|
Name |
Accession |
Description |
Interval |
E-value |
| AIF_C |
pfam14721 |
Apoptosis-inducing factor, mitochondrion-associated, C-term; This C-terminal domain appears to ... |
465-594 |
1.03e-81 |
|
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: 252.57 E-value: 1.03e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 465 AGENMTGAAKPYWHQSMFWSDLGPDVGYEAIGLVDSSLPTVGVFAKATAQDNPKSATEQSGTGIRSESETESEASEITIP 544
Cdd:pfam14721 1 AGENMTGAGKPYWHQSMFWSDLGPDVGYEAIGIVDSSLPTVGVFAKATEKDTPKAVVEESGESIRSESEEEATASASAAP 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 4757732 545 PSTPAVPQAPVQGEDYGKGVIFYLRDKVVVGIVLWNIFNRMPIARKIIKD 594
Cdd:pfam14721 81 SSEDVASEDPSPGEDYGKGVIFYLRDDKVVGIVLWNVFNRMPIARKIIKD 130
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
148-596 |
3.24e-66 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 221.94 E-value: 3.24e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 148 RSIRARDPGARVLIVSEDPELPYMRPPLSKELwfsddpnvtktlrfkqwNGK--ERSIYFQPPSFYvsaqdlphiENGGV 225
Cdd:COG1251 18 EELRKLDPDGEITVIGAEPHPPYNRPPLSKVL-----------------AGEtdEEDLLLRPADFY---------EENGI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 226 AVLTGKKVVQLDVRDNMVKLNDGSQITYEKCLIATGGTPRSLSAidrAGAEVKSRTTlFRKIGDFRSLEKISREVKSITI 305
Cdd:COG1251 72 DLRLGTRVTAIDRAARTVTLADGETLPYDKLVLATGSRPRVPPI---PGADLPGVFT-LRTLDDADALRAALAPGKRVVV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 306 IGGGFLGSELACALgrkaRALGTEVIQLFPEKGNMGKILPEYLSNWTMEKVRREGVKVMPNAIVQSVGVSSGKLLIKLKD 385
Cdd:COG1251 148 IGGGLIGLEAAAAL----RKRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTGVRLAD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 386 GRKVETDHIVAAVGLEPNVELAKTGGLEIDsdfGGFRVNAELQA-RSNIWVAGDAACFYDIKLGRRRVEHHDHAVVSGRL 464
Cdd:COG1251 224 GEELPADLVVVAIGVRPNTELARAAGLAVD---RGIVVDDYLRTsDPDIYAAGDCAEHPGPVYGRRVLELVAPAYEQARV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 465 AGENMTGAAKPYWH-QSMFWSDLgPDVGYEAIGLVDsslptvgvfakataqdnpksATEQSgtgirseseteseaseiti 543
Cdd:COG1251 301 AAANLAGGPAAYEGsVPSTKLKV-FGVDVASAGDAE--------------------GDEEV------------------- 340
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 4757732 544 ppstpavpqapVQGEDYGKGVI--FYLRDKVVVGIVLWNIFNRMPIARKIIKDGE 596
Cdd:COG1251 341 -----------VVRGDPARGVYkkLVLRDGRLVGAVLVGDTSDAGALRQLIKNGR 384
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
150-462 |
2.10e-39 |
|
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: 146.31 E-value: 2.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 150 IRARDPGARVLIVSEDPELPYMRPPLSKELWFSDDPnvtktlrfkqwngkeRSIYFQPPSFYVSAQDLPHIENGGVAVLT 229
Cdd:pfam07992 17 LTLAQLGGKVTLIEDEGTCPYGGCVLSKALLGAAEA---------------PEIASLWADLYKRKEEVVKKLNNGIEVLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 230 GKKVVQLD-----VRDNMVKLNDGSQITYEKCLIATGGTPRSLSAidrAGAEvKSRTTLFRKIGDFRSLEKISREvKSIT 304
Cdd:pfam07992 82 GTEVVSIDpgakkVVLEELVDGDGETITYDRLVIATGARPRLPPI---PGVE-LNVGFLVRTLDSAEALRLKLLP-KRVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 305 IIGGGFLGSELACALgrkaRALGTEV--IQLFPEkgnMGKILPEYLSNWTMEKVRREGVKVMPNAIVQSVGVSSGKLLIK 382
Cdd:pfam07992 157 VVGGGYIGVELAAAL----AKLGKEVtlIEALDR---LLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGVEVI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 383 LKDGRKVETDHIVAAVGLEPNVELAKTGGLEIDSDfGGFRVNAELQ-ARSNIWVAGDAacfydiklGRRRVEHHDHAVVS 461
Cdd:pfam07992 230 LKDGTEIDADLVVVAIGRRPNTELLEAAGLELDER-GGIVVDEYLRtSVPGIYAAGDC--------RVGGPELAQNAVAQ 300
|
.
gi 4757732 462 G 462
Cdd:pfam07992 301 G 301
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
149-485 |
5.09e-24 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 104.62 E-value: 5.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 149 SIRARDPGARVLIVSEDPELPYMRPPLSKELWFSDDPNVTktlrfkqwngkersiYFQPPSFYVSAQdlphienggVAVL 228
Cdd:PRK09754 21 SLRQQGFTGELHLFSDERHLPYERPPLSKSMLLEDSPQLQ---------------QVLPANWWQENN---------VHLH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 229 TGKKVVQLDVRDNMVKLNDGSQITYEKCLIATGGTPRSLSAIDRAGAEVKSrttlFRKIGDFRSLEKISREVKSITIIGG 308
Cdd:PRK09754 77 SGVTIKTLGRDTRELVLTNGESWHWDQLFIATGAAARPLPLLDALGERCFT----LRHAGDAARLREVLQPERSVVIVGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 309 GFLGSELACAlgrkARALGTEVIQLFPEKGNMGKILPEYLSNWTMEKVRREGVKVMPNAIVQSVgVSSGKLLIKLKDGRK 388
Cdd:PRK09754 153 GTIGLELAAS----ATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHV-VDGEKVELTLQSGET 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 389 VETDHIVAAVGLEPNVELAKTGGLEIDsdfGGFRVNAELQ-ARSNIWVAGDAACFYDIKLGRRRVEHHDHAVVSGRLAGE 467
Cdd:PRK09754 228 LQADVVIYGIGISANDQLAREANLDTA---NGIVIDEACRtCDPAIFAGGDVAITRLDNGALHRCESWENANNQAQIAAA 304
|
330
....*....|....*...
gi 4757732 468 NMTGAAKPYWHQSMFWSD 485
Cdd:PRK09754 305 AMLGLPLPLLPPPWFWSD 322
|
|
| AIF-MLS |
pfam14962 |
Mitochondria localization Sequence; This family contains a protein found in eukaryotes. ... |
52-133 |
4.28e-05 |
|
Mitochondria localization Sequence; This family contains a protein found in eukaryotes. Proteins in this family are typically between 240 and 613 amino acids in length. The family is found in association with pfam07992. This protein family is an N-terminal domain for the mitochondrial localization sequence for an apoptosis-inducing factor. The protein is also known as Corneal endothelium-specific protein 1 or as Ovary-specific acidic protein. It is thought to be important for membrane function and is expressed in the ovary and corneal endothelium.
Pssm-ID: 464407 [Multi-domain] Cd Length: 192 Bit Score: 44.82 E-value: 4.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 52 RQMASS---GASGgkiDNSVLVLIVGLsTVGAGAY-AYKTMKEDEKRYNERISGLgltpeQKQKKAALSASEGEE---VP 124
Cdd:pfam14962 31 RRMSSNkfpGSSG---SNMIYYLVVGV-TVSAGGYyTYKTVTSEQAKHTEHVTNL-----KEKTKAELHPLQGEKenvAE 101
|
....*....
gi 4757732 125 QDKAPSHVP 133
Cdd:pfam14962 102 AEKASSEAP 110
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| AIF_C |
pfam14721 |
Apoptosis-inducing factor, mitochondrion-associated, C-term; This C-terminal domain appears to ... |
465-594 |
1.03e-81 |
|
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: 252.57 E-value: 1.03e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 465 AGENMTGAAKPYWHQSMFWSDLGPDVGYEAIGLVDSSLPTVGVFAKATAQDNPKSATEQSGTGIRSESETESEASEITIP 544
Cdd:pfam14721 1 AGENMTGAGKPYWHQSMFWSDLGPDVGYEAIGIVDSSLPTVGVFAKATEKDTPKAVVEESGESIRSESEEEATASASAAP 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 4757732 545 PSTPAVPQAPVQGEDYGKGVIFYLRDKVVVGIVLWNIFNRMPIARKIIKD 594
Cdd:pfam14721 81 SSEDVASEDPSPGEDYGKGVIFYLRDDKVVGIVLWNVFNRMPIARKIIKD 130
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
148-596 |
3.24e-66 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 221.94 E-value: 3.24e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 148 RSIRARDPGARVLIVSEDPELPYMRPPLSKELwfsddpnvtktlrfkqwNGK--ERSIYFQPPSFYvsaqdlphiENGGV 225
Cdd:COG1251 18 EELRKLDPDGEITVIGAEPHPPYNRPPLSKVL-----------------AGEtdEEDLLLRPADFY---------EENGI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 226 AVLTGKKVVQLDVRDNMVKLNDGSQITYEKCLIATGGTPRSLSAidrAGAEVKSRTTlFRKIGDFRSLEKISREVKSITI 305
Cdd:COG1251 72 DLRLGTRVTAIDRAARTVTLADGETLPYDKLVLATGSRPRVPPI---PGADLPGVFT-LRTLDDADALRAALAPGKRVVV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 306 IGGGFLGSELACALgrkaRALGTEVIQLFPEKGNMGKILPEYLSNWTMEKVRREGVKVMPNAIVQSVGVSSGKLLIKLKD 385
Cdd:COG1251 148 IGGGLIGLEAAAAL----RKRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTGVRLAD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 386 GRKVETDHIVAAVGLEPNVELAKTGGLEIDsdfGGFRVNAELQA-RSNIWVAGDAACFYDIKLGRRRVEHHDHAVVSGRL 464
Cdd:COG1251 224 GEELPADLVVVAIGVRPNTELARAAGLAVD---RGIVVDDYLRTsDPDIYAAGDCAEHPGPVYGRRVLELVAPAYEQARV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 465 AGENMTGAAKPYWH-QSMFWSDLgPDVGYEAIGLVDsslptvgvfakataqdnpksATEQSgtgirseseteseaseiti 543
Cdd:COG1251 301 AAANLAGGPAAYEGsVPSTKLKV-FGVDVASAGDAE--------------------GDEEV------------------- 340
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 4757732 544 ppstpavpqapVQGEDYGKGVI--FYLRDKVVVGIVLWNIFNRMPIARKIIKDGE 596
Cdd:COG1251 341 -----------VVRGDPARGVYkkLVLRDGRLVGAVLVGDTSDAGALRQLIKNGR 384
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
152-486 |
3.71e-50 |
|
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: 176.54 E-value: 3.71e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 152 ARDPGARVLIVSEDPELPYMRPPLSKELWFSDDpnvtktlrfkqwngKERSIYFQPPSFYVSAqdlphiengGVAVLTGK 231
Cdd:COG0446 1 RLGPDAEITVIEKGPHHSYQPCGLPYYVGGGIK--------------DPEDLLVRTPESFERK---------GIDVRTGT 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 232 KVVQLDVRDNMVKLNDGSQITYEKCLIATGGTPRSLsAIDraGAEVKSRTTLfRKIGDFRSL-EKI-SREVKSITIIGGG 309
Cdd:COG0446 58 EVTAIDPEAKTVTLRDGETLSYDKLVLATGARPRPP-PIP--GLDLPGVFTL-RTLDDADALrEALkEFKGKRAVVIGGG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 310 FLGSELACALgrkaRALGTEVIQLFPEKGNMGKILPEYlSNWTMEKVRREGVKVMPNAIVQSVgVSSGKLLIKLKDGRKV 389
Cdd:COG0446 134 PIGLELAEAL----RKRGLKVTLVERAPRLLGVLDPEM-AALLEEELREHGVELRLGETVVAI-DGDDKVAVTLTDGEEI 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 390 ETDHIVAAVGLEPNVELAKTGGLEIDSDfGGFRVNAELQAR-SNIWVAGDAACFYDIKLGRR-RVEHHDHAVVSGRLAGE 467
Cdd:COG0446 208 PADLVVVAPGVRPNTELAKDAGLALGER-GWIKVDETLQTSdPDVYAAGDCAEVPHPVTGKTvYIPLASAANKQGRVAAE 286
|
330
....*....|....*....
gi 4757732 468 NMTGAAKPYWHQSMFWSDL 486
Cdd:COG0446 287 NILGGPAPFPGLGTFISKV 305
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
150-462 |
2.10e-39 |
|
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: 146.31 E-value: 2.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 150 IRARDPGARVLIVSEDPELPYMRPPLSKELWFSDDPnvtktlrfkqwngkeRSIYFQPPSFYVSAQDLPHIENGGVAVLT 229
Cdd:pfam07992 17 LTLAQLGGKVTLIEDEGTCPYGGCVLSKALLGAAEA---------------PEIASLWADLYKRKEEVVKKLNNGIEVLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 230 GKKVVQLD-----VRDNMVKLNDGSQITYEKCLIATGGTPRSLSAidrAGAEvKSRTTLFRKIGDFRSLEKISREvKSIT 304
Cdd:pfam07992 82 GTEVVSIDpgakkVVLEELVDGDGETITYDRLVIATGARPRLPPI---PGVE-LNVGFLVRTLDSAEALRLKLLP-KRVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 305 IIGGGFLGSELACALgrkaRALGTEV--IQLFPEkgnMGKILPEYLSNWTMEKVRREGVKVMPNAIVQSVGVSSGKLLIK 382
Cdd:pfam07992 157 VVGGGYIGVELAAAL----AKLGKEVtlIEALDR---LLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGVEVI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 383 LKDGRKVETDHIVAAVGLEPNVELAKTGGLEIDSDfGGFRVNAELQ-ARSNIWVAGDAacfydiklGRRRVEHHDHAVVS 461
Cdd:pfam07992 230 LKDGTEIDADLVVVAIGRRPNTELLEAAGLELDER-GGIVVDEYLRtSVPGIYAAGDC--------RVGGPELAQNAVAQ 300
|
.
gi 4757732 462 G 462
Cdd:pfam07992 301 G 301
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
220-471 |
4.94e-26 |
|
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: 111.33 E-value: 4.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 220 IENGGVAVLTGKKVVqldVRDNMVKLNDGSQITYEKCLIATGGTPRSLSAIDRAGAEVKSRTTLFrkigdfrSLEKIsre 299
Cdd:COG1249 101 LKKNGVDVIRGRARF---VDPHTVEVTGGETLTADHIVIATGSRPRVPPIPGLDEVRVLTSDEAL-------ELEEL--- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 300 VKSITIIGGGFLGSELACALgrkaRALGTEVIQLfpekGNMGKILP---EYLSNWTMEKVRREGVKVMPNAIVQSVGVSS 376
Cdd:COG1249 168 PKSLVVIGGGYIGLEFAQIF----ARLGSEVTLV----ERGDRLLPgedPEISEALEKALEKEGIDILTGAKVTSVEKTG 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 377 GKLLIKLKDGRKVET---DHIVAAVGLEPNVE---LAKTgGLEIDSDfGGFRVNAELQ-ARSNIWVAGDAAcfydiklGR 449
Cdd:COG1249 240 DGVTVTLEDGGGEEAveaDKVLVATGRRPNTDglgLEAA-GVELDER-GGIKVDEYLRtSVPGIYAIGDVT-------GG 310
|
250 260
....*....|....*....|..
gi 4757732 450 RRVEHhdHAVVSGRLAGENMTG 471
Cdd:COG1249 311 PQLAH--VASAEGRVAAENILG 330
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
149-485 |
5.09e-24 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 104.62 E-value: 5.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 149 SIRARDPGARVLIVSEDPELPYMRPPLSKELWFSDDPNVTktlrfkqwngkersiYFQPPSFYVSAQdlphienggVAVL 228
Cdd:PRK09754 21 SLRQQGFTGELHLFSDERHLPYERPPLSKSMLLEDSPQLQ---------------QVLPANWWQENN---------VHLH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 229 TGKKVVQLDVRDNMVKLNDGSQITYEKCLIATGGTPRSLSAIDRAGAEVKSrttlFRKIGDFRSLEKISREVKSITIIGG 308
Cdd:PRK09754 77 SGVTIKTLGRDTRELVLTNGESWHWDQLFIATGAAARPLPLLDALGERCFT----LRHAGDAARLREVLQPERSVVIVGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 309 GFLGSELACAlgrkARALGTEVIQLFPEKGNMGKILPEYLSNWTMEKVRREGVKVMPNAIVQSVgVSSGKLLIKLKDGRK 388
Cdd:PRK09754 153 GTIGLELAAS----ATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHV-VDGEKVELTLQSGET 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 389 VETDHIVAAVGLEPNVELAKTGGLEIDsdfGGFRVNAELQ-ARSNIWVAGDAACFYDIKLGRRRVEHHDHAVVSGRLAGE 467
Cdd:PRK09754 228 LQADVVIYGIGISANDQLAREANLDTA---NGIVIDEACRtCDPAIFAGGDVAITRLDNGALHRCESWENANNQAQIAAA 304
|
330
....*....|....*...
gi 4757732 468 NMTGAAKPYWHQSMFWSD 485
Cdd:PRK09754 305 AMLGLPLPLLPPPWFWSD 322
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
218-468 |
4.53e-23 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 101.36 E-value: 4.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 218 PHIENGGVAVLTGKkVVQLDVRDNMVKLNDGSQITYEKCLIATGGTPRsLSAIDraGAE-----VKSR---TTLFRKIgd 289
Cdd:COG1252 64 ELLRRAGVRFIQGE-VTGIDPEARTVTLADGRTLSYDYLVIATGSVTN-FFGIP--GLAehalpLKTLedaLALRERL-- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 290 FRSLEKISREVK-SITIIGGGFLGSELACALGRKARALGTEViQLFPEKGN------MGKILPEY---LSNWTMEKVRRE 359
Cdd:COG1252 138 LAAFERAERRRLlTIVVVGGGPTGVELAGELAELLRKLLRYP-GIDPDKVRitlveaGPRILPGLgekLSEAAEKELEKR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 360 GVKVMPNAIVQSvgVSSGKllIKLKDGRKVETDHIVAAVGLEPNvELAKTGGLEIDSDfGGFRVNAELQARS--NIWVAG 437
Cdd:COG1252 217 GVEVHTGTRVTE--VDADG--VTLEDGEEIPADTVIWAAGVKAP-PLLADLGLPTDRR-GRVLVDPTLQVPGhpNVFAIG 290
|
250 260 270
....*....|....*....|....*....|....*..
gi 4757732 438 DAACFYDI------KLGRrrvehhdHAVVSGRLAGEN 468
Cdd:COG1252 291 DCAAVPDPdgkpvpKTAQ-------AAVQQAKVLAKN 320
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
224-476 |
3.53e-19 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 90.48 E-value: 3.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 224 GVAVLTGKKVVQLDVRDNMVK---LNDGSQI--TYEKCLIATGGTPrSLSAIDraGAEVKSRTTLfRKIGDFRSLEKISR 298
Cdd:PRK09564 70 GIDVKTEHEVVKVDAKNKTITvknLKTGSIFndTYDKLMIATGARP-IIPPIK--NINLENVYTL-KSMEDGLALKELLK 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 299 --EVKSITIIGGGFLGSELACAlgrkARALGTEV--IQLfpEKGNMGKILPEYLSNWTMEKVRREGVKVMPNAIVQSVgV 374
Cdd:PRK09564 146 deEIKNIVIIGAGFIGLEAVEA----AKHLGKNVriIQL--EDRILPDSFDKEITDVMEEELRENGVELHLNEFVKSL-I 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 375 SSGKLLIKLKDGRKVETDHIVAAVGLEPNVELAKTGGLEIDSDfGGFRVNAELQAR-SNIWVAGDAACFYDIKLGRRR-V 452
Cdd:PRK09564 219 GEDKVEGVVTDKGEYEADVVIVATGVKPNTEFLEDTGLKTLKN-GAIIVDEYGETSiENIYAAGDCATIYNIVSNKNVyV 297
|
250 260
....*....|....*....|....
gi 4757732 453 EHHDHAVVSGRLAGENMTGAAKPY 476
Cdd:PRK09564 298 PLATTANKLGRMVGENLAGRHVSF 321
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
225-440 |
4.92e-18 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 86.12 E-value: 4.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 225 VAVLTGKKVVQLDVRDNMVKLNDGsQITYEKCLIATGGTP--------------RSLSaidragaevksrttlfrkigDF 290
Cdd:PRK04965 73 LRLFPHTWVTDIDAEAQVVKSQGN-QWQYDKLVLATGASAfvppipgrelmltlNSQQ--------------------EY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 291 RSLEKISREVKSITIIGGGFLGSELACALgrkARAlGTEVIQLFPEKGNMGKILPEYLSNWTMEKVRREGVKVMPNAIVQ 370
Cdd:PRK04965 132 RAAETQLRDAQRVLVVGGGLIGTELAMDL---CRA-GKAVTLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQLQ 207
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4757732 371 SVGVSSGKLLIKLKDGRKVETDHIVAAVGLEPNVELAKTGGLEIDSdfgGFRVNAELQ-ARSNIWVAGDAA 440
Cdd:PRK04965 208 GLEKTDSGIRATLDSGRSIEVDAVIAAAGLRPNTALARRAGLAVNR---GIVVDSYLQtSAPDIYALGDCA 275
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
221-438 |
1.19e-16 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 82.90 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 221 ENGGVAVLTGKKVVqldVRDNMVKLNdGSQITYEKCLIATGGTPrslSAIDRAGAE--VKSRttlfrkigDFRSLEKISr 298
Cdd:PRK06116 104 ENNGVDLIEGFARF---VDAHTVEVN-GERYTADHILIATGGRP---SIPDIPGAEygITSD--------GFFALEELP- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 299 evKSITIIGGGFLGSELACALgrkaRALGTEVIQLFpeKGNmgKIL---PEYLSNWTMEKVRREGVKVMPNAIVQSVG-V 374
Cdd:PRK06116 168 --KRVAVVGAGYIAVEFAGVL----NGLGSETHLFV--RGD--APLrgfDPDIRETLVEEMEKKGIRLHTNAVPKAVEkN 237
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4757732 375 SSGKLLIKLKDGRKVETDHIVAAVGLEPNVE---LAKTgGLEIDsDFGGFRVNAELQ-ARSNIWVAGD 438
Cdd:PRK06116 238 ADGSLTLTLEDGETLTVDCLIWAIGREPNTDglgLENA-GVKLN-EKGYIIVDEYQNtNVPGIYAVGD 303
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
221-440 |
3.18e-16 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 82.47 E-value: 3.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 221 ENGGVAVLTGKKVVQLDVRDNMVKLNDGSQITYEKCLIATGGTPrSLSAIdrAGAEVKSrTTLFRKIGDFRSLEKISREV 300
Cdd:PRK14989 70 EKHGIKVLVGERAITINRQEKVIHSSAGRTVFYDKLIMATGSYP-WIPPI--KGSETQD-CFVYRTIEDLNAIEACARRS 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 301 KSITIIGGGFLGSELACALgrKARALGTEVIQLFPekgnmgKILPEYLSNWTMEKVRRE----GVKVMPN----AIVQSv 372
Cdd:PRK14989 146 KRGAVVGGGLLGLEAAGAL--KNLGVETHVIEFAP------MLMAEQLDQMGGEQLRRKiesmGVRVHTSkntlEIVQE- 216
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4757732 373 GVSSGKLLiKLKDGRKVETDHIVAAVGLEPNVELAKTGGLEIdSDFGGFRVNAELQ-ARSNIWVAGDAA 440
Cdd:PRK14989 217 GVEARKTM-RFADGSELEVDFIVFSTGIRPQDKLATQCGLAV-APRGGIVINDSCQtSDPDIYAIGECA 283
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
224-438 |
7.01e-14 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 74.08 E-value: 7.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 224 GVAVLTGKKVVQLDvrdnmvklndGSQITYEKCLIATGGTPR--SLSAIDRAGAevKSRTTLFrkigdfrSLEKISRevk 301
Cdd:PRK06370 115 GHARFESPNTVRVG----------GETLRAKRIFINTGARAAipPIPGLDEVGY--LTNETIF-------SLDELPE--- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 302 SITIIGGGFLGSELACALGRkaraLGTEVIQLfpEKGNmgKILP---EYLSNWTMEKVRREGVKVMPNAIVQSVGVSSGK 378
Cdd:PRK06370 173 HLVIIGGGYIGLEFAQMFRR----FGSEVTVI--ERGP--RLLPredEDVAAAVREILEREGIDVRLNAECIRVERDGDG 244
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4757732 379 LLIKLK---DGRKVETDHIVAAVGLEPNVE---LAKTgGLEIDSDfGGFRVNAELQAR-SNIWVAGD 438
Cdd:PRK06370 245 IAVGLDcngGAPEITGSHILVAVGRVPNTDdlgLEAA-GVETDAR-GYIKVDDQLRTTnPGIYAAGD 309
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
224-476 |
1.12e-13 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 73.67 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 224 GVAVLTGKKVVQLDvrdnmvklndGSQITYEKCLIATGGTPRSLSAIDRA-GAEVKSRTTLFrkigdfrSLEKISrevKS 302
Cdd:PRK06292 112 GTARFVDPNTVEVN----------GERIEAKNIVIATGSRVPPIPGVWLIlGDRLLTSDDAF-------ELDKLP---KS 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 303 ITIIGGGFLGSELACALGRkaraLGTEVIqLFPEKGNMGKILPEYLSNWTMEKVRREgVKVMPNAIVQSVGVSSGKLLIK 382
Cdd:PRK06292 172 LAVIGGGVIGLELGQALSR----LGVKVT-VFERGDRILPLEDPEVSKQAQKILSKE-FKIKLGAKVTSVEKSGDEKVEE 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 383 LKDGRKVET---DHIVAAVGLEPNVE---LAKTgGLEIDSDfgGF-RVNAEL-QARSNIWVAGDAAcfydiklGRRRVEH 454
Cdd:PRK06292 246 LEKGGKTETieaDYVLVATGRRPNTDglgLENT-GIELDER--GRpVVDEHTqTSVPGIYAAGDVN-------GKPPLLH 315
|
250 260
....*....|....*....|..
gi 4757732 455 hdHAVVSGRLAGENMTGAAKPY 476
Cdd:PRK06292 316 --EAADEGRIAAENAAGDVAGG 335
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
302-386 |
2.11e-11 |
|
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: 59.91 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 302 SITIIGGGFLGSELACALgrkaRALGTEViQLFPEKGNMGKILPEYLSNWTMEKVRREGVKVMPNAIVQSVGVSSGKLLI 381
Cdd:pfam00070 1 RVVVVGGGYIGLELAGAL----ARLGSKV-TVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVV 75
|
....*
gi 4757732 382 KLKDG 386
Cdd:pfam00070 76 VLTDG 80
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
243-474 |
6.34e-11 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 64.79 E-value: 6.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 243 VKLNDGS--QITYEKCLIATGGTPRSLSAIDRAGaevksrttlfRKIGDFRSLEKISREVKSITIIGGGFLGSELACALg 320
Cdd:PRK05249 126 VECPDGEveTLTADKIVIATGSRPYRPPDVDFDH----------PRIYDSDSILSLDHLPRSLIIYGAGVIGCEYASIF- 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 321 rkaRALGTEVIQLfpekgNMGKILPEYLSNWTME----KVRREGVKVMPNAIVQSVGVSSGKLLIKLKDGRKVETDHIVA 396
Cdd:PRK05249 195 ---AALGVKVTLI-----NTRDRLLSFLDDEISDalsyHLRDSGVTIRHNEEVEKVEGGDDGVIVHLKSGKKIKADCLLY 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 397 AVGLEPNVE---LAKTgGLEIDSDfGGFRVNAELQ-ARSNIWVAGD-------AACFYDiklgrrrvehhdhavvSGRLA 465
Cdd:PRK05249 267 ANGRTGNTDglnLENA-GLEADSR-GQLKVNENYQtAVPHIYAVGDvigfpslASASMD----------------QGRIA 328
|
....*....
gi 4757732 466 GENMTGAAK 474
Cdd:PRK05249 329 AQHAVGEAT 337
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
224-440 |
2.11e-10 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 63.24 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 224 GVAVLTGKKVVQldvrdnmVKLNDGSQ-ITYEKCLIATGGTPRSLSAIDRAGaevksrttlfRKIGDFR---SLEKISre 299
Cdd:PRK06416 112 GEAKLVDPNTVR-------VMTEDGEQtYTAKNIILATGSRPRELPGIEIDG----------RVIWTSDealNLDEVP-- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 300 vKSITIIGGGFLGSELACALgrkaRALGTEVI------QLFP-EKGNMGKILpeylsnwtmEKV-RREGVKVMPNAIVQS 371
Cdd:PRK06416 173 -KSLVVIGGGYIGVEFASAY----ASLGAEVTivealpRILPgEDKEISKLA---------ERAlKKRGIKIKTGAKAKK 238
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4757732 372 VGVSSGKLLIKLKDGRKVET---DHIVAAVGLEPNVE---LAKTgGLEIDsdfGGF-RVNAELQAR-SNIWVAGDAA 440
Cdd:PRK06416 239 VEQTDDGVTVTLEDGGKEETleaDYVLVAVGRRPNTEnlgLEEL-GVKTD---RGFiEVDEQLRTNvPNIYAIGDIV 311
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
238-439 |
1.62e-09 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 60.78 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 238 VRDNMVKLNDGSQITYEKCLIATGGTPRSlsaIDRAGAEVKSRTTLFRKIgdfrslekisREVKSITIIGGGFLGSELAC 317
Cdd:PTZ00058 188 VSAGVSQLDDGQVIEGKNILIAVGNKPIF---PDVKGKEFTISSDDFFKI----------KEAKRIGIAGSGYIAVELIN 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 318 ALgrkaRALGTEViQLFPEKGNMGKILPEYLSNWTMEKVRREGVKVMPNAIVQSV-GVSSGKLLIKLKDGRKVET-DHIV 395
Cdd:PTZ00058 255 VV----NRLGAES-YIFARGNRLLRKFDETIINELENDMKKNNINIITHANVEEIeKVKEKNLTIYLSDGRKYEHfDYVI 329
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 4757732 396 AAVGLEPNVELAKTGGLEIDSDFGGFRVNaELQARS--NIWVAGDA 439
Cdd:PTZ00058 330 YCVGRSPNTEDLNLKALNIKTPKGYIKVD-DNQRTSvkHIYAVGDC 374
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
224-438 |
6.27e-07 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 52.17 E-value: 6.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 224 GVAVLTGK-KVVQLDVRDNMVK--LNDGSQITYEK--CLIATGGTPRSLsaidrAGAEVKSRTTL-FRKIGDfrsLEKIS 297
Cdd:PRK07845 106 GVRVIAGRgRLIDPGLGPHRVKvtTADGGEETLDAdvVLIATGASPRIL-----PTAEPDGERILtWRQLYD---LDELP 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 298 REvksITIIGGGFLGSELACALgrkaRALGTEVI------QLFP-EKGNMGKILpeylsnwtmEKV-RREGVKVMPNAIV 369
Cdd:PRK07845 178 EH---LIVVGSGVTGAEFASAY----TELGVKVTlvssrdRVLPgEDADAAEVL---------EEVfARRGMTVLKRSRA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 370 QSVGVSSGKLLIKLKDGRKVETDHIVAAVGLEPN----------VELAKTGGLEIDsdfggfRVnaelqARSN---IWVA 436
Cdd:PRK07845 242 ESVERTGDGVVVTLTDGRTVEGSHALMAVGSVPNtaglgleeagVELTPSGHITVD------RV-----SRTSvpgIYAA 310
|
..
gi 4757732 437 GD 438
Cdd:PRK07845 311 GD 312
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
219-440 |
3.25e-06 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 49.35 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 219 HIENGGVAVLTGKkVVQLDVRDN--MVKLNDGSQITYEKCLIATGGTPRSLSAidrAGAE----------VKSRTTLFRK 286
Cdd:COG0492 66 QAERFGAEILLEE-VTSVDKDDGpfRVTTDDGTEYEAKAVIIATGAGPRKLGL---PGEEefegrgvsycATCDGFFFRG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 287 igdfrslekisrevKSITIIGGGFLGSELACALGRKARalgtEVIqLFPEKGNM--GKILpeylsnwtMEKVRR-EGVKV 363
Cdd:COG0492 142 --------------KDVVVVGGGDSALEEALYLTKFAS----KVT-LIHRRDELraSKIL--------VERLRAnPKIEV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 364 MPNAIVQSV----GVSSgkllIKLKDG-----RKVETDHIVAAVGLEPNVELAKTGGLEIDSDfGGFRVNAELQ-ARSNI 433
Cdd:COG0492 195 LWNTEVTEIegdgRVEG----VTLKNVktgeeKELEVDGVFVAIGLKPNTELLKGLGLELDED-GYIVVDEDMEtSVPGV 269
|
....*..
gi 4757732 434 WVAGDAA 440
Cdd:COG0492 270 FAAGDVR 276
|
|
| AIF-MLS |
pfam14962 |
Mitochondria localization Sequence; This family contains a protein found in eukaryotes. ... |
52-133 |
4.28e-05 |
|
Mitochondria localization Sequence; This family contains a protein found in eukaryotes. Proteins in this family are typically between 240 and 613 amino acids in length. The family is found in association with pfam07992. This protein family is an N-terminal domain for the mitochondrial localization sequence for an apoptosis-inducing factor. The protein is also known as Corneal endothelium-specific protein 1 or as Ovary-specific acidic protein. It is thought to be important for membrane function and is expressed in the ovary and corneal endothelium.
Pssm-ID: 464407 [Multi-domain] Cd Length: 192 Bit Score: 44.82 E-value: 4.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 52 RQMASS---GASGgkiDNSVLVLIVGLsTVGAGAY-AYKTMKEDEKRYNERISGLgltpeQKQKKAALSASEGEE---VP 124
Cdd:pfam14962 31 RRMSSNkfpGSSG---SNMIYYLVVGV-TVSAGGYyTYKTVTSEQAKHTEHVTNL-----KEKTKAELHPLQGEKenvAE 101
|
....*....
gi 4757732 125 QDKAPSHVP 133
Cdd:pfam14962 102 AEKASSEAP 110
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
303-417 |
6.64e-05 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 45.29 E-value: 6.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 303 ITIIGGGFLGSELACALGRKaralGTEVIQLFPEKGnMGKILPEY---LSNWT----MEKVRREGVKVMPNAIVQSVGVS 375
Cdd:pfam13738 158 VVVIGGYNSAVDAALELVRK----GARVTVLYRGSE-WEDRDSDPsysLSPDTlnrlEELVKNGKIKAHFNAEVKEITEV 232
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 4757732 376 SGKLLIKLKDGRKVETDHI-VAAVGLEPNVELAKTGGLEIDSD 417
Cdd:pfam13738 233 DVSYKVHTEDGRKVTSNDDpILATGYHPDLSFLKKGLFELDED 275
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
205-440 |
1.17e-04 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 44.77 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 205 FQPPSFYvsaqdlphiENGGVAVLTGKKVVQLDVRDNMV-----KLNDGSQITYEKCLIATGGTPRSLsaidraGAEVKS 279
Cdd:PRK13512 62 YTPEKFY---------DRKQITVKTYHEVIAINDERQTVtvlnrKTNEQFEESYDKLILSPGASANSL------GFESDI 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 280 RTTLfRKIGDFRSLEK-ISR-EVKSITIIGGGFLGSELACALgrKARALGTEVIQlfpEKGNMGKILPEYLSNWTMEKVR 357
Cdd:PRK13512 127 TFTL-RNLEDTDAIDQfIKAnQVDKALVVGAGYISLEVLENL--YERGLHPTLIH---RSDKINKLMDADMNQPILDELD 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 358 REGVKVMPNAIVQSVGVSsgklLIKLKDGRKVETDHIVAAVGLEPNVELAKTGGLEIDsDFGGFRVNAELQAR-SNIWVA 436
Cdd:PRK13512 201 KREIPYRLNEEIDAINGN----EVTFKSGKVEHYDMIIEGVGTHPNSKFIESSNIKLD-DKGFIPVNDKFETNvPNIYAI 275
|
....
gi 4757732 437 GDAA 440
Cdd:PRK13512 276 GDII 279
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
243-438 |
2.60e-03 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 40.68 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 243 VKLNDGSQITYEKCLIATGGTPRSLSaidraGAEVKSRTTLfrkigDFRSLEKISREVKSITIIGGGFLGselaCALGRK 322
Cdd:PRK06327 136 VTGEDETVITAKHVIIATGSEPRHLP-----GVPFDNKIIL-----DNTGALNFTEVPKKLAVIGAGVIG----LELGSV 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 323 ARALGTEVIQLfpekgnmgKILPEYL-------SNWTMEKVRREGVKVMPNAIVQSVGVSSGKLLIKLKDG----RKVET 391
Cdd:PRK06327 202 WRRLGAEVTIL--------EALPAFLaaadeqvAKEAAKAFTKQGLDIHLGVKIGEIKTGGKGVSVAYTDAdgeaQTLEV 273
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 4757732 392 DHIVAAVGLEPNVE--LAKTGGLEIDsDFGGFRVNAELQAR-SNIWVAGD 438
Cdd:PRK06327 274 DKLIVSIGRVPNTDglGLEAVGLKLD-ERGFIPVDDHCRTNvPNVYAIGD 322
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
222-439 |
4.35e-03 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 39.80 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 222 NGGVAVLTGKKVVqldVRDNMVKLN--DGSQITY--EKCLIATGGTPRSLsAIDRAGAEVKSRTTLfrkigdfrSLEKIS 297
Cdd:PLN02507 136 NAGVKLYEGEGKI---VGPNEVEVTqlDGTKLRYtaKHILIATGSRAQRP-NIPGKELAITSDEAL--------SLEELP 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 298 REVksiTIIGGGFLGSELACALgrkaRALGTEVIQLF----PEKG---NMGKILPEYLSNwtmekvrrEGVKVMPNAIVQ 370
Cdd:PLN02507 204 KRA---VVLGGGYIAVEFASIW----RGMGATVDLFFrkelPLRGfddEMRAVVARNLEG--------RGINLHPRTNLT 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 371 SVGVSSGKLLIKLKDGRKVETDHIVAAVGLEPN----------VELAKTGGLEIDSdfggfrvnaelQARSN---IWVAG 437
Cdd:PLN02507 269 QLTKTEGGIKVITDHGEEFVADVVLFATGRAPNtkrlnleavgVELDKAGAVKVDE-----------YSRTNipsIWAIG 337
|
..
gi 4757732 438 DA 439
Cdd:PLN02507 338 DV 339
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
251-440 |
8.28e-03 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 38.98 E-value: 8.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 251 ITYEKCLIATGGTPRSLSAidragAEVKSRTTLFRKIGDFR-------------SLEKISREVK----SITIIGGGFLGS 313
Cdd:PTZ00318 112 VPYDKLVVAHGARPNTFNI-----PGVEERAFFLKEVNHARgirkrivqcieraSLPTTSVEERkrllHFVVVGGGPTGV 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4757732 314 ELACALG----RKARALGTEVIQLFP----EKGnmGKILPEY---LSNWTMEKVRREGVKVMPNAIVqsVGVSSGKLLik 382
Cdd:PTZ00318 187 EFAAELAdffrDDVRNLNPELVEECKvtvlEAG--SEVLGSFdqaLRKYGQRRLRRLGVDIRTKTAV--KEVLDKEVV-- 260
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4757732 383 LKDGRKVETDHIVAAVGLEPNvelAKTGGLEIDSDFGG-FRVNAELQAR--SNIWVAGDAA 440
Cdd:PTZ00318 261 LKDGEVIPTGLVVWSTGVGPG---PLTKQLKVDKTSRGrISVDDHLRVKpiPNVFALGDCA 318
|
|
|