|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
2-509 |
0e+00 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 923.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 2 ILDADIKSQLAQYLNLMEGDILLKVSAGSDNTSNDMLTLINEIAGMSSKIKVEKVTL-QRTPSFSINRPHEDTGVIFAGV 80
Cdd:PRK15317 1 MLDANLKTQLKQYLELLERPIELVASLDDSEKSAELKELLEEIASLSDKITVEEDSLdVRKPSFSITRPGEDTGVRFAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 81 PLGQEFTSLVLALLQTSGRAPKVDSEILEQITNVKGNYNFETYASLSCHNCPDVVQALNLMSILNPNITHTMIDGAVFKK 160
Cdd:PRK15317 81 PMGHEFTSLVLALLQVGGHPPKLDQEVIEQIKALDGDFHFETYVSLSCHNCPDVVQALNLMAVLNPNITHTMIDGALFQD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 161 EVEDKNIMAVPSVYLNGNHFNSGRMTLTDILSKIGS---STKPSEIFNKTPYDVLVVGAGPAGATAAIYAARKGIRTGII 237
Cdd:PRK15317 161 EVEARNIMAVPTVFLNGEEFGQGRMTLEEILAKLDTgaaARAAEELNAKDPYDVLVVGGGPAGAAAAIYAARKGIRTGIV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 238 AERLGGQVTDTVGIENFTGTKYIEGPKLSANLEEHIKEYNVDIITSQYAIGL-KKKELIEIQLKNGTLLKSKTVILSTGA 316
Cdd:PRK15317 241 AERFGGQVLDTMGIENFISVPETEGPKLAAALEEHVKEYDVDIMNLQRASKLePAAGLIEVELANGAVLKAKTVILATGA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 317 SWRNVGVPGEKELKNKGVTYCPHCDGPLFKGKNTAVIGGGNSGIEAAIDLGGIVNHVTVLEFMPELKADDVLQKRLNSLS 396
Cdd:PRK15317 321 RWRNMNVPGEDEYRNKGVAYCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVKHVTVLEFAPELKADQVLQDKLRSLP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 397 NVTVIKNVKIKEITG-IDKVNGITYADRLTGEKHHIELQGVFVQIGLIPNTDWLDKTITRNSRGEIVVDSHGATDIPGVF 475
Cdd:PRK15317 401 NVTIITNAQTTEVTGdGDKVTGLTYKDRTTGEEHHLELEGVFVQIGLVPNTEWLKGTVELNRRGEIIVDARGATSVPGVF 480
|
490 500 510
....*....|....*....|....*....|....
gi 500757664 476 ASGDCTNSPYKQIIISMGSGATAALSAFDYLIRS 509
Cdd:PRK15317 481 AAGDCTTVPYKQIIIAMGEGAKAALSAFDYLIRN 514
|
|
| AhpF |
TIGR03140 |
alkyl hydroperoxide reductase subunit F; This enzyme is the partner of the peroxiredoxin ... |
2-508 |
0e+00 |
|
alkyl hydroperoxide reductase subunit F; This enzyme is the partner of the peroxiredoxin (alkyl hydroperoxide reductase) AhpC which contains the peroxide-reactive cysteine. AhpF contains the reductant (NAD(P)H) binding domain (pfam00070) and presumably acts to resolve the disulfide which forms after oxidation of the active site cysteine in AphC. This proteins contains two paired conserved cysteine motifs, CxxCP and CxHCDGP. [Cellular processes, Detoxification, Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 274444 [Multi-domain] Cd Length: 515 Bit Score: 753.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 2 ILDADIKSQLAQYLNLMEGDILLKVSAGSDNTSNDMLTLINEIAGMSSKIKVEKVT--LQRTPSFSINRPHEDTGVIFAG 79
Cdd:TIGR03140 1 MLDQSLLAQLKSYLASLENPVTLVLSAGSHEKSKELLELLDEIASLSDKISLTQNTadTLRKPSFTILRDGADTGIRFAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 80 VPLGQEFTSLVLALLQTSGRAPKVDSEILEQITNVKGNYNFETYASLSCHNCPDVVQALNLMSILNPNITHTMIDGAVFK 159
Cdd:TIGR03140 81 IPGGHEFTSLVLAILQVGGHGPKLDEGIIDRIRRLNGPLHFETYVSLTCQNCPDVVQALNQMALLNPNISHTMIDGALFQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 160 KEVEDKNIMAVPSVYLNGNHFNSGRMTLTDILSKIGS---STKPSEIFNKTPYDVLVVGAGPAGATAAIYAARKGIRTGI 236
Cdd:TIGR03140 161 DEVEALGIQGVPAVFLNGEEFHNGRMDLAELLEKLEEtagVEAASALEQLDPYDVLVVGGGPAGAAAAIYAARKGLRTAM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 237 IAERLGGQVTDTVGIENFTGTKYIEGPKLSANLEEHIKEYNVDIITSQYAIGLKKKE-LIEIQLKNGTLLKSKTVILSTG 315
Cdd:TIGR03140 241 VAERIGGQVKDTVGIENLISVPYTTGSQLAANLEEHIKQYPIDLMENQRAKKIETEDgLIVVTLESGEVLKAKSVIVATG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 316 ASWRNVGVPGEKELKNKGVTYCPHCDGPLFKGKNTAVIGGGNSGIEAAIDLGGIVNHVTVLEFMPELKADDVLQKRLNSL 395
Cdd:TIGR03140 321 ARWRKLGVPGEKEYIGKGVAYCPHCDGPFFKGKDVAVIGGGNSGIEAAIDLAGIVRHVTVLEFADELKADKVLQDKLKSL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 396 SNVTVIKNVKIKEITG-IDKVNGITYADRLTGEKHHIELQGVFVQIGLIPNTDWLDKTITRNSRGEIVVDSHGATDIPGV 474
Cdd:TIGR03140 401 PNVDILTSAQTTEIVGdGDKVTGIRYQDRNSGEEKQLDLDGVFVQIGLVPNTEWLKDAVELNRRGEIVIDERGRTSVPGI 480
|
490 500 510
....*....|....*....|....*....|....
gi 500757664 475 FASGDCTNSPYKQIIISMGSGATAALSAFDYLIR 508
Cdd:TIGR03140 481 FAAGDVTTVPYKQIIIAMGEGAKAALSAFDYLIR 514
|
|
| AhpF |
COG3634 |
Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms]; |
1-196 |
7.35e-96 |
|
Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms];
Pssm-ID: 442851 [Multi-domain] Cd Length: 200 Bit Score: 288.57 E-value: 7.35e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 1 MILDADIKSQLAQYLNLMEGDILLKVSAGSDNTSNDMLTLINEIAGMSSKIKVEKVTLQ---RTPSFSINRPHEDTGVIF 77
Cdd:COG3634 2 AMLDDELKAQLKEYLEKLKNPVELVLFLDDCEKSEELRELLEEIASLSDKISLEVYDKDdveRAPSFAILRDGEDTGIRF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 78 AGVPLGQEFTSLVLALLQTSGRAPKVDSEILEQITNVKGNYNFETYASLSCHNCPDVVQALNLMSILNPNITHTMIDGAV 157
Cdd:COG3634 82 AGIPSGHEFTSLVLALLQVSGHPPKLSEETIEQIKALDGPVHFEVFVSLSCPNCPDVVQALNLMAVLNPNITHEMIDGAE 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 500757664 158 FKKEVEDKNIMAVPSVYLNGNHFNSGRMTLTDILSKIGS 196
Cdd:COG3634 162 FPDEAEKYGVMSVPTVVLNGEVFFVGRMPEEEILEKLDT 200
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
229-506 |
3.70e-92 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 283.16 E-value: 3.70e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 229 RKGIRTGII-AERLGGQVTDTVGIENFTGTKY-IEGPKLSANLEEHIKEYNVDIITSQyAIGLKK-KELIEIQLKNGTLL 305
Cdd:COG0492 21 RAGLKTLVIeGGEPGGQLATTKEIENYPGFPEgISGPELAERLREQAERFGAEILLEE-VTSVDKdDGPFRVTTDDGTEY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 306 KSKTVILSTGASWRNVGVPGEKELKNKGVTYCPHCDGPLFKGKNTAVIGGGNSGIEAAIDLGGIVNHVTVLEFMPELKAD 385
Cdd:COG0492 100 EAKAVIIATGAGPRKLGLPGEEEFEGRGVSYCATCDGFFFRGKDVVVVGGGDSALEEALYLTKFASKVTLIHRRDELRAS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 386 DVLQKRLNSLSNVTVIKNVKIKEITGIDKVNGITYADRLTGEKHHIELQGVFVQIGLIPNTDWL-DKTITRNSRGEIVVD 464
Cdd:COG0492 180 KILVERLRANPKIEVLWNTEVTEIEGDGRVEGVTLKNVKTGEEKELEVDGVFVAIGLKPNTELLkGLGLELDEDGYIVVD 259
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 500757664 465 SHGATDIPGVFASGDCTNSPYKQIIISMGSGATAALSAFDYL 506
Cdd:COG0492 260 EDMETSVPGVFAAGDVRDYKYRQAATAAGEGAIAALSAARYL 301
|
|
| TRX_reduct |
TIGR01292 |
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ... |
242-506 |
1.88e-76 |
|
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: 242.53 E-value: 1.88e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 242 GGQVTDTVGIENFTGTK-YIEGPKLSANLEEHIKEYNVDIITSQYAIGLKKKELIEIQLKNGTLLKSKTVILSTGASWRN 320
Cdd:TIGR01292 34 GGQLTTTTEVENYPGFPeGISGPELMEKMKEQAVKFGAEIIYEEVIKVDKSDRPFKVYTGDGKEYTAKAVIIATGASARK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 321 VGVPGEKELKNKGVTYCPHCDGPLFKGKNTAVIGGGNSGIEAAIDLGGIVNHVTVLEFMPELKADDVLQKRLNSLSNVTV 400
Cdd:TIGR01292 114 LGIPGEDEFWGRGVSYCATCDGPFFKNKEVAVVGGGDSAIEEALYLTRIAKKVTLVHRRDKFRAEKILLDRLKKNPKIEF 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 401 IKNVKIKEITGIDKVNGITYADRLTGEKHHIELQGVFVQIGLIPNTDWLDKTITRNSRGEIVVDSHGATDIPGVFASGDC 480
Cdd:TIGR01292 194 LWNSTVEEIVGDNKVEGVKIKNTVTGEEEELEVDGVFIAIGHEPNTELLKGLLELDENGYIVTDEGMRTSVPGVFAAGDV 273
|
250 260
....*....|....*....|....*.
gi 500757664 481 TNSPYKQIIISMGSGATAALSAFDYL 506
Cdd:TIGR01292 274 RDKGYRQAVTAAGDGCIAALSAERYL 299
|
|
| AhpF_NTD_C |
cd03026 |
TRX-GRX-like family, Alkyl hydroperoxide reductase F subunit (AhpF) N-terminal domain (NTD) ... |
105-193 |
5.27e-47 |
|
TRX-GRX-like family, Alkyl hydroperoxide reductase F subunit (AhpF) N-terminal domain (NTD) subfamily, C-terminal TRX-fold subdomain; AhpF is a homodimeric flavoenzyme which catalyzes the NADH-dependent reduction of the peroxiredoxin AhpC, which then reduces hydrogen peroxide and organic hydroperoxides. AhpF contains an NTD containing two contiguous TRX-fold subdomains similar to Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO). It also contains a catalytic core similar to TRX reductase containing FAD and NADH binding domains with an active site disulfide. The proposed mechanism of action of AhpF is similar to a TRX/TRX reductase system. The flow of reducing equivalents goes from NADH -> catalytic core of AhpF -> NTD of AhpF -> AhpC -> peroxide substrates. The catalytic CXXC motif of the NTD of AhpF is contained in its C-terminal TRX subdomain.
Pssm-ID: 239324 [Multi-domain] Cd Length: 89 Bit Score: 158.23 E-value: 5.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 105 SEILEQITNVKGNYNFETYASLSCHNCPDVVQALNLMSILNPNITHTMIDGAVFKKEVEDKNIMAVPSVYLNGNHFNSGR 184
Cdd:cd03026 1 EDLLEQIRRLNGPINFETYVSLSCHNCPDVVQALNLMAVLNPNIEHEMIDGALFQDEVEERGIMSVPAIFLNGELFGFGR 80
|
....*....
gi 500757664 185 MTLTDILSK 193
Cdd:cd03026 81 MTLEEILAK 89
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
209-495 |
3.06e-38 |
|
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: 141.69 E-value: 3.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 209 YDVLVVGAGPAGATAAIYAARKGIRTGIIAER---LGGQVTDTVGIENFTGTKYI--EGPKLSANLEEHIKEYNVDII-- 281
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDEgtcPYGGCVLSKALLGAAEAPEIasLWADLYKRKEEVVKKLNNGIEvl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 282 --TSQYAIGLKKKELIEIQLK--NGTLLKSKTVILSTGASWRNVGVPGEKELKNKGVTYCPHCDGPLFK--GKNTAVIGG 355
Cdd:pfam07992 81 lgTEVVSIDPGAKKVVLEELVdgDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKllPKRVVVVGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 356 GNSGIEAAIDLGGIVNHVTVLEFMPEL------KADDVLQKRLNSLsNVTVIKNVKIKEITGIDKVngityADRLTGEKH 429
Cdd:pfam07992 161 GYIGVELAAALAKLGKEVTLIEALDRLlrafdeEISAALEKALEKN-GVEVRLGTSVKEIIGDGDG-----VEVILKDGT 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500757664 430 HIELQGVFVQIGLIPNTDWLDKT-ITRNSRGEIVVDSHGATDIPGVFASGDCTNSPYKQIIISMGSG 495
Cdd:pfam07992 235 EIDADLVVVAIGRRPNTELLEAAgLELDERGGIVVDEYLRTSVPGIYAAGDCRVGGPELAQNAVAQG 301
|
|
| AhpF_NTD_N |
cd02974 |
Alkyl hydroperoxide reductase F subunit (AhpF) N-terminal domain (NTD) family, N-terminal ... |
2-94 |
4.82e-35 |
|
Alkyl hydroperoxide reductase F subunit (AhpF) N-terminal domain (NTD) family, N-terminal TRX-fold subdomain; AhpF is a homodimeric flavoenzyme which catalyzes the NADH-dependent reduction of the peroxiredoxin AhpC, which in turn catalyzes the reduction of hydrogen peroxide and organic hydroperoxides. AhpF contains an NTD forming two contiguous TRX-fold subdomain similar to Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO). It also contains a catalytic core similar to TRX reductase containing FAD and NADH binding domains with an active site disulfide. The proposed mechanism of action of AhpF is similar to a TRX/TRX reductase system. The flow of reducing equivalents goes from NADH -> catalytic core of AhpF -> NTD of AhpF -> AhpC -> peroxide substrates. The N-terminal TRX-fold subdomain of AhpF NTD is redox inactive, but is proposed to contain an important residue that aids in the catalytic function of the redox-active CXXC motif contained in the C-terminal TRX-fold subdomain.
Pssm-ID: 239272 [Multi-domain] Cd Length: 94 Bit Score: 126.15 E-value: 4.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 2 ILDADIKSQLAQYLNLMEGDILLKVSAGSDNTSNDMLTLINEIAGMSSKIKVEKVTLQ-RTPSFSINRPHEDTGVIFAGV 80
Cdd:cd02974 1 MLDANLKQQLKAYLERLENPVELVASLDDSEKSAELLELLEEIASLSDKITLEEDNDDeRKPSFSINRPGEDTGIRFAGI 80
|
90
....*....|....
gi 500757664 81 PLGQEFTSLVLALL 94
Cdd:cd02974 81 PMGHEFTSLVLALL 94
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
242-506 |
4.85e-32 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 125.17 E-value: 4.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 242 GGQVTDTVGIENFTGTKY-IEGPKLSANLEEHIKEYNVDIITSQY-AIGLKKKELiEIQLKNGTLlKSKTVILSTGASWR 319
Cdd:PRK10262 41 GGQLTTTTEVENWPGDPNdLTGPLLMERMHEHATKFETEIIFDHInKVDLQNRPF-RLTGDSGEY-TCDALIIATGASAR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 320 NVGVPGEKELKNKGVTYCPHCDGPLFKGKNTAVIGGGNSGIEAAIDLGGIVNHVTVLEFMPELKADDVLQKRLN---SLS 396
Cdd:PRK10262 119 YLGLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDGFRAEKILIKRLMdkvENG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 397 NVTVIKNVKIKEITGIDK-VNGITYAD-RLTGEKHHIELQGVFVQIGLIPNTDWLDKTITRNSrGEIVVDS--HG---AT 469
Cdd:PRK10262 199 NIILHTNRTLEEVTGDQMgVTGVRLRDtQNSDNIESLDVAGLFVAIGHSPNTAIFEGQLELEN-GYIKVQSgiHGnatQT 277
|
250 260 270
....*....|....*....|....*....|....*..
gi 500757664 470 DIPGVFASGDCTNSPYKQIIISMGSGATAALSAFDYL 506
Cdd:PRK10262 278 SIPGVFAAGDVMDHIYRQAITSAGTGCMAALDAERYL 314
|
|
| AhpF_homolog |
TIGR03143 |
putative alkyl hydroperoxide reductase F subunit; This family of thioredoxin reductase ... |
3-195 |
1.63e-30 |
|
putative alkyl hydroperoxide reductase F subunit; This family of thioredoxin reductase homologs is found adjacent to alkylhydroperoxide reductase C subunit predominantly in cases where there is only one C subunit in the genome and that genome is lacking the F subunit partner (also a thioredcxin reductase homolog) that is usually found (TIGR03140).
Pssm-ID: 132187 [Multi-domain] Cd Length: 555 Bit Score: 124.89 E-value: 1.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 3 LDADIKSQLAQYLNLMEGDI-LLKVSAGSDNTSNDMLTLINEIAGMSSKIKVE------------KVTLQRTPSFSINRP 69
Cdd:TIGR03143 349 LDDSLRQQLVGIFGRLENPVtLLLFLDGSNEKSAELQSFLGEFASLSEKLNSEavnrgeepesetLPKITKLPTVALLDD 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 70 HED-TGVIFAGVPLGQEFTSLVLALLQTSGRAPKVDSEILEQITNVKGNYNFETYASLSCHNCPDVVQALNLMSILNPNI 148
Cdd:TIGR03143 429 DGNyTGLKFHGVPSGHELNSFILALYNAAGPGQPLGEELLEKIKKITKPVNIKIGVSLSCTLCPDVVLAAQRIASLNPNV 508
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 500757664 149 THTMIDGAVFKKEVEDKNIMAVPSVYLNGNHFNSGRMTLTDILSKIG 195
Cdd:TIGR03143 509 EAEMIDVSHFPDLKDEYGIMSVPAIVVDDQQVYFGKKTIEEMLELIG 555
|
|
| TRX_GRX_like |
cd02973 |
Thioredoxin (TRX)-Glutaredoxin (GRX)-like family; composed of archaeal and bacterial proteins ... |
118-184 |
4.23e-28 |
|
Thioredoxin (TRX)-Glutaredoxin (GRX)-like family; composed of archaeal and bacterial proteins that show similarity to both TRX and GRX, including the C-terminal TRX-fold subdomain of Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO). All members contain a redox-active CXXC motif and may function as PDOs. The archaeal proteins Mj0307 and Mt807 show structures more similar to GRX, but activities more similar to TRX. Some members of the family are similar to PfPDO in that they contain a second CXXC motif located in a second TRX-fold subdomain at the N-terminus; the superimposable N- and C-terminal TRX subdomains form a compact structure. PfPDO is postulated to be the archaeal counterpart of bacterial DsbA and eukaryotic protein disulfide isomerase (PDI). The C-terminal CXXC motif of PfPDO is required for its oxidase, reductase and isomerase activities. Also included in the family is the C-terminal TRX-fold subdomain of the N-terminal domain (NTD) of bacterial AhpF, which has a similar fold as PfPDO with two TRX-fold subdomains but without the second CXXC motif.
Pssm-ID: 239271 [Multi-domain] Cd Length: 67 Bit Score: 106.50 E-value: 4.23e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500757664 118 YNFETYASLSCHNCPDVVQALNLMSILNPNITHTMIDGAVFKKEVEDKNIMAVPSVYLNGNHFNSGR 184
Cdd:cd02973 1 VNIEVFVSPTCPYCPDAVQAANRIAALNPNISAEMIDAAEFPDLADEYGVMSVPAIVINGKVEFVGR 67
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
264-496 |
1.72e-21 |
|
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: 95.26 E-value: 1.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 264 KLSANLEEHIKEYNVDIITSQYAIGL--KKKELIeiqLKNGTLLKSKTVILSTGASWRNVGVPGekeLKNKGVTYCPHCD 341
Cdd:COG0446 37 DLLVRTPESFERKGIDVRTGTEVTAIdpEAKTVT---LRDGETLSYDKLVLATGARPRPPPIPG---LDLPGVFTLRTLD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 342 GPL--------FKGKNTAVIGGGNSGIEAA---IDLGGivnHVTVLEFMPEL--KAD----DVLQKRLNSlSNVTVIKNV 404
Cdd:COG0446 111 DADalrealkeFKGKRAVVIGGGPIGLELAealRKRGL---KVTLVERAPRLlgVLDpemaALLEEELRE-HGVELRLGE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 405 KIKEITGIDKVnGITYADrltgeKHHIELQGVFVQIGLIPNTDWLDKT-ITRNSRGEIVVDSHGATDIPGVFASGDCTNS 483
Cdd:COG0446 187 TVVAIDGDDKV-AVTLTD-----GEEIPADLVVVAPGVRPNTELAKDAgLALGERGWIKVDETLQTSDPDVYAAGDCAEV 260
|
250
....*....|....*..
gi 500757664 484 PY----KQIIISMGSGA 496
Cdd:COG0446 261 PHpvtgKTVYIPLASAA 277
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
257-481 |
2.58e-19 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 89.82 E-value: 2.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 257 TKYIEGPK----LSANLEEHIKEYNVDIITSQYAIGL--KKKElieIQLKNGTLLKSKTVILSTGASWRNVGVPGeKELK 330
Cdd:COG1251 46 SKVLAGETdeedLLLRPADFYEENGIDLRLGTRVTAIdrAART---VTLADGETLPYDKLVLATGSRPRVPPIPG-ADLP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 331 nkGVTYC---PHCD---GPLFKGKNTAVIGGGNSGIEAAIDL--GGIvnHVTVLEFMPEL-------KADDVLQKRLNSL 395
Cdd:COG1251 122 --GVFTLrtlDDADalrAALAPGKRVVVIGGGLIGLEAAAALrkRGL--EVTVVERAPRLlprqldeEAGALLQRLLEAL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 396 sNVTVIKNVKIKEITGIDKVNGITYADrltGEkhHIELQGVFVQIGLIPNTDWLDKT-ITRNsRGeIVVDSHGATDIPGV 474
Cdd:COG1251 198 -GVEVRLGTGVTEIEGDDRVTGVRLAD---GE--ELPADLVVVAIGVRPNTELARAAgLAVD-RG-IVVDDYLRTSDPDI 269
|
....*..
gi 500757664 475 FASGDCT 481
Cdd:COG1251 270 YAAGDCA 276
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
310-501 |
1.16e-18 |
|
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: 88.27 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 310 VILSTGAS-WRNVGVPGEkELKN--------KGVTYCPHCDGPLFKGKNTAVIGGGNSGIEA---AIDLGgiVNHVTVLE 377
Cdd:COG0493 210 VFLATGAGkPRDLGIPGE-DLKGvhsamdflTAVNLGEAPDTILAVGKRVVVIGGGNTAMDCartALRLG--AESVTIVY 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 378 FMP--ELKADDvlQKRLNSLS-NVTVIKNVKIKEITGID--KVNGITYAD---------------RLTGEKHHIELQGVF 437
Cdd:COG0493 287 RRTreEMPASK--EEVEEALEeGVEFLFLVAPVEIIGDEngRVTGLECVRmelgepdesgrrrpvPIEGSEFTLPADLVI 364
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500757664 438 VQIGLIPNTDWLDKT--ITRNSRGEIVVD-SHGATDIPGVFASGDCTNSPyKQIIISMGSGATAALS 501
Cdd:COG0493 365 LAIGQTPDPSGLEEElgLELDKRGTIVVDeETYQTSLPGVFAGGDAVRGP-SLVVWAIAEGRKAARA 430
|
|
| GlrX_arch |
TIGR02187 |
Glutaredoxin-like domain protein; This family of archaeal proteins contains a C-terminal ... |
35-178 |
1.13e-17 |
|
Glutaredoxin-like domain protein; This family of archaeal proteins contains a C-terminal domain with homology to bacterial and eukaryotic glutaredoxins, including a CPYC motif. There is an N-terminal domain which has even more distant homology to glutaredoxins. The name "glutaredoxin" may be inappropriate in the sense of working in tandem with glutathione and glutathione reductase which may not be present in the archaea. The overall domain structure appears to be related to bacterial alkylhydroperoxide reductases, but the homology may be distant enough that the function of this family is wholly different.
Pssm-ID: 274021 [Multi-domain] Cd Length: 215 Bit Score: 81.72 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 35 NDMLTL-INEIAGMSSKIKVEKVTLQRTPSFSINRPHEDTGVIFAGVPLGQEFTSLVLALLQTSGRAPKVDSEILEQITN 113
Cdd:TIGR02187 51 SPKLKLeIYDFDTPEDKEEAEKYGVERVPTTIILEEGKDGGIRYTGIPAGYEFAALIEDIVRVSQGEPGLSEKTVELLQS 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500757664 114 VKGNYNFETYASLSCHNCPDVVQALNLMSILNPNITHTMIDGAVFKKEVEDKNIMAVPSVYLNGN 178
Cdd:TIGR02187 131 LDEPVRIEVFVTPTCPYCPYAVLMAHKFALANDKILGEMIEANENPDLAEKYGVMSVPKIVINKG 195
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
295-484 |
2.01e-17 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 84.59 E-value: 2.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 295 IEIQLKNGTLLKSKTVILSTGASWRNV-GVP--GEKELKNKGV---TYCPhcdgplfkgKNTAVIGGGNSGIEAA---ID 365
Cdd:PRK06327 134 IKVTGEDETVITAKHVIIATGSEPRHLpGVPfdNKIILDNTGAlnfTEVP---------KKLAVIGAGVIGLELGsvwRR 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 366 LGGivnHVTVLEFMPELKA---DDVLQKRLNSLSN--VTVIKNVKIKEITGIDKVNGITYADRlTGEKHHIELQGVFVQI 440
Cdd:PRK06327 205 LGA---EVTILEALPAFLAaadEQVAKEAAKAFTKqgLDIHLGVKIGEIKTGGKGVSVAYTDA-DGEAQTLEVDKLIVSI 280
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 500757664 441 GLIPNTDWL--DKT-ITRNSRGEIVVDSHGATDIPGVFASGDCTNSP 484
Cdd:PRK06327 281 GRVPNTDGLglEAVgLKLDERGFIPVDDHCRTNVPNVYAIGDVVRGP 327
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
264-484 |
3.40e-17 |
|
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: 83.98 E-value: 3.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 264 KLSANLEEHIKEYNVDIITSqYAiglkkkELI---EIQLKNGTLLKSKTVILSTGASWRNVGVPGEKElkNKGVTYcphc 340
Cdd:COG1249 92 RLRGGVEELLKKNGVDVIRG-RA------RFVdphTVEVTGGETLTADHIVIATGSRPRVPPIPGLDE--VRVLTS---- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 341 DG-------PlfkgKNTAVIGGGNSGIEaaidLGGIVN----HVTVLEFMPEL--KAD----DVLQKRLNSLsNVTVIKN 403
Cdd:COG1249 159 DEaleleelP----KSLVVIGGGYIGLE----FAQIFArlgsEVTLVERGDRLlpGEDpeisEALEKALEKE-GIDILTG 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 404 VKIKEITGIDKVNGITYADRltGEKHHIELQGVFVQIGLIPNTDW--LDKT-ITRNSRGEIVVDSHGATDIPGVFASGDC 480
Cdd:COG1249 230 AKVTSVEKTGDGVTVTLEDG--GGEEAVEADKVLVATGRRPNTDGlgLEAAgVELDERGGIKVDEYLRTSVPGIYAIGDV 307
|
....
gi 500757664 481 TNSP 484
Cdd:COG1249 308 TGGP 311
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
310-482 |
7.66e-13 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 70.21 E-value: 7.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 310 VILSTGAS-WRNVGVPGEkELKN--KGVTYCP-----HCDGPLFKGKNTAVIGGGNSGIEAA---IDLGgiVNHVTVL-- 376
Cdd:PRK11749 229 VFIGTGAGlPRFLGIPGE-NLGGvySAVDFLTrvnqaVADYDLPVGKRVVVIGGGNTAMDAArtaKRLG--AESVTIVyr 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 377 ---EFMP----EL---KADdvlqkrlnslsNVTVIKNVKIKEITGIDKVN-GITYAD-RL-------------TGEKHHI 431
Cdd:PRK11749 306 rgrEEMPaseeEVehaKEE-----------GVEFEWLAAPVEILGDEGRVtGVEFVRmELgepdasgrrrvpiEGSEFTL 374
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 500757664 432 ELQGVFVQIGLIPNTD--WLDKTITRNSRGEIVVD-SHGATDIPGVFASGDCTN 482
Cdd:PRK11749 375 PADLVIKAIGQTPNPLilSTTPGLELNRWGTIIADdETGRTSLPGVFAGGDIVT 428
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
229-506 |
1.38e-12 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 68.86 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 229 RKGIRTGIiaERLGGQvtdtvGIENFTGTKYIEGPKLSANLEEHIKEYNVDIitsqyaiglkkKELIEiqlkngtllKSK 308
Cdd:PRK12770 68 IERVREGV--KELEEA-----GVVFHTRTKVCCGEPLHEEEGDEFVERIVSL-----------EELVK---------KYD 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 309 TVILSTGaSW--RNVGVPGEkELKnkGVT---------------YCPHCDGPLFKGKNTAVIGGGNSGIEAAID---LGg 368
Cdd:PRK12770 121 AVLIATG-TWksRKLGIPGE-DLP--GVYsaleylfriraaklgYLPWEKVPPVEGKKVVVVGAGLTAVDAALEavlLG- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 369 iVNHVTV-----LEFMPELKAD-DVLQKRlnslsNVTVIKNVKIKEITGIDKVNGITYAD-RL--------------TGE 427
Cdd:PRK12770 196 -AEKVYLayrrtINEAPAGKYEiERLIAR-----GVEFLELVTPVRIIGEGRVEGVELAKmRLgepdesgrprpvpiPGS 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 428 KHHIELQGVFVQIGLIP----NTDWLDktITRNSRGEIVVDSHGATDIPGVFASGDCTNSPYKqIIISMGSGATAALSAF 503
Cdd:PRK12770 270 EFVLEADTVVFAIGEIPtppfAKECLG--IELNRKGEIVVDEKHMTSREGVFAAGDVVTGPSK-IGKAIKSGLRAAQSIH 346
|
...
gi 500757664 504 DYL 506
Cdd:PRK12770 347 EWL 349
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
301-484 |
1.10e-11 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 66.74 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 301 NGTLLKSKTVILSTGAswRNVGVPGEKELKNKG-VTYcphcdGPLFK----GKNTAVIGGGNSGIEAAIDLGGIVNHVTV 375
Cdd:PRK06292 125 NGERIEAKNIVIATGS--RVPPIPGVWLILGDRlLTS-----DDAFEldklPKSLAVIGGGVIGLELGQALSRLGVKVTV 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 376 LEFMPEL----------KADDVLQKRLNslsnvtVIKNVKIKEITGIDKVNGITYadRLTGEKHHIELQGVFVQIGLIPN 445
Cdd:PRK06292 198 FERGDRIlpledpevskQAQKILSKEFK------IKLGAKVTSVEKSGDEKVEEL--EKGGKTETIEADYVLVATGRRPN 269
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 500757664 446 TDWL--DKT-ITRNSRGEIVVDSHGATDIPGVFASGDCTNSP 484
Cdd:PRK06292 270 TDGLglENTgIELDERGRPVVDEHTQTSVPGIYAAGDVNGKP 311
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
348-480 |
2.87e-11 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 65.45 E-value: 2.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 348 KNTAVIGGGNSGIEAAIDLGGIVNHVTVLE---------FMPELKadDVLQKRLNSlSNVTVIKNVKIKEITGIDKVNGI 418
Cdd:PRK09564 150 KNIVIIGAGFIGLEAVEAAKHLGKNVRIIQledrilpdsFDKEIT--DVMEEELRE-NGVELHLNEFVKSLIGEDKVEGV 226
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500757664 419 TyadrltGEKHHIELQGVFVQIGLIPNTDWL-DKTITRNSRGEIVVDSHGATDIPGVFASGDC 480
Cdd:PRK09564 227 V------TDKGEYEADVVIVATGVKPNTEFLeDTGLKTLKNGAIIVDEYGETSIENIYAAGDC 283
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
209-506 |
3.68e-11 |
|
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: 64.97 E-value: 3.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 209 YDVLVVGAGPAGATAAIYAARKGIRTGII-AERLGG-----------------QVTDTVG--------IENFT------- 255
Cdd:TIGR01350 2 YDVIVIGGGPGGYVAAIRAAQLGLKVALVeKEYLGGtclnvgciptkallhsaEVYDEIKhakdlgieVENVSvdwekmq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 256 GTKYIEGPKLSANLEEHIKEYNVDIITSqYAIGLKKKElIEIQLKNGT-LLKSKTVILSTGASWRnvGVPGEKELKNKGV 334
Cdd:TIGR01350 82 KRKNKVVKKLVGGVSGLLKKNKVTVIKG-EAKFLDPGT-VSVTGENGEeTLEAKNIIIATGSRPR--SLPGPFDFDGKVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 335 -TYcphcDGPL-FKG--KNTAVIGGGNSGIEAAIDLGGIVNHVTVLEFMPEL------KADDVLQKRLNSLsNVTVIKNV 404
Cdd:TIGR01350 158 iTS----TGALnLEEvpESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRIlpgedaEVSKVLQKALKKK-GVKILTNT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 405 KIKEITGIDkvNGITY------ADRLTGEKhhielqgVFVQIGLIPNTDW--LDKT-ITRNSRGEIVVDSHGATDIPGVF 475
Cdd:TIGR01350 233 KVTAVEKND--DQVTYenkggeTETLTGEK-------VLVAVGRKPNTEGlgLEKLgVELDERGRIVVDEYMRTNVPGIY 303
|
330 340 350
....*....|....*....|....*....|....*..
gi 500757664 476 ASGDCTNSP------YKQIIISMGSGATAALSAFDYL 506
Cdd:TIGR01350 304 AIGDVIGGPmlahvaSHEGIVAAENIAGKEPAHIDYD 340
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
264-479 |
4.98e-11 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 64.78 E-value: 4.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 264 KLSANLEEHIKEYNVDIITsqyaiG---LKKKELIEI-QLKNGTLLKSKTVILSTGAswRNVGVPGEKELKNKGVTYcph 339
Cdd:PRK06416 93 RLTGGVEGLLKKNKVDIIR-----GeakLVDPNTVRVmTEDGEQTYTAKNIILATGS--RPRELPGIEIDGRVIWTS--- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 340 cDGPL---FKGKNTAVIGGGNSGIEAAI---DLGGivnHVTVLEFMPEL----------KADDVLQKRlnslsNVTVIKN 403
Cdd:PRK06416 163 -DEALnldEVPKSLVVIGGGYIGVEFASayaSLGA---EVTIVEALPRIlpgedkeiskLAERALKKR-----GIKIKTG 233
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500757664 404 VKIKEITgiDKVNGITYADRLTGEKHHIELQGVFVQIGLIPNTD--WLDKTITRNSRGEIVVDSHGATDIPGVFASGD 479
Cdd:PRK06416 234 AKAKKVE--QTDDGVTVTLEDGGKEETLEADYVLVAVGRRPNTEnlGLEELGVKTDRGFIEVDEQLRTNVPNIYAIGD 309
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
271-506 |
1.50e-10 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 63.11 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 271 EHIKEYNVDIITSqYAIG--LKKKELIEIQlkngtllKSKTVILSTGASW-RNVGVPGE--------KEL---KNKGVTY 336
Cdd:PRK12831 199 ENIKKLGVKIETN-VVVGktVTIDELLEEE-------GFDAVFIGSGAGLpKFMGIPGEnlngvfsaNEFltrVNLMKAY 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 337 CPHCDGPLFKGKNTAVIGGGNSGIEAA---IDLGG---IVNHVTVLEfMPELKAD-----------DVLQKRLNSLS--- 396
Cdd:PRK12831 271 KPEYDTPIKVGKKVAVVGGGNVAMDAArtaLRLGAevhIVYRRSEEE-LPARVEEvhhakeegvifDLLTNPVEILGden 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 397 -NVTVIKNVKIK----EITGIDKVNGItyadrlTGEKHHIELQGVFVQIGLIPNTDWLDKT--ITRNSRGEIVVDS-HGA 468
Cdd:PRK12831 350 gWVKGMKCIKMElgepDASGRRRPVEI------EGSEFVLEVDTVIMSLGTSPNPLISSTTkgLKINKRGCIVADEeTGL 423
|
250 260 270
....*....|....*....|....*....|....*...
gi 500757664 469 TDIPGVFASGDCTNSPyKQIIISMGSGATAALSAFDYL 506
Cdd:PRK12831 424 TSKEGVFAGGDAVTGA-ATVILAMGAGKKAAKAIDEYL 460
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
349-423 |
5.88e-10 |
|
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: 55.67 E-value: 5.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 349 NTAVIGGGNSGIEAAIDLGGIVNHVTVLEFMPELK------ADDVLQKRLNSLsNVTVIKNVKIKEITGIDKVNGITYAD 422
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLpgfdpeIAKILQEKLEKN-GIEFLLNTTVEAIEGNGDGVVVVLTD 79
|
.
gi 500757664 423 R 423
Cdd:pfam00070 80 G 80
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
260-478 |
1.04e-09 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 59.54 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 260 IEGPKLSAN-----LEEHIKEYNVDIITSQYAIGLKK-KELIEIQLKNGTLlKSKTVILSTGaswrNVGVPGEKELKNKG 333
Cdd:pfam13738 67 FNREHPSGNeyaeyLRRVADHFELPINLFEEVTSVKKeDDGFVVTTSKGTY-QARYVIIATG----EFDFPNKLGVPELP 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 334 VTYCPHCDGPLFKGKNTAVIGGGNSGIEAAIDLGGIVNHVTVLEFMPELKAD----------DVLQkRLNSLSNVTVIK- 402
Cdd:pfam13738 142 KHYSYVKDFHPYAGQKVVVIGGYNSAVDAALELVRKGARVTVLYRGSEWEDRdsdpsyslspDTLN-RLEELVKNGKIKa 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 403 --NVKIKEITGIDKVNGITYADrltGEKHHIELQgVFVQIGLIPNTDWLDK-TITRNSRGEIVVDSHG-ATDIPGVFASG 478
Cdd:pfam13738 221 hfNAEVKEITEVDVSYKVHTED---GRKVTSNDD-PILATGYHPDLSFLKKgLFELDEDGRPVLTEETeSTNVPGLFLAG 296
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
304-484 |
7.61e-09 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 57.84 E-value: 7.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 304 LLKSKTVILSTGASWRNVGVPGEKELKN----KGVTYCPHcdgplfKGKNTAVIGGGNSGIEAAIDLGGIVNHVTVLEFM 379
Cdd:PRK07251 116 ELTAETIVINTGAVSNVLPIPGLADSKHvydsTGIQSLET------LPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAA 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 380 PEL--KADDVLQ---KRLNSLSNVTVIKNVKIKEITG-----IDKVNGITYA-DRL---TGEKHHIElqgvfvQIGLiPN 445
Cdd:PRK07251 190 STIlpREEPSVAalaKQYMEEDGITFLLNAHTTEVKNdgdqvLVVTEDETYRfDALlyaTGRKPNTE------PLGL-EN 262
|
170 180 190
....*....|....*....|....*....|....*....
gi 500757664 446 TDwldktITRNSRGEIVVDSHGATDIPGVFASGDCTNSP 484
Cdd:PRK07251 263 TD-----IELTERGAIKVDDYCQTSVPGVFAVGDVNGGP 296
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
264-479 |
1.26e-08 |
|
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: 57.17 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 264 KLSANLEEHIKE----YNVDI----ITSQYAIG-LKKKELIEIQLKNGT--LLKSKTVILSTGASWRNVGVPGEKELknk 332
Cdd:TIGR01438 90 RLVEAVQNHIGSlnwgYRVALrekkVKYENAYAeFVDKHRIKATNKKGKekIYSAERFLIATGERPRYPGIPGAKEL--- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 333 GVT--------YCPhcdgplfkGKnTAVIGGGNSGIEAAIDLGGIVNHVTVLEFMPELKADDvlQKRLNSL------SNV 398
Cdd:TIGR01438 167 CITsddlfslpYCP--------GK-TLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFD--QDCANKVgehmeeHGV 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 399 TVIKNVKIKEITGIDKVNGITYADRLTGEKHhiELQGVFVQIGLIPNTDWLD----KTITRNSRGEIVVDSHGATDIPGV 474
Cdd:TIGR01438 236 KFKRQFVPIKVEQIEAKVLVEFTDSTNGIEE--EYDTVLLAIGRDACTRKLNlenvGVKINKKTGKIPADEEEQTNVPYI 313
|
....*
gi 500757664 475 FASGD 479
Cdd:TIGR01438 314 YAVGD 318
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
310-480 |
1.53e-08 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 57.10 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 310 VILSTGAS-WRNVGVPGEkELKnkGVT----YCP----HCDG------PLFKGKNTAVIGGGNSGIEA---AIDLGGIvn 371
Cdd:PRK12810 232 VFLGTGAYkPRDLGIPGR-DLD--GVHfamdFLIqntrRVLGdetepfISAKGKHVVVIGGGDTGMDCvgtAIRQGAK-- 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 372 HVTVLEFM---PELKADDV---LQKRLNSLSN-----VTVIKNVKIKEITGID-KVNGITYAD---------RLTGEKHH 430
Cdd:PRK12810 307 SVTQRDIMpmpPSRRNKNNpwpYWPMKLEVSNaheegVEREFNVQTKEFEGENgKVTGVKVVRtelgegdfePVEGSEFV 386
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 500757664 431 IELQGVFVQIGLI-PNTDWLDK-TITRNSRGEIVVDSHG-ATDIPGVFASGDC 480
Cdd:PRK12810 387 LPADLVLLAMGFTgPEAGLLAQfGVELDERGRVAAPDNAyQTSNPKVFAAGDM 439
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
351-486 |
1.26e-07 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 54.05 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 351 AVIGGGNSGIE---AAIDLGgivNHVTVLEFMPEL------KADDVLQKRLNSLSnVTVIKNVKIKEITGIDkvNGITYA 421
Cdd:PRK06370 175 VIIGGGYIGLEfaqMFRRFG---SEVTVIERGPRLlpredeDVAAAVREILEREG-IDVRLNAECIRVERDG--DGIAVG 248
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500757664 422 DRLTGEKHHIELQGVFVQIGLIPNTDW--LDKT-ITRNSRGEIVVDSHGATDIPGVFASGDCtNSPYK 486
Cdd:PRK06370 249 LDCNGGAPEITGSHILVAVGRVPNTDDlgLEAAgVETDARGYIKVDDQLRTTNPGIYAAGDC-NGRGA 315
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
257-480 |
1.37e-07 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 54.45 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 257 TKYIEG----PKLSANLEEHIKEYNVDIITSQYAIGLKKKELIEIQlKNGTLLKSKTVILSTGASWRNVGVPGEKElknK 332
Cdd:TIGR02374 44 SSVLQGeadlDDITLNSKDWYEKHGITLYTGETVIQIDTDQKQVIT-DAGRTLSYDKLILATGSYPFILPIPGADK---K 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 333 GVTY---CPHCDGPLFKGKNT---AVIGGGNSGIEAAIDLGGIVNHVTVLEFMPELKADDV-------LQKRLNSLSnVT 399
Cdd:TIGR02374 120 GVYVfrtIEDLDAIMAMAQRFkkaAVIGGGLLGLEAAVGLQNLGMDVSVIHHAPGLMAKQLdqtagrlLQRELEQKG-LT 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 400 VIKNVKIKEITGIDKVNGITYADrltGEKhhIELQGVFVQIGLIPNTDWLDKTITRNSRGeIVVDSHGATDIPGVFASGD 479
Cdd:TIGR02374 199 FLLEKDTVEIVGATKADRIRFKD---GSS--LEADLIVMAAGIRPNDELAVSAGIKVNRG-IIVNDSMQTSDPDIYAVGE 272
|
.
gi 500757664 480 C 480
Cdd:TIGR02374 273 C 273
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
268-480 |
6.48e-07 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 51.67 E-value: 6.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 268 NLEEHIKEYNVDIITSQ-YAIGLKKKElieIQLKNGTLLKSKTVILSTGASWRNVGVPGEKElknkgvtYCPHCDGP--- 343
Cdd:COG1252 61 PLRELLRRAGVRFIQGEvTGIDPEART---VTLADGRTLSYDYLVIATGSVTNFFGIPGLAE-------HALPLKTLeda 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 344 ---------LF------KGKNTAVIGGGNSGIEAA---------------IDLGGIvnHVTVLEFMPEL------KADDV 387
Cdd:COG1252 131 lalrerllaAFeraerrRLLTIVVVGGGPTGVELAgelaellrkllrypgIDPDKV--RITLVEAGPRIlpglgeKLSEA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 388 LQKRLNSLsNVTVIKNVKIKEITGidkvNGITYADrltGEKHHIELqgVFVQIGLIPNtDWLDKT-ITRNSRGEIVVDSH 466
Cdd:COG1252 209 AEKELEKR-GVEVHTGTRVTEVDA----DGVTLED---GEEIPADT--VIWAAGVKAP-PLLADLgLPTDRRGRVLVDPT 277
|
250
....*....|....*
gi 500757664 467 G-ATDIPGVFASGDC 480
Cdd:COG1252 278 LqVPGHPNVFAIGDC 292
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
418-484 |
1.75e-06 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 50.54 E-value: 1.75e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500757664 418 ITYADR-LTGEKHHIELQG--VFVQIGLIPNTDWLD---KTITRNSRGEIVVDSHGATDIPGVFASGDCTNSP 484
Cdd:PRK13748 336 VAHVDGeFVLTTGHGELRAdkLLVATGRAPNTRSLAldaAGVTVNAQGAIVIDQGMRTSVPHIYAAGDCTDQP 408
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
340-480 |
2.65e-06 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 49.53 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 340 CDGPLFKGKNTAVIGGGNSGIEAAIDLGGIVNHVTVLE----FMPELKADDV---LQKRLNSLSnVTVIKNVKIKEITGI 412
Cdd:PRK04965 134 AETQLRDAQRVLVVGGGLIGTELAMDLCRAGKAVTLVDnaasLLASLMPPEVssrLQHRLTEMG-VHLLLKSQLQGLEKT 212
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500757664 413 DKvnGItyadRLTGEKHH-IELQGVFVQIGLIPNTDWLDKTITRNSRGeIVVDSHGATDIPGVFASGDC 480
Cdd:PRK04965 213 DS--GI----RATLDSGRsIEVDAVIAAAGLRPNTALARRAGLAVNRG-IVVDSYLQTSAPDIYALGDC 274
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
308-506 |
2.74e-06 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 50.13 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 308 KTVILSTGASWRN-VGVPGEKEL----KNKGVT-------YCPHCDGPLFKGKNTAVIGGGNSGIEA---AIDLGGivNH 372
Cdd:PRK12778 519 KGIFIASGAGLPNfMNIPGENSNgvmsSNEYLTrvnlmdaASPDSDTPIKFGKKVAVVGGGNTAMDSartAKRLGA--ER 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 373 VTVL-----EFMP----ELKADDVLQKRLNSLSNVTVIKNVKIKEITGI--DKV-------NGITYADRLTGEKHHIELQ 434
Cdd:PRK12778 597 VTIVyrrseEEMParleEVKHAKEEGIEFLTLHNPIEYLADEKGWVKQVvlQKMelgepdaSGRRRPVAIPGSTFTVDVD 676
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500757664 435 GVFVQIGLIPNTdWLDKTITR---NSRGEIVVDSHGATDIPGVFASGDCTNSPyKQIIISMGSGATAALSAFDYL 506
Cdd:PRK12778 677 LVIVSVGVSPNP-LVPSSIPGlelNRKGTIVVDEEMQSSIPGIYAGGDIVRGG-ATVILAMGDGKRAAAAIDEYL 749
|
|
| Thioredoxin_3 |
pfam13192 |
Thioredoxin domain; |
125-194 |
3.22e-06 |
|
Thioredoxin domain;
Pssm-ID: 433026 [Multi-domain] Cd Length: 71 Bit Score: 44.90 E-value: 3.22e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 125 SLSCHNCPDVVQALNlMSILNPNITHTMIDGAVFKkEVEDKNIMAVPSVYLNGNHFNSGRMTLTDILSKI 194
Cdd:pfam13192 2 GPGCPKCPQLEKAVK-EAAAELGIDAEVEKVTDFP-EIAKYGVMSTPALVINGKVVSSGKVPSEEEIRKL 69
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
341-506 |
3.58e-06 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 49.49 E-value: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 341 DGPLFKGKNTAVIGGGNSGIEA---AIDLGG----IVNHVTVlEFMPELK--ADDVLQKrlnslsnvtvikNVKIKEITG 411
Cdd:PRK12771 261 GEPPFLGKRVVVIGGGNTAMDAartARRLGAeevtIVYRRTR-EDMPAHDeeIEEALRE------------GVEINWLRT 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 412 IDKV----NGITYADRL----------------TGEKHHIELQGVFVQIGLIPNTDWLDK-TITRNSRGEIVVD-SHGAT 469
Cdd:PRK12771 328 PVEIegdeNGATGLRVItvekmeldedgrpspvTGEEETLEADLVVLAIGQDIDSAGLESvPGVEVGRGVVQVDpNFMMT 407
|
170 180 190
....*....|....*....|....*....|....*..
gi 500757664 470 DIPGVFASGDCTNSPyKQIIISMGSGATAALSAFDYL 506
Cdd:PRK12771 408 GRPGVFAGGDMVPGP-RTVTTAIGHGKKAARNIDAFL 443
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
348-482 |
1.27e-05 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 47.46 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 348 KNTAVIGGGNSGIEAAidlgGIVN----HVTVL--------EFMPELKadDVLQKRLNSlSNVTVIKNVKIKEItgiDKV 415
Cdd:PRK06116 168 KRVAVVGAGYIAVEFA----GVLNglgsETHLFvrgdaplrGFDPDIR--ETLVEEMEK-KGIRLHTNAVPKAV---EKN 237
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500757664 416 ngityAD-RLTGEKHH---IELQGVFVQIGLIPNTDW--LDKT-ITRNSRGEIVVDSHGATDIPGVFASGDCTN 482
Cdd:PRK06116 238 -----ADgSLTLTLEDgetLTVDCLIWAIGREPNTDGlgLENAgVKLNEKGYIIVDEYQNTNVPGIYAVGDVTG 306
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
352-486 |
5.02e-05 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 45.72 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 352 VIGGGNSGIEAAIDLGGIVNHVTVLEFMPEL--KADDVLQKRLNSLSNVTVikNVKI-KEITGIDKV-NGITYadRLTGE 427
Cdd:PRK07846 171 IVGGGFIAAEFAHVFSALGVRVTVVNRSGRLlrHLDDDISERFTELASKRW--DVRLgRNVVGVSQDgSGVTL--RLDDG 246
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500757664 428 KHhIELQGVFVQIGLIPNTDWLDKT---ITRNSRGEIVVDSHGATDIPGVFASGDCTnSPYK 486
Cdd:PRK07846 247 ST-VEADVLLVATGRVPNGDLLDAAaagVDVDEDGRVVVDEYQRTSAEGVFALGDVS-SPYQ 306
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
346-480 |
1.55e-04 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 44.34 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 346 KGKNTAVIGGGNSGIEAAIDLG--GIVNHvtVLEFMPELKAD-------DVLQKRLNSLS-NVTVIKNVKIKEITGIDKV 415
Cdd:PRK14989 144 RSKRGAVVGGGLLGLEAAGALKnlGVETH--VIEFAPMLMAEqldqmggEQLRRKIESMGvRVHTSKNTLEIVQEGVEAR 221
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 416 NGITYADRLTGEKHHIelqgVFvQIGLIPNtdwlDKTITR-----NSRGEIVVDSHGATDIPGVFASGDC 480
Cdd:PRK14989 222 KTMRFADGSELEVDFI----VF-STGIRPQ----DKLATQcglavAPRGGIVINDSCQTSDPDIYAIGEC 282
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
298-489 |
3.26e-04 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 43.45 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 298 QLKNGTLLKSKTVILSTGaswrnvgvpGEKELKN-KGVTYCPHCDG--PLFKGKNTAVIGGGnsgiEAAIDLGGIVN--- 371
Cdd:PTZ00058 194 QLDDGQVIEGKNILIAVG---------NKPIFPDvKGKEFTISSDDffKIKEAKRIGIAGSG----YIAVELINVVNrlg 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 372 ---HVTVLEFMPELKAD-DVLQKRLNSL--SNVTVIKNVKIKEITGIDKVNGITYadrLTGEKHHIELQGVFVQIGLIPN 445
Cdd:PTZ00058 261 aesYIFARGNRLLRKFDeTIINELENDMkkNNINIITHANVEEIEKVKEKNLTIY---LSDGRKYEHFDYVIYCVGRSPN 337
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 500757664 446 TDWLD--KTITRNSRGEIVVDSHGATDIPGVFASGDCTNSPYKQII 489
Cdd:PTZ00058 338 TEDLNlkALNIKTPKGYIKVDDNQRTSVKHIYAVGDCCMVKKNQEI 383
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
345-376 |
5.58e-04 |
|
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];
Pssm-ID: 441675 [Multi-domain] Cd Length: 414 Bit Score: 42.16 E-value: 5.58e-04
10 20 30
....*....|....*....|....*....|..
gi 500757664 345 FKGKNTAVIGGGNSGIEAAIDLGGIVNHVTVL 376
Cdd:COG2072 169 LAGKRVLVVGTGASAVQIAPELARVAAHVTVF 200
|
|
| PfPDO_like_N |
cd02975 |
Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO)-like family, N-terminal TRX-fold ... |
21-90 |
1.62e-03 |
|
Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO)-like family, N-terminal TRX-fold subdomain; composed of proteins with similarity to PfPDO, a redox active thermostable protein believed to be the archaeal counterpart of bacterial DsbA and eukaryotic protein disulfide isomerase (PDI), which are both involved in oxidative protein folding. PfPDO contains two redox active CXXC motifs in two contiguous TRX-fold subdomains. The active site in the N-terminal TRX-fold subdomain is required for isomerase but not for reductase activity of PfPDO. The exclusive presence of PfPDO-like proteins in extremophiles may suggest that they have a special role in adaptation to extreme conditions.
Pssm-ID: 239273 [Multi-domain] Cd Length: 113 Bit Score: 38.14 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 21 DILLKVSAGSDNTSNDMLTLINEIAGMSSKIK------------VEKVTLQRTPSFSINR-PHEDTGVIFAGVPLGQEFT 87
Cdd:cd02975 24 DLVVFSSKEGCQYCEVTKQLLEELSELSDKLKleiydfdedkekAEKYGVERVPTTIFLQdGGKDGGIRYYGLPAGYEFA 103
|
...
gi 500757664 88 SLV 90
Cdd:cd02975 104 SLI 106
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
436-481 |
3.30e-03 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 39.84 E-value: 3.30e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 500757664 436 VFVQIGLIPNTDWL---DKTITRNSRGEIVVDSHGATDIPGVFASGDCT 481
Cdd:PRK07845 266 ALMAVGSVPNTAGLgleEAGVELTPSGHITVDRVSRTSVPGIYAAGDCT 314
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
348-411 |
5.02e-03 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 39.46 E-value: 5.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 348 KNTAVIGGGNSGIEAAIDLG--GIvnHVTVLEFMPEL------------KADDV------LQKRLNSLSNVTVIKNVKIK 407
Cdd:COG1148 141 KRALVIGGGIAGMTAALELAeqGY--EVYLVEKEPELggraaqlhktfpGLDCPqcilepLIAEVEANPNITVYTGAEVE 218
|
....
gi 500757664 408 EITG 411
Cdd:COG1148 219 EVSG 222
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
346-409 |
5.23e-03 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 39.23 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 346 KGKNTAVIGGGNSGIEAAIDLGGIVNHVTVLEFM-----------PE--LKADDVLQKRLNSL--------SNVTVIKNV 404
Cdd:PRK12831 139 KGKKVAVIGSGPAGLTCAGDLAKMGYDVTIFEALhepggvlvygiPEfrLPKETVVKKEIENIkklgvkieTNVVVGKTV 218
|
....*
gi 500757664 405 KIKEI 409
Cdd:PRK12831 219 TIDEL 223
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
350-483 |
6.10e-03 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 38.98 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 350 TAVIGGGNSGIEAAIDLGG------------IVNH--VTVLEFMPELKA--DDVL----QKRLNSLsNVTVIKNVKIKEI 409
Cdd:PTZ00318 176 FVVVGGGPTGVEFAAELADffrddvrnlnpeLVEEckVTVLEAGSEVLGsfDQALrkygQRRLRRL-GVDIRTKTAVKEV 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500757664 410 TgidkvngityadrltgEKHHIELQGVFVQIGLI---------PNTDWLDktITRNSRGEIVVDSH-GATDIPGVFASGD 479
Cdd:PTZ00318 255 L----------------DKEVVLKDGEVIPTGLVvwstgvgpgPLTKQLK--VDKTSRGRISVDDHlRVKPIPNVFALGD 316
|
....
gi 500757664 480 CTNS 483
Cdd:PTZ00318 317 CAAN 320
|
|
| |
