAAKMSAQlnmRIEPFTWVKE 82
Cdd:TIGR02374 1 LVLVGNGMAGHRCIEEVLKLNRHMfEITIFGEEPHPNYNRILLSSVLQGEADLDDITLNSKDWYEKH---GITLYTGETV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 83 ILAERHELVLEKDGViSQQPYSKLILAVGANPIRLAIAGDGSDDIHVVNSLIDYRSFReNLAQRKDKRVVIlGAGLIGCE 162
Cdd:TIGR02374 78 IQIDTDQKQVITDAG-RTLSYDKLILATGSYPFILPIPGADKKGVYVFRTIEDLDAIM-AMAQRFKKAAVI-GGGLLGLE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 163 FANDLLHSEYDVTVIDLAPQPLGRLLPSHIASAFQQNLEEAGVKFALGTTVEKVSKINNGEdyAVTLANGQTLVADIVLS 242
Cdd:TIGR02374 155 AAVGLQNLGMDVSVIHHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLEKDTVEIVGATKAD--RIRFKDGSSLEADLIVM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 243 AIGLQPNISLAQSANIQTSRGVITNSLLETNQADIYAIGDCAEVNGTLLPYVMPIMQQARALAKTLSGQQTNvhypAMPV 322
Cdd:TIGR02374 233 AAGIRPNDELAVSAGIKVNRGIIVNDSMQTSDPDIYAVGECAEHNGRVYGLVAPLYEQAKVLADHICGVECE----EYEG 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446475553 323 AVktPAAPLTVLpaPVDV----DVNwETEE------FD--DGMLAKAIDNEGTLRGFVLLGATAGKQRL 379
Cdd:TIGR02374 309 SD--LSAKLKLL--GVDVwsagDAQ-ETERttsikiYDeqKGIYKKLVLSDDKLLGAVLFGDTSDYGRL 372
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
2-283 |
3.52e-45 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 400379 [Multi-domain] Cd Length: 301 Bit Score: 157.87 E-value: 3.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 2 HPIVIIGSGMAGYTLAREFRKLNPEqeLVMICADDAVNYAKPTLSNAFAGKKAPEQIPLGDA---AKMSAQLNMRIEPFT 78
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGK--VTLIEDEGTCPYGGCVLSKALLGAAEAPEIASLWAdlyKRKEEVVKKLNNGIE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 79 W-----VKEILAERHELVLEK--DGVISQQPYSKLILAVGANPIRLAIAGDGSDDIHVVNSLIDYRSFRENLaqrKDKRV 151
Cdd:pfam07992 79 VllgteVVSIDPGAKKVVLEElvDGDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKL---LPKRV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 152 VILGAGLIGCEFANDLLHSEYDVTVIDLAPQpLGRLLPSHIASAFQQNLEEAGVKFALGTTVEKVskINNGEDYAVTLAN 231
Cdd:pfam07992 156 VVVGGGYIGVELAAALAKLGKEVTLIEALDR-LLRAFDEEISAALEKALEKNGVEVRLGTSVKEI--IGDGDGVEVILKD 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 446475553 232 GQTLVADIVLSAIGLQPNISLAQSANIQTSR--GVITNSLLETNQADIYAIGDC 283
Cdd:pfam07992 233 GTEIDADLVVVAIGRRPNTELLEAAGLELDErgGIVVDEYLRTSVPGIYAAGDC 286
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
4-290 |
4.69e-35 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 133.13 E-value: 4.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 4 IVIIGSGMAGYTLAREFRKLNPEQELVMICADDAVNYAKPTLSNAFAGKKAPE-QIPLGDAAKMSAQLNMRIEpfTWVKE 82
Cdd:PRK09754 6 IIIVGGGQAAAMAAASLRQQGFTGELHLFSDERHLPYERPPLSKSMLLEDSPQlQQVLPANWWQENNVHLHSG--VTIKT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 83 ILAERHELVLEKDGVISqqpYSKLILAVGANPIRLAIAGDGSDDIHVVNSLIDYRSFREnlAQRKDKRVVILGAGLIGCE 162
Cdd:PRK09754 84 LGRDTRELVLTNGESWH---WDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLRE--VLQPERSVVIVGAGTIGLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 163 FANDLLHSEYDVTVIDLAPQPLGRLLPSHIASAFQQNLEEAGVKFALGTTVEKVSKinnGEDYAVTLANGQTLVADIVLS 242
Cdd:PRK09754 159 LAASATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVD---GEKVELTLQSGETLQADVVIY 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 446475553 243 AIGLQPNISLAQSANIQTSRGVITNSLLETNQADIYAIGDCA---EVNGTL 290
Cdd:PRK09754 236 GIGISANDQLAREANLDTANGIVIDEACRTCDPAIFAGGDVAitrLDNGAL 286
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
1-308 |
5.49e-30 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 119.08 E-value: 5.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 1 MHPIVIIGSGMAGYTLAREFRK-LNPEQELVMIcadDAVNYA--KPTLSNAFAGKKAPEQI--PLGDAAKmSAQLNMRIE 75
Cdd:COG1252 1 MKRIVIVGGGFAGLEAARRLRKkLGGDAEVTLI---DPNPYHlfQPLLPEVAAGTLSPDDIaiPLRELLR-RAGVRFIQG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 76 PftwVKEILAERHELVLEKDGVIsqqPYSKLILAVGANPIRLAIAGDGSDDIHV--VNSLIDYR----SFRENLAQRKDK 149
Cdd:COG1252 77 E---VTGIDPEARTVTLADGRTL---SYDYLVIATGSVTNFFGIPGLAEHALPLktLEDALALRerllAAFERAERRRLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 150 RVVILGAGLIGCEFA---NDLLH----------SEYDVTVIDLAPQPLGRlLPSHIASAFQQNLEEAGVKFALGTTVEKV 216
Cdd:COG1252 151 TIVVVGGGPTGVELAgelAELLRkllrypgidpDKVRITLVEAGPRILPG-LGEKLSEAAEKELEKRGVEVHTGTRVTEV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 217 skinngEDYAVTLANGQTLVADIVLSAIGLQPNiSLAQSANIQTSRG--VITNSLLET-NQADIYAIGDCAEV---NGTL 290
Cdd:COG1252 230 ------DADGVTLEDGEEIPADTVIWAAGVKAP-PLLADLGLPTDRRgrVLVDPTLQVpGHPNVFAIGDCAAVpdpDGKP 302
|
330
....*....|....*....
gi 446475553 291 LPYV-MPIMQQARALAKTL 308
Cdd:COG1252 303 VPKTaQAAVQQAKVLAKNI 321
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
105-324 |
4.67e-29 |
|
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation
Pssm-ID: 440861 [Multi-domain] Cd Length: 456 Bit Score: 117.49 E-value: 4.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 105 KLILAVGANPIRLAIagDGSDDIHVVNSlidyrsfRENLAQRKD-KRVVILGAGLIGCEFANdLLH---SEydVTVIDLA 180
Cdd:COG1249 133 HIVIATGSRPRVPPI--PGLDEVRVLTS-------DEALELEELpKSLVVIGGGYIGLEFAQ-IFArlgSE--VTLVERG 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 181 PQPLGRLLPShIASAFQQNLEEAGVKFALGTTVEKVSKINNGedYAVTLANG---QTLVADIVLSAIGLQPNISL--AQS 255
Cdd:COG1249 201 DRLLPGEDPE-ISEALEKALEKEGIDILTGAKVTSVEKTGDG--VTVTLEDGggeEAVEADKVLVATGRRPNTDGlgLEA 277
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446475553 256 ANIQTSR--GVITNSLLETNQADIYAIGDCaeVNGTLLPYVMpiMQQARALAKTLSGQQ-TNVHYPAMPVAV 324
Cdd:COG1249 278 AGVELDErgGIKVDEYLRTSVPGIYAIGDV--TGGPQLAHVA--SAEGRVAAENILGKKpRPVDYRAIPSVV 345
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
4-287 |
1.91e-25 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 107.05 E-value: 1.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 4 IVIIGSGMAGYTLAREFRKLNPEQELVMICADDAVNYAKPTLSnAFAGK----------KAPEQiplgdAAKmsAQLNMR 73
Cdd:PRK09564 3 IIIIGGTAAGMSAAAKAKRLNKELEITVYEKTDIVSFGACGLP-YFVGGffddpntmiaRTPEE-----FIK--SGIDVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 74 IEpfTWVKEILAERHELVLE--KDGVISQQPYSKLILAVGANPIRLAIAGDGSDDIHVVNSLIDYRSFRENLAQRKDKRV 151
Cdd:PRK09564 75 TE--HEVVKVDAKNKTITVKnlKTGSIFNDTYDKLMIATGARPIIPPIKNINLENVYTLKSMEDGLALKELLKDEEIKNI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 152 VILGAGLIGCEFANDLLHSEYDVTVIDLAPQPLGRLLPSHIASAFQQNLEEAGVKFALGTTVEkvSKINNGEDYAVTLAN 231
Cdd:PRK09564 153 VIIGAGFIGLEAVEAAKHLGKNVRIIQLEDRILPDSFDKEITDVMEEELRENGVELHLNEFVK--SLIGEDKVEGVVTDK 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 446475553 232 GqTLVADIVLSAIGLQPNISLAQSANIQTSR--GVITNSLLETNQADIYAIGDCAEVN 287
Cdd:PRK09564 231 G-EYEADVVIVATGVKPNTEFLEDTGLKTLKngAIIVDEYGETSIENIYAAGDCATIY 287
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
88-326 |
1.38e-24 |
|
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide.
Pssm-ID: 273568 [Multi-domain] Cd Length: 460 Bit Score: 104.65 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 88 HELVLEKDGVISQQPYSKLILAVGANPIRLAIAGDGSDDIhVVNSlidyrsfRENLA-QRKDKRVVILGAGLIGCEFAND 166
Cdd:TIGR01350 117 GTVSVTGENGEETLEAKNIIIATGSRPRSLPGPFDFDGKV-VITS-------TGALNlEEVPESLVIIGGGVIGIEFASI 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 167 LLHSEYDVTVIDLAPqplgRLLP---SHIASAFQQNLEEAGVKFALGTTVEKVSKINNGEDYAVTLANGQTLVADIVLSA 243
Cdd:TIGR01350 189 FASLGSKVTVIEMLD----RILPgedAEVSKVLQKALKKKGVKILTNTKVTAVEKNDDQVTYENKGGETETLTGEKVLVA 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 244 IGLQPNIS---LAQSANIQTSRGVI-TNSLLETNQADIYAIGDCAEvnGTLLPYVMpiMQQARALAKTLSGQQTN-VHYP 318
Cdd:TIGR01350 265 VGRKPNTEglgLEKLGVELDERGRIvVDEYMRTNVPGIYAIGDVIG--GPMLAHVA--SHEGIVAAENIAGKEPAhIDYD 340
|
....*...
gi 446475553 319 AMPVAVKT 326
Cdd:TIGR01350 341 AVPSVIYT 348
|
|
| Rbx_binding |
pfam18113 |
Rubredoxin binding C-terminal domain; This is the C-terminal domain found in rubredoxin ... |
315-383 |
3.22e-23 |
|
Rubredoxin binding C-terminal domain; This is the C-terminal domain found in rubredoxin reductase (RdxR) present in Pseudomonas aeruginosa. RdxR are important in prokaryotes as they allow for the metabolism of inert n-alkanes and RdxR is also crucial for archaea and anaerobic bacteria in the response to oxidative stress. This domain is known to recognize and bind to rubredoxin.
Pssm-ID: 436282 Cd Length: 71 Bit Score: 91.92 E-value: 3.22e-23
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446475553 315 VHYPAMPVAVKTPAAPLTVLPAPVDVDVNWETEEFDDGMLAKAIDNEGTLRGFVLLGATAgKQRLTLTK 383
Cdd:pfam18113 2 VVYPAMPVIVKTPACPLVVAPPAVGAEGEWQIEGDGEGLTARFYDADGQLLGFALTGEAV-AQRMALLK 69
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
4-313 |
4.53e-22 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 98.27 E-value: 4.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 4 IVIIGSGMAGYTLAREF-RKLNPEQ-ELVMICADDAVNYAKPTLSNAFAGKKAPEqiplgdaakmsaqlnmriepFTWVK 81
Cdd:PRK14989 6 LAIIGNGMVGHRFIEDLlDKADAANfDITVFCEEPRIAYDRVHLSSYFSHHTAEE--------------------LSLVR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 82 EILAERHE---LVLEKDGVISQQ------------PYSKLILAVGANPIRLAIAGDGSDDIHVVNSLIDYRSFREnlAQR 146
Cdd:PRK14989 66 EGFYEKHGikvLVGERAITINRQekvihssagrtvFYDKLIMATGSYPWIPPIKGSETQDCFVYRTIEDLNAIEA--CAR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 147 KDKRVVILGAGLIGCEFANDLLHSEYDVTVIDLAPQPLGRLLPSHIASAFQQNLEEAGVKFALGTTVEKVskINNGEDYA 226
Cdd:PRK14989 144 RSKRGAVVGGGLLGLEAAGALKNLGVETHVIEFAPMLMAEQLDQMGGEQLRRKIESMGVRVHTSKNTLEI--VQEGVEAR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 227 VTL--ANGQTLVADIVLSAIGLQPNISLAQSANIQTSR--GVITNSLLETNQADIYAIGDCAEVNGTLLPYVMPIMQQAR 302
Cdd:PRK14989 222 KTMrfADGSELEVDFIVFSTGIRPQDKLATQCGLAVAPrgGIVINDSCQTSDPDIYAIGECASWNNRVFGLVAPGYKMAQ 301
|
330
....*....|.
gi 446475553 303 ALAKTLSGQQT 313
Cdd:PRK14989 302 VAVDHLLGSEN 312
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
149-282 |
1.17e-20 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 93.29 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 149 KRVVILGAGLIGCEFAndllhSEY-----DVTVIDLAPqplgRLLP---SHIASAFQQNLEEAGVKFALGTTVEKVSKIN 220
Cdd:PRK06416 173 KSLVVIGGGYIGVEFA-----SAYaslgaEVTIVEALP----RILPgedKEISKLAERALKKRGIKIKTGAKAKKVEQTD 243
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446475553 221 NGedYAVTLANG---QTLVADIVLSAIGLQPNIS---LAQsANIQTSRG-VITNSLLETNQADIYAIGD 282
Cdd:PRK06416 244 DG--VTVTLEDGgkeETLEADYVLVAVGRRPNTEnlgLEE-LGVKTDRGfIEVDEQLRTNVPNIYAIGD 309
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
1-285 |
1.81e-20 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 92.54 E-value: 1.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 1 MHPIVIIGSGMAGYTLAREFRKLNPEQELVMICADDAVNYAKPTL----SNAFAGKK-----APEQiplgdaakMSAQLN 71
Cdd:PRK13512 1 MPKIIVVGAVAGGATCASQIRRLDKESDIIIFEKDRDMSFANCALpyyiGEVVEDRKyalayTPEK--------FYDRKQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 72 MRIEPFTWVKEILAERHELVL---EKDGVISQQpYSKLILAVGANPIRLaiaGDGSDDIHVVNSLIDYRSFRENLAQRKD 148
Cdd:PRK13512 73 ITVKTYHEVIAINDERQTVTVlnrKTNEQFEES-YDKLILSPGASANSL---GFESDITFTLRNLEDTDAIDQFIKANQV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 149 KRVVILGAGLIGCEFANDLLHSEYDVTVIDLAPQpLGRLLPSHIASAFQQNLEEAGVKFALGttvEKVSKINngeDYAVT 228
Cdd:PRK13512 149 DKALVVGAGYISLEVLENLYERGLHPTLIHRSDK-INKLMDADMNQPILDELDKREIPYRLN---EEIDAIN---GNEVT 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 446475553 229 LANGQTLVADIVLSAIGLQPNISLAQSANIQ-TSRGVI-TNSLLETNQADIYAIGDCAE 285
Cdd:PRK13512 222 FKSGKVEHYDMIIEGVGTHPNSKFIESSNIKlDDKGFIpVNDKFETNVPNIYAIGDIIT 280
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
106-290 |
9.54e-19 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 87.50 E-value: 9.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 106 LILAVGANPIRLAIAGDgSDDIHVVNSlidyrSFRENLAQRKdKRVVILGAGLIGCEFANdlLHSEY--DVTVIDLAPQP 183
Cdd:PRK07251 122 IVINTGAVSNVLPIPGL-ADSKHVYDS-----TGIQSLETLP-ERLGIIGGGNIGLEFAG--LYNKLgsKVTVLDAASTI 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 184 LGRLLPShIASAFQQNLEEAGVKFALGTTVEKVSkiNNGEDYAVTlANGQTLVADIVLSAIGLQPNISLAQSANIQ---T 260
Cdd:PRK07251 193 LPREEPS-VAALAKQYMEEDGITFLLNAHTTEVK--NDGDQVLVV-TEDETYRFDALLYATGRKPNTEPLGLENTDielT 268
|
170 180 190
....*....|....*....|....*....|.
gi 446475553 261 SRGVI-TNSLLETNQADIYAIGDcaeVNGTL 290
Cdd:PRK07251 269 ERGAIkVDDYCQTSVPGVFAVGD---VNGGP 296
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
149-324 |
1.07e-18 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 87.13 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 149 KRVVILGAGLIGCEFANdLLHS-EYDVTVIDLAPQPLGRLLPShIASAFQQNLEEAGVKFALGTTVEKVSKINNGEdYAV 227
Cdd:PRK06116 168 KRVAVVGAGYIAVEFAG-VLNGlGSETHLFVRGDAPLRGFDPD-IRETLVEEMEKKGIRLHTNAVPKAVEKNADGS-LTL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 228 TLANGQTLVADIVLSAIGLQPN---ISLAQsANIQT-SRG-VITNSLLETNQADIYAIGDCA-EVNGTllpyvmPI-MQQ 300
Cdd:PRK06116 245 TLEDGETLTVDCLIWAIGREPNtdgLGLEN-AGVKLnEKGyIIVDEYQNTNVPGIYAVGDVTgRVELT------PVaIAA 317
|
170 180
....*....|....*....|....*.
gi 446475553 301 ARALAKTLSGQQTNVH--YPAMPVAV 324
Cdd:PRK06116 318 GRRLSERLFNNKPDEKldYSNIPTVV 343
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
149-324 |
4.25e-17 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 82.53 E-value: 4.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 149 KRVVILGAGLIGCEFANDL--LHSEydVTVIDLAPQpLGRLLPSHIASAFQQNLEEAgVKFALGTTVEKVSKiNNGEDYA 226
Cdd:PRK06292 170 KSLAVIGGGVIGLELGQALsrLGVK--VTVFERGDR-ILPLEDPEVSKQAQKILSKE-FKIKLGAKVTSVEK-SGDEKVE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 227 VTLANG--QTLVADIVLSAIGLQPNI-SLA-QSANIQT-SRGVI-TNSLLETNQADIYAIGDcaeVNGtllpyVMPIMQ- 299
Cdd:PRK06292 245 ELEKGGktETIEADYVLVATGRRPNTdGLGlENTGIELdERGRPvVDEHTQTSVPGIYAAGD---VNG-----KPPLLHe 316
|
170 180
....*....|....*....|....*....
gi 446475553 300 ---QARALAKTLSGQQTN-VHYPAMPVAV 324
Cdd:PRK06292 317 aadEGRIAAENAAGDVAGgVRYHPIPSVV 345
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
149-283 |
5.93e-17 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 82.17 E-value: 5.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 149 KRVVILGAGLIGCEFANDL--LHSEydVTVIDLAPQPLGRlLPSHIASAFQQNLEEAGVKFALGTTVEKVSKINNGEDYA 226
Cdd:PRK06370 172 EHLVIIGGGYIGLEFAQMFrrFGSE--VTVIERGPRLLPR-EDEDVAAAVREILEREGIDVRLNAECIRVERDGDGIAVG 248
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446475553 227 VTLANGQ-TLVADIVLSAIGLQPNIS---LAQsANIQTSR--GVITNSLLETNQADIYAIGDC 283
Cdd:PRK06370 249 LDCNGGApEITGSHILVAVGRVPNTDdlgLEA-AGVETDArgYIKVDDQLRTTNPGIYAAGDC 310
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
149-282 |
1.32e-16 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 80.97 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 149 KRVVILGAGLIGCEFANDLLHSEYDVTVIDLAPQPLGrLLPSHIASAFQQNLEEAGVKFALGTTVEKVSKINNGedYAVT 228
Cdd:PRK05249 176 RSLIIYGAGVIGCEYASIFAALGVKVTLINTRDRLLS-FLDDEISDALSYHLRDSGVTIRHNEEVEKVEGGDDG--VIVH 252
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 446475553 229 LANGQTLVADIVLSAIGLQPNI-SLA-QSANIQT-SRGVIT-NSLLETNQADIYAIGD 282
Cdd:PRK05249 253 LKSGKKIKADCLLYANGRTGNTdGLNlENAGLEAdSRGQLKvNENYQTAVPHIYAVGD 310
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
149-321 |
1.57e-16 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 80.74 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 149 KRVVILGAGLIGCEFAN--DLLHSEydVTVIDLAPQPLGrLLPSHIASAFQQNLEEAGVKFALGTTVEKVSKINNGEDYA 226
Cdd:PRK06327 184 KKLAVIGAGVIGLELGSvwRRLGAE--VTILEALPAFLA-AADEQVAKEAAKAFTKQGLDIHLGVKIGEIKTGGKGVSVA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 227 VTLANG--QTLVADIVLSAIGLQPNIS--LAQSANIQ-TSRGVI-TNSLLETNQADIYAIGDCaeVNGTLLPYVMpiMQQ 300
Cdd:PRK06327 261 YTDADGeaQTLEVDKLIVSIGRVPNTDglGLEAVGLKlDERGFIpVDDHCRTNVPNVYAIGDV--VRGPMLAHKA--EEE 336
|
170 180
....*....|....*....|.
gi 446475553 301 ARALAKTLSGQQTNVHYPAMP 321
Cdd:PRK06327 337 GVAVAERIAGQKGHIDYNTIP 357
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
150-232 |
2.03e-16 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 425450 [Multi-domain] Cd Length: 80 Bit Score: 73.39 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 150 RVVILGAGLIGCEFANDLLHSEYDVTVIDLAPQPLgRLLPSHIASAFQQNLEEAGVKFALGTTVEKVSKINNGEdyAVTL 229
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLL-PGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGV--VVVL 77
|
...
gi 446475553 230 ANG 232
Cdd:pfam00070 78 TDG 80
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
4-284 |
1.26e-13 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 70.92 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 4 IVIIGSGMAGYT----LARefRKLNPeqelVMIcaddavnyAKPTLSNAFAGKKAPEQIPlGDAAKMSAQ---LNMR--I 74
Cdd:COG0492 3 VVIIGAGPAGLTaaiyAAR--AGLKT----LVI--------EGGEPGGQLATTKEIENYP-GFPEGISGPelaERLReqA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 75 EPF------TWVKEILAE--RHELVLEKDGVIsqqpYSK-LILAVGANPIRLAIAG---------------DGsddihvv 130
Cdd:COG0492 68 ERFgaeillEEVTSVDKDdgPFRVTTDDGTEY----EAKaVIIATGAGPRKLGLPGeeefegrgvsycatcDG------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 131 nslidyrsfrenlAQRKDKRVVILGAGLIGCEFANDLlhSEY--DVTVIDLAPQPlgRLLPSHIASAFqqnlEEAGVKFA 208
Cdd:COG0492 137 -------------FFFRGKDVVVVGGGDSALEEALYL--TKFasKVTLIHRRDEL--RASKILVERLR----ANPKIEVL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 209 LGTTVEKVskinNGEDY--AVTLANGQT-----LVADIVLSAIGLQPNISLAQSANIQTSRG--VITNSLLETNQADIYA 279
Cdd:COG0492 196 WNTEVTEI----EGDGRveGVTLKNVKTgeekeLEVDGVFVAIGLKPNTELLKGLGLELDEDgyIVVDEDMETSVPGVFA 271
|
....*
gi 446475553 280 IGDCA 284
Cdd:COG0492 272 AGDVR 276
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
103-333 |
3.05e-13 |
|
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon for the detoxification of mercury compounds. MerA is a FAD-containing flavoprotein which reduces Hg(II) to Hg(0) utilizing NADPH. [Cellular processes, Detoxification]
Pssm-ID: 273944 [Multi-domain] Cd Length: 463 Bit Score: 70.91 E-value: 3.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 103 YSKLILAVGANPIRLAIagDGSDDIhvvnsliDYRSFRENLA-QRKDKRVVILGAGLIGCEFANDLLHSEYDVTVIdlap 181
Cdd:TIGR02053 129 AKRFLIATGARPAIPPI--PGLKEA-------GYLTSEEALAlDRIPESLAVIGGGAIGVELAQAFARLGSEVTIL---- 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 182 QPLGRLLP--SHIASAFQQN-LEEAGVKFALGTTVEKVSkINNGEDYAVTLANG--QTLVADIVLSAIGLQPNISLA--Q 254
Cdd:TIGR02053 196 QRSDRLLPreEPEISAAVEEaLAEEGIEVVTSAQVKAVS-VRGGGKIITVEKPGgqGEVEADELLVATGRRPNTDGLglE 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 255 SANIQTSR--GVITNSLLETNQADIYAIGDCaeVNGTLLPYVMPiMQQARALAKTLSGQQTNVHYPAMPVAVKTPAAPLT 332
Cdd:TIGR02053 275 KAGVKLDErgGILVDETLRTSNPGIYAAGDV--TGGLQLEYVAA-KEGVVAAENALGGANAKLDLLVIPRVVFTDPAVAS 351
|
.
gi 446475553 333 V 333
Cdd:TIGR02053 352 V 352
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
84-327 |
1.56e-10 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 62.53 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 84 LAERHELVLEKDGVISQQPYSKLILAVGANP---------IRLAIAgdgSDDIhvvnslidyrsfrenLAQRKDK-RVVI 153
Cdd:PTZ00052 126 LKDEHTVSYGDNSQEETITAKYILIATGGRPsipedvpgaKEYSIT---SDDI---------------FSLSKDPgKTLI 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 154 LGAGLIGCEFANDLLHSEYDVTVIdLAPQPLgRLLPSHIASAFQQNLEEAGVKFALGTTVEKVSKINngEDYAVTLANGQ 233
Cdd:PTZ00052 188 VGASYIGLETAGFLNELGFDVTVA-VRSIPL-RGFDRQCSEKVVEYMKEQGTLFLEGVVPINIEKMD--DKIKVLFSDGT 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 234 TLVADIVLSAIGLQPNISL--AQSANIQTSRG---VITNSLleTNQADIYAIGDCAEVngtlLPYVMPIMQQA-RALAKT 307
Cdd:PTZ00052 264 TELFDTVLYATGRKPDIKGlnLNAIGVHVNKSnkiIAPNDC--TNIPNIFAVGDVVEG----RPELTPVAIKAgILLARR 337
|
250 260
....*....|....*....|.
gi 446475553 308 LSGQ-QTNVHYPAMPVAVKTP 327
Cdd:PTZ00052 338 LFKQsNEFIDYTFIPTTIFTP 358
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
149-324 |
2.10e-10 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 62.14 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 149 KRVVILGAGLIGCEFANdlLHSEYDVTViDL---APQPLgRLLPSHIASAFQQNLEEAGVKFALGTTVEKVSKINNGedY 225
Cdd:PLN02507 204 KRAVVLGGGYIAVEFAS--IWRGMGATV-DLffrKELPL-RGFDDEMRAVVARNLEGRGINLHPRTNLTQLTKTEGG--I 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 226 AVTLANGQTLVADIVLSAIGLQPN---ISL-AQSANIQTSRGVITNSLLETNQADIYAIGDCA-EVNGTllpyvmPI-MQ 299
Cdd:PLN02507 278 KVITDHGEEFVADVVLFATGRAPNtkrLNLeAVGVELDKAGAVKVDEYSRTNIPSIWAIGDVTnRINLT------PVaLM 351
|
170 180
....*....|....*....|....*.
gi 446475553 300 QARALAKT-LSGQQTNVHYPAMPVAV 324
Cdd:PLN02507 352 EGTCFAKTvFGGQPTKPDYENVACAV 377
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
88-310 |
6.82e-10 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 60.17 E-value: 6.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 88 HELVLEKDGVIsqqPYSKLILAVGANPIRLAIAGdGSDDIHVVNSLIDYRSFRENLAQ------------RKDKR---VV 152
Cdd:PTZ00318 102 SNNANVNTFSV---PYDKLVVAHGARPNTFNIPG-VEERAFFLKEVNHARGIRKRIVQcieraslpttsvEERKRllhFV 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 153 ILGAGLIGCEFANDL--------------LHSEYDVTVIDLApqplgrllpSHIASAFQQNLEEAGVKF--ALGTTVEKV 216
Cdd:PTZ00318 178 VVGGGPTGVEFAAELadffrddvrnlnpeLVEECKVTVLEAG---------SEVLGSFDQALRKYGQRRlrRLGVDIRTK 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 217 SKINNGEDYAVTLANGQTLVADIVLSAIGLQPNISLAQSANIQTSRGVIT--NSLLETNQADIYAIGDCAEVNGTLLPYV 294
Cdd:PTZ00318 249 TAVKEVLDKEVVLKDGEVIPTGLVVWSTGVGPGPLTKQLKVDKTSRGRISvdDHLRVKPIPNVFALGDCAANEERPLPTL 328
|
250
....*....|....*..
gi 446475553 295 MPIM-QQARALAKTLSG 310
Cdd:PTZ00318 329 AQVAsQQGVYLAKEFNN 345
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
105-327 |
3.71e-09 |
|
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member of the pyridine nucleotide disulfide oxidoreductase family contains a C-terminal motif Cys-SeCys-Gly, where SeCys is selenocysteine encoded by TGA (in some sequence reports interpreted as a stop codon). In some members of this subfamily, Cys-SeCys-Gly is replaced by Cys-Cys-Gly. The reach of the selenium atom at the C-term arm of the protein is proposed to allow broad substrate specificity.
Pssm-ID: 273624 [Multi-domain] Cd Length: 484 Bit Score: 58.32 E-value: 3.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 105 KLILAVGANPIRLAIAGDG-----SDDIHvvnslidyrsfreNLAQRKDKRVVIlGAGLIGCEFANDLLHSEYDVTVidL 179
Cdd:TIGR01438 146 RFLIATGERPRYPGIPGAKelcitSDDLF-------------SLPYCPGKTLVV-GASYVALECAGFLAGIGLDVTV--M 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 180 APQPLGRLLPSHIASAFQQNLEEAGVKFALGTTVEKVSKInnGEDYAVTLANGQTLVA---DIVLSAIGLQPNI-SLA-Q 254
Cdd:TIGR01438 210 VRSILLRGFDQDCANKVGEHMEEHGVKFKRQFVPIKVEQI--EAKVLVEFTDSTNGIEeeyDTVLLAIGRDACTrKLNlE 287
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446475553 255 SANIQTSRG---VITNSLLETNQADIYAIGDCAEVNGTLLPYVmpiMQQARALAKTL-SGQQTNVHYPAMPVAVKTP 327
Cdd:TIGR01438 288 NVGVKINKKtgkIPADEEEQTNVPYIYAVGDILEDKPELTPVA---IQAGRLLAQRLfKGSTVICDYENVPTTVFTP 361
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
87-282 |
4.87e-09 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 57.66 E-value: 4.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 87 RHELVLEKDGVISQQpysKLILAVGANP-IRLAIAGDG-----SDDIHVVNSLidyrsfrenlaqrkDKRVVILGAGLIG 160
Cdd:PRK07846 116 PKTLRTGDGEEITAD---QVVIAAGSRPvIPPVIADSGvryhtSDTIMRLPEL--------------PESLVIVGGGFIA 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 161 CEFAN--DLLHSEydVTVIDLAPQPLgRLLPSHIASAFqqnLEEAGVKFALGTTVEKVSKINNGEDYAVTLANGQTLVAD 238
Cdd:PRK07846 179 AEFAHvfSALGVR--VTVVNRSGRLL-RHLDDDISERF---TELASKRWDVRLGRNVVGVSQDGSGVTLRLDDGSTVEAD 252
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446475553 239 IVLSAIGLQPNISL--AQSANIQTSRG--VITNSLLETNQADIYAIGD 282
Cdd:PRK07846 253 VLLVATGRVPNGDLldAAAAGVDVDEDgrVVVDEYQRTSAEGVFALGD 300
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
100-283 |
1.22e-08 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 56.66 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 100 QQPYSKLILAVGAN-PIRLAIAGDGSDDihvVNSLIDY-RSFRENLAQRKDKRVVILGAGligcefaNdllhseydvTVI 177
Cdd:PRK12814 276 QKEFDAVLLAVGAQkASKMGIPGEELPG---VISGIDFlRNVALGTALHPGKKVVVIGGG-------N---------TAI 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 178 DLAPQPLgRLLPSHIA----------SAFQQNLEEA---GVKFALGTTVEKVSKINNG-EDYAVTLANGQ---------- 233
Cdd:PRK12814 337 DAARTAL-RLGAESVTilyrrtreemPANRAEIEEAlaeGVSLRELAAPVSIERSEGGlELTAIKMQQGEpdesgrrrpv 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 234 -------TLVADIVLSAIGLQPNISLAQSANIQTSRG---VITNSLLETNQADIYAIGDC 283
Cdd:PRK12814 416 pvegsefTLQADTVISAIGQQVDPPIAEAAGIGTSRNgtvKVDPETLQTSVAGVFAGGDC 475
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
142-282 |
6.62e-08 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 54.25 E-value: 6.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 142 NLAQRKdKRVVILGAGLIGCEFANDLLHSEYDVTVIDLAPQPLGRlLPSHIASAFQQNLEEAGVKFALGTTVEKVSKINN 221
Cdd:PRK08010 153 NLKELP-GHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPR-EDRDIADNIATILRDQGVDIILNAHVERISHHEN 230
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446475553 222 GedYAVTLANGQTLVaDIVLSAIGLQPNISLAQSAN----IQTSRGVITNSLLETNQADIYAIGD 282
Cdd:PRK08010 231 Q--VQVHSEHAQLAV-DALLIASGRQPATASLHPENagiaVNERGAIVVDKYLHTTADNIWAMGD 292
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
74-284 |
1.37e-07 |
|
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis
Pssm-ID: 440259 [Multi-domain] Cd Length: 434 Bit Score: 53.22 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 74 IEPFTWVKEILAERHELvLEKDGV-----------IS----QQPYSKLILAVGA-NPIRLAIAGDGSDDIHvvnSLIDY- 136
Cdd:COG0493 164 IPEFRLPKDVLDREIEL-IEALGVefrtnvevgkdITldelLEEFDAVFLATGAgKPRDLGIPGEDLKGVH---SAMDFl 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 137 RSFRENLAQ----RKDKRVVILGAGLIgcefAND-----LLHSEYDVTVIDLAPQ---PlgrllpshiASAF-QQNLEEA 203
Cdd:COG0493 240 TAVNLGEAPdtilAVGKRVVVIGGGNT----AMDcartaLRLGAESVTIVYRRTReemP---------ASKEeVEEALEE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 204 GVKFALGTTVEKVSKINNGEDYAVTL---------ANG-----------QTLVADIVLSAIGLQPNIS-LAQSANIQTS- 261
Cdd:COG0493 307 GVEFLFLVAPVEIIGDENGRVTGLECvrmelgepdESGrrrpvpiegseFTLPADLVILAIGQTPDPSgLEEELGLELDk 386
|
250 260
....*....|....*....|....*
gi 446475553 262 RGVI--TNSLLETNQADIYAIGDCA 284
Cdd:COG0493 387 RGTIvvDEETYQTSLPGVFAGGDAV 411
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
106-282 |
8.40e-07 |
|
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of spermidine, is (in its reduced form) an important antioxidant found in trypanosomatids (Crithidia, Leishmania, Trypanosoma). This model describes trypanothione reductase, a possible antitrypanosomal drug target closely related to some forms of glutathione reductase.
Pssm-ID: 200098 [Multi-domain] Cd Length: 486 Bit Score: 50.74 E-value: 8.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 106 LILAVGANPIRLAIAGDGsddiHVVNSlidyrsfreNLA---QRKDKRVVILGAGLIGCEFANDLLHSEYDVTVIDLAPQ 182
Cdd:TIGR01423 155 ILLATGSWPQMLGIPGIE----HCISS---------NEAfylDEPPRRVLTVGGGFISVEFAGIFNAYKPRGGKVTLCYR 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 183 --PLGRLLPSHIASAFQQNLEEAGVKFALGTTVEKVSKINNGEDYaVTLANGQTLVADIVLSAIGLQPNISLAQSANIQ- 259
Cdd:TIGR01423 222 nnMILRGFDSTLRKELTKQLRANGINIMTNENPAKVTLNADGSKH-VTFESGKTLDVDVVMMAIGRVPRTQTLQLDKVGv 300
|
170 180
....*....|....*....|....*.
gi 446475553 260 --TSRGVI-TNSLLETNQADIYAIGD 282
Cdd:TIGR01423 301 elTKKGAIqVDEFSRTNVPNIYAIGD 326
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
106-286 |
2.64e-06 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 49.23 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 106 LILAVGANPIrlaiagdgSDDIHVVNSLIDYRSFrenLAQRKDKRVVILGAGLIGCEFANDLLHSEYDVTVIDLAPQPLg 185
Cdd:PTZ00058 206 ILIAVGNKPI--------FPDVKGKEFTISSDDF---FKIKEAKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLL- 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 186 RLLPSHIASAFQQNLEEAGVKFALGTTVEKVSKINNGEDYAVTLANGQTLVADIVLSAIGLQPNISL--AQSANIQTSRG 263
Cdd:PTZ00058 274 RKFDETIINELENDMKKNNINIITHANVEEIEKVKEKNLTIYLSDGRKYEHFDYVIYCVGRSPNTEDlnLKALNIKTPKG 353
|
170 180
....*....|....*....|....
gi 446475553 264 -VITNSLLETNQADIYAIGDCAEV 286
Cdd:PTZ00058 354 yIKVDDNQRTSVKHIYAVGDCCMV 377
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
149-247 |
1.04e-04 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 44.33 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 149 KRVVILGAGLIGCEFANDLLHSEYDVTVIDLAPQPLGRL--------LPSHIASAFQQNLEEAGVKFALGTTVekvskin 220
Cdd:PRK12814 194 KKVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGMMrygiprfrLPESVIDADIAPLRAMGAEFRFNTVF------- 266
|
90 100
....*....|....*....|....*..
gi 446475553 221 nGEDyaVTLANGQTLVaDIVLSAIGLQ 247
Cdd:PRK12814 267 -GRD--ITLEELQKEF-DAVLLAVGAQ 289
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
149-379 |
5.39e-04 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 42.06 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 149 KRVVILGAGLIGCEFANDLLHSEYDVTVidLAPQPL-GRLLPShIASAFQQNLEEAGVKFALGTTVEKVSKINNgeDYAV 227
Cdd:PRK13748 271 ERLAVIGSSVVALELAQAFARLGSKVTI--LARSTLfFREDPA-IGEAVTAAFRAEGIEVLEHTQASQVAHVDG--EFVL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 228 TLANGqTLVADIVLSAIGLQPNI-SLA-QSANIQT-SRGVIT-NSLLETNQADIYAIGDCAEvngtllpyvMPIMQQARA 303
Cdd:PRK13748 346 TTGHG-ELRADKLLVATGRAPNTrSLAlDAAGVTVnAQGAIViDQGMRTSVPHIYAAGDCTD---------QPQFVYVAA 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 304 LAKT-----LSGQQTNVHYPAMPVAVKTPAAPLTVLPApvdvdvnwETEEFDDGM-----------LAKAIDNEGTlRGF 367
Cdd:PRK13748 416 AAGTraainMTGGDAALDLTAMPAVVFTDPQVATVGYS--------EAEAHHDGIetdsrtltldnVPRALANFDT-RGF 486
|
250
....*....|..
gi 446475553 368 VLLGATAGKQRL 379
Cdd:PRK13748 487 IKLVIEEGSGRL 498
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
150-286 |
8.92e-04 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 41.38 E-value: 8.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 150 RVVILGAGLIGCEFANDLLHSEYDVTVI---DlapqplgRLLP---SHIASAFQQNLEEAGVKFALGTTVEKVSKINNGe 223
Cdd:PRK07845 179 HLIVVGSGVTGAEFASAYTELGVKVTLVssrD-------RVLPgedADAAEVLEEVFARRGMTVLKRSRAESVERTGDG- 250
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446475553 224 dYAVTLANGQTLVADIVLSAIGLQPN---ISLAQsANIQTSRG--VITNSLLETNQADIYAIGDCAEV 286
Cdd:PRK07845 251 -VVVTLTDGRTVEGSHALMAVGSVPNtagLGLEE-AGVELTPSghITVDRVSRTSVPGIYAAGDCTGV 316
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
128-235 |
2.02e-03 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 40.14 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 128 HVVNS--LIDYRSFRENLAQRKDKRVVILGAGLIGCEFANDLLHSEYDVTVIDLAPQPLGRL---LPSHIA--SAFQQN- 199
Cdd:PRK13984 261 YIVDNvpVEKYSEILDDEPEKKNKKVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGGVMrygIPSYRLpdEALDKDi 340
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 446475553 200 --LEEAGVKFALGTTVEK---VSKINNGEDyAVTLANGQTL 235
Cdd:PRK13984 341 afIEALGVKIHLNTRVGKdipLEELREKHD-AVFLSTGFTL 380
|
|
| trkA |
PRK09496 |
Trk system potassium transporter TrkA; |
150-206 |
2.45e-03 |
|
Trk system potassium transporter TrkA;
Pssm-ID: 236541 [Multi-domain] Cd Length: 453 Bit Score: 39.72 E-value: 2.45e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446475553 150 RVVILGAGLIGCEFANDLLHSEYDVTVIDLAPQPLGRLLPSHIASAFQQN------LEEAGVK 206
Cdd:PRK09496 2 KIIIVGAGQVGYTLAENLSGENNDVTVIDTDEERLRRLQDRLDVRTVVGNgsspdvLREAGAE 64
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
144-215 |
3.30e-03 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 39.73 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 144 AQRKDKRVVILGAGLIGCEFANDLLHSEYDVTVIDLAPQPLGRL--------LPSHIASAFQQNLEEAGVKFALGTTVEK 215
Cdd:PRK12778 427 AEKNGKKVAVIGSGPAGLSFAGDLAKRGYDVTVFEALHEIGGVLkygipefrLPKKIVDVEIENLKKLGVKFETDVIVGK 506
|
|
| PRK09126 |
PRK09126 |
FAD-dependent hydroxylase; |
180-243 |
7.26e-03 |
|
FAD-dependent hydroxylase;
Pssm-ID: 236385 [Multi-domain] Cd Length: 392 Bit Score: 38.38 E-value: 7.26e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446475553 180 APQPLGRLLPSHI--ASAFQQNLEEAGVKFALGTTVEKVskiNNGEDYA-VTLANGQTLVADIVLSA 243
Cdd:PRK09126 99 GADALGYLVPNHLirRAAYEAVSQQDGIELLTGTRVTAV---RTDDDGAqVTLANGRRLTARLLVAA 162
|
|
| TrkA |
COG0569 |
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ... |
114-206 |
8.83e-03 |
|
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: 37.74 E-value: 8.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475553 114 PIRLAIAGDGSDDIHVVNSLIDYRSFRENLAQ-RKDKRVVILGAGLIGCEFANDLLHSEYDVTVIDLAPQPLGRLLPSHI 192
Cdd:COG0569 60 IPLGYTLITFGDAVLFGGLLEALRRRRMERGIkKLKMHVIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAEEDV 139
|
90
....*....|....*....
gi 446475553 193 ----ASAFQQN-LEEAGVK 206
Cdd:COG0569 140 lvivGDATDEEvLEEAGIE 158
|
|
| |
