|
Name |
Accession |
Description |
Interval |
E-value |
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
1-428 |
0e+00 |
|
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: 595.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 1 MHQAALLGGLIQDAPNYGWEVAQPVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCGVAKGGKE 80
Cdd:TIGR01438 60 MHQAALLGQALKDSRNYGWKVEETVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGKE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 81 ILLSADHIIIATGGRPRYPtHIEGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSIPLRGF 160
Cdd:TIGR01438 140 KIYSAERFLIATGERPRYP-GIPGAKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGF 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 161 DQQMSSMVIEHMASHGTRFLRGCAPSRVRRLpDGQLQVTWEDSTTGKEdtGTFDTVLWAIGRVPDTRSLNLEKAGVDTSP 240
Cdd:TIGR01438 219 DQDCANKVGEHMEEHGVKFKRQFVPIKVEQI-EAKVLVEFTDSTNGIE--EEYDTVLLAIGRDACTRKLNLENVGVKINK 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 241 DTQKILVDSREATSVPHIYAIGDVVEGRPELTPIAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAV 320
Cdd:TIGR01438 296 KTGKIPADEEEQTNVPYIYAVGDILEDKPELTPVAIQAGRLLAQRLFKGSTVICDYENVPTTVFTPLEYGACGLSEEKAV 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 321 ARHGQEHVEVYHAHYKPLEFTVAGRD-ASQCYVKMVCLREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVG 399
Cdd:TIGR01438 376 EKFGEENVEVFHSYFWPLEWTIPSRDnHNKCYAKLVCNKKENERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIG 455
|
410 420
....*....|....*....|....*....
gi 1205913889 400 IHPTCSEEVVKLRISKRSGLDPTVTGCUG 428
Cdd:TIGR01438 456 IHPVCAEVFTTLSVTKRSGQDILQQGCCG 484
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
1-428 |
3.84e-162 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 465.84 E-value: 3.84e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 1 MHQAALLGGLIQ-DAPNYGWEVAQPvpHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVcGVAKGGK 79
Cdd:PTZ00052 63 MHYAANIGSIFHhDSQMYGWKTSSS--FNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTV-SYGDNSQ 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 80 EILLSADHIIIATGGRPRYPTHIEGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSIPLRG 159
Cdd:PTZ00052 140 EETITAKYILIATGGRPSIPEDVPGAKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVAVRSIPLRG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 160 FDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDgQLQVTWEDSTTGKedtgtFDTVLWAIGRVPDTRSLNLEKAGVDTS 239
Cdd:PTZ00052 220 FDRQCSEKVVEYMKEQGTLFLEGVVPINIEKMDD-KIKVLFSDGTTEL-----FDTVLYATGRKPDIKGLNLNAIGVHVN 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 240 PDTQKILVDsrEATSVPHIYAIGDVVEGRPELTPIAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEA 319
Cdd:PTZ00052 294 KSNKIIAPN--DCTNIPNIFAVGDVVEGRPELTPVAIKAGILLARRLFKQSNEFIDYTFIPTTIFTPIEYGACGYSSEAA 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 320 VARHGQEHVEVYHAHYKPLEFTVAGRD--------------ASQCYVKMVCLREPPQLVLGLHFLGPNAGEVTQGFALGI 385
Cdd:PTZ00052 372 IAKYGEDDIEEYLQEFNTLEIAAVHREkherarkdeydfdvSSNCLAKLVCVKSEDNKVVGFHFVGPNAGEITQGFSLAL 451
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1205913889 386 KCGASYAQVMRTVGIHPTCSEEVVKLRISKRSGLDPTVTGCUG 428
Cdd:PTZ00052 452 KLGAKKSDFDSMIGIHPTDAEVFMNLSVTRRSGESFAAKGGCG 494
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
12-412 |
6.84e-129 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 379.50 E-value: 6.84e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 12 QDAPNYGWEVAQPVpHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVcgvAKGGKEIllSADHIIIA 91
Cdd:PRK06116 65 DYAPGYGFDVTENK-FDWAKLIANRDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTV---EVNGERY--TADHILIA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 92 TGGRPRYPThIEGAlEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRS-IPLRGFDQQMSSMVIE 170
Cdd:PRK06116 139 TGGRPSIPD-IPGA-EYGITSDGFFALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGdAPLRGFDPDIRETLVE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 171 HMASHGTRFLRGCAPSRVRRLPDGQLQVTWEDsttGKEDTgtFDTVLWAIGRVPDTRSLNLEKAGVDTSpDTQKILVDSR 250
Cdd:PRK06116 217 EMEKKGIRLHTNAVPKAVEKNADGSLTLTLED---GETLT--VDCLIWAIGREPNTDGLGLENAGVKLN-EKGYIIVDEY 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 251 EATSVPHIYAIGDVvEGRPELTPIAIMAGRLLVQRLFGGSSDL-MDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQEHVE 329
Cdd:PRK06116 291 QNTNVPGIYAVGDV-TGRVELTPVAIAAGRRLSERLFNNKPDEkLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEDNVK 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 330 VYHAHYKPLEFTVAGRDAsQCYVKMVCLREPPQlVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVV 409
Cdd:PRK06116 370 VYRSSFTPMYTALTGHRQ-PCLMKLVVVGKEEK-VVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAEEFV 447
|
...
gi 1205913889 410 KLR 412
Cdd:PRK06116 448 TMR 450
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
1-409 |
2.41e-104 |
|
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: 316.64 E-value: 2.41e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 1 MHQAALLGGLIQDAPNYGWEVAQPvPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVcgVAKGGKE 80
Cdd:COG1249 52 LLHAAEVAHEARHAAEFGISAGAP-SVDWAALMARKDKVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTV--EVTGGET 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 81 IllSADHIIIATGGRPRYPTHIEGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIM-MRSIPLRG 159
Cdd:COG1249 129 L--TADHIVIATGSRPRVPPIPGLDEVRVLTSDEALELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVeRGDRLLPG 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 160 FDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGqLQVTWEDSttGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTS 239
Cdd:COG1249 207 EDPEISEALEKALEKEGIDILTGAKVTSVEKTGDG-VTVTLEDG--GGEEAVEADKVLVATGRRPNTDGLGLEAAGVELD 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 240 PDTQkILVDSREATSVPHIYAIGDVVeGRPELTPIAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEA 319
Cdd:COG1249 284 ERGG-IKVDEYLRTSVPGIYAIGDVT-GGPQLAHVASAEGRVAAENILGKKPRPVDYRAIPSVVFTDPEIASVGLTEEEA 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 320 VARHGQehVEVYHAHYKPLEFTVAGRDAsQCYVKMVCLREpPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVG 399
Cdd:COG1249 362 REAGID--VKVGKFPFAANGRALALGET-EGFVKLIADAE-TGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIH 437
|
410
....*....|
gi 1205913889 400 IHPTCSEEVV 409
Cdd:COG1249 438 AHPTLSEALK 447
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
4-416 |
1.07e-83 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 265.14 E-value: 1.07e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 4 AALLGGLIQDAPNYGWEVAQPVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCGVAKGGKEILL 83
Cdd:PLN02507 87 GATFGGEFEDAKNYGWEINEKVDFNWKKLLQKKTDEILRLNGIYKRLLANAGVKLYEGEGKIVGPNEVEVTQLDGTKLRY 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 84 SADHIIIATGGRPRYPThIEGAlEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMR-SIPLRGFDQ 162
Cdd:PLN02507 167 TAKHILIATGSRAQRPN-IPGK-ELAITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRkELPLRGFDD 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 163 QMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGqLQVTwedSTTGKEDTGtfDTVLWAIGRVPDTRSLNLEKAGVDTSpDT 242
Cdd:PLN02507 245 EMRAVVARNLEGRGINLHPRTNLTQLTKTEGG-IKVI---TDHGEEFVA--DVVLFATGRAPNTKRLNLEAVGVELD-KA 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 243 QKILVDSREATSVPHIYAIGDVVEgRPELTPIAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVAR 322
Cdd:PLN02507 318 GAVKVDEYSRTNIPSIWAIGDVTN-RINLTPVALMEGTCFAKTVFGGQPTKPDYENVACAVFCIPPLSVVGLSEEEAVEQ 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 323 HGQEhVEVYHAHYKPLEFTVAGRDaSQCYVKMVCLREPPQlVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHP 402
Cdd:PLN02507 397 AKGD-ILVFTSSFNPMKNTISGRQ-EKTVMKLIVDAETDK-VLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHP 473
|
410
....*....|....
gi 1205913889 403 TCSEEVVKLRISKR 416
Cdd:PLN02507 474 SAAEEFVTMRSVTR 487
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
12-416 |
1.31e-74 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 243.24 E-value: 1.31e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 12 QDAPNYGWEVAQPVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVcgvAKGGKeiLLSADHIIIA 91
Cdd:PLN02546 149 EESRGFGWKYETEPKHDWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGKIVDPHTV---DVDGK--LYTARNILIA 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 92 TGGRPRYPtHIEGaLEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSIP-LRGFDQQMSSMVIE 170
Cdd:PLN02546 224 VGGRPFIP-DIPG-IEHAIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHVFIRQKKvLRGFDEEVRDFVAE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 171 HMASHGTRFLRGCAPSRVRRLPDGQLQVTwedstTGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSpDTQKILVDSR 250
Cdd:PLN02546 302 QMSLRGIEFHTEESPQAIIKSADGSLSLK-----TNKGTVEGFSHVMFATGRKPNTKNLGLEEVGVKMD-KNGAIEVDEY 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 251 EATSVPHIYAIGDVVEgRPELTPIAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQehVEV 330
Cdd:PLN02546 376 SRTSVPSIWAVGDVTD-RINLTPVALMEGGALAKTLFGNEPTKPDYRAVPSAVFSQPPIGQVGLTEEQAIEEYGD--VDV 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 331 YHAHYKPLEFTVAGRDASQCYVKMVCLREppQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVVK 410
Cdd:PLN02546 453 FTANFRPLKATLSGLPDRVFMKLIVCAKT--NKVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAEEFVT 530
|
....*.
gi 1205913889 411 LRISKR 416
Cdd:PLN02546 531 MRTPTR 536
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
1-411 |
4.00e-69 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 228.73 E-value: 4.00e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 1 MHQAALLGGLIQDAPNYGWEVAQPVphDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVC--GVAKGG 78
Cdd:PTZ00058 97 MFNAASIHDILENSRHYGFDTQFSF--NLPLLVERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSLLSENQVLikKVSQVD 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 79 KEI----------------------LLSADHIIIATGGRPRYPtHIEGaLEYGITSDDIFWLKEsPGKTLVVGASYVALE 136
Cdd:PTZ00058 175 GEAdesdddevtivsagvsqlddgqVIEGKNILIAVGNKPIFP-DVKG-KEFTISSDDFFKIKE-AKRIGIAGSGYIAVE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 137 CAGFLTGIGLDTTIMMR-SIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQLQVTWEDSttGKEDTgtFDT 215
Cdd:PTZ00058 252 LINVVNRLGAESYIFARgNRLLRKFDETIINELENDMKKNNINIITHANVEEIEKVKEKNLTIYLSDG--RKYEH--FDY 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 216 VLWAIGRVPDTRSLNLEKAGVDTSPDTqkILVDSREATSVPHIYAIGDVVEGRP-------------------------- 269
Cdd:PTZ00058 328 VIYCVGRSPNTEDLNLKALNIKTPKGY--IKVDDNQRTSVKHIYAVGDCCMVKKnqeiedlnllklyneepylkkkents 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 270 -------ELTPIAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQEHVEVYHAHYKPLEFTV 342
Cdd:PTZ00058 406 gesyynvQLTPVAINAGRLLADRLFGPFSRTTNYKLIPSVIFSHPPIGTIGLSEQEAIDIYGKENVKIYESRFTNLFFSV 485
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1205913889 343 AGRDASQ---CYVKMVCLrEPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVVKL 411
Cdd:PTZ00058 486 YDMDPAQkekTYLKLVCV-GKEELIKGLHIVGLNADEILQGFAVALKMNATKADFDETIPIHPTAAEEFVTM 556
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
11-412 |
9.72e-65 |
|
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: 215.22 E-value: 9.72e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 11 IQDAPNYGWEV-AQPVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRK-VKYFNIKASFVDEHTVCgVAKGG------KEiL 82
Cdd:TIGR01423 72 LRESAGFGWEFdRSSVKANWKALIAAKNKAVLDINKSYEGMFADTEgLTFFLGWGALEDKNVVL-VRESAdpksavKE-R 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 83 LSADHIIIATGGRPRYPThIEGaLEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTG---IGLDTTIMMRSIP-LR 158
Cdd:TIGR01423 150 LQAEHILLATGSWPQMLG-IPG-IEHCISSNEAFYLDEPPRRVLTVGGGFISVEFAGIFNAykpRGGKVTLCYRNNMiLR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 159 GFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQLQVTWEdstTGKedTGTFDTVLWAIGRVPDTRSLNLEKAGVDT 238
Cdd:TIGR01423 228 GFDSTLRKELTKQLRANGINIMTNENPAKVTLNADGSKHVTFE---SGK--TLDVDVVMMAIGRVPRTQTLQLDKVGVEL 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 239 SPDTqKILVDSREATSVPHIYAIGDVVeGRPELTPIAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEE 318
Cdd:TIGR01423 303 TKKG-AIQVDEFSRTNVPNIYAIGDVT-DRVMLTPVAINEGAAFVDTVFGNKPRKTDHTRVASAVFSIPPIGTCGLVEED 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 319 AVARHgqEHVEVYHAHYKPLEFTVAGRDASQCYVKMVClREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTV 398
Cdd:TIGR01423 381 AAKKF--EKVAVYESSFTPLMHNISGSKYKKFVAKIVT-NHADGTVLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTI 457
|
410
....*....|....
gi 1205913889 399 GIHPTCSEEVVKLR 412
Cdd:TIGR01423 458 GVHPTSAEELCSMR 471
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
11-406 |
2.99e-61 |
|
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: 205.57 E-value: 2.99e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 11 IQDAPNYGWEVAQpVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVcGVAKGGKEILLSADHIII 90
Cdd:TIGR01350 60 IKHAKDLGIEVEN-VSVDWEKMQKRKNKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTV-SVTGENGEETLEAKNIII 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 91 ATGGRPRY-PTHIEGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTI--MMRSIpLRGFDQQMSSM 167
Cdd:TIGR01350 138 ATGSRPRSlPGPFDFDGKVVITSTGALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVieMLDRI-LPGEDAEVSKV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 168 VIEHMASHGTRFLRGCAPSRVRRLPDgqlQVTWEDSTtGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDtQKILV 247
Cdd:TIGR01350 217 LQKALKKKGVKILTNTKVTAVEKNDD---QVTYENKG-GETETLTGEKVLVAVGRKPNTEGLGLEKLGVELDER-GRIVV 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 248 DSREATSVPHIYAIGDVVEGrPELTPIAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGqeh 327
Cdd:TIGR01350 292 DEYMRTNVPGIYAIGDVIGG-PMLAHVASHEGIVAAENIAGKEPAHIDYDAVPSVIYTDPEVASVGLTEEQAKEAGY--- 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 328 vevyhaHYKPLEFTVA--GR----DASQCYVKMVCLREpPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIH 401
Cdd:TIGR01350 368 ------DVKIGKFPFAanGKalalGETDGFVKIIADKK-TGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPH 440
|
....*
gi 1205913889 402 PTCSE 406
Cdd:TIGR01350 441 PTLSE 445
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
11-406 |
2.89e-56 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 192.28 E-value: 2.89e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 11 IQDAPNYGWEvAQPVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVcGVAKGGKEILLSADHIII 90
Cdd:PRK06416 63 ARHSEDFGIK-AENVGIDFKKVQEWKNGVVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTV-RVMTEDGEQTYTAKNIIL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 91 ATGGRPRYPTHIEGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTI--MMRSIpLRGFDQQMSSMV 168
Cdd:PRK06416 141 ATGSRPRELPGIEIDGRVIWTSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIveALPRI-LPGEDKEISKLA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 169 IEHMASHGTRFLRGcapSRVRRLPDGQLQVTWEDSTTGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTspDTQKILVD 248
Cdd:PRK06416 220 ERALKKRGIKIKTG---AKAKKVEQTDDGVTVTLEDGGKEETLEADYVLVAVGRRPNTENLGLEELGVKT--DRGFIEVD 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 249 SREATSVPHIYAIGDVVEGrPELTPIAIMAGRLLVQRLFGGSSDlMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQehV 328
Cdd:PRK06416 295 EQLRTNVPNIYAIGDIVGG-PMLAHKASAEGIIAAEAIAGNPHP-IDYRGIPAVTYTHPEVASVGLTEAKAKEEGFD--V 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 329 EVYhahykplEFTVAGR------DASQCYVKMVcLREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHP 402
Cdd:PRK06416 371 KVV-------KFPFAGNgkalalGETDGFVKLI-FDKKDGEVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHP 442
|
....
gi 1205913889 403 TCSE 406
Cdd:PRK06416 443 TLSE 446
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
9-411 |
2.03e-55 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 190.03 E-value: 2.03e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 9 GLIQDAPNYGWEVAQPVPHDWRK----MAEAVQN-HVKSLNWghrvqLQDRK-VKYFNIKASFVDEHTVCgVAkggkEIL 82
Cdd:PRK06370 62 HLARRAAEYGVSVGGPVSVDFKAvmarKRRIRARsRHGSEQW-----LRGLEgVDVFRGHARFESPNTVR-VG----GET 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 83 LSADHIIIATGGRPRYPtHIEGALEYG-ITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSiP--LRG 159
Cdd:PRK06370 132 LRAKRIFINTGARAAIP-PIPGLDEVGyLTNETIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERG-PrlLPR 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 160 FDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGqlqVTWEDSTTGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTS 239
Cdd:PRK06370 210 EDEDVAAAVREILEREGIDVRLNAECIRVERDGDG---IAVGLDCNGGAPEITGSHILVAVGRVPNTDDLGLEAAGVETD 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 240 PDTQkILVDSREATSVPHIYAIGDvVEGRPELTPIAIMAGRLLVQRLFGGS----SDLmdydNVPTTVFTPLEYGCVGLS 315
Cdd:PRK06370 287 ARGY-IKVDDQLRTTNPGIYAAGD-CNGRGAFTHTAYNDARIVAANLLDGGrrkvSDR----IVPYATYTDPPLARVGMT 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 316 EEEAVARhGQEhVEVYHahykpLEFTVAGR----DASQCYVKMVcLREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASY 391
Cdd:PRK06370 361 EAEARKS-GRR-VLVGT-----RPMTRVGRavekGETQGFMKVV-VDADTDRILGATILGVHGDEMIHEILDAMYAGAPY 432
|
410 420
....*....|....*....|
gi 1205913889 392 AQVMRTVGIHPTCSEEVVKL 411
Cdd:PRK06370 433 TTLSRAIHIHPTVSELIPTL 452
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
51-428 |
1.34e-52 |
|
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: 182.62 E-value: 1.34e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 51 LQDRKVKYFNIKASFVDEHTVcgVAKGGKEILlSADHIIIATGGRPRYPtHIEGALEYG-ITSDDIFWLKESPGKTLVVG 129
Cdd:TIGR02053 98 LSSYGVDYLRGRARFKDPKTV--KVDLGREVR-GAKRFLIATGARPAIP-PIPGLKEAGyLTSEEALALDRIPESLAVIG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 130 ASYVALECAGFLTGIGLDTTIMMRS-IPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQLQVTwedSTTGKE 208
Cdd:TIGR02053 174 GGAIGVELAQAFARLGSEVTILQRSdRLLPREEPEISAAVEEALAEEGIEVVTSAQVKAVSVRGGGKIITV---EKPGGQ 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 209 DTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDTQkILVDSREATSVPHIYAIGDVVeGRPELTPIAIMAGRLLVQRLFG 288
Cdd:TIGR02053 251 GEVEADELLVATGRRPNTDGLGLEKAGVKLDERGG-ILVDETLRTSNPGIYAAGDVT-GGLQLEYVAAKEGVVAAENALG 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 289 GSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAvarhgQEHVEVYHAHYKPLEFTVAGR--DASQCYVKMVCLREPPQlVLG 366
Cdd:TIGR02053 329 GANAKLDLLVIPRVVFTDPAVASVGLTEAEA-----QKAGIECDCRTLPLTNVPRARinRDTRGFIKLVAEPGTGK-VLG 402
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1205913889 367 LHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEevvKLRISKRSGL-DPTVTGCUG 428
Cdd:TIGR02053 403 VQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAE---GLKLAAQTFYrDVSKLSCCA 462
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
24-279 |
1.31e-51 |
|
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: 175.58 E-value: 1.31e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 24 PVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCGvakggKEILLSADHIIIATGGRPRYPThIE 103
Cdd:pfam07992 54 EIASLWADLYKRKEEVVKKLNNGIEVLLGTEVVSIDPGAKKVVLEELVDG-----DGETITYDRLVIATGARPRLPP-IP 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 104 GALEYG------ITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIM-MRSIPLRGFDQQMSSMVIEHMASHG 176
Cdd:pfam07992 128 GVELNVgflvrtLDSAEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIeALDRLLRAFDEEISAALEKALEKNG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 177 TRFLRGCAPSRVRRLPDGQLQVTwedsttGKEDTGTFDTVLWAIGRVPDTRslNLEKAGVDTSPDTQkILVDSREATSVP 256
Cdd:pfam07992 208 VEVRLGTSVKEIIGDGDGVEVIL------KDGTEIDADLVVVAIGRRPNTE--LLEAAGLELDERGG-IVVDEYLRTSVP 278
|
250 260
....*....|....*....|...
gi 1205913889 257 HIYAIGDVVEGRPELTPIAIMAG 279
Cdd:pfam07992 279 GIYAAGDCRVGGPELAQNAVAQG 301
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
11-410 |
2.75e-51 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 178.83 E-value: 2.75e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 11 IQDAPNYGWEVAQPVPhDWRKMAEAVQNHVKSLNWGH-RVQLQDRKVKYFNIKASFVDEHTVcgvAKGGKEIllSADHII 89
Cdd:PRK06292 62 AKHAEEFGIHADGPKI-DFKKVMARVRRERDRFVGGVvEGLEKKPKIDKIKGTARFVDPNTV---EVNGERI--EAKNIV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 90 IATGGR-PRYPThIEGALEYGI-TSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTI--MMRSIpLRGFDQQMS 165
Cdd:PRK06292 136 IATGSRvPPIPG-VWLILGDRLlTSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVfeRGDRI-LPLEDPEVS 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 166 SMVIEHMASHgTRFLRGCAPSRVRRLPDGQLQVTWEDsttGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSpDTQKI 245
Cdd:PRK06292 214 KQAQKILSKE-FKIKLGAKVTSVEKSGDEKVEELEKG---GKTETIEADYVLVATGRRPNTDGLGLENTGIELD-ERGRP 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 246 LVDSREATSVPHIYAIGDVVeGRPELTPIAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARhGQ 325
Cdd:PRK06292 289 VVDEHTQTSVPGIYAAGDVN-GKPPLLHEAADEGRIAAENAAGDVAGGVRYHPIPSVVFTDPQIASVGLTEEELKAA-GI 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 326 EHVEVYHahykplEFTVAGR----DASQCYVKMVCLREpPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIH 401
Cdd:PRK06292 367 DYVVGEV------PFEAQGRarvmGKNDGFVKVYADKK-TGRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYH 439
|
....*....
gi 1205913889 402 PTcSEEVVK 410
Cdd:PRK06292 440 PT-LSEGLR 447
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
47-376 |
2.79e-43 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 157.63 E-value: 2.79e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 47 HRVQLQDRKVKYFNIKASFVDEHTVCGVAKGGKEILLSADHIIIATGGRPRYPTHIEGALEYGITSDDIFWLKESPGKTL 126
Cdd:PRK05249 100 RRGQYERNRVDLIQGRARFVDPHTVEVECPDGEVETLTADKIVIATGSRPYRPPDVDFDHPRIYDSDSILSLDHLPRSLI 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 127 VVGASYVALECAGFLTGIGLDTT-IMMRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQLqVTWEDstt 205
Cdd:PRK05249 180 IYGAGVIGCEYASIFAALGVKVTlINTRDRLLSFLDDEISDALSYHLRDSGVTIRHNEEVEKVEGGDDGVI-VHLKS--- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 206 GKEDTGtfDTVLWAIGRVPDTRSLNLEKAGVDTSPDTQkILVDSREATSVPHIYAIGDVVeGRPELTPIAIMAGRLLVQR 285
Cdd:PRK05249 256 GKKIKA--DCLLYANGRTGNTDGLNLENAGLEADSRGQ-LKVNENYQTAVPHIYAVGDVI-GFPSLASASMDQGRIAAQH 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 286 LFGGSSDLMdYDNVPTTVFTPLEYGCVGLSEEEAVARHGqeHVEVYHAHYKPLeftvA-GRDASQCY--VKMVCLREPPQ 362
Cdd:PRK05249 332 AVGEATAHL-IEDIPTGIYTIPEISSVGKTEQELTAAKV--PYEVGRARFKEL----ArAQIAGDNVgmLKILFHRETLE 404
|
330
....*....|....
gi 1205913889 363 LvLGLHFLGPNAGE 376
Cdd:PRK05249 405 I-LGVHCFGERATE 417
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
299-411 |
1.55e-36 |
|
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases.
Pssm-ID: 427019 [Multi-domain] Cd Length: 109 Bit Score: 129.60 E-value: 1.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 299 VPTTVFTPLEYGCVGLSEEEAVARHGQehVEVYHAHYKPLEFTVAGRDASqCYVKMVCLREPpQLVLGLHFLGPNAGEVT 378
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGGE--VKVGKFPFAANGRALAYGDTD-GFVKLVADRET-GKILGAHIVGPNAGELI 76
|
90 100 110
....*....|....*....|....*....|...
gi 1205913889 379 QGFALGIKCGASYAQVMRTVGIHPTCSEEVVKL 411
Cdd:pfam02852 77 QEAALAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
59-408 |
1.74e-35 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 136.24 E-value: 1.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 59 FNIKASFVDEHTVCgVAKGGkeiLLSADHIIIATGGRPRYPTHI-EGALEYGiTSDDIFWLKESPGKTLVVGASYVALEC 137
Cdd:PRK07846 107 YRGHARFIGPKTLR-TGDGE---EITADQVVIAAGSRPVIPPVIaDSGVRYH-TSDTIMRLPELPESLVIVGGGFIAAEF 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 138 AGFLTGIGLDTTIMMRS-IPLRGFDQQMSSMVIEHMashGTRF-LR-GCAPSRVRRLPDGqLQVTWEDSTtgkedTGTFD 214
Cdd:PRK07846 182 AHVFSALGVRVTVVNRSgRLLRHLDDDISERFTELA---SKRWdVRlGRNVVGVSQDGSG-VTLRLDDGS-----TVEAD 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 215 TVLWAIGRVPDTRSLNLEKAGVDTSPDtQKILVDSREATSVPHIYAIGDVveGRP-ELTPIAIMAGRLLVQRLFGGSSDL 293
Cdd:PRK07846 253 VLLVATGRVPNGDLLDAAAAGVDVDED-GRVVVDEYQRTSAEGVFALGDV--SSPyQLKHVANHEARVVQHNLLHPDDLI 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 294 -MDYDNVPTTVFTPLEYGCVGLSEEEAVARhGQEHVeVYHAHYKPLEFTVAGRDASQCyVKMVCLREPPQLvLGLHFLGP 372
Cdd:PRK07846 330 aSDHRFVPAAVFTHPQIASVGLTENEARAA-GLDIT-VKVQNYGDVAYGWAMEDTTGF-VKLIADRDTGRL-LGAHIIGP 405
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1205913889 373 NAGEVTQGF----ALGIKcgasyAQVM--RTVGIHPTCSEEV 408
Cdd:PRK07846 406 QASTLIQPLiqamSFGLD-----AREMarGQYWIHPALPEVV 442
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
28-417 |
4.90e-34 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 132.36 E-value: 4.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 28 DWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFV---DEHTVCGVAKGGKEILlSADHIIIATGGRPRyptHIEG 104
Cdd:PRK06327 87 DVAKMIARKDKVVKKMTGGIEGLFKKNKITVLKGRGSFVgktDAGYEIKVTGEDETVI-TAKHVIIATGSEPR---HLPG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 105 AL---EYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIM--MRSIpLRGFDQQMSSMVIEHMASHGTRF 179
Cdd:PRK06327 163 VPfdnKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILeaLPAF-LAAADEQVAKEAAKAFTKQGLDI 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 180 LRGCAPSRVRRLPDGqLQVTWEDSTtGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSpDTQKILVDSREATSVPHIY 259
Cdd:PRK06327 242 HLGVKIGEIKTGGKG-VSVAYTDAD-GEAQTLEVDKLIVSIGRVPNTDGLGLEAVGLKLD-ERGFIPVDDHCRTNVPNVY 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 260 AIGDVVEGrPELTPIAIMAGrLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVArhgqEHVEvYHAHYKPle 339
Cdd:PRK06327 319 AIGDVVRG-PMLAHKAEEEG-VAVAERIAGQKGHIDYNTIPWVIYTSPEIAWVGKTEQQLKA----EGVE-YKAGKFP-- 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 340 FTVAGR----DASQCYVKMVCLREPPQlVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSeEVVK---LR 412
Cdd:PRK06327 390 FMANGRalamGEPDGFVKIIADAKTDE-ILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLS-EVWHeaaLA 467
|
....*
gi 1205913889 413 ISKRS 417
Cdd:PRK06327 468 VDKRP 472
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
67-313 |
7.71e-30 |
|
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: 117.99 E-value: 7.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 67 DEHTVcgVAKGGKEIllSADHIIIATGGRPRYPtHIEGALEYGITS----DDIFWLKE-----SPGKTLVVGASYVALEC 137
Cdd:COG0446 65 EAKTV--TLRDGETL--SYDKLVLATGARPRPP-PIPGLDLPGVFTlrtlDDADALREalkefKGKRAVVIGGGPIGLEL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 138 AGFLTGIGLDTTIM-MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRrlPDGQLQVTWEDsttgkEDTGTFDTV 216
Cdd:COG0446 140 AEALRKRGLKVTLVeRAPRLLGVLDPEMAALLEEELREHGVELRLGETVVAID--GDDKVAVTLTD-----GEEIPADLV 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 217 LWAIGRVPDTrSLnLEKAGVDTSPdTQKILVDSREATSVPHIYAIGDVVE------GRPELTP---IAIMAGRLLVQRLF 287
Cdd:COG0446 213 VVAPGVRPNT-EL-AKDAGLALGE-RGWIKVDETLQTSDPDVYAAGDCAEvphpvtGKTVYIPlasAANKQGRVAAENIL 289
|
250 260
....*....|....*....|....*...
gi 1205913889 288 GGSsdlMDYDNVPTTVFT--PLEYGCVG 313
Cdd:COG0446 290 GGP---APFPGLGTFISKvfDLCIASTG 314
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
54-386 |
2.36e-29 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 120.26 E-value: 2.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 54 RKVKYFNI------------KASFVDEHTVCGVAKGGKEILLSADHIIIATGGRPRYPThIEGALE--YGiTSDDIFWLK 119
Cdd:PRK13748 190 RHAKYEGIldgnpaitvlhgEARFKDDQTLIVRLNDGGERVVAFDRCLIATGASPAVPP-IPGLKEtpYW-TSTEALVSD 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 120 ESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLpDGQLQVT 199
Cdd:PRK13748 268 TIPERLAVIGSSVVALELAQAFARLGSKVTILARSTLFFREDPAIGEAVTAAFRAEGIEVLEHTQASQVAHV-DGEFVLT 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 200 wedstTGKedtGTF--DTVLWAIGRVPDTRSLNLEKAGVDTSPDTQkILVDSREATSVPHIYAIGDVVEgRPELTPIAIM 277
Cdd:PRK13748 347 -----TGH---GELraDKLLVATGRAPNTRSLALDAAGVTVNAQGA-IVIDQGMRTSVPHIYAAGDCTD-QPQFVYVAAA 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 278 AGRLLVQRLFGGSSDLmDYDNVPTTVFTPLEYGCVGLSEEEavARHGQEHVEVYHAHYKPLEFTVAGRDaSQCYVKMVcL 357
Cdd:PRK13748 417 AGTRAAINMTGGDAAL-DLTAMPAVVFTDPQVATVGYSEAE--AHHDGIETDSRTLTLDNVPRALANFD-TRGFIKLV-I 491
|
330 340
....*....|....*....|....*....
gi 1205913889 358 REPPQLVLGLHFLGPNAGEVTQGFALGIK 386
Cdd:PRK13748 492 EEGSGRLIGVQAVAPEAGELIQTAALAIR 520
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
51-406 |
4.74e-27 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 112.15 E-value: 4.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 51 LQDRKVKYFNIKASFVDEHTVCGVAkGGKEILLSADHIIIATGGRPRYPThIEGALE--YGITSDDIFWLKESPGKTLVV 128
Cdd:PRK07251 86 LAGSGVDLYDAEAHFVSNKVIEVQA-GDEKIELTAETIVINTGAVSNVLP-IPGLADskHVYDSTGIQSLETLPERLGII 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 129 GASYVALECAGFLTGIGLDTTIM-MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRlPDGQLQVTWEDSTTgk 207
Cdd:PRK07251 164 GGGNIGLEFAGLYNKLGSKVTVLdAASTILPREEPSVAALAKQYMEEDGITFLLNAHTTEVKN-DGDQVLVVTEDETY-- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 208 edtgTFDTVLWAIGRVPDTRSLNLEKAGVDTSpDTQKILVDSREATSVPHIYAIGDvVEGRPELTPIAIMAGRLLVQRLF 287
Cdd:PRK07251 241 ----RFDALLYATGRKPNTEPLGLENTDIELT-ERGAIKVDDYCQTSVPGVFAVGD-VNGGPQFTYISLDDFRIVFGYLT 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 288 GGSS-DLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQehvevyhahYKPLEFTVAG--RDASQCYVK---MVCLREPP 361
Cdd:PRK07251 315 GDGSyTLEDRGNVPTTMFITPPLSQVGLTEKEAKEAGLP---------YAVKELLVAAmpRAHVNNDLRgafKVVVNTET 385
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1205913889 362 QLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSE 406
Cdd:PRK07251 386 KEILGATLFGEGSQEIINLITMAMDNKIPYTYFKKQIFTHPTMAE 430
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
67-323 |
2.89e-22 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 97.90 E-value: 2.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 67 DEHTVcgVAKGGKEIllSADHIIIATGGRPRYPThIEGALEYGITS----DDIFWLKE--SPGKTLVV-GASYVALECAG 139
Cdd:COG1251 85 AARTV--TLADGETL--PYDKLVLATGSRPRVPP-IPGADLPGVFTlrtlDDADALRAalAPGKRVVViGGGLIGLEAAA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 140 FLTGIGLDTT-IMMRSIPL-RGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRlPDGQLQVTWEDsttgkedtGTF---D 214
Cdd:COG1251 160 ALRKRGLEVTvVERAPRLLpRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEG-DDRVTGVRLAD--------GEElpaD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 215 TVLWAIGRVPDTrSLnLEKAGVDTSpdtQKILVDSREATSVPHIYAIGDVVE------GRP--ELTPIAIMAGRLLVQRL 286
Cdd:COG1251 231 LVVVAIGVRPNT-EL-ARAAGLAVD---RGIVVDDYLRTSDPDIYAAGDCAEhpgpvyGRRvlELVAPAYEQARVAAANL 305
|
250 260 270
....*....|....*....|....*....|....*....
gi 1205913889 287 FGGSSDLMDYDNVPTTVFTPLEYGCVGLSE--EEAVARH 323
Cdd:COG1251 306 AGGPAAYEGSVPSTKLKVFGVDVASAGDAEgdEEVVVRG 344
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
66-405 |
1.11e-18 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 87.61 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 66 VDEHTVCGVAKGGKEILLSADHIIIATGGRPRYpthIEGALEYG---ITSDDIFWLKESPGKTLVVGASYVALECAGFLT 142
Cdd:PRK07845 121 LGPHRVKVTTADGGEETLDADVVLIATGASPRI---LPTAEPDGeriLTWRQLYDLDELPEHLIVVGSGVTGAEFASAYT 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 143 GIGLDTT-IMMRSIPLRGFDQQmSSMVIEH-MASHGTRFLRGCAPSRVRRLPDGQLqVTWEDsttGKEDTGTFdtVLWAI 220
Cdd:PRK07845 198 ELGVKVTlVSSRDRVLPGEDAD-AAEVLEEvFARRGMTVLKRSRAESVERTGDGVV-VTLTD---GRTVEGSH--ALMAV 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 221 GRVPDTRSLNLEKAGVDTSPdTQKILVD--SReaTSVPHIYAIGDVVEGRPeLTPIAIMAGRLLVQRLFGGSSDLMDYDN 298
Cdd:PRK07845 271 GSVPNTAGLGLEEAGVELTP-SGHITVDrvSR--TSVPGIYAAGDCTGVLP-LASVAAMQGRIAMYHALGEAVSPLRLKT 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 299 VPTTVFTPLEYGCVGLSeeEAVARHGQEHVEVY------HAHYKPLEFtvagRDAsqcYVKMVClREPPQLVLGLHFLGP 372
Cdd:PRK07845 347 VASNVFTRPEIATVGVS--QAAIDSGEVPARTVmlplatNPRAKMSGL----RDG---FVKLFC-RPGTGVVIGGVVVAP 416
|
330 340 350
....*....|....*....|....*....|...
gi 1205913889 373 NAGEVTQGFALGIKCGASYAQVMRTVGIHPTCS 405
Cdd:PRK07845 417 RASELILPIALAVQNRLTVDDLAQTFTVYPSLS 449
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
35-411 |
3.91e-18 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 86.22 E-value: 3.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 35 AVQNHVKSLNWGHRVQLQDrkVKYFNIKASFVDEHTVcGVAKGGKEILLSADHIIIATGGRPRYP-----THIEGALEyg 109
Cdd:PRK08010 73 EVVNFLRNKNFHNLADMPN--IDVIDGQAEFINNHSL-RVHRPEGNLEIHGEKIFINTGAQTVVPpipgiTTTPGVYD-- 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 110 itSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIM-MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRV 188
Cdd:PRK08010 148 --STGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILeAASLFLPREDRDIADNIATILRDQGVDIILNAHVERI 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 189 RRlPDGQLQVTWEDSTTgkedtgTFDTVLWAIGRVPDTRSLNLEKAGVDTSpDTQKILVDSREATSVPHIYAIGDVVEGR 268
Cdd:PRK08010 226 SH-HENQVQVHSEHAQL------AVDALLIASGRQPATASLHPENAGIAVN-ERGAIVVDKYLHTTADNIWAMGDVTGGL 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 269 pELTPIAIMAGRLLVQRLFG-GSSDLMDYDNVPTTVFTPLEYGCVGLSEEEavARHGQEHVEVYHAHYKPLEFTVAGRDA 347
Cdd:PRK08010 298 -QFTYISLDDYRIVRDELLGeGKRSTDDRKNVPYSVFMTPPLSRVGMTEEQ--ARESGADIQVVTLPVAAIPRARVMNDT 374
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1205913889 348 SQCYVKMVCLREppQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVVKL 411
Cdd:PRK08010 375 RGVLKAIVDNKT--QRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESLNDL 436
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
42-355 |
1.49e-17 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 84.32 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 42 SLNWGHRVQLQDRKVKYFNIKAsfvdehtvcgvAKGGKEILLSADHIIIATGGRPRYPTHIEGALE--YGITS-DDIFWL 118
Cdd:PRK09564 72 DVKTEHEVVKVDAKNKTITVKN-----------LKTGSIFNDTYDKLMIATGARPIIPPIKNINLEnvYTLKSmEDGLAL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 119 KESPGKT-----LVVGASYVALECAGFLTGIGLDTTIMMRS--IPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVrrl 191
Cdd:PRK09564 141 KELLKDEeikniVIIGAGFIGLEAVEAAKHLGKNVRIIQLEdrILPDSFDKEITDVMEEELRENGVELHLNEFVKSL--- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 192 pDGQLQVTWEDSTTGKEDTgtfDTVLWAIGRVPDTRSLnlEKAGVDTSpDTQKILVDSREATSVPHIYAIGD------VV 265
Cdd:PRK09564 218 -IGEDKVEGVVTDKGEYEA---DVVIVATGVKPNTEFL--EDTGLKTL-KNGAIIVDEYGETSIENIYAAGDcatiynIV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 266 EGRPELTPIAIMA---GRLLVQRLFG---------GSSDLMDYDnvpttvftpLEYGCVGLSEEEAVArHGQEHVEVY-- 331
Cdd:PRK09564 291 SNKNVYVPLATTAnklGRMVGENLAGrhvsfkgtlGSACIKVLD---------LEAARTGLTEEEAKK-LGIDYKTVFik 360
|
330 340
....*....|....*....|....*..
gi 1205913889 332 ---HAHYKPleftvagrDASQCYVKMV 355
Cdd:PRK09564 361 dknHTNYYP--------GQEDLYVKLI 379
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
74-281 |
1.45e-16 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 79.78 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 74 VAKGGKEILLSADHIIIATGGRPRYPThIEGALE-------YGITSDDIFWlkesPGKT-LVVGASYVALECAGFLTGIG 145
Cdd:COG0492 90 RVTTDDGTEYEAKAVIIATGAGPRKLG-LPGEEEfegrgvsYCATCDGFFF----RGKDvVVVGGGDSALEEALYLTKFA 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 146 LDTTIMMRSIPLRGfdqqmSSMVIEHMASH-GTRFLRGCAPSRVrrLPDGQLQ-VTWEDSTTGKEDTGTFDTVLWAIGRV 223
Cdd:COG0492 165 SKVTLIHRRDELRA-----SKILVERLRANpKIEVLWNTEVTEI--EGDGRVEgVTLKNVKTGEEKELEVDGVFVAIGLK 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1205913889 224 PDTrSLnLEKAGVDTSPDtQKILVDSREATSVPHIYAIGDVVEGRPELTPIAIMAGRL 281
Cdd:COG0492 238 PNT-EL-LKGLGLELDED-GYIVVDEDMETSVPGVFAAGDVRDYKYRQAATAAGEGAI 292
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
21-406 |
1.88e-16 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 81.50 E-value: 1.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 21 VAQPVPHDWRKMAEAVQNHVKSLNWG-------HRVQLQDRKVKYFNIKASFVDEHTVCGvAKGGKEilLSADHIIIATG 93
Cdd:PTZ00153 207 VADTVQIDITKLKEYTQSVIDKLRGGienglksKKFCKNSEHVQVIYERGHIVDKNTIKS-EKSGKE--FKVKNIIIATG 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 94 GRPRYPTHIEGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSiplrgfdQQMSSMVIEHMA 173
Cdd:PTZ00153 284 STPNIPDNIEVDQKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVSFEYS-------PQLLPLLDADVA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 174 SHGTRFLRGCAPSRVR--------RLPDGQLQVT--WEDSTTGKEDTGTF----------DTVLWAIGRVPDTRSLNLEK 233
Cdd:PTZ00153 357 KYFERVFLKSKPVRVHlntlieyvRAGKGNQPVIigHSERQTGESDGPKKnmndiketyvDSCLVATGRKPNTNNLGLDK 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 234 AGVDTS----PDTQKILVDSREATSVPHIYAIGDVvEGRPELTP------------IAIMAGRLLVQRLFGGSSDLMDYD 297
Cdd:PTZ00153 437 LKIQMKrgfvSVDEHLRVLREDQEVYDNIFCIGDA-NGKQMLAHtashqalkvvdwIEGKGKENVNINVENWASKPIIYK 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 298 NVPTTVFTPLEYGCVGLSEEEAVARHGQEHVEVYHAHYKP-------LEFTVAGRDASQCY--------------VKMVC 356
Cdd:PTZ00153 516 NIPSVCYTTPELAFIGLTEKEAKELYPPDNVGVEISFYKAnskvlceNNISFPNNSKNNSYnkgkyntvdntegmVKIVY 595
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1205913889 357 LREPPQlVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSE 406
Cdd:PTZ00153 596 LKDTKE-ILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISE 644
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
124-199 |
1.24e-14 |
|
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: 68.77 E-value: 1.24e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1205913889 124 KTLVVGASYVALECAGFLTGIGLDTTIM-MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQLQVT 199
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVeRRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVL 77
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
79-286 |
2.80e-10 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 61.54 E-value: 2.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 79 KEILLSADHIIIATGG-RPRYPThIEG--------ALEY---------GITSddifWLKESP---GKTLVVGASYVALEC 137
Cdd:PRK12770 113 EELVKKYDAVLIATGTwKSRKLG-IPGedlpgvysALEYlfriraaklGYLP----WEKVPPvegKKVVVVGAGLTAVDA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 138 A--GFLTGIGLDTTIMMRSIPlrgfDQQMSSMVIEHMASHGTRFLRGCAP------SRVRRLPDGQLQVTWEDST----- 204
Cdd:PRK12770 188 AleAVLLGAEKVYLAYRRTIN----EAPAGKYEIERLIARGVEFLELVTPvriigeGRVEGVELAKMRLGEPDESgrprp 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 205 ---TGKEDTGTFDTVLWAIGRVPdTRSLNLEKAGVDTSPDTqKILVDSREATSVPHIYAIGDVVEGrPELTPIAIMAGRL 281
Cdd:PRK12770 264 vpiPGSEFVLEADTVVFAIGEIP-TPPFAKECLGIELNRKG-EIVVDEKHMTSREGVFAAGDVVTG-PSKIGKAIKSGLR 340
|
....*
gi 1205913889 282 LVQRL 286
Cdd:PRK12770 341 AAQSI 345
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
67-321 |
4.30e-10 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 60.92 E-value: 4.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 67 DEHTVcgVAKGGKEIllSADHIIIATGGRPRYPtHIEGALEYGITSDDI-----FW----------LKESPGKTLVVGAS 131
Cdd:COG1252 84 EARTV--TLADGRTL--SYDYLVIATGSVTNFF-GIPGLAEHALPLKTLedalaLRerllaaferaERRRLLTIVVVGGG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 132 Y----VALECAGFLTGIGLDTTIMMRSI----------PLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRrlPDGqlq 197
Cdd:COG1252 159 PtgveLAGELAELLRKLLRYPGIDPDKVritlveagprILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEVD--ADG--- 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 198 VTWEDSTTGKedtgtFDTVLWAIG-RVPDTrslnLEKAGVDTSPDTQkILVDSR-EATSVPHIYAIGDVV-----EGRPe 270
Cdd:COG1252 234 VTLEDGEEIP-----ADTVIWAAGvKAPPL----LADLGLPTDRRGR-VLVDPTlQVPGHPNVFAIGDCAavpdpDGKP- 302
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1205913889 271 LTPIAIMA-------GRLLVQRLFGGssdlmdydnvPTTVFTPLEYGC-VGLSEEEAVA 321
Cdd:COG1252 303 VPKTAQAAvqqakvlAKNIAALLRGK----------PLKPFRYRDKGClASLGRGAAVA 351
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
124-337 |
4.59e-10 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 61.34 E-value: 4.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 124 KTLVVGASYVALECAGFLTGIGLDTTIMMRSIP-LRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVrrlpDGQLqVTWEd 202
Cdd:PRK13512 150 KALVVGAGYISLEVLENLYERGLHPTLIHRSDKiNKLMDADMNQPILDELDKREIPYRLNEEIDAI----NGNE-VTFK- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 203 stTGKEDtgTFDTVLWAIGRVPDTRSlnLEKAGVDTSpDTQKILVDSREATSVPHIYAIGDVVEG------RPELTPIAI 276
Cdd:PRK13512 224 --SGKVE--HYDMIIEGVGTHPNSKF--IESSNIKLD-DKGFIPVNDKFETNVPNIYAIGDIITShyrhvdLPASVPLAW 296
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1205913889 277 MAGR---LLVQRLFGGSS-DLMDYDNVPTTVFTPLEYGCVGLSEEEaVARHGQEHVEV---YHAHYKP 337
Cdd:PRK13512 297 GAHRaasIVAEQIAGNDTiEFKGFLGNNIVKFFDYTFASVGVKPNE-LKQFDYKMVEVtqgAHANYYP 363
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
86-280 |
1.07e-06 |
|
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: 50.52 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 86 DHIIIATG-GRPRyPTHIEG--------ALEY--GITSDDIFWLKESPGKTLVV-GASYVALECAGflTGIGL---DTTI 150
Cdd:COG0493 208 DAVFLATGaGKPR-DLGIPGedlkgvhsAMDFltAVNLGEAPDTILAVGKRVVViGGGNTAMDCAR--TALRLgaeSVTI 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 151 MMRsiplRGFDQqMSSMV--IEHMASHGTRFLRGCAPSRVRRLPDGQL------QVTW-EDSTTGK----EDTGTF---- 213
Cdd:COG0493 285 VYR----RTREE-MPASKeeVEEALEEGVEFLFLVAPVEIIGDENGRVtglecvRMELgEPDESGRrrpvPIEGSEftlp 359
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1205913889 214 -DTVLWAIGRVPDTRSLnLEKAGVDTSPDTqKILVDSRE-ATSVPHIYAIGDVVEGrPELTPIAIMAGR 280
Cdd:COG0493 360 aDLVILAIGQTPDPSGL-EEELGLELDKRG-TIVVDEETyQTSLPGVFAGGDAVRG-PSLVVWAIAEGR 425
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
126-293 |
4.34e-06 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 48.37 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 126 LVVGASYVALECAGFLTGIGLDTTIMMRSiplrgfDQQMSSMV-------IEH-MASHGTRFLRGCAPSRVRRLPDGqLQ 197
Cdd:PRK04965 145 LVVGGGLIGTELAMDLCRAGKAVTLVDNA------ASLLASLMppevssrLQHrLTEMGVHLLLKSQLQGLEKTDSG-IR 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 198 VTWEDSttgkeDTGTFDTVLWAIGRVPDTrSLNLEkAGVDTSpdtQKILVDSREATSVPHIYAIGDVVE--GR--PELTP 273
Cdd:PRK04965 218 ATLDSG-----RSIEVDAVIAAAGLRPNT-ALARR-AGLAVN---RGIVVDSYLQTSAPDIYALGDCAEinGQvlPFLQP 287
|
170 180
....*....|....*....|
gi 1205913889 274 IaIMAGRLLVQRLFGGSSDL 293
Cdd:PRK04965 288 I-QLSAMALAKNLLGQNTPL 306
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
47-266 |
7.48e-06 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 48.29 E-value: 7.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 47 HRVQLqdrkvkYFNIKASFVDEHTVCGVAKGGKeiLLSADHIIIATGGRPRYPThIEGALEYGITS-------DDIFWLK 119
Cdd:TIGR02374 67 HGITL------YTGETVIQIDTDQKQVITDAGR--TLSYDKLILATGSYPFILP-IPGADKKGVYVfrtiedlDAIMAMA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 120 ESPGKTLVVGASYVALECAGFLTGIGLDTTI--MMRSIPLRGFDQQMSSMVIEHMASHGTRFLRGcapsrvrrlpdgqlQ 197
Cdd:TIGR02374 138 QRFKKAAVIGGGLLGLEAAVGLQNLGMDVSVihHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLE--------------K 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1205913889 198 VTWEDSTTGKEDTGTF--------DTVLWAIGRVPDTRsLNLEkAGVDTSpdtQKILVDSREATSVPHIYAIGDVVE 266
Cdd:TIGR02374 204 DTVEIVGATKADRIRFkdgssleaDLIVMAAGIRPNDE-LAVS-AGIKVN---RGIIVNDSMQTSDPDIYAVGECAE 275
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
86-267 |
1.16e-05 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 47.48 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 86 DHIIIATG-GRPRyPTHIEG--------ALEYGITSDDIFWLKESP-GKTLVV-GASYVALECAGflTGIGL---DTTIM 151
Cdd:PRK11749 227 DAVFIGTGaGLPR-FLGIPGenlggvysAVDFLTRVNQAVADYDLPvGKRVVViGGGNTAMDAAR--TAKRLgaeSVTIV 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 152 MRsiplRGFDQqMSSMV--IEHMASHGTRFLRGCAPSRVRRLPDGQLQVTWE--------DSTTGKE----DTGTF--DT 215
Cdd:PRK11749 304 YR----RGREE-MPASEeeVEHAKEEGVEFEWLAAPVEILGDEGRVTGVEFVrmelgepdASGRRRVpiegSEFTLpaDL 378
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1205913889 216 VLWAIGRVPDTRSLNLEKaGVDTSPDTQKILVDSREATSVPHIYAIGDVVEG 267
Cdd:PRK11749 379 VIKAIGQTPNPLILSTTP-GLELNRWGTIIADDETGRTSLPGVFAGGDIVTG 429
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
193-264 |
2.91e-04 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 42.84 E-value: 2.91e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1205913889 193 DGQlQVT---WEDSTTGKEDTGTFDTVLWAIGRVPDTRSLnleKAGVDTSPDTQkILVDSREATSVPHIYAIGDV 264
Cdd:PRK15317 416 DGD-KVTgltYKDRTTGEEHHLELEGVFVQIGLVPNTEWL---KGTVELNRRGE-IIVDARGATSVPGVFAAGDC 485
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
124-280 |
1.19e-03 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 41.16 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 124 KTLVVGASYVALECAGFLTGIGLDTTIMMRsiplRGfDQQMSSMV--IEHMASHGTRFLRGCAPsrVRRLPDG------- 194
Cdd:PRK12831 283 KVAVVGGGNVAMDAARTALRLGAEVHIVYR----RS-EEELPARVeeVHHAKEEGVIFDLLTNP--VEILGDEngwvkgm 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913889 195 ---QLQVTWEDST--------TGKEDTGTFDTVLWAIGRVPDtRSLNLEKAGVDTSPDtQKILVDSRE-ATSVPHIYAIG 262
Cdd:PRK12831 356 kciKMELGEPDASgrrrpveiEGSEFVLEVDTVIMSLGTSPN-PLISSTTKGLKINKR-GCIVADEETgLTSKEGVFAGG 433
|
170
....*....|....*....
gi 1205913889 263 DVVEGrpELTPIAIM-AGR 280
Cdd:PRK12831 434 DAVTG--AATVILAMgAGK 450
|
|
| Met_tRNA_FMT_C |
cd08704 |
C-terminal domain of Formyltransferase and other enzymes; C-terminal domain of formyl ... |
28-94 |
1.23e-03 |
|
C-terminal domain of Formyltransferase and other enzymes; C-terminal domain of formyl transferase and other proteins with diverse enzymatic activities. Proteins found in this family include methionyl-tRNA formyltransferase, ArnA, and 10-formyltetrahydrofolate dehydrogenase. Methionyl-tRNA formyltransferases constitute the majority of the family and also demonstrate greater sequence diversity. Although most proteins with formyltransferase activity contain the C-terminal domain, some formyltransferases ( for example, prokaryotic glycinamide ribonucleotide transformylase (GART)) only have the core catalytic domain, indicating that the C-terminal domain is not a requirement for catalytic activity and may be involved in substrate binding. For example, the C-terminal domain of methionyl-tRNA formyltransferase is involved in the tRNA binding.
Pssm-ID: 187732 [Multi-domain] Cd Length: 87 Bit Score: 37.51 E-value: 1.23e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1205913889 28 DWRKMAEAVQNHVKSLNW--GHRVQLQDRKVKYFniKASFVDEHTvcgVAKGGKEILLSADHIIIATGG 94
Cdd:cd08704 6 DWSKSAEEIHNLIRALNPwpGAYTTLNGKRLKIL--KAEVLEESG---EAAPGTILAVDKKGLLVACGD 69
|
|
| |
