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Conserved domains on  [gi|4757732|ref|NP_004199|]
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apoptosis-inducing factor 1, mitochondrial isoform AIF precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 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
AIF-MLS super family cl25936
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.


The actual alignment was detected with superfamily member pfam14962:

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
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
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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