|
Name |
Accession |
Description |
Interval |
E-value |
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
16-292 |
8.39e-130 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 371.76 E-value: 8.39e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 16 PAGLTAALYSSRARAKTVVFESGLPGGQIVTTDWVENYPGFPDGISGMEIGDLMHRQAEKFGAEFRTfAAIEKIEPQGID 95
Cdd:COG0492 10 PAGLTAAIYAARAGLKTLVIEGGEPGGQLATTKEIENYPGFPEGISGPELAERLREQAERFGAEILL-EEVTSVDKDDGP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 96 FLLTDSEGAQVVAHAVILATGAVPKRLGVPGEAEFTGRGVSWCATCDGAFFRDKVVAVIGGGDAAVEEALFLTKFASKVH 175
Cdd:COG0492 89 FRVTTDDGTEYEAKAVIIATGAGPRKLGLPGEEEFEGRGVSYCATCDGFFFRGKDVVVVGGGDSALEEALYLTKFASKVT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 176 IVHRRDELRATKCIQEKCFANEKIAFELSRVVSEVVGEnGKVTGIKLASTKGDPELLLPLDGVFIFVGVEPKSELVADL- 254
Cdd:COG0492 169 LIHRRDELRASKILVERLRANPKIEVLWNTEVTEIEGD-GRVEGVTLKNVKTGEEKELEVDGVFVAIGLKPNTELLKGLg 247
|
250 260 270
....*....|....*....|....*....|....*...
gi 1309179808 255 CDLDQAGYIKIDHNGLTSYPGLYAAGDVTDSDLKQVIT 292
Cdd:COG0492 248 LELDEDGYIVVDEDMETSVPGVFAAGDVRDYKYRQAAT 285
|
|
| TRX_reduct |
TIGR01292 |
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ... |
16-292 |
3.27e-125 |
|
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a member of the pyridine nucleotide-disulphide oxidoreductases (pfam00070). [Energy metabolism, Electron transport]
Pssm-ID: 273540 [Multi-domain] Cd Length: 299 Bit Score: 360.02 E-value: 3.27e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 16 PAGLTAALYSSRARAKTVVFESGLPGGQIVTTDWVENYPGFPDGISGMEIGDLMHRQAEKFGAEFRtFAAIEKIEPQGID 95
Cdd:TIGR01292 9 PAGLTAAIYAARANLKPLLIEGMEPGGQLTTTTEVENYPGFPEGISGPELMEKMKEQAVKFGAEII-YEEVIKVDKSDRP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 96 FLLTDSEGAQVVAHAVILATGAVPKRLGVPGEAEFTGRGVSWCATCDGAFFRDKVVAVIGGGDAAVEEALFLTKFASKVH 175
Cdd:TIGR01292 88 FKVYTGDGKEYTAKAVIIATGASARKLGIPGEDEFWGRGVSYCATCDGPFFKNKEVAVVGGGDSAIEEALYLTRIAKKVT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 176 IVHRRDELRATKCIQEKCFANEKIAFELSRVVSEVVGENgKVTGIKLASTKGDPELLLPLDGVFIFVGVEPKSELVADLC 255
Cdd:TIGR01292 168 LVHRRDKFRAEKILLDRLKKNPKIEFLWNSTVEEIVGDN-KVEGVKIKNTVTGEEEELEVDGVFIAIGHEPNTELLKGLL 246
|
250 260 270
....*....|....*....|....*....|....*..
gi 1309179808 256 DLDQAGYIKIDHNGLTSYPGLYAAGDVTDSDLKQVIT 292
Cdd:TIGR01292 247 ELDENGYIVTDEGMRTSVPGVFAAGDVRDKGYRQAVT 283
|
|
| AhpF_homolog |
TIGR03143 |
putative alkyl hydroperoxide reductase F subunit; This family of thioredoxin reductase ... |
16-292 |
5.69e-73 |
|
putative alkyl hydroperoxide reductase F subunit; This family of thioredoxin reductase homologs is found adjacent to alkylhydroperoxide reductase C subunit predominantly in cases where there is only one C subunit in the genome and that genome is lacking the F subunit partner (also a thioredcxin reductase homolog) that is usually found (TIGR03140).
Pssm-ID: 132187 [Multi-domain] Cd Length: 555 Bit Score: 234.67 E-value: 5.69e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 16 PAGLTAALYSSRARAKTVVFESGLPGGQIVTTDWVENYPGFPDgISGMEIGDLMHRQAEKFGAEFRTFAAIEKIEPQGID 95
Cdd:TIGR03143 14 PAGLSAGIYAGRAKLDTLIIEKDDFGGQITITSEVVNYPGILN-TTGPELMQEMRQQAQDFGVKFLQAEVLDVDFDGDIK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 96 FLLTDSegAQVVAHAVILATGAVPKRLGVPGEAEFTGRGVSWCATCDGAFFRDKVVAVIGGGDAAVEEALFLTKFASKVH 175
Cdd:TIGR03143 93 TIKTAR--GDYKTLAVLIATGASPRKLGFPGEEEFTGRGVAYCATCDGEFFTGMDVFVIGGGFAAAEEAVFLTRYASKVT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 176 IVHRRDELRATKCIQEKCFANEKIAFELSRVVSEVVGENG-KVTGIKLASTKGDPELLLPLD----GVFIFVGVEPKSEL 250
Cdd:TIGR03143 171 VIVREPDFTCAKLIAEKVKNHPKIEVKFNTELKEATGDDGlRYAKFVNNVTGEITEYKAPKDagtfGVFVFVGYAPSSEL 250
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1309179808 251 VADLCDLDQAGYIKIDHNGLTSYPGLYAAGDVTDSDLKQVIT 292
Cdd:TIGR03143 251 FKGVVELDKRGYIPTNEDMETNVPGVYAAGDLRPKELRQVVT 292
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
16-309 |
2.30e-63 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 203.37 E-value: 2.30e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 16 PAGLTAALYSSRARAKTVVFESGLPGGQIVTTDWVENYPGFPDGISGMEIGDLMHRQAEKFGAEFrTFAAIEKIEPQGID 95
Cdd:PRK10262 16 PAGYTAAVYAARANLQPVLITGMEKGGQLTTTTEVENWPGDPNDLTGPLLMERMHEHATKFETEI-IFDHINKVDLQNRP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 96 FLLTDSEGaQVVAHAVILATGAVPKRLGVPGEAEFTGRGVSWCATCDGAFFRDKVVAVIGGGDAAVEEALFLTKFASKVH 175
Cdd:PRK10262 95 FRLTGDSG-EYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEALYLSNIASEVH 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 176 IVHRRDELRATKCIQEKCF---ANEKIAFELSRVVSEVVGENGKVTGIKLASTKgDPELLLPLD--GVFIFVGVEPKSEL 250
Cdd:PRK10262 174 LIHRRDGFRAEKILIKRLMdkvENGNIILHTNRTLEEVTGDQMGVTGVRLRDTQ-NSDNIESLDvaGLFVAIGHSPNTAI 252
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1309179808 251 VADLCDLDQaGYIKIdHNGL------TSYPGLYAAGDVTDSDLKQVITAAAKGASAAFEALRWID 309
Cdd:PRK10262 253 FEGQLELEN-GYIKV-QSGIhgnatqTSIPGVFAAGDVMDHIYRQAITSAGTGCMAALDAERYLD 315
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
16-291 |
1.52e-52 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 179.97 E-value: 1.52e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 16 PAGLTAALYSSRARAKT-VVFESGlpGGQIVTTDWVENYPGFPDgISGMEIGDLMHRQAEKFGAEFRTFAAIEKIEPQGI 94
Cdd:PRK15317 221 PAGAAAAIYAARKGIRTgIVAERF--GGQVLDTMGIENFISVPE-TEGPKLAAALEEHVKEYDVDIMNLQRASKLEPAAG 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 95 DFLLTDSEGAQVVAHAVILATGAVPKRLGVPGEAEFTGRGVSWCATCDGAFFRDKVVAVIGGGDAAVEEALFLTKFASKV 174
Cdd:PRK15317 298 LIEVELANGAVLKAKTVILATGARWRNMNVPGEDEYRNKGVAYCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVKHV 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 175 HIVHRRDELRATKCIQEKCFANEKIAFELSRVVSEVVGENGKVTGIKLASTKGDPELLLPLDGVFIFVGVEPKSELVADL 254
Cdd:PRK15317 378 TVLEFAPELKADQVLQDKLRSLPNVTIITNAQTTEVTGDGDKVTGLTYKDRTTGEEHHLELEGVFVQIGLVPNTEWLKGT 457
|
250 260 270
....*....|....*....|....*....|....*..
gi 1309179808 255 CDLDQAGYIKIDHNGLTSYPGLYAAGDVTDSDLKQVI 291
Cdd:PRK15317 458 VELNRRGEIIVDARGATSVPGVFAAGDCTTVPYKQII 494
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
16-292 |
2.22e-46 |
|
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: 158.64 E-value: 2.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 16 PAGLTAALYSSRARAKTVVFESG--LPGGQIVTTDWVENYPGFPDGIS-GMEIGDLMHRQAEKFGAEFRTFAAIE--KIE 90
Cdd:pfam07992 10 PAGLAAALTLAQLGGKVTLIEDEgtCPYGGCVLSKALLGAAEAPEIASlWADLYKRKEEVVKKLNNGIEVLLGTEvvSID 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 91 PQGIDFLLT---DSEGAQVVAHAVILATGAVPKRLGVPGEAEFTGRGVSWCATCDGAFF--RDKVVAVIGGGDAAVEEAL 165
Cdd:pfam07992 90 PGAKKVVLEelvDGDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLklLPKRVVVVGGGYIGVELAA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 166 FLTKFASKVHIVHRRDEL------RATKCIQeKCFANEKIAFELSRVVSEVVGENGKVTgiklasTKGDPELLLPLDGVF 239
Cdd:pfam07992 170 ALAKLGKEVTLIEALDRLlrafdeEISAALE-KALEKNGVEVRLGTSVKEIIGDGDGVE------VILKDGTEIDADLVV 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1309179808 240 IFVGVEPKSELVADL-CDLDQAGYIKIDHNGLTSYPGLYAAGDVTDSDLKQVIT 292
Cdd:pfam07992 243 VAIGRRPNTELLEAAgLELDERGGIVVDEYLRTSVPGIYAAGDCRVGGPELAQN 296
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
16-284 |
6.21e-19 |
|
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: 86.68 E-value: 6.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 16 PAGLTAALYSSRARAKTVVFESGLPGG-----------------QIVttDWVENYPGFpdGISGMEIG-DL--MHRQAEK 75
Cdd:COG1249 13 PGGYVAAIRAAQLGLKVALVEKGRLGGtclnvgcipskallhaaEVA--HEARHAAEF--GISAGAPSvDWaaLMARKDK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 76 FGAEFRTFAAiEKIEPQGIDFL-----LTDS-----EGAQVV-AHAVILATGAVPKRLGVPGEAEftGRGVSWcatcDGA 144
Cdd:COG1249 89 VVDRLRGGVE-ELLKKNGVDVIrgrarFVDPhtvevTGGETLtADHIVIATGSRPRVPPIPGLDE--VRVLTS----DEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 145 FFRDKV---VAVIGGGDAAVEEALFLTKFASKVHIVHRRDEL------RATKCIQEKcFANEKIAFELSRVVSEVVGENG 215
Cdd:COG1249 162 LELEELpksLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLlpgedpEISEALEKA-LEKEGIDILTGAKVTSVEKTGD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1309179808 216 KVTgikLASTKGDPELLLPLDGVFIFVGVEPKSELV----ADLcDLDQAGYIKIDHNGLTSYPGLYAAGDVTD 284
Cdd:COG1249 241 GVT---VTLEDGGGEEAVEADKVLVATGRRPNTDGLgleaAGV-ELDERGGIKVDEYLRTSVPGIYAIGDVTG 309
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
16-283 |
7.77e-19 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 86.39 E-value: 7.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 16 PAGLTAALYSSRARAKTVVFES-GLPGGqivttdwVENY--PGF--PDGISGMEIGDLmhrqaEKFGAEFRTFAAIekie 90
Cdd:PRK11749 150 PAGLTAAHRLARKGYDVTIFEArDKAGG-------LLRYgiPEFrlPKDIVDREVERL-----LKLGVEIRTNTEV---- 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 91 pqGIDFLLTD-SEGAqvvaHAVILATGA-VPKRLGVPGEA--------EFTGRgvSWCATCDGAFFRDKVVAVIGGGDAA 160
Cdd:PRK11749 214 --GRDITLDElRAGY----DAVFIGTGAgLPRFLGIPGENlggvysavDFLTR--VNQAVADYDLPVGKRVVVIGGGNTA 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 161 VEEALFLTKF-ASKVHIVHRRDELRATKCIQEKCFANEK-IAFELSRVVSEVVGENGKVTGIKLASTK-GDP-------- 229
Cdd:PRK11749 286 MDAARTAKRLgAESVTIVYRRGREEMPASEEEVEHAKEEgVEFEWLAAPVEILGDEGRVTGVEFVRMElGEPdasgrrrv 365
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1309179808 230 -----ELLLPLDGVFIFVGVEPKSELVADLCDLD---QAGYIKIDHNGLTSYPGLYAAGDVT 283
Cdd:PRK11749 366 piegsEFTLPADLVIKAIGQTPNPLILSTTPGLElnrWGTIIADDETGRTSLPGVFAGGDIV 427
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
16-281 |
8.94e-18 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 83.53 E-value: 8.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 16 PAGLTAALYSSRARAKTVVFESgL--PGGQIVttdwvenYpGFP------DGISGMEIGDLmhrqaEKFGAEF------- 80
Cdd:PRK12831 150 PAGLTCAGDLAKMGYDVTIFEA-LhePGGVLV-------Y-GIPefrlpkETVVKKEIENI-----KKLGVKIetnvvvg 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 81 RTFAAIEKIEPQGIDflltdsegaqvvahAVILATGA-VPKRLGVPGEA--------EFTGR---GVSWCATCDGAFFRD 148
Cdd:PRK12831 216 KTVTIDELLEEEGFD--------------AVFIGSGAgLPKFMGIPGENlngvfsanEFLTRvnlMKAYKPEYDTPIKVG 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 149 KVVAVIGGGDAAVEEALFLTKFASKVHIVHRRDELRATKCIQEKCFANEK-IAFELSRVVSEVVG-ENGKVTGIKL---- 222
Cdd:PRK12831 282 KKVAVVGGGNVAMDAARTALRLGAEVHIVYRRSEEELPARVEEVHHAKEEgVIFDLLTNPVEILGdENGWVKGMKCikme 361
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1309179808 223 -----ASTKGDP------ELLLPLDGVFIFVGVEPK---SELVADLcDLDQAGYIKIDHN-GLTSYPGLYAAGD 281
Cdd:PRK12831 362 lgepdASGRRRPveiegsEFVLEVDTVIMSLGTSPNpliSSTTKGL-KINKRGCIVADEEtGLTSKEGVFAGGD 434
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
54-283 |
2.65e-17 |
|
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: 81.01 E-value: 2.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 54 PGFPDGISG--MEIGDLMHRQAEKF---GAEFRTFAAIEKIEPQGiDFLLTDSeGAQVVAHAVILATGAVPKRLGVPGEA 128
Cdd:COG0446 22 CGLPYYVGGgiKDPEDLLVRTPESFerkGIDVRTGTEVTAIDPEA-KTVTLRD-GETLSYDKLVLATGARPRPPPIPGLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 129 E---FTGRGVSWCATCDGAFFRDKV--VAVIGGGDAAVEEALFLTKFASKVHIVHRRDEL----------RATKCIQEKc 193
Cdd:COG0446 100 LpgvFTLRTLDDADALREALKEFKGkrAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLlgvldpemaaLLEEELREH- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 194 faneKIAFELSRVVSEVVGENGkvtgIKLASTKGDPellLPLDGVFIFVGVEPKSELVADL-CDLDQAGYIKIDHNGLTS 272
Cdd:COG0446 179 ----GVELRLGETVVAIDGDDK----VAVTLTDGEE---IPADLVVVAPGVRPNTELAKDAgLALGERGWIKVDETLQTS 247
|
250
....*....|.
gi 1309179808 273 YPGLYAAGDVT 283
Cdd:COG0446 248 DPDVYAAGDCA 258
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
16-282 |
1.24e-16 |
|
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: 79.79 E-value: 1.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 16 PAGLTAALYSSRARAKTVVFESG-LPGG----QIvttdwvenyPGF--PDGIsgmeigdLMHR--QAEKFGAEFRTFAAI 86
Cdd:COG0493 131 PAGLAAAYQLARAGHEVTVFEALdKPGGllryGI---------PEFrlPKDV-------LDREieLIEALGVEFRTNVEV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 87 ekiepqGIDFLLtdsegAQVVA--HAVILATGA-VPKRLGVPGEA--------EF---TGRGVSWcatcDGAFFRDKVVA 152
Cdd:COG0493 195 ------GKDITL-----DELLEefDAVFLATGAgKPRDLGIPGEDlkgvhsamDFltaVNLGEAP----DTILAVGKRVV 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 153 VIGGGDAAVE---EALFLTkfASKVHIVHRRDELRATKCIQEKCFA-NEKIAFELSRVVSEVVG-ENGKVTGIKLASTK- 226
Cdd:COG0493 260 VIGGGNTAMDcarTALRLG--AESVTIVYRRTREEMPASKEEVEEAlEEGVEFLFLVAPVEIIGdENGRVTGLECVRMEl 337
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1309179808 227 GDP--------------ELLLPLDGVFIFVGVEPKSELVADLCDL--DQAGYIKIDH-NGLTSYPGLYAAGDV 282
Cdd:COG0493 338 GEPdesgrrrpvpiegsEFTLPADLVILAIGQTPDPSGLEEELGLelDKRGTIVVDEeTYQTSLPGVFAGGDA 410
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
73-283 |
5.94e-14 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 71.71 E-value: 5.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 73 AEKFGAEFRTFAAIEKIEPQGidFLLTDSEGAQVVAHAVILATGAVPKRLGVPG-EAE--FTGRGVSWCATCDGAFFRDK 149
Cdd:COG1251 66 YEENGIDLRLGTRVTAIDRAA--RTVTLADGETLPYDKLVLATGSRPRVPPIPGaDLPgvFTLRTLDDADALRAALAPGK 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 150 VVAVIGGG----DAAveEAlfLTKFASKVHIVHRRDEL-------RATKCIQEKcFANEKIAFELSRVVSEVVGEnGKVT 218
Cdd:COG1251 144 RVVVIGGGliglEAA--AA--LRKRGLEVTVVERAPRLlprqldeEAGALLQRL-LEALGVEVRLGTGVTEIEGD-DRVT 217
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1309179808 219 GIKLAStkGDpelLLPLDGVFIFVGVEPKSELVADlCDLDQAGYIKIDHNGLTSYPGLYAAGDVT 283
Cdd:COG1251 218 GVRLAD--GE---ELPADLVVVAIGVRPNTELARA-AGLAVDRGIVVDDYLRTSDPDIYAAGDCA 276
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
16-283 |
2.00e-12 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 67.51 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 16 PAGLTAALYSSRARAKTVVFESGLPGG-----------------QIVTTdwVENYPGFpdGISGMEIG----DLMHR-QA 73
Cdd:PRK06292 13 PAGYVAARRAAKLGKKVALIEKGPLGGtclnvgcipskaliaaaEAFHE--AKHAEEF--GIHADGPKidfkKVMARvRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 74 EKfgAEFRTFAAIEKIEPQGIDFL-----LTDS-----EGAQVVAHAVILATGA-VPKrlgVPGEAEFTGRGVswcATCD 142
Cdd:PRK06292 89 ER--DRFVGGVVEGLEKKPKIDKIkgtarFVDPntvevNGERIEAKNIVIATGSrVPP---IPGVWLILGDRL---LTSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 143 GAFFRDKV---VAVIGGGDAAVEEALFLTKFASKVHIVHRRDEL----------RATKCIQEKcfanekIAFEL-SRVVS 208
Cdd:PRK06292 161 DAFELDKLpksLAVIGGGVIGLELGQALSRLGVKVTVFERGDRIlpledpevskQAQKILSKE------FKIKLgAKVTS 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1309179808 209 EVVGENGKVTGIKlastKGDPELLLPLDGVFIFVGVEPKSELV----ADLcDLDQAGYIKIDHNGLTSYPGLYAAGDVT 283
Cdd:PRK06292 235 VEKSGDEKVEELE----KGGKTETIEADYVLVATGRRPNTDGLglenTGI-ELDERGRPVVDEHTQTSVPGIYAAGDVN 308
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
151-225 |
4.84e-12 |
|
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: 60.68 E-value: 4.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 151 VAVIGGGDAAVEEALFLTKFASKVHIVHRRDELR------ATKCIQEKcFANEKIAFELSRVVSEVVGeNGKVTGIKLAS 224
Cdd:pfam00070 2 VVVVGGGYIGLELAGALARLGSKVTVVERRDRLLpgfdpeIAKILQEK-LEKNGIEFLLNTTVEAIEG-NGDGVVVVLTD 79
|
.
gi 1309179808 225 T 225
Cdd:pfam00070 80 G 80
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
16-287 |
1.95e-11 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 64.41 E-value: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 16 PAGLTAALYSSRARAKTVVFE-SGLPGGqIVTtdwvenYpgfpdGISGMEI-GDLMHR---QAEKFGAEFRTFAAIekie 90
Cdd:PRK12810 153 PAGLAAADQLARAGHKVTVFErADRIGG-LLR------Y-----GIPDFKLeKEVIDRrieLMEAEGIEFRTNVEV---- 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 91 pqGIDF----LLTDSEgaqvvahAVILATGA-VPKRLGVPGEaEFTG---------------RGVSWCATCDgafFRDKV 150
Cdd:PRK12810 217 --GKDItaeeLLAEYD-------AVFLGTGAyKPRDLGIPGR-DLDGvhfamdfliqntrrvLGDETEPFIS---AKGKH 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 151 VAVIGGGDAAV--------EEAlfltkfASkvhiVHRRDE-----LRATKCIQEKCFAN---------EKIAFELSRVVS 208
Cdd:PRK12810 284 VVVIGGGDTGMdcvgtairQGA------KS----VTQRDImpmppSRRNKNNPWPYWPMklevsnaheEGVEREFNVQTK 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 209 EVVGENGKVTGIKLASTK---GDP------ELLLPLDGVFI---FVGVEPksELVADL-CDLDQAGYIKIDHNGL-TSYP 274
Cdd:PRK12810 354 EFEGENGKVTGVKVVRTElgeGDFepvegsEFVLPADLVLLamgFTGPEA--GLLAQFgVELDERGRVAAPDNAYqTSNP 431
|
330
....*....|....
gi 1309179808 275 GLYAAGD-VTDSDL 287
Cdd:PRK12810 432 KVFAAGDmRRGQSL 445
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
17-284 |
1.08e-10 |
|
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: 62.05 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 17 AGLTAALYSSRARAKTVVFESGLPGGQIVTTDWV---------ENYPGF---PDGISGMEI----GDLMhRQAEKFGAEF 80
Cdd:TIGR02053 11 AAFAAAIKAAELGASVAMVERGPLGGTCVNVGCVpskmllraaEVAHYArkpPFGGLAATVavdfGELL-EGKREVVEEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 81 RTFAAIEKIEPQGIDFLL------------TDSEGAQVVAHAVILATGAVPKRLGVPG--EAEFTgrgvswcaTCDGAFF 146
Cdd:TIGR02053 90 RHEKYEDVLSSYGVDYLRgrarfkdpktvkVDLGREVRGAKRFLIATGARPAIPPIPGlkEAGYL--------TSEEALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 147 RDKV---VAVIGGGDAAVEEALFLTKFASKVHIVHR------RDELRATKCIQEkCFANEKIAFELSRVVSEVVGENGkv 217
Cdd:TIGR02053 162 LDRIpesLAVIGGGAIGVELAQAFARLGSEVTILQRsdrllpREEPEISAAVEE-ALAEEGIEVVTSAQVKAVSVRGG-- 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1309179808 218 tGIKLASTKGDPELLLPLDGVFIFVGVEPkselVADLCDLDQAGyIKIDHNG--------LTSYPGLYAAGDVTD 284
Cdd:TIGR02053 239 -GKIITVEKPGGQGEVEADELLVATGRRP----NTDGLGLEKAG-VKLDERGgilvdetlRTSNPGIYAAGDVTG 307
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
111-283 |
1.20e-10 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 62.09 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 111 VILATGAVPKRLgvPGeAEFTGRGVswcATCDGAFFRDKV---VAVIGGGDAAVEEALFLTKFASKVHIVHRRDELRA-- 185
Cdd:PRK06416 138 IILATGSRPREL--PG-IEIDGRVI---WTSDEALNLDEVpksLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILPge 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 186 ----TKcIQEKCFANEKIAFELSRVVSEVV-GENGkvtgIKLASTKGDPELLLPLDGVFIFVGVEPKSElvaDLcDLDQA 260
Cdd:PRK06416 212 dkeiSK-LAERALKKRGIKIKTGAKAKKVEqTDDG----VTVTLEDGGKEETLEADYVLVAVGRRPNTE---NL-GLEEL 282
|
170 180
....*....|....*....|....*....
gi 1309179808 261 ------GYIKIDHNGLTSYPGLYAAGDVT 283
Cdd:PRK06416 283 gvktdrGFIEVDEQLRTNVPNIYAIGDIV 311
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
103-284 |
1.55e-10 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 61.71 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 103 GAQVVAHAVILATGAVPKRLGVPGeAEFtgrgvswCATCDGAFFRDKV---VAVIGGGDAAVEEALFLTKFASKVHIVHR 179
Cdd:PRK06116 127 GERYTADHILIATGGRPSIPDIPG-AEY-------GITSDGFFALEELpkrVAVVGAGYIAVEFAGVLNGLGSETHLFVR 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 180 RDE-LRA-----TKCIQEkCFANEKIAFELSRVVSEVV-GENGKVTgIKLASTKgdpelLLPLDGVFIFVGVEPKSE--- 249
Cdd:PRK06116 199 GDApLRGfdpdiRETLVE-EMEKKGIRLHTNAVPKAVEkNADGSLT-LTLEDGE-----TLTVDCLIWAIGREPNTDglg 271
|
170 180 190
....*....|....*....|....*....|....*
gi 1309179808 250 LVADLCDLDQAGYIKIDHNGLTSYPGLYAAGDVTD 284
Cdd:PRK06116 272 LENAGVKLNEKGYIIVDEYQNTNVPGIYAVGDVTG 306
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
110-282 |
5.55e-10 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 59.62 E-value: 5.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 110 AVILATGA-VPKRLGVPGE--------AEFTGR-------GVSWCATCDgafFRDKVVAVIGGG----DAAVEEALfltK 169
Cdd:PRK12770 121 AVLIATGTwKSRKLGIPGEdlpgvysaLEYLFRiraaklgYLPWEKVPP---VEGKKVVVVGAGltavDAALEAVL---L 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 170 FASKVHIVHRR--DELRATKCIQEKCFANEKIAFELSRVVsEVVGEnGKVTGIKLASTK-GDP--------------ELL 232
Cdd:PRK12770 195 GAEKVYLAYRRtiNEAPAGKYEIERLIARGVEFLELVTPV-RIIGE-GRVEGVELAKMRlGEPdesgrprpvpipgsEFV 272
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1309179808 233 LPLDGVFIFVGVEPKSELVADLCD--LDQAGYIKIDHNGLTSYPGLYAAGDV 282
Cdd:PRK12770 273 LEADTVVFAIGEIPTPPFAKECLGieLNRKGEIVVDEKHMTSREGVFAAGDV 324
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
16-280 |
9.42e-10 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 58.39 E-value: 9.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 16 PAGLTAALYSSRARAKT-VVFESGLPG---------GQIVTTDWVENYPGFPD-----------------GISGMEIGDL 68
Cdd:pfam13738 1 PAGIGCAIALKKAGLEDyLILEKGNIGnsfyrypthMTFFSPSFTSNGFGIPDlnaispgtspaftfnreHPSGNEYAEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 69 MHRQAEKFGAEFRTFAAIEKIEPQGIDFLLTDSEGaQVVAHAVILATG--AVPKRLGVPGEAEFTGRGVSWcatcdgAFF 146
Cdd:pfam13738 81 LRRVADHFELPINLFEEVTSVKKEDDGFVVTTSKG-TYQARYVIIATGefDFPNKLGVPELPKHYSYVKDF------HPY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 147 RDKVVAVIGGGDAAVEEALFLTKFASKVHIVHRRDELRA------------TKCIQEKCFANEKIAFELSRVVSEVVGEN 214
Cdd:pfam13738 154 AGQKVVVIGGYNSAVDAALELVRKGARVTVLYRGSEWEDrdsdpsyslspdTLNRLEELVKNGKIKAHFNAEVKEITEVD 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1309179808 215 GKVtgiKLASTKGDPellLPLDGVFIF-VGVEP-KSELVADLCDLDQAGYIKIDHNGL-TSYPGLYAAG 280
Cdd:pfam13738 234 VSY---KVHTEDGRK---VTSNDDPILaTGYHPdLSFLKKGLFELDEDGRPVLTEETEsTNVPGLFLAG 296
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
90-286 |
2.41e-09 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 58.30 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 90 EPQGIDFLL------TDSEGAQVVAHA--------VILATGAVPKRLGVPG---EAEFTGRGVSWCATCDGAFFRDKVVA 152
Cdd:TIGR02374 65 EKHGITLYTgetviqIDTDQKQVITDAgrtlsydkLILATGSYPFILPIPGadkKGVYVFRTIEDLDAIMAMAQRFKKAA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 153 VIGGGDAAVEEALFLTKFASKVHIVHRRDELRATKCIQ------EKCFANEKIAFELSRVVSEVVGEnGKVTGIKLASTK 226
Cdd:TIGR02374 145 VIGGGLLGLEAAVGLQNLGMDVSVIHHAPGLMAKQLDQtagrllQRELEQKGLTFLLEKDTVEIVGA-TKADRIRFKDGS 223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 227 GdpellLPLDGVFIFVGVEPKSELVADlCDLDQAGYIKIDHNGLTSYPGLYAAGDVTDSD 286
Cdd:TIGR02374 224 S-----LEADLIVMAAGIRPNDELAVS-AGIKVNRGIIVNDSMQTSDPDIYAVGECAEHN 277
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
89-284 |
2.84e-09 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 57.90 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 89 IEPQGIDFLLTDSEGAQVVAHAVILATGAVPKRLGVPGEaeftgrgvSWCATCDGAFFRD---KVVAVIGGGDAAVEEAL 165
Cdd:PLN02507 149 VGPNEVEVTQLDGTKLRYTAKHILIATGSRAQRPNIPGK--------ELAITSDEALSLEelpKRAVVLGGGYIAVEFAS 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 166 FLTKFASKVHIVHRR--------DELRAtkcIQEKCFANEKIAFELSRVVSEVVGENGkvtGIKLASTKGDpELLLplDG 237
Cdd:PLN02507 221 IWRGMGATVDLFFRKelplrgfdDEMRA---VVARNLEGRGINLHPRTNLTQLTKTEG---GIKVITDHGE-EFVA--DV 291
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1309179808 238 VFIFVGVEPKSE---LVADLCDLDQAGYIKIDHNGLTSYPGLYAAGDVTD 284
Cdd:PLN02507 292 VLFATGRAPNTKrlnLEAVGVELDKAGAVKVDEYSRTNIPSIWAIGDVTN 341
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
16-282 |
7.02e-09 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 56.67 E-value: 7.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 16 PAGLTAALYSSRARAKTVVFES-GLPGGqivttdwVENY--PGF--PDGISGMEIGDLMhrqaeKFGAEFRT------FA 84
Cdd:PRK12778 441 PAGLSFAGDLAKRGYDVTVFEAlHEIGG-------VLKYgiPEFrlPKKIVDVEIENLK-----KLGVKFETdvivgkTI 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 85 AIEKIEPQGIDflltdsegaqvvahAVILATGA-VPKRLGVPGE--------AEFTGRgvswcATCDGAFFRD------- 148
Cdd:PRK12778 509 TIEELEEEGFK--------------GIFIASGAgLPNFMNIPGEnsngvmssNEYLTR-----VNLMDAASPDsdtpikf 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 149 -KVVAVIGGGDAAVEEALFLTKF-ASKVHIVHRRDELRATKCIQEKCFANEK-IAF-ELSRVVSEVVGENGKVTGIKLAS 224
Cdd:PRK12778 570 gKKVAVVGGGNTAMDSARTAKRLgAERVTIVYRRSEEEMPARLEEVKHAKEEgIEFlTLHNPIEYLADEKGWVKQVVLQK 649
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1309179808 225 TK-GDP--------------ELLLPLDGVFIFVGVEPkSELVADLC---DLDQAGYIKIDHNGLTSYPGLYAAGDV 282
Cdd:PRK12778 650 MElGEPdasgrrrpvaipgsTFTVDVDLVIVSVGVSP-NPLVPSSIpglELNRKGTIVVDEEMQSSIPGIYAGGDI 724
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
101-283 |
1.43e-07 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 52.44 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 101 SEGAQVVAHAVILATGAVPKRLGVPGEAE----FTGRGVSWCATcdgaffRDKVVAVIGGGDAAVEEALFLTKFASKVHI 176
Cdd:PRK07251 112 DEKIELTAETIVINTGAVSNVLPIPGLADskhvYDSTGIQSLET------LPERLGIIGGGNIGLEFAGLYNKLGSKVTV 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 177 VHRRDEL--RATKCIQEkcFANE-----KIAFELSRVVSEVVGENGKVtgikLASTKGDPELLlplDGVFIFVGVEPKSE 249
Cdd:PRK07251 186 LDAASTIlpREEPSVAA--LAKQymeedGITFLLNAHTTEVKNDGDQV----LVVTEDETYRF---DALLYATGRKPNTE 256
|
170 180 190
....*....|....*....|....*....|....*...
gi 1309179808 250 LVA----DLcDLDQAGYIKIDHNGLTSYPGLYAAGDVT 283
Cdd:PRK07251 257 PLGlentDI-ELTERGAIKVDDYCQTSVPGVFAVGDVN 293
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
16-287 |
2.10e-07 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 52.04 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 16 PAGLTAALYSSRARAKTVVFESG-LPGGQIvttdwveNY--PGF--PDGISGMEIGDLmhrqaEKFGAEFR---TFaaie 87
Cdd:PRK12814 203 PAGLTAAYYLLRKGHDVTIFDANeQAGGMM-------RYgiPRFrlPESVIDADIAPL-----RAMGAEFRfntVF---- 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 88 kiepqGIDFLLtdsEGAQVVAHAVILATGA-VPKRLGVPGEAEftgRGVswcaTCDGAFFRD----------KVVAVIGG 156
Cdd:PRK12814 267 -----GRDITL---EELQKEFDAVLLAVGAqKASKMGIPGEEL---PGV----ISGIDFLRNvalgtalhpgKKVVVIGG 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 157 GDAAVEEA-LFLTKFASKVHIVHRR--DELRATKCIQEKCFAnEKIAF-ELSRVVSEVVGENG-KVTGIKL------AST 225
Cdd:PRK12814 332 GNTAIDAArTALRLGAESVTILYRRtrEEMPANRAEIEEALA-EGVSLrELAAPVSIERSEGGlELTAIKMqqgepdESG 410
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1309179808 226 KGDP------ELLLPLDGVFIFVG--VEPKSELVADLcDLDQAGYIKIDHNGL-TSYPGLYAAGD-VTDSDL 287
Cdd:PRK12814 411 RRRPvpvegsEFTLQADTVISAIGqqVDPPIAEAAGI-GTSRNGTVKVDPETLqTSVAGVFAGGDcVTGADI 481
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
152-282 |
2.59e-07 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 51.74 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 152 AVIGGGDAAVEEALFLTKFASKVHIVHR------RDELRATKCIQEKcFANEKIAFELSRVVSEVVGENGKVTgIKLAST 225
Cdd:PRK06370 175 VIIGGGYIGLEFAQMFRRFGSEVTVIERgprllpREDEDVAAAVREI-LEREGIDVRLNAECIRVERDGDGIA-VGLDCN 252
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1309179808 226 KGDPELllPLDGVFIFVGVEPKSElvaDLcDLDQAG-------YIKIDHNGLTSYPGLYAAGDV 282
Cdd:PRK06370 253 GGAPEI--TGSHILVAVGRVPNTD---DL-GLEAAGvetdargYIKVDDQLRTTNPGIYAAGDC 310
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
98-284 |
4.51e-07 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 50.92 E-value: 4.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 98 LTDSEGAQVVAHAVILATGAVPKRLGVPGEAEFTgrgvSWCATcdGAFFRDKV---VAVIGGGDAAVEEALFLTKFASKV 174
Cdd:PRK13748 223 LNDGGERVVAFDRCLIATGASPAVPPIPGLKETP----YWTST--EALVSDTIperLAVIGSSVVALELAQAFARLGSKV 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 175 HIVHRRDEL-RATKCIQEK---CFANEKIAFELSRVVSEVVGENGKVTgikLASTKGDpellLPLDGVFIFVGVEPKS-- 248
Cdd:PRK13748 297 TILARSTLFfREDPAIGEAvtaAFRAEGIEVLEHTQASQVAHVDGEFV---LTTGHGE----LRADKLLVATGRAPNTrs 369
|
170 180 190
....*....|....*....|....*....|....*..
gi 1309179808 249 -ELVADLCDLDQAGYIKIDHNGLTSYPGLYAAGDVTD 284
Cdd:PRK13748 370 lALDAAGVTVNAQGAIVIDQGMRTSVPHIYAAGDCTD 406
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
147-292 |
8.89e-07 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 50.13 E-value: 8.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 147 RDKVVAVIGGGDAA---VEEALflTKFASKVHIVHRRDELRATKCIQE-KCFANEKIAFELS-RVVSEVVGENGKVTGIK 221
Cdd:PRK12769 467 AGLNVVVLGGGDTAmdcVRTAL--RHGASNVTCAYRRDEANMPGSKKEvKNAREEGANFEFNvQPVALELNEQGHVCGIR 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 222 LASTK-GDP--------------ELLLPLDGVFIFVGVEPKSE--LVADLCDLDQAGYIKIDHNG----LTSYPGLYAAG 280
Cdd:PRK12769 545 FLRTRlGEPdaqgrrrpvpipgsEFVMPADAVIMAFGFNPHGMpwLESHGVTVDKWGRIIADVESqyryQTSNPKIFAGG 624
|
170
....*....|...
gi 1309179808 281 D-VTDSDLkqVIT 292
Cdd:PRK12769 625 DaVRGADL--VVT 635
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
14-180 |
4.13e-06 |
|
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];
Pssm-ID: 441675 [Multi-domain] Cd Length: 414 Bit Score: 47.94 E-value: 4.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 14 GGPAGLTAALYSSRARAKTVVFE-SGLPGG----------QIVTTDWVENYPGFPDG------ISGMEIGDLMHRQAEKF 76
Cdd:COG2072 14 AGQAGLAAAYHLRRAGIDFVVLEkADDVGGtwrdnrypglRLDTPSHLYSLPFFPNWsddpdfPTGDEILAYLEAYADKF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 77 GA----EFRTfaAIEKIEPQGID--FLLTDSEGAQVVAHAVILATGA--VPKRLGVPGEAEFTGR---GVSWCATCDgaf 145
Cdd:COG2072 94 GLrrpiRFGT--EVTSARWDEADgrWTVTTDDGETLTARFVVVATGPlsRPKIPDIPGLEDFAGEqlhSADWRNPVD--- 168
|
170 180 190
....*....|....*....|....*....|....*
gi 1309179808 146 FRDKVVAVIGGGDAAVEEALFLTKFASKVHIVHRR 180
Cdd:COG2072 169 LAGKRVLVVGTGASAVQIAPELARVAAHVTVFQRT 203
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
108-284 |
7.87e-06 |
|
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: 47.27 E-value: 7.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 108 AHAVILATGAVPKRLGVPgeaeftgrGVSWCATCDGAFFRD---KVVAVIGGGDAAVEEALFLTKF---ASKVHIvhrrd 181
Cdd:TIGR01423 152 AEHILLATGSWPQMLGIP--------GIEHCISSNEAFYLDeppRRVLTVGGGFISVEFAGIFNAYkprGGKVTL----- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 182 elratkciqekCFANEKIAFELSRVVSEVVGENGKVTGIKLASTKGDPELLLPLDG----------------VFIFVGVE 245
Cdd:TIGR01423 219 -----------CYRNNMILRGFDSTLRKELTKQLRANGINIMTNENPAKVTLNADGskhvtfesgktldvdvVMMAIGRV 287
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1309179808 246 PKS---ELVADLCDLDQAGYIKIDHNGLTSYPGLYAAGDVTD 284
Cdd:TIGR01423 288 PRTqtlQLDKVGVELTKKGAIQVDEFSRTNVPNIYAIGDVTD 329
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
100-291 |
1.04e-05 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 46.92 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 100 DSEGAQVVAHAVILATGAVPKRLGVPGEaEFTgrgvswcATCDGaFFR---DKVVAVIGGGDAAVEEALFLTKFASKVHI 176
Cdd:PTZ00058 195 LDDGQVIEGKNILIAVGNKPIFPDVKGK-EFT-------ISSDD-FFKikeAKRIGIAGSGYIAVELINVVNRLGAESYI 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 177 VHRRDELRATkciqekcfANEKIAFELS--------RVVSE-VVGENGKVTGIKLASTKGDPELLLPLDGVFIFVGVEPK 247
Cdd:PTZ00058 266 FARGNRLLRK--------FDETIINELEndmkknniNIITHaNVEEIEKVKEKNLTIYLSDGRKYEHFDYVIYCVGRSPN 337
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1309179808 248 SELVA--DLCDLDQAGYIKIDHNGLTSYPGLYAAGDVTDSDLKQVI 291
Cdd:PTZ00058 338 TEDLNlkALNIKTPKGYIKVDDNQRTSVKHIYAVGDCCMVKKNQEI 383
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
15-282 |
1.07e-05 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 46.86 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 15 GPAGLTAALYSSRARAKTVVFES-GLPGGqivttdwVENYpGFPDGISGMEIGDLMHRQAEKFGAEFRTFAAIEKIEPqg 93
Cdd:PRK12775 439 GPAGLAAAADLVKYGVDVTVYEAlHVVGG-------VLQY-GIPSFRLPRDIIDREVQRLVDIGVKIETNKVIGKTFT-- 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 94 IDFLLTDSEgaqvvAHAVILATGA-VPKRLGVPGEA--------EFTGR----GVSWCATCDGAFFRDKVVAVIGGGDAA 160
Cdd:PRK12775 509 VPQLMNDKG-----FDAVFLGVGAgAPTFLGIPGEFagqvysanEFLTRvnlmGGDKFPFLDTPISLGKSVVVIGAGNTA 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 161 VeEALFLTKF--ASKVHIVHRRDELRATKCIQEKCFANEKIA--FELSRVVSEVVGENGKVTGIKLASTK-GDPE----- 230
Cdd:PRK12775 584 M-DCLRVAKRlgAPTVRCVYRRSEAEAPARIEEIRHAKEEGIdfFFLHSPVEIYVDAEGSVRGMKVEEMElGEPDekgrr 662
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1309179808 231 --------LLLPLDGVFIFVGVEPK---SELVADLCdLDQAGYIKIDHNGL-----TSYPGLYAAGDV 282
Cdd:PRK12775 663 kpmptgefKDLECDTVIYALGTKANpiiTQSTPGLA-LNKWGNIAADDGKLestqsTNLPGVFAGGDI 729
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
149-281 |
1.83e-05 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 45.80 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 149 KVVAVIGGGDAAVEEALFLTKFASKVHIVHRRDEL-------RATKCIQEKCFANEkIAFELSRVVSEVVGENgKVTGIK 221
Cdd:PRK09564 150 KNIVIIGAGFIGLEAVEAAKHLGKNVRIIQLEDRIlpdsfdkEITDVMEEELRENG-VELHLNEFVKSLIGED-KVEGVV 227
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1309179808 222 laSTKGDPELllplDGVFIFVGVEPKSELVADLC-DLDQAGYIKIDHNGLTSYPGLYAAGD 281
Cdd:PRK09564 228 --TDKGEYEA----DVVIVATGVKPNTEFLEDTGlKTLKNGAIIVDEYGETSIENIYAAGD 282
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
111-290 |
5.68e-05 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 44.39 E-value: 5.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 111 VILATGAVPKRLGVPGEAEFTGRGVSWCATCDGAFFRDKV--VAVIGGGDAAVEEALFLTKFASKVHIVHRRDELratkc 188
Cdd:PRK13512 109 LILSPGASANSLGFESDITFTLRNLEDTDAIDQFIKANQVdkALVVGAGYISLEVLENLYERGLHPTLIHRSDKI----- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 189 iqekcfaNEKIAFELSRVVSEVVGENG----------KVTGIKLASTKGDPElllPLDGVFIFVGVEPKSELVADL-CDL 257
Cdd:PRK13512 184 -------NKLMDADMNQPILDELDKREipyrlneeidAINGNEVTFKSGKVE---HYDMIIEGVGTHPNSKFIESSnIKL 253
|
170 180 190
....*....|....*....|....*....|...
gi 1309179808 258 DQAGYIKIDHNGLTSYPGLYAAGDVTDSDLKQV 290
Cdd:PRK13512 254 DDKGFIPVNDKFETNVPNIYAIGDIITSHYRHV 286
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
80-283 |
6.45e-05 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 44.15 E-value: 6.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 80 FRTFAAIEKIEPQGIDFLLTDSEGAQVVAHAVILATGAVPKRLgvPGeAEFTGRGVswcATCDGAFFRDKV---VAVIGG 156
Cdd:PRK06327 118 LKGRGSFVGKTDAGYEIKVTGEDETVITAKHVIIATGSEPRHL--PG-VPFDNKII---LDNTGALNFTEVpkkLAVIGA 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 157 GDAAVEEALFLTKFASKVHIVHRRDELRATKCIQ-----EKCFANEKIAFELSRVVSEV-VGENGkVTgIKLASTKGDPE 230
Cdd:PRK06327 192 GVIGLELGSVWRRLGAEVTILEALPAFLAAADEQvakeaAKAFTKQGLDIHLGVKIGEIkTGGKG-VS-VAYTDADGEAQ 269
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1309179808 231 LLlPLDGVFIFVGVEPKSE-LVADLC--DLDQAGYIKIDHNGLTSYPGLYAAGDVT 283
Cdd:PRK06327 270 TL-EVDKLIVSIGRVPNTDgLGLEAVglKLDERGFIPVDDHCRTNVPNVYAIGDVV 324
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
16-282 |
6.90e-05 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 44.10 E-value: 6.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 16 PAGLTAALYSSRARAKTVVFESG-LPGGQIvttdwveNY--PG--FPDGISGMEIGDLmhrqaEKFGAEFRTFAAIekie 90
Cdd:PRK12771 147 PAGLSAAYHLRRMGHAVTIFEAGpKLGGMM-------RYgiPAyrLPREVLDAEIQRI-----LDLGVEVRLGVRV---- 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 91 pqGIDFLLTDSEGAQvvaHAVILATGA-VPKRLGVPGEAefTGRGVSwcATcdgAFFRD----------KVVAVIGGGDA 159
Cdd:PRK12771 211 --GEDITLEQLEGEF---DAVFVAIGAqLGKRLPIPGED--AAGVLD--AV---DFLRAvgegeppflgKRVVVIGGGNT 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 160 AVEEA-LFLTKFASKVHIVHRRDELRATkciqekCFAN-------EKIAFELSRVVSEVVGENGKVTGIKLA-------- 223
Cdd:PRK12771 279 AMDAArTARRLGAEEVTIVYRRTREDMP------AHDEeieealrEGVEINWLRTPVEIEGDENGATGLRVItvekmeld 352
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1309179808 224 -----STKGDPELLLPLDGVFIFVGVEPKSELVADL-CDLDQAGYIKIDHNGL-TSYPGLYAAGDV 282
Cdd:PRK12771 353 edgrpSPVTGEEETLEADLVVLAIGQDIDSAGLESVpGVEVGRGVVQVDPNFMmTGRPGVFAGGDM 418
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
102-311 |
1.33e-04 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 43.48 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 102 EGAQVVAHAVILATGAVPKRLGVPGEAEFTGRGVswcatcdgaffRDKVVAVIGGGDAAVE-EALFLTKFASKVHIVHRR 180
Cdd:PRK12809 416 EDAPGVIQALPFLTAHTRQLMGLPESEEYPLTDV-----------EGKRVVVLGGGDTTMDcLRTSIRLNAASVTCAYRR 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 181 DELRATKCIQEKCFANEK-IAFELS-RVVSEVVGENGKVTGIKLASTK-GDP--------------ELLLPLDGVFIFVG 243
Cdd:PRK12809 485 DEVSMPGSRKEVVNAREEgVEFQFNvQPQYIACDEDGRLTAVGLIRTAmGEPgpdgrrrprpvagsEFELPADVLIMAFG 564
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1309179808 244 VEPKSE--LVADLCDLDQAGYIKIDHNGL----TSYPGLYAAGD-VTDSDLkqVITAAAKGASAAFEALRWIDER 311
Cdd:PRK12809 565 FQAHAMpwLQGSGIKLDKWGLIQTGDVGYlptqTHLKKVFAGGDaVHGADL--VVTAMAAGRQAARDMLTLFDTK 637
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
87-282 |
1.37e-04 |
|
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: 43.30 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 87 EKIEPQGIDFLLTDSEGAQVVAHAVILATGAVPKRLGVPGEAEFtgrgvswCATCDGAFFRDKV---VAVIGGGDAAVEE 163
Cdd:TIGR01438 123 EFVDKHRIKATNKKGKEKIYSAERFLIATGERPRYPGIPGAKEL-------CITSDDLFSLPYCpgkTLVVGASYVALEC 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 164 ALFLTKFASKVHIVHRRDELRAtkcIQEKC--FANEKIAFELSRVVSEVVGEngKVTGI----KLASTKGDPELLLPLDG 237
Cdd:TIGR01438 196 AGFLAGIGLDVTVMVRSILLRG---FDQDCanKVGEHMEEHGVKFKRQFVPI--KVEQIeakvLVEFTDSTNGIEEEYDT 270
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1309179808 238 VFIFVGVEPKSelvaDLCDLDQAGY--------IKIDHNGLTSYPGLYAAGDV 282
Cdd:TIGR01438 271 VLLAIGRDACT----RKLNLENVGVkinkktgkIPADEEEQTNVPYIYAVGDI 319
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
151-290 |
3.24e-04 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 42.25 E-value: 3.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 151 VAVIGGGDAAVEEALFLTKFASKVHIVHRRDELrATKCIQEKCFANEKIA---FELsRVVSEVVGENGKVTGIKLASTKG 227
Cdd:PRK07846 169 LVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRL-LRHLDDDISERFTELAskrWDV-RLGRNVVGVSQDGSGVTLRLDDG 246
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1309179808 228 DPellLPLDGVFIFVGVEPKSELVaDL----CDLDQAGYIKIDHNGLTSYPGLYAAGDV-TDSDLKQV 290
Cdd:PRK07846 247 ST---VEADVLLVATGRVPNGDLL-DAaaagVDVDEDGRVVVDEYQRTSAEGVFALGDVsSPYQLKHV 310
|
|
| YhiN |
COG2081 |
Predicted flavoprotein YhiN [General function prediction only]; |
16-170 |
1.57e-03 |
|
Predicted flavoprotein YhiN [General function prediction only];
Pssm-ID: 441684 [Multi-domain] Cd Length: 402 Bit Score: 39.65 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 16 PAGLTAALYSSRARAKTVVFE-----------SG---------LPGGQIV---------------------TTDWVENYp 54
Cdd:COG2081 7 AAGLMAAITAAERGARVLLLEknpkvgrkiliSGggrcnftnsEPLPEFLnyyggnphflksalsrftpedLIAFFEGL- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 55 G-----------FPDGISGMEIGDLMHRQAEKFGAEFRTFAAIEKIEPQGIDFLLTDSEGAQVVAHAVILATG--AVPK- 120
Cdd:COG2081 86 GietkeessgrvFPDSSKASDILRALLAELREAGVEIRLRTRVTGIEKEDGGFGVETPDGETVRADAVVLATGglSYPKl 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1309179808 121 -----------RLGV------PGEAEFTGRGvSWCATCDGAFFRDKVVAVIGGGDAAVEEALFLTKF 170
Cdd:COG2081 166 gstgdgyrlaeQFGHtitplrPALVPLTLSE-HFFKRLAGLSLKNVALSVGGKKIASFRGELLFTHR 231
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
17-282 |
4.59e-03 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 38.19 E-value: 4.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 17 AGLTAALYSSRARAKTVvfesglpggQIVttdWVE--NY----PGFPDGISG-MEIGDLMH---RQAEKFGAEFRTfAAI 86
Cdd:COG1252 12 AGLEAARRLRKKLGGDA---------EVT---LIDpnPYhlfqPLLPEVAAGtLSPDDIAIplrELLRRAGVRFIQ-GEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 87 EKIEPQGiDFLLTDSeGAQVVAHAVILATGAVPKRLGVPGEAEFTgrgVSWCATCDGAFFRDKV--------------VA 152
Cdd:COG1252 79 TGIDPEA-RTVTLAD-GRTLSYDYLVIATGSVTNFFGIPGLAEHA---LPLKTLEDALALRERLlaaferaerrrlltIV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 153 VIGGGDAAVEEALFLTKFASK-------------VHIVHRRDEL--RATKCIQEKC---FANEKIAFELSRVVSEVVGEn 214
Cdd:COG1252 154 VVGGGPTGVELAGELAELLRKllrypgidpdkvrITLVEAGPRIlpGLGEKLSEAAekeLEKRGVEVHTGTRVTEVDAD- 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179808 215 gkvtGIKLASTKgdpelLLPLDGVFIFVGVEPkSELVADL-CDLDQAGYIKID-HNGLTSYPGLYAAGDV 282
Cdd:COG1252 233 ----GVTLEDGE-----EIPADTVIWAAGVKA-PPLLADLgLPTDRRGRVLVDpTLQVPGHPNVFAIGDC 292
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
257-284 |
7.68e-03 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 37.92 E-value: 7.68e-03
10 20
....*....|....*....|....*...
gi 1309179808 257 LDQAGYIKIDHNGLTSYPGLYAAGDVTD 284
Cdd:PRK07845 288 LTPSGHITVDRVSRTSVPGIYAAGDCTG 315
|
|
| |
