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Conserved domains on  [gi|22202629|ref|NP_665811|]
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apoptosis-inducing factor 1, mitochondrial isoform AIF-exB 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 ...
 461-590 1.09e-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: 1.09e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629   461 AGENMTGAAKPYWHQSMFWSDLGPDVGYEAIGLVDSSLPTVGVFAKATAQDNPKSATEQSGTGIRSESETESEASEITIP 540
Cdd:pfam14721   1 AGENMTGAGKPYWHQSMFWSDLGPDVGYEAIGIVDSSLPTVGVFAKATEKDTPKAVVEESGESIRSESEEEATASASAAP 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 22202629   541 PSTPAVPQAPVQGEDYGKGVIFYLRDKVVVGIVLWNIFNRMPIARKIIKD 590
Cdd:pfam14721  81 SSEDVASEDPSPGEDYGKGVIFYLRDDKVVGIVLWNVFNRMPIARKIIKD 130
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
144-592 3.49e-66

NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];


:

Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 221.55  E-value: 3.49e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629 144 RSIRARDPGARVLIVSEDPELPYMRPPLSKELwfsddpnvtktlrfkqwNGK--ERSIYFQPPSFYvsaqdlphiENGGV 221
Cdd:COG1251  18 EELRKLDPDGEITVIGAEPHPPYNRPPLSKVL-----------------AGEtdEEDLLLRPADFY---------EENGI 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629 222 AVLTGKKVVQLDVRDNMVKLNDGSQITYEKCLIATGGTPRSLSAidrAGAEVKSRTTlFRKIGDFRSLEKISREVKSITI 301
Cdd:COG1251  72 DLRLGTRVTAIDRAARTVTLADGETLPYDKLVLATGSRPRVPPI---PGADLPGVFT-LRTLDDADALRAALAPGKRVVV 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629 302 IGGGFLGSELACALgrkaRALGTEVIQLFPEKGNMGKILPEYLSNWTMEKVRREGVKVMPNAIVQSVGVSSGKLLIKLKD 381
Cdd:COG1251 148 IGGGLIGLEAAAAL----RKRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTGVRLAD 223

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629 382 GRKVETDHIVAAVGLEPNVELAKTGGLEIDsdfGGFRVNAELQA-RSNIWVAGDAACFYDIKLGRRRVEHHDHAVVSGRL 460
Cdd:COG1251 224 GEELPADLVVVAIGVRPNTELARAAGLAVD---RGIVVDDYLRTsDPDIYAAGDCAEHPGPVYGRRVLELVAPAYEQARV 300

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629 461 AGENMTGAAKPYWH-QSMFWSDLgPDVGYEAIGLVDsslptvgvfakataqdnpksATEQSgtgirseseteseaseiti 539
Cdd:COG1251 301 AAANLAGGPAAYEGsVPSTKLKV-FGVDVASAGDAE--------------------GDEEV------------------- 340

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*
gi 22202629 540 ppstpavpqapVQGEDYGKGVI--FYLRDKVVVGIVLWNIFNRMPIARKIIKDGE 592
Cdd:COG1251 341 -----------VVRGDPARGVYkkLVLRDGRLVGAVLVGDTSDAGALRQLIKNGR 384
AIF-MLS super family cl25936
Mitochondria localization Sequence; This family contains a protein found in eukaryotes. ...
 47-129 4.10e-11

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: 62.54  E-value: 4.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629    47 RSLASTGASGKDGSNLVYFLIVGATVTgAGVYYAYKTMKEDEKRYNERISGLgltpeQKQKKAALSASEGEE---VPQDK 123
Cdd:pfam14962  31 RRMSSNKFPGSSGSNMIYYLVVGVTVS-AGGYYTYKTVTSEQAKHTEHVTNL-----KEKTKAELHPLQGEKenvAEAEK 104


                  ....*.
gi 22202629   124 APSHVP 129
Cdd:pfam14962 105 ASSEAP 110
 
Name Accession Description Interval E-value
AIF_C pfam14721
Apoptosis-inducing factor, mitochondrion-associated, C-term; This C-terminal domain appears to ...
 461-590 1.09e-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: 1.09e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629   461 AGENMTGAAKPYWHQSMFWSDLGPDVGYEAIGLVDSSLPTVGVFAKATAQDNPKSATEQSGTGIRSESETESEASEITIP 540
Cdd:pfam14721   1 AGENMTGAGKPYWHQSMFWSDLGPDVGYEAIGIVDSSLPTVGVFAKATEKDTPKAVVEESGESIRSESEEEATASASAAP 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 22202629   541 PSTPAVPQAPVQGEDYGKGVIFYLRDKVVVGIVLWNIFNRMPIARKIIKD 590
Cdd:pfam14721  81 SSEDVASEDPSPGEDYGKGVIFYLRDDKVVGIVLWNVFNRMPIARKIIKD 130
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
144-592 3.49e-66

NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 221.55  E-value: 3.49e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629 144 RSIRARDPGARVLIVSEDPELPYMRPPLSKELwfsddpnvtktlrfkqwNGK--ERSIYFQPPSFYvsaqdlphiENGGV 221
Cdd:COG1251  18 EELRKLDPDGEITVIGAEPHPPYNRPPLSKVL-----------------AGEtdEEDLLLRPADFY---------EENGI 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629 222 AVLTGKKVVQLDVRDNMVKLNDGSQITYEKCLIATGGTPRSLSAidrAGAEVKSRTTlFRKIGDFRSLEKISREVKSITI 301
Cdd:COG1251  72 DLRLGTRVTAIDRAARTVTLADGETLPYDKLVLATGSRPRVPPI---PGADLPGVFT-LRTLDDADALRAALAPGKRVVV 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629 302 IGGGFLGSELACALgrkaRALGTEVIQLFPEKGNMGKILPEYLSNWTMEKVRREGVKVMPNAIVQSVGVSSGKLLIKLKD 381
Cdd:COG1251 148 IGGGLIGLEAAAAL----RKRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTGVRLAD 223

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629 382 GRKVETDHIVAAVGLEPNVELAKTGGLEIDsdfGGFRVNAELQA-RSNIWVAGDAACFYDIKLGRRRVEHHDHAVVSGRL 460
Cdd:COG1251 224 GEELPADLVVVAIGVRPNTELARAAGLAVD---RGIVVDDYLRTsDPDIYAAGDCAEHPGPVYGRRVLELVAPAYEQARV 300

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629 461 AGENMTGAAKPYWH-QSMFWSDLgPDVGYEAIGLVDsslptvgvfakataqdnpksATEQSgtgirseseteseaseiti 539
Cdd:COG1251 301 AAANLAGGPAAYEGsVPSTKLKV-FGVDVASAGDAE--------------------GDEEV------------------- 340

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*
gi 22202629 540 ppstpavpqapVQGEDYGKGVI--FYLRDKVVVGIVLWNIFNRMPIARKIIKDGE 592
Cdd:COG1251 341 -----------VVRGDPARGVYkkLVLRDGRLVGAVLVGDTSDAGALRQLIKNGR 384
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 146-458 2.56e-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: 2.56e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629   146 IRARDPGARVLIVSEDPELPYMRPPLSKELWFSDDPnvtktlrfkqwngkeRSIYFQPPSFYVSAQDLPHIENGGVAVLT 225
Cdd:pfam07992  17 LTLAQLGGKVTLIEDEGTCPYGGCVLSKALLGAAEA---------------PEIASLWADLYKRKEEVVKKLNNGIEVLL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629   226 GKKVVQLD-----VRDNMVKLNDGSQITYEKCLIATGGTPRSLSAidrAGAEvKSRTTLFRKIGDFRSLEKISREvKSIT 300
Cdd:pfam07992  82 GTEVVSIDpgakkVVLEELVDGDGETITYDRLVIATGARPRLPPI---PGVE-LNVGFLVRTLDSAEALRLKLLP-KRVV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629   301 IIGGGFLGSELACALgrkaRALGTEV--IQLFPEkgnMGKILPEYLSNWTMEKVRREGVKVMPNAIVQSVGVSSGKLLIK 378
Cdd:pfam07992 157 VVGGGYIGVELAAAL----AKLGKEVtlIEALDR---LLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGVEVI 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629   379 LKDGRKVETDHIVAAVGLEPNVELAKTGGLEIDSDfGGFRVNAELQ-ARSNIWVAGDAacfydiklGRRRVEHHDHAVVS 457
Cdd:pfam07992 230 LKDGTEIDADLVVVAIGRRPNTELLEAAGLELDER-GGIVVDEYLRtSVPGIYAAGDC--------RVGGPELAQNAVAQ 300


                  .
gi 22202629   458 G 458
Cdd:pfam07992 301 G 301
PRK09754 PRK09754
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
 145-481 3.01e-24

phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional


Pssm-ID: 170080 [Multi-domain]  Cd Length: 396  Bit Score: 105.39  E-value: 3.01e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629  145 SIRARDPGARVLIVSEDPELPYMRPPLSKELWFSDDPNVTktlrfkqwngkersiYFQPPSFYVSAQdlphienggVAVL 224
Cdd:PRK09754  21 SLRQQGFTGELHLFSDERHLPYERPPLSKSMLLEDSPQLQ---------------QVLPANWWQENN---------VHLH 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629  225 TGKKVVQLDVRDNMVKLNDGSQITYEKCLIATGGTPRSLSAIDRAGAEVKSrttlFRKIGDFRSLEKISREVKSITIIGG 304
Cdd:PRK09754  77 SGVTIKTLGRDTRELVLTNGESWHWDQLFIATGAAARPLPLLDALGERCFT----LRHAGDAARLREVLQPERSVVIVGA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629  305 GFLGSELACAlgrkARALGTEVIQLFPEKGNMGKILPEYLSNWTMEKVRREGVKVMPNAIVQSVgVSSGKLLIKLKDGRK 384
Cdd:PRK09754 153 GTIGLELAAS----ATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHV-VDGEKVELTLQSGET 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629  385 VETDHIVAAVGLEPNVELAKTGGLEIDsdfGGFRVNAELQ-ARSNIWVAGDAACFYDIKLGRRRVEHHDHAVVSGRLAGE 463
Cdd:PRK09754 228 LQADVVIYGIGISANDQLAREANLDTA---NGIVIDEACRtCDPAIFAGGDVAITRLDNGALHRCESWENANNQAQIAAA 304

                        330
                 ....*....|....*...
gi 22202629  464 NMTGAAKPYWHQSMFWSD 481
Cdd:PRK09754 305 AMLGLPLPLLPPPWFWSD 322
AIF-MLS pfam14962
Mitochondria localization Sequence; This family contains a protein found in eukaryotes. ...
 47-129 4.10e-11

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: 62.54  E-value: 4.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629    47 RSLASTGASGKDGSNLVYFLIVGATVTgAGVYYAYKTMKEDEKRYNERISGLgltpeQKQKKAALSASEGEE---VPQDK 123
Cdd:pfam14962  31 RRMSSNKFPGSSGSNMIYYLVVGVTVS-AGGYYTYKTVTSEQAKHTEHVTNL-----KEKTKAELHPLQGEKenvAEAEK 104


                  ....*.
gi 22202629   124 APSHVP 129
Cdd:pfam14962 105 ASSEAP 110
 
Name Accession Description Interval E-value
AIF_C pfam14721
Apoptosis-inducing factor, mitochondrion-associated, C-term; This C-terminal domain appears to ...
 461-590 1.09e-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: 1.09e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629   461 AGENMTGAAKPYWHQSMFWSDLGPDVGYEAIGLVDSSLPTVGVFAKATAQDNPKSATEQSGTGIRSESETESEASEITIP 540
Cdd:pfam14721   1 AGENMTGAGKPYWHQSMFWSDLGPDVGYEAIGIVDSSLPTVGVFAKATEKDTPKAVVEESGESIRSESEEEATASASAAP 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 22202629   541 PSTPAVPQAPVQGEDYGKGVIFYLRDKVVVGIVLWNIFNRMPIARKIIKD 590
Cdd:pfam14721  81 SSEDVASEDPSPGEDYGKGVIFYLRDDKVVGIVLWNVFNRMPIARKIIKD 130
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
144-592 3.49e-66

NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 221.55  E-value: 3.49e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629 144 RSIRARDPGARVLIVSEDPELPYMRPPLSKELwfsddpnvtktlrfkqwNGK--ERSIYFQPPSFYvsaqdlphiENGGV 221
Cdd:COG1251  18 EELRKLDPDGEITVIGAEPHPPYNRPPLSKVL-----------------AGEtdEEDLLLRPADFY---------EENGI 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629 222 AVLTGKKVVQLDVRDNMVKLNDGSQITYEKCLIATGGTPRSLSAidrAGAEVKSRTTlFRKIGDFRSLEKISREVKSITI 301
Cdd:COG1251  72 DLRLGTRVTAIDRAARTVTLADGETLPYDKLVLATGSRPRVPPI---PGADLPGVFT-LRTLDDADALRAALAPGKRVVV 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629 302 IGGGFLGSELACALgrkaRALGTEVIQLFPEKGNMGKILPEYLSNWTMEKVRREGVKVMPNAIVQSVGVSSGKLLIKLKD 381
Cdd:COG1251 148 IGGGLIGLEAAAAL----RKRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTGVRLAD 223

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629 382 GRKVETDHIVAAVGLEPNVELAKTGGLEIDsdfGGFRVNAELQA-RSNIWVAGDAACFYDIKLGRRRVEHHDHAVVSGRL 460
Cdd:COG1251 224 GEELPADLVVVAIGVRPNTELARAAGLAVD---RGIVVDDYLRTsDPDIYAAGDCAEHPGPVYGRRVLELVAPAYEQARV 300

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629 461 AGENMTGAAKPYWH-QSMFWSDLgPDVGYEAIGLVDsslptvgvfakataqdnpksATEQSgtgirseseteseaseiti 539
Cdd:COG1251 301 AAANLAGGPAAYEGsVPSTKLKV-FGVDVASAGDAE--------------------GDEEV------------------- 340

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*
gi 22202629 540 ppstpavpqapVQGEDYGKGVI--FYLRDKVVVGIVLWNIFNRMPIARKIIKDGE 592
Cdd:COG1251 341 -----------VVRGDPARGVYkkLVLRDGRLVGAVLVGDTSDAGALRQLIKNGR 384
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 148-482 4.51e-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: 176.16  E-value: 4.51e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629 148 ARDPGARVLIVSEDPELPYMRPPLSKELWFSDDpnvtktlrfkqwngKERSIYFQPPSFYVSAqdlphiengGVAVLTGK 227
Cdd:COG0446   1 RLGPDAEITVIEKGPHHSYQPCGLPYYVGGGIK--------------DPEDLLVRTPESFERK---------GIDVRTGT 57

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629 228 KVVQLDVRDNMVKLNDGSQITYEKCLIATGGTPRSLsAIDraGAEVKSRTTLfRKIGDFRSL-EKI-SREVKSITIIGGG 305
Cdd:COG0446  58 EVTAIDPEAKTVTLRDGETLSYDKLVLATGARPRPP-PIP--GLDLPGVFTL-RTLDDADALrEALkEFKGKRAVVIGGG 133

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629 306 FLGSELACALgrkaRALGTEVIQLFPEKGNMGKILPEYlSNWTMEKVRREGVKVMPNAIVQSVgVSSGKLLIKLKDGRKV 385
Cdd:COG0446 134 PIGLELAEAL----RKRGLKVTLVERAPRLLGVLDPEM-AALLEEELREHGVELRLGETVVAI-DGDDKVAVTLTDGEEI 207

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629 386 ETDHIVAAVGLEPNVELAKTGGLEIDSDfGGFRVNAELQAR-SNIWVAGDAACFYDIKLGRR-RVEHHDHAVVSGRLAGE 463
Cdd:COG0446 208 PADLVVVAPGVRPNTELAKDAGLALGER-GWIKVDETLQTSdPDVYAAGDCAEVPHPVTGKTvYIPLASAANKQGRVAAE 286

                       330
                ....*....|....*....
gi 22202629 464 NMTGAAKPYWHQSMFWSDL 482
Cdd:COG0446 287 NILGGPAPFPGLGTFISKV 305
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 146-458 2.56e-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: 2.56e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629   146 IRARDPGARVLIVSEDPELPYMRPPLSKELWFSDDPnvtktlrfkqwngkeRSIYFQPPSFYVSAQDLPHIENGGVAVLT 225
Cdd:pfam07992  17 LTLAQLGGKVTLIEDEGTCPYGGCVLSKALLGAAEA---------------PEIASLWADLYKRKEEVVKKLNNGIEVLL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629   226 GKKVVQLD-----VRDNMVKLNDGSQITYEKCLIATGGTPRSLSAidrAGAEvKSRTTLFRKIGDFRSLEKISREvKSIT 300
Cdd:pfam07992  82 GTEVVSIDpgakkVVLEELVDGDGETITYDRLVIATGARPRLPPI---PGVE-LNVGFLVRTLDSAEALRLKLLP-KRVV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629   301 IIGGGFLGSELACALgrkaRALGTEV--IQLFPEkgnMGKILPEYLSNWTMEKVRREGVKVMPNAIVQSVGVSSGKLLIK 378
Cdd:pfam07992 157 VVGGGYIGVELAAAL----AKLGKEVtlIEALDR---LLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGVEVI 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629   379 LKDGRKVETDHIVAAVGLEPNVELAKTGGLEIDSDfGGFRVNAELQ-ARSNIWVAGDAacfydiklGRRRVEHHDHAVVS 457
Cdd:pfam07992 230 LKDGTEIDADLVVVAIGRRPNTELLEAAGLELDER-GGIVVDEYLRtSVPGIYAAGDC--------RVGGPELAQNAVAQ 300


                  .
gi 22202629   458 G 458
Cdd:pfam07992 301 G 301
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 216-467 5.78e-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: 5.78e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629 216 IENGGVAVLTGKKVVqldVRDNMVKLNDGSQITYEKCLIATGGTPRSLSAIDRAGAEVKSRTTLFrkigdfrSLEKIsre 295
Cdd:COG1249 101 LKKNGVDVIRGRARF---VDPHTVEVTGGETLTADHIVIATGSRPRVPPIPGLDEVRVLTSDEAL-------ELEEL--- 167

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629 296 VKSITIIGGGFLGSELACALgrkaRALGTEVIQLfpekGNMGKILPEY---LSNWTMEKVRREGVKVMPNAIVQSVGVSS 372
Cdd:COG1249 168 PKSLVVIGGGYIGLEFAQIF----ARLGSEVTLV----ERGDRLLPGEdpeISEALEKALEKEGIDILTGAKVTSVEKTG 239

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629 373 GKLLIKLKDGRKVET---DHIVAAVGLEPNVE---LAKTgGLEIDSDfGGFRVNAELQ-ARSNIWVAGDAAcfydiklGR 445
Cdd:COG1249 240 DGVTVTLEDGGGEEAveaDKVLVATGRRPNTDglgLEAA-GVELDER-GGIKVDEYLRtSVPGIYAIGDVT-------GG 310

                       250       260
                ....*....|....*....|..
gi 22202629 446 RRVEHhdHAVVSGRLAGENMTG 467
Cdd:COG1249 311 PQLAH--VASAEGRVAAENILG 330
PRK09754 PRK09754
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
 145-481 3.01e-24

phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional


Pssm-ID: 170080 [Multi-domain]  Cd Length: 396  Bit Score: 105.39  E-value: 3.01e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629  145 SIRARDPGARVLIVSEDPELPYMRPPLSKELWFSDDPNVTktlrfkqwngkersiYFQPPSFYVSAQdlphienggVAVL 224
Cdd:PRK09754  21 SLRQQGFTGELHLFSDERHLPYERPPLSKSMLLEDSPQLQ---------------QVLPANWWQENN---------VHLH 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629  225 TGKKVVQLDVRDNMVKLNDGSQITYEKCLIATGGTPRSLSAIDRAGAEVKSrttlFRKIGDFRSLEKISREVKSITIIGG 304
Cdd:PRK09754  77 SGVTIKTLGRDTRELVLTNGESWHWDQLFIATGAAARPLPLLDALGERCFT----LRHAGDAARLREVLQPERSVVIVGA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629  305 GFLGSELACAlgrkARALGTEVIQLFPEKGNMGKILPEYLSNWTMEKVRREGVKVMPNAIVQSVgVSSGKLLIKLKDGRK 384
Cdd:PRK09754 153 GTIGLELAAS----ATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHV-VDGEKVELTLQSGET 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629  385 VETDHIVAAVGLEPNVELAKTGGLEIDsdfGGFRVNAELQ-ARSNIWVAGDAACFYDIKLGRRRVEHHDHAVVSGRLAGE 463
Cdd:PRK09754 228 LQADVVIYGIGISANDQLAREANLDTA---NGIVIDEACRtCDPAIFAGGDVAITRLDNGALHRCESWENANNQAQIAAA 304

                        330
                 ....*....|....*...
gi 22202629  464 NMTGAAKPYWHQSMFWSD 481
Cdd:PRK09754 305 AMLGLPLPLLPPPWFWSD 322
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
214-464 4.81e-23

NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 101.36  E-value: 4.81e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629 214 PHIENGGVAVLTGKkVVQLDVRDNMVKLNDGSQITYEKCLIATGGTPRsLSAIDraGAE-----VKSR---TTLFRKIgd 285
Cdd:COG1252  64 ELLRRAGVRFIQGE-VTGIDPEARTVTLADGRTLSYDYLVIATGSVTN-FFGIP--GLAehalpLKTLedaLALRERL-- 137

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629 286 FRSLEKISREVK-SITIIGGGFLGSELACALGRKARALGTEViQLFPEKGN------MGKILPEY---LSNWTMEKVRRE 355
Cdd:COG1252 138 LAAFERAERRRLlTIVVVGGGPTGVELAGELAELLRKLLRYP-GIDPDKVRitlveaGPRILPGLgekLSEAAEKELEKR 216

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629 356 GVKVMPNAIVQSvgVSSGKllIKLKDGRKVETDHIVAAVGLEPNvELAKTGGLEIDSDfGGFRVNAELQARS--NIWVAG 433
Cdd:COG1252 217 GVEVHTGTRVTE--VDADG--VTLEDGEEIPADTVIWAAGVKAP-PLLADLGLPTDRR-GRVLVDPTLQVPGhpNVFAIG 290

                       250       260       270
                ....*....|....*....|....*....|....*..
gi 22202629 434 DAACFYDI------KLGRrrvehhdHAVVSGRLAGEN 464
Cdd:COG1252 291 DCAAVPDPdgkpvpKTAQ-------AAVQQAKVLAKN 320
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 220-472 3.78e-19

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 90.48  E-value: 3.78e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629  220 GVAVLTGKKVVQLDVRDNMVK---LNDGSQI--TYEKCLIATGGTPrSLSAIDraGAEVKSRTTLfRKIGDFRSLEKISR 294
Cdd:PRK09564  70 GIDVKTEHEVVKVDAKNKTITvknLKTGSIFndTYDKLMIATGARP-IIPPIK--NINLENVYTL-KSMEDGLALKELLK 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629  295 --EVKSITIIGGGFLGSELACAlgrkARALGTEV--IQLfpEKGNMGKILPEYLSNWTMEKVRREGVKVMPNAIVQSVgV 370
Cdd:PRK09564 146 deEIKNIVIIGAGFIGLEAVEA----AKHLGKNVriIQL--EDRILPDSFDKEITDVMEEELRENGVELHLNEFVKSL-I 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629  371 SSGKLLIKLKDGRKVETDHIVAAVGLEPNVELAKTGGLEIDSDfGGFRVNAELQAR-SNIWVAGDAACFYDIKLGRRR-V 448
Cdd:PRK09564 219 GEDKVEGVVTDKGEYEADVVIVATGVKPNTEFLEDTGLKTLKN-GAIIVDEYGETSiENIYAAGDCATIYNIVSNKNVyV 297

                        250       260
                 ....*....|....*....|....
gi 22202629  449 EHHDHAVVSGRLAGENMTGAAKPY 472
Cdd:PRK09564 298 PLATTANKLGRMVGENLAGRHVSF 321
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
221-436 3.80e-18

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 86.51  E-value: 3.80e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629  221 VAVLTGKKVVQLDVRDNMVKLNDGsQITYEKCLIATGGTP--------------RSLSaidragaevksrttlfrkigDF 286
Cdd:PRK04965  73 LRLFPHTWVTDIDAEAQVVKSQGN-QWQYDKLVLATGASAfvppipgrelmltlNSQQ--------------------EY 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629  287 RSLEKISREVKSITIIGGGFLGSELACALgrkARAlGTEVIQLFPEKGNMGKILPEYLSNWTMEKVRREGVKVMPNAIVQ 366
Cdd:PRK04965 132 RAAETQLRDAQRVLVVGGGLIGTELAMDL---CRA-GKAVTLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQLQ 207

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22202629  367 SVGVSSGKLLIKLKDGRKVETDHIVAAVGLEPNVELAKTGGLEIDSdfgGFRVNAELQ-ARSNIWVAGDAA 436
Cdd:PRK04965 208 GLEKTDSGIRATLDSGRSIEVDAVIAAAGLRPNTALARRAGLAVNR---GIVVDSYLQtSAPDIYALGDCA 275
PRK06116 PRK06116
glutathione reductase; Validated
 217-434 1.56e-16

glutathione reductase; Validated


Pssm-ID: 235701 [Multi-domain]  Cd Length: 450  Bit Score: 82.51  E-value: 1.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629  217 ENGGVAVLTGKKVVqldVRDNMVKLNdGSQITYEKCLIATGGTPrslSAIDRAGAE--VKSRttlfrkigDFRSLEKISr 294
Cdd:PRK06116 104 ENNGVDLIEGFARF---VDAHTVEVN-GERYTADHILIATGGRP---SIPDIPGAEygITSD--------GFFALEELP- 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629  295 evKSITIIGGGFLGSELACALgrkaRALGTEVIQLFpeKGNmgKIL---PEYLSNWTMEKVRREGVKVMPNAIVQSVG-V 370
Cdd:PRK06116 168 --KRVAVVGAGYIAVEFAGVL----NGLGSETHLFV--RGD--APLrgfDPDIRETLVEEMEKKGIRLHTNAVPKAVEkN 237

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22202629  371 SSGKLLIKLKDGRKVETDHIVAAVGLEPNVE---LAKTgGLEIDsDFGGFRVNAELQ-ARSNIWVAGD 434
Cdd:PRK06116 238 ADGSLTLTLEDGETLTVDCLIWAIGREPNTDglgLENA-GVKLN-EKGYIIVDEYQNtNVPGIYAVGD 303
PRK14989 PRK14989
nitrite reductase subunit NirD; Provisional
 217-436 3.13e-16

nitrite reductase subunit NirD; Provisional


Pssm-ID: 184951 [Multi-domain]  Cd Length: 847  Bit Score: 82.47  E-value: 3.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629  217 ENGGVAVLTGKKVVQLDVRDNMVKLNDGSQITYEKCLIATGGTPrSLSAIdrAGAEVKSrTTLFRKIGDFRSLEKISREV 296
Cdd:PRK14989  70 EKHGIKVLVGERAITINRQEKVIHSSAGRTVFYDKLIMATGSYP-WIPPI--KGSETQD-CFVYRTIEDLNAIEACARRS 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629  297 KSITIIGGGFLGSELACALgrKARALGTEVIQLFPekgnmgKILPEYLSNWTMEKVRRE----GVKVMPN----AIVQSv 368
Cdd:PRK14989 146 KRGAVVGGGLLGLEAAGAL--KNLGVETHVIEFAP------MLMAEQLDQMGGEQLRRKiesmGVRVHTSkntlEIVQE- 216

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22202629  369 GVSSGKLLiKLKDGRKVETDHIVAAVGLEPNVELAKTGGLEIdSDFGGFRVNAELQ-ARSNIWVAGDAA 436
Cdd:PRK14989 217 GVEARKTM-RFADGSELEVDFIVFSTGIRPQDKLATQCGLAV-APRGGIVINDSCQtSDPDIYAIGECA 283
PRK06370 PRK06370
FAD-containing oxidoreductase;
220-434 7.57e-14

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 74.08  E-value: 7.57e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629  220 GVAVLTGKKVVQLDvrdnmvklndGSQITYEKCLIATGGTPR--SLSAIDRAGAevKSRTTLFrkigdfrSLEKISRevk 297
Cdd:PRK06370 115 GHARFESPNTVRVG----------GETLRAKRIFINTGARAAipPIPGLDEVGY--LTNETIF-------SLDELPE--- 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629  298 SITIIGGGFLGSELACALGRkaraLGTEVIQLfpEKGNmgKILP---EYLSNWTMEKVRREGVKVMPNAIVQSVGVSSGK 374
Cdd:PRK06370 173 HLVIIGGGYIGLEFAQMFRR----FGSEVTVI--ERGP--RLLPredEDVAAAVREILEREGIDVRLNAECIRVERDGDG 244

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22202629  375 LLIKLK---DGRKVETDHIVAAVGLEPNVE---LAKTgGLEIDSDfGGFRVNAELQAR-SNIWVAGD 434
Cdd:PRK06370 245 IAVGLDcngGAPEITGSHILVAVGRVPNTDdlgLEAA-GVETDAR-GYIKVDDQLRTTnPGIYAAGD 309
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 220-472 1.21e-13

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 73.29  E-value: 1.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629  220 GVAVLTGKKVVQLDvrdnmvklndGSQITYEKCLIATGGTPRSLSAIDRA-GAEVKSRTTLFrkigdfrSLEKISrevKS 298
Cdd:PRK06292 112 GTARFVDPNTVEVN----------GERIEAKNIVIATGSRVPPIPGVWLIlGDRLLTSDDAF-------ELDKLP---KS 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629  299 ITIIGGGFLGSELACALGRkaraLGTEVIqLFPEKGNMGKILPEYLSNWTMEKVRREgVKVMPNAIVQSVGVSSGKLLIK 378
Cdd:PRK06292 172 LAVIGGGVIGLELGQALSR----LGVKVT-VFERGDRILPLEDPEVSKQAQKILSKE-FKIKLGAKVTSVEKSGDEKVEE 245

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629  379 LKDGRKVET---DHIVAAVGLEPNVE---LAKTgGLEIDSDfgGF-RVNAEL-QARSNIWVAGDAAcfydiklGRRRVEH 450
Cdd:PRK06292 246 LEKGGKTETieaDYVLVATGRRPNTDglgLENT-GIELDER--GRpVVDEHTqTSVPGIYAAGDVN-------GKPPLLH 315

                        250       260
                 ....*....|....*....|..
gi 22202629  451 hdHAVVSGRLAGENMTGAAKPY 472
Cdd:PRK06292 316 --EAADEGRIAAENAAGDVAGG 335
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 298-382 2.00e-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: 2.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629   298 SITIIGGGFLGSELACALgrkaRALGTEViQLFPEKGNMGKILPEYLSNWTMEKVRREGVKVMPNAIVQSVGVSSGKLLI 377
Cdd:pfam00070   1 RVVVVGGGYIGLELAGAL----ARLGSKV-TVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVV 75


                  ....*
gi 22202629   378 KLKDG 382
Cdd:pfam00070  76 VLTDG 80
AIF-MLS pfam14962
Mitochondria localization Sequence; This family contains a protein found in eukaryotes. ...
 47-129 4.10e-11

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: 62.54  E-value: 4.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629    47 RSLASTGASGKDGSNLVYFLIVGATVTgAGVYYAYKTMKEDEKRYNERISGLgltpeQKQKKAALSASEGEE---VPQDK 123
Cdd:pfam14962  31 RRMSSNKFPGSSGSNMIYYLVVGVTVS-AGGYYTYKTVTSEQAKHTEHVTNL-----KEKTKAELHPLQGEKenvAEAEK 104


                  ....*.
gi 22202629   124 APSHVP 129
Cdd:pfam14962 105 ASSEAP 110
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
239-470 6.85e-11

Si-specific NAD(P)(+) transhydrogenase;


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 64.79  E-value: 6.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629  239 VKLNDGS--QITYEKCLIATGGTPRSLSAIDRAGaevksrttlfRKIGDFRSLEKISREVKSITIIGGGFLGSELACALg 316
Cdd:PRK05249 126 VECPDGEveTLTADKIVIATGSRPYRPPDVDFDH----------PRIYDSDSILSLDHLPRSLIIYGAGVIGCEYASIF- 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629  317 rkaRALGTEVIQLfpekgNMGKILPEYLSNWTME----KVRREGVKVMPNAIVQSVGVSSGKLLIKLKDGRKVETDHIVA 392
Cdd:PRK05249 195 ---AALGVKVTLI-----NTRDRLLSFLDDEISDalsyHLRDSGVTIRHNEEVEKVEGGDDGVIVHLKSGKKIKADCLLY 266

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629  393 AVGLEPNVE---LAKTgGLEIDSDfGGFRVNAELQ-ARSNIWVAGD-------AACFYDiklgrrrvehhdhavvSGRLA 461
Cdd:PRK05249 267 ANGRTGNTDglnLENA-GLEADSR-GQLKVNENYQtAVPHIYAVGDvigfpslASASMD----------------QGRIA 328


                 ....*....
gi 22202629  462 GENMTGAAK 470
Cdd:PRK05249 329 AQHAVGEAT 337
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 220-436 2.89e-10

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 62.86  E-value: 2.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629  220 GVAVLTGKKVVQldvrdnmVKLNDGSQ-ITYEKCLIATGGTPRSLSAIDRAGaevksrttlfRKIGDFR---SLEKISre 295
Cdd:PRK06416 112 GEAKLVDPNTVR-------VMTEDGEQtYTAKNIILATGSRPRELPGIEIDG----------RVIWTSDealNLDEVP-- 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629  296 vKSITIIGGGFLGSELACALgrkaRALGTEVI------QLFP-EKGNMGKILpeylsnwtmEKV-RREGVKVMPNAIVQS 367
Cdd:PRK06416 173 -KSLVVIGGGYIGVEFASAY----ASLGAEVTivealpRILPgEDKEISKLA---------ERAlKKRGIKIKTGAKAKK 238

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22202629  368 VGVSSGKLLIKLKDGRKVET---DHIVAAVGLEPNVE---LAKTgGLEIDsdfGGF-RVNAELQAR-SNIWVAGDAA 436
Cdd:PRK06416 239 VEQTDDGVTVTLEDGGKEETleaDYVLVAVGRRPNTEnlgLEEL-GVKTD---RGFiEVDEQLRTNvPNIYAIGDIV 311
PTZ00058 PTZ00058
glutathione reductase; Provisional
 234-435 1.88e-09

glutathione reductase; Provisional


Pssm-ID: 185420 [Multi-domain]  Cd Length: 561  Bit Score: 60.40  E-value: 1.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629  234 VRDNMVKLNDGSQITYEKCLIATGGTPRSlsaIDRAGAEVKSRTTLFRKIgdfrslekisREVKSITIIGGGFLGSELAC 313
Cdd:PTZ00058 188 VSAGVSQLDDGQVIEGKNILIAVGNKPIF---PDVKGKEFTISSDDFFKI----------KEAKRIGIAGSGYIAVELIN 254

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629  314 ALgrkaRALGTEViQLFPEKGNMGKILPEYLSNWTMEKVRREGVKVMPNAIVQSV-GVSSGKLLIKLKDGRKVET-DHIV 391
Cdd:PTZ00058 255 VV----NRLGAES-YIFARGNRLLRKFDETIINELENDMKKNNINIITHANVEEIeKVKEKNLTIYLSDGRKYEHfDYVI 329

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 22202629  392 AAVGLEPNVELAKTGGLEIDSDFGGFRVNaELQARS--NIWVAGDA 435
Cdd:PTZ00058 330 YCVGRSPNTEDLNLKALNIKTPKGYIKVD-DNQRTSvkHIYAVGDC 374
PRK07845 PRK07845
flavoprotein disulfide reductase; Reviewed
 220-434 8.50e-07

flavoprotein disulfide reductase; Reviewed


Pssm-ID: 236112 [Multi-domain]  Cd Length: 466  Bit Score: 51.78  E-value: 8.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629  220 GVAVLTGK-KVVQLDVRDNMVK--LNDGSQITYEK--CLIATGGTPRSLsaidrAGAEVKSRTTL-FRKIGDfrsLEKIS 293
Cdd:PRK07845 106 GVRVIAGRgRLIDPGLGPHRVKvtTADGGEETLDAdvVLIATGASPRIL-----PTAEPDGERILtWRQLYD---LDELP 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629  294 REvksITIIGGGFLGSELACALgrkaRALGTEVI------QLFP-EKGNMGKILpeylsnwtmEKV-RREGVKVMPNAIV 365
Cdd:PRK07845 178 EH---LIVVGSGVTGAEFASAY----TELGVKVTlvssrdRVLPgEDADAAEVL---------EEVfARRGMTVLKRSRA 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629  366 QSVGVSSGKLLIKLKDGRKVETDHIVAAVGLEPN----------VELAKTGGLEIDsdfggfRVnaelqARSN---IWVA 432
Cdd:PRK07845 242 ESVERTGDGVVVTLTDGRTVEGSHALMAVGSVPNtaglgleeagVELTPSGHITVD------RV-----SRTSvpgIYAA 310


                 ..
gi 22202629  433 GD 434
Cdd:PRK07845 311 GD 312
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
215-436 3.86e-06

Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 48.96  E-value: 3.86e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629 215 HIENGGVAVLTGKkVVQLDVRDN--MVKLNDGSQITYEKCLIATGGTPRSLSAidrAGAE----------VKSRTTLFRK 282
Cdd:COG0492  66 QAERFGAEILLEE-VTSVDKDDGpfRVTTDDGTEYEAKAVIIATGAGPRKLGL---PGEEefegrgvsycATCDGFFFRG 141

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629 283 igdfrslekisrevKSITIIGGGFLGSELACALGRKARalgtEVIqLFPEKGNM--GKILpeylsnwtMEKVRR-EGVKV 359
Cdd:COG0492 142 --------------KDVVVVGGGDSALEEALYLTKFAS----KVT-LIHRRDELraSKIL--------VERLRAnPKIEV 194

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629 360 MPNAIVQSV----GVSSgkllIKLKDG-----RKVETDHIVAAVGLEPNVELAKTGGLEIDSDfGGFRVNAELQ-ARSNI 429
Cdd:COG0492 195 LWNTEVTEIegdgRVEG----VTLKNVktgeeKELEVDGVFVAIGLKPNTELLKGLGLELDED-GYIVVDEDMEtSVPGV 269


                ....*..
gi 22202629 430 WVAGDAA 436
Cdd:COG0492 270 FAAGDVR 276
Pyr_redox_3 pfam13738
Pyridine nucleotide-disulphide oxidoreductase;
299-413 6.58e-05

Pyridine nucleotide-disulphide oxidoreductase;


Pssm-ID: 404603 [Multi-domain]  Cd Length: 296  Bit Score: 45.29  E-value: 6.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629   299 ITIIGGGFLGSELACALGRKaralGTEVIQLFPEKGnMGKILPEY---LSNWT----MEKVRREGVKVMPNAIVQSVGVS 371
Cdd:pfam13738 158 VVVIGGYNSAVDAALELVRK----GARVTVLYRGSE-WEDRDSDPsysLSPDTlnrlEELVKNGKIKAHFNAEVKEITEV 232

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 22202629   372 SGKLLIKLKDGRKVETDHI-VAAVGLEPNVELAKTGGLEIDSD 413
Cdd:pfam13738 233 DVSYKVHTEDGRKVTSNDDpILATGYHPDLSFLKKGLFELDED 275
PRK13512 PRK13512
coenzyme A disulfide reductase; Provisional
 201-436 1.16e-04

coenzyme A disulfide reductase; Provisional


Pssm-ID: 184103 [Multi-domain]  Cd Length: 438  Bit Score: 44.77  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629  201 FQPPSFYvsaqdlphiENGGVAVLTGKKVVQLDVRDNMV-----KLNDGSQITYEKCLIATGGTPRSLsaidraGAEVKS 275
Cdd:PRK13512  62 YTPEKFY---------DRKQITVKTYHEVIAINDERQTVtvlnrKTNEQFEESYDKLILSPGASANSL------GFESDI 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629  276 RTTLfRKIGDFRSLEK-ISR-EVKSITIIGGGFLGSELACALgrKARALGTEVIQlfpEKGNMGKILPEYLSNWTMEKVR 353
Cdd:PRK13512 127 TFTL-RNLEDTDAIDQfIKAnQVDKALVVGAGYISLEVLENL--YERGLHPTLIH---RSDKINKLMDADMNQPILDELD 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629  354 REGVKVMPNAIVQSVGVSsgklLIKLKDGRKVETDHIVAAVGLEPNVELAKTGGLEIDsDFGGFRVNAELQAR-SNIWVA 432
Cdd:PRK13512 201 KREIPYRLNEEIDAINGN----EVTFKSGKVEHYDMIIEGVGTHPNSKFIESSNIKLD-DKGFIPVNDKFETNvPNIYAI 275


                 ....
gi 22202629  433 GDAA 436
Cdd:PRK13512 276 GDII 279
PRK06327 PRK06327
dihydrolipoamide dehydrogenase; Validated
 239-434 2.79e-03

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235779 [Multi-domain]  Cd Length: 475  Bit Score: 40.68  E-value: 2.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629  239 VKLNDGSQITYEKCLIATGGTPRSLSaidraGAEVKSRTTLfrkigDFRSLEKISREVKSITIIGGGFLGselaCALGRK 318
Cdd:PRK06327 136 VTGEDETVITAKHVIIATGSEPRHLP-----GVPFDNKIIL-----DNTGALNFTEVPKKLAVIGAGVIG----LELGSV 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629  319 ARALGTEVIQLfpekgnmgKILPEYL-------SNWTMEKVRREGVKVMPNAIVQSVGVSSGKLLIKLKDG----RKVET 387
Cdd:PRK06327 202 WRRLGAEVTIL--------EALPAFLaaadeqvAKEAAKAFTKQGLDIHLGVKIGEIKTGGKGVSVAYTDAdgeaQTLEV 273

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 22202629  388 DHIVAAVGLEPNVE--LAKTGGLEIDsDFGGFRVNAELQAR-SNIWVAGD 434
Cdd:PRK06327 274 DKLIVSIGRVPNTDglGLEAVGLKLD-ERGFIPVDDHCRTNvPNVYAIGD 322
PLN02507 PLN02507
glutathione reductase
 218-435 4.70e-03

glutathione reductase


Pssm-ID: 215281 [Multi-domain]  Cd Length: 499  Bit Score: 39.80  E-value: 4.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629  218 NGGVAVLTGKKVVqldVRDNMVKLN--DGSQITY--EKCLIATGGTPRSLsAIDRAGAEVKSRTTLfrkigdfrSLEKIS 293
Cdd:PLN02507 136 NAGVKLYEGEGKI---VGPNEVEVTqlDGTKLRYtaKHILIATGSRAQRP-NIPGKELAITSDEAL--------SLEELP 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629  294 REVksiTIIGGGFLGSELACALgrkaRALGTEVIQLF----PEKG---NMGKILPEYLSNwtmekvrrEGVKVMPNAIVQ 366
Cdd:PLN02507 204 KRA---VVLGGGYIAVEFASIW----RGMGATVDLFFrkelPLRGfddEMRAVVARNLEG--------RGINLHPRTNLT 268

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629  367 SVGVSSGKLLIKLKDGRKVETDHIVAAVGLEPN----------VELAKTGGLEIDSdfggfrvnaelQARSN---IWVAG 433
Cdd:PLN02507 269 QLTKTEGGIKVITDHGEEFVADVVLFATGRAPNtkrlnleavgVELDKAGAVKVDE-----------YSRTNipsIWAIG 337


                 ..
gi 22202629  434 DA 435
Cdd:PLN02507 338 DV 339
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
 247-436 9.27e-03

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 38.98  E-value: 9.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629  247 ITYEKCLIATGGTPRSLSAidragAEVKSRTTLFRKIGDFR-------------SLEKISREVK----SITIIGGGFLGS 309
Cdd:PTZ00318 112 VPYDKLVVAHGARPNTFNI-----PGVEERAFFLKEVNHARgirkrivqcieraSLPTTSVEERkrllHFVVVGGGPTGV 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22202629  310 ELACALG----RKARALGTEVIQLFP----EKGnmGKILPEY---LSNWTMEKVRREGVKVMPNAIVqsVGVSSGKLLik 378
Cdd:PTZ00318 187 EFAAELAdffrDDVRNLNPELVEECKvtvlEAG--SEVLGSFdqaLRKYGQRRLRRLGVDIRTKTAV--KEVLDKEVV-- 260

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22202629  379 LKDGRKVETDHIVAAVGLEPNvelAKTGGLEIDSDFGG-FRVNAELQAR--SNIWVAGDAA 436
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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