|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
1-377 |
0e+00 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 717.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 1 MSRGIIIIGSGFAARQLVKNIRKQDAHVPLTLIAADSMDEYNKPDLSHVISQSQRADDLTRQLAGEFAEQFNLRRFPHTW 80
Cdd:PRK04965 1 MSNGIVIIGSGFAARQLVKNIRKQDAHIPITLITADSGDEYNKPDLSHVFSQGQRADDLTRQSAGEFAEQFNLRLFPHTW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 81 VADIDADAHVVKSQDKQWQYDKLVLATGATAFVPPIAGRELMLTLNSQQEYRACETQLRDAQRVLIVGGGLIGSELAMDF 160
Cdd:PRK04965 81 VTDIDAEAQVVKSQGNQWQYDKLVLATGASAFVPPIPGRELMLTLNSQQEYRAAETQLRDAQRVLVVGGGLIGTELAMDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 161 CRAGKTVTLMDNAASLLASLMPPEVSSRLQHHLTDMGVHLLLKSQLQKLEKTEAGIRATLVSQHSIEVDAVIAATGLRPE 240
Cdd:PRK04965 161 CRAGKAVTLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSGIRATLDSGRSIEVDAVIAAAGLRPN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 241 TALARRAGVAVNRGVCVDSYLQTSHPDIYAIGDCAEINGQVLPFLQPIQLSAMYLAKNLLGGNAPLKLPAMLVKVKTPEL 320
Cdd:PRK04965 241 TALARRAGLAVNRGIVVDSYLQTSAPDIYALGDCAEINGQVLPFLQPIQLSAMALAKNLLGQNTPLKLPAMLVKVKTPEL 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 900269912 321 PLHLAGETQRRDLSWHITAESDGMIAKGMSGEGQLRAFVVSEDRMKEAFALLKTLSV 377
Cdd:PRK04965 321 PLQLAGETQRQDLRWQINAESQGMVAKGVDEAGQLRAFVVSEDRMKEAFPLLKELPV 377
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
2-364 |
1.10e-105 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 316.31 E-value: 1.10e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 2 SRGIIIIGSGFAARQLVKNIRKQDAHVPLTLIAADSMDEYNKPDLSHVISQSQRADDLTRQlAGEFAEQFNLRRFPHTWV 81
Cdd:COG1251 1 KMRIVIIGAGMAGVRAAEELRKLDPDGEITVIGAEPHPPYNRPPLSKVLAGETDEEDLLLR-PADFYEENGIDLRLGTRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 82 ADIDADAHVVKSQD-KQWQYDKLVLATGATAFVPPIAGREL--MLTLNSQQEYRACETQLRDAQRVLIVGGGLIGSELAM 158
Cdd:COG1251 80 TAIDRAARTVTLADgETLPYDKLVLATGSRPRVPPIPGADLpgVFTLRTLDDADALRAALAPGKRVVVIGGGLIGLEAAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 159 DFCRAGKTVTLMDNAASLLASLMPPEVSSRLQHHLTDMGVHLLLKSQLQKLEKTEAGIRATLVSQHSIEVDAVIAATGLR 238
Cdd:COG1251 160 ALRKRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTGVRLADGEELPADLVVVAIGVR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 239 PETALARRAGVAVNRGVCVDSYLQTSHPDIYAIGDCAEINGQV-----LPFLQPIQLSAMYLAKNLLGGNAPLKLPAMLV 313
Cdd:COG1251 240 PNTELARAAGLAVDRGIVVDDYLRTSDPDIYAAGDCAEHPGPVygrrvLELVAPAYEQARVAAANLAGGPAAYEGSVPST 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 900269912 314 KVKTPELPLHLAGETQRRDLSwhitaesdgmIAKGMSGEGQLRAFVVSEDR 364
Cdd:COG1251 320 KLKVFGVDVASAGDAEGDEEV----------VVRGDPARGVYKKLVLRDGR 360
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
23-305 |
4.60e-62 |
|
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: 201.96 E-value: 4.60e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 23 KQDAHVPLTLIAADSMDEYNKPDLS-HVISQSQRADDLTRQLAgEFAEQFNLRRFPHTWVADIDADAHVVKSQD-KQWQY 100
Cdd:COG0446 1 RLGPDAEITVIEKGPHHSYQPCGLPyYVGGGIKDPEDLLVRTP-ESFERKGIDVRTGTEVTAIDPEAKTVTLRDgETLSY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 101 DKLVLATGATAFVPPIAGREL--MLTLNSQQEYRACETQLR--DAQRVLIVGGGLIGSELAMDFCRAGKTVTLMDNAASL 176
Cdd:COG0446 80 DKLVLATGARPRPPPIPGLDLpgVFTLRTLDDADALREALKefKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 177 LASlMPPEVSSRLQHHLTDMGVHLLLKSQLQKLEKtEAGIRATLVSQHSIEVDAVIAATGLRPETALARRAGVAVNR--G 254
Cdd:COG0446 160 LGV-LDPEMAALLEEELREHGVELRLGETVVAIDG-DDKVAVTLTDGEEIPADLVVVAPGVRPNTELAKDAGLALGErgW 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 900269912 255 VCVDSYLQTSHPDIYAIGDCAEINGQV------LPFLQPIQLSAMYLAKNLLGGNAP 305
Cdd:COG0446 238 IKVDETLQTSDPDVYAAGDCAEVPHPVtgktvyIPLASAANKQGRVAAENILGGPAP 294
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
5-363 |
2.10e-49 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 177.71 E-value: 2.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 5 IIIIGSGFAARQLVKNIRKQDAH-VPLTLIAADSMDEYNKPDLSHVISQSQRADDLTrqLAGE-FAEQFNLRRFPHTWVA 82
Cdd:TIGR02374 1 LVLVGNGMAGHRCIEEVLKLNRHmFEITIFGEEPHPNYNRILLSSVLQGEADLDDIT--LNSKdWYEKHGITLYTGETVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 83 DIDADAHVVKSQDKQWQ-YDKLVLATGATAFVPPIAGREL-----MLTLNSQQEYRACETQLRDAqrvLIVGGGLIGSEL 156
Cdd:TIGR02374 79 QIDTDQKQVITDAGRTLsYDKLILATGSYPFILPIPGADKkgvyvFRTIEDLDAIMAMAQRFKKA---AVIGGGLLGLEA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 157 AMDFCRAGKTVTLMDNAASLLASLMPPEVSSRLQHHLTDMG--VHLLLKSQLQKLEKTEAGIRatLVSQHSIEVDAVIAA 234
Cdd:TIGR02374 156 AVGLQNLGMDVSVIHHAPGLMAKQLDQTAGRLLQRELEQKGltFLLEKDTVEIVGATKADRIR--FKDGSSLEADLIVMA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 235 TGLRPETALARRAGVAVNRGVCVDSYLQTSHPDIYAIGDCAEINGQVLPFLQPIQLSAMYLAKNLLGG-NAPLKLPAMLV 313
Cdd:TIGR02374 234 AGIRPNDELAVSAGIKVNRGIIVNDSMQTSDPDIYAVGECAEHNGRVYGLVAPLYEQAKVLADHICGVeCEEYEGSDLSA 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 900269912 314 KVKTPELPLHLAGETQR--RDLSWHITAESDGMIAKGMSGEGQLRAFVVSED 363
Cdd:TIGR02374 314 KLKLLGVDVWSAGDAQEteRTTSIKIYDEQKGIYKKLVLSDDKLLGAVLFGD 365
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
5-274 |
1.82e-46 |
|
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: 160.56 E-value: 1.82e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 5 IIIIGSGFAARQLVKNIRKQDAHVplTLIAADSMDEYNKPDLSHVISQSQRADD---LTRQLAGEFAEQF-----NLRRF 76
Cdd:pfam07992 3 VVVIGGGPAGLAAALTLAQLGGKV--TLIEDEGTCPYGGCVLSKALLGAAEAPEiasLWADLYKRKEEVVkklnnGIEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 77 PHTWVADIDADAHVVKSQDKQW------QYDKLVLATGATAFVPPIAGRELMLTLNSqqeyRACET--QLRDA---QRVL 145
Cdd:pfam07992 81 LGTEVVSIDPGAKKVVLEELVDgdgetiTYDRLVIATGARPRLPPIPGVELNVGFLV----RTLDSaeALRLKllpKRVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 146 IVGGGLIGSELAMDFCRAGKTVTLMDnAASLLASLMPPEVSSRLQHHLTDMGVHLLLKSQLQKLEKTEAGIRATLVSQHS 225
Cdd:pfam07992 157 VVGGGYIGVELAAALAKLGKEVTLIE-ALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGVEVILKDGTE 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 900269912 226 IEVDAVIAATGLRPETALARRAGVAVNR--GVCVDSYLQTSHPDIYAIGDC 274
Cdd:pfam07992 236 IDADLVVVAIGRRPNTELLEAAGLELDErgGIVVDEYLRTSVPGIYAAGDC 286
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
1-316 |
2.62e-29 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 119.84 E-value: 2.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 1 MSR-GIIIIGSGFAARQLVKN-IRKQDAH-VPLTLIAADSMDEYNKPDLSHVISQsQRADDLTRQLAGeFAEQFNLRRFP 77
Cdd:PRK14989 1 MSKvRLAIIGNGMVGHRFIEDlLDKADAAnFDITVFCEEPRIAYDRVHLSSYFSH-HTAEELSLVREG-FYEKHGIKVLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 78 HTWVADIDADAHVVKS-QDKQWQYDKLVLATGATAFVPPIAGRELM--LTLNSQQEYRACETQLRDAQRVLIVGGGLIGS 154
Cdd:PRK14989 79 GERAITINRQEKVIHSsAGRTVFYDKLIMATGSYPWIPPIKGSETQdcFVYRTIEDLNAIEACARRSKRGAVVGGGLLGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 155 ELAMDFCRAGKTVTLMDNAASLLASLMPPEVSSRLQHHLTDMGV--HLLLKSQLQKLEKTEAGIRATLVSQHSIEVDAVI 232
Cdd:PRK14989 159 EAAGALKNLGVETHVIEFAPMLMAEQLDQMGGEQLRRKIESMGVrvHTSKNTLEIVQEGVEARKTMRFADGSELEVDFIV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 233 AATGLRPETALARRAGVAVNR--GVCVDSYLQTSHPDIYAIGDCAEINGQVLPFLQPIQLSAMYLAKNLLGGNAPLKLPA 310
Cdd:PRK14989 239 FSTGIRPQDKLATQCGLAVAPrgGIVINDSCQTSDPDIYAIGECASWNNRVFGLVAPGYKMAQVAVDHLLGSENAFEGAD 318
|
....*.
gi 900269912 311 MLVKVK 316
Cdd:PRK14989 319 LSAKLK 324
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
5-300 |
5.17e-29 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 116.00 E-value: 5.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 5 IIIIGSGFA----ARQLVKNIRKQdahVPLTLIAADSMDEYnKPDLSHVISQSQRADDLTRQLAgEFAEQFNLRrFPHTW 80
Cdd:COG1252 4 IVIVGGGFAgleaARRLRKKLGGD---AEVTLIDPNPYHLF-QPLLPEVAAGTLSPDDIAIPLR-ELLRRAGVR-FIQGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 81 VADIDADAHVVKSQDKQW-QYDKLVLATGATAFVPPIAG-RELMLTLNSQQE----YRACETQLRDAQR-----VLIVGG 149
Cdd:COG1252 78 VTGIDPEARTVTLADGRTlSYDYLVIATGSVTNFFGIPGlAEHALPLKTLEDalalRERLLAAFERAERrrlltIVVVGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 150 GLIGSELAM-------DFCRAGK------TVTLMDNAASLLASlMPPEVSSRLQHHLTDMGVHLllksqlqkleKTEAGI 216
Cdd:COG1252 158 GPTGVELAGelaellrKLLRYPGidpdkvRITLVEAGPRILPG-LGEKLSEAAEKELEKRGVEV----------HTGTRV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 217 ------RATLVSQHSIEVDAVIAATGLRPeTALARRAGVAVNRG--VCVDSYLQT-SHPDIYAIGDCAEINGQVLPFL-- 285
Cdd:COG1252 227 tevdadGVTLEDGEEIPADTVIWAAGVKA-PPLLADLGLPTDRRgrVLVDPTLQVpGHPNVFAIGDCAAVPDPDGKPVpk 305
|
330
....*....|....*..
gi 900269912 286 --QPIQLSAMYLAKNLL 300
Cdd:COG1252 306 taQAAVQQAKVLAKNIA 322
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
86-304 |
6.47e-29 |
|
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: 116.72 E-value: 6.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 86 ADAHVVK-SQDKQWQYDKLVLATGATAFVPPIAGRELMLTLNSqqeyracetqlRDA-------QRVLIVGGGLIGSELA 157
Cdd:COG1249 116 VDPHTVEvTGGETLTADHIVIATGSRPRVPPIPGLDEVRVLTS-----------DEAleleelpKSLVVIGGGYIGLEFA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 158 MDFCRAGKTVTLMDNAASLLaSLMPPEVSSRLQHHLTDMGVHLLLKSQLQKLEKTEAGIRATLVS---QHSIEVDAVIAA 234
Cdd:COG1249 185 QIFARLGSEVTLVERGDRLL-PGEDPEISEALEKALEKEGIDILTGAKVTSVEKTGDGVTVTLEDgggEEAVEADKVLVA 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 235 TGLRPETA---LARrAGVAVNR--GVCVDSYLQTSHPDIYAIGDCaeiNGqvlpflqPIQLS------AMYLAKNLLGGN 303
Cdd:COG1249 264 TGRRPNTDglgLEA-AGVELDErgGIKVDEYLRTSVPGIYAIGDV---TG-------GPQLAhvasaeGRVAAENILGKK 332
|
.
gi 900269912 304 A 304
Cdd:COG1249 333 P 333
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
2-275 |
1.50e-26 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 109.24 E-value: 1.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 2 SRGIIIIGSGFAARQLVKNIRKQDAHVPLTLIAadsmDEYNKPDLSHVISQSQRADDLTrQLAGEFAEQFNLRRFPH--- 78
Cdd:PRK09754 3 EKTIIIVGGGQAAAMAAASLRQQGFTGELHLFS----DERHLPYERPPLSKSMLLEDSP-QLQQVLPANWWQENNVHlhs 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 79 -TWVADIDADAH-VVKSQDKQWQYDKLVLATGATAFVPPIAGR--ELMLTLNSQQEYRACETQLRDAQRVLIVGGGLIGS 154
Cdd:PRK09754 78 gVTIKTLGRDTReLVLTNGESWHWDQLFIATGAAARPLPLLDAlgERCFTLRHAGDAARLREVLQPERSVVIVGAGTIGL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 155 ELAMDFCRAGKTVTLMDNAASLLASLMPPEVSSRLQHHLTDMGVHLLLKSQLQKLEKTEAgIRATLVSQHSIEVDAVIAA 234
Cdd:PRK09754 158 ELAASATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGEK-VELTLQSGETLQADVVIYG 236
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 900269912 235 TGLRPETALARRAGVAVNRGVCVDSYLQTSHPDIYAIGDCA 275
Cdd:PRK09754 237 IGISANDQLAREANLDTANGIVIDEACRTCDPAIFAGGDVA 277
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
86-274 |
5.81e-25 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 105.67 E-value: 5.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 86 ADAHVVKSQDKQWQYDKLVLATGATAFVPPIAG--------RELMLTLNSQQEyracetqlrdaqRVLIVGGGLIGSELA 157
Cdd:PRK06370 120 ESPNTVRVGGETLRAKRIFINTGARAAIPPIPGldevgyltNETIFSLDELPE------------HLVIIGGGYIGLEFA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 158 MDFCRAGKTVTLMDNAASLLASlMPPEVSSRLQHHLTDMGVHLLLKSQLQKLEKTEAGIRATLVS---QHSIEVDAVIAA 234
Cdd:PRK06370 188 QMFRRFGSEVTVIERGPRLLPR-EDEDVAAAVREILEREGIDVRLNAECIRVERDGDGIAVGLDCnggAPEITGSHILVA 266
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 900269912 235 TGLRPET---ALArRAGVAVNR--GVCVDSYLQTSHPDIYAIGDC 274
Cdd:PRK06370 267 VGRVPNTddlGLE-AAGVETDArgYIKVDDQLRTTNPGIYAAGDC 310
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
81-307 |
1.89e-24 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 103.97 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 81 VADIDADAH--VVKSQDKQWQ----YDKLVLATGATAFVPPIAGREL--MLTLNSQQEYRACETQLRDA--QRVLIVGGG 150
Cdd:PRK09564 79 VVKVDAKNKtiTVKNLKTGSIfndtYDKLMIATGARPIIPPIKNINLenVYTLKSMEDGLALKELLKDEeiKNIVIIGAG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 151 LIGSELAMDFCRAGKTVTLMDNAASLLASLMPPEVSSRLQHHLTDMGV--HLLLKSQLQKLEKTEAGIRAtlvSQHSIEV 228
Cdd:PRK09564 159 FIGLEAVEAAKHLGKNVRIIQLEDRILPDSFDKEITDVMEEELRENGVelHLNEFVKSLIGEDKVEGVVT---DKGEYEA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 229 DAVIAATGLRPETALARRAGV--AVNRGVCVDSYLQTSHPDIYAIGDCAEINGQVL--PFLQPIQLSAMYLAK----NLL 300
Cdd:PRK09564 236 DVVIVATGVKPNTEFLEDTGLktLKNGAIIVDEYGETSIENIYAAGDCATIYNIVSnkNVYVPLATTANKLGRmvgeNLA 315
|
....*..
gi 900269912 301 GGNAPLK 307
Cdd:PRK09564 316 GRHVSFK 322
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
87-308 |
1.08e-21 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 95.99 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 87 DAHVVKSQDKQWQYDKLVLATGATAFVPPIAGRELMLTLNsqqEYRACETQlrdAQRVLIVGGGLIGSELAMDFCRAGKT 166
Cdd:PRK06116 119 DAHTVEVNGERYTADHILIATGGRPSIPDIPGAEYGITSD---GFFALEEL---PKRVAVVGAGYIAVEFAGVLNGLGSE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 167 VTLMDNAASLLASLmPPEVSSRLQHHLTDMGVHLLLKSQLQKLEKTEAG-IRATLVSQHSIEVDAVIAATGLRPETA--- 242
Cdd:PRK06116 193 THLFVRGDAPLRGF-DPDIRETLVEEMEKKGIRLHTNAVPKAVEKNADGsLTLTLEDGETLTVDCLIWAIGREPNTDglg 271
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 243 LARrAGVAVN-RG-VCVDSYLQTSHPDIYAIGDCA-EINgqvlpfLQPIQLSA-MYLAKNLLGGNAPLKL 308
Cdd:PRK06116 272 LEN-AGVKLNeKGyIIVDEYQNTNVPGIYAVGDVTgRVE------LTPVAIAAgRRLSERLFNNKPDEKL 334
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
86-274 |
1.19e-21 |
|
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon for the detoxification of mercury compounds. MerA is a FAD-containing flavoprotein which reduces Hg(II) to Hg(0) utilizing NADPH. [Cellular processes, Detoxification]
Pssm-ID: 273944 [Multi-domain] Cd Length: 463 Bit Score: 95.95 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 86 ADAHVVKSQDKQ--WQYDKLVLATGATAFVPPIAG-RELMLTLNSQqeyrACETQlRDAQRVLIVGGGLIGSELAMDFCR 162
Cdd:TIGR02053 113 KDPKTVKVDLGRevRGAKRFLIATGARPAIPPIPGlKEAGYLTSEE----ALALD-RIPESLAVIGGGAIGVELAQAFAR 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 163 AGKTVTLMDNAASLLaSLMPPEVSSRLQHHLTDMGVHLLLKSQLQKLEKTEAGIRATL---VSQHSIEVDAVIAATGLRP 239
Cdd:TIGR02053 188 LGSEVTILQRSDRLL-PREEPEISAAVEEALAEEGIEVVTSAQVKAVSVRGGGKIITVekpGGQGEVEADELLVATGRRP 266
|
170 180 190
....*....|....*....|....*....|....*....
gi 900269912 240 ETALA--RRAGVAVNR--GVCVDSYLQTSHPDIYAIGDC 274
Cdd:TIGR02053 267 NTDGLglEKAGVKLDErgGILVDETLRTSNPGIYAAGDV 305
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
103-273 |
4.75e-19 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 88.28 E-value: 4.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 103 LVLATGATAFVPP---IAGRELM-----LTLNsqqeyracetqlRDAQRVLIVGGGLIGSELAmDFCRA-GKTVTLMDna 173
Cdd:PRK06416 138 IILATGSRPRELPgieIDGRVIWtsdeaLNLD------------EVPKSLVVIGGGYIGVEFA-SAYASlGAEVTIVE-- 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 174 asLLASLMP---PEVSSRLQHHLTDMGVHLLLKSQLQKLEKTEAGIRATLVSQ---HSIEVDAVIAATGLRPETA---LA 244
Cdd:PRK06416 203 --ALPRILPgedKEISKLAERALKKRGIKIKTGAKAKKVEQTDDGVTVTLEDGgkeETLEADYVLVAVGRRPNTEnlgLE 280
|
170 180 190
....*....|....*....|....*....|
gi 900269912 245 RrAGVAVNRG-VCVDSYLQTSHPDIYAIGD 273
Cdd:PRK06416 281 E-LGVKTDRGfIEVDEQLRTNVPNIYAIGD 309
|
|
| Rbx_binding |
pfam18113 |
Rubredoxin binding C-terminal domain; This is the C-terminal domain found in rubredoxin ... |
305-375 |
1.60e-18 |
|
Rubredoxin binding C-terminal domain; This is the C-terminal domain found in rubredoxin reductase (RdxR) present in Pseudomonas aeruginosa. RdxR are important in prokaryotes as they allow for the metabolism of inert n-alkanes and RdxR is also crucial for archaea and anaerobic bacteria in the response to oxidative stress. This domain is known to recognize and bind to rubredoxin.
Pssm-ID: 436282 Cd Length: 71 Bit Score: 78.82 E-value: 1.60e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 900269912 305 PLKLPAMLVKVKTPELPLHLAGETQRRDLSWHITAESDGMIAKGMSGEGQLRAFVVSEDRMKEAFALLKTL 375
Cdd:pfam18113 1 AVVYPAMPVIVKTPACPLVVAPPAVGAEGEWQIEGDGEGLTARFYDADGQLLGFALTGEAVAQRMALLKQL 71
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
87-285 |
6.43e-18 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 84.84 E-value: 6.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 87 DAHVVKSQDKQWQYDKLVLATGATafVPPIAGRELMLtlnsqqeyracETQL---RDA-------QRVLIVGGGLIGSEL 156
Cdd:PRK06292 118 DPNTVEVNGERIEAKNIVIATGSR--VPPIPGVWLIL-----------GDRLltsDDAfeldklpKSLAVIGGGVIGLEL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 157 AMDFCRAGKTVTLMDNAASLLaSLMPPEVSSRLQHHL-------TDMGVHLLLKSQLQKLEKTEAGiratlVSQHSIEVD 229
Cdd:PRK06292 185 GQALSRLGVKVTVFERGDRIL-PLEDPEVSKQAQKILskefkikLGAKVTSVEKSGDEKVEELEKG-----GKTETIEAD 258
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 230 AVIAATGLRPETAL--ARRAGVAV-NRG-VCVDSYLQTSHPDIYAIGDcaeINGQvLPFL 285
Cdd:PRK06292 259 YVLVATGRRPNTDGlgLENTGIELdERGrPVVDEHTQTSVPGIYAAGD---VNGK-PPLL 314
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
87-303 |
3.45e-17 |
|
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide.
Pssm-ID: 273568 [Multi-domain] Cd Length: 460 Bit Score: 82.69 E-value: 3.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 87 DAHVVKSQDKQW----QYDKLVLATGATAFVPPIA---GRELMLTLNSQQEYRacetqlRDAQRVLIVGGGLIGSELAMD 159
Cdd:TIGR01350 115 DPGTVSVTGENGeetlEAKNIIIATGSRPRSLPGPfdfDGKVVITSTGALNLE------EVPESLVIIGGGVIGIEFASI 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 160 FCRAGKTVTLMDNAASLLAsLMPPEVSSRLQHHLTDMGVHLLLKSQLQKLEKTEAGIRATLVSQH--SIEVDAVIAATGL 237
Cdd:TIGR01350 189 FASLGSKVTVIEMLDRILP-GEDAEVSKVLQKALKKKGVKILTNTKVTAVEKNDDQVTYENKGGEteTLTGEKVLVAVGR 267
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 900269912 238 RPETALARRAGVAV---NRG-VCVDSYLQTSHPDIYAIGDCAEingqvlpflqPIQLS------AMYLAKNLLGGN 303
Cdd:TIGR01350 268 KPNTEGLGLEKLGVeldERGrIVVDEYMRTNVPGIYAIGDVIG----------GPMLAhvasheGIVAAENIAGKE 333
|
|
| Nterm_to_SelD |
TIGR03169 |
pyridine nucleotide-disulfide oxidoreductase family protein; Members of this protein family ... |
58-275 |
4.39e-17 |
|
pyridine nucleotide-disulfide oxidoreductase family protein; Members of this protein family include N-terminal sequence regions of (probable) bifunctional proteins whose C-terminal sequences are SelD, or selenide,water dikinase, the selenium donor protein necessary for selenium incorporation into protein (as selenocysteine), tRNA (as 2-selenouridine), or both. However, some members of this family occur in species that do not show selenium incorporation, and the function of this protein family is unknown.
Pssm-ID: 274465 Cd Length: 364 Bit Score: 81.48 E-value: 4.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 58 DLtRQLAgefaeQFNLRRFPHTWVADIDADAHVVKSQDK-QWQYDKLVLATGATAFVPPIAG--------RELMLTLNSQ 128
Cdd:TIGR03169 59 DL-VRLA-----RFAGARLILDRAIGLDLAAKQVICAGRpPIAYDVLSIDIGSTPALPDVPGfaehaipaKPLGQFAQRW 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 129 QEYRAcETQLRDAQRVLIVGGGLIGSELAMD----FCRAGKT--VTLMDNAASLLASlMPPEVSSRLQHHLTDMGVHLLL 202
Cdd:TIGR03169 133 QRFLE-RAKPQQPPRIAVIGGGAAGVELALAmahrLRQLGRNaeVTLIDRGNVLLPG-HNARVRRRLERALQERGVTLHL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 203 KSQLQklEKTEAGIRatLVSQHSIEVDAVIAATGLRP-----ETALARRAgvavnRG-VCVDSYLQT-SHPDIYAIGDCA 275
Cdd:TIGR03169 211 GATVA--EVTADAVR--LEDGQTLPADFTFWATGARPpgwlaESGLALDE-----DGfIRVGPTLQSlSHPDIFAAGDCA 281
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
84-279 |
6.78e-14 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 72.47 E-value: 6.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 84 IDADAH--------VVKSQDKQ-WQYDKLVLATGATAFVPPIAGrelmlTLNSQQEYRACETQLRDA--QRVLIVGGGLI 152
Cdd:PRK07251 94 YDAEAHfvsnkvieVQAGDEKIeLTAETIVINTGAVSNVLPIPG-----LADSKHVYDSTGIQSLETlpERLGIIGGGNI 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 153 GSELAMDFCRAGKTVTLMDNAASLLASlMPPEVSSRLQHHLTDMGVHLLLKSQLQKLeKTEAGIRATLVSQHSIEVDAVI 232
Cdd:PRK07251 169 GLEFAGLYNKLGSKVTVLDAASTILPR-EEPSVAALAKQYMEEDGITFLLNAHTTEV-KNDGDQVLVVTEDETYRFDALL 246
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 900269912 233 AATGLRPETA---LARRAGVAVNRG-VCVDSYLQTSHPDIYAIGDcaeING 279
Cdd:PRK07251 247 YATGRKPNTEplgLENTDIELTERGaIKVDDYCQTSVPGVFAVGD---VNG 294
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
5-276 |
7.06e-14 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 72.51 E-value: 7.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 5 IIIIGSGFAARQLVKNIRKQDAHVPLTLIAADSMDEYNKPDLSHVISQ--SQRaDDLTRQLAGEFAEQFNLRRFPHTWVA 82
Cdd:PRK13512 4 IIVVGAVAGGATCASQIRRLDKESDIIIFEKDRDMSFANCALPYYIGEvvEDR-KYALAYTPEKFYDRKQITVKTYHEVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 83 DIDADAHVVKSQDKQWQ------YDKLVLATGATAFVPPIAGrELMLTLNSQQEYRACETQLR--DAQRVLIVGGGLIGS 154
Cdd:PRK13512 83 AINDERQTVTVLNRKTNeqfeesYDKLILSPGASANSLGFES-DITFTLRNLEDTDAIDQFIKanQVDKALVVGAGYISL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 155 ELAMDFCRAGKTVTLMDNAASLLaSLMPPEVSSRLQHHLTDMGVHLLLKSQLQKLEKTEAgiraTLVSQHSIEVDAVIAA 234
Cdd:PRK13512 162 EVLENLYERGLHPTLIHRSDKIN-KLMDADMNQPILDELDKREIPYRLNEEIDAINGNEV----TFKSGKVEHYDMIIEG 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 900269912 235 TGLRPETALARRAGVAVNRG--VCVDSYLQTSHPDIYAIGDCAE 276
Cdd:PRK13512 237 VGTHPNSKFIESSNIKLDDKgfIPVNDKFETNVPNIYAIGDIIT 280
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
100-311 |
1.42e-13 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 71.72 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 100 YDKLVLATGATAFVPPIAGrelmltLNSQQEYRACETQLRDA--QRVLIVGGGLIGSELAMDFCRAGKTVTLMdnAASLL 177
Cdd:PRK13748 233 FDRCLIATGASPAVPPIPG------LKETPYWTSTEALVSDTipERLAVIGSSVVALELAQAFARLGSKVTIL--ARSTL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 178 ASLMPPEVSSRLQHHLTDMGVhlllksqlQKLEKTEAGIRA------TLVSQH-SIEVDAVIAATGLRPETA-LA-RRAG 248
Cdd:PRK13748 305 FFREDPAIGEAVTAAFRAEGI--------EVLEHTQASQVAhvdgefVLTTGHgELRADKLLVATGRAPNTRsLAlDAAG 376
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 900269912 249 VAVNRG--VCVDSYLQTSHPDIYAIGDCAEingqvlpflQPiQLsaMYLAK--------NLLGGNAPLKLPAM 311
Cdd:PRK13748 377 VTVNAQgaIVIDQGMRTSVPHIYAAGDCTD---------QP-QF--VYVAAaagtraaiNMTGGDAALDLTAM 437
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
101-273 |
2.55e-13 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 70.75 E-value: 2.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 101 DKLVLATGATAFVPPIAGrelmltlNSQQEYRACETQLRDAQ---RVLIVGGGLIGSELAMDFCRAGKTVTLMDNAASLL 177
Cdd:PRK07846 130 DQVVIAAGSRPVIPPVIA-------DSGVRYHTSDTIMRLPElpeSLVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRLL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 178 ASLmPPEVSSRlqhhLTDMG---VHLLLKSQLQKLEKTEAGIRATLVSQHSIEVDAVIAATGLRPETAL--ARRAGVAVN 252
Cdd:PRK07846 203 RHL-DDDISER----FTELAskrWDVRLGRNVVGVSQDGSGVTLRLDDGSTVEADVLLVATGRVPNGDLldAAAAGVDVD 277
|
170 180
....*....|....*....|...
gi 900269912 253 RG--VCVDSYLQTSHPDIYAIGD 273
Cdd:PRK07846 278 EDgrVVVDEYQRTSAEGVFALGD 300
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
10-273 |
2.68e-13 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 70.96 E-value: 2.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 10 SGFAARQLVKNIRkqdahVPLTLIAADSMDEynkpdLSHVISQsQRaDDLTRQLAGEFAEQFNLR-RF--PHT-WVADID 85
Cdd:PRK05249 63 IGFNQNPLYSSYR-----VKLRITFADLLAR-----ADHVINK-QV-EVRRGQYERNRVDLIQGRaRFvdPHTvEVECPD 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 86 ADAHVVKSqdkqwqyDKLVLATGATAFVP---PIAGREL-----MLTLNsqqeyracetqlRDAQRVLIVGGGLIGSELA 157
Cdd:PRK05249 131 GEVETLTA-------DKIVIATGSRPYRPpdvDFDHPRIydsdsILSLD------------HLPRSLIIYGAGVIGCEYA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 158 MDFCRAGKTVTLMDNAASLLaSLMPPEVSSRLQHHLTDMGVHLLLKSQLQKLEKTEAGIRATLVSQHSIEVDAVIAATGL 237
Cdd:PRK05249 192 SIFAALGVKVTLINTRDRLL-SFLDDEISDALSYHLRDSGVTIRHNEEVEKVEGGDDGVIVHLKSGKKIKADCLLYANGR 270
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 900269912 238 RPETA---LArRAGVAVN-RG-VCVDSYLQTSHPDIYAIGD 273
Cdd:PRK05249 271 TGNTDglnLE-NAGLEADsRGqLKVNENYQTAVPHIYAVGD 310
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
102-304 |
3.91e-13 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 70.61 E-value: 3.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 102 KLVLATGATAFVPPIAGRELMLTLN---SQQEYracetqlrdAQRVLIVGGGLIGSELAMDFCRAGKTVTLMDNAASLLA 178
Cdd:PLN02507 170 HILIATGSRAQRPNIPGKELAITSDealSLEEL---------PKRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELPLR 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 179 SLmPPEVSSRLQHHLTDMGVHLLLKSQLQKLEKTEAGIRATLVSQHSIEVDAVIAATGLRPETALA--RRAGVAVNR--G 254
Cdd:PLN02507 241 GF-DDEMRAVVARNLEGRGINLHPRTNLTQLTKTEGGIKVITDHGEEFVADVVLFATGRAPNTKRLnlEAVGVELDKagA 319
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 900269912 255 VCVDSYLQTSHPDIYAIGDCA-EINgqvlpfLQPIQL-SAMYLAKNLLGGNA 304
Cdd:PLN02507 320 VKVDEYSRTNIPSIWAIGDVTnRIN------LTPVALmEGTCFAKTVFGGQP 365
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
41-275 |
4.08e-13 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 69.38 E-value: 4.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 41 YNKPDLSHVISQSQRADDLTRQlagefAEQFNLRrFPHTWVADIDADA---HVVKSQDKQWQYDKLVLATGATAFVPPIA 117
Cdd:COG0492 45 ENYPGFPEGISGPELAERLREQ-----AERFGAE-ILLEEVTSVDKDDgpfRVTTDDGTEYEAKAVIIATGAGPRKLGLP 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 118 GRElmltlnsqqEYR-----ACET----QLRDaQRVLIVGGGLIGSELAMDFCRAGKTVTLMDNAASLLASlmpPEVSSR 188
Cdd:COG0492 119 GEE---------EFEgrgvsYCATcdgfFFRG-KDVVVVGGGDSALEEALYLTKFASKVTLIHRRDELRAS---KILVER 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 189 LQHHlTDMGVHLLLKSQLQKLEKTEAGIRATLV---SQHSIEVDAVIAATGLRPETALARRAGVAVNRG--VCVDSYLQT 263
Cdd:COG0492 186 LRAN-PKIEVLWNTEVTEIEGDGRVEGVTLKNVktgEEKELEVDGVFVAIGLKPNTELLKGLGLELDEDgyIVVDEDMET 264
|
250
....*....|..
gi 900269912 264 SHPDIYAIGDCA 275
Cdd:COG0492 265 SVPGVFAAGDVR 276
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
101-273 |
1.59e-12 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 68.50 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 101 DKLVLATGATAFVPPIAGrelMLTLNSQQEYRACETQLRDAQRVLIVGGGLIGSELAMDFCRAGKTVTLMDnAASLLASL 180
Cdd:PRK08010 121 EKIFINTGAQTVVPPIPG---ITTTPGVYDSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILE-AASLFLPR 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 181 MPPEVSSRLQHHLTDMGVHLLLKSQLQKLEKTEAGIRA-TLVSQHSieVDAVIAATGLRPETA--LARRAGVAVNR--GV 255
Cdd:PRK08010 197 EDRDIADNIATILRDQGVDIILNAHVERISHHENQVQVhSEHAQLA--VDALLIASGRQPATAslHPENAGIAVNErgAI 274
|
170
....*....|....*...
gi 900269912 256 CVDSYLQTSHPDIYAIGD 273
Cdd:PRK08010 275 VVDKYLHTTADNIWAMGD 292
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
143-198 |
4.22e-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: 58.37 E-value: 4.22e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 900269912 143 RVLIVGGGLIGSELAMDFCRAGKTVTLMDNAASLLAsLMPPEVSSRLQHHLTDMGV 198
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLP-GFDPEIAKILQEKLEKNGI 55
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
99-307 |
2.88e-10 |
|
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of spermidine, is (in its reduced form) an important antioxidant found in trypanosomatids (Crithidia, Leishmania, Trypanosoma). This model describes trypanothione reductase, a possible antitrypanosomal drug target closely related to some forms of glutathione reductase.
Pssm-ID: 200098 [Multi-domain] Cd Length: 486 Bit Score: 61.53 E-value: 2.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 99 QYDKLVLATGATAFVPPIAGRELMLTlnSQQEYRACETqlrdAQRVLIVGGGLIGSELAMDF----CRAGKtVTLMDNAA 174
Cdd:TIGR01423 151 QAEHILLATGSWPQMLGIPGIEHCIS--SNEAFYLDEP----PRRVLTVGGGFISVEFAGIFnaykPRGGK-VTLCYRNN 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 175 SLLASLmPPEVSSRLQHHLTDMGVHLLLKSQLQKLEKTEAGIR-ATLVSQHSIEVDAVIAATGLRPETALAR--RAGVAV 251
Cdd:TIGR01423 224 MILRGF-DSTLRKELTKQLRANGINIMTNENPAKVTLNADGSKhVTFESGKTLDVDVVMMAIGRVPRTQTLQldKVGVEL 302
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 900269912 252 --NRGVCVDSYLQTSHPDIYAIGDcaeINGQVLpfLQPIQLSAMYLAKNLLGGNAPLK 307
Cdd:TIGR01423 303 tkKGAIQVDEFSRTNVPNIYAIGD---VTDRVM--LTPVAINEGAAFVDTVFGNKPRK 355
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
142-275 |
7.39e-10 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 60.32 E-value: 7.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 142 QRVLIVGGGLIGSELAMDFCRAGKTVTLMDNAASLLASlMPPEVSSRLQHHLTDMGVHLLLKSQLQKLEKTEAGIRATLV 221
Cdd:PRK06327 184 KKLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFLAA-ADEQVAKEAAKAFTKQGLDIHLGVKIGEIKTGGKGVSVAYT 262
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 900269912 222 ----SQHSIEVDAVIAATGLRPETA--LARRAGVAVN-RG-VCVDSYLQTSHPDIYAIGDCA 275
Cdd:PRK06327 263 dadgEAQTLEVDKLIVSIGRVPNTDglGLEAVGLKLDeRGfIPVDDHCRTNVPNVYAIGDVV 324
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
99-282 |
4.33e-09 |
|
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis
Pssm-ID: 440259 [Multi-domain] Cd Length: 434 Bit Score: 57.84 E-value: 4.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 99 QYDKLVLATGAT-AFVPPIAGREL--------MLTlnSQQEYRACETQLRDAQRVLIVGGGLIgselAMDfC-----RAG 164
Cdd:COG0493 206 EFDAVFLATGAGkPRDLGIPGEDLkgvhsamdFLT--AVNLGEAPDTILAVGKRVVVIGGGNT----AMD-CartalRLG 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 165 -KTVTLM------DNAASLL----A---------SLMPPEVSSRLQHHLTdmGVHLllksqlqklEKTEAGI-----RAT 219
Cdd:COG0493 279 aESVTIVyrrtreEMPASKEeveeAleegveflfLVAPVEIIGDENGRVT--GLEC---------VRMELGEpdesgRRR 347
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 900269912 220 LV----SQHSIEVDAVIAATGLRPETALARRA-GVAVNRGVCV---DSYLQTSHPDIYAIGDCaeINGQVL 282
Cdd:COG0493 348 PVpiegSEFTLPADLVILAIGQTPDPSGLEEElGLELDKRGTIvvdEETYQTSLPGVFAGGDA--VRGPSL 416
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
85-274 |
7.13e-08 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 54.24 E-value: 7.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 85 DADAHVVKSQDKQWQYDK------LVLATGATAFVPPIAGRELmlTLNSQQEYracetQLRDAQRVLIVGGGLIGSELAM 158
Cdd:PTZ00058 182 DDEVTIVSAGVSQLDDGQviegknILIAVGNKPIFPDVKGKEF--TISSDDFF-----KIKEAKRIGIAGSGYIAVELIN 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 159 DFCRAGKTVTLMDNAASLLASLmPPEVSSRLQHHLTDMGVHLLLKSQLQKLEKTEAGIRATLVSQHSIEV--DAVIAATG 236
Cdd:PTZ00058 255 VVNRLGAESYIFARGNRLLRKF-DETIINELENDMKKNNINIITHANVEEIEKVKEKNLTIYLSDGRKYEhfDYVIYCVG 333
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 900269912 237 LRPET-ALARRA-GVAVNRG-VCVDSYLQTSHPDIYAIGDC 274
Cdd:PTZ00058 334 RSPNTeDLNLKAlNIKTPKGyIKVDDNQRTSVKHIYAVGDC 374
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
101-308 |
6.68e-07 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 51.01 E-value: 6.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 101 DKLVLATGATAFVPPIA---GrELMLTLnsqqeyraceTQLRDAQRV---LIV-GGGLIGSELAMDFCRAGKTVTLmdna 173
Cdd:PRK07845 141 DVVLIATGASPRILPTAepdG-ERILTW----------RQLYDLDELpehLIVvGSGVTGAEFASAYTELGVKVTL---- 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 174 asllaslmppeVSSR--------------LQHHLTDMGVHLLLKSQLQKLEKTEAGIRATLVSQHSIEVDAVIAATGLRP 239
Cdd:PRK07845 206 -----------VSSRdrvlpgedadaaevLEEVFARRGMTVLKRSRAESVERTGDGVVVTLTDGRTVEGSHALMAVGSVP 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 240 ETA---LARrAGVAVNRG--VCVDSYLQTSHPDIYAIGDC---------AEINGQVlpflqpiqlsAMYLAknlLG-GNA 304
Cdd:PRK07845 275 NTAglgLEE-AGVELTPSghITVDRVSRTSVPGIYAAGDCtgvlplasvAAMQGRI----------AMYHA---LGeAVS 340
|
....
gi 900269912 305 PLKL 308
Cdd:PRK07845 341 PLRL 344
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
87-307 |
1.75e-06 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 49.87 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 87 DAHVVKSQDKQWQYDKLVLATGATAFVPPIAGRELM------LTLNSQQEyracetqlrdaqRVLIVGGGLIGSELAMDF 160
Cdd:PLN02546 204 DPHTVDVDGKLYTARNILIAVGGRPFIPDIPGIEHAidsdaaLDLPSKPE------------KIAIVGGGYIALEFAGIF 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 161 CRAGKTVTLMDNAASLLASLmPPEVSSRLQHHLTDMGVHLLLKSQLQKLEKTEAGIRATLVSQHSIE-VDAVIAATGLRP 239
Cdd:PLN02546 272 NGLKSDVHVFIRQKKVLRGF-DEEVRDFVAEQMSLRGIEFHTEESPQAIIKSADGSLSLKTNKGTVEgFSHVMFATGRKP 350
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 900269912 240 ETALARRAGVAV----NRGVCVDSYLQTSHPDIYAIGDCAE-INgqvlpfLQPIQL-SAMYLAKNLLgGNAPLK 307
Cdd:PLN02546 351 NTKNLGLEEVGVkmdkNGAIEVDEYSRTSVPSIWAVGDVTDrIN------LTPVALmEGGALAKTLF-GNEPTK 417
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
87-303 |
3.02e-06 |
|
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member of the pyridine nucleotide disulfide oxidoreductase family contains a C-terminal motif Cys-SeCys-Gly, where SeCys is selenocysteine encoded by TGA (in some sequence reports interpreted as a stop codon). In some members of this subfamily, Cys-SeCys-Gly is replaced by Cys-Cys-Gly. The reach of the selenium atom at the C-term arm of the protein is proposed to allow broad substrate specificity.
Pssm-ID: 273624 [Multi-domain] Cd Length: 484 Bit Score: 49.08 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 87 DAHVVKSQDKQ-----WQYDKLVLATGATAFVPPIAG-RELMLTLNSQQEYRACetqlrdAQRVLIVGGGLIGSELAMDF 160
Cdd:TIGR01438 126 DKHRIKATNKKgkekiYSAERFLIATGERPRYPGIPGaKELCITSDDLFSLPYC------PGKTLVVGASYVALECAGFL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 161 CRAGKTVTLMdnAASLLASLMPPEVSSRLQHHLTDMGVHLLLKSQLQKLEKTEAGIRATLVSQHSI---EVDAVIAATGL 237
Cdd:TIGR01438 200 AGIGLDVTVM--VRSILLRGFDQDCANKVGEHMEEHGVKFKRQFVPIKVEQIEAKVLVEFTDSTNGieeEYDTVLLAIGR 277
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 900269912 238 RPETALA--RRAGVAVNRG---VCVDSYLQTSHPDIYAIGDCAEINGQVLPFlqPIQlSAMYLAKNLLGGN 303
Cdd:TIGR01438 278 DACTRKLnlENVGVKINKKtgkIPADEEEQTNVPYIYAVGDILEDKPELTPV--AIQ-AGRLLAQRLFKGS 345
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
66-169 |
3.19e-06 |
|
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];
Pssm-ID: 441675 [Multi-domain] Cd Length: 414 Bit Score: 48.71 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 66 EFAEQFNLR---RFPH--TWVADIDADA--HVVKSQDKQWQYDKLVLATGA--TAFVPPIAGRE-----LMLTlnsqQEY 131
Cdd:COG2072 88 AYADKFGLRrpiRFGTevTSARWDEADGrwTVTTDDGETLTARFVVVATGPlsRPKIPDIPGLEdfageQLHS----ADW 163
|
90 100 110
....*....|....*....|....*....|....*...
gi 900269912 132 RACEtQLRDaQRVLIVGGGLIGSELAMDFCRAGKTVTL 169
Cdd:COG2072 164 RNPV-DLAG-KRVLVVGTGASAVQIAPELARVAAHVTV 199
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
99-274 |
2.84e-05 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 45.93 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 99 QYDKLVLATGATafVP---PIAGREL------M--LTLNSQQEYRACETQLRDA--QRVLIVGGGligsELAMDfC---- 161
Cdd:PRK12810 228 EYDAVFLGTGAY--KPrdlGIPGRDLdgvhfaMdfLIQNTRRVLGDETEPFISAkgKHVVVIGGG----DTGMD-Cvgta 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 162 -RAG-KTVTLMDNAAsllaslMPP----------------EVSS------RLQHHLTDM----------GVHLLLKSQLQ 207
Cdd:PRK12810 301 iRQGaKSVTQRDIMP------MPPsrrnknnpwpywpmklEVSNaheegvEREFNVQTKefegengkvtGVKVVRTELGE 374
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 900269912 208 KLEKTEAGiratlvSQHSIEVDAVIAATGLR-PETALARRAGVAVN-RG--VCVDSYLQTSHPDIYAIGDC 274
Cdd:PRK12810 375 GDFEPVEG------SEFVLPADLVLLAMGFTgPEAGLLAQFGVELDeRGrvAAPDNAYQTSNPKVFAAGDM 439
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
99-307 |
6.96e-05 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 44.76 E-value: 6.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 99 QYDKLVLATGA---TAFVPPIAGRELMLT-LNSQQEYRA----C-------ETQLRDAQRVL---IVGGGLIGSELAM-- 158
Cdd:PTZ00318 113 PYDKLVVAHGArpnTFNIPGVEERAFFLKeVNHARGIRKrivqCieraslpTTSVEERKRLLhfvVVGGGPTGVEFAAel 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 159 -DFCRagktvtlmDNAASLlaslmPPEVSSRLQHHLTDMGVHLLLKSQLQKLEKTEAGIRATLV----SQHSIEV--DAV 231
Cdd:PTZ00318 193 aDFFR--------DDVRNL-----NPELVEECKVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVdirtKTAVKEVldKEV 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 232 IAATGLRPETAL-ARRAGVA------------VNRG-VCVDSYLQTSH-PDIYAIGDCAEINGQVLPFL-QPIQLSAMYL 295
Cdd:PTZ00318 260 VLKDGEVIPTGLvVWSTGVGpgpltkqlkvdkTSRGrISVDDHLRVKPiPNVFALGDCAANEERPLPTLaQVASQQGVYL 339
|
250
....*....|....*
gi 900269912 296 AK---NLLGGNAPLK 307
Cdd:PTZ00318 340 AKefnNELKGKPMSK 354
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
68-272 |
1.26e-04 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 43.37 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 68 AEQFNLRRFPHTWVADIDADAH--VVKSQDKQWQYDKLVLATG-----ATAFVPPIAgrelmlTLNSQqeYRACEtQLRD 140
Cdd:pfam13738 85 ADHFELPINLFEEVTSVKKEDDgfVVTTSKGTYQARYVIIATGefdfpNKLGVPELP------KHYSY--VKDFH-PYAG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 141 aQRVLIVGGGLIGSELAMDFCRAGKTVTLMDNAASLLASLMPPEVS------SRLQHHLTDMGVHLLLKSQLQKLEKTEA 214
Cdd:pfam13738 156 -QKVVVIGGYNSAVDAALELVRKGARVTVLYRGSEWEDRDSDPSYSlspdtlNRLEELVKNGKIKAHFNAEVKEITEVDV 234
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 900269912 215 GIRATLVSQHSIEV-DAVIAATGLRPETALARRAGVAVNRG---VCVDSYLQTSHPDIYAIG 272
Cdd:pfam13738 235 SYKVHTEDGRKVTSnDDPILATGYHPDLSFLKKGLFELDEDgrpVLTEETESTNVPGLFLAG 296
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
97-274 |
9.38e-04 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 41.25 E-value: 9.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 97 QWQYDKLVLATGAT-AFVPPIAGRELMLTLNSQQEYR--ACETQLRDAQRVLIVGGGLIGSELAMDFCRAG-KTVTLMDN 172
Cdd:PRK12814 276 QKEFDAVLLAVGAQkASKMGIPGEELPGVISGIDFLRnvALGTALHPGKKVVVIGGGNTAIDAARTALRLGaESVTILYR 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 173 AASllaSLMP---PEVSSRLQHhltdmGVHLLLKSQLQKLEKTEAGIRATLV--------------------SQHSIEVD 229
Cdd:PRK12814 356 RTR---EEMPanrAEIEEALAE-----GVSLRELAAPVSIERSEGGLELTAIkmqqgepdesgrrrpvpvegSEFTLQAD 427
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 900269912 230 AVIAATGLRPETALARRAGVAVNRG--VCVDS-YLQTSHPDIYAIGDC 274
Cdd:PRK12814 428 TVISAIGQQVDPPIAEAAGIGTSRNgtVKVDPeTLQTSVAGVFAGGDC 475
|
|
| ThiF |
pfam00899 |
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ... |
137-172 |
1.22e-03 |
|
ThiF family; This domain is found in ubiquitin activating E1 family and members of the bacterial ThiF/MoeB/HesA family. It is repeated in Ubiquitin-activating enzyme E1.
Pssm-ID: 459987 [Multi-domain] Cd Length: 238 Bit Score: 39.93 E-value: 1.22e-03
10 20 30
....*....|....*....|....*....|....*..
gi 900269912 137 QLRDAqRVLIVGGGLIGSELAMDFCRAG-KTVTLMDN 172
Cdd:pfam00899 17 KLRNS-RVLIVGAGGLGSEAAKYLARAGvGKITLVDF 52
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
226-275 |
3.40e-03 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 39.39 E-value: 3.40e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 900269912 226 IEVDAVIAATGLRPET---------ALARRAGVAVnrgvcVDSYLQTSHPDIYAIGDCA 275
Cdd:PRK11749 374 LPADLVIKAIGQTPNPlilsttpglELNRWGTIIA-----DDETGRTSLPGVFAGGDIV 427
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
87-282 |
6.12e-03 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 38.74 E-value: 6.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 87 DAHVVKSQD--KQWQYDKLVLATGATAFVP---PIAGRELM-----LTLNSQQEYracetqlrdaqrVLIVGGGLIGSEL 156
Cdd:PTZ00153 260 DKNTIKSEKsgKEFKVKNIIIATGSTPNIPdniEVDQKSVFtsdtaVKLEGLQNY------------MGIVGMGIIGLEF 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 157 AMDFCRAGKTVTLMDNAASLLAsLMPPEVSS---RLQHHLTDMGVHLLLKSQLQKLEKTEA-----------------GI 216
Cdd:PTZ00153 328 MDIYTALGSEVVSFEYSPQLLP-LLDADVAKyfeRVFLKSKPVRVHLNTLIEYVRAGKGNQpviighserqtgesdgpKK 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 900269912 217 RATLVSQhsIEVDAVIAATGLRPETALA--RRAGVAVNRG-VCVDSYLQTSHPD------IYAIGDCaeiNGQVL 282
Cdd:PTZ00153 407 NMNDIKE--TYVDSCLVATGRKPNTNNLglDKLKIQMKRGfVSVDEHLRVLREDqevydnIFCIGDA---NGKQM 476
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
87-303 |
8.51e-03 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 38.27 E-value: 8.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 87 DAHVVK----SQDKQWQYDKLVLATGATAFVPPIAGRELMLTLNSQQEYraceTQLRDAQRVLIVGGGLIGSELAMDFCR 162
Cdd:PTZ00052 128 DEHTVSygdnSQEETITAKYILIATGGRPSIPEDVPGAKEYSITSDDIF----SLSKDPGKTLIVGASYIGLETAGFLNE 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 900269912 163 AGKTVTLMdnAASLLASLMPPEVSSRLQHHLTDMGVHLLLKSQLQKLEKTEAGIRATLVSQHSIEVDAVIAATGLRPETA 242
Cdd:PTZ00052 204 LGFDVTVA--VRSIPLRGFDRQCSEKVVEYMKEQGTLFLEGVVPINIEKMDDKIKVLFSDGTTELFDTVLYATGRKPDIK 281
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 900269912 243 LAR--RAGVAVNR-GVCVDSYLQTSHPDIYAIGDCAEingqVLPFLQPIQLSA-MYLAKNLLGGN 303
Cdd:PTZ00052 282 GLNlnAIGVHVNKsNKIIAPNDCTNIPNIFAVGDVVE----GRPELTPVAIKAgILLARRLFKQS 342
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