|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
1-405 |
0e+00 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 674.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 1 MSWSWGpvgvlTASYVRDVDHSKYKVTVVSPRDHMLFTPLLASTTVGTLEHRSIIEPVRPQAAKNGWRYLQAEATNLDLQ 80
Cdd:PTZ00318 16 LGTGWA-----GAYFVRNLDPKKYNITVISPRNHMLFTPLLPQTTTGTLEFRSICEPVRPALAKLPNRYLRAVVYDVDFE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 81 QQRITCRMSSLHVSGVQKDTVIDYNHLVVAIGAQPHTLNVPGVDEsRVFFLKETEHARNIRSHIHDCLEAASNTTLSPEV 160
Cdd:PTZ00318 91 EKRVKCGVVSKSNNANVNTFSVPYDKLVVAHGARPNTFNIPGVEE-RAFFLKEVNHARGIRKRIVQCIERASLPTTSVEE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 161 RRRLTTFCVVGGGPTGVEFAAELSDFLEQDAARLYPELTMLPQVIIFEAGTSILGSFDQALSEYGLMRMKRQHVDIRLQT 240
Cdd:PTZ00318 170 RKRLLHFVVVGGGPTGVEFAAELADFFRDDVRNLNPELVEECKVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVDIRTKT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 241 QVKEVKDQSLVLSTGEEVNTSTIVWSTGVAPRSLVQQLDAKHKSNGSIGVDECLQIQEAQNAYALGDCASLERR-LPTVA 319
Cdd:PTZ00318 250 AVKEVLDKEVVLKDGEVIPTGLVVWSTGVGPGPLTKQLKVDKTSRGRISVDDHLRVKPIPNVFALGDCAANEERpLPTLA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 320 QVAEQQGAYLARHFNQNFS---SAKPFAFASKGMLAYLGSYGG------VKLSGFKAWLVWRGGYLTKLGTWRSRLQVPF 390
Cdd:PTZ00318 330 QVASQQGVYLAKEFNNELKgkpMSKPFVYRSLGSLAYLGNYSAivqlgaFDLSGFKALLFWRSAYLTILGSWRSKLYVLV 409
|
410
....*....|....*
gi 167517391 391 DWAKTMFFGRDPARF 405
Cdd:PTZ00318 410 NWAGTAIFGRDITRF 424
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
6-390 |
1.44e-94 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 288.57 E-value: 1.44e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 6 GPVGVLTASYVRDVDHSKYKVTVVSPRDHMLFTPLLASTTVGTLEHRSIIEPVRPQAAKNGWRYLQAEATNLDLQQQRIT 85
Cdd:COG1252 10 GFAGLEAARRLRKKLGGDAEVTLIDPNPYHLFQPLLPEVAAGTLSPDDIAIPLRELLRRAGVRFIQGEVTGIDPEARTVT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 86 CrmsslhvsgvQKDTVIDYNHLVVAIGAQPHTLNVPGVDEsRVFFLKETEHARNIRSHIHDCLEAASnttlspevRRRLT 165
Cdd:COG1252 90 L----------ADGRTLSYDYLVIATGSVTNFFGIPGLAE-HALPLKTLEDALALRERLLAAFERAE--------RRRLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 166 TFCVVGGGPTGVEFAAELSDFLEQdaARLYPELTM-LPQVIIFEAGTSILGSFDQALSEYGLMRMKRQHVDIRLQTQVKE 244
Cdd:COG1252 151 TIVVVGGGPTGVELAGELAELLRK--LLRYPGIDPdKVRITLVEAGPRILPGLGEKLSEAAEKELEKRGVEVHTGTRVTE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 245 VKDQSLVLSTGEEVNTSTIVWSTGVAPRSLVQQLDAKHKSNGSIGVDECLQIQEAQNAYALGDCASLE----RRLPTVAQ 320
Cdd:COG1252 229 VDADGVTLEDGEEIPADTVIWAAGVKAPPLLADLGLPTDRRGRVLVDPTLQVPGHPNVFAIGDCAAVPdpdgKPVPKTAQ 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167517391 321 VAEQQGAYLARHFNQNFS--SAKPFAFASKGMLAYLG------SYGGVKLSGFKAWLVWRGGYLTKLGTWRSRLQVPF 390
Cdd:COG1252 309 AAVQQAKVLAKNIAALLRgkPLKPFRYRDKGCLASLGrgaavaDVGGLKLSGFLAWLLKRAIHLYFLPGFRGRLRVLL 386
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
6-326 |
4.06e-40 |
|
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: 144.77 E-value: 4.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 6 GPVGVLTASYVRdvdHSKYKVTVVSPRDHML-FTPLLASTTVGTLEHRSII-------EPVRPQAAKNGW---RYLQAEA 74
Cdd:pfam07992 9 GPAGLAAALTLA---QLGGKVTLIEDEGTCPyGGCVLSKALLGAAEAPEIAslwadlyKRKEEVVKKLNNgieVLLGTEV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 75 TNLDLQQQRITCRmsslHVSGVqKDTVIDYNHLVVAIGAQPHTLNVPGVDESRVFFLKETEHARNIRSHihdcleaasnt 154
Cdd:pfam07992 86 VSIDPGAKKVVLE----ELVDG-DGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLK----------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 155 tlspEVRRRLTtfcVVGGGPTGVEFAAELSDFleqdaarlypeltmLPQVIIFEAGTSILGSFDQALSEYGLMRMKRQHV 234
Cdd:pfam07992 150 ----LLPKRVV---VVGGGYIGVELAAALAKL--------------GKEVTLIEALDRLLRAFDEEISAALEKALEKNGV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 235 DIRLQTQVKEVKDQS----LVLSTGEEVNTSTIVWSTGVAPRS-LVQQLDAKHKSNGSIGVDECLQIqEAQNAYALGDCA 309
Cdd:pfam07992 209 EVRLGTSVKEIIGDGdgveVILKDGTEIDADLVVVAIGRRPNTeLLEAAGLELDERGGIVVDEYLRT-SVPGIYAAGDCR 287
|
330
....*....|....*..
gi 167517391 310 sleRRLPTVAQVAEQQG 326
Cdd:pfam07992 288 ---VGGPELAQNAVAQG 301
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
101-333 |
1.93e-12 |
|
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: 68.44 E-value: 1.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 101 VIDYNHLVVAIGAQPHTLNVPgVDESRVFflketeharnirshIHDCLEAASNttlsPEVRRRLTtfcVVGGGPTGVEFA 180
Cdd:TIGR01350 129 TLEAKNIIIATGSRPRSLPGP-FDFDGKV--------------VITSTGALNL----EEVPESLV---IIGGGVIGIEFA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 181 AELSdfleqdaarlypelTMLPQVIIFEAGTSILGSFDQALSEYGLMRMKRQHVDIRLQTQVKEVK---DQSLVLSTGEE 257
Cdd:TIGR01350 187 SIFA--------------SLGSKVTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILTNTKVTAVEkndDQVTYENKGGE 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 258 VNTST---IVWSTGVAPRSL---VQQLDAKHKSNGSIGVDECLQIQeAQNAYALGDCasleRRLPTVAQVAEQQGAYLAR 331
Cdd:TIGR01350 253 TETLTgekVLVAVGRKPNTEglgLEKLGVELDERGRIVVDEYMRTN-VPGIYAIGDV----IGGPMLAHVASHEGIVAAE 327
|
..
gi 167517391 332 HF 333
Cdd:TIGR01350 328 NI 329
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
1-405 |
0e+00 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 674.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 1 MSWSWGpvgvlTASYVRDVDHSKYKVTVVSPRDHMLFTPLLASTTVGTLEHRSIIEPVRPQAAKNGWRYLQAEATNLDLQ 80
Cdd:PTZ00318 16 LGTGWA-----GAYFVRNLDPKKYNITVISPRNHMLFTPLLPQTTTGTLEFRSICEPVRPALAKLPNRYLRAVVYDVDFE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 81 QQRITCRMSSLHVSGVQKDTVIDYNHLVVAIGAQPHTLNVPGVDEsRVFFLKETEHARNIRSHIHDCLEAASNTTLSPEV 160
Cdd:PTZ00318 91 EKRVKCGVVSKSNNANVNTFSVPYDKLVVAHGARPNTFNIPGVEE-RAFFLKEVNHARGIRKRIVQCIERASLPTTSVEE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 161 RRRLTTFCVVGGGPTGVEFAAELSDFLEQDAARLYPELTMLPQVIIFEAGTSILGSFDQALSEYGLMRMKRQHVDIRLQT 240
Cdd:PTZ00318 170 RKRLLHFVVVGGGPTGVEFAAELADFFRDDVRNLNPELVEECKVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVDIRTKT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 241 QVKEVKDQSLVLSTGEEVNTSTIVWSTGVAPRSLVQQLDAKHKSNGSIGVDECLQIQEAQNAYALGDCASLERR-LPTVA 319
Cdd:PTZ00318 250 AVKEVLDKEVVLKDGEVIPTGLVVWSTGVGPGPLTKQLKVDKTSRGRISVDDHLRVKPIPNVFALGDCAANEERpLPTLA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 320 QVAEQQGAYLARHFNQNFS---SAKPFAFASKGMLAYLGSYGG------VKLSGFKAWLVWRGGYLTKLGTWRSRLQVPF 390
Cdd:PTZ00318 330 QVASQQGVYLAKEFNNELKgkpMSKPFVYRSLGSLAYLGNYSAivqlgaFDLSGFKALLFWRSAYLTILGSWRSKLYVLV 409
|
410
....*....|....*
gi 167517391 391 DWAKTMFFGRDPARF 405
Cdd:PTZ00318 410 NWAGTAIFGRDITRF 424
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
6-390 |
1.44e-94 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 288.57 E-value: 1.44e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 6 GPVGVLTASYVRDVDHSKYKVTVVSPRDHMLFTPLLASTTVGTLEHRSIIEPVRPQAAKNGWRYLQAEATNLDLQQQRIT 85
Cdd:COG1252 10 GFAGLEAARRLRKKLGGDAEVTLIDPNPYHLFQPLLPEVAAGTLSPDDIAIPLRELLRRAGVRFIQGEVTGIDPEARTVT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 86 CrmsslhvsgvQKDTVIDYNHLVVAIGAQPHTLNVPGVDEsRVFFLKETEHARNIRSHIHDCLEAASnttlspevRRRLT 165
Cdd:COG1252 90 L----------ADGRTLSYDYLVIATGSVTNFFGIPGLAE-HALPLKTLEDALALRERLLAAFERAE--------RRRLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 166 TFCVVGGGPTGVEFAAELSDFLEQdaARLYPELTM-LPQVIIFEAGTSILGSFDQALSEYGLMRMKRQHVDIRLQTQVKE 244
Cdd:COG1252 151 TIVVVGGGPTGVELAGELAELLRK--LLRYPGIDPdKVRITLVEAGPRILPGLGEKLSEAAEKELEKRGVEVHTGTRVTE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 245 VKDQSLVLSTGEEVNTSTIVWSTGVAPRSLVQQLDAKHKSNGSIGVDECLQIQEAQNAYALGDCASLE----RRLPTVAQ 320
Cdd:COG1252 229 VDADGVTLEDGEEIPADTVIWAAGVKAPPLLADLGLPTDRRGRVLVDPTLQVPGHPNVFAIGDCAAVPdpdgKPVPKTAQ 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167517391 321 VAEQQGAYLARHFNQNFS--SAKPFAFASKGMLAYLG------SYGGVKLSGFKAWLVWRGGYLTKLGTWRSRLQVPF 390
Cdd:COG1252 309 AAVQQAKVLAKNIAALLRgkPLKPFRYRDKGCLASLGrgaavaDVGGLKLSGFLAWLLKRAIHLYFLPGFRGRLRVLL 386
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
6-326 |
4.06e-40 |
|
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: 144.77 E-value: 4.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 6 GPVGVLTASYVRdvdHSKYKVTVVSPRDHML-FTPLLASTTVGTLEHRSII-------EPVRPQAAKNGW---RYLQAEA 74
Cdd:pfam07992 9 GPAGLAAALTLA---QLGGKVTLIEDEGTCPyGGCVLSKALLGAAEAPEIAslwadlyKRKEEVVKKLNNgieVLLGTEV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 75 TNLDLQQQRITCRmsslHVSGVqKDTVIDYNHLVVAIGAQPHTLNVPGVDESRVFFLKETEHARNIRSHihdcleaasnt 154
Cdd:pfam07992 86 VSIDPGAKKVVLE----ELVDG-DGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLK----------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 155 tlspEVRRRLTtfcVVGGGPTGVEFAAELSDFleqdaarlypeltmLPQVIIFEAGTSILGSFDQALSEYGLMRMKRQHV 234
Cdd:pfam07992 150 ----LLPKRVV---VVGGGYIGVELAAALAKL--------------GKEVTLIEALDRLLRAFDEEISAALEKALEKNGV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 235 DIRLQTQVKEVKDQS----LVLSTGEEVNTSTIVWSTGVAPRS-LVQQLDAKHKSNGSIGVDECLQIqEAQNAYALGDCA 309
Cdd:pfam07992 209 EVRLGTSVKEIIGDGdgveVILKDGTEIDADLVVVAIGRRPNTeLLEAAGLELDERGGIVVDEYLRT-SVPGIYAAGDCR 287
|
330
....*....|....*..
gi 167517391 310 sleRRLPTVAQVAEQQG 326
Cdd:pfam07992 288 ---VGGPELAQNAVAQG 301
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
25-355 |
4.37e-35 |
|
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: 131.86 E-value: 4.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 25 KVTVVSPRDHMLFTPLLASTTVGTL--EHRSIIepVRPQA--AKNG--WRyLQAEATNLDLQQQRITcrmsslhvsgVQK 98
Cdd:COG0446 7 EITVIEKGPHHSYQPCGLPYYVGGGikDPEDLL--VRTPEsfERKGidVR-TGTEVTAIDPEAKTVT----------LRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 99 DTVIDYNHLVVAIGAQPHTLNVPGVDESRVFFLKETEHARNIRSHIHDcleaasnttlsPEVRRrlttFCVVGGGPTGVE 178
Cdd:COG0446 74 GETLSYDKLVLATGARPRPPPIPGLDLPGVFTLRTLDDADALREALKE-----------FKGKR----AVVIGGGPIGLE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 179 FAAELSdfleqdAARLypeltmlpQVIIFEAGTSILGSFDQALSEYGLMRMKRQHVDIRLQTQVKEVKDQ---SLVLSTG 255
Cdd:COG0446 139 LAEALR------KRGL--------KVTLVERAPRLLGVLDPEMAALLEEELREHGVELRLGETVVAIDGDdkvAVTLTDG 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 256 EEVNTSTIVWSTGVAPRS-LVQQLDAKHKSNGSIGVDECLQIQeAQNAYALGDCASL------ERRLPTVAQVAEQQGAY 328
Cdd:COG0446 205 EEIPADLVVVAPGVRPNTeLAKDAGLALGERGWIKVDETLQTS-DPDVYAAGDCAEVphpvtgKTVYIPLASAANKQGRV 283
|
330 340 350
....*....|....*....|....*....|....*..
gi 167517391 329 LARH--------FNQNFSSAKPF--AFASKGMLAYLG 355
Cdd:COG0446 284 AAENilggpapfPGLGTFISKVFdlCIASTGTGRLLG 320
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
6-332 |
8.09e-25 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 104.84 E-value: 8.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 6 GPVGVLTASYVRDVDHSkYKVTVVSPRDH------MLfTPLLAsttvGTLEHRSIIEPVRPQAAKNGWR-YLQAEATNLD 78
Cdd:COG1251 10 GMAGVRAAEELRKLDPD-GEITVIGAEPHppynrpPL-SKVLA----GETDEEDLLLRPADFYEENGIDlRLGTRVTAID 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 79 LQQQRITCrmsslhvsgvQKDTVIDYNHLVVAIGAQPHTLNVPGVDESRVFFLKETEHARNIRSHIHDCLEAAsnttlsp 158
Cdd:COG1251 84 RAARTVTL----------ADGETLPYDKLVLATGSRPRVPPIPGADLPGVFTLRTLDDADALRAALAPGKRVV------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 159 evrrrlttfcVVGGGPTGVEFAAelsDFLEQDAarlypeltmlpQVIIFEAGTSILGS-FDQALSEYGLMRMKRQHVDIR 237
Cdd:COG1251 147 ----------VIGGGLIGLEAAA---ALRKRGL-----------EVTVVERAPRLLPRqLDEEAGALLQRLLEALGVEVR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 238 LQTQVKEVKDQS----LVLSTGEEVNTSTIVWSTGVAPR-SLVQqlDAKHKSNGSIGVDECLQ-----IqeaqnaYALGD 307
Cdd:COG1251 203 LGTGVTEIEGDDrvtgVRLADGEELPADLVVVAIGVRPNtELAR--AAGLAVDRGIVVDDYLRtsdpdI------YAAGD 274
|
330 340 350
....*....|....*....|....*....|.
gi 167517391 308 CASLE------RRLPTVAqVAEQQGAYLARH 332
Cdd:COG1251 275 CAEHPgpvygrRVLELVA-PAYEQARVAAAN 304
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
96-332 |
1.06e-18 |
|
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: 87.45 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 96 VQKDTVIDYNHLVVAIGAQPHTLNVPGVDESRVFflkeTeharnirshihdcleaaSNTTLS-PEVRRRLTtfcVVGGGP 174
Cdd:COG1249 123 VTGGETLTADHIVIATGSRPRVPPIPGLDEVRVL----T-----------------SDEALElEELPKSLV---VIGGGY 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 175 TGVEFAAELSDFleqDAarlypeltmlpQVIIFEAGTSILGSFDQALSEYGLMRMKRQHVDIRLQTQVKEVKDQS----L 250
Cdd:COG1249 179 IGLEFAQIFARL---GS-----------EVTLVERGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVEKTGdgvtV 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 251 VLSTGEEVNTST---IVWSTGVAPRslVQQLDA-----KHKSNGSIGVDECLQIqEAQNAYALGDCAsleRRLPtVAQVA 322
Cdd:COG1249 245 TLEDGGGEEAVEadkVLVATGRRPN--TDGLGLeaagvELDERGGIKVDEYLRT-SVPGIYAIGDVT---GGPQ-LAHVA 317
|
250
....*....|
gi 167517391 323 EQQGAYLARH 332
Cdd:COG1249 318 SAEGRVAAEN 327
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
101-333 |
1.93e-12 |
|
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: 68.44 E-value: 1.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 101 VIDYNHLVVAIGAQPHTLNVPgVDESRVFflketeharnirshIHDCLEAASNttlsPEVRRRLTtfcVVGGGPTGVEFA 180
Cdd:TIGR01350 129 TLEAKNIIIATGSRPRSLPGP-FDFDGKV--------------VITSTGALNL----EEVPESLV---IIGGGVIGIEFA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 181 AELSdfleqdaarlypelTMLPQVIIFEAGTSILGSFDQALSEYGLMRMKRQHVDIRLQTQVKEVK---DQSLVLSTGEE 257
Cdd:TIGR01350 187 SIFA--------------SLGSKVTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILTNTKVTAVEkndDQVTYENKGGE 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 258 VNTST---IVWSTGVAPRSL---VQQLDAKHKSNGSIGVDECLQIQeAQNAYALGDCasleRRLPTVAQVAEQQGAYLAR 331
Cdd:TIGR01350 253 TETLTgekVLVAVGRKPNTEglgLEKLGVELDERGRIVVDEYMRTN-VPGIYAIGDV----IGGPMLAHVASHEGIVAAE 327
|
..
gi 167517391 332 HF 333
Cdd:TIGR01350 328 NI 329
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
61-311 |
2.46e-10 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 61.98 E-value: 2.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 61 QAAKNGWR-YLQAEATNLDLQQQRITcrmsslhVSGVQKDTVID--YNHLVVAIGAQPHTLNVPGVDESRVFFLKETEHA 137
Cdd:PRK09564 65 EFIKSGIDvKTEHEVVKVDAKNKTIT-------VKNLKTGSIFNdtYDKLMIATGARPIIPPIKNINLENVYTLKSMEDG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 138 RNIRSHIHDcleaasnttlsPEVRRrlttFCVVGGGPTGVEfAAELSDFLEQDaarlypeltmlpqVIIFEAGTSILG-S 216
Cdd:PRK09564 138 LALKELLKD-----------EEIKN----IVIIGAGFIGLE-AVEAAKHLGKN-------------VRIIQLEDRILPdS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 217 FDQALSEYGLMRMKRQHVDIRLQTQVKEVKDQS---LVLSTGEEVNTSTIVWSTGVAPRS-LVQQLDAKHKSNGSIGVDE 292
Cdd:PRK09564 189 FDKEITDVMEEELRENGVELHLNEFVKSLIGEDkveGVVTDKGEYEADVVIVATGVKPNTeFLEDTGLKTLKNGAIIVDE 268
|
250
....*....|....*....
gi 167517391 293 CLQiQEAQNAYALGDCASL 311
Cdd:PRK09564 269 YGE-TSIENIYAAGDCATI 286
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
106-307 |
3.42e-10 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 61.30 E-value: 3.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 106 HLVVAIGAQPHTLNVPGVDESRvfflketeharnirsHIHDCLEAASNTTLsPEvrrRLTtfcVVGGGPTGVEFAAelsd 185
Cdd:PRK07251 121 TIVINTGAVSNVLPIPGLADSK---------------HVYDSTGIQSLETL-PE---RLG---IIGGGNIGLEFAG---- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 186 fleqdaarLYPELTmlPQVIIFEAGTSILGSFDQALSEYGLMRMKRQHVDIRLQTQVKEVK---DQSLVLSTGEEVNTST 262
Cdd:PRK07251 175 --------LYNKLG--SKVTVLDAASTILPREEPSVAALAKQYMEEDGITFLLNAHTTEVKndgDQVLVVTEDETYRFDA 244
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 167517391 263 IVWSTGVAPRSLVQQL---DAKHKSNGSIGVDECLQiQEAQNAYALGD 307
Cdd:PRK07251 245 LLYATGRKPNTEPLGLentDIELTERGAIKVDDYCQ-TSVPGVFAVGD 291
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
169-246 |
8.97e-09 |
|
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: 51.82 E-value: 8.97e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167517391 169 VVGGGPTGVEFAAELSDFleqdAArlypeltmlpQVIIFEAGTSILGSFDQALSEYGLMRMKRQHVDIRLQTQVKEVK 246
Cdd:pfam00070 4 VVGGGYIGLELAGALARL----GS----------KVTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIE 67
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
169-308 |
2.20e-07 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 52.49 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 169 VVGGGPTGVEFAAELSdfleqdaarlypelTMLPQVIIFEAGTSILGSFDQALSEYGLMRMKRQhVDIRLQTQVKEVKDQ 248
Cdd:PRK06292 174 VIGGGVIGLELGQALS--------------RLGVKVTVFERGDRILPLEDPEVSKQAQKILSKE-FKIKLGAKVTSVEKS 238
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 249 SLVLSTGEEVNTSTIVW-------STGVAP--RSL-VQQLDAKHKSNGSIGVDECLQiQEAQNAYALGDC 308
Cdd:PRK06292 239 GDEKVEELEKGGKTETIeadyvlvATGRRPntDGLgLENTGIELDERGRPVVDEHTQ-TSVPGIYAAGDV 307
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
66-307 |
7.08e-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: 51.13 E-value: 7.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 66 GWRYLQaeatnldlQQQRITCRMSSLHVSGVQKdtVIDYNHLVVAIGAQPHTLNVPGVDEsrvfflketeharnirshih 145
Cdd:TIGR01423 124 GWGALE--------DKNVVLVRESADPKSAVKE--RLQAEHILLATGSWPQMLGIPGIEH-------------------- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 146 dCLEAASNTTLSPEVRRRLTtfcvVGGGPTGVEFAAELSDFLEQDAarlypeltmlpQVIIFEAGTSILGSFDQALSEYG 225
Cdd:TIGR01423 174 -CISSNEAFYLDEPPRRVLT----VGGGFISVEFAGIFNAYKPRGG-----------KVTLCYRNNMILRGFDSTLRKEL 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 226 LMRMKRQHVDIRLQTQVKEVK-----DQSLVLSTGEEVNTSTIVWSTGVAPRSLVQQLD---AKHKSNGSIGVDEcLQIQ 297
Cdd:TIGR01423 238 TKQLRANGINIMTNENPAKVTlnadgSKHVTFESGKTLDVDVVMMAIGRVPRTQTLQLDkvgVELTKKGAIQVDE-FSRT 316
|
250
....*....|
gi 167517391 298 EAQNAYALGD 307
Cdd:TIGR01423 317 NVPNIYAIGD 326
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
75-315 |
1.01e-06 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 50.30 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 75 TNLDLQQQRITCrmsslhvsgvqKDTVIDYNHLVVAIGAQPHTLNVPGvDEsRVFFLKETEHARNIRSHIHDcleaasnt 154
Cdd:PRK04965 82 TDIDAEAQVVKS-----------QGNQWQYDKLVLATGASAFVPPIPG-RE-LMLTLNSQQEYRAAETQLRD-------- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 155 tlspeVRRRLttfcVVGGGPTGVEFAAELsdfleQDAARlypeltmlpQVIIFEAGTSILGSfdqalseygLM------- 227
Cdd:PRK04965 141 -----AQRVL----VVGGGLIGTELAMDL-----CRAGK---------AVTLVDNAASLLAS---------LMppevssr 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 228 ---RMKRQHVDIRLQTQVKEVK--DQSLV--LSTGEEVNTSTIVWSTGVAPR-SLVQQldAKHKSNGSIGVDECLQIQeA 299
Cdd:PRK04965 189 lqhRLTEMGVHLLLKSQLQGLEktDSGIRatLDSGRSIEVDAVIAAAGLRPNtALARR--AGLAVNRGIVVDSYLQTS-A 265
|
250
....*....|....*.
gi 167517391 300 QNAYALGDCASLERRL 315
Cdd:PRK04965 266 PDIYALGDCAEINGQV 281
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
99-308 |
2.04e-06 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 49.82 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 99 DTVIDYNHLVVAIGAQPHTLNVPGVDESRvfFLketeharnirshihdcleaaSNTTLSP--EVRRRLTtfcVVGGGPTG 176
Cdd:PRK06370 129 GETLRAKRIFINTGARAAIPPIPGLDEVG--YL--------------------TNETIFSldELPEHLV---IIGGGYIG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 177 VEFAaelsdfleQDAARLYpeltmlPQVIIFEAGTSILGSFD----QALSEYglmrMKRQHVDIRLQTQVKEVKDQS--- 249
Cdd:PRK06370 184 LEFA--------QMFRRFG------SEVTVIERGPRLLPREDedvaAAVREI----LEREGIDVRLNAECIRVERDGdgi 245
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 167517391 250 ---LVLSTGE-EVNTSTIVWSTGVAPRSLVQQLDA---KHKSNGSIGVDECLQiQEAQNAYALGDC 308
Cdd:PRK06370 246 avgLDCNGGApEITGSHILVAVGRVPNTDDLGLEAagvETDARGYIKVDDQLR-TTNPGIYAAGDC 310
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
90-326 |
4.88e-06 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 48.60 E-value: 4.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 90 SLHVSGVQKDTVIDYNHLVVAIGAQPHTLnvPG--VDESRVFFlkeTEHARNIrshihdcleaasnttlsPEVRRRLttf 167
Cdd:PRK06416 121 TVRVMTEDGEQTYTAKNIILATGSRPREL--PGieIDGRVIWT---SDEALNL-----------------DEVPKSL--- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 168 CVVGGGPTGVEFAaelsdfleqDAARlypelTMLPQVIIFEAGTSILGSFDQALSEYGLMRMKRQHVDIRLQTQVKEVKD 247
Cdd:PRK06416 176 VVIGGGYIGVEFA---------SAYA-----SLGAEVTIVEALPRILPGEDKEISKLAERALKKRGIKIKTGAKAKKVEQ 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 248 QS----LVLSTGEEVNTST----IVwSTGVAPRS----LVQQ---LDakhksNGSIGVDECLQiQEAQNAYALGDCASle 312
Cdd:PRK06416 242 TDdgvtVTLEDGGKEETLEadyvLV-AVGRRPNTenlgLEELgvkTD-----RGFIEVDEQLR-TNVPNIYAIGDIVG-- 312
|
250
....*....|....
gi 167517391 313 rrLPTVAQVAEQQG 326
Cdd:PRK06416 313 --GPMLAHKASAEG 324
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
158-310 |
1.18e-05 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 47.26 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 158 PEVRRRLTtfcVVGGGPTGVEFAAELSDFLEqdaarlypeltmlpQVIIFEAGTSILGSFDQALSEyGLMRMKRQHVDIR 237
Cdd:PRK07846 163 PELPESLV---IVGGGFIAAEFAHVFSALGV--------------RVTVVNRSGRLLRHLDDDISE-RFTELASKRWDVR 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 238 LQTQVKEVKDQ----SLVLSTGEEVNTSTIVWSTGVAPRSlvQQLDAKH-----KSNGSIGVDEcLQIQEAQNAYALGDC 308
Cdd:PRK07846 225 LGRNVVGVSQDgsgvTLRLDDGSTVEADVLLVATGRVPNG--DLLDAAAagvdvDEDGRVVVDE-YQRTSAEGVFALGDV 301
|
..
gi 167517391 309 AS 310
Cdd:PRK07846 302 SS 303
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
93-331 |
2.04e-05 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 46.46 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 93 VSGvQKDTVIDYNHLVVAIGAQPHTLnvPGV--DESRVFflketeharnirshihdCLEAASNTTlspEVRRRLTtfcVV 170
Cdd:PRK06327 136 VTG-EDETVITAKHVIIATGSEPRHL--PGVpfDNKIIL-----------------DNTGALNFT---EVPKKLA---VI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 171 GGGPTGVEFAaelSDFleqdaARLYPELTMLpqviifEAGTSILGSFDQALSEYGLMRMKRQHVDIRLQTQVKEVKD--- 247
Cdd:PRK06327 190 GAGVIGLELG---SVW-----RRLGAEVTIL------EALPAFLAAADEQVAKEAAKAFTKQGLDIHLGVKIGEIKTggk 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 248 -------------QS-----LVLSTGEEVNTSTI-VWSTGVaprslvqQLDAkhksNGSIGVDECLQIQeAQNAYALGDC 308
Cdd:PRK06327 256 gvsvaytdadgeaQTlevdkLIVSIGRVPNTDGLgLEAVGL-------KLDE----RGFIPVDDHCRTN-VPNVYAIGDV 323
|
250 260
....*....|....*....|...
gi 167517391 309 AslerRLPTVAQVAEQQGAYLAR 331
Cdd:PRK06327 324 V----RGPMLAHKAEEEGVAVAE 342
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
104-317 |
4.96e-05 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 45.30 E-value: 4.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 104 YNHLVVAIGAQPHTLnvPGVDE--SRVFFLKETEHARNIRShihdcleaasntTLSPEVRrrlttFCVVGGGPTGVEFAA 181
Cdd:PRK09754 101 WDQLFIATGAAARPL--PLLDAlgERCFTLRHAGDAARLRE------------VLQPERS-----VVIVGAGTIGLELAA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 182 ELSDfleqdaarlypeltMLPQVIIFEAGTSILG-SFDQALSEYGLMRMKRQHVDIRLQTQVKEVKDQS---LVLSTGEE 257
Cdd:PRK09754 162 SATQ--------------RRCKVTVIELAATVMGrNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGEkveLTLQSGET 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 258 VNTSTIVWSTGVAPRSLVQQlDAKHKSNGSIGVDECLQIQEAqNAYALGDCASleRRLPT 317
Cdd:PRK09754 228 LQADVVIYGIGISANDQLAR-EANLDTANGIVIDEACRTCDP-AIFAGGDVAI--TRLDN 283
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
64-322 |
5.83e-05 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 45.49 E-value: 5.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 64 KNGWRYLQAE-ATNLDLQQQRItcrmsslHVSgvqKDTVIDYNHLVVAIGAQPHTLNVPGVDESRVFFLKETEHARNIRS 142
Cdd:PRK14989 71 KHGIKVLVGErAITINRQEKVI-------HSS---AGRTVFYDKLIMATGSYPWIPPIKGSETQDCFVYRTIEDLNAIEA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 143 hihdcleaasnttlspeVRRRLTTFCVVGGGPTGVEFAAELSDF-LEQDAARLYPELtMLPQViifeagtsilgsfDQAL 221
Cdd:PRK14989 141 -----------------CARRSKRGAVVGGGLLGLEAAGALKNLgVETHVIEFAPML-MAEQL-------------DQMG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167517391 222 SEygLMRMKRQHVDIRLQT--QVKEVKDQ------SLVLSTGEEVNTSTIVWSTGVAPR-SLVQQLDAKHKSNGSIGVDE 292
Cdd:PRK14989 190 GE--QLRRKIESMGVRVHTskNTLEIVQEgvearkTMRFADGSELEVDFIVFSTGIRPQdKLATQCGLAVAPRGGIVIND 267
|
250 260 270
....*....|....*....|....*....|....*..
gi 167517391 293 CLQIQEAqNAYALGDCASLERRL-----P--TVAQVA 322
Cdd:PRK14989 268 SCQTSDP-DIYAIGECASWNNRVfglvaPgyKMAQVA 303
|
|
| |
