|
Name |
Accession |
Description |
Interval |
E-value |
| AIF_C |
pfam14721 |
Apoptosis-inducing factor, mitochondrion-associated, C-term; This C-terminal domain appears to ... |
537-659 |
5.45e-71 |
|
Apoptosis-inducing factor, mitochondrion-associated, C-term; This C-terminal domain appears to be a dimerization domain of the mitochondrial apoptosis-inducing factor 1. protein. The domain also appears at the C-terminus of FAD-dependent pyridine nucleotide-disulfide oxidoreductases. Apoptosis inducing factor (AIF) is a bifunctional mitochondrial flavoprotein critical for energy metabolism and induction of caspase-independent apoptosis. On reduction with NADH, AIF undergoes dimerization and forms tight, long-lived FADH2-NAD charge-transfer complexes proposed to be functionally important.
:
Pssm-ID: 464279 Cd Length: 130 Bit Score: 226.37 E-value: 5.45e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 537 AGENMTGAKKPYQHQSMFWSDLGPEIGYEGIGLVDSSLPTVGVFALPSPNDKR---AVNHTEAVVDTTSSDRVKIIGDGT 613
Cdd:pfam14721 1 AGENMTGAGKPYWHQSMFWSDLGPDVGYEAIGIVDSSLPTVGVFAKATEKDTPkavVEESGESIRSESEEEATASASAAP 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 195034902 614 E----MSCDPSEEPNYGKGVIFYLQNDKIVGILLWNLFNRIGLARTIISQ 659
Cdd:pfam14721 81 SsedvASEDPSPGEDYGKGVIFYLRDDKVVGIVLWNVFNRMPIARKIIKD 130
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
202-662 |
3.46e-62 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
:
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 212.69 E-value: 3.46e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 202 PYLIVGGGTAAFSAFRAIKSNDARAKVLMISNEYRKPYMRPPLSKELwytpnpnedpikdyrfkqwTG--SERSLYFEPD 279
Cdd:COG1251 3 RIVIIGAGMAGVRAAEELRKLDPDGEITVIGAEPHPPYNRPPLSKVL-------------------AGetDEEDLLLRPA 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 280 EFFVDPekldesvngGIAVAQGFAVKKIDAQNRIATLNDGYQIGYDVCLIATGCAPKNLPMfhdtAPSVREKVMVYRTPD 359
Cdd:COG1251 64 DFYEEN---------GIDLRLGTRVTAIDRAARTVTLADGETLPYDKLVLATGSRPRVPPI----PGADLPGVFTLRTLD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 360 DFDRLRRYAKEKRSITIVGNGFVGSELACSLAHysrhnNGGKIYQVFPEKGNMSRVLPNYLSTWTTRKVQAQGVCVIPEA 439
Cdd:COG1251 131 DADALRAALAPGKRVVVIGGGLIGLEAAAALRK-----RGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGT 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 440 SIKSATRDDSQLKLELNNGMSVLSDIVVVCVGCSPNTAMAGPSKLEVDRtlgGFVVNAELEARR-NLYVAGDACCFYDPL 518
Cdd:COG1251 206 GVTEIEGDDRVTGVRLADGEELPADLVVVAIGVRPNTELARAAGLAVDR---GIVVDDYLRTSDpDIYAAGDCAEHPGPV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 519 LGRRRVEHHDHSVVSGRLAGENMTGAKKPYQH-QSMFWSDLGpeigyeGIGLVdsslpTVGvfalpspndkravnhteav 597
Cdd:COG1251 283 YGRRVLELVAPAYEQARVAAANLAGGPAAYEGsVPSTKLKVF------GVDVA-----SAG------------------- 332
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 195034902 598 vDTTSSDRVKIIGDGTEmscdpseepnyGKGVIFYLQNDKIVGILLWNLFNRIGLARTIISQNTD 662
Cdd:COG1251 333 -DAEGDEEVVVRGDPAR-----------GVYKKLVLRDGRLVGAVLVGDTSDAGALRQLIKNGRP 385
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AIF_C |
pfam14721 |
Apoptosis-inducing factor, mitochondrion-associated, C-term; This C-terminal domain appears to ... |
537-659 |
5.45e-71 |
|
Apoptosis-inducing factor, mitochondrion-associated, C-term; This C-terminal domain appears to be a dimerization domain of the mitochondrial apoptosis-inducing factor 1. protein. The domain also appears at the C-terminus of FAD-dependent pyridine nucleotide-disulfide oxidoreductases. Apoptosis inducing factor (AIF) is a bifunctional mitochondrial flavoprotein critical for energy metabolism and induction of caspase-independent apoptosis. On reduction with NADH, AIF undergoes dimerization and forms tight, long-lived FADH2-NAD charge-transfer complexes proposed to be functionally important.
Pssm-ID: 464279 Cd Length: 130 Bit Score: 226.37 E-value: 5.45e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 537 AGENMTGAKKPYQHQSMFWSDLGPEIGYEGIGLVDSSLPTVGVFALPSPNDKR---AVNHTEAVVDTTSSDRVKIIGDGT 613
Cdd:pfam14721 1 AGENMTGAGKPYWHQSMFWSDLGPDVGYEAIGIVDSSLPTVGVFAKATEKDTPkavVEESGESIRSESEEEATASASAAP 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 195034902 614 E----MSCDPSEEPNYGKGVIFYLQNDKIVGILLWNLFNRIGLARTIISQ 659
Cdd:pfam14721 81 SsedvASEDPSPGEDYGKGVIFYLRDDKVVGIVLWNVFNRMPIARKIIKD 130
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
202-662 |
3.46e-62 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 212.69 E-value: 3.46e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 202 PYLIVGGGTAAFSAFRAIKSNDARAKVLMISNEYRKPYMRPPLSKELwytpnpnedpikdyrfkqwTG--SERSLYFEPD 279
Cdd:COG1251 3 RIVIIGAGMAGVRAAEELRKLDPDGEITVIGAEPHPPYNRPPLSKVL-------------------AGetDEEDLLLRPA 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 280 EFFVDPekldesvngGIAVAQGFAVKKIDAQNRIATLNDGYQIGYDVCLIATGCAPKNLPMfhdtAPSVREKVMVYRTPD 359
Cdd:COG1251 64 DFYEEN---------GIDLRLGTRVTAIDRAARTVTLADGETLPYDKLVLATGSRPRVPPI----PGADLPGVFTLRTLD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 360 DFDRLRRYAKEKRSITIVGNGFVGSELACSLAHysrhnNGGKIYQVFPEKGNMSRVLPNYLSTWTTRKVQAQGVCVIPEA 439
Cdd:COG1251 131 DADALRAALAPGKRVVVIGGGLIGLEAAAALRK-----RGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGT 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 440 SIKSATRDDSQLKLELNNGMSVLSDIVVVCVGCSPNTAMAGPSKLEVDRtlgGFVVNAELEARR-NLYVAGDACCFYDPL 518
Cdd:COG1251 206 GVTEIEGDDRVTGVRLADGEELPADLVVVAIGVRPNTELARAAGLAVDR---GIVVDDYLRTSDpDIYAAGDCAEHPGPV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 519 LGRRRVEHHDHSVVSGRLAGENMTGAKKPYQH-QSMFWSDLGpeigyeGIGLVdsslpTVGvfalpspndkravnhteav 597
Cdd:COG1251 283 YGRRVLELVAPAYEQARVAAANLAGGPAAYEGsVPSTKLKVF------GVDVA-----SAG------------------- 332
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 195034902 598 vDTTSSDRVKIIGDGTEmscdpseepnyGKGVIFYLQNDKIVGILLWNLFNRIGLARTIISQNTD 662
Cdd:COG1251 333 -DAEGDEEVVVRGDPAR-----------GVYKKLVLRDGRLVGAVLVGDTSDAGALRQLIKNGRP 385
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
203-534 |
4.08e-37 |
|
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: 140.53 E-value: 4.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 203 YLIVGGGTAAFSAfrAIKSNDARAKVLMISNEYRKPYMRPPLSKELWYTPNPNEDPIKDYRFKQWtgserslyfepdeff 282
Cdd:pfam07992 3 VVVIGGGPAGLAA--ALTLAQLGGKVTLIEDEGTCPYGGCVLSKALLGAAEAPEIASLWADLYKR--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 283 vdPEKLDESVNGGIAVAQGFAVKKIDAQNRIATL-----NDGYQIGYDVCLIATGCAPKNLPMfhdtaPSVREKV-MVYR 356
Cdd:pfam07992 66 --KEEVVKKLNNGIEVLLGTEVVSIDPGAKKVVLeelvdGDGETITYDRLVIATGARPRLPPI-----PGVELNVgFLVR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 357 TPDDFDRLRRYAKEKRsITIVGNGFVGSELACSLAHYsrhnnGGKIYQVFpekgNMSRVLPNY---LSTWTTRKVQAQGV 433
Cdd:pfam07992 139 TLDSAEALRLKLLPKR-VVVVGGGYIGVELAAALAKL-----GKEVTLIE----ALDRLLRAFdeeISAALEKALEKNGV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 434 CVIPEASIKSATRDDSQLKLELNNGMSVLSDIVVVCVGCSPNTAMAGPSKLEVDRTlGGFVVNAELE-ARRNLYVAGDAc 512
Cdd:pfam07992 209 EVRLGTSVKEIIGDGDGVEVILKDGTEIDADLVVVAIGRRPNTELLEAAGLELDER-GGIVVDEYLRtSVPGIYAAGDC- 286
|
330 340
....*....|....*....|..
gi 195034902 513 cfydpllGRRRVEHHDHSVVSG 534
Cdd:pfam07992 287 -------RVGGPELAQNAVAQG 301
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
203-557 |
1.74e-31 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 126.96 E-value: 1.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 203 YLIVGGGTAAFSAFRAIKSNDARAKVLMISNEYRKPYMRPPLSKElwYTPNPNEDPikdyrfkqwtgsersLYFEPDEFF 282
Cdd:PRK09754 6 IIIVGGGQAAAMAAASLRQQGFTGELHLFSDERHLPYERPPLSKS--MLLEDSPQL---------------QQVLPANWW 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 283 vdpekldesVNGGIAVAQGFAVKKIDAQNRIATLNDGYQIGYDVCLIATGCAPKNLPMFHdtapSVREKVMVYRTPDDFD 362
Cdd:PRK09754 69 ---------QENNVHLHSGVTIKTLGRDTRELVLTNGESWHWDQLFIATGAAARPLPLLD----ALGERCFTLRHAGDAA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 363 RLRRYAKEKRSITIVGNGFVGSELACSLAHYsrhnnGGKIYQVFPEKGNMSRVLPNYLSTWTTRKVQAQGVCVIPEASIK 442
Cdd:PRK09754 136 RLREVLQPERSVVIVGAGTIGLELAASATQR-----RCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIE 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 443 SAtRDDSQLKLELNNGMSVLSDIVVVCVGCSPNTAMAGPSKLEVDrtlGGFVVNAELE-ARRNLYVAGDACCFYDPLLGR 521
Cdd:PRK09754 211 HV-VDGEKVELTLQSGETLQADVVIYGIGISANDQLAREANLDTA---NGIVIDEACRtCDPAIFAGGDVAITRLDNGAL 286
|
330 340 350
....*....|....*....|....*....|....*.
gi 195034902 522 RRVEHHDHSVVSGRLAGENMTGAKKPYQHQSMFWSD 557
Cdd:PRK09754 287 HRCESWENANNQAQIAAAAMLGLPLPLLPPPWFWSD 322
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AIF_C |
pfam14721 |
Apoptosis-inducing factor, mitochondrion-associated, C-term; This C-terminal domain appears to ... |
537-659 |
5.45e-71 |
|
Apoptosis-inducing factor, mitochondrion-associated, C-term; This C-terminal domain appears to be a dimerization domain of the mitochondrial apoptosis-inducing factor 1. protein. The domain also appears at the C-terminus of FAD-dependent pyridine nucleotide-disulfide oxidoreductases. Apoptosis inducing factor (AIF) is a bifunctional mitochondrial flavoprotein critical for energy metabolism and induction of caspase-independent apoptosis. On reduction with NADH, AIF undergoes dimerization and forms tight, long-lived FADH2-NAD charge-transfer complexes proposed to be functionally important.
Pssm-ID: 464279 Cd Length: 130 Bit Score: 226.37 E-value: 5.45e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 537 AGENMTGAKKPYQHQSMFWSDLGPEIGYEGIGLVDSSLPTVGVFALPSPNDKR---AVNHTEAVVDTTSSDRVKIIGDGT 613
Cdd:pfam14721 1 AGENMTGAGKPYWHQSMFWSDLGPDVGYEAIGIVDSSLPTVGVFAKATEKDTPkavVEESGESIRSESEEEATASASAAP 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 195034902 614 E----MSCDPSEEPNYGKGVIFYLQNDKIVGILLWNLFNRIGLARTIISQ 659
Cdd:pfam14721 81 SsedvASEDPSPGEDYGKGVIFYLRDDKVVGIVLWNVFNRMPIARKIIKD 130
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
202-662 |
3.46e-62 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 212.69 E-value: 3.46e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 202 PYLIVGGGTAAFSAFRAIKSNDARAKVLMISNEYRKPYMRPPLSKELwytpnpnedpikdyrfkqwTG--SERSLYFEPD 279
Cdd:COG1251 3 RIVIIGAGMAGVRAAEELRKLDPDGEITVIGAEPHPPYNRPPLSKVL-------------------AGetDEEDLLLRPA 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 280 EFFVDPekldesvngGIAVAQGFAVKKIDAQNRIATLNDGYQIGYDVCLIATGCAPKNLPMfhdtAPSVREKVMVYRTPD 359
Cdd:COG1251 64 DFYEEN---------GIDLRLGTRVTAIDRAARTVTLADGETLPYDKLVLATGSRPRVPPI----PGADLPGVFTLRTLD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 360 DFDRLRRYAKEKRSITIVGNGFVGSELACSLAHysrhnNGGKIYQVFPEKGNMSRVLPNYLSTWTTRKVQAQGVCVIPEA 439
Cdd:COG1251 131 DADALRAALAPGKRVVVIGGGLIGLEAAAALRK-----RGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGT 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 440 SIKSATRDDSQLKLELNNGMSVLSDIVVVCVGCSPNTAMAGPSKLEVDRtlgGFVVNAELEARR-NLYVAGDACCFYDPL 518
Cdd:COG1251 206 GVTEIEGDDRVTGVRLADGEELPADLVVVAIGVRPNTELARAAGLAVDR---GIVVDDYLRTSDpDIYAAGDCAEHPGPV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 519 LGRRRVEHHDHSVVSGRLAGENMTGAKKPYQH-QSMFWSDLGpeigyeGIGLVdsslpTVGvfalpspndkravnhteav 597
Cdd:COG1251 283 YGRRVLELVAPAYEQARVAAANLAGGPAAYEGsVPSTKLKVF------GVDVA-----SAG------------------- 332
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 195034902 598 vDTTSSDRVKIIGDGTEmscdpseepnyGKGVIFYLQNDKIVGILLWNLFNRIGLARTIISQNTD 662
Cdd:COG1251 333 -DAEGDEEVVVRGDPAR-----------GVYKKLVLRDGRLVGAVLVGDTSDAGALRQLIKNGRP 385
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
222-558 |
1.62e-38 |
|
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: 145.34 E-value: 1.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 222 NDARAKVLMISNEYRKPYMRPPLSKELwytpnpnEDPIKDyrfkqwtgsERSLYFEPDEFFVDPekldesvngGIAVAQG 301
Cdd:COG0446 2 LGPDAEITVIEKGPHHSYQPCGLPYYV-------GGGIKD---------PEDLLVRTPESFERK---------GIDVRTG 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 302 FAVKKIDAQNRIATLNDGYQIGYDVCLIATGCAPKNLPMFHDTAPsvreKVMVYRTPDDFDRLRRYAKEK--RSITIVGN 379
Cdd:COG0446 57 TEVTAIDPEAKTVTLRDGETLSYDKLVLATGARPRPPPIPGLDLP----GVFTLRTLDDADALREALKEFkgKRAVVIGG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 380 GFVGSELACSLAHysrhnNGGKIYQVFPekgnMSRVLPNY---LSTWTTRKVQAQGVCVIPEASIKSATRDDsQLKLELN 456
Cdd:COG0446 133 GPIGLELAEALRK-----RGLKVTLVER----APRLLGVLdpeMAALLEEELREHGVELRLGETVVAIDGDD-KVAVTLT 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 457 NGMSVLSDIVVVCVGCSPNTAMAGPSKLEVDRTlGGFVVNAELEAR-RNLYVAGDACCFYDPLLGRR-RVEHHDHSVVSG 534
Cdd:COG0446 203 DGEEIPADLVVVAPGVRPNTELAKDAGLALGER-GWIKVDETLQTSdPDVYAAGDCAEVPHPVTGKTvYIPLASAANKQG 281
|
330 340
....*....|....*....|....
gi 195034902 535 RLAGENMTGAKKPYQHQSMFWSDL 558
Cdd:COG0446 282 RVAAENILGGPAPFPGLGTFISKV 305
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
203-534 |
4.08e-37 |
|
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: 140.53 E-value: 4.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 203 YLIVGGGTAAFSAfrAIKSNDARAKVLMISNEYRKPYMRPPLSKELWYTPNPNEDPIKDYRFKQWtgserslyfepdeff 282
Cdd:pfam07992 3 VVVIGGGPAGLAA--ALTLAQLGGKVTLIEDEGTCPYGGCVLSKALLGAAEAPEIASLWADLYKR--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 283 vdPEKLDESVNGGIAVAQGFAVKKIDAQNRIATL-----NDGYQIGYDVCLIATGCAPKNLPMfhdtaPSVREKV-MVYR 356
Cdd:pfam07992 66 --KEEVVKKLNNGIEVLLGTEVVSIDPGAKKVVLeelvdGDGETITYDRLVIATGARPRLPPI-----PGVELNVgFLVR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 357 TPDDFDRLRRYAKEKRsITIVGNGFVGSELACSLAHYsrhnnGGKIYQVFpekgNMSRVLPNY---LSTWTTRKVQAQGV 433
Cdd:pfam07992 139 TLDSAEALRLKLLPKR-VVVVGGGYIGVELAAALAKL-----GKEVTLIE----ALDRLLRAFdeeISAALEKALEKNGV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 434 CVIPEASIKSATRDDSQLKLELNNGMSVLSDIVVVCVGCSPNTAMAGPSKLEVDRTlGGFVVNAELE-ARRNLYVAGDAc 512
Cdd:pfam07992 209 EVRLGTSVKEIIGDGDGVEVILKDGTEIDADLVVVAIGRRPNTELLEAAGLELDER-GGIVVDEYLRtSVPGIYAAGDC- 286
|
330 340
....*....|....*....|..
gi 195034902 513 cfydpllGRRRVEHHDHSVVSG 534
Cdd:pfam07992 287 -------RVGGPELAQNAVAQG 301
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
203-557 |
1.74e-31 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 126.96 E-value: 1.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 203 YLIVGGGTAAFSAFRAIKSNDARAKVLMISNEYRKPYMRPPLSKElwYTPNPNEDPikdyrfkqwtgsersLYFEPDEFF 282
Cdd:PRK09754 6 IIIVGGGQAAAMAAASLRQQGFTGELHLFSDERHLPYERPPLSKS--MLLEDSPQL---------------QQVLPANWW 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 283 vdpekldesVNGGIAVAQGFAVKKIDAQNRIATLNDGYQIGYDVCLIATGCAPKNLPMFHdtapSVREKVMVYRTPDDFD 362
Cdd:PRK09754 69 ---------QENNVHLHSGVTIKTLGRDTRELVLTNGESWHWDQLFIATGAAARPLPLLD----ALGERCFTLRHAGDAA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 363 RLRRYAKEKRSITIVGNGFVGSELACSLAHYsrhnnGGKIYQVFPEKGNMSRVLPNYLSTWTTRKVQAQGVCVIPEASIK 442
Cdd:PRK09754 136 RLREVLQPERSVVIVGAGTIGLELAASATQR-----RCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIE 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 443 SAtRDDSQLKLELNNGMSVLSDIVVVCVGCSPNTAMAGPSKLEVDrtlGGFVVNAELE-ARRNLYVAGDACCFYDPLLGR 521
Cdd:PRK09754 211 HV-VDGEKVELTLQSGETLQADVVIYGIGISANDQLAREANLDTA---NGIVIDEACRtCDPAIFAGGDVAITRLDNGAL 286
|
330 340 350
....*....|....*....|....*....|....*.
gi 195034902 522 RRVEHHDHSVVSGRLAGENMTGAKKPYQHQSMFWSD 557
Cdd:PRK09754 287 HRCESWENANNQAQIAAAAMLGLPLPLLPPPWFWSD 322
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
204-517 |
6.88e-27 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 113.30 E-value: 6.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 204 LIVGGGTAAFSAFRAI-KSNDARAKVLMISneyRKPYMrpplskelWYTPnpnedpikdyrfkqwtgserSLY------F 276
Cdd:COG1252 5 VIVGGGFAGLEAARRLrKKLGGDAEVTLID---PNPYH--------LFQP--------------------LLPevaagtL 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 277 EPDEFFVDPEKLDEsvNGGIAVAQGfAVKKIDAQNRIATLNDGYQIGYDVCLIATGCApknlPMFHDTaPSVREKVMVYR 356
Cdd:COG1252 54 SPDDIAIPLRELLR--RAGVRFIQG-EVTGIDPEARTVTLADGRTLSYDYLVIATGSV----TNFFGI-PGLAEHALPLK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 357 TPDDFDRLRR---------YAKEKRSITIVGNGFVGSELACSLAHYSRHNNggKIYQVFPEKGN------MSRVLPNY-- 419
Cdd:COG1252 126 TLEDALALRErllaaferaERRRLLTIVVVGGGPTGVELAGELAELLRKLL--RYPGIDPDKVRitlveaGPRILPGLge 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 420 -LSTWTTRKVQAQGVCVIPEASIKSATRDdsqlKLELNNGMSVLSDIVVVCVGCSPNTAMAGpSKLEVDRtlGGFV-VNA 497
Cdd:COG1252 204 kLSEAAEKELEKRGVEVHTGTRVTEVDAD----GVTLEDGEEIPADTVIWAAGVKAPPLLAD-LGLPTDR--RGRVlVDP 276
|
330 340
....*....|....*....|..
gi 195034902 498 ELEARR--NLYVAGDACCFYDP 517
Cdd:COG1252 277 TLQVPGhpNVFAIGDCAAVPDP 298
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
204-546 |
2.62e-14 |
|
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: 75.51 E-value: 2.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 204 LIVGGGTAAFSAfrAIKSNDARAKVLMIsnEyrkpymRPPL-----------SKELWYTPNPNEDpIKDYRFKQWTGSER 272
Cdd:COG1249 7 VVIGAGPGGYVA--AIRAAQLGLKVALV--E------KGRLggtclnvgcipSKALLHAAEVAHE-ARHAAEFGISAGAP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 273 SlyfepdeffVDPEKLDESVNG----------------GIAVAQGFAvkKIDAQNRIaTLNDGYQIGYDVCLIATGCAPK 336
Cdd:COG1249 76 S---------VDWAALMARKDKvvdrlrggveellkknGVDVIRGRA--RFVDPHTV-EVTGGETLTADHIVIATGSRPR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 337 NLPMfhdtaPSVREKVMVyrTPDDFDRLRRYAKekrSITIVGNGFVGSELACSLAHYsrhnnGGKIYQVfpekGNMSRVL 416
Cdd:COG1249 144 VPPI-----PGLDEVRVL--TSDEALELEELPK---SLVVIGGGYIGLEFAQIFARL-----GSEVTLV----ERGDRLL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 417 PNY---LSTWTTRKVQAQGVCVIPEASIKSATRDDSQLKLELNNG---MSVLSDIVVVCVGCSPNTAMAGPSKLEVDRTL 490
Cdd:COG1249 205 PGEdpeISEALEKALEKEGIDILTGAKVTSVEKTGDGVTVTLEDGggeEAVEADKVLVATGRRPNTDGLGLEAAGVELDE 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 195034902 491 GGFV-VNAELE-ARRNLYVAGDACcfydpllGRRRVEH---HDhsvvsGRLAGENMTGAKK 546
Cdd:COG1249 285 RGGIkVDEYLRtSVPGIYAIGDVT-------GGPQLAHvasAE-----GRVAAENILGKKP 333
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
202-510 |
2.75e-14 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 74.95 E-value: 2.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 202 PYLIVGGGTAAFSAFRAIKSNDARAKVLMISN----EYRKPYMRPPLSKElwYTPnpnEDPIKDyrfkqwTGSErslyfe 277
Cdd:PRK04965 4 GIVIIGSGFAARQLVKNIRKQDAHIPITLITAdsgdEYNKPDLSHVFSQG--QRA---DDLTRQ------SAGE------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 278 pdeffvdpekLDESVNggIAVAQGFAVKKIDAQNRIATLNDGyQIGYDVCLIATGCAPKNLPMFHD----TAPSVREkvm 353
Cdd:PRK04965 67 ----------FAEQFN--LRLFPHTWVTDIDAEAQVVKSQGN-QWQYDKLVLATGASAFVPPIPGRelmlTLNSQQE--- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 354 vYRTPDDfdRLRRyakeKRSITIVGNGFVGSELACSLAHysrhnNGGKIYQVFPEKGNMSRVLPNYLSTWTTRKVQAQGV 433
Cdd:PRK04965 131 -YRAAET--QLRD----AQRVLVVGGGLIGTELAMDLCR-----AGKAVTLVDNAASLLASLMPPEVSSRLQHRLTEMGV 198
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 195034902 434 CVIPEASIKSATRDDSQLKLELNNGMSVLSDIVVVCVGCSPNTAMAGPSKLEVDRtlgGFVVNAELE-ARRNLYVAGD 510
Cdd:PRK04965 199 HLLLKSQLQGLEKTDSGIRATLDSGRSIEVDAVIAAAGLRPNTALARRAGLAVNR---GIVVDSYLQtSAPDIYALGD 273
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
280-549 |
2.90e-12 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 69.30 E-value: 2.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 280 EFFVDPEKL-----DESVNGGIAVAQGFAVKKIDAQNRIATL-----NDGYQIGYDVCLIATGCAPKnLPMFHDTAPsvr 349
Cdd:PRK09564 50 GFFDDPNTMiartpEEFIKSGIDVKTEHEVVKVDAKNKTITVknlktGSIFNDTYDKLMIATGARPI-IPPIKNINL--- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 350 EKVMVYRTPDDFDRLRRYAKEKR--SITIVGNGFVGSELACSLAHYSRHNnggKIYQ----VFPEK--GNMSRVLPNYLs 421
Cdd:PRK09564 126 ENVYTLKSMEDGLALKELLKDEEikNIVIIGAGFIGLEAVEAAKHLGKNV---RIIQledrILPDSfdKEITDVMEEEL- 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 422 twttrkvQAQGVCVIPEASIKSATRDDSQLKLELNNGmSVLSDIVVVCVGCSPNTAMAGPSKLEVDRTlGGFVVNAELEA 501
Cdd:PRK09564 202 -------RENGVELHLNEFVKSLIGEDKVEGVVTDKG-EYEADVVIVATGVKPNTEFLEDTGLKTLKN-GAIIVDEYGET 272
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 195034902 502 R-RNLYVAGDACCFYDPLLGRRrvehhDHSVVS------GRLAGENMTGAKKPYQ 549
Cdd:PRK09564 273 SiENIYAAGDCATIYNIVSNKN-----VYVPLAttanklGRMVGENLAGRHVSFK 322
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
373-458 |
1.91e-06 |
|
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: 46.04 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 373 SITIVGNGFVGSELACSLAHYsrhnnGGKIYqVFPEKGNMSRVLPNYLSTWTTRKVQAQGVCVIPEASIKSATRDDSQLK 452
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARL-----GSKVT-VVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVV 74
|
....*.
gi 195034902 453 LELNNG 458
Cdd:pfam00070 75 VVLTDG 80
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
295-392 |
1.70e-05 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 48.19 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 295 GIAVAQGFAVKKIDAQNRIATLNDGYQIGYDVCLIATGCAPKNLPMfhdtAPSVREKVMVYRTPDDFDRLRRYAKEKRSI 374
Cdd:PRK14989 73 GIKVLVGERAITINRQEKVIHSSAGRTVFYDKLIMATGSYPWIPPI----KGSETQDCFVYRTIEDLNAIEACARRSKRG 148
|
90
....*....|....*...
gi 195034902 375 TIVGNGFVGSELACSLAH 392
Cdd:PRK14989 149 AVVGGGLLGLEAAGALKN 166
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
316-512 |
2.18e-04 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 44.22 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 316 LNDGYQIGYDVCLIATGcapkNLPMFhdtaPSVREKVMVYRTpDDFDRLrryaKEKRSITIVGNGFVGSELACSLahysr 395
Cdd:PTZ00058 195 LDDGQVIEGKNILIAVG----NKPIF----PDVKGKEFTISS-DDFFKI----KEAKRIGIAGSGYIAVELINVV----- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195034902 396 hNNGGKIYQVFPEKGNMSRVLPNYLSTWTTRKVQAQGVCVIPEASIKSATRDDSQ--LKLELNNGMSVLSDIVVVCVGCS 473
Cdd:PTZ00058 257 -NRLGAESYIFARGNRLLRKFDETIINELENDMKKNNINIITHANVEEIEKVKEKnlTIYLSDGRKYEHFDYVIYCVGRS 335
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 195034902 474 PNTAMAGPSKLeVDRTLGGFVV--NAELEARRNLYVAGDAC 512
Cdd:PTZ00058 336 PNTEDLNLKAL-NIKTPKGYIKvdDNQRTSVKHIYAVGDCC 375
|
|
| |
