|
Name |
Accession |
Description |
Interval |
E-value |
| AIF_C |
pfam14721 |
Apoptosis-inducing factor, mitochondrion-associated, C-term; This C-terminal domain appears to ... |
464-593 |
4.73e-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: 251.03 E-value: 4.73e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 464 AGENMTGAAKPYWHQSMFWSDLGPDVGYEAIGLVDSSLPTVGVFAKATAQDNPKSATEQSGTGIRSESETESEASEITIP 543
Cdd:pfam14721 1 AGENMTGAGKPYWHQSMFWSDLGPDVGYEAIGIVDSSLPTVGVFAKATEKDTPKAVVEESGESIRSESEEEATASASAAP 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 13431781 544 PSAPAVPQVPVEGEDYGKGVIFYLRDKVVVGIVLWNVFNRMPIARKIIKD 593
Cdd:pfam14721 81 SSEDVASEDPSPGEDYGKGVIFYLRDDKVVGIVLWNVFNRMPIARKIIKD 130
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
147-595 |
2.85e-65 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 219.24 E-value: 2.85e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 147 RSIRARDPGARVLIVSEDPELPYMRPPLSKELwfsddpnvtktlqfrqwNGK--ERSIYFQPPSFYvsaqdlpniENGGV 224
Cdd:COG1251 18 EELRKLDPDGEITVIGAEPHPPYNRPPLSKVL-----------------AGEtdEEDLLLRPADFY---------EENGI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 225 AVLTGKKVVHLDVRGNMVKLNDGSQITFEKCLIATGGTPRSLSAidrAGAEVKSRTTlFRKIGDFRALEKISREVKSITV 304
Cdd:COG1251 72 DLRLGTRVTAIDRAARTVTLADGETLPYDKLVLATGSRPRVPPI---PGADLPGVFT-LRTLDDADALRAALAPGKRVVV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 305 IGGGFLGSELACALgrksQASGIEVIQLFPEKGNMGKILPQYLSNWTMEKVKREGVKVMPNAIVQSVGVSGGRLLIKLKD 384
Cdd:COG1251 148 IGGGLIGLEAAAAL----RKRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTGVRLAD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 385 GRKVETDHIVTAVGLEPNVELAKTGGLEIDsdfGGFRVNAELQA-RSNIWVAGDAACFYDIKLGRRRVEHHDHAVVSGRL 463
Cdd:COG1251 224 GEELPADLVVVAIGVRPNTELARAAGLAVD---RGIVVDDYLRTsDPDIYAAGDCAEHPGPVYGRRVLELVAPAYEQARV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 464 AGENMTGAAKPYWH-QSMFWSDLgPDVGYEAIGLVDsslptvgvfakataqdnpksATEQSgtgirseseteseaseiti 542
Cdd:COG1251 301 AAANLAGGPAAYEGsVPSTKLKV-FGVDVASAGDAE--------------------GDEEV------------------- 340
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 13431781 543 ppsapavpqVPVEGEDYGKGVIFYLRDKVVVGIVLWNVFNRMPIARKIIKDGE 595
Cdd:COG1251 341 ---------VVRGDPARGVYKKLVLRDGRLVGAVLVGDTSDAGALRQLIKNGR 384
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
149-461 |
6.05e-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: 145.15 E-value: 6.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 149 IRARDPGARVLIVSEDPELPYMRPPLSKELWFSDDPnvtktlqfrqwngkeRSIYFQPPSFYVSAQDLPNIENGGVAVLT 228
Cdd:pfam07992 17 LTLAQLGGKVTLIEDEGTCPYGGCVLSKALLGAAEA---------------PEIASLWADLYKRKEEVVKKLNNGIEVLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 229 GKKVVHLD-----VRGNMVKLNDGSQITFEKCLIATGGTPRSLSAidrAGAEvKSRTTLFRKIGDFRALEKISREvKSIT 303
Cdd:pfam07992 82 GTEVVSIDpgakkVVLEELVDGDGETITYDRLVIATGARPRLPPI---PGVE-LNVGFLVRTLDSAEALRLKLLP-KRVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 304 VIGGGFLGSELACALgrKSQASGIEVIQLFPEkgnMGKILPQYLSNWTMEKVKREGVKVMPNAIVQSVGVSGGRLLIKLK 383
Cdd:pfam07992 157 VVGGGYIGVELAAAL--AKLGKEVTLIEALDR---LLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGVEVILK 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13431781 384 DGRKVETDHIVTAVGLEPNVELAKTGGLEIDSDfGGFRVNAELQ-ARSNIWVAGDAacfydiklGRRRVEHHDHAVVSG 461
Cdd:pfam07992 232 DGTEIDADLVVVAIGRRPNTELLEAAGLELDER-GGIVVDEYLRtSVPGIYAAGDC--------RVGGPELAQNAVAQG 301
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
148-484 |
6.60e-23 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 101.16 E-value: 6.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 148 SIRARDPGARVLIVSEDPELPYMRPPLSKELWFSDDPNVTktlqfrqwngkersiYFQPPSFYVSAQdlpnienggVAVL 227
Cdd:PRK09754 21 SLRQQGFTGELHLFSDERHLPYERPPLSKSMLLEDSPQLQ---------------QVLPANWWQENN---------VHLH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 228 TGKKVVHLDVRGNMVKLNDGSQITFEKCLIATGGTPRSLSAIDRAGAEVKSrttlFRKIGDFRALEKISREVKSITVIGG 307
Cdd:PRK09754 77 SGVTIKTLGRDTRELVLTNGESWHWDQLFIATGAAARPLPLLDALGERCFT----LRHAGDAARLREVLQPERSVVIVGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 308 GFLGSELA---CALGRKsqasgIEVIQLfpEKGNMGKILPQYLSNWTMEKVKREGVKVMPNAIVQSVgVSGGRLLIKLKD 384
Cdd:PRK09754 153 GTIGLELAasaTQRRCK-----VTVIEL--AATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHV-VDGEKVELTLQS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 385 GRKVETDHIVTAVGLEPNVELAKTGGLEIDsdfGGFRVNAELQ-ARSNIWVAGDAACFYDIKLGRRRVEHHDHAVVSGRL 463
Cdd:PRK09754 225 GETLQADVVIYGIGISANDQLAREANLDTA---NGIVIDEACRtCDPAIFAGGDVAITRLDNGALHRCESWENANNQAQI 301
|
330 340
....*....|....*....|.
gi 13431781 464 AGENMTGAAKPYWHQSMFWSD 484
Cdd:PRK09754 302 AAAAMLGLPLPLLPPPWFWSD 322
|
|
| AIF-MLS |
pfam14962 |
Mitochondria localization Sequence; This family contains a protein found in eukaryotes. ... |
51-128 |
4.12e-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: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 51 RQMASS---GSSGGKMdnsVLVLIVGLSTIGAGAYAYKTIKEDQKRYNERVMGLG------LSPEEKQRRAIASATEGGS 121
Cdd:pfam14962 31 RRMSSNkfpGSSGSNM---IYYLVVGVTVSAGGYYTYKTVTSEQAKHTEHVTNLKektkaeLHPLQGEKENVAEAEKASS 107
|
....*...
gi 13431781 122 -VPQIRAP 128
Cdd:pfam14962 108 eAPEVSVV 115
|
|
| vWA_transcription_factor_IIH_type |
cd01453 |
Transcription factors IIH type: TFIIH is a multiprotein complex that is one of the five ... |
47-121 |
9.62e-03 |
|
Transcription factors IIH type: TFIIH is a multiprotein complex that is one of the five general transcription factors that binds RNA polymerase II holoenzyme. Orthologues of these genes are found in all completed eukaryotic genomes and all these proteins contain a VWA domain. The p44 subunit of TFIIH functions as a DNA helicase in RNA polymerase II transcription initiation and DNA repair, and its transcriptional activity is dependent on its C-terminal Zn-binding domains. The function of the vWA domain is unclear, but may be involved in complex assembly. The MIDAS motif is not conserved in this sub-group.
Pssm-ID: 238730 Cd Length: 183 Bit Score: 37.70 E-value: 9.62e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13431781 47 LQMARQ----MASSGSsggkmdNSVLVLIVGLSTIGAGAYaYKTIKEdQKRYNERVMGLGLSPEEKQRRAIASATEGGS 121
Cdd:cd01453 92 LEMALEslkhMPSHGS------REVLIIFSSLSTCDPGNI-YETIDK-LKKENIRVSVIGLSAEMHICKEICKATNGTY 162
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| AIF_C |
pfam14721 |
Apoptosis-inducing factor, mitochondrion-associated, C-term; This C-terminal domain appears to ... |
464-593 |
4.73e-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: 251.03 E-value: 4.73e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 464 AGENMTGAAKPYWHQSMFWSDLGPDVGYEAIGLVDSSLPTVGVFAKATAQDNPKSATEQSGTGIRSESETESEASEITIP 543
Cdd:pfam14721 1 AGENMTGAGKPYWHQSMFWSDLGPDVGYEAIGIVDSSLPTVGVFAKATEKDTPKAVVEESGESIRSESEEEATASASAAP 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 13431781 544 PSAPAVPQVPVEGEDYGKGVIFYLRDKVVVGIVLWNVFNRMPIARKIIKD 593
Cdd:pfam14721 81 SSEDVASEDPSPGEDYGKGVIFYLRDDKVVGIVLWNVFNRMPIARKIIKD 130
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
147-595 |
2.85e-65 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 219.24 E-value: 2.85e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 147 RSIRARDPGARVLIVSEDPELPYMRPPLSKELwfsddpnvtktlqfrqwNGK--ERSIYFQPPSFYvsaqdlpniENGGV 224
Cdd:COG1251 18 EELRKLDPDGEITVIGAEPHPPYNRPPLSKVL-----------------AGEtdEEDLLLRPADFY---------EENGI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 225 AVLTGKKVVHLDVRGNMVKLNDGSQITFEKCLIATGGTPRSLSAidrAGAEVKSRTTlFRKIGDFRALEKISREVKSITV 304
Cdd:COG1251 72 DLRLGTRVTAIDRAARTVTLADGETLPYDKLVLATGSRPRVPPI---PGADLPGVFT-LRTLDDADALRAALAPGKRVVV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 305 IGGGFLGSELACALgrksQASGIEVIQLFPEKGNMGKILPQYLSNWTMEKVKREGVKVMPNAIVQSVGVSGGRLLIKLKD 384
Cdd:COG1251 148 IGGGLIGLEAAAAL----RKRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTGVRLAD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 385 GRKVETDHIVTAVGLEPNVELAKTGGLEIDsdfGGFRVNAELQA-RSNIWVAGDAACFYDIKLGRRRVEHHDHAVVSGRL 463
Cdd:COG1251 224 GEELPADLVVVAIGVRPNTELARAAGLAVD---RGIVVDDYLRTsDPDIYAAGDCAEHPGPVYGRRVLELVAPAYEQARV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 464 AGENMTGAAKPYWH-QSMFWSDLgPDVGYEAIGLVDsslptvgvfakataqdnpksATEQSgtgirseseteseaseiti 542
Cdd:COG1251 301 AAANLAGGPAAYEGsVPSTKLKV-FGVDVASAGDAE--------------------GDEEV------------------- 340
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 13431781 543 ppsapavpqVPVEGEDYGKGVIFYLRDKVVVGIVLWNVFNRMPIARKIIKDGE 595
Cdd:COG1251 341 ---------VVRGDPARGVYKKLVLRDGRLVGAVLVGDTSDAGALRQLIKNGR 384
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
151-485 |
7.05e-48 |
|
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: 170.38 E-value: 7.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 151 ARDPGARVLIVSEDPELPYMRPPLSKELWFSDDpnvtktlqfrqwngKERSIYFQPPSFYVSAqdlpniengGVAVLTGK 230
Cdd:COG0446 1 RLGPDAEITVIEKGPHHSYQPCGLPYYVGGGIK--------------DPEDLLVRTPESFERK---------GIDVRTGT 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 231 KVVHLDVRGNMVKLNDGSQITFEKCLIATGGTPRSLsAIDraGAEVKSRTTLfRKIGDFRAL-EKI-SREVKSITVIGGG 308
Cdd:COG0446 58 EVTAIDPEAKTVTLRDGETLSYDKLVLATGARPRPP-PIP--GLDLPGVFTL-RTLDDADALrEALkEFKGKRAVVIGGG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 309 FLGSELACALGRKsqasGIEVIQLFPEKGNMGKILPQYlSNWTMEKVKREGVKVMPNAIVQSVgVSGGRLLIKLKDGRKV 388
Cdd:COG0446 134 PIGLELAEALRKR----GLKVTLVERAPRLLGVLDPEM-AALLEEELREHGVELRLGETVVAI-DGDDKVAVTLTDGEEI 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 389 ETDHIVTAVGLEPNVELAKTGGLEIDSDfGGFRVNAELQAR-SNIWVAGDAACFYDIKLGRR-RVEHHDHAVVSGRLAGE 466
Cdd:COG0446 208 PADLVVVAPGVRPNTELAKDAGLALGER-GWIKVDETLQTSdPDVYAAGDCAEVPHPVTGKTvYIPLASAANKQGRVAAE 286
|
330
....*....|....*....
gi 13431781 467 NMTGAAKPYWHQSMFWSDL 485
Cdd:COG0446 287 NILGGPAPFPGLGTFISKV 305
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
149-461 |
6.05e-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: 145.15 E-value: 6.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 149 IRARDPGARVLIVSEDPELPYMRPPLSKELWFSDDPnvtktlqfrqwngkeRSIYFQPPSFYVSAQDLPNIENGGVAVLT 228
Cdd:pfam07992 17 LTLAQLGGKVTLIEDEGTCPYGGCVLSKALLGAAEA---------------PEIASLWADLYKRKEEVVKKLNNGIEVLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 229 GKKVVHLD-----VRGNMVKLNDGSQITFEKCLIATGGTPRSLSAidrAGAEvKSRTTLFRKIGDFRALEKISREvKSIT 303
Cdd:pfam07992 82 GTEVVSIDpgakkVVLEELVDGDGETITYDRLVIATGARPRLPPI---PGVE-LNVGFLVRTLDSAEALRLKLLP-KRVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 304 VIGGGFLGSELACALgrKSQASGIEVIQLFPEkgnMGKILPQYLSNWTMEKVKREGVKVMPNAIVQSVGVSGGRLLIKLK 383
Cdd:pfam07992 157 VVGGGYIGVELAAAL--AKLGKEVTLIEALDR---LLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGVEVILK 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13431781 384 DGRKVETDHIVTAVGLEPNVELAKTGGLEIDSDfGGFRVNAELQ-ARSNIWVAGDAacfydiklGRRRVEHHDHAVVSG 461
Cdd:pfam07992 232 DGTEIDADLVVVAIGRRPNTELLEAAGLELDER-GGIVVDEYLRtSVPGIYAAGDC--------RVGGPELAQNAVAQG 301
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
219-470 |
2.12e-23 |
|
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: 103.63 E-value: 2.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 219 IENGGVAVLTGKKVVhldVRGNMVKLNDGSQITFEKCLIATGGTPRSLSAIDRAGAEVKSRTTLFrkigdfrALEKIsre 298
Cdd:COG1249 101 LKKNGVDVIRGRARF---VDPHTVEVTGGETLTADHIVIATGSRPRVPPIPGLDEVRVLTSDEAL-------ELEEL--- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 299 VKSITVIGGGFLGSELACALgrksQASGIEVIQLfpekGNMGKILPQY---LSNWTMEKVKREGVKVMPNAIVQSVGVSG 375
Cdd:COG1249 168 PKSLVVIGGGYIGLEFAQIF----ARLGSEVTLV----ERGDRLLPGEdpeISEALEKALEKEGIDILTGAKVTSVEKTG 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 376 GRLLIKLKDGRKVET---DHIVTAVGLEPNVE---LAKTgGLEIDSDfGGFRVNAELQ-ARSNIWVAGDAAcfydiklGR 448
Cdd:COG1249 240 DGVTVTLEDGGGEEAveaDKVLVATGRRPNTDglgLEAA-GVELDER-GGIKVDEYLRtSVPGIYAIGDVT-------GG 310
|
250 260
....*....|....*....|..
gi 13431781 449 RRVEHhdHAVVSGRLAGENMTG 470
Cdd:COG1249 311 PQLAH--VASAEGRVAAENILG 330
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
148-484 |
6.60e-23 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 101.16 E-value: 6.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 148 SIRARDPGARVLIVSEDPELPYMRPPLSKELWFSDDPNVTktlqfrqwngkersiYFQPPSFYVSAQdlpnienggVAVL 227
Cdd:PRK09754 21 SLRQQGFTGELHLFSDERHLPYERPPLSKSMLLEDSPQLQ---------------QVLPANWWQENN---------VHLH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 228 TGKKVVHLDVRGNMVKLNDGSQITFEKCLIATGGTPRSLSAIDRAGAEVKSrttlFRKIGDFRALEKISREVKSITVIGG 307
Cdd:PRK09754 77 SGVTIKTLGRDTRELVLTNGESWHWDQLFIATGAAARPLPLLDALGERCFT----LRHAGDAARLREVLQPERSVVIVGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 308 GFLGSELA---CALGRKsqasgIEVIQLfpEKGNMGKILPQYLSNWTMEKVKREGVKVMPNAIVQSVgVSGGRLLIKLKD 384
Cdd:PRK09754 153 GTIGLELAasaTQRRCK-----VTVIEL--AATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHV-VDGEKVELTLQS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 385 GRKVETDHIVTAVGLEPNVELAKTGGLEIDsdfGGFRVNAELQ-ARSNIWVAGDAACFYDIKLGRRRVEHHDHAVVSGRL 463
Cdd:PRK09754 225 GETLQADVVIYGIGISANDQLAREANLDTA---NGIVIDEACRtCDPAIFAGGDVAITRLDNGALHRCESWENANNQAQI 301
|
330 340
....*....|....*....|.
gi 13431781 464 AGENMTGAAKPYWHQSMFWSD 484
Cdd:PRK09754 302 AAAAMLGLPLPLLPPPWFWSD 322
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
223-467 |
3.82e-21 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 95.58 E-value: 3.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 223 GVAVLTGKkVVHLDVRGNMVKLNDGSQITFEKCLIATGGTPRsLSAIDraGAE-----VKSR---TTLFRKIgdFRALEK 294
Cdd:COG1252 70 GVRFIQGE-VTGIDPEARTVTLADGRTLSYDYLVIATGSVTN-FFGIP--GLAehalpLKTLedaLALRERL--LAAFER 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 295 ISREVK-SITVIGGGFLGSELACAL----GRKSQASGIEviqlfPEKGN------MGKILPQY---LSNWTMEKVKREGV 360
Cdd:COG1252 144 AERRRLlTIVVVGGGPTGVELAGELaellRKLLRYPGID-----PDKVRitlveaGPRILPGLgekLSEAAEKELEKRGV 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 361 KVMPNAIVQSVGVSGgrllIKLKDGRKVETDHIVTAVGLEPNvELAKTGGLEIDSDfGGFRVNAELQARS--NIWVAGDA 438
Cdd:COG1252 219 EVHTGTRVTEVDADG----VTLEDGEEIPADTVIWAAGVKAP-PLLADLGLPTDRR-GRVLVDPTLQVPGhpNVFAIGDC 292
|
250 260 270
....*....|....*....|....*....|....*
gi 13431781 439 ACFYDI------KLGRrrvehhdHAVVSGRLAGEN 467
Cdd:COG1252 293 AAVPDPdgkpvpKTAQ-------AAVQQAKVLAKN 320
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
223-475 |
1.09e-17 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 85.86 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 223 GVAVLTGKKVVHLDVRGNMVK---LNDGSQI--TFEKCLIATGGTPrSLSAIDraGAEVKSRTTLfRKIGDFRALEKISR 297
Cdd:PRK09564 70 GIDVKTEHEVVKVDAKNKTITvknLKTGSIFndTYDKLMIATGARP-IIPPIK--NINLENVYTL-KSMEDGLALKELLK 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 298 --EVKSITVIGGGFLGSELACALgrKSQASGIEVIQLfpEKGNMGKILPQYLSNWTMEKVKREGVKVMPNAIVQSVgVSG 375
Cdd:PRK09564 146 deEIKNIVIIGAGFIGLEAVEAA--KHLGKNVRIIQL--EDRILPDSFDKEITDVMEEELRENGVELHLNEFVKSL-IGE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 376 GRLLIKLKDGRKVETDHIVTAVGLEPNVELAKTGGLEIDSDfGGFRVNAELQAR-SNIWVAGDAACFYDIKLGRRR-VEH 453
Cdd:PRK09564 221 DKVEGVVTDKGEYEADVVIVATGVKPNTEFLEDTGLKTLKN-GAIIVDEYGETSiENIYAAGDCATIYNIVSNKNVyVPL 299
|
250 260
....*....|....*....|..
gi 13431781 454 HDHAVVSGRLAGENMTGAAKPY 475
Cdd:PRK09564 300 ATTANKLGRMVGENLAGRHVSF 321
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
289-439 |
5.26e-17 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 83.04 E-value: 5.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 289 FRALEKISREVKSITVIGGGFLGSELACALGRksqaSGIEVIQLFPEKGNMGKILPQYLSNWTMEKVKREGVKVMPNAIV 368
Cdd:PRK04965 131 YRAAETQLRDAQRVLVVGGGLIGTELAMDLCR----AGKAVTLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQL 206
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13431781 369 QSVGVSGGRLLIKLKDGRKVETDHIVTAVGLEPNVELAKTGGLEIDSdfgGFRVNAELQ-ARSNIWVAGDAA 439
Cdd:PRK04965 207 QGLEKTDSGIRATLDSGRSIEVDAVIAAAGLRPNTALARRAGLAVNR---GIVVDSYLQtSAPDIYALGDCA 275
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
220-439 |
4.89e-16 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 82.09 E-value: 4.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 220 ENGGVAVLTGKKVVHLDVRGNMVKLNDGSQITFEKCLIATGGTPrSLSAIdrAGAEVKSrTTLFRKIGDFRALEKISREV 299
Cdd:PRK14989 70 EKHGIKVLVGERAITINRQEKVIHSSAGRTVFYDKLIMATGSYP-WIPPI--KGSETQD-CFVYRTIEDLNAIEACARRS 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 300 KSITVIGGGFLGSELACALgrksQASGIE--VIQLFPEKgnMGKILPQYLSNWTMEKVKREGVKVMPNAIVQSVGVSG-- 375
Cdd:PRK14989 146 KRGAVVGGGLLGLEAAGAL----KNLGVEthVIEFAPML--MAEQLDQMGGEQLRRKIESMGVRVHTSKNTLEIVQEGve 219
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13431781 376 GRLLIKLKDGRKVETDHIVTAVGLEPNVELAKTGGLEIdSDFGGFRVNAELQ-ARSNIWVAGDAA 439
Cdd:PRK14989 220 ARKTMRFADGSELEVDFIVFSTGIRPQDKLATQCGLAV-APRGGIVINDSCQtSDPDIYAIGECA 283
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
220-437 |
6.19e-15 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 77.50 E-value: 6.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 220 ENGGVAVLTGKKVVhldVRGNMVKLNdGSQITFEKCLIATGGTPrslSAIDRAGAE--VKSRttlfrkigDFRALEKISr 297
Cdd:PRK06116 104 ENNGVDLIEGFARF---VDAHTVEVN-GERYTADHILIATGGRP---SIPDIPGAEygITSD--------GFFALEELP- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 298 evKSITVIGGGFLGSELACALgrksQASGIEVIQLFpeKGNmgKIL---PQYLSNWTMEKVKREGVKVMPNAIVQSVG-V 373
Cdd:PRK06116 168 --KRVAVVGAGYIAVEFAGVL----NGLGSETHLFV--RGD--APLrgfDPDIRETLVEEMEKKGIRLHTNAVPKAVEkN 237
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13431781 374 SGGRLLIKLKDGRKVETDHIVTAVGLEPNVE---LAKTgGLEIDsDFGGFRVNAELQ-ARSNIWVAGD 437
Cdd:PRK06116 238 ADGSLTLTLEDGETLTVDCLIWAIGREPNTDglgLENA-GVKLN-EKGYIIVDEYQNtNVPGIYAVGD 303
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
246-475 |
3.97e-12 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 68.67 E-value: 3.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 246 DGSQITFEKCLIATGGTPRSLSAIDRA-GAEVKSRTTLFRkigdfraLEKISrevKSITVIGGGFLGSELACALGRksqa 324
Cdd:PRK06292 125 NGERIEAKNIVIATGSRVPPIPGVWLIlGDRLLTSDDAFE-------LDKLP---KSLAVIGGGVIGLELGQALSR---- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 325 SGIEVIqLFpekGNMGKILPQY---LSNWTMEKVKREgVKVMPNAIVQSVGVSGGRLLIKLKDGRKVET---DHIVTAVG 398
Cdd:PRK06292 191 LGVKVT-VF---ERGDRILPLEdpeVSKQAQKILSKE-FKIKLGAKVTSVEKSGDEKVEELEKGGKTETieaDYVLVATG 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 399 LEPNVE---LAKTgGLEIDSDfgGF-RVNAEL-QARSNIWVAGDAAcfydiklGRRRVEHhdHAVVSGRLAGENMTGAAK 473
Cdd:PRK06292 266 RRPNTDglgLENT-GIELDER--GRpVVDEHTqTSVPGIYAAGDVN-------GKPPLLH--EAADEGRIAAENAAGDVA 333
|
..
gi 13431781 474 PY 475
Cdd:PRK06292 334 GG 335
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
246-437 |
8.17e-12 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 67.53 E-value: 8.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 246 DGSQITFEKCLIATGGTPR--SLSAIDRAGAevKSRTTLFrkigdfrALEKISRevkSITVIGGGFLGSELACALGRksq 323
Cdd:PRK06370 128 GGETLRAKRIFINTGARAAipPIPGLDEVGY--LTNETIF-------SLDELPE---HLVIIGGGYIGLEFAQMFRR--- 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 324 aSGIEVIQLfpEKGNmgKILPQY---LSNWTMEKVKREGVKVMPNAIVQSVGVSGGRLLIKLK---DGRKVETDHIVTAV 397
Cdd:PRK06370 193 -FGSEVTVI--ERGP--RLLPREdedVAAAVREILEREGIDVRLNAECIRVERDGDGIAVGLDcngGAPEITGSHILVAV 267
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 13431781 398 GLEPNVE---LAKTgGLEIDSDfGGFRVNAELQAR-SNIWVAGD 437
Cdd:PRK06370 268 GRVPNTDdlgLEAA-GVETDAR-GYIKVDDQLRTTnPGIYAAGD 309
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
301-385 |
1.97e-09 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 425450 [Multi-domain] Cd Length: 80 Bit Score: 54.52 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 301 SITVIGGGFLGSELACALGRKsqasGIEViQLFPEKGNMGKILPQYLSNWTMEKVKREGVKVMPNAIVQSVGVSGGRLLI 380
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARL----GSKV-TVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVV 75
|
....*
gi 13431781 381 KLKDG 385
Cdd:pfam00070 76 VLTDG 80
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
242-473 |
9.88e-09 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 57.86 E-value: 9.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 242 VKLNDGS--QITFEKCLIATGGTPRSLSAIDRAGAEVKSRTTLfrkigdfraLEkISREVKSITVIGGGFLGSELAC--- 316
Cdd:PRK05249 126 VECPDGEveTLTADKIVIATGSRPYRPPDVDFDHPRIYDSDSI---------LS-LDHLPRSLIIYGAGVIGCEYASifa 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 317 ALGRKsqasgIEVIQlfpekgNMGKILPqYLSNWTMEKVK---RE-GVKVMPNAIVQSVGVSGGRLLIKLKDGRKVETDH 392
Cdd:PRK05249 196 ALGVK-----VTLIN------TRDRLLS-FLDDEISDALSyhlRDsGVTIRHNEEVEKVEGGDDGVIVHLKSGKKIKADC 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 393 IVTAVGLEPNVE---LAKTgGLEIDSDfGGFRVNAELQ-ARSNIWVAGD-------AACFYDiklgrrrvehhdhavvSG 461
Cdd:PRK05249 264 LLYANGRTGNTDglnLENA-GLEADSR-GQLKVNENYQtAVPHIYAVGDvigfpslASASMD----------------QG 325
|
250
....*....|..
gi 13431781 462 RLAGENMTGAAK 473
Cdd:PRK05249 326 RIAAQHAVGEAT 337
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
223-439 |
1.70e-08 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 57.08 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 223 GVAVLTGKKVVhldvrgnMVKLNDGSQ-ITFEKCLIATGGTPRSLSAIDRAGaevksrttlfRKIGD-FRALeKISREVK 300
Cdd:PRK06416 112 GEAKLVDPNTV-------RVMTEDGEQtYTAKNIILATGSRPRELPGIEIDG----------RVIWTsDEAL-NLDEVPK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 301 SITVIGGGFLGSELACA---LGrkSQASGIEVI-QLFP-EKGNMGKILpqylsnwtmEKV-KREGVKVMPNAIVQSVGVS 374
Cdd:PRK06416 174 SLVVIGGGYIGVEFASAyasLG--AEVTIVEALpRILPgEDKEISKLA---------ERAlKKRGIKIKTGAKAKKVEQT 242
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13431781 375 GGRLLIKLKDGRKVET---DHIVTAVGLEPNVE---LAKTgGLEIDsdfGGF-RVNAELQAR-SNIWVAGDAA 439
Cdd:PRK06416 243 DDGVTVTLEDGGKEETleaDYVLVAVGRRPNTEnlgLEEL-GVKTD---RGFiEVDEQLRTNvPNIYAIGDIV 311
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
244-438 |
5.04e-08 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 55.78 E-value: 5.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 244 LNDGSQITFEKCLIATGGTPRSlsaIDRAGAEVKSRTTLFRKIgdfralekisREVKSITVIGGGFLGSELACALgrksQ 323
Cdd:PTZ00058 195 LDDGQVIEGKNILIAVGNKPIF---PDVKGKEFTISSDDFFKI----------KEAKRIGIAGSGYIAVELINVV----N 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 324 ASGIEViQLFPEKGNMGKILPQYLSNWTMEKVKREGVKVMPNAIVQSV-GVSGGRLLIKLKDGRKVET-DHIVTAVGLEP 401
Cdd:PTZ00058 258 RLGAES-YIFARGNRLLRKFDETIINELENDMKKNNINIITHANVEEIeKVKEKNLTIYLSDGRKYEHfDYVIYCVGRSP 336
|
170 180 190
....*....|....*....|....*....|....*...
gi 13431781 402 NVELAKTGGLEIDSDFGGFRVNA-ELQARSNIWVAGDA 438
Cdd:PTZ00058 337 NTEDLNLKALNIKTPKGYIKVDDnQRTSVKHIYAVGDC 374
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
223-437 |
7.81e-08 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 55.25 E-value: 7.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 223 GVAVLTGK-KVVHLDVRGNMVK--LNDGSQITFEK--CLIATGGTPRSLsaidrAGAEVKSRTTL-FRKIGDFRAL-EKI 295
Cdd:PRK07845 106 GVRVIAGRgRLIDPGLGPHRVKvtTADGGEETLDAdvVLIATGASPRIL-----PTAEPDGERILtWRQLYDLDELpEHL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 296 srevksiTVIGGGFLGSELACALgrksQASGIEVI------QLFP-EKGNMGKILpqylsnwtmEKV-KREGVKVMPNAI 367
Cdd:PRK07845 181 -------IVVGSGVTGAEFASAY----TELGVKVTlvssrdRVLPgEDADAAEVL---------EEVfARRGMTVLKRSR 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 368 VQSVGVSGGRLLIKLKDGRKVETDHIVTAVGLEPN----------VELAKTGGLEIDsdfggfRVnaelqARSN---IWV 434
Cdd:PRK07845 241 AESVERTGDGVVVTLTDGRTVEGSHALMAVGSVPNtaglgleeagVELTPSGHITVD------RV-----SRTSvpgIYA 309
|
...
gi 13431781 435 AGD 437
Cdd:PRK07845 310 AGD 312
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
231-439 |
4.48e-06 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 48.96 E-value: 4.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 231 KVVHLDVRGN--MVKLNDGSQITFEKCLIATGGTPRSLSAidrAGAE----------VKSRTTLFRKigdfralekisre 298
Cdd:COG0492 78 EVTSVDKDDGpfRVTTDDGTEYEAKAVIIATGAGPRKLGL---PGEEefegrgvsycATCDGFFFRG------------- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 299 vKSITVIGGGFLGSELACAL------------GRKSQASGIEVIQLFpekgnmgkilpqylsnwtmekvKREGVKVMPNA 366
Cdd:COG0492 142 -KDVVVVGGGDSALEEALYLtkfaskvtlihrRDELRASKILVERLR----------------------ANPKIEVLWNT 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 367 IVQSV----GVSGgrllIKLKDG-----RKVETDHIVTAVGLEPNVELAKTGGLEIDSDfGGFRVNAELQ-ARSNIWVAG 436
Cdd:COG0492 199 EVTEIegdgRVEG----VTLKNVktgeeKELEVDGVFVAIGLKPNTELLKGLGLELDED-GYIVVDEDMEtSVPGVFAAG 273
|
...
gi 13431781 437 DAA 439
Cdd:COG0492 274 DVR 276
|
|
| AIF-MLS |
pfam14962 |
Mitochondria localization Sequence; This family contains a protein found in eukaryotes. ... |
51-128 |
4.12e-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: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 51 RQMASS---GSSGGKMdnsVLVLIVGLSTIGAGAYAYKTIKEDQKRYNERVMGLG------LSPEEKQRRAIASATEGGS 121
Cdd:pfam14962 31 RRMSSNkfpGSSGSNM---IYYLVVGVTVSAGGYYTYKTVTSEQAKHTEHVTNLKektkaeLHPLQGEKENVAEAEKASS 107
|
....*...
gi 13431781 122 -VPQIRAP 128
Cdd:pfam14962 108 eAPEVSVV 115
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
302-416 |
3.20e-04 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 42.98 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 302 ITVIGGGFLGSELACALGRKsqasGIEVIQLFP--EKGNMGKILPQYLSNWT----MEKVKREGVKVMPNAIVQSVGVSG 375
Cdd:pfam13738 158 VVVIGGYNSAVDAALELVRK----GARVTVLYRgsEWEDRDSDPSYSLSPDTlnrlEELVKNGKIKAHFNAEVKEITEVD 233
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 13431781 376 GRLLIKLKDGRKVETDHI-VTAVGLEPNVELAKTGGLEIDSD 416
Cdd:pfam13738 234 VSYKVHTEDGRKVTSNDDpILATGYHPDLSFLKKGLFELDED 275
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
204-439 |
1.23e-03 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 41.69 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 204 FQPPSFYvsaqdlpniENGGVAVLTGKKVVHLDVRGNMV-----KLNDGSQITFEKCLIATGGTPRSLsaidraGAEVKS 278
Cdd:PRK13512 62 YTPEKFY---------DRKQITVKTYHEVIAINDERQTVtvlnrKTNEQFEESYDKLILSPGASANSL------GFESDI 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 279 RTTLfRKIGDFRALEK-ISR-EVKSITVIGGGFLGSELACALgrksQASGIEViQLFPEKGNMGKILPQYLSNWTMEKVK 356
Cdd:PRK13512 127 TFTL-RNLEDTDAIDQfIKAnQVDKALVVGAGYISLEVLENL----YERGLHP-TLIHRSDKINKLMDADMNQPILDELD 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 357 REGVKVMPNAIVQSVGVSggrlLIKLKDGRKVETDHIVTAVGLEPNVELAKTGGLEIDsDFGGFRVNAELQAR-SNIWVA 435
Cdd:PRK13512 201 KREIPYRLNEEIDAINGN----EVTFKSGKVEHYDMIIEGVGTHPNSKFIESSNIKLD-DKGFIPVNDKFETNvPNIYAI 275
|
....
gi 13431781 436 GDAA 439
Cdd:PRK13512 276 GDII 279
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
221-437 |
3.09e-03 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 40.29 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 221 NGGVAVLTGK-KVVHLDVRGNMVKLNDGS-----------QITFEKCLIATGGTPRSLSAIDRAGAEVKSRTTlfrkigd 288
Cdd:PRK06327 103 TGGIEGLFKKnKITVLKGRGSFVGKTDAGyeikvtgedetVITAKHVIIATGSEPRHLPGVPFDNKIILDNTG------- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 289 frALEkISREVKSITVIGGGFLGSELACALGRksqaSGIEVIQLfpekgnmgKILPQYL-------SNWTMEKVKREGVK 361
Cdd:PRK06327 176 --ALN-FTEVPKKLAVIGAGVIGLELGSVWRR----LGAEVTIL--------EALPAFLaaadeqvAKEAAKAFTKQGLD 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13431781 362 VMPNAIVQSVGVSGGRLLIKLKDG----RKVETDHIVTAVGLEPNVE--LAKTGGLEIDsDFGGFRVNAELQAR-SNIWV 434
Cdd:PRK06327 241 IHLGVKIGEIKTGGKGVSVAYTDAdgeaQTLEVDKLIVSIGRVPNTDglGLEAVGLKLD-ERGFIPVDDHCRTNvPNVYA 319
|
...
gi 13431781 435 AGD 437
Cdd:PRK06327 320 IGD 322
|
|
| vWA_transcription_factor_IIH_type |
cd01453 |
Transcription factors IIH type: TFIIH is a multiprotein complex that is one of the five ... |
47-121 |
9.62e-03 |
|
Transcription factors IIH type: TFIIH is a multiprotein complex that is one of the five general transcription factors that binds RNA polymerase II holoenzyme. Orthologues of these genes are found in all completed eukaryotic genomes and all these proteins contain a VWA domain. The p44 subunit of TFIIH functions as a DNA helicase in RNA polymerase II transcription initiation and DNA repair, and its transcriptional activity is dependent on its C-terminal Zn-binding domains. The function of the vWA domain is unclear, but may be involved in complex assembly. The MIDAS motif is not conserved in this sub-group.
Pssm-ID: 238730 Cd Length: 183 Bit Score: 37.70 E-value: 9.62e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13431781 47 LQMARQ----MASSGSsggkmdNSVLVLIVGLSTIGAGAYaYKTIKEdQKRYNERVMGLGLSPEEKQRRAIASATEGGS 121
Cdd:cd01453 92 LEMALEslkhMPSHGS------REVLIIFSSLSTCDPGNI-YETIDK-LKKENIRVSVIGLSAEMHICKEICKATNGTY 162
|
|
|