|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
1-561 |
0e+00 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 1146.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 1 MTTLKITGMTCDSCAAHVKEALEKVPGVQSALVSYPKGTAQLAIEAGTSSDALTTAVAGLGYEATLADAPPTDNRAGLLD 80
Cdd:PRK13748 1 MTTLKITGMTCDSCAAHVKDALEKVPGVQSADVSYPKGSAQLAIEVGTSPDALTAAVAGLGYRATLADAPPTDNRGGLLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 81 KMRGWIGAADKPSGNERPLQVVVIGSGGAAMAAALKAVEQGAQVTLIERGTIGGTCVNVGCVPSKIMIRAAHIAHLRRES 160
Cdd:PRK13748 81 KMRGWLGGADKHSGNERPLHVAVIGSGGAAMAAALKAVEQGARVTLIERGTIGGTCVNVGCVPSKIMIRAAHIAHLRRES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 161 PFDGGMPPTPPTILRERLLAQQQARVEELRHAKYEGILDGNSAITVLHGEARFKDDQSLIVSLNEGGERVVMFDRCLVAT 240
Cdd:PRK13748 161 PFDGGIAATVPTIDRSRLLAQQQARVDELRHAKYEGILDGNPAITVLHGEARFKDDQTLIVRLNDGGERVVAFDRCLIAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 241 GASPAVPPIPGLKESPYWTSTEALASDTIPERLAVIGSSVVALELAQAFARLGSKVTALARNTLFFREDPAIGEAVTAAF 320
Cdd:PRK13748 241 GASPAVPPIPGLKETPYWTSTEALVSDTIPERLAVIGSSVVALELAQAFARLGSKVTILARSTLFFREDPAIGEAVTAAF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 321 RAEGIEVLEHTQASQVAHMDGEFVLTTTHGELRADKLLVATGRTPNTRSLALEAAGVAVNAQGAIVIDKGMRTSSPNIYA 400
Cdd:PRK13748 321 RAEGIEVLEHTQASQVAHVDGEFVLTTGHGELRADKLLVATGRAPNTRSLALDAAGVTVNAQGAIVIDQGMRTSVPHIYA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 401 AGDCTDQPQFVYVAAAAGTRAAINMTGGDAALDLTAMPAVVFTDPQVATVGYSEAEAHHDGIETDSRLLTLDNVPRALAN 480
Cdd:PRK13748 401 AGDCTDQPQFVYVAAAAGTRAAINMTGGDAALDLTAMPAVVFTDPQVATVGYSEAEAHHDGIETDSRTLTLDNVPRALAN 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 481 FDTRGFIKLVIEEGSGRLIGVQAVAPEAGELIQTAVLAIRNRMTVQELADQLFPYLTMVEGLKLAAQTFSKDVKQLSCCA 560
Cdd:PRK13748 481 FDTRGFIKLVIEEGSGRLIGVQAVAPEAGELIQTAALAIRNRMTVQELADQLFPYLTMVEGLKLAAQTFNKDVKQLSCCA 560
|
.
gi 446131441 561 G 561
Cdd:PRK13748 561 G 561
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
101-561 |
0e+00 |
|
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: 572.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 101 VVVIGSGGAAMAAALKAVEQGAQVTLIERGTIGGTCVNVGCVPSKIMIRAAHIAHLRRESPFdgGMPPTPPTILRERLLA 180
Cdd:TIGR02053 3 LVIIGSGAAAFAAAIKAAELGASVAMVERGPLGGTCVNVGCVPSKMLLRAAEVAHYARKPPF--GGLAATVAVDFGELLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 181 QQQARVEELRHAKYEGILDGnSAITVLHGEARFKDDQSLIVSLnegGERVVMFDRCLVATGASPAVPPIPGLKESPYWTS 260
Cdd:TIGR02053 81 GKREVVEELRHEKYEDVLSS-YGVDYLRGRARFKDPKTVKVDL---GREVRGAKRFLIATGARPAIPPIPGLKEAGYLTS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 261 TEALASDTIPERLAVIGSSVVALELAQAFARLGSKVTALARNT-LFFREDPAIGEAVTAAFRAEGIEVLEHTQASQVAHm 339
Cdd:TIGR02053 157 EEALALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSDrLLPREEPEISAAVEEALAEEGIEVVTSAQVKAVSV- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 340 DGEFVLTTTH-----GELRADKLLVATGRTPNTRSLALEAAGVAVNAQGAIVIDKGMRTSSPNIYAAGDCTDQPQFVYVA 414
Cdd:TIGR02053 236 RGGGKIITVEkpggqGEVEADELLVATGRRPNTDGLGLEKAGVKLDERGGILVDETLRTSNPGIYAAGDVTGGLQLEYVA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 415 AAAGTRAAINMTGG-DAALDLTAMPAVVFTDPQVATVGYSEAEAHHDGIETDSRLLTLDNVPRALANFDTRGFIKLVIEE 493
Cdd:TIGR02053 316 AKEGVVAAENALGGaNAKLDLLVIPRVVFTDPAVASVGLTEAEAQKAGIECDCRTLPLTNVPRARINRDTRGFIKLVAEP 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446131441 494 GSGRLIGVQAVAPEAGELIQTAVLAIRNRMTVQELADQLFPYLTMVEGLKLAAQTFSKDVKQLSCCAG 561
Cdd:TIGR02053 396 GTGKVLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAEGLKLAAQTFYRDVSKLSCCAG 463
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
101-552 |
6.79e-159 |
|
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: 461.09 E-value: 6.79e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 101 VVVIGSGGAAMAAALKAVEQGAQVTLIERGTIGGTCVNVGCVPSKIMIRAAHIAHLRRESPFDGgMPPTPPTILRERLLA 180
Cdd:COG1249 6 LVVIGAGPGGYVAAIRAAQLGLKVALVEKGRLGGTCLNVGCIPSKALLHAAEVAHEARHAAEFG-ISAGAPSVDWAALMA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 181 QQQARVEELRhAKYEGILDGNsAITVLHGEARFKDDQSLIVSlnegGERVVMFDRCLVATGASPAVPPIPGLKESPYWTS 260
Cdd:COG1249 85 RKDKVVDRLR-GGVEELLKKN-GVDVIRGRARFVDPHTVEVT----GGETLTADHIVIATGSRPRVPPIPGLDEVRVLTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 261 TEALASDTIPERLAVIGSSVVALELAQAFARLGSKVTALAR-NTLFFREDPAIGEAVTAAFRAEGIEVLEHTQASQVAHM 339
Cdd:COG1249 159 DEALELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERgDRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVEKT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 340 DGEFVLTTTHGE----LRADKLLVATGRTPNTRSLALEAAGVAVNAQGAIVIDKGMRTSSPNIYAAGDCTDQPQFVYVAA 415
Cdd:COG1249 239 GDGVTVTLEDGGgeeaVEADKVLVATGRRPNTDGLGLEAAGVELDERGGIKVDEYLRTSVPGIYAIGDVTGGPQLAHVAS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 416 AAGTRAAINMTGGDAA-LDLTAMPAVVFTDPQVATVGYSEAEAHHDGIETDSRLLTLDNVPRALANFDTRGFIKLVIEEG 494
Cdd:COG1249 319 AEGRVAAENILGKKPRpVDYRAIPSVVFTDPEIASVGLTEEEAREAGIDVKVGKFPFAANGRALALGETEGFVKLIADAE 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 446131441 495 SGRLIGVQAVAPEAGELIQTAVLAIRNRMTVQELADQLFPYLTMVEGLKLAAQTFSKD 552
Cdd:COG1249 399 TGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEAALALLGR 456
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
102-553 |
2.10e-118 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 357.98 E-value: 2.10e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 102 VVIGSGGAAMAAALKAVEQGAQVTLIERGTIGGTCVNVGCVPSKIMIRAAHIAHL-RRESPFdGGMPPTPPTILRERLLA 180
Cdd:PRK06370 9 IVIGAGQAGPPLAARAAGLGMKVALIERGLLGGTCVNTGCVPTKTLIASARAAHLaRRAAEY-GVSVGGPVSVDFKAVMA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 181 QQQARVEELRHaKYEGILDGNSAITVLHGEARFKDDQSLIVslnegGERVVMFDRCLVATGASPAVPPIPGLKESPYWTS 260
Cdd:PRK06370 88 RKRRIRARSRH-GSEQWLRGLEGVDVFRGHARFESPNTVRV-----GGETLRAKRIFINTGARAAIPPIPGLDEVGYLTN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 261 TEALASDTIPERLAVIGSSVVALELAQAFARLGSKVTALAR-NTLFFREDPAIGEAVTAAFRAEGIEVLEHTQASQVA-H 338
Cdd:PRK06370 162 ETIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERgPRLLPREDEDVAAAVREILEREGIDVRLNAECIRVErD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 339 MDGEFVLTTTHG---ELRADKLLVATGRTPNTRSLALEAAGVAVNAQGAIVIDKGMRTSSPNIYAAGDCTDQPQFVYVAA 415
Cdd:PRK06370 242 GDGIAVGLDCNGgapEITGSHILVAVGRVPNTDDLGLEAAGVETDARGYIKVDDQLRTTNPGIYAAGDCNGRGAFTHTAY 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 416 AAGTRAAINMT-GGDAALDLTAMPAVVFTDPQVATVGYSEAEAHHDGIETDSRLLTLDNVPRALANFDTRGFIKLVIEEG 494
Cdd:PRK06370 322 NDARIVAANLLdGGRRKVSDRIVPYATYTDPPLARVGMTEAEARKSGRRVLVGTRPMTRVGRAVEKGETQGFMKVVVDAD 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 446131441 495 SGRLIGVQAVAPEAGELIQTAVLAIRNRMTVQELADQLFPYLTMVEGLKLAAQTFSKDV 553
Cdd:PRK06370 402 TDRILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSELIPTLAQALRRTR 460
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
101-546 |
5.21e-113 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 344.08 E-value: 5.21e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 101 VVVIGSGGAAMAAALKAVEQGAQVTLIERGTIGGTCVNVGCVPSKIMIRAAHIAHLRRESPfDGGMPPTPPTILrerlLA 180
Cdd:PRK06292 6 VIVIGAGPAGYVAARRAAKLGKKVALIEKGPLGGTCLNVGCIPSKALIAAAEAFHEAKHAE-EFGIHADGPKID----FK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 181 QQQARVEELRHAKYEGI---LDGNSAITVLHGEARFKDDQSLIVslnegGERVVMFDRCLVATGASpaVPPIPGL---KE 254
Cdd:PRK06292 81 KVMARVRRERDRFVGGVvegLEKKPKIDKIKGTARFVDPNTVEV-----NGERIEAKNIVIATGSR--VPPIPGVwliLG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 255 SPYWTSTEALASDTIPERLAVIGSSVVALELAQAFARLGSKVTALARN-TLFFREDPAIGEAVTAAFRAEgIEVLEHTQA 333
Cdd:PRK06292 154 DRLLTSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGdRILPLEDPEVSKQAQKILSKE-FKIKLGAKV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 334 SQVAHMDGEFVLTTTHG----ELRADKLLVATGRTPNTRSLALEAAGVAVNAQGAIVIDKGMRTSSPNIYAAGDCTDQPQ 409
Cdd:PRK06292 233 TSVEKSGDEKVEELEKGgkteTIEADYVLVATGRRPNTDGLGLENTGIELDERGRPVVDEHTQTSVPGIYAAGDVNGKPP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 410 FVYVAAAAGTRAAINMTGGDAA-LDLTAMPAVVFTDPQVATVGYSEAEAHHDGIETDSRLLTLDNVPRALANFDTRGFIK 488
Cdd:PRK06292 313 LLHEAADEGRIAAENAAGDVAGgVRYHPIPSVVFTDPQIASVGLTEEELKAAGIDYVVGEVPFEAQGRARVMGKNDGFVK 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 446131441 489 LVIEEGSGRLIGVQAVAPEAGELIQTAVLAIRNRMTVQELADQLFPYLTMVEGLKLAA 546
Cdd:PRK06292 393 VYADKKTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPTLSEGLRTAL 450
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
101-546 |
2.20e-100 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 311.31 E-value: 2.20e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 101 VVVIGSGGAAMAAALKAVEQGAQVTLIERGTIGGTCVNVGCVPSKIMIRAAHIAHLRRESPfDGGMPPTPPTILRERLLA 180
Cdd:PRK06416 7 VIVIGAGPGGYVAAIRAAQLGLKVAIVEKEKLGGTCLNRGCIPSKALLHAAERADEARHSE-DFGIKAENVGIDFKKVQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 181 QQQARVEELrHAKYEGILDGNSaITVLHGEARFKDDQSLIVSlNEGGERVVMFDRCLVATGASPAVppIPGLKESPY--W 258
Cdd:PRK06416 86 WKNGVVNRL-TGGVEGLLKKNK-VDIIRGEAKLVDPNTVRVM-TEDGEQTYTAKNIILATGSRPRE--LPGIEIDGRviW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 259 TSTEALASDTIPERLAVIGSSVVALELAQAFARLGSKVT---ALARntLFFREDPAIGEAVTAAFRAEGIEVLEHTQASQ 335
Cdd:PRK06416 161 TSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTiveALPR--ILPGEDKEISKLAERALKKRGIKIKTGAKAKK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 336 VAHMDGEFVLTTTHGE----LRADKLLVATGRTPNTRSLALEAAGVAVNaQGAIVIDKGMRTSSPNIYAAGDCTDQPQFV 411
Cdd:PRK06416 239 VEQTDDGVTVTLEDGGkeetLEADYVLVAVGRRPNTENLGLEELGVKTD-RGFIEVDEQLRTNVPNIYAIGDIVGGPMLA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 412 YVAAAAGTRAAINMTGGDAALDLTAMPAVVFTDPQVATVGYSEAEAHHDGIETDSRLLTLDNVPRALANFDTRGFIKLVI 491
Cdd:PRK06416 318 HKASAEGIIAAEAIAGNPHPIDYRGIPAVTYTHPEVASVGLTEAKAKEEGFDVKVVKFPFAGNGKALALGETDGFVKLIF 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 446131441 492 EEGSGRLIGVQAVAPEAGELIQTAVLAIRNRMTVQELADQLFPYLTMVEGLKLAA 546
Cdd:PRK06416 398 DKKDGEVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEALGEAA 452
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
101-546 |
8.43e-100 |
|
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: 309.96 E-value: 8.43e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 101 VVVIGSGGAAMAAALKAVEQGAQVTLIERGTIGGTCVNVGCVPSKIMIRAAHIAHLRRESPfDGGMPPTPPTILRERLLA 180
Cdd:TIGR01350 4 VIVIGGGPGGYVAAIRAAQLGLKVALVEKEYLGGTCLNVGCIPTKALLHSAEVYDEIKHAK-DLGIEVENVSVDWEKMQK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 181 QQQARVEELRhAKYEGILDGNSaITVLHGEARFKDDQSLIVSlNEGGERVVMFDRCLVATGASPAVPPIPGLKESPY-WT 259
Cdd:TIGR01350 83 RKNKVVKKLV-GGVSGLLKKNK-VTVIKGEAKFLDPGTVSVT-GENGEETLEAKNIIIATGSRPRSLPGPFDFDGKVvIT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 260 STEALASDTIPERLAVIGSSVVALELAQAFARLGSKVTAL-ARNTLFFREDPAIGEAVTAAFRAEGIEVLEHTQASQVAH 338
Cdd:TIGR01350 160 STGALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVIeMLDRILPGEDAEVSKVLQKALKKKGVKILTNTKVTAVEK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 339 MDGEFVLTTTHGE---LRADKLLVATGRTPNTRSLALEAAGVAVNAQGAIVIDKGMRTSSPNIYAAGDCTDQPQFVYVAA 415
Cdd:TIGR01350 240 NDDQVTYENKGGEtetLTGEKVLVAVGRKPNTEGLGLEKLGVELDERGRIVVDEYMRTNVPGIYAIGDVIGGPMLAHVAS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 416 AAGTRAAINMTGGD-AALDLTAMPAVVFTDPQVATVGYSEAEAHHDGIETDSRLLTLDNVPRALANFDTRGFIKLVIEEG 494
Cdd:TIGR01350 320 HEGIVAAENIAGKEpAHIDYDAVPSVIYTDPEVASVGLTEEQAKEAGYDVKIGKFPFAANGKALALGETDGFVKIIADKK 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 446131441 495 SGRLIGVQAVAPEAGELIQTAVLAIRNRMTVQELADQLFPYLTMVEGLKLAA 546
Cdd:TIGR01350 400 TGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEAIKEAA 451
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
121-513 |
1.11e-75 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 246.99 E-value: 1.11e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 121 GAQVTLIERGTIGGTCVNVGCVPSKIMIRAAHIA-HLRRESPfDGGMPPTPPTILRERLLAQQQARVEELrHAKYEGILD 199
Cdd:PRK06116 27 GAKVALIEAKRLGGTCVNVGCVPKKLMWYGAQIAeAFHDYAP-GYGFDVTENKFDWAKLIANRDAYIDRL-HGSYRNGLE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 200 gNSAITVLHGEARFKDDQSLIVslneGGERVVMfDRCLVATGASPAVPPIPGLKESpyWTSTEALASDTIPERLAVIGSS 279
Cdd:PRK06116 105 -NNGVDLIEGFARFVDAHTVEV----NGERYTA-DHILIATGGRPSIPDIPGAEYG--ITSDGFFALEELPKRVAVVGAG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 280 VVALELAQAFARLGSKVTALARNTLFFRE-DPAIGEAVTAAFRAEGIEVLEHTQASQV-AHMDGEFVLTTTHGE-LRADK 356
Cdd:PRK06116 177 YIAVEFAGVLNGLGSETHLFVRGDAPLRGfDPDIRETLVEEMEKKGIRLHTNAVPKAVeKNADGSLTLTLEDGEtLTVDC 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 357 LLVATGRTPNTRSLALEAAGVAVNAQGAIVIDKGMRTSSPNIYAAGDCTDQPQFVYVAAAAGTRAAINMTGG--DAALDL 434
Cdd:PRK06116 257 LIWAIGREPNTDGLGLENAGVKLNEKGYIIVDEYQNTNVPGIYAVGDVTGRVELTPVAIAAGRRLSERLFNNkpDEKLDY 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 435 TAMPAVVFTDPQVATVGYSEAEA----HHDGIET-DSRLLTLDNvprALANFDTRGFIKLVIEEGSGRLIGVQAVAPEAG 509
Cdd:PRK06116 337 SNIPTVVFSHPPIGTVGLTEEEAreqyGEDNVKVyRSSFTPMYT---ALTGHRQPCLMKLVVVGKEEKVVGLHGIGFGAD 413
|
....
gi 446131441 510 ELIQ 513
Cdd:PRK06116 414 EMIQ 417
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
124-529 |
1.14e-71 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 236.39 E-value: 1.14e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 124 VTLIERGTIGGTCVNVGCVPSKIMIRAAHIAHLRRESP---FDGGMPPTPPTILRERLLAqqqaRVEELRHAKYEGILDG 200
Cdd:PRK07846 25 IAIVEKGTFGGTCLNVGCIPTKMFVYAADVARTIREAArlgVDAELDGVRWPDIVSRVFG----RIDPIAAGGEEYRGRD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 201 NSAITVLHGEARFKDDQSLIVSLNE--GGERVVmfdrclVATGASPAVPPIPGLKESPYWTSTEALASDTIPERLAVIGS 278
Cdd:PRK07846 101 TPNIDVYRGHARFIGPKTLRTGDGEeiTADQVV------IAAGSRPVIPPVIADSGVRYHTSDTIMRLPELPESLVIVGG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 279 SVVALELAQAFARLGSKVTALARNTLFFR-EDPAIGEAVTAAFRAEgIEVLEHTQASQVAHMDGEFVLTTTHGE-LRADK 356
Cdd:PRK07846 175 GFIAAEFAHVFSALGVRVTVVNRSGRLLRhLDDDISERFTELASKR-WDVRLGRNVVGVSQDGSGVTLRLDDGStVEADV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 357 LLVATGRTPNTRSLALEAAGVAVNAQGAIVIDKGMRTSSPNIYAAGDCTDQPQFVYVAAAAGTRAAINMTGGDA--ALDL 434
Cdd:PRK07846 254 LLVATGRVPNGDLLDAAAAGVDVDEDGRVVVDEYQRTSAEGVFALGDVSSPYQLKHVANHEARVVQHNLLHPDDliASDH 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 435 TAMPAVVFTDPQVATVGYSEAEAHHDGIETDSRLLTLDNVPRALANFDTRGFIKLVIEEGSGRLIGVQAVAPEAGELIQT 514
Cdd:PRK07846 334 RFVPAAVFTHPQIASVGLTENEARAAGLDITVKVQNYGDVAYGWAMEDTTGFVKLIADRDTGRLLGAHIIGPQASTLIQP 413
|
410
....*....|....*
gi 446131441 515 AVLAIRNRMTVQELA 529
Cdd:PRK07846 414 LIQAMSFGLDAREMA 428
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
101-542 |
1.44e-71 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 235.80 E-value: 1.44e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 101 VVVIGSGGAAMAAALKAVEQGAQVTLIERGTI--GGTCVNVGCVPSKIMIRAAHIAHlrresPFDGGMpptpptilrerl 178
Cdd:PRK07251 6 LIVIGFGKAGKTLAAKLASAGKKVALVEESKAmyGGTCINIGCIPTKTLLVAAEKNL-----SFEQVM------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 179 lAQQQARVEELRhAKYEGILDGNSAiTVLHGEARFKDDQslIVSLNEGGERVVMF-DRCLVATGASPAVPPIPGLKESPY 257
Cdd:PRK07251 69 -ATKNTVTSRLR-GKNYAMLAGSGV-DLYDAEAHFVSNK--VIEVQAGDEKIELTaETIVINTGAVSNVLPIPGLADSKH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 258 -WTSTEALASDTIPERLAVIGSSVVALELAQAFARLGSKVTAL-ARNTLFFREDPAIGEAVTAAFRAEGIEVLEHTQASQ 335
Cdd:PRK07251 144 vYDSTGIQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLdAASTILPREEPSVAALAKQYMEEDGITFLLNAHTTE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 336 VAHMDGEFVLTTTHGELRADKLLVATGRTPNTRSLALEAAGVAVNAQGAIVIDKGMRTSSPNIYAAGDCTDQPQFVYVAA 415
Cdd:PRK07251 224 VKNDGDQVLVVTEDETYRFDALLYATGRKPNTEPLGLENTDIELTERGAIKVDDYCQTSVPGVFAVGDVNGGPQFTYISL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 416 AAGTRAAINMTG-GDAAL-DLTAMPAVVFTDPQVATVGYSEAEAHHDGIETDSRLLTLDNVPRALANFDTRGFIKLVIEE 493
Cdd:PRK07251 304 DDFRIVFGYLTGdGSYTLeDRGNVPTTMFITPPLSQVGLTEKEAKEAGLPYAVKELLVAAMPRAHVNNDLRGAFKVVVNT 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 446131441 494 GSGRLIGVQAVAPEAGELIQTAVLAIRNRMTVQELADQLFPYLTMVEGL 542
Cdd:PRK07251 384 ETKEILGATLFGEGSQEIINLITMAMDNKIPYTYFKKQIFTHPTMAENL 432
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
100-542 |
8.07e-71 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 234.14 E-value: 8.07e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 100 QVVVIGSGGAAMAAALKAVEQGAQVTLIERGT--IGGTCVNVGCVPSKIMIRAAhiahlRRESPFdggmpptpptilrER 177
Cdd:PRK08010 5 QAVIIGFGKAGKTLAVTLAKAGWRVALIEQSNamYGGTCINIGCIPTKTLVHDA-----QQHTDF-------------VR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 178 LLAQQQARVEELRHAKYEGILDGNSaITVLHGEARFKDDQSLIVsLNEGGERVVMFDRCLVATGASPAVPPIPGLKESP- 256
Cdd:PRK08010 67 AIQRKNEVVNFLRNKNFHNLADMPN-IDVIDGQAEFINNHSLRV-HRPEGNLEIHGEKIFINTGAQTVVPPIPGITTTPg 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 257 YWTSTEALASDTIPERLAVIGSSVVALELAQAFARLGSKVTALARNTLFF-REDPAIGEAVTAAFRAEGIEVLEHTQASQ 335
Cdd:PRK08010 145 VYDSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLpREDRDIADNIATILRDQGVDIILNAHVER 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 336 VAHMDGEFVLTTTHGELRADKLLVATGRTPNTRSLALEAAGVAVNAQGAIVIDKGMRTSSPNIYAAGDCTDQPQFVYVAA 415
Cdd:PRK08010 225 ISHHENQVQVHSEHAQLAVDALLIASGRQPATASLHPENAGIAVNERGAIVVDKYLHTTADNIWAMGDVTGGLQFTYISL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 416 AAGTRAAINMTGGD--AALDLTAMPAVVFTDPQVATVGYSEAEAHHDGIETDSRLLTLDNVPRALANFDTRGFIKLVIEE 493
Cdd:PRK08010 305 DDYRIVRDELLGEGkrSTDDRKNVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVAAIPRARVMNDTRGVLKAIVDN 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 446131441 494 GSGRLIGVQAVAPEAGELIQTAVLAIRNRMTVQELADQLFPYLTMVEGL 542
Cdd:PRK08010 385 KTQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESL 433
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
101-546 |
2.13e-70 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 233.66 E-value: 2.13e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 101 VVVIGSGGAAMAAALKAVEQGAQVTLIE-------RGTIGGTCVNVGCVPSKIMIRAAHIAHLRRESPFDGGMPPTPPTI 173
Cdd:PRK06327 7 VVVIGAGPGGYVAAIRAAQLGLKVACIEawknpkgKPALGGTCLNVGCIPSKALLASSEEFENAGHHFADHGIHVDGVKI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 174 LRERLLAQQQARVEELRhAKYEGILDGNSaITVLHGEARF--KDDQSLIVSLNEGGERVVMFDRCLVATGASPAvpPIPG 251
Cdd:PRK06327 87 DVAKMIARKDKVVKKMT-GGIEGLFKKNK-ITVLKGRGSFvgKTDAGYEIKVTGEDETVITAKHVIIATGSEPR--HLPG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 252 LK--ESPYWTSTEALASDTIPERLAVIGSSVVALELAQAFARLGSKVTAL-ARNTLFFREDPAIGEAVTAAFRAEGIEVL 328
Cdd:PRK06327 163 VPfdNKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILeALPAFLAAADEQVAKEAAKAFTKQGLDIH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 329 EHTQASQVAHMDGEFVLTTTHGE-----LRADKLLVATGRTPNTRSLALEAAGVAVNAQGAIVIDKGMRTSSPNIYAAGD 403
Cdd:PRK06327 243 LGVKIGEIKTGGKGVSVAYTDADgeaqtLEVDKLIVSIGRVPNTDGLGLEAVGLKLDERGFIPVDDHCRTNVPNVYAIGD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 404 CTDQPQFVYVAAAAGTRAAINMTGGDAALDLTAMPAVVFTDPQVATVGYSEAEAHHDGIETDSRLLTLDNVPRALANFDT 483
Cdd:PRK06327 323 VVRGPMLAHKAEEEGVAVAERIAGQKGHIDYNTIPWVIYTSPEIAWVGKTEQQLKAEGVEYKAGKFPFMANGRALAMGEP 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446131441 484 RGFIKLVIEEGSGRLIGVQAVAPEAGELIQTAVLAIRNRMTVQELADQLFPYLTMVEGLKLAA 546
Cdd:PRK06327 403 DGFVKIIADAKTDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLSEVWHEAA 465
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
100-413 |
8.63e-65 |
|
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: 213.72 E-value: 8.63e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 100 QVVVIGSGGAAMAAALKAVEQGAQVTLIERGtigGTCVNVGCVPSKIMIRAAHIAHLRREspfdggmpptpptilRERLL 179
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGGKVTLIEDE---GTCPYGGCVLSKALLGAAEAPEIASL---------------WADLY 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 180 AQQQARVEELRHaKYEGILdGNSAITVLHGEARFKDDQslivsLNEGGERVVMFDRCLVATGASPAVPPIPGLKESP--- 256
Cdd:pfam07992 64 KRKEEVVKKLNN-GIEVLL-GTEVVSIDPGAKKVVLEE-----LVDGDGETITYDRLVIATGARPRLPPIPGVELNVgfl 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 257 --YWTSTEALASDTIPERLAVIGSSVVALELAQAFARLGSKVTAL-ARNTLFFREDPAIGEAVTAAFRAEGIEVLEHTQA 333
Cdd:pfam07992 137 vrTLDSAEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIeALDRLLRAFDEEISAALEKALEKNGVEVRLGTSV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 334 SQVAHMDGEFVLTTTHG-ELRADKLLVATGRTPNTRslALEAAGVAVNAQGAIVIDKGMRTSSPNIYAAGDCT-DQPQFV 411
Cdd:pfam07992 217 KEIIGDGDGVEVILKDGtEIDADLVVVAIGRRPNTE--LLEAAGLELDERGGIVVDEYLRTSVPGIYAAGDCRvGGPELA 294
|
..
gi 446131441 412 YV 413
Cdd:pfam07992 295 QN 296
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
101-530 |
9.36e-64 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 215.88 E-value: 9.36e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 101 VVVIGSGGAAMAAALKAVEQGAQVTLIERGTIGGTCVNVGCVPSKIMIRAAHIAHLRRESPFDGGMPPTPPTILRErlLA 180
Cdd:PRK07845 4 IVIIGGGPGGYEAALVAAQLGADVTVIERDGLGGAAVLTDCVPSKTLIATAEVRTELRRAAELGIRFIDDGEARVD--LP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 181 QQQARVEELRHAKYEGILDG--NSAITVLHGEARFKDD----QSLIVSLNEGGERVVMFDRCLVATGASPAVPP--IPGL 252
Cdd:PRK07845 82 AVNARVKALAAAQSADIRARleREGVRVIAGRGRLIDPglgpHRVKVTTADGGEETLDADVVLIATGASPRILPtaEPDG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 253 KESPYWTSTEALasDTIPERLAVIGSSVVALELAQAFARLGSKVTALA-RNTLFFREDPAIGEAVTAAFRAEGIEVLEHT 331
Cdd:PRK07845 162 ERILTWRQLYDL--DELPEHLIVVGSGVTGAEFASAYTELGVKVTLVSsRDRVLPGEDADAAEVLEEVFARRGMTVLKRS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 332 QASQVAHMDGEFVLTTTHG-ELRADKLLVATGRTPNTRSLALEAAGVAVNAQGAIVIDKGMRTSSPNIYAAGDCTDQPQF 410
Cdd:PRK07845 240 RAESVERTGDGVVVTLTDGrTVEGSHALMAVGSVPNTAGLGLEEAGVELTPSGHITVDRVSRTSVPGIYAAGDCTGVLPL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 411 VYVAAaagtraainMTG--------GDAA--LDLTAMPAVVFTDPQVATVGYSEAEAHHDGIETDSRLLTLDNVPRALAN 480
Cdd:PRK07845 320 ASVAA---------MQGriamyhalGEAVspLRLKTVASNVFTRPEIATVGVSQAAIDSGEVPARTVMLPLATNPRAKMS 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 446131441 481 FDTRGFIKLVIEEGSGRLIGVQAVAPEAGELIQTAVLAIRNRMTVQELAD 530
Cdd:PRK07845 391 GLRDGFVKLFCRPGTGVVIGGVVVAPRASELILPIALAVQNRLTVDDLAQ 440
|
|
| gluta_reduc_2 |
TIGR01424 |
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, ... |
103-520 |
9.24e-56 |
|
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, e.g., for maintaining the cellular thiol/disulfide status and for protecting against reactive oxygen species such as hydrogen peroxide. Glutathione-disulfide reductase regenerates reduced glutathione from oxidized glutathione (glutathione disulfide) + NADPH. This model represents one of two closely related subfamilies of glutathione-disulfide reductase. Both are closely related to trypanothione reductase, and separate models are built so each of the three can describe proteins with conserved function. This model describes glutathione-disulfide reductases of plants and some bacteria, including cyanobacteria. [Energy metabolism, Electron transport]
Pssm-ID: 213618 [Multi-domain] Cd Length: 446 Bit Score: 194.26 E-value: 9.24e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 103 VIGSGGAAMAAALKAVEQGAQVTLIERGTIGGTCVNVGCVPSKIMIRAAHI-AHLRRESPFdgGMPPTPPTILRERLLAQ 181
Cdd:TIGR01424 7 VIGAGSGGVRAARLAAALGAKVAIAEEFRVGGTCVIRGCVPKKLMVYASQFaEHFEDAAGY--GWTVGKARFDWKKLLAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 182 QQARVEELRHAKYEGIldGNSAITVLHGEARFKDDQSliVSLNEGGeRVVMFDRCLVATGASPAVPPIPGLKESpyWTST 261
Cdd:TIGR01424 85 KDQEIARLSGLYRKGL--ANAGAELLDGRAELVGPNT--VEVLASG-KTYTAEKILIAVGGRPPKPALPGHELG--ITSN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 262 EALASDTIPERLAVIGSSVVALELAQAFARLGSKVTALARNTLFFRE-DPAIGEAVTAAFRAEGIEVL---EHTQASQVA 337
Cdd:TIGR01424 158 EAFHLPTLPKSILIAGGGYIAVEFAGIFRGLGVQTTLIYRGKEILRGfDDDMRRGLAAALEERGIRILpedSITSISKDD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 338 hmDGEFVLTTTHG-ELRADKLLVATGRTPNTRSLALEAAGVAVNAQGAIVIDKGMRTSSPNIYAAGDCTDQPQFVYVAAA 416
Cdd:TIGR01424 238 --DGRLKATLSKHeEIVADVVLFATGRSPNTNGLGLEAAGVRLNDLGAIAVDEYSRTSTPSIYAVGDVTDRINLTPVAIH 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 417 AGTRAAINMTGGD-AALDLTAMPAVVFTDPQVATVGYSEAEAHHDGIETDSRLLTLDNVPRALANFDTRGFIKLVIEEGS 495
Cdd:TIGR01424 316 EATCFAETEFGNNpTSFDHDLIATAVFSQPPIGTVGLTEEEARRKFGDIEVYRAEFRPMKATFSGRQEKTLMKLVVDAKD 395
|
410 420
....*....|....*....|....*
gi 446131441 496 GRLIGVQAVAPEAGELIQTAVLAIR 520
Cdd:TIGR01424 396 DKVLGAHMVGPDAAEIIQGLAIALK 420
|
|
| gluta_reduc_1 |
TIGR01421 |
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ... |
102-520 |
5.15e-54 |
|
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important reductant, e.g., for maintaining the cellular thiol/disulfide status and for protecting against reactive oxygen species such as hydrogen peroxide. Glutathione-disulfide reductase regenerates reduced glutathione from oxidized glutathione (glutathione disulfide) + NADPH. This model represents one of two closely related subfamilies of glutathione-disulfide reductase. Both are closely related to trypanothione reductase, and separate models are built so each of the three can describe proteins with conserved function. This model describes glutathione-disulfide reductases of animals, yeast, and a number of animal-resident bacteria. [Energy metabolism, Electron transport]
Pssm-ID: 273614 [Multi-domain] Cd Length: 450 Bit Score: 189.67 E-value: 5.15e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 102 VVIGSGGAAMAAALKAVEQGAQVTLIERGTIGGTCVNVGCVPSKIMIRAAHIAHlRRESPFDGGMPPTPPTILRERLLAQ 181
Cdd:TIGR01421 6 LVIGGGSGGIASARRAAEHGAKALLVEAKKLGGTCVNVGCVPKKVMWYASDLAE-RMHDAADYGFYQNDENTFNWPELKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 182 QQARVEELRHAKYEGILDGNSaITVLHGEARFKDDQSLIVSlneggERVVMFDRCLVATGASPAVPP-IPGlkESPYWTS 260
Cdd:TIGR01421 85 KRDAYVDRLNGIYQKNLEKNK-VDVIFGHARFTKDGTVEVN-----GRDYTAPHILIATGGKPSFPEnIPG--AELGTDS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 261 TEALASDTIPERLAVIGSSVVALELAQAFARLGSKVTALARNTLFFRE-DPAIGEAVTAAFRAEGIEVLEHTQASQVAH- 338
Cdd:TIGR01421 157 DGFFALEELPKRVVIVGAGYIAVELAGVLHGLGSETHLVIRHERVLRSfDSMISETITEEYEKEGINVHKLSKPVKVEKt 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 339 MDGEFVLTTTHGEL--RADKLLVATGRTPNTRSLALEAAGVAVNAQGAIVIDKGMRTSSPNIYAAGDCTDQPQFVYVAAA 416
Cdd:TIGR01421 237 VEGKLVIHFEDGKSidDVDELIWAIGRKPNTKGLGLENVGIKLNEKGQIIVDEYQNTNVPGIYALGDVVGKVELTPVAIA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 417 AGTRAAINMTGG--DAALDLTAMPAVVFTDPQVATVGYSEAEAHH----DGIETDSRLLTldNVPRALANFDTRGFIKLV 490
Cdd:TIGR01421 317 AGRKLSERLFNGktDDKLDYNNVPTVVFSHPPIGTIGLTEKEAIEkygkENIKVYNSSFT--PMYYAMTSEKQKCRMKLV 394
|
410 420 430
....*....|....*....|....*....|
gi 446131441 491 IEEGSGRLIGVQAVAPEAGELIQTAVLAIR 520
Cdd:TIGR01421 395 CAGKEEKVVGLHGIGDGVDEMLQGFAVAIK 424
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
101-546 |
1.91e-52 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 185.36 E-value: 1.91e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 101 VVVIGSGGAAMAAALKAVEQGAQVTLIERGT-IGGTCVNVGCVPSKIMIRAA-HIAHLRRESPFDGGMPP---TPPTILR 175
Cdd:PRK05249 8 LVVIGSGPAGEGAAMQAAKLGKRVAVIERYRnVGGGCTHTGTIPSKALREAVlRLIGFNQNPLYSSYRVKlriTFADLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 176 --ERLLAQQqarVEELRHAkyegiLDGNSaITVLHGEARFKDDQSLIVSLNEGGERVVMFDRCLVATGASPAVPP-IPGL 252
Cdd:PRK05249 88 raDHVINKQ---VEVRRGQ-----YERNR-VDLIQGRARFVDPHTVEVECPDGEVETLTADKIVIATGSRPYRPPdVDFD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 253 KESPYwTSTEALASDTIPERLAVIGSSVVALELAQAFARLGSKVTAL-ARNTLFFREDPAIGEAVTAAFRAEGIEVLEHT 331
Cdd:PRK05249 159 HPRIY-DSDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLInTRDRLLSFLDDEISDALSYHLRDSGVTIRHNE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 332 QASQVAHMDGEFVLTTTHG-ELRADKLLVATGRTPNTRSLALEAAGVAVNAQGAIVIDKGMRTSSPNIYAAGDCT----- 405
Cdd:PRK05249 238 EVEKVEGGDDGVIVHLKSGkKIKADCLLYANGRTGNTDGLNLENAGLEADSRGQLKVNENYQTAVPHIYAVGDVIgfpsl 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 406 -----DQPQFVyvaaaagtraAINMTGGDAALDLTAMPAVVFTDPQVATVGYSEAEahhdgietdsrlLTLDNVP----- 475
Cdd:PRK05249 318 asasmDQGRIA----------AQHAVGEATAHLIEDIPTGIYTIPEISSVGKTEQE------------LTAAKVPyevgr 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 476 -------RALANFDTRGFIKLVIEEGSGRLIGVQAVAPEAGELIQT--AVLAIRNrmTVQELADQLFPYLTMVEGLKLAA 546
Cdd:PRK05249 376 arfkelaRAQIAGDNVGMLKILFHRETLEILGVHCFGERATEIIHIgqAIMEQKG--TIEYFVNTTFNYPTMAEAYRVAA 453
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
103-520 |
3.60e-47 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 171.92 E-value: 3.60e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 103 VIGSGGAAMAAALKAVEQGAQVTLIE----------RGTIGGTCVNVGCVPSKIMIRAAHIAHLRRESPFDGGMPPTPPT 172
Cdd:PLN02507 30 VIGAGSGGVRAARFSANFGAKVGICElpfhpissesIGGVGGTCVIRGCVPKKILVYGATFGGEFEDAKNYGWEINEKVD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 173 ILRERLLAQQQARVEELrHAKYEGILdGNSAITVLHGEARFKDDQSLIVSLNEGGERVVMFDRCLVATGASPAVPPIPGl 252
Cdd:PLN02507 110 FNWKKLLQKKTDEILRL-NGIYKRLL-ANAGVKLYEGEGKIVGPNEVEVTQLDGTKLRYTAKHILIATGSRAQRPNIPG- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 253 KESPYwTSTEALASDTIPERLAVIGSSVVALELAQAFARLGSKVTALARNTLFFRE-DPAIGEAVTAAFRAEGIEVLEHT 331
Cdd:PLN02507 187 KELAI-TSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGfDDEMRAVVARNLEGRGINLHPRT 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 332 QASQVAHMDGEFVLTTTHG-ELRADKLLVATGRTPNTRSLALEAAGVAVNAQGAIVIDKGMRTSSPNIYAAGDCTDQPQF 410
Cdd:PLN02507 266 NLTQLTKTEGGIKVITDHGeEFVADVVLFATGRAPNTKRLNLEAVGVELDKAGAVKVDEYSRTNIPSIWAIGDVTNRINL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 411 VYVAAAAGTRAAINMTGGDAAL-DLTAMPAVVFTDPQVATVGYSEAEAhHDGIETDSRLLTLDNVP--RALANFDTRGFI 487
Cdd:PLN02507 346 TPVALMEGTCFAKTVFGGQPTKpDYENVACAVFCIPPLSVVGLSEEEA-VEQAKGDILVFTSSFNPmkNTISGRQEKTVM 424
|
410 420 430
....*....|....*....|....*....|...
gi 446131441 488 KLVIEEGSGRLIGVQAVAPEAGELIQTAVLAIR 520
Cdd:PLN02507 425 KLIVDAETDKVLGASMCGPDAPEIMQGIAVALK 457
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
75-527 |
3.51e-46 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 170.44 E-value: 3.51e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 75 RAGLLDKMRGWIGAADKPSGNERP----LQVVVIGSGGAAMAAALKAVEQGAQVTLIE----------RGTIGGTCVNVG 140
Cdd:PLN02546 52 RPLSHHHRRRSVSRAAAPNGAESErhydFDLFTIGAGSGGVRASRFASNFGASAAVCElpfatissdtLGGVGGTCVLRG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 141 CVPSKIMIRAAHIAHLRRESPFDGGMPPTPPTILRERLLAQQQARVEELRhAKYEGILDgNSAITVLHGEARFKDDQSLI 220
Cdd:PLN02546 132 CVPKKLLVYASKYSHEFEESRGFGWKYETEPKHDWNTLIANKNAELQRLT-GIYKNILK-NAGVTLIEGRGKIVDPHTVD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 221 VSLNEGGERVVmfdrcLVATGASPAVPPIPGLKESpyWTSTEALASDTIPERLAVIGSSVVALELAQAFARLGSKVTALA 300
Cdd:PLN02546 210 VDGKLYTARNI-----LIAVGGRPFIPDIPGIEHA--IDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHVFI 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 301 RNTLFFRE-DPAIGEAVTAAFRAEGIEVleHTQASQVAHM---DGEFVLTTTHGELRA-DKLLVATGRTPNTRSLALEAA 375
Cdd:PLN02546 283 RQKKVLRGfDEEVRDFVAEQMSLRGIEF--HTEESPQAIIksaDGSLSLKTNKGTVEGfSHVMFATGRKPNTKNLGLEEV 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 376 GVAVNAQGAIVIDKGMRTSSPNIYAAGDCTDQPQFVYVAAaagtraainMTGGDAAL----------DLTAMPAVVFTDP 445
Cdd:PLN02546 361 GVKMDKNGAIEVDEYSRTSVPSIWAVGDVTDRINLTPVAL---------MEGGALAKtlfgneptkpDYRAVPSAVFSQP 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 446 QVATVGYSEAEAHHDGIETDSRLLTLDNVPRALANFDTRGFIKLVIEEGSGRLIGVQAVAPEAGELIQTAVLAIRNRMTV 525
Cdd:PLN02546 432 PIGQVGLTEEQAIEEYGDVDVFTANFRPLKATLSGLPDRVFMKLIVCAKTNKVLGVHMCGEDAPEIIQGFAVAVKAGLTK 511
|
..
gi 446131441 526 QE 527
Cdd:PLN02546 512 AD 513
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
102-528 |
5.24e-44 |
|
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: 163.10 E-value: 5.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 102 VVIGSGGAAMAAALKAVEQGAQVTLIE------RGT---IGGTCVNVGCVPSKIMIRAAHIAHLRRESPFDGGMPPTPPT 172
Cdd:TIGR01438 6 IVIGGGSGGLAAAKEAAAYGAKVMLLDfvtptpLGTrwgIGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKVEETVK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 173 ILRERLLAQQQARVEELRHAKYEGIldGNSAITVLHGEARFKDDQSLIVSLNEGGERVVMFDRCLVATGASPAVPPIPGL 252
Cdd:TIGR01438 86 HDWKRLVEAVQNHIGSLNWGYRVAL--REKKVKYENAYAEFVDKHRIKATNKKGKEKIYSAERFLIATGERPRYPGIPGA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 253 KEspYWTSTEALAS-DTIPERLAVIGSSVVALELAQAFARLGSKVTALARNTLFFREDPAIGEAVTAAFRAEGIEVLEHT 331
Cdd:TIGR01438 164 KE--LCITSDDLFSlPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDCANKVGEHMEEHGVKFKRQF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 332 QASQVAHMDGEFVLTTTH----GELRADKLLVATGRTPNTRSLALEAAGVAVNAQ-GAIVIDKGMRTSSPNIYAAGDCT- 405
Cdd:TIGR01438 242 VPIKVEQIEAKVLVEFTDstngIEEEYDTVLLAIGRDACTRKLNLENVGVKINKKtGKIPADEEEQTNVPYIYAVGDILe 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 406 DQPQFVYVAAAAGTRAAINMTGG-DAALDLTAMPAVVFTDPQVATVGYSEAEAHH----DGIETDSRLLTldNVPRALAN 480
Cdd:TIGR01438 322 DKPELTPVAIQAGRLLAQRLFKGsTVICDYENVPTTVFTPLEYGACGLSEEKAVEkfgeENVEVFHSYFW--PLEWTIPS 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 446131441 481 FDTRGF--IKLV-IEEGSGRLIGVQAVAPEAGELIQTAVLAIRNRMTVQEL 528
Cdd:TIGR01438 400 RDNHNKcyAKLVcNKKENERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDL 450
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
97-520 |
3.08e-43 |
|
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: 160.91 E-value: 3.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 97 RPLQVVVIGSG-GAAMAAALKAVEQGAQVTLIERGT---------IGGTCVNVGCVPSKIMIRAA-HIAHLRRESPFDGG 165
Cdd:TIGR01423 2 KAFDLVVIGAGsGGLEAGWNAATLYKKRVAVVDVQThhgppfyaaLGGTCVNVGCVPKKLMVTGAqYMDTLRESAGFGWE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 166 MPPTPPTILRERLLAQQQARVEELRHAkYEGILDGNSAITVLHGEARFKDDQSLIVSLNEGGERVVM----FDRCLVATG 241
Cdd:TIGR01423 82 FDRSSVKANWKALIAAKNKAVLDINKS-YEGMFADTEGLTFFLGWGALEDKNVVLVRESADPKSAVKerlqAEHILLATG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 242 ASPAVPPIPGLKESpyWTSTEALASDTIPERLAVIGSSVVALELA---QAFARLGSKVTALARNTLFFRE-DPAIGEAVT 317
Cdd:TIGR01423 161 SWPQMLGIPGIEHC--ISSNEAFYLDEPPRRVLTVGGGFISVEFAgifNAYKPRGGKVTLCYRNNMILRGfDSTLRKELT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 318 AAFRAEGIEVLEHTQASQVA-HMDGEFVLTTTHG-ELRADKLLVATGRTPNTRSLALEAAGVAVNAQGAIVIDKGMRTSS 395
Cdd:TIGR01423 239 KQLRANGINIMTNENPAKVTlNADGSKHVTFESGkTLDVDVVMMAIGRVPRTQTLQLDKVGVELTKKGAIQVDEFSRTNV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 396 PNIYAAGDCTDQPQFVYVAAAAGTRAAINMTGGDA-ALDLTAMPAVVFTDPQVATVGYSEAEAHHDGIETDSRLLTLDNV 474
Cdd:TIGR01423 319 PNIYAIGDVTDRVMLTPVAINEGAAFVDTVFGNKPrKTDHTRVASAVFSIPPIGTCGLVEEDAAKKFEKVAVYESSFTPL 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 446131441 475 PRALANFDTRGFI-KLVIEEGSGRLIGVQAVAPEAGELIQTAVLAIR 520
Cdd:TIGR01423 399 MHNISGSKYKKFVaKIVTNHADGTVLGVHLLGDSSPEIIQAVGICLK 445
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
233-411 |
2.11e-34 |
|
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: 132.63 E-value: 2.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 233 FDRCLVATGASPAVPPIPGLKESPYWT--------STEALASDTIPERLAVIGSSVVALELAQAFARLGSKVTALARN-T 303
Cdd:COG0446 79 YDKLVLATGARPRPPPIPGLDLPGVFTlrtlddadALREALKEFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERApR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 304 LFFREDPAIGEAVTAAFRAEGIEVLEHTQASQVAHMDGEFVLTTTHGELRADKLLVATGRTPNTrSLAlEAAGVAVNAQG 383
Cdd:COG0446 159 LLGVLDPEMAALLEEELREHGVELRLGETVVAIDGDDKVAVTLTDGEEIPADLVVVAPGVRPNT-ELA-KDAGLALGERG 236
|
170 180
....*....|....*....|....*...
gi 446131441 384 AIVIDKGMRTSSPNIYAAGDCTDQPQFV 411
Cdd:COG0446 237 WIKVDETLQTSDPDVYAAGDCAEVPHPV 264
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
102-520 |
2.44e-34 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 136.11 E-value: 2.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 102 VVIGSGGAAMAAALKAVEQGAQVTLIE------RGT---IGGTCVNVGCVPSKIMIRAAHIAHL----------RRESPF 162
Cdd:PTZ00052 9 VVIGGGSGGMAAAKEAAAHGKKVALFDyvkpstQGTkwgLGGTCVNVGCVPKKLMHYAANIGSIfhhdsqmygwKTSSSF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 163 DGGmpptpptilreRLLAQQQARVEELRHAKYEGILDGNsaITVLHGEARFKDDQSLIVSLNeGGERVVMFDRCLVATGA 242
Cdd:PTZ00052 89 NWG-----------KLVTTVQNHIRSLNFSYRTGLRSSK--VEYINGLAKLKDEHTVSYGDN-SQEETITAKYILIATGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 243 SPAVP-PIPGLKESPYwTSTEALASDTIPERLAVIGSSVVALELAQAFARLGSKVTALARNTLFFREDPAIGEAVTAAFR 321
Cdd:PTZ00052 155 RPSIPeDVPGAKEYSI-TSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVAVRSIPLRGFDRQCSEKVVEYMK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 322 AEGIEVLEHTQASQVAHMDGEFVLTTTHGELRA-DKLLVATGRTPNTRSLALEAAGVAVNAQGAIVIDKGMrTSSPNIYA 400
Cdd:PTZ00052 234 EQGTLFLEGVVPINIEKMDDKIKVLFSDGTTELfDTVLYATGRKPDIKGLNLNAIGVHVNKSNKIIAPNDC-TNIPNIFA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 401 AGDCT-DQPQFVYVAAAAGTRAAINMTGG-DAALDLTAMPAVVFTDPQVATVGYSEAEAHHDGIETD-----SRLLTLD- 472
Cdd:PTZ00052 313 VGDVVeGRPELTPVAIKAGILLARRLFKQsNEFIDYTFIPTTIFTPIEYGACGYSSEAAIAKYGEDDieeylQEFNTLEi 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 473 ------NVPRALAN-FDT----RGFIKLVIEEGSG-RLIGVQAVAPEAGELIQTAVLAIR 520
Cdd:PTZ00052 393 aavhreKHERARKDeYDFdvssNCLAKLVCVKSEDnKVVGFHFVGPNAGEITQGFSLALK 452
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
437-545 |
1.39e-33 |
|
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: 123.43 E-value: 1.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 437 MPAVVFTDPQVATVGYSEAEAHHDGIETDSRLLTLDNVPRALANFDTRGFIKLVIEEGSGRLIGVQAVAPEAGELIQTAV 516
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGGEVKVGKFPFAANGRALAYGDTDGFVKLVADRETGKILGAHIVGPNAGELIQEAA 80
|
90 100
....*....|....*....|....*....
gi 446131441 517 LAIRNRMTVQELADQLFPYLTMVEGLKLA 545
Cdd:pfam02852 81 LAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
102-528 |
2.24e-32 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 131.28 E-value: 2.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 102 VVIGSGGAAMAAALKAVEQGAQVTLIERGTIGGTCVNVGCVPSKIMIRAAHIAHLRRES---PFDGGMPPTPPTIL--RE 176
Cdd:PTZ00058 52 IVIGGGSGGMAAARRAARNKAKVALVEKDYLGGTCVNVGCVPKKIMFNAASIHDILENSrhyGFDTQFSFNLPLLVerRD 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 177 RLLAQ---------QQARVEELRHAKY---EGILDGNSAITVLHGEARFKDDQSLIVSLNEGGE---RVVMFDRCLVATG 241
Cdd:PTZ00058 132 KYIRRlndiyrqnlKKDNVEYFEGKGSllsENQVLIKKVSQVDGEADESDDDEVTIVSAGVSQLddgQVIEGKNILIAVG 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 242 ASPAVPPIPGLKESpywTSTEALASDTIPERLAVIGSSVVALELAQAFARLGSKVTALARNTLFFRE-DPAIGEAVTAAF 320
Cdd:PTZ00058 212 NKPIFPDVKGKEFT---ISSDDFFKIKEAKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLLRKfDETIINELENDM 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 321 RAEGIEVLEHTQASQVAHMDGEFVLT---TTHGELRADKLLVATGRTPNTRSLALEAAGVaVNAQGAIVIDKGMRTSSPN 397
Cdd:PTZ00058 289 KKNNINIITHANVEEIEKVKEKNLTIylsDGRKYEHFDYVIYCVGRSPNTEDLNLKALNI-KTPKGYIKVDDNQRTSVKH 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 398 IYAAGDC--------TDQPQFVYVAAAAGTRAAINMTGGDAA--LDLT-------------------------AMPAVVF 442
Cdd:PTZ00058 368 IYAVGDCcmvkknqeIEDLNLLKLYNEEPYLKKKENTSGESYynVQLTpvainagrlladrlfgpfsrttnykLIPSVIF 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 443 TDPQVATVGYSEAEA----HHDGIET-DSRLLTLdnvprALANFDT------RGFIKLVIEEGSGRLIGVQAVAPEAGEL 511
Cdd:PTZ00058 448 SHPPIGTIGLSEQEAidiyGKENVKIyESRFTNL-----FFSVYDMdpaqkeKTYLKLVCVGKEELIKGLHIVGLNADEI 522
|
490
....*....|....*..
gi 446131441 512 IQTAVLAIRNRMTVQEL 528
Cdd:PTZ00058 523 LQGFAVALKMNATKADF 539
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
225-534 |
1.54e-31 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 126.41 E-value: 1.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 225 EGGERVVmFDRCLVATGASPAVPPIPGLkESP----YWT--STEALASDTIP-ERLAVIGSSVVALELAQAFARLGSKVT 297
Cdd:COG1251 92 ADGETLP-YDKLVLATGSRPRVPPIPGA-DLPgvftLRTldDADALRAALAPgKRVVVIGGGLIGLEAAAALRKRGLEVT 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 298 ALARNTLFFRE--DPAIGEAVTAAFRAEGIEVLEHTQASQVAHMDGEFVLTTTHGE-LRADKLLVATGRTPNTrSLAlEA 374
Cdd:COG1251 170 VVERAPRLLPRqlDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTGVRLADGEeLPADLVVVAIGVRPNT-ELA-RA 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 375 AGVAVNaqGAIVIDKGMRTSSPNIYAAGDCTDQPQFVYVAAAAGTRAAI---------NMTGGDAALDlTAMPAVV--FT 443
Cdd:COG1251 248 AGLAVD--RGIVVDDYLRTSDPDIYAAGDCAEHPGPVYGRRVLELVAPAyeqarvaaaNLAGGPAAYE-GSVPSTKlkVF 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 444 DPQVATVGYSEAeahhdgietDSRLLTLDNVPRalanfdtRGFIKLVIEEgsGRLIGVQAV--APEAGELIQtavlAIRN 521
Cdd:COG1251 325 GVDVASAGDAEG---------DEEVVVRGDPAR-------GVYKKLVLRD--GRLVGAVLVgdTSDAGALRQ----LIKN 382
|
330
....*....|....*
gi 446131441 522 RMTV--QELADQLFP 534
Cdd:COG1251 383 GRPLppRALLDAALP 397
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
213-535 |
3.24e-29 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 120.15 E-value: 3.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 213 FKDDQSLIVSLNEGGERVVMFDRCLVATGASPAVPPIPGLKESPYWTSTE--------ALASDTIPERLAVIGSSVVALE 284
Cdd:PRK09564 84 AKNKTITVKNLKTGSIFNDTYDKLMIATGARPIIPPIKNINLENVYTLKSmedglalkELLKDEEIKNIVIIGAGFIGLE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 285 LAQAFARLGSKVTALARNTLFFRE--DPAIGEAVTAAFRAEGIEVleHTQASqVAHMDGE---FVLTTTHGELRADKLLV 359
Cdd:PRK09564 164 AVEAAKHLGKNVRIIQLEDRILPDsfDKEITDVMEEELRENGVEL--HLNEF-VKSLIGEdkvEGVVTDKGEYEADVVIV 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 360 ATGRTPNTRslALEAAGVAVNAQGAIVIDKGMRTSSPNIYAAGDC-------TDQPQFVYVAAAAGTRAAI---NMTGGD 429
Cdd:PRK09564 241 ATGVKPNTE--FLEDTGLKTLKNGAIIVDEYGETSIENIYAAGDCatiynivSNKNVYVPLATTANKLGRMvgeNLAGRH 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 430 AAL--DLTAMPAVVFtDPQVATVGYSEAEAHHDGIETDSRLLTLDNVPRALANFDTRgFIKLVIEEGSGRLIGVQAVApE 507
Cdd:PRK09564 319 VSFkgTLGSACIKVL-DLEAARTGLTEEEAKKLGIDYKTVFIKDKNHTNYYPGQEDL-YVKLIYEADTKVILGGQIIG-K 395
|
330 340 350
....*....|....*....|....*....|
gi 446131441 508 AGELIQTAVLA--IRNRMTVQELADQLFPY 535
Cdd:PRK09564 396 KGAVLRIDALAvaIYAKLTTQELGMMDFCY 425
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
95-551 |
1.06e-28 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 120.79 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 95 NERPLQVVVIGSGGAAMAAALKAVEQGAQVTLIERG--TIGGTCVNVGCVPSKIMIRAA-------HIAHLRRESPFDGG 165
Cdd:PTZ00153 113 SDEEYDVGIIGCGVGGHAAAINAMERGLKVIIFTGDddSIGGTCVNVGCIPSKALLYATgkyrelkNLAKLYTYGIYTNA 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 166 MPPTPPT-ILRERLLAQQ------------QARVEELRHakyeGILDG--------NSAITVLHGEARFKDDQSLIVSLN 224
Cdd:PTZ00153 193 FKNGKNDpVERNQLVADTvqiditklkeytQSVIDKLRG----GIENGlkskkfckNSEHVQVIYERGHIVDKNTIKSEK 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 225 EGGERVVmfDRCLVATGASPAVPPIPGLKESPYWTSTEALASDTIPERLAVIGSSVVALELAQAFARLGSKVTALARNT- 303
Cdd:PTZ00153 269 SGKEFKV--KNIIIATGSTPNIPDNIEVDQKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVSFEYSPq 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 304 ---------------LFFREDP------AIGEAVTAAFRAEGIEVlEHTQAsQVAHMDGEFVLTTTHGELRADKLLVATG 362
Cdd:PTZ00153 347 llplldadvakyferVFLKSKPvrvhlnTLIEYVRAGKGNQPVII-GHSER-QTGESDGPKKNMNDIKETYVDSCLVATG 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 363 RTPNTRSLALEAAGVAVNaQGAIVIDKGMRTSSP------NIYAAGDCTDQPQFVYVAAAAGTRAAINMTG-GDAALDLT 435
Cdd:PTZ00153 425 RKPNTNNLGLDKLKIQMK-RGFVSVDEHLRVLREdqevydNIFCIGDANGKQMLAHTASHQALKVVDWIEGkGKENVNIN 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 436 A------------MPAVVFTDPQVATVGYSEAEA------HHDGIET-----DSRLLTLDNVP-------------RALA 479
Cdd:PTZ00153 504 VenwaskpiiyknIPSVCYTTPELAFIGLTEKEAkelyppDNVGVEIsfykaNSKVLCENNISfpnnsknnsynkgKYNT 583
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446131441 480 NFDTRGFIKLVIEEGSGRLIGVQAVAPEAGELIQTAVLAIRNRMTVQELADQLFPYLTMVEGLKLAAQTFSK 551
Cdd:PTZ00153 584 VDNTEGMVKIVYLKDTKEILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISEVLDAAFKAIAG 655
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
214-406 |
1.18e-19 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 89.79 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 214 KDDQSLIVSLNEGGE---RVVmfdrcLVATGASPAVPPIPGLKESP-----YWTSTEA-LASDtipERLAVIGSSVVALE 284
Cdd:COG0492 84 KDDGPFRVTTDDGTEyeaKAV-----IIATGAGPRKLGLPGEEEFEgrgvsYCATCDGfFFRG---KDVVVVGGGDSALE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 285 LAQAFARLGSKVTALARNTLFfREDPAIgeaVTAAFRAEGIEVLEHTQasqVAHMDGEFVLTT---------THGELRAD 355
Cdd:COG0492 156 EALYLTKFASKVTLIHRRDEL-RASKIL---VERLRANPKIEVLWNTE---VTEIEGDGRVEGvtlknvktgEEKELEVD 228
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446131441 356 KLLVATGRTPNTrSLaLEAAGVAVNAQGAIVIDKGMRTSSPNIYAAGDCTD 406
Cdd:COG0492 229 GVFVAIGLKPNT-EL-LKGLGLELDEDGYIVVDEDMETSVPGVFAAGDVRD 277
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
227-404 |
2.23e-19 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 89.98 E-value: 2.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 227 GERVVMFDRCLVATGASPAVPPIPG---------LKEspYWTSTEALASdtiPERLAVIGSSVVALELAQAFARLGSKVT 297
Cdd:PRK04965 94 QGNQWQYDKLVLATGASAFVPPIPGrelmltlnsQQE--YRAAETQLRD---AQRVLVVGGGLIGTELAMDLCRAGKAVT 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 298 ALARNT--LFFREDPAIGEAVTAAFRAEGIEVLEHTQASQVAHMDGEFVLTTTHGE-LRADKLLVATGRTPNTrSLAlEA 374
Cdd:PRK04965 169 LVDNAAslLASLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSGIRATLDSGRsIEVDAVIAAAGLRPNT-ALA-RR 246
|
170 180 190
....*....|....*....|....*....|
gi 446131441 375 AGVAVNaQGaIVIDKGMRTSSPNIYAAGDC 404
Cdd:PRK04965 247 AGLAVN-RG-IVVDSYLQTSAPDIYALGDC 274
|
|
| HMA |
cd00371 |
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid ... |
3-65 |
4.05e-17 |
|
Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid residues found in a number of proteins that transport or detoxify heavy metals, for example, the CPx-type heavy metal ATPases and copper chaperones. HMA domain contains two cysteine residues that are important in binding and transfer of metal ions, such as copper, cadmium, cobalt and zinc. In the case of copper, stoichiometry of binding is one Cu+ ion per binding domain. Repeats of the HMA domain in copper chaperone has been associated with Menkes/Wilson disease due to binding of multiple copper ions.
Pssm-ID: 238219 [Multi-domain] Cd Length: 63 Bit Score: 75.72 E-value: 4.05e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446131441 3 TLKITGMTCDSCAAHVKEALEKVPGVQSALVSYPKGTAQLAIEAGTSSDALTTAVAGLGYEAT 65
Cdd:cd00371 1 ELSVEGMTCAGCVSKIEKALEKLPGVESVEVDLETGKATVEYDPEVSPEELLEAIEDAGYKAR 63
|
|
| CopZ |
COG2608 |
Copper chaperone CopZ [Inorganic ion transport and metabolism]; |
1-67 |
5.19e-17 |
|
Copper chaperone CopZ [Inorganic ion transport and metabolism];
Pssm-ID: 442020 [Multi-domain] Cd Length: 71 Bit Score: 75.33 E-value: 5.19e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446131441 1 MTTLKITGMTCDSCAAHVKEALEKVPGVQSALVSYPKGTAQLAI-EAGTSSDALTTAVAGLGYEATLA 67
Cdd:COG2608 3 TVTLKVEGMTCGHCVARVEKALKALDGVASVEVDLATGTATVTYdPEKVSLEDIKAAIEEAGYEVEKA 70
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
204-412 |
6.34e-16 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 81.03 E-value: 6.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 204 ITVLHGEARFK---DDQSLIVSlnegGERVVMFDRCLVATGASPAVPPIPGL-KESPYWTST-------EALASDTipER 272
Cdd:TIGR02374 69 ITLYTGETVIQidtDQKQVITD----AGRTLSYDKLILATGSYPFILPIPGAdKKGVYVFRTiedldaiMAMAQRF--KK 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 273 LAVIGSSVVALELAQAFARLGSKVTALARNTLFFRE--DPAIGE---------AVTAAFRAEGIEVLEHTQASQVAHMDG 341
Cdd:TIGR02374 143 AAVIGGGLLGLEAAVGLQNLGMDVSVIHHAPGLMAKqlDQTAGRllqreleqkGLTFLLEKDTVEIVGATKADRIRFKDG 222
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446131441 342 EfvlttthgELRADKLLVATGRTPNTRsLALEAaGVAVNaqGAIVIDKGMRTSSPNIYAAGDCTDQPQFVY 412
Cdd:TIGR02374 223 S--------SLEADLIVMAAGIRPNDE-LAVSA-GIKVN--RGIIVNDSMQTSDPDIYAVGECAEHNGRVY 281
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
204-409 |
1.01e-15 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 79.02 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 204 ITVLHGEARFKDDQSLIVSLNEGgeRVVMFDRCLVATGASPAVPPIPGLKE--SPYWTSTEAL------------ASDTI 269
Cdd:COG1252 71 VRFIQGEVTGIDPEARTVTLADG--RTLSYDYLVIATGSVTNFFGIPGLAEhaLPLKTLEDALalrerllaaferAERRR 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 270 PERLAVIGSSVVALELAQAFARLGSKVTAL-------ARNTLFFRED-------PAIGEAVTAAFRAEGIEVLEHTqasQ 335
Cdd:COG1252 149 LLTIVVVGGGPTGVELAGELAELLRKLLRYpgidpdkVRITLVEAGPrilpglgEKLSEAAEKELEKRGVEVHTGT---R 225
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446131441 336 VAHMDGEFVLTTTHGELRADKLLVATGRTPNTrslALEAAGVAVNAQGAIVIDKGMRTSS-PNIYAAGDCTDQPQ 409
Cdd:COG1252 226 VTEVDADGVTLEDGEEIPADTVIWAAGVKAPP---LLADLGLPTDRRGRVLVDPTLQVPGhPNVFAIGDCAAVPD 297
|
|
| TRX_reduct |
TIGR01292 |
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ... |
234-406 |
1.31e-12 |
|
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a member of the pyridine nucleotide-disulphide oxidoreductases (pfam00070). [Energy metabolism, Electron transport]
Pssm-ID: 273540 [Multi-domain] Cd Length: 299 Bit Score: 68.81 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 234 DRCLVATGASPAVPPIPGlkESPYW--------TSTEALASDtipERLAVIGSSVVALELAQAFARLGSKVTALARNTLF 305
Cdd:TIGR01292 101 KAVIIATGASARKLGIPG--EDEFWgrgvsycaTCDGPFFKN---KEVAVVGGGDSAIEEALYLTRIAKKVTLVHRRDKF 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 306 fREDPAIgeaVTAAFRAEGIEVLEHTQASQVahmDGE---------FVLTTTHGELRADKLLVATGRTPNTrslALEAAG 376
Cdd:TIGR01292 176 -RAEKIL---LDRLKKNPKIEFLWNSTVEEI---VGDnkvegvkikNTVTGEEEELEVDGVFIAIGHEPNT---ELLKGL 245
|
170 180 190
....*....|....*....|....*....|
gi 446131441 377 VAVNAQGAIVIDKGMRTSSPNIYAAGDCTD 406
Cdd:TIGR01292 246 LELDENGYIVTDEGMRTSVPGVFAAGDVRD 275
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
272-348 |
4.58e-12 |
|
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: 61.84 E-value: 4.58e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446131441 272 RLAVIGSSVVALELAQAFARLGSKVTALARNTLFFR-EDPAIGEAVTAAFRAEGIEVLEHTQASQVAHMDGEFVLTTT 348
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPgFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVLT 78
|
|
| ZntA |
COG2217 |
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism]; |
2-76 |
4.74e-12 |
|
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism];
Pssm-ID: 441819 [Multi-domain] Cd Length: 717 Bit Score: 68.63 E-value: 4.74e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446131441 2 TTLKITGMTCDSCAAHVKEALEKVPGVQSALVSYPKGTAQLAIEAG-TSSDALTTAVAGLGYEATLADAPPTDNRA 76
Cdd:COG2217 3 VRLRIEGMTCAACAWLIEKALRKLPGVLSARVNLATERARVEYDPGkVSLEELIAAVEKAGYEAEPADADAAAEEA 78
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
186-412 |
1.49e-10 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 63.98 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 186 VEELRHAKyEGILDGNsAITVLHGEARFK-DDQSLIVSLNEGgeRVVMFDRCLVATGASPAVPPIPGlKESP----YWT- 259
Cdd:PRK14989 58 AEELSLVR-EGFYEKH-GIKVLVGERAITiNRQEKVIHSSAG--RTVFYDKLIMATGSYPWIPPIKG-SETQdcfvYRTi 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 260 ----STEALASDTipERLAVIGSSVVALELAQAFARLG--SKVTALARNTLFFREDPAIGEAVTAAFRAEGIEVLEHTQA 333
Cdd:PRK14989 133 edlnAIEACARRS--KRGAVVGGGLLGLEAAGALKNLGveTHVIEFAPMLMAEQLDQMGGEQLRRKIESMGVRVHTSKNT 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 334 SQVAH--MDGEFVLTTTHG-ELRADKLLVATGRTPNTRsLALEAaGVAVNAQGAIVIDKGMRTSSPNIYAAGDCTDQPQF 410
Cdd:PRK14989 211 LEIVQegVEARKTMRFADGsELEVDFIVFSTGIRPQDK-LATQC-GLAVAPRGGIVINDSCQTSDPDIYAIGECASWNNR 288
|
..
gi 446131441 411 VY 412
Cdd:PRK14989 289 VF 290
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
233-404 |
9.71e-10 |
|
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: 60.92 E-value: 9.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 233 FDRCLVATGAS-PAVPPIPG------------LKESpywtsTEALASDTIP---ERLAVIGSSVVALELAQAFARLGSK- 295
Cdd:COG0493 207 FDAVFLATGAGkPRDLGIPGedlkgvhsamdfLTAV-----NLGEAPDTILavgKRVVVIGGGNTAMDCARTALRLGAEs 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 296 VTALARNTlfFREDPAIGEAVTAAfRAEGIEVLEHTQ--------ASQVAHM------------DGEFVLTTTHGE---L 352
Cdd:COG0493 282 VTIVYRRT--REEMPASKEEVEEA-LEEGVEFLFLVApveiigdeNGRVTGLecvrmelgepdeSGRRRPVPIEGSeftL 358
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446131441 353 RADKLLVATGRTPNTrSLALEAAGVAVNAQGAIVIDKG-MRTSSPNIYAAGDC 404
Cdd:COG0493 359 PADLVILAIGQTPDP-SGLEEELGLELDKRGTIVVDEEtYQTSLPGVFAGGDA 410
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
234-402 |
2.58e-09 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 58.77 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 234 DRCLVATG--ASPAVPPIPGLKESPYwtsTEALASDTIPERLAVIG---SSV-VALELAqafaRLGSKVTALARNTLFFR 307
Cdd:pfam13738 120 RYVIIATGefDFPNKLGVPELPKHYS---YVKDFHPYAGQKVVVIGgynSAVdAALELV----RKGARVTVLYRGSEWED 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 308 ED--------PAIGEAVTAAFRAEGIEVLEHTQASQVAHMDGEFVLTTTHGE--LRADKLLVATGRTPNTRSlaLEAAGV 377
Cdd:pfam13738 193 RDsdpsyslsPDTLNRLEELVKNGKIKAHFNAEVKEITEVDVSYKVHTEDGRkvTSNDDPILATGYHPDLSF--LKKGLF 270
|
170 180
....*....|....*....|....*.
gi 446131441 378 AVNAQGAIVIDK-GMRTSSPNIYAAG 402
Cdd:pfam13738 271 ELDEDGRPVLTEeTESTNVPGLFLAG 296
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
225-403 |
1.22e-08 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 57.24 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 225 EGGERVvMFDRCLVATGASP-AVPPIPGLKESPYWTST--------EALASDtipERLAVIGSSVVALELAQAFARLGSK 295
Cdd:PRK09754 94 TNGESW-HWDQLFIATGAAArPLPLLDALGERCFTLRHagdaarlrEVLQPE---RSVVIVGAGTIGLELAASATQRRCK 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 296 VTA--LARNTLFFREDPAIGEAVTAAFRAEGIEVLEHTQASQVAHMDgEFVLTTTHGE-LRADKLLVATGRTPNTRsLAL 372
Cdd:PRK09754 170 VTVieLAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGE-KVELTLQSGEtLQADVVIYGIGISANDQ-LAR 247
|
170 180 190
....*....|....*....|....*....|.
gi 446131441 373 EAAgvaVNAQGAIVIDKGMRTSSPNIYAAGD 403
Cdd:PRK09754 248 EAN---LDTANGIVIDEACRTCDPAIFAGGD 275
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
233-404 |
1.84e-08 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 57.05 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 233 FDRCLVATGASPAVP-PIPGlKESPYWTS----TEALASDTIPE---RLAVIGSSVVALELAQAFARLG-SKVTALARNT 303
Cdd:PRK12814 279 FDAVLLAVGAQKASKmGIPG-EELPGVISgidfLRNVALGTALHpgkKVVVIGGGNTAIDAARTALRLGaESVTILYRRT 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 304 lffRED-PA----IGEAVtaafrAEGIEVLEHTQASQVAHMDGEFVLTTT---HGE------------------LRADKL 357
Cdd:PRK12814 358 ---REEmPAnraeIEEAL-----AEGVSLRELAAPVSIERSEGGLELTAIkmqQGEpdesgrrrpvpvegseftLQADTV 429
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446131441 358 LVATGRTPNTRslALEAAGVAVNAQGAIVIDKG-MRTSSPNIYAAGDC 404
Cdd:PRK12814 430 ISAIGQQVDPP--IAEAAGIGTSRNGTVKVDPEtLQTSVAGVFAGGDC 475
|
|
| HMA |
pfam00403 |
Heavy-metal-associated domain; |
3-42 |
3.49e-08 |
|
Heavy-metal-associated domain;
Pssm-ID: 459804 [Multi-domain] Cd Length: 58 Bit Score: 49.93 E-value: 3.49e-08
10 20 30 40
....*....|....*....|....*....|....*....|
gi 446131441 3 TLKITGMTCDSCAAHVKEALEKVPGVQSALVSYPKGTAQL 42
Cdd:pfam00403 1 TFRVSGMHCGGCAAKVEKALSELPGVLSVSVDLATKTVTV 40
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
220-411 |
4.61e-08 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 55.00 E-value: 4.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 220 IVSLnegGERVVMFDRCLVATGA-SPAVPPIPG---------------LKESPYWTSTEALASDTIPERLAVIGSSVVAL 283
Cdd:PRK12770 109 IVSL---EELVKKYDAVLIATGTwKSRKLGIPGedlpgvysaleylfrIRAAKLGYLPWEKVPPVEGKKVVVVGAGLTAV 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 284 ELAQAFARLGS-KVTALARNTLffREDPAiGEAVTAAFRAEGIEVLEHT-----------QASQVAHM-----DGEF--- 343
Cdd:PRK12770 186 DAALEAVLLGAeKVYLAYRRTI--NEAPA-GKYEIERLIARGVEFLELVtpvriigegrvEGVELAKMrlgepDESGrpr 262
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 344 --VLTTTHGELRADKLLVATGRTPnTRSLALEAAGVAVNAQGAIVIDKGMRTSSPNIYAAGDCTDQPQFV 411
Cdd:PRK12770 263 pvPIPGSEFVLEADTVVFAIGEIP-TPPFAKECLGIELNRKGEIVVDEKHMTSREGVFAAGDVVTGPSKI 331
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
233-405 |
2.43e-07 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 53.26 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 233 FDRCLVATGASpAVP--PIPG------------LKESpywTSTEALASDTIPERLAVIGSSVVALELAQAFARLGSK-VT 297
Cdd:PRK11749 226 YDAVFIGTGAG-LPRflGIPGenlggvysavdfLTRV---NQAVADYDLPVGKRVVVIGGGNTAMDAARTAKRLGAEsVT 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 298 ALARNTlffRED-PAIGEAVTAAfRAEGIEVLEHTQ------------ASQVAHMD---------GEFVLTTTHGELRAD 355
Cdd:PRK11749 302 IVYRRG---REEmPASEEEVEHA-KEEGVEFEWLAApveilgdegrvtGVEFVRMElgepdasgrRRVPIEGSEFTLPAD 377
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446131441 356 KLLVATGRTPNTRSLALeAAGVAVNAQGAIVID-KGMRTSSPNIYAAGDCT 405
Cdd:PRK11749 378 LVIKAIGQTPNPLILST-TPGLELNRWGTIIADdETGRTSLPGVFAGGDIV 427
|
|
| MerP |
TIGR02052 |
mercuric transport protein periplasmic component; This model represents the periplasmic ... |
3-66 |
2.63e-06 |
|
mercuric transport protein periplasmic component; This model represents the periplasmic mercury (II) binding protein of the bacterial mercury detoxification system which passes mercuric ion to the MerT transporter for subsequent reduction to Hg(0) by the mercuric reductase MerA. MerP contains a distinctive GMTCXXC motif associated with metal binding. MerP is related to a larger family of metal binding proteins (pfam00403). [Cellular processes, Detoxification]
Pssm-ID: 131107 [Multi-domain] Cd Length: 92 Bit Score: 45.80 E-value: 2.63e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446131441 3 TLKITGMTCDSCAAHVKEALEKVPGVQSALVSYPKGTAQLAI-EAGTSSDALTTAVAGLGYEATL 66
Cdd:TIGR02052 26 TLEVPGMTCVACPITVETALQKVDGVSKAEVTFKTKLAVVTFdDEKTNVKALTEATTDAGYPSSL 90
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
233-403 |
1.12e-05 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 48.20 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 233 FDRCLVATGAS-PAVPPIPGLKESPYWTSTEALA-----------SDT---IPERLAVIGSSVVALELAQAFARLGSKvt 297
Cdd:PRK12778 518 FKGIFIASGAGlPNFMNIPGENSNGVMSSNEYLTrvnlmdaaspdSDTpikFGKKVAVVGGGNTAMDSARTAKRLGAE-- 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 298 alaRNTLFFR----EDPAIGEAVTAAfRAEGIEVLE-HTQASQVAHMDGE----------------------FVLTTTHG 350
Cdd:PRK12778 596 ---RVTIVYRrseeEMPARLEEVKHA-KEEGIEFLTlHNPIEYLADEKGWvkqvvlqkmelgepdasgrrrpVAIPGSTF 671
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446131441 351 ELRADKLLVATGRTPN---TRSLAleaaGVAVNAQGAIVIDKGMRTSSPNIYAAGD 403
Cdd:PRK12778 672 TVDVDLVIVSVGVSPNplvPSSIP----GLELNRKGTIVVDEEMQSSIPGIYAGGD 723
|
|
| UxxU_metal_bind |
NF041115 |
metal-binding (seleno)protein; Known members of this family are selenoproteins with an ... |
3-64 |
1.42e-05 |
|
metal-binding (seleno)protein; Known members of this family are selenoproteins with an exceptional UXXU motif, with two selenocysteines. Known members so far derive primarily from MAGs, and have an N-terminal signal peptide N-terminal to the region represented in the seed alignment. Note that this model represents a specific clade of a more widely distributed domain that frequently appears 3 or 4 times in a single protein, so the domain-specific cutoff is critical to identification. Homologous domains, outside the scope of this model, are found in CopZ family copper chaperones and heavy metal-translocating P-type ATPases.
Pssm-ID: 469038 [Multi-domain] Cd Length: 74 Bit Score: 43.09 E-value: 1.42e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446131441 3 TLKITGMTCDSCAAHVKEALEKVPGVQSALVSYPKGTAQLAIE-AGTSSDALTTAVAGLGYEA 64
Cdd:NF041115 7 ILAIEGMTUASUPLIAKKALEGLEGVEKADVSYKEGRAEVAFDpDKVSAAQMVDAVNRIGFRA 69
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
359-408 |
2.37e-05 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 47.08 E-value: 2.37e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 446131441 359 VATGRTPNTRslALEAAgVAVNAQGAIVIDKGMRTSSPNIYAAGDCTDQP 408
Cdd:PRK15317 443 VQIGLVPNTE--WLKGT-VELNRRGEIIVDARGATSVPGVFAAGDCTTVP 489
|
|
| YdhS |
COG4529 |
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only]; |
183-328 |
3.82e-05 |
|
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];
Pssm-ID: 443597 [Multi-domain] Cd Length: 466 Bit Score: 46.49 E-value: 3.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 183 QARVEELRHAkyegiLDGNSAITVLHGEAR--FKDDQSLIVSLNEGgeRVVMFDRCLVATGASPAVPPI------PGLKE 254
Cdd:COG4529 106 RERLAEALAR-----APAGVRLRHIRAEVVdlERDDGGYRVTLADG--ETLRADAVVLATGHPPPAPPPglaagsPRYIA 178
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446131441 255 SPYwtSTEALASDTIPERLAVIGSSVVALELAQAFARLG--SKVTALARNTLFFREDPAIGEAVTAAFRAEGIEVL 328
Cdd:COG4529 179 DPW--PPGALARIPPDARVLIIGTGLTAIDVVLSLAARGhrGPITALSRRGLLPRAHPPGAPLPLKFLTPEALEEL 252
|
|
| copA |
PRK10671 |
copper-exporting P-type ATPase CopA; |
2-67 |
4.31e-05 |
|
copper-exporting P-type ATPase CopA;
Pssm-ID: 182635 [Multi-domain] Cd Length: 834 Bit Score: 46.66 E-value: 4.31e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446131441 2 TTLKITGMTCDSCAAHVKEALEKVPGVQSALVSypkgTAQLAIEAGTSSDALTTAVAGLGYEATLA 67
Cdd:PRK10671 5 IDLTLDGLSCGHCVKRVKESLEQRPDVEQADVS----ITEAHVTGTASAEALIETIKQAGYDASVS 66
|
|
| copA |
PRK10671 |
copper-exporting P-type ATPase CopA; |
4-64 |
9.40e-05 |
|
copper-exporting P-type ATPase CopA;
Pssm-ID: 182635 [Multi-domain] Cd Length: 834 Bit Score: 45.50 E-value: 9.40e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446131441 4 LKITGMTCDSCAAHVKEALEKVPGVQSALVSYPKGTAqlAIEAGTSSDALTTAVAGLGYEA 64
Cdd:PRK10671 103 LLLSGMSCASCVSRVQNALQSVPGVTQARVNLAERTA--LVMGSASPQDLVQAVEKAGYGA 161
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
233-403 |
1.07e-04 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 45.01 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 233 FDRCLVATGAS-PAVPPIPGLKESPYWTSTEALA-----------SDT---IPERLAVIGSSVVALELAQAFARLGSKVT 297
Cdd:PRK12831 229 FDAVFIGSGAGlPKFMGIPGENLNGVFSANEFLTrvnlmkaykpeYDTpikVGKKVAVVGGGNVAMDAARTALRLGAEVH 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 298 ALARNTlffRED-PAIGEAVTAAfRAEGIEVLEHTQ-------------ASQVAHMD-GE---------FVLTTTHGELR 353
Cdd:PRK12831 309 IVYRRS---EEElPARVEEVHHA-KEEGVIFDLLTNpveilgdengwvkGMKCIKMElGEpdasgrrrpVEIEGSEFVLE 384
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446131441 354 ADKLLVATGRTPNtRSLALEAAGVAVNAQGAIVIDK--GMrTSSPNIYAAGD 403
Cdd:PRK12831 385 VDTVIMSLGTSPN-PLISSTTKGLKINKRGCIVADEetGL-TSKEGVFAGGD 434
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
271-403 |
1.45e-04 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 44.39 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 271 ERLAVIGSSVVALELAQAFARLGSKVTALARNTLFFRE-DPAIGEAVTAAFRAEGIEvleHTQASQVAHMDGEFVLTTTH 349
Cdd:PRK13512 149 DKALVVGAGYISLEVLENLYERGLHPTLIHRSDKINKLmDADMNQPILDELDKREIP---YRLNEEIDAINGNEVTFKSG 225
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 446131441 350 GELRADKLLVATGRTPNTRslALEAAGVAVNAQGAIVIDKGMRTSSPNIYAAGD 403
Cdd:PRK13512 226 KVEHYDMIIEGVGTHPNSK--FIESSNIKLDDKGFIPVNDKFETNVPNIYAIGD 277
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
321-404 |
3.48e-04 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 43.23 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446131441 321 RAEGIEVlehtqaSQVAHMDGEFV-LTTTHGELRADKLLVATGRTPNTRSLaLEAAGVAVNAQGAIV-IDKGMRTSSPNI 398
Cdd:PRK12810 361 KVTGVKV------VRTELGEGDFEpVEGSEFVLPADLVLLAMGFTGPEAGL-LAQFGVELDERGRVAaPDNAYQTSNPKV 433
|
....*.
gi 446131441 399 YAAGDC 404
Cdd:PRK12810 434 FAAGDM 439
|
|
| zntA |
PRK11033 |
zinc/cadmium/mercury/lead-transporting ATPase; Provisional |
5-78 |
6.84e-04 |
|
zinc/cadmium/mercury/lead-transporting ATPase; Provisional
Pssm-ID: 236827 [Multi-domain] Cd Length: 741 Bit Score: 42.67 E-value: 6.84e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446131441 5 KITGMTCDSCAAHVKEALEKVPGVQSALVSYpkGTAQLAIEA-GTSSDALTTAVAGLGYEATLADAPPTDNRAGL 78
Cdd:PRK11033 58 KVSGMDCPSCARKVENAVRQLAGVNQVQVLF--ATEKLVVDAdNDIRAQVESAVQKAGFSLRDEQAAAAAPESRL 130
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
314-362 |
1.47e-03 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 40.67 E-value: 1.47e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 446131441 314 EAVTAAFraeGIEVLEHTQASQVAHMDGEFVLTTTHGELRADKLLVATG 362
Cdd:pfam13738 82 RRVADHF---ELPINLFEEVTSVKKEDDGFVVTTSKGTYQARYVIIATG 127
|
|
| PLN02957 |
PLN02957 |
copper, zinc superoxide dismutase |
9-66 |
2.26e-03 |
|
copper, zinc superoxide dismutase
Pssm-ID: 215516 [Multi-domain] Cd Length: 238 Bit Score: 39.73 E-value: 2.26e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 446131441 9 MTCDSCAAHVKEALEKVPGVQSALVSYpkGTAQLAIEAGTSSDALTTAVAGLGYEATL 66
Cdd:PLN02957 14 MKCEGCVAAVKNKLETLEGVKAVEVDL--SNQVVRVLGSSPVKAMTAALEQTGRKARL 69
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
318-362 |
3.30e-03 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 39.89 E-value: 3.30e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 446131441 318 AAFRAEGIEVLEHTQASQVAHMDGEFV-LTTTHGELRADKLLVATG 362
Cdd:COG0665 159 RAARAAGVRIREGTPVTGLEREGGRVTgVRTERGTVRADAVVLAAG 204
|
|
| |
