|
Name |
Accession |
Description |
Interval |
E-value |
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
24-350 |
1.56e-81 |
|
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: 254.35 E-value: 1.56e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 24 DSNYEVILIDKKSEISYLECGTSLFIKGEVSNLEDLFYQNRMTLnseIKK---LFLETEVDKIDIQNKKISCvkKDGTRF 100
Cdd:COG0446 3 GPDAEITVIEKGPHHSYQPCGLPYYVGGGIKDPEDLLVRTPESF---ERKgidVRTGTEVTAIDPEAKTVTL--RDGETL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 101 SqeYDKVILATGSKQIMLDIPGNNLANIFSIKNFPNAKEIFKALDDSTIKKVGIIGAGYIGVEIAEAIRKRGKEVYLFDV 180
Cdd:COG0446 78 S--YDKLVLATGARPRPPPIPGLDLPGVFTLRTLDDADALREALKEFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVER 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 181 ADRVLSTyYDRSFSDKVEEILSKNGIHLCLSESPKKYLGRKKIeKIVTTSGTQYSMDMVVQAIGFLSNSPIGEK-ELLRD 259
Cdd:COG0446 156 APRLLGV-LDPEMAALLEEELREHGVELRLGETVVAIDGDDKV-AVTLTDGEEIPADLVVVAPGVRPNTELAKDaGLALG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 260 VSGAYLTNEYQQTNIKDIYAIGDCATTFFTSINRSSVDFSISNALRTAYIATQHINNQDFTPSGsQFTNGFSIFNYNFYA 339
Cdd:COG0446 234 ERGWIKVDETLQTSDPDVYAAGDCAEVPHPVTGKTVYIPLASAANKQGRVAAENILGGPAPFPG-LGTFISKVFDLCIAS 312
|
330
....*....|.
gi 2090489534 340 AGlnlkTARLL 350
Cdd:COG0446 313 TG----TGRLL 319
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
3-430 |
4.60e-69 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 226.08 E-value: 4.60e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 3 KIVIIGSNHSGLAAARFLNLSDSNYEVILIDKKSEISYLECGTSLFIKGEVSNledlfyQNRM---TLNSEIKK---LFL 76
Cdd:PRK09564 2 KIIIIGGTAAGMSAAAKAKRLNKELEITVYEKTDIVSFGACGLPYFVGGFFDD------PNTMiarTPEEFIKSgidVKT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 77 ETEVDKIDIQNKKIScVK--KDGTRFSQEYDKVILATGSKQIMLDIPGNNLANIFSIKNFPNAKEIFKALDDSTIKKVGI 154
Cdd:PRK09564 76 EHEVVKVDAKNKTIT-VKnlKTGSIFNDTYDKLMIATGARPIIPPIKNINLENVYTLKSMEDGLALKELLKDEEIKNIVI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 155 IGAGYIGVEIAEAIRKRGKEVYLFDVADRVLSTYYDRSFSDKVEEILSKNGIHLCLSESPKKYLGRKKIEKIVTTSGTqY 234
Cdd:PRK09564 155 IGAGFIGLEAVEAAKHLGKNVRIIQLEDRILPDSFDKEITDVMEEELRENGVELHLNEFVKSLIGEDKVEGVVTDKGE-Y 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 235 SMDMVVQAIGFLSNSPIGEKELLRDVS-GAYLTNEYQQTNIKDIYAIGDCATTFFTSINRSSVDFSISNALRTAYIATQH 313
Cdd:PRK09564 234 EADVVIVATGVKPNTEFLEDTGLKTLKnGAIIVDEYGETSIENIYAAGDCATIYNIVSNKNVYVPLATTANKLGRMVGEN 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 314 INNQDFTPSGSQFTNGFSIFNYNFYAAGLNLKTARLLSesIDY--IEIEDFIRPAFLRKNSRVKLRISFEKNTKRIVGVQ 391
Cdd:PRK09564 314 LAGRHVSFKGTLGSACIKVLDLEAARTGLTEEEAKKLG--IDYktVFIKDKNHTNYYPGQEDLYVKLIYEADTKVILGGQ 391
|
410 420 430
....*....|....*....|....*....|....*....
gi 2090489534 392 LCSQEDLSGLLSMFSLAIEEQITLDKLKMLDYLFHPSFS 430
Cdd:PRK09564 392 IIGKKGAVLRIDALAVAIYAKLTTQELGMMDFCYAPPFA 430
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
3-283 |
6.55e-61 |
|
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: 200.24 E-value: 6.55e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 3 KIVIIGSNHSGLAAARFLnlSDSNYEVILIDKKSEISYLECGTSLFIKGEVSNLEDLFYQNRM---------TLNSEIKK 73
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTL--AQLGGKVTLIEDEGTCPYGGCVLSKALLGAAEAPEIASLWADLykrkeevvkKLNNGIEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 74 LfLETEVDKIDIQNKKISCVK-KDGTRFSQEYDKVILATGSKQIMLDIPGNNLANIFSIKNFPNAKEIFKALDDstiKKV 152
Cdd:pfam07992 80 L-LGTEVVSIDPGAKKVVLEElVDGDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKLLP---KRV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 153 GIIGAGYIGVEIAEAIRKRGKEVYLFDVADRVLSTyYDRSFSDKVEEILSKNGIHLCLSESPKKYLGRKKIEKIVTTSGT 232
Cdd:pfam07992 156 VVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRA-FDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGVEVILKDGT 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2090489534 233 QYSMDMVVQAIGFLSNSPIGEKE-LLRDVSGAYLTNEYQQTNIKDIYAIGDC 283
Cdd:pfam07992 235 EIDADLVVVAIGRRPNTELLEAAgLELDERGGIVVDEYLRTSVPGIYAAGDC 286
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
1-342 |
1.20e-53 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 184.19 E-value: 1.20e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 1 MEKIVIIGSNHSGLAAARFLNLSDSNYEVILIDKKSEISYLECGTSLFIKGEVSnLEDL------FY-QNRMTLnseikk 73
Cdd:COG1251 1 KMRIVIIGAGMAGVRAAEELRKLDPDGEITVIGAEPHPPYNRPPLSKVLAGETD-EEDLllrpadFYeENGIDL------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 74 lFLETEVDKIDIQNKKISCvkKDGTRFSqeYDKVILATGSKQIMLDIPGNNLANIFSIKNFPNAKEIFKALDDStiKKVG 153
Cdd:COG1251 74 -RLGTRVTAIDRAARTVTL--ADGETLP--YDKLVLATGSRPRVPPIPGADLPGVFTLRTLDDADALRAALAPG--KRVV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 154 IIGAGYIGVEIAEAIRKRGKEVYLFDVADRVLSTYYDRSFSDKVEEILSKNGIHLCLSESPKKYLGRKKIEKIVTTSGTQ 233
Cdd:COG1251 147 VIGGGLIGLEAAAALRKRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTGVRLADGEE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 234 YSMDMVVQAIGFLSNSpigekELLRD----VSGAYLTNEYQQTNIKDIYAIGDCAtTFFTSINRSSVDFSISNALRTAYI 309
Cdd:COG1251 227 LPADLVVVAIGVRPNT-----ELARAaglaVDRGIVVDDYLRTSDPDIYAAGDCA-EHPGPVYGRRVLELVAPAYEQARV 300
|
330 340 350
....*....|....*....|....*....|...
gi 2090489534 310 ATQHINNQDFTPSGSQFTNGFSIFNYNFYAAGL 342
Cdd:COG1251 301 AAANLAGGPAAYEGSVPSTKLKVFGVDVASAGD 333
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
1-436 |
3.85e-41 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 151.86 E-value: 3.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 1 MEKIVIIGSNHSGLAAARFLNLSDSNYEVILIDKKSEISYLECGTSLFIKGEVSNLEDL-------FYQNRmtlNSEIKK 73
Cdd:PRK13512 1 MPKIIVVGAVAGGATCASQIRRLDKESDIIIFEKDRDMSFANCALPYYIGEVVEDRKYAlaytpekFYDRK---QITVKT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 74 LFletEVDKIDIQNKKISCV-KKDGTRFSQEYDKVILATGSKQIMLDIpgnNLANIFSIKNFPNAKEIFKALDDSTIKKV 152
Cdd:PRK13512 78 YH---EVIAINDERQTVTVLnRKTNEQFEESYDKLILSPGASANSLGF---ESDITFTLRNLEDTDAIDQFIKANQVDKA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 153 GIIGAGYIGVEIAEAIRKRGKEVYLFDVADRVLSTyYDRSFSDKVEEILSKNGIHLCLSESPKKYLGRkkiekIVT-TSG 231
Cdd:PRK13512 152 LVVGAGYISLEVLENLYERGLHPTLIHRSDKINKL-MDADMNQPILDELDKREIPYRLNEEIDAINGN-----EVTfKSG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 232 TQYSMDMVVQAIGFLSNSP-IGEKELLRDVSGAYLTNEYQQTNIKDIYAIGDCATTFFTSINRSSVDFSISNALRTAYIA 310
Cdd:PRK13512 226 KVEHYDMIIEGVGTHPNSKfIESSNIKLDDKGFIPVNDKFETNVPNIYAIGDIITSHYRHVDLPASVPLAWGAHRAASIV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 311 TQHI-NNQDFTPSGSQFTNGFSIFNYNFYAAGLNLKtaRLLSESIDYIEIEDFIRPAFLRKNSRVKLRISFEKNTKRIVG 389
Cdd:PRK13512 306 AEQIaGNDTIEFKGFLGNNIVKFFDYTFASVGVKPN--ELKQFDYKMVEVTQGAHANYYPGNSPLHLRVYYDTSNRKILR 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2090489534 390 VQLCSQEDLSGLLSMFSLAIEEQITLDKLKMLDYLFHPSFSQPYNFI 436
Cdd:PRK13512 384 AAAVGKEGADKRIDVLSMAMMNQLTVDELTEFEVAYAPPYSHPKDLI 430
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
1-284 |
4.63e-35 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 134.10 E-value: 4.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 1 MEKIVIIGSNHSGLAAARFL-NLSDSNYEVILIDKKSEISYL----ECGTSLFIKGEVS-NLEDLFYQNRMTlnseikkl 74
Cdd:COG1252 1 MKRIVIVGGGFAGLEAARRLrKKLGGDAEVTLIDPNPYHLFQpllpEVAAGTLSPDDIAiPLRELLRRAGVR-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 75 FLETEVDKIDIQNKKISCvkKDGTRFSqeYDKVILATGSKQIMLDIPGnnLA-NIFSIKNFPNAKEIFKALDDSTIK--- 150
Cdd:COG1252 73 FIQGEVTGIDPEARTVTL--ADGRTLS--YDYLVIATGSVTNFFGIPG--LAeHALPLKTLEDALALRERLLAAFERaer 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 151 ----KVGIIGAGYIGVE----IAEAIRKRGK---------EVYLFDVADRVLSTyYDRSFSDKVEEILSKNGIHLCLSES 213
Cdd:COG1252 147 rrllTIVVVGGGPTGVElageLAELLRKLLRypgidpdkvRITLVEAGPRILPG-LGEKLSEAAEKELEKRGVEVHTGTR 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2090489534 214 PKKYLGrkkiEKIVTTSGTQYSMDMVVQAIGFLSNSPIGEKELLRDVSGAYLTNEYQQT-NIKDIYAIGDCA 284
Cdd:COG1252 226 VTEVDA----DGVTLEDGEEIPADTVIWAAGVKAPPLLADLGLPTDRRGRVLVDPTLQVpGHPNVFAIGDCA 293
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
105-430 |
6.45e-27 |
|
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: 112.10 E-value: 6.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 105 DKVILATGSKQIMLDIPGNNLANI------FSIKNFPnakeifkalddstiKKVGIIGAGYIGVEIAEAIRKRGKEVYLF 178
Cdd:COG1249 132 DHIVIATGSRPRVPPIPGLDEVRVltsdeaLELEELP--------------KSLVVIGGGYIGLEFAQIFARLGSEVTLV 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 179 DVADRVLSTyYDRSFSDKVEEILSKNGIHLCLSESPKKyLGRKKIEKIVTTSG----TQYSMDMVVQAIGFLSNSP-IG- 252
Cdd:COG1249 198 ERGDRLLPG-EDPEISEALEKALEKEGIDILTGAKVTS-VEKTGDGVTVTLEDgggeEAVEADKVLVATGRRPNTDgLGl 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 253 EK---ELlrDVSGAYLTNEYQQTNIKDIYAIGDCATTF-FTSInrssvdfsisnALRTAYIATQHINNQDFTPsgsqftn 328
Cdd:COG1249 276 EAagvEL--DERGGIKVDEYLRTSVPGIYAIGDVTGGPqLAHV-----------ASAEGRVAAENILGKKPRP------- 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 329 gfsiFNYNFYAA-----------GLNLKTARllSESIDYIEIEdfirpAFLRKNSR----------VKLrIsFEKNTKRI 387
Cdd:COG1249 336 ----VDYRAIPSvvftdpeiasvGLTEEEAR--EAGIDVKVGK-----FPFAANGRalalgetegfVKL-I-ADAETGRI 402
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2090489534 388 VGVQLCSqEDLSGLLSMFSLAIEEQITLDKLkmLDYLF-HPSFS 430
Cdd:COG1249 403 LGAHIVG-PHAGELIHEAALAMEMGLTVEDL--ADTIHaHPTLS 443
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
4-284 |
1.91e-25 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 109.53 E-value: 1.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 4 IVIIGSnhsGLAAARF----LNLSDSNYEVILIDKKSEISYLECGTSLFIKGEVSnLEDLfyqnrmTLNSE-------IK 72
Cdd:TIGR02374 1 LVLVGN---GMAGHRCieevLKLNRHMFEITIFGEEPHPNYNRILLSSVLQGEAD-LDDI------TLNSKdwyekhgIT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 73 kLFLETEVDKIDIQNKKiscVKKDGTRfSQEYDKVILATGSKQIMLDIPGNNLANIFSIKNFPNAKEIFKALDDStiKKV 152
Cdd:TIGR02374 71 -LYTGETVIQIDTDQKQ---VITDAGR-TLSYDKLILATGSYPFILPIPGADKKGVYVFRTIEDLDAIMAMAQRF--KKA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 153 GIIGAGYIGVEIAEAIRKRGKEVYLFDVADRVLSTYYDRSFSDKVEEILSKNGIHLCLSESPKKYLGRKKIEKIVTTSGT 232
Cdd:TIGR02374 144 AVIGGGLLGLEAAVGLQNLGMDVSVIHHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLEKDTVEIVGATKADRIRFKDGS 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2090489534 233 QYSMDMVVQAIGFLSNSPIGEKELLrDVSGAYLTNEYQQTNIKDIYAIGDCA 284
Cdd:TIGR02374 224 SLEADLIVMAAGIRPNDELAVSAGI-KVNRGIIVNDSMQTSDPDIYAVGECA 274
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
74-284 |
6.72e-23 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 99.61 E-value: 6.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 74 LFLETEVDKIDIQNKkisCVKKDGTRFSqeYDKVILATGSKQIMLDIPGNNLA---NifSIKNFPNAKEifkALDDStiK 150
Cdd:PRK04965 75 LFPHTWVTDIDAEAQ---VVKSQGNQWQ--YDKLVLATGASAFVPPIPGRELMltlN--SQQEYRAAET---QLRDA--Q 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 151 KVGIIGAGYIGVEIAEAIRKRGKEVYLFDVADRVLSTYYDRSFSDKVEEILSKNGIHLCLsespKKYLGRkkIEK----- 225
Cdd:PRK04965 143 RVLVVGGGLIGTELAMDLCRAGKAVTLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLL----KSQLQG--LEKtdsgi 216
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 226 -IVTTSGTQYSMDMVVQAIGFLSNSPIGEKELLrDVSGAYLTNEYQQTNIKDIYAIGDCA 284
Cdd:PRK04965 217 rATLDSGRSIEVDAVIAAAGLRPNTALARRAGL-AVNRGIVVDSYLQTSAPDIYALGDCA 275
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
93-283 |
1.59e-19 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 90.60 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 93 VKKDGTRFSQeyDKVILATGSKQIMLDIPGNNLAnIFSiknfpnaKEIFkALDDsTIKKVGIIGAGYIGVEIAEAIRKRG 172
Cdd:PRK06116 123 VEVNGERYTA--DHILIATGGRPSIPDIPGAEYG-ITS-------DGFF-ALEE-LPKRVAVVGAGYIAVEFAGVLNGLG 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 173 KEVYLFDVADRVLSTYyDRSFSDKVEEILSKNGIHLCLSESPKKylgrkkIEK-------IVTTSGTQYSMDMVVQAIGF 245
Cdd:PRK06116 191 SETHLFVRGDAPLRGF-DPDIRETLVEEMEKKGIRLHTNAVPKA------VEKnadgsltLTLEDGETLTVDCLIWAIGR 263
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2090489534 246 --------LSNSPIgekELlrDVSGAYLTNEYQQTNIKDIYAIGDC 283
Cdd:PRK06116 264 epntdglgLENAGV---KL--NEKGYIIVDEYQNTNVPGIYAVGDV 304
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
93-283 |
6.84e-18 |
|
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: 85.39 E-value: 6.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 93 VKKDGTRFSQEYDKVILATGSKQIMLdipgnNLANIFSIKNFPNAKEIFkALDdSTIKKVGIIGAGYIGVEIAEAIRKRG 172
Cdd:TIGR01350 121 VTGENGEETLEAKNIIIATGSRPRSL-----PGPFDFDGKVVITSTGAL-NLE-EVPESLVIIGGGVIGIEFASIFASLG 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 173 KEVYLFDVADRVLStYYDRSFSDKVEEILSKNGIHLCLSESPKKYLGRKKiEKIVTTSGTQYSM---DMVVQAIGFLSNS 249
Cdd:TIGR01350 194 SKVTVIEMLDRILP-GEDAEVSKVLQKALKKKGVKILTNTKVTAVEKNDD-QVTYENKGGETETltgEKVLVAVGRKPNT 271
|
170 180 190
....*....|....*....|....*....|....*..
gi 2090489534 250 P-IGEKEL--LRDVSGAYLTNEYQQTNIKDIYAIGDC 283
Cdd:TIGR01350 272 EgLGLEKLgvELDERGRIVVDEYMRTNVPGIYAIGDV 308
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
3-285 |
7.99e-17 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 80.55 E-value: 7.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 3 KIVIIGSNHSGLAAArfLNLSDSNYEVILIDKKseisylECGTSLFIKGEVSNL---------EDLFyqNRMTlnSEIKK 73
Cdd:COG0492 2 DVVIIGAGPAGLTAA--IYAARAGLKTLVIEGG------EPGGQLATTKEIENYpgfpegisgPELA--ERLR--EQAER 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 74 L---FLETEVDKIDIQNKKISCVKKDGTRFsqEYDKVILATGSKQIMLDIPGNNLaniFSIKN-----------FPNake 139
Cdd:COG0492 70 FgaeILLEEVTSVDKDDGPFRVTTDDGTEY--EAKAVIIATGAGPRKLGLPGEEE---FEGRGvsycatcdgffFRG--- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 140 ifkalddstiKKVGIIGAGYIGVEIAEAIRKRGKEVYLFDVADRVLSTYYDrsfsdkVEEILSKNGIHLCLSESPKKYLG 219
Cdd:COG0492 142 ----------KDVVVVGGGDSALEEALYLTKFASKVTLIHRRDELRASKIL------VERLRANPKIEVLWNTEVTEIEG 205
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2090489534 220 RKKIEKIVTTSG-----TQYSMDMVVQAIGFLSNS-PIGEKELLRDVSGAYLTNEYQQTNIKDIYAIGDCAT 285
Cdd:COG0492 206 DGRVEGVTLKNVktgeeKELEVDGVFVAIGLKPNTeLLKGLGLELDEDGYIVVDEDMETSVPGVFAAGDVRD 277
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
151-231 |
1.52e-16 |
|
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: 74.16 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 151 KVGIIGAGYIGVEIAEAIRKRGKEVYLFDVADRVLStYYDRSFSDKVEEILSKNGIHLCLSESPKKYLGRKKIEKIVTTS 230
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLP-GFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVLTD 79
|
.
gi 2090489534 231 G 231
Cdd:pfam00070 80 G 80
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
107-283 |
2.91e-15 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 77.73 E-value: 2.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 107 VILATGSKQIMLDIPGnnLANIFSIKNFPNAKEIfkalddstiKKVGIIGAGYIGVEIAEAIRKRGKEVYLFDVADRVLS 186
Cdd:PTZ00058 206 ILIAVGNKPIFPDVKG--KEFTISSDDFFKIKEA---------KRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLLR 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 187 TyYDRSFSDKVEEILSKNGIHLCLSESPKKY--LGRKKIEKIVTTSGTQYSMDMVVQAIGFLSNSP-IGEKELLRDVSGA 263
Cdd:PTZ00058 275 K-FDETIINELENDMKKNNINIITHANVEEIekVKEKNLTIYLSDGRKYEHFDYVIYCVGRSPNTEdLNLKALNIKTPKG 353
|
170 180
....*....|....*....|.
gi 2090489534 264 Y-LTNEYQQTNIKDIYAIGDC 283
Cdd:PTZ00058 354 YiKVDDNQRTSVKHIYAVGDC 374
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
105-430 |
3.88e-15 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 77.14 E-value: 3.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 105 DKVILATGSKQIMldIPGNNLAN---------IFSIKNFPnakeifkalddstiKKVGIIGAGYIGVEIAEAIRKRGKEV 175
Cdd:PRK06292 132 KNIVIATGSRVPP--IPGVWLILgdrlltsddAFELDKLP--------------KSLAVIGGGVIGLELGQALSRLGVKV 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 176 YLFDVADRVLSTyYDRSFSDKVEEILSKNgIHLCLSESPKKYLGRKKIEKIVTTSG--TQY-SMDMVVQAIGFLSNSPIG 252
Cdd:PRK06292 196 TVFERGDRILPL-EDPEVSKQAQKILSKE-FKIKLGAKVTSVEKSGDEKVEELEKGgkTETiEADYVLVATGRRPNTDGL 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 253 --EK---ELlrDVSGAYLTNEYQQTNIKDIYAIGDCA--TTFFTSINRSSVdFSISNALRTA-----YIATQHINnqdFT 320
Cdd:PRK06292 274 glENtgiEL--DERGRPVVDEHTQTSVPGIYAAGDVNgkPPLLHEAADEGR-IAAENAAGDVaggvrYHPIPSVV---FT 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 321 -PSgsqftngfsifnynfyAAGLNLKTARLLSESIDYIEIEdfirpAFLRKNSRVK--------LRISFEKNTKRIVGVQ 391
Cdd:PRK06292 348 dPQ----------------IASVGLTEEELKAAGIDYVVGE-----VPFEAQGRARvmgkndgfVKVYADKKTGRLLGAH 406
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2090489534 392 LCSqEDLSGLLSMFSLAIEEQITL-DKLKMLDYlfHPSFS 430
Cdd:PRK06292 407 IIG-PDAEHLIHLLAWAMQQGLTVeDLLRMPFY--HPTLS 443
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
67-282 |
9.19e-15 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 76.01 E-value: 9.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 67 LNSEIKKLFLETEVDKIDIQNK-----KISCVKKDGTRFSQEYDKVILATGSKQIMLDIPGNNLA----NIFSIKNFPna 137
Cdd:PLN02507 126 LNGIYKRLLANAGVKLYEGEGKivgpnEVEVTQLDGTKLRYTAKHILIATGSRAQRPNIPGKELAitsdEALSLEELP-- 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 138 keifkalddstiKKVGIIGAGYIGVEIAEAIRKRGKEVYLFDVADRVLstyydRSFSDKVEEILSKN----GIHLclseS 213
Cdd:PLN02507 204 ------------KRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELPL-----RGFDDEMRAVVARNlegrGINL----H 262
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2090489534 214 PKKYLGR-KKIE---KIVTTSGTQYSMDMVVQAIGFLSNSPIGEKELL---RDVSGAYLTNEYQQTNIKDIYAIGD 282
Cdd:PLN02507 263 PRTNLTQlTKTEggiKVITDHGEEFVADVVLFATGRAPNTKRLNLEAVgveLDKAGAVKVDEYSRTNIPSIWAIGD 338
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
3-285 |
1.09e-14 |
|
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: 75.56 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 3 KIVIIGSNHSGLAAARFLNLSdsNYEVILIDKKSEI---------SY-LECGtslFIKGEVSNLEDL---FYQNrmtlns 69
Cdd:COG0493 123 KVAVVGSGPAGLAAAYQLARA--GHEVTVFEALDKPggllrygipEFrLPKD---VLDREIELIEALgveFRTN------ 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 70 eikklfleTEVDK-IDIQNKKiscvkkdgtrfsQEYDKVILATGS-KQIMLDIPGNNLANIFSIKNF--PNAKEIFKALD 145
Cdd:COG0493 192 --------VEVGKdITLDELL------------EEFDAVFLATGAgKPRDLGIPGEDLKGVHSAMDFltAVNLGEAPDTI 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 146 DSTIKKVGIIGAGYIGVEIA-EAIRKRGKEVYLFDVADRVLSTYYDRSFSDKVEEilsknGIHLCLSESPKKYLGRK--- 221
Cdd:COG0493 252 LAVGKRVVVIGGGNTAMDCArTALRLGAESVTIVYRRTREEMPASKEEVEEALEE-----GVEFLFLVAPVEIIGDEngr 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 222 -------KIE----------KIVTTSGTQYSM--DMVVQAIGFLSNSPI--GEKELLRDVSGAYLTNE-YQQTNIKDIYA 279
Cdd:COG0493 327 vtglecvRMElgepdesgrrRPVPIEGSEFTLpaDLVILAIGQTPDPSGleEELGLELDKRGTIVVDEeTYQTSLPGVFA 406
|
....*.
gi 2090489534 280 IGDCAT 285
Cdd:COG0493 407 GGDAVR 412
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
93-283 |
1.60e-14 |
|
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: 75.15 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 93 VKKDGTRFSQEYDKVILATGSKQIMLDIPGNNLANIFSiknfpnAKEIFKAldDSTIKKVGIIGAGYIGVEIAEAIRKRG 172
Cdd:TIGR02053 118 VKVDLGREVRGAKRFLIATGARPAIPPIPGLKEAGYLT------SEEALAL--DRIPESLAVIGGGAIGVELAQAFARLG 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 173 KEVYLFDVADRVLStYYDRSFSDKVEEILSKNGIHLCLS---ESPKKYLGRKKIEKIVTTSGTQYSMDMVVQAIGFLSNS 249
Cdd:TIGR02053 190 SEVTILQRSDRLLP-REEPEISAAVEEALAEEGIEVVTSaqvKAVSVRGGGKIITVEKPGGQGEVEADELLVATGRRPNT 268
|
170 180 190
....*....|....*....|....*....|....*..
gi 2090489534 250 -PIG-EKELLR-DVSGAYLTNEYQQTNIKDIYAIGDC 283
Cdd:TIGR02053 269 dGLGlEKAGVKlDERGGILVDETLRTSNPGIYAAGDV 305
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
103-283 |
1.12e-13 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 72.54 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 103 EYDKVILATGSKQIMLDIPGNN----LAN--IFSIKNFPnakeifkalddstiKKVGIIGAGYIGVEIAEAIRKRGKEVY 176
Cdd:PRK06370 133 RAKRIFINTGARAAIPPIPGLDevgyLTNetIFSLDELP--------------EHLVIIGGGYIGLEFAQMFRRFGSEVT 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 177 LFDVADRVLSTyYDRSFSDKVEEILSKNGIHLCLSESPKKY--LGRKKIEKIVTTSGTQY-SMDMVVQAIGFLSNSpige 253
Cdd:PRK06370 199 VIERGPRLLPR-EDEDVAAAVREILEREGIDVRLNAECIRVerDGDGIAVGLDCNGGAPEiTGSHILVAVGRVPNT---- 273
|
170 180 190
....*....|....*....|....*....|....*...
gi 2090489534 254 kELL--------RDVSGAYLTNEYQQTNIKDIYAIGDC 283
Cdd:PRK06370 274 -DDLgleaagveTDARGYIKVDDQLRTTNPGIYAAGDC 310
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
105-282 |
4.04e-13 |
|
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: 71.16 E-value: 4.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 105 DKVILATGSKQIMLDIPGNNLAnIFSIKNFpnakeifkALDDSTiKKVGIIGAGYIGVEIA---EAIRKRGKEVYLFDVA 181
Cdd:TIGR01423 153 EHILLATGSWPQMLGIPGIEHC-ISSNEAF--------YLDEPP-RRVLTVGGGFISVEFAgifNAYKPRGGKVTLCYRN 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 182 DRVLSTYyDRSFSDKVEEILSKNGIHLCLSESPKKY-LGRKKIEKIVTTSGTQYSMDMVVQAIGFLSNSpigeKELLRDV 260
Cdd:TIGR01423 223 NMILRGF-DSTLRKELTKQLRANGINIMTNENPAKVtLNADGSKHVTFESGKTLDVDVVMMAIGRVPRT----QTLQLDK 297
|
170 180
....*....|....*....|....*....
gi 2090489534 261 SGAYLT-------NEYQQTNIKDIYAIGD 282
Cdd:TIGR01423 298 VGVELTkkgaiqvDEFSRTNVPNIYAIGD 326
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
3-285 |
4.68e-13 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 70.02 E-value: 4.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 3 KIVIIGSNHSGLAAARFLnlSDSNYEVILIDKKSEISylecGTSLF-----------IKGEVSNLEDL---FYQNRMTLN 68
Cdd:PRK12770 20 KVAIIGAGPAGLAAAGYL--ACLGYEVHVYDKLPEPG----GLMLFgipefripierVREGVKELEEAgvvFHTRTKVCC 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 69 SEIKKLFLETEVDKIDIQNKKIscVKKdgtrfsqeYDKVILATGS-KQIMLDIPGNNLANIFS------------IKNFP 135
Cdd:PRK12770 94 GEPLHEEEGDEFVERIVSLEEL--VKK--------YDAVLIATGTwKSRKLGIPGEDLPGVYSaleylfriraakLGYLP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 136 NAKeifkaLDDSTIKKVGIIGAGYIGVEIA-EAIRKRGKEVYLFdvadrvlstyYDRSFSD----KVE-EILSKNGIHLC 209
Cdd:PRK12770 164 WEK-----VPPVEGKKVVVVGAGLTAVDAAlEAVLLGAEKVYLA----------YRRTINEapagKYEiERLIARGVEFL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 210 LSESPKKYLGRKKIEKI--------------------VTTSGTQYSMDMVVQAIGFLSNSPIGEK----ELLRDvsGAYL 265
Cdd:PRK12770 229 ELVTPVRIIGEGRVEGVelakmrlgepdesgrprpvpIPGSEFVLEADTVVFAIGEIPTPPFAKEclgiELNRK--GEIV 306
|
330 340
....*....|....*....|
gi 2090489534 266 TNEYQQTNIKDIYAIGDCAT 285
Cdd:PRK12770 307 VDEKHMTSREGVFAAGDVVT 326
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
67-282 |
3.61e-12 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 67.85 E-value: 3.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 67 LNSEIKKLFLETEVDKID-----IQNKKISCVKKDgTRFSQEYDKVILATGSKQIMLDIPGnnlanIFSIKNFPNAKEIF 141
Cdd:PRK07251 78 LRGKNYAMLAGSGVDLYDaeahfVSNKVIEVQAGD-EKIELTAETIVINTGAVSNVLPIPG-----LADSKHVYDSTGIQ 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 142 KAldDSTIKKVGIIGAGYIGVEIAEAIRKRGKEVYLFDVADRVLSTYYDrSFSDKVEEILSKNGIHLCLSESPKKyLGRK 221
Cdd:PRK07251 152 SL--ETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTILPREEP-SVAALAKQYMEEDGITFLLNAHTTE-VKND 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2090489534 222 KIEKIVTTSGTQYSMDMVVQAIGFLSN-SPIG--EKELLRDVSGAYLTNEYQQTNIKDIYAIGD 282
Cdd:PRK07251 228 GDQVLVVTEDETYRFDALLYATGRKPNtEPLGleNTDIELTERGAIKVDDYCQTSVPGVFAVGD 291
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
107-282 |
6.24e-12 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 67.09 E-value: 6.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 107 VILATGSKQImlDIPGnnlanifsIKnfPNAKEIF---KALDDSTI-KKVGIIGAGYIGVEIAEAIRKRGKEVYLFDVAD 182
Cdd:PRK06416 138 IILATGSRPR--ELPG--------IE--IDGRVIWtsdEALNLDEVpKSLVVIGGGYIGVEFASAYASLGAEVTIVEALP 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 183 RVLSTyYDRSFSDKVEEILSKNGIhlclsespKKYLGR--KKIEK-----IVTTSGTQYS----MDMVVQAIGFLSNSP- 250
Cdd:PRK06416 206 RILPG-EDKEISKLAERALKKRGI--------KIKTGAkaKKVEQtddgvTVTLEDGGKEetleADYVLVAVGRRPNTEn 276
|
170 180 190
....*....|....*....|....*....|....*.
gi 2090489534 251 IG-EK---ELLRdvsGAYLTNEYQQTNIKDIYAIGD 282
Cdd:PRK06416 277 LGlEElgvKTDR---GFIEVDEQLRTNVPNIYAIGD 309
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
2-285 |
1.70e-11 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 65.97 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 2 EKIVIIGSNHSGLAAARFLNLSdsNYEVILIDKKSEIS-YLECGTSLFikgevsnledlfyqnRMTlnseikKLFLETEV 80
Cdd:PRK11749 141 KKVAVIGAGPAGLTAAHRLARK--GYDVTIFEARDKAGgLLRYGIPEF---------------RLP------KDIVDREV 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 81 DK-----IDIQ-NKKIscvkkdGTRFS-----QEYDKVILATG-SKQIMLDIPGNNLANIFSIKNFPNAKEIFKALDDST 148
Cdd:PRK11749 198 ERllklgVEIRtNTEV------GRDITldelrAGYDAVFIGTGaGLPRFLGIPGENLGGVYSAVDFLTRVNQAVADYDLP 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 149 I-KKVGIIGAGYIGVEIA-EAIRKRGKEVYLfdvadrvlstYYDRSFSD---KVEEILS--KNGIHLCLSESPKKYLGRK 221
Cdd:PRK11749 272 VgKRVVVIGGGNTAMDAArTAKRLGAESVTI----------VYRRGREEmpaSEEEVEHakEEGVEFEWLAAPVEILGDE 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 222 KIEKIVTT----------SGTQ--------YSM--DMVVQAIGFLSNSPI--GEKELLRDVSGAYLTNE-YQQTNIKDIY 278
Cdd:PRK11749 342 GRVTGVEFvrmelgepdaSGRRrvpiegseFTLpaDLVIKAIGQTPNPLIlsTTPGLELNRWGTIIADDeTGRTSLPGVF 421
|
....*..
gi 2090489534 279 AIGDCAT 285
Cdd:PRK11749 422 AGGDIVT 428
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
80-434 |
6.35e-11 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 63.88 E-value: 6.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 80 VDKID-----IQNKKISCVKKDGTRFSQEyDKVILATGSKQIMLDIPG-NNLANIFSIKNFPNAKEIFKALddstikkvG 153
Cdd:PRK08010 92 IDVIDgqaefINNHSLRVHRPEGNLEIHG-EKIFINTGAQTVVPPIPGiTTTPGVYDSTGLLNLKELPGHL--------G 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 154 IIGAGYIGVEIAEAIRKRGKEVYLFDVADRVLSTyYDRSFSDKVEEILSKNGIHLCLSESPKKyLGRKKIEKIVTTSGTQ 233
Cdd:PRK08010 163 ILGGGYIGVEFASMFANFGSKVTILEAASLFLPR-EDRDIADNIATILRDQGVDIILNAHVER-ISHHENQVQVHSEHAQ 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 234 YSMDMVVQAIG--------FLSNSPIGEKEllrdvSGAYLTNEYQQTNIKDIYAIGDcattfftsinrssvdfsISNALR 305
Cdd:PRK08010 241 LAVDALLIASGrqpataslHPENAGIAVNE-----RGAIVVDKYLHTTADNIWAMGD-----------------VTGGLQ 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 306 TAYIATQ--HINNQDFTPSGSQFTNGFSIFNYNFYAA------GLNLKTARLLSESIDYIEIEDFIRP-AFLRKNSRVKL 376
Cdd:PRK08010 299 FTYISLDdyRIVRDELLGEGKRSTDDRKNVPYSVFMTpplsrvGMTEEQARESGADIQVVTLPVAAIPrARVMNDTRGVL 378
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 377 RISFEKNTKRIVGVQ-LCSqeDLSGLLSMFSLAIEEQITLDKLKmlDYLF-HPSFSQPYN 434
Cdd:PRK08010 379 KAIVDNKTQRILGASlLCV--DSHEMINIVKMVMDAGLPYSILR--DQIFtHPSMSESLN 434
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
75-316 |
4.17e-10 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 61.32 E-value: 4.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 75 FLETEVDKIDIQNKKISCVKKDGTR------FSQEYDKVILATGSKQIMLDIPGNNlANIFSIKNFPNAKEIFKALDDS- 147
Cdd:PTZ00318 79 YLRAVVYDVDFEEKRVKCGVVSKSNnanvntFSVPYDKLVVAHGARPNTFNIPGVE-ERAFFLKEVNHARGIRKRIVQCi 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 148 --------------TIKKVGIIGAGYIGVE----IAEAIRKRGKEVY----------LFDVADRVLSTyYDRSFSDKVEE 199
Cdd:PTZ00318 158 eraslpttsveerkRLLHFVVVGGGPTGVEfaaeLADFFRDDVRNLNpelveeckvtVLEAGSEVLGS-FDQALRKYGQR 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 200 ILSKNGIHLCLSESPKKYLGrkkiEKIVTTSGTQYSMDMVVQAIGFLSNSPIGEKELLRDVSGAYLTNEYQQT-NIKDIY 278
Cdd:PTZ00318 237 RLRRLGVDIRTKTAVKEVLD----KEVVLKDGEVIPTGLVVWSTGVGPGPLTKQLKVDKTSRGRISVDDHLRVkPIPNVF 312
|
250 260 270
....*....|....*....|....*....|....*....
gi 2090489534 279 AIGDCAttfftSINRSSVDFSISNALRT-AYIAtQHINN 316
Cdd:PTZ00318 313 ALGDCA-----ANEERPLPTLAQVASQQgVYLA-KEFNN 345
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
3-285 |
8.54e-10 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 60.90 E-value: 8.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 3 KIVIIGSnhsGLAAARFL-NLSD----SNYEVILIDKKSEISY----LECGTSLFIKGEVSNLEDLFYQNRMTlnseikK 73
Cdd:PRK14989 5 RLAIIGN---GMVGHRFIeDLLDkadaANFDITVFCEEPRIAYdrvhLSSYFSHHTAEELSLVREGFYEKHGI------K 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 74 LFLETEVDKIDIQNKKIscvkKDGTRFSQEYDKVILATGSKQIMLDIPGNNLANIFSIKNFPNAKEIFKALDDStiKKVG 153
Cdd:PRK14989 76 VLVGERAITINRQEKVI----HSSAGRTVFYDKLIMATGSYPWIPPIKGSETQDCFVYRTIEDLNAIEACARRS--KRGA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 154 IIGAGYIGVEIAEAIRKRGKEVYLFDVADRVLSTYYDRSFSDKVEEILSKNGIHLCLSESPKKYL--GRKKIEKIVTTSG 231
Cdd:PRK14989 150 VVGGGLLGLEAAGALKNLGVETHVIEFAPMLMAEQLDQMGGEQLRRKIESMGVRVHTSKNTLEIVqeGVEARKTMRFADG 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2090489534 232 TQYSMDMVVQAIGFLSNSPIGEK-ELLRDVSGAYLTNEYQQTNIKDIYAIGDCAT 285
Cdd:PRK14989 230 SELEVDFIVFSTGIRPQDKLATQcGLAVAPRGGIVINDSCQTSDPDIYAIGECAS 284
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
93-282 |
7.38e-09 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 57.96 E-value: 7.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 93 VKKDGTRFSQEYdkVILATGSKQIMLDIPGNNLAnIFSiknfpNAkeifkALD-DSTIKKVGIIGAGYIGVEIAEAIRKR 171
Cdd:PLN02546 208 VDVDGKLYTARN--ILIAVGGRPFIPDIPGIEHA-IDS-----DA-----ALDlPSKPEKIAIVGGGYIALEFAGIFNGL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 172 GKEVYLFDVADRVLSTyYDRSFSDKVEEILSKNGIHLCLSESPKKYL-GRKKIEKIVTTSGTQYSMDMVVQAIGFLSNSp 250
Cdd:PLN02546 275 KSDVHVFIRQKKVLRG-FDEEVRDFVAEQMSLRGIEFHTEESPQAIIkSADGSLSLKTNKGTVEGFSHVMFATGRKPNT- 352
|
170 180 190
....*....|....*....|....*....|....*....
gi 2090489534 251 igeKEL-LRDV------SGAYLTNEYQQTNIKDIYAIGD 282
Cdd:PLN02546 353 ---KNLgLEEVgvkmdkNGAIEVDEYSRTSVPSIWAVGD 388
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
2-286 |
1.32e-08 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 56.47 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 2 EKIVIIGSNHSGLAAARFLNLSDSNYEVILIDKKSEISYLE--CGTSLFIKGEV---SNLEDLFYQNrmtlnseiKKLFL 76
Cdd:PRK09754 4 KTIIIVGGGQAAAMAAASLRQQGFTGELHLFSDERHLPYERppLSKSMLLEDSPqlqQVLPANWWQE--------NNVHL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 77 ETEVDKIDIQNKKISCVKKDGTRFsqEYDKVILATGSKQ---IMLDIPGNNlanIFSIKNFPNAKEIFKALDDStiKKVG 153
Cdd:PRK09754 76 HSGVTIKTLGRDTRELVLTNGESW--HWDQLFIATGAAArplPLLDALGER---CFTLRHAGDAARLREVLQPE--RSVV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 154 IIGAGYIGVEIAEAIRKRGKEVYLFDVADRVLSTYYDRSFSDKVEEILSKNGIHLCLSESPKKYLGRKKIEKIVTTsGTQ 233
Cdd:PRK09754 149 IVGAGTIGLELAASATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGEKVELTLQS-GET 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2090489534 234 YSMDMVVQAIGFLSNSPIGEKELLrDVSGAYLTNEYQQTNIKDIYAIGDCATT 286
Cdd:PRK09754 228 LQADVVIYGIGISANDQLAREANL-DTANGIVIDEACRTCDPAIFAGGDVAIT 279
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
2-291 |
2.20e-08 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 56.18 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 2 EKIVIIGSNHSGLAAARflNLSDSNYEVILIDKKSEIS-YLECGTSLF-------IKGEVSNledlfyqnrmtlnseIKK 73
Cdd:PRK12831 141 KKVAVIGSGPAGLTCAG--DLAKMGYDVTIFEALHEPGgVLVYGIPEFrlpketvVKKEIEN---------------IKK 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 74 LFLETEVDKIDIQNKKISCVKKDGTrfsqeYDKVILATGSKQIM-LDIPGNNLANIFSIKNFPNAKEIFKALD---DSTI 149
Cdd:PRK12831 204 LGVKIETNVVVGKTVTIDELLEEEG-----FDAVFIGSGAGLPKfMGIPGENLNGVFSANEFLTRVNLMKAYKpeyDTPI 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 150 ---KKVGIIGAGYIGVEIAEAIRKRGKEVYLFdvadrvlstyYDRSFSD---KVEEI--LSKNGIHLCLSESPKKYLGRK 221
Cdd:PRK12831 279 kvgKKVAVVGGGNVAMDAARTALRLGAEVHIV----------YRRSEEElpaRVEEVhhAKEEGVIFDLLTNPVEILGDE 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 222 ----------KIE----------KIVTTSGTQYSM--DMVVQAIGFLSNSPIGE--KELLRDVSGAYLTNEYQ-QTNIKD 276
Cdd:PRK12831 349 ngwvkgmkciKMElgepdasgrrRPVEIEGSEFVLevDTVIMSLGTSPNPLISSttKGLKINKRGCIVADEETgLTSKEG 428
|
330
....*....|....*
gi 2090489534 277 IYAIGDCATTFFTSI 291
Cdd:PRK12831 429 VFAGGDAVTGAATVI 443
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
105-284 |
1.93e-07 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 53.01 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 105 DKVILATGSKQIMLdiPGnnlanifsiknFPNAKEIF----KALD-DSTIKKVGIIGAGYIGVEIAEAIRKRGKEVYLFD 179
Cdd:PRK06327 147 KHVIIATGSEPRHL--PG-----------VPFDNKIIldntGALNfTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILE 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 180 VADRVLSTyYDRSFSDKVEEILSKNGIHLCLSESPKKYlgrKKIEKIVTTSGTQ-------YSMDMVVQAIGFLSNSP-I 251
Cdd:PRK06327 214 ALPAFLAA-ADEQVAKEAAKAFTKQGLDIHLGVKIGEI---KTGGKGVSVAYTDadgeaqtLEVDKLIVSIGRVPNTDgL 289
|
170 180 190
....*....|....*....|....*....|....*
gi 2090489534 252 GEKE--LLRDVSGAYLTNEYQQTNIKDIYAIGDCA 284
Cdd:PRK06327 290 GLEAvgLKLDERGFIPVDDHCRTNVPNVYAIGDVV 324
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
3-291 |
2.23e-07 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 53.21 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 3 KIVIIGSNHSGLAAARflNLSDSNYEVILIDKKSEIS-YLECGTSLF------IKGEVSNLedlfyqnrmtlnseiKKLF 75
Cdd:PRK12778 433 KVAVIGSGPAGLSFAG--DLAKRGYDVTVFEALHEIGgVLKYGIPEFrlpkkiVDVEIENL---------------KKLG 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 76 LETEVDKIDIQNKKISCVKKDGtrfsqeYDKVILATGSK-QIMLDIPGNNLANIFSIKNFPNAKEIFKALDDSTI----- 149
Cdd:PRK12778 496 VKFETDVIVGKTITIEELEEEG------FKGIFIASGAGlPNFMNIPGENSNGVMSSNEYLTRVNLMDAASPDSDtpikf 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 150 -KKVGIIGAGYIGVEIAEAIRKRGkevylfdvADRVLsTYYDRSFSD---KVEEI--LSKNGIHLCLSESPKKYLG---- 219
Cdd:PRK12778 570 gKKVAVVGGGNTAMDSARTAKRLG--------AERVT-IVYRRSEEEmpaRLEEVkhAKEEGIEFLTLHNPIEYLAdekg 640
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 220 --------------------RKKIEkiVTTSGTQYSMDMVVQAIGFLSN----SPIGEKELLRdvSGAYLTNEYQQTNIK 275
Cdd:PRK12778 641 wvkqvvlqkmelgepdasgrRRPVA--IPGSTFTVDVDLVIVSVGVSPNplvpSSIPGLELNR--KGTIVVDEEMQSSIP 716
|
330
....*....|....*.
gi 2090489534 276 DIYAIGDCATTFFTSI 291
Cdd:PRK12778 717 GIYAGGDIVRGGATVI 732
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
89-284 |
6.08e-07 |
|
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: 51.78 E-value: 6.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 89 KISCVKKDGTRFSQEYDKVILATGSKQIMLDIPGNNLANIFSIKNFPNAKEIFKALddstikkvgIIGAGYIGVEIAEAI 168
Cdd:TIGR01438 129 RIKATNKKGKEKIYSAERFLIATGERPRYPGIPGAKELCITSDDLFSLPYCPGKTL---------VVGASYVALECAGFL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 169 RKRGKEVylfDVADR-VLSTYYDRSFSDKVEEILSKNGIHLCLSESPKKYL---GRKKIEKIVTTSGTQYSMDMVVQAIG 244
Cdd:TIGR01438 200 AGIGLDV---TVMVRsILLRGFDQDCANKVGEHMEEHGVKFKRQFVPIKVEqieAKVLVEFTDSTNGIEEEYDTVLLAIG 276
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2090489534 245 FLSNS-PIGEKEL---LRDVSGAYLTNEYQQTNIKDIYAIGDCA 284
Cdd:TIGR01438 277 RDACTrKLNLENVgvkINKKTGKIPADEEEQTNVPYIYAVGDIL 320
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
82-281 |
7.12e-07 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 50.69 E-value: 7.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 82 KIDIQ-NKKISCVKKDGTRF-----SQEY--DKVILATGskqimldipgnnlanIFSIKNFPNAKEI------FKALDDS 147
Cdd:pfam13738 89 ELPINlFEEVTSVKKEDDGFvvttsKGTYqaRYVIIATG---------------EFDFPNKLGVPELpkhysyVKDFHPY 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 148 TIKKVGIIGAGYIGVEIAEAIRKRGKEVYLFDVADRVLSTYYDRSFSDK------VEEILSKNGIhlclsespkKYLGRK 221
Cdd:pfam13738 154 AGQKVVVIGGYNSAVDAALELVRKGARVTVLYRGSEWEDRDSDPSYSLSpdtlnrLEELVKNGKI---------KAHFNA 224
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2090489534 222 KIEKI--------VTTS-GTQY-SMDMVVQAIGFLSN-SPIGEKELLRDVSG-AYLTNEYQQTNIKDIYAIG 281
Cdd:pfam13738 225 EVKEItevdvsykVHTEdGRKVtSNDDPILATGYHPDlSFLKKGLFELDEDGrPVLTEETESTNVPGLFLAG 296
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
3-283 |
9.36e-07 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 51.31 E-value: 9.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 3 KIVIIGSNHSGLAAARFLnlSDSNYEVILIDKKSEisylecgtslfiKGEVSNLEDLFYQnrmtLNSEIkklfLETEVDK 82
Cdd:PRK13984 285 KVAIVGSGPAGLSAAYFL--ATMGYEVTVYESLSK------------PGGVMRYGIPSYR----LPDEA----LDKDIAF 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 83 IDIQNKKISC---VKKDGT--RFSQEYDKVILATG-SKQIMLDIPGNNLANIfsIKNFPNAKEIFKALDDSTIK-----K 151
Cdd:PRK13984 343 IEALGVKIHLntrVGKDIPleELREKHDAVFLSTGfTLGRSTRIPGTDHPDV--IQALPLLREIRDYLRGEGPKpkiprS 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 152 VGIIGAGYIGVEIAEAIRKRGKEVYlFDVADRVLStyYDRSFSD---KVEEIL--SKNGIHLCLSESPKKYL---GR--- 220
Cdd:PRK13984 421 LVVIGGGNVAMDIARSMARLQKMEY-GEVNVKVTS--LERTFEEmpaDMEEIEegLEEGVVIYPGWGPMEVVienDKvkg 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 221 ---KKIEKIVTTSG-----------TQYSMDMVVQAIGFLSN-SPIGE--KELLRDVSGAYLTNEYQQTNIKDIYAIGDC 283
Cdd:PRK13984 498 vkfKKCVEVFDEEGrfnpkfdesdqIIVEADMVVEAIGQAPDySYLPEelKSKLEFVRGRILTNEYGQTSIPWLFAGGDI 577
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
2-283 |
1.20e-06 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 50.55 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 2 EKIVIIGSNHSGLAAARFLNLSdsNYEVILIDKKSEIS-YLECGTSLFiKgevsnLEDLFYQNRMTLNSE--IKkLFLET 78
Cdd:PRK12810 144 KKVAVVGSGPAGLAAADQLARA--GHKVTVFERADRIGgLLRYGIPDF-K-----LEKEVIDRRIELMEAegIE-FRTNV 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 79 EVDKiDIQNKKIScvkkdgtrfsQEYDKVILATGSKQIM-LDIPGNNLANIFSIKNF--PNAKEIFKALDDSTI----KK 151
Cdd:PRK12810 215 EVGK-DITAEELL----------AEYDAVFLGTGAYKPRdLGIPGRDLDGVHFAMDFliQNTRRVLGDETEPFIsakgKH 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 152 VGIIGAGYIGVE-IAEAIRKRGKEVYLFDVADR----------------VLSTYY------DRSFSDKVEEILSKNG--- 205
Cdd:PRK12810 284 VVVIGGGDTGMDcVGTAIRQGAKSVTQRDIMPMppsrrnknnpwpywpmKLEVSNaheegvEREFNVQTKEFEGENGkvt 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 206 -IHLCLSEspkkyLGRKKIEKIvttSGTQYSM--DMVVQAIGFLSNspigEKELL------RDVSG--AYLTNEYqQTNI 274
Cdd:PRK12810 364 gVKVVRTE-----LGEGDFEPV---EGSEFVLpaDLVLLAMGFTGP----EAGLLaqfgveLDERGrvAAPDNAY-QTSN 430
|
....*....
gi 2090489534 275 KDIYAIGDC 283
Cdd:PRK12810 431 PKVFAAGDM 439
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
3-114 |
6.12e-06 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 48.32 E-value: 6.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 3 KIVIIGSNHSGLAAArfLNLSDSNYEVILIDKKSEI-----------SYLECGTSLfikgevsnLEDLFyqNRMTLNSEI 71
Cdd:COG1148 142 RALVIGGGIAGMTAA--LELAEQGYEVYLVEKEPELggraaqlhktfPGLDCPQCI--------LEPLI--AEVEANPNI 209
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2090489534 72 KkLFLETEVDKID--IQNKKISCVKKDGTRFSQEYDKVILATGSK 114
Cdd:COG1148 210 T-VYTGAEVEEVSgyVGNFTVTIKKGPREEIEIEVGAIVLATGFK 253
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
94-283 |
9.93e-06 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 47.84 E-value: 9.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 94 KKDGTRFSQEYDKVILATGSKQIMLDIPGnnlanifsIKNFP--NAKEifkALDDSTI-KKVGIIGAGYIGVEIAEAIRK 170
Cdd:PRK13748 223 LNDGGERVVAFDRCLIATGASPAVPPIPG--------LKETPywTSTE---ALVSDTIpERLAVIGSSVVALELAQAFAR 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 171 RGKEVYLfdVADRVLSTYYDRSFSDKVEEILSKNGIHLcLSESPKKYLGRKKIEKIVTTSGTQYSMDMVVQAIGFLSNSP 250
Cdd:PRK13748 292 LGSKVTI--LARSTLFFREDPAIGEAVTAAFRAEGIEV-LEHTQASQVAHVDGEFVLTTGHGELRADKLLVATGRAPNTR 368
|
170 180 190
....*....|....*....|....*....|....*.
gi 2090489534 251 IGEKE---LLRDVSGAYLTNEYQQTNIKDIYAIGDC 283
Cdd:PRK13748 369 SLALDaagVTVNAQGAIVIDQGMRTSVPHIYAAGDC 404
|
|
| FadB |
COG1250 |
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ... |
148-185 |
1.33e-05 |
|
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA dehydrogenase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440862 [Multi-domain] Cd Length: 281 Bit Score: 46.64 E-value: 1.33e-05
10 20 30
....*....|....*....|....*....|....*...
gi 2090489534 148 TIKKVGIIGAGYIGVEIAEAIRKRGKEVYLFDVADRVL 185
Cdd:COG1250 1 EIKKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEAL 38
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
1-112 |
4.20e-05 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 45.29 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 1 MEKIVIIGSNHSGLAAArfLNLSDSNYEVILIDKKSEISYLECGTSLFIKGEVSN-LEDLFYQNRMtlnseikKLFLETE 79
Cdd:pfam13738 155 GQKVVVIGGYNSAVDAA--LELVRKGARVTVLYRGSEWEDRDSDPSYSLSPDTLNrLEELVKNGKI-------KAHFNAE 225
|
90 100 110
....*....|....*....|....*....|...
gi 2090489534 80 VDKIDIQNKKISCVKKDGTRFsQEYDKVILATG 112
Cdd:pfam13738 226 VKEITEVDVSYKVHTEDGRKV-TSNDDPILATG 257
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
96-262 |
6.55e-05 |
|
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: 44.85 E-value: 6.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 96 DGTRFsqEYDKVILATG--SKQIMLDIPGNNLaniFSIK-----NFPNAKEifkaLDDstiKKVGIIGAGYIGVEIAEAI 168
Cdd:COG2072 123 DGETL--TARFVVVATGplSRPKIPDIPGLED---FAGEqlhsaDWRNPVD----LAG---KRVLVVGTGASAVQIAPEL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 169 RKRGKEVYLF-----------DVAD-----------------------RVLSTYYDRSFSDKVEEILSKN----GIHLCL 210
Cdd:COG2072 191 ARVAAHVTVFqrtppwvlprpNYDPergrpanylgleappalnrrdarAWLRRLLRAQVKDPELGLLTPDyppgCKRPLL 270
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2090489534 211 SESPKKYLGRKKIE------------KIVTTSGTQYSMDMVVQAIGFLSNSPIGEKELLRDVSG 262
Cdd:COG2072 271 STDYYEALRRGNVElvtggieritedGVVFADGTEHEVDVIVWATGFRADLPWLAPLDVRGRDG 334
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
107-284 |
2.68e-04 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 43.27 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 107 VILATGSK-QIMLDIPG-NNLA----NIFSIKNFPNakeifkalddstikKVGIIGAGYIGVEIAEAIRKRGkevylFDV 180
Cdd:PTZ00052 148 ILIATGGRpSIPEDVPGaKEYSitsdDIFSLSKDPG--------------KTLIVGASYIGLETAGFLNELG-----FDV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 181 ADRVLSTY---YDRSFSDKVEEILSKNGIHLCLSESPKKYlgrKKIE---KIVTTSGTQYSMDMVVQAIG------FLSN 248
Cdd:PTZ00052 209 TVAVRSIPlrgFDRQCSEKVVEYMKEQGTLFLEGVVPINI---EKMDdkiKVLFSDGTTELFDTVLYATGrkpdikGLNL 285
|
170 180 190
....*....|....*....|....*....|....*.
gi 2090489534 249 SPIGEKelLRDVSGAYLTNEyqQTNIKDIYAIGDCA 284
Cdd:PTZ00052 286 NAIGVH--VNKSNKIIAPND--CTNIPNIFAVGDVV 317
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
6-60 |
9.64e-04 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 37.51 E-value: 9.64e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2090489534 6 IIGSNHSGLAAARFlnLSDSNYEVILIDKKSEI-----SY------LECGTSLFIKGEVSNLEDLF 60
Cdd:pfam13450 1 IVGAGLAGLVAAAL--LAKRGFRVLVLEKRDRLggnaySYrvpgyvFDYGAHIFHGSDEPNVRDLL 64
|
|
| PLN02545 |
PLN02545 |
3-hydroxybutyryl-CoA dehydrogenase |
147-243 |
1.26e-03 |
|
3-hydroxybutyryl-CoA dehydrogenase
Pssm-ID: 215300 [Multi-domain] Cd Length: 295 Bit Score: 40.48 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 147 STIKKVGIIGAGYIGVEIAEAIRKRGKEVYLFDVADRVLSTYYDrSFSDKVEEILSKNGIhlcLSESPKKYLGRkkiekI 226
Cdd:PLN02545 2 AEIKKVGVVGAGQMGSGIAQLAAAAGMDVWLLDSDPAALSRGLD-SISSSLARLVKKGKM---SQEEADATLGR-----I 72
|
90
....*....|....*....
gi 2090489534 227 VTTSGTQ--YSMDMVVQAI 243
Cdd:PLN02545 73 RCTTNLEelRDADFIIEAI 91
|
|
| PRK05808 |
PRK05808 |
3-hydroxybutyryl-CoA dehydrogenase; Validated |
148-182 |
4.07e-03 |
|
3-hydroxybutyryl-CoA dehydrogenase; Validated
Pssm-ID: 180269 [Multi-domain] Cd Length: 282 Bit Score: 38.79 E-value: 4.07e-03
10 20 30
....*....|....*....|....*....|....*
gi 2090489534 148 TIKKVGIIGAGYIGVEIAEAIRKRGKEVYLFDVAD 182
Cdd:PRK05808 2 GIQKIGVIGAGTMGNGIAQVCAVAGYDVVMVDISD 36
|
|
| TyrA |
COG0287 |
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ... |
149-199 |
4.69e-03 |
|
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440056 [Multi-domain] Cd Length: 278 Bit Score: 38.57 E-value: 4.69e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2090489534 149 IKKVGIIGAGYIGVEIAEAIRKRG--KEVYLFDVADRVLSTYYDRSFSDKVEE 199
Cdd:COG0287 1 FMRIAIIGLGLIGGSLALALKRAGlaHEVVGVDRSPETLERALELGVIDRAAT 53
|
|
| 3HCDH_N |
pfam02737 |
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ... |
151-185 |
7.21e-03 |
|
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda crystallin.
Pssm-ID: 397037 [Multi-domain] Cd Length: 180 Bit Score: 37.52 E-value: 7.21e-03
10 20 30
....*....|....*....|....*....|....*
gi 2090489534 151 KVGIIGAGYIGVEIAEAIRKRGKEVYLFDVADRVL 185
Cdd:pfam02737 1 KVAVIGAGTMGAGIAQVFALAGLEVVLVDISEEAL 35
|
|
| MurD |
COG0771 |
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ... |
150-243 |
7.58e-03 |
|
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramoylalanine-D-glutamate ligase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440534 [Multi-domain] Cd Length: 445 Bit Score: 38.52 E-value: 7.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 150 KKVGIIGAGYIGVEIAEAIRKRGKEVYLFDvadrvlstyyDRSFSDKVEEILSKNGIHLCLSESPKKYLgrKKIEKIVTT 229
Cdd:COG0771 5 KKVLVLGLGKSGLAAARLLAKLGAEVTVSD----------DRPAPELAAAELEAPGVEVVLGEHPEELL--DGADLVVKS 72
|
90
....*....|....
gi 2090489534 230 SGTQYSMDMVVQAI 243
Cdd:COG0771 73 PGIPPDHPLLKAAR 86
|
|
| NAD_bind_Glutamyl_tRNA_reduct |
cd05213 |
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the ... |
137-243 |
9.01e-03 |
|
NADP-binding domain of glutamyl-tRNA reductase; Glutamyl-tRNA reductase catalyzes the conversion of glutamyl-tRNA to glutamate-1-semialdehyde, initiating the synthesis of tetrapyrrole. Whereas tRNAs are generally associated with peptide bond formation in protein translation, here the tRNA activates glutamate in the initiation of tetrapyrrole biosynthesis in archaea, plants and many bacteria. In the first step, activated glutamate is reduced to glutamate-1-semi-aldehyde via the NADPH dependent glutamyl-tRNA reductase. Glutamyl-tRNA reductase forms a V-shaped dimer. Each monomer has 3 domains: an N-terminal catalytic domain, a classic nucleotide binding domain, and a C-terminal dimerization domain. Although the representative structure 1GPJ lacks a bound NADPH, a theoretical binding pocket has been described. (PMID 11172694). Amino acid dehydrogenase (DH)-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.
Pssm-ID: 133452 [Multi-domain] Cd Length: 311 Bit Score: 38.02 E-value: 9.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2090489534 137 AKEIFKALDDstiKKVGIIGAGYIGVEIAEAI-RKRGKEVYlfdVADRvlsTYydrsfsDKVEEILSKNGIHLCLSESPK 215
Cdd:cd05213 169 AEKIFGNLKG---KKVLVIGAGEMGELAAKHLaAKGVAEIT---IANR---TY------ERAEELAKELGGNAVPLDELL 233
|
90 100
....*....|....*....|....*...
gi 2090489534 216 KYLGRKKIekIVTTSGTQYSMDMVVQAI 243
Cdd:cd05213 234 ELLNEADV--VISATGAPHYAKIVERAM 259
|
|
| |
