|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
2-508 |
0e+00 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 996.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 2 ILDADIKTQLSQYLQLMENDILLKVSAGDDNVSKDMLSLVDELATMSSKITVEKVEL-ERTPSFSVNRPGEDTGVVFAGI 80
Cdd:PRK15317 1 MLDANLKTQLKQYLELLERPIELVASLDDSEKSAELKELLEEIASLSDKITVEEDSLdVRKPSFSITRPGEDTGVRFAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 81 PLGHEFTSLVLALLQVSGRAPKVEQKLIDQIKNIQGEYHFESYISLSCHNCPDVVQALNVMSVLNSGITHTMIDGAAFKE 160
Cdd:PRK15317 81 PMGHEFTSLVLALLQVGGHPPKLDQEVIEQIKALDGDFHFETYVSLSCHNCPDVVQALNLMAVLNPNITHTMIDGALFQD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 161 EVESKDIMAVPTVYLNGESFGSGRMTLEEILAKMGNG---PDASELSDKDPYDVLVVGGGPAGASAAIYAARKGIRTGIV 237
Cdd:PRK15317 161 EVEARNIMAVPTVFLNGEEFGQGRMTLEEILAKLDTGaaaRAAEELNAKDPYDVLVVGGGPAGAAAAIYAARKGIRTGIV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 238 AERFGGQVMDTMGIENFISVKRTEGPKLVASLEEHVKEYDIDVMNLQRAKRLEKK-ELIEVELENGAILKSKSVIVSTGA 316
Cdd:PRK15317 241 AERFGGQVLDTMGIENFISVPETEGPKLAAALEEHVKEYDVDIMNLQRASKLEPAaGLIEVELANGAVLKAKTVILATGA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 317 RWRNVGVPGEAEFKNKGVAYCPHCDGPLFIGKDVAVIGGGNSGIEAAIDLAGIVKHVTVLEFMPELKADAVLQERLNSLP 396
Cdd:PRK15317 321 RWRNMNVPGEDEYRNKGVAYCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVKHVTVLEFAPELKADQVLQDKLRSLP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 397 NVTVLKNVQTKEITGT-DKVNGISYIDRETEEVHHVELQGVFVQIGLVPNTDWLGETVERV-RGEIVTDKHGATNVPGVF 474
Cdd:PRK15317 401 NVTIITNAQTTEVTGDgDKVTGLTYKDRTTGEEHHLELEGVFVQIGLVPNTEWLKGTVELNrRGEIIVDARGATSVPGVF 480
|
490 500 510
....*....|....*....|....*....|....
gi 488053536 475 GAGDCTNNPYKQIIISMGSGANAALGAFDYLIRN 508
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: 803.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 2 ILDADIKTQLSQYLQLMENDILLKVSAGDDNVSKDMLSLVDELATMSSKITVEK--VELERTPSFSVNRPGEDTGVVFAG 79
Cdd:TIGR03140 1 MLDQSLLAQLKSYLASLENPVTLVLSAGSHEKSKELLELLDEIASLSDKISLTQntADTLRKPSFTILRDGADTGIRFAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 80 IPLGHEFTSLVLALLQVSGRAPKVEQKLIDQIKNIQGEYHFESYISLSCHNCPDVVQALNVMSVLNSGITHTMIDGAAFK 159
Cdd:TIGR03140 81 IPGGHEFTSLVLAILQVGGHGPKLDEGIIDRIRRLNGPLHFETYVSLTCQNCPDVVQALNQMALLNPNISHTMIDGALFQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 160 EEVESKDIMAVPTVYLNGESFGSGRMTLEEILAKMGNG---PDASELSDKDPYDVLVVGGGPAGASAAIYAARKGIRTGI 236
Cdd:TIGR03140 161 DEVEALGIQGVPAVFLNGEEFHNGRMDLAELLEKLEETagvEAASALEQLDPYDVLVVGGGPAGAAAAIYAARKGLRTAM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 237 VAERFGGQVMDTMGIENFISVKRTEGPKLVASLEEHVKEYDIDVMNLQRAKRLEKKE-LIEVELENGAILKSKSVIVSTG 315
Cdd:TIGR03140 241 VAERIGGQVKDTVGIENLISVPYTTGSQLAANLEEHIKQYPIDLMENQRAKKIETEDgLIVVTLESGEVLKAKSVIVATG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 316 ARWRNVGVPGEAEFKNKGVAYCPHCDGPLFIGKDVAVIGGGNSGIEAAIDLAGIVKHVTVLEFMPELKADAVLQERLNSL 395
Cdd:TIGR03140 321 ARWRKLGVPGEKEYIGKGVAYCPHCDGPFFKGKDVAVIGGGNSGIEAAIDLAGIVRHVTVLEFADELKADKVLQDKLKSL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 396 PNVTVLKNVQTKEITGT-DKVNGISYIDRETEEVHHVELQGVFVQIGLVPNTDWLGETVER-VRGEIVTDKHGATNVPGV 473
Cdd:TIGR03140 401 PNVDILTSAQTTEIVGDgDKVTGIRYQDRNSGEEKQLDLDGVFVQIGLVPNTEWLKDAVELnRRGEIVIDERGRTSVPGI 480
|
490 500 510
....*....|....*....|....*....|....*
gi 488053536 474 FGAGDCTNNPYKQIIISMGSGANAALGAFDYLIRN 508
Cdd:TIGR03140 481 FAAGDVTTVPYKQIIIAMGEGAKAALSAFDYLIRQ 515
|
|
| AhpF |
COG3634 |
Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms]; |
1-193 |
2.03e-103 |
|
Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms];
Pssm-ID: 442851 [Multi-domain] Cd Length: 200 Bit Score: 307.83 E-value: 2.03e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 1 MILDADIKTQLSQYLQLMENDILLKVSAGDDNVSKDMLSLVDELATMSSKITVE---KVELERTPSFSVNRPGEDTGVVF 77
Cdd:COG3634 2 AMLDDELKAQLKEYLEKLKNPVELVLFLDDCEKSEELRELLEEIASLSDKISLEvydKDDVERAPSFAILRDGEDTGIRF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 78 AGIPLGHEFTSLVLALLQVSGRAPKVEQKLIDQIKNIQGEYHFESYISLSCHNCPDVVQALNVMSVLNSGITHTMIDGAA 157
Cdd:COG3634 82 AGIPSGHEFTSLVLALLQVSGHPPKLSEETIEQIKALDGPVHFEVFVSLSCPNCPDVVQALNLMAVLNPNITHEMIDGAE 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 488053536 158 FKEEVESKDIMAVPTVYLNGESFGSGRMTLEEILAK 193
Cdd:COG3634 162 FPDEAEKYGVMSVPTVVLNGEVFFVGRMPEEEILEK 197
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
229-505 |
3.98e-88 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 272.76 E-value: 3.98e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 229 RKGIRTGIV-AERFGGQVMDTMGIENFISVKR-TEGPKLVASLEEHVKEYDIDVMnLQRAKRLEK-KELIEVELENGAIL 305
Cdd:COG0492 21 RAGLKTLVIeGGEPGGQLATTKEIENYPGFPEgISGPELAERLREQAERFGAEIL-LEEVTSVDKdDGPFRVTTDDGTEY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 306 KSKSVIVSTGARWRNVGVPGEAEFKNKGVAYCPHCDGPLFIGKDVAVIGGGNSGIEAAIDLAGIVKHVTVLEFMPELKAD 385
Cdd:COG0492 100 EAKAVIIATGAGPRKLGLPGEEEFEGRGVSYCATCDGFFFRGKDVVVVGGGDSALEEALYLTKFASKVTLIHRRDELRAS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 386 AVLQERLNSLPNVTVLKNVQTKEITGTDKVNGISYIDRETEEVHHVELQGVFVQIGLVPNTDWL-GETVERV-RGEIVTD 463
Cdd:COG0492 180 KILVERLRANPKIEVLWNTEVTEIEGDGRVEGVTLKNVKTGEEKELEVDGVFVAIGLKPNTELLkGLGLELDeDGYIVVD 259
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 488053536 464 KHGATNVPGVFGAGDCTNNPYKQIIISMGSGANAALGAFDYL 505
Cdd:COG0492 260 EDMETSVPGVFAAGDVRDYKYRQAATAAGEGAIAALSAARYL 301
|
|
| TRX_reduct |
TIGR01292 |
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ... |
241-505 |
2.00e-72 |
|
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: 232.13 E-value: 2.00e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 241 FGGQVMDTMGIENFISVKRT-EGPKLVASLEEHVKEYDIDVMNLQRAKRLEKKELIEVELENGAILKSKSVIVSTGARWR 319
Cdd:TIGR01292 33 PGGQLTTTTEVENYPGFPEGiSGPELMEKMKEQAVKFGAEIIYEEVIKVDKSDRPFKVYTGDGKEYTAKAVIIATGASAR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 320 NVGVPGEAEFKNKGVAYCPHCDGPLFIGKDVAVIGGGNSGIEAAIDLAGIVKHVTVLEFMPELKADAVLQERLNSLPNVT 399
Cdd:TIGR01292 113 KLGIPGEDEFWGRGVSYCATCDGPFFKNKEVAVVGGGDSAIEEALYLTRIAKKVTLVHRRDKFRAEKILLDRLKKNPKIE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 400 VLKNVQTKEITGTDKVNGISYIDRETEEVHHVELQGVFVQIGLVPNTDWLGETVERVR-GEIVTDKHGATNVPGVFGAGD 478
Cdd:TIGR01292 193 FLWNSTVEEIVGDNKVEGVKIKNTVTGEEEELEVDGVFIAIGHEPNTELLKGLLELDEnGYIVTDEGMRTSVPGVFAAGD 272
|
250 260
....*....|....*....|....*..
gi 488053536 479 CTNNPYKQIIISMGSGANAALGAFDYL 505
Cdd:TIGR01292 273 VRDKGYRQAVTAAGDGCIAALSAERYL 299
|
|
| AhpF_NTD_C |
cd03026 |
TRX-GRX-like family, Alkyl hydroperoxide reductase F subunit (AhpF) N-terminal domain (NTD) ... |
105-193 |
6.29e-49 |
|
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: 163.24 E-value: 6.29e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 105 QKLIDQIKNIQGEYHFESYISLSCHNCPDVVQALNVMSVLNSGITHTMIDGAAFKEEVESKDIMAVPTVYLNGESFGSGR 184
Cdd:cd03026 1 EDLLEQIRRLNGPINFETYVSLSCHNCPDVVQALNLMAVLNPNIEHEMIDGALFQDEVEERGIMSVPAIFLNGELFGFGR 80
|
....*....
gi 488053536 185 MTLEEILAK 193
Cdd:cd03026 81 MTLEEILAK 89
|
|
| AhpF_homolog |
TIGR03143 |
putative alkyl hydroperoxide reductase F subunit; This family of thioredoxin reductase ... |
209-505 |
9.67e-44 |
|
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: 162.64 E-value: 9.67e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 209 YDVLVVGGGPAGASAAIYAARKGIRTGIV-AERFGGQVMDTMGIENFISVKRTEGPKLVASLEEHVKEYDIDVMNlqrak 287
Cdd:TIGR03143 5 YDLIIIGGGPAGLSAGIYAGRAKLDTLIIeKDDFGGQITITSEVVNYPGILNTTGPELMQEMRQQAQDFGVKFLQ----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 288 rlekKELIEVELE--------NGAILKSKSVIVSTGARWRNVGVPGEAEFKNKGVAYCPHCDGPLFIGKDVAVIGGGNSG 359
Cdd:TIGR03143 80 ----AEVLDVDFDgdiktiktARGDYKTLAVLIATGASPRKLGFPGEEEFTGRGVAYCATCDGEFFTGMDVFVIGGGFAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 360 IEAAIDLAGIVKHVTVLEFMPELKADAVLQERLNSLPNVTVLKNVQTKEITGTDKVNGISYIDRETEEVHHVELQ----- 434
Cdd:TIGR03143 156 AEEAVFLTRYASKVTVIVREPDFTCAKLIAEKVKNHPKIEVKFNTELKEATGDDGLRYAKFVNNVTGEITEYKAPkdagt 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488053536 435 -GVFVQIGLVPNTDWLGETVE-RVRGEIVTDKHGATNVPGVFGAGDCTNNPYKQIIISMGSGANAALGAFDYL 505
Cdd:TIGR03143 236 fGVFVFVGYAPSSELFKGVVElDKRGYIPTNEDMETNVPGVYAAGDLRPKELRQVVTAVADGAIAATSAERYV 308
|
|
| AhpF_NTD_N |
cd02974 |
Alkyl hydroperoxide reductase F subunit (AhpF) N-terminal domain (NTD) family, N-terminal ... |
2-94 |
5.89e-43 |
|
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: 147.34 E-value: 5.89e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 2 ILDADIKTQLSQYLQLMENDILLKVSAGDDNVSKDMLSLVDELATMSSKITVEKVEL-ERTPSFSVNRPGEDTGVVFAGI 80
Cdd:cd02974 1 MLDANLKQQLKAYLERLENPVELVASLDDSEKSAELLELLEEIASLSDKITLEEDNDdERKPSFSINRPGEDTGIRFAGI 80
|
90
....*....|....
gi 488053536 81 PLGHEFTSLVLALL 94
Cdd:cd02974 81 PMGHEFTSLVLALL 94
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
209-494 |
2.17e-36 |
|
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: 136.68 E-value: 2.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 209 YDVLVVGGGPAGASAAIYAARKGIRTGIVAER---FGGQVMDTMGIENFISVKRT--EGPKLVASLEEHVKEYDIDVMNL 283
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDEgtcPYGGCVLSKALLGAAEAPEIasLWADLYKRKEEVVKKLNNGIEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 284 QRAKRLE----KKELIEVELE--NGAILKSKSVIVSTGARWRNVGVPGEAEFKNKGVAYCPHCDGPLF--IGKDVAVIGG 355
Cdd:pfam07992 81 LGTEVVSidpgAKKVVLEELVdgDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLklLPKRVVVVGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 356 GNSGIEAAIDLAGIVKHVTVLEFMPEL------KADAVLQERLNSLpNVTVLKNVQTKEITGTDKVngisyIDRETEEVH 429
Cdd:pfam07992 161 GYIGVELAAALAKLGKEVTLIEALDRLlrafdeEISAALEKALEKN-GVEVRLGTSVKEIIGDGDG-----VEVILKDGT 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488053536 430 HVELQGVFVQIGLVPNTDWLGET-VERV-RGEIVTDKHGATNVPGVFGAGDCTNNPYKQIIISMGSG 494
Cdd:pfam07992 235 EIDADLVVVAIGRRPNTELLEAAgLELDeRGGIVVDEYLRTSVPGIYAAGDCRVGGPELAQNAVAQG 301
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
242-505 |
3.64e-31 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 122.86 E-value: 3.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 242 GGQVMDTMGIENFI-SVKRTEGPKLVASLEEHVKEYDIDVMNLQRAKRLEKKELIEVELENGAiLKSKSVIVSTGARWRN 320
Cdd:PRK10262 41 GGQLTTTTEVENWPgDPNDLTGPLLMERMHEHATKFETEIIFDHINKVDLQNRPFRLTGDSGE-YTCDALIIATGASARY 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 321 VGVPGEAEFKNKGVAYCPHCDGPLFIGKDVAVIGGGNSGIEAAIDLAGIVKHVTVLEFMPELKADAVLQERLN---SLPN 397
Cdd:PRK10262 120 LGLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDGFRAEKILIKRLMdkvENGN 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 398 VTVLKNVQTKEITGTDK-VNGISYID-RETEEVHHVELQGVFVQIGLVPNTDWLGETVERVRGEIVTDK--HG---ATNV 470
Cdd:PRK10262 200 IILHTNRTLEEVTGDQMgVTGVRLRDtQNSDNIESLDVAGLFVAIGHSPNTAIFEGQLELENGYIKVQSgiHGnatQTSI 279
|
250 260 270
....*....|....*....|....*....|....*
gi 488053536 471 PGVFGAGDCTNNPYKQIIISMGSGANAALGAFDYL 505
Cdd:PRK10262 280 PGVFAAGDVMDHIYRQAITSAGTGCMAALDAERYL 314
|
|
| AhpF_homolog |
TIGR03143 |
putative alkyl hydroperoxide reductase F subunit; This family of thioredoxin reductase ... |
3-191 |
6.76e-31 |
|
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: 126.05 E-value: 6.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 3 LDADIKTQLSQYLQLMENDI-LLKVSAGDDNVSKDMLSLVDELATMSSKITVE------------KVELERTPSFSV-NR 68
Cdd:TIGR03143 349 LDDSLRQQLVGIFGRLENPVtLLLFLDGSNEKSAELQSFLGEFASLSEKLNSEavnrgeepesetLPKITKLPTVALlDD 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 69 PGEDTGVVFAGIPLGHEFTSLVLALLQVSGRAPKVEQKLIDQIKNIQGEYHFESYISLSCHNCPDVVQALNVMSVLNSGI 148
Cdd:TIGR03143 429 DGNYTGLKFHGVPSGHELNSFILALYNAAGPGQPLGEELLEKIKKITKPVNIKIGVSLSCTLCPDVVLAAQRIASLNPNV 508
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488053536 149 THTMIDGAAFKEEVESKDIMAVPTVYLNGESFGSGRMTLEEIL 191
Cdd:TIGR03143 509 EAEMIDVSHFPDLKDEYGIMSVPAIVVDDQQVYFGKKTIEEML 551
|
|
| TRX_GRX_like |
cd02973 |
Thioredoxin (TRX)-Glutaredoxin (GRX)-like family; composed of archaeal and bacterial proteins ... |
118-184 |
6.67e-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: 105.73 E-value: 6.67e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488053536 118 YHFESYISLSCHNCPDVVQALNVMSVLNSGITHTMIDGAAFKEEVESKDIMAVPTVYLNGESFGSGR 184
Cdd:cd02973 1 VNIEVFVSPTCPYCPDAVQAANRIAALNPNISAEMIDAAEFPDLADEYGVMSVPAIVINGKVEFVGR 67
|
|
| GlrX_arch |
TIGR02187 |
Glutaredoxin-like domain protein; This family of archaeal proteins contains a C-terminal ... |
36-177 |
1.82e-20 |
|
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: 89.81 E-value: 1.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 36 DMLSL-VDELATMSSKITVEKVELERTPSFSVNRPGEDTGVVFAGIPLGHEFTSLVLALLQVSGRAPKVEQKLIDQIKNI 114
Cdd:TIGR02187 52 PKLKLeIYDFDTPEDKEEAEKYGVERVPTTIILEEGKDGGIRYTGIPAGYEFAALIEDIVRVSQGEPGLSEKTVELLQSL 131
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488053536 115 QGEYHFESYISLSCHNCPDVVQALNVMSVLNSGITHTMIDGAAFKEEVESKDIMAVPTVYLNG 177
Cdd:TIGR02187 132 DEPVRIEVFVTPTCPYCPYAVLMAHKFALANDKILGEMIEANENPDLAEKYGVMSVPKIVINK 194
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
264-496 |
2.85e-20 |
|
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: 91.41 E-value: 2.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 264 KLVASLEEHVKEYDIDVMNLQRAKRL--EKKElieVELENGAILKSKSVIVSTGARWRNVGVPGEAE---FKNKGVAYCP 338
Cdd:COG0446 37 DLLVRTPESFERKGIDVRTGTEVTAIdpEAKT---VTLRDGETLSYDKLVLATGARPRPPPIPGLDLpgvFTLRTLDDAD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 339 HCDGPL--FIGKDVAVIGGGNSGIEAAIDLAGIVKHVTVLEFMPEL--KAD----AVLQERLNSLpNVTVLKNVQTKEIT 410
Cdd:COG0446 114 ALREALkeFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLlgVLDpemaALLEEELREH-GVELRLGETVVAID 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 411 GTDKVnGISYIDRETEEVHHVelqgVFVqIGLVPNTDWLGET-VER-VRGEIVTDKHGATNVPGVFGAGDCTNNPY---- 484
Cdd:COG0446 193 GDDKV-AVTLTDGEEIPADLV----VVA-PGVRPNTELAKDAgLALgERGWIKVDETLQTSDPDVYAAGDCAEVPHpvtg 266
|
250
....*....|..
gi 488053536 485 KQIIISMGSGAN 496
Cdd:COG0446 267 KTVYIPLASAAN 278
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
270-480 |
8.94e-19 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 88.27 E-value: 8.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 270 EEHVKEYDIDVMNLQRAKRL--EKKElieVELENGAILKSKSVIVSTGARWRNVGVPGEAEfknKGV------------- 334
Cdd:COG1251 63 ADFYEENGIDLRLGTRVTAIdrAART---VTLADGETLPYDKLVLATGSRPRVPPIPGADL---PGVftlrtlddadalr 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 335 AYCPHcdgplfiGKDVAVIGGGNSGIEAAIDLAGIVKHVTVLEFMPEL-------KADAVLQERLNSLpNVTVLKNVQTK 407
Cdd:COG1251 137 AALAP-------GKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLlprqldeEAGALLQRLLEAL-GVEVRLGTGVT 208
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488053536 408 EITGTDKVNGISYIDRETeevhhVELQGVFVQIGLVPNTDWLGETVERVRGEIVTDKHGATNVPGVFGAGDCT 480
Cdd:COG1251 209 EIEGDDRVTGVRLADGEE-----LPADLVVVAIGVRPNTELARAAGLAVDRGIVVDDYLRTSDPDIYAAGDCA 276
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
264-483 |
1.48e-18 |
|
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: 88.22 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 264 KLVASLEEHVKEYDIDVMNlQRAKRLEKKElieVELENGAILKSKSVIVSTGARWRNVGVPGEaefknkgvaycphcDGP 343
Cdd:COG1249 92 RLRGGVEELLKKNGVDVIR-GRARFVDPHT---VEVTGGETLTADHIVIATGSRPRVPPIPGL--------------DEV 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 344 LFIG-----------KDVAVIGGGNSGIEAAIDLAGIVKHVTVLEFMPEL--KAD----AVLQERLNSLpNVTVLKNVQT 406
Cdd:COG1249 154 RVLTsdealeleelpKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLlpGEDpeisEALEKALEKE-GIDILTGAKV 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 407 KEITGTDKVNGISYIDRETEEVHHVELqgVFVQIGLVPNTDWLGetVERV------RGEIVTDKHGATNVPGVFGAGDCT 480
Cdd:COG1249 233 TSVEKTGDGVTVTLEDGGGEEAVEADK--VLVATGRRPNTDGLG--LEAAgveldeRGGIKVDEYLRTSVPGIYAIGDVT 308
|
...
gi 488053536 481 NNP 483
Cdd:COG1249 309 GGP 311
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
310-498 |
1.08e-17 |
|
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: 85.19 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 310 VIVSTGA-RWRNVGVPGEA--------EF---KNKGVAYcphcDGPLFIGKDVAVIGGGNSgieaAIDLAGI-----VKH 372
Cdd:COG0493 210 VFLATGAgKPRDLGIPGEDlkgvhsamDFltaVNLGEAP----DTILAVGKRVVVIGGGNT----AMDCARTalrlgAES 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 373 VTVL-----EFMP--ELKADAVLQErlnslpNVTVLKNVQTKEITGTD--KVNGISYIDRE-----------------TE 426
Cdd:COG0493 282 VTIVyrrtrEEMPasKEEVEEALEE------GVEFLFLVAPVEIIGDEngRVTGLECVRMElgepdesgrrrpvpiegSE 355
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488053536 427 EVHHVELqgVFVQIGLVPNTDWLGET----VERvRGEIVTDK-HGATNVPGVFGAGDCTNNPyKQIIISMGSGANAA 498
Cdd:COG0493 356 FTLPADL--VILAIGQTPDPSGLEEElgleLDK-RGTIVVDEeTYQTSLPGVFAGGDAVRGP-SLVVWAIAEGRKAA 428
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
295-483 |
5.33e-15 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 77.27 E-value: 5.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 295 IEVELENGAILKSKSVIVSTGARWRNVgvPGeAEFKNKGVaycpHC-DGPLFIG---KDVAVIGGGNSGIEAAIDLAGIV 370
Cdd:PRK06327 134 IKVTGEDETVITAKHVIIATGSEPRHL--PG-VPFDNKII----LDnTGALNFTevpKKLAVIGAGVIGLELGSVWRRLG 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 371 KHVTVLEFMPELKA---DAVLQERLNSLPN--VTVLKNVQTKEITGTDKVNGISYIDRETEEvHHVELQGVFVQIGLVPN 445
Cdd:PRK06327 207 AEVTILEALPAFLAaadEQVAKEAAKAFTKqgLDIHLGVKIGEIKTGGKGVSVAYTDADGEA-QTLEVDKLIVSIGRVPN 285
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488053536 446 TDWLG-ETVERV---RGEIVTDKHGATNVPGVFGAGDCTNNP 483
Cdd:PRK06327 286 TDGLGlEAVGLKldeRGFIPVDDHCRTNVPNVYAIGDVVRGP 327
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
288-478 |
4.84e-14 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 74.03 E-value: 4.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 288 RLEKKELIEVELENGA-ILKSKSVIVSTGARWRNVgvPGeAEFKNKGVAYCPHCDGPLFIGKDVAVIGGGNSGIEAAIDL 366
Cdd:PRK06416 115 KLVDPNTVRVMTEDGEqTYTAKNIILATGSRPREL--PG-IEIDGRVIWTSDEALNLDEVPKSLVVIGGGYIGVEFASAY 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 367 AGIVKHVTVLEFMPEL-----KADAVLQERLNSLPNVTVLKNVQTKEITGTDkvNGISYIDRETEEVHHVELQGVFVQIG 441
Cdd:PRK06416 192 ASLGAEVTIVEALPRIlpgedKEISKLAERALKKRGIKIKTGAKAKKVEQTD--DGVTVTLEDGGKEETLEADYVLVAVG 269
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488053536 442 LVPNTDWLG--ET-VERVRGEIVTDKHGATNVPGVFGAGD 478
Cdd:PRK06416 270 RRPNTENLGleELgVKTDRGFIEVDEQLRTNVPNIYAIGD 309
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
269-477 |
5.94e-13 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 69.56 E-value: 5.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 269 LEEHVKEYDIDVMNLQRAKRLEK-KELIEVELENGAIlKSKSVIVSTGarwrNVGVPGEAEFKNKGV--AYCPHCDgPLF 345
Cdd:pfam13738 81 LRRVADHFELPINLFEEVTSVKKeDDGFVVTTSKGTY-QARYVIIATG----EFDFPNKLGVPELPKhySYVKDFH-PYA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 346 iGKDVAVIGGGNSGIEAAIDLAGIVKHVTVLEFMPELKAD---------AVLQERLNSLPN---VTVLKNVQTKEITGTD 413
Cdd:pfam13738 155 -GQKVVVIGGYNSAVDAALELVRKGARVTVLYRGSEWEDRdsdpsyslsPDTLNRLEELVKngkIKAHFNAEVKEITEVD 233
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488053536 414 KVNGISYIDRETEEVHHVelqgVFVQIGLVPNTDWLgetverVRGEIVTDKHGA---------TNVPGVFGAG 477
Cdd:pfam13738 234 VSYKVHTEDGRKVTSNDD----PILATGYHPDLSFL------KKGLFELDEDGRpvlteetesTNVPGLFLAG 296
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
308-481 |
5.03e-12 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 67.90 E-value: 5.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 308 KSVIVSTGA-RWRNVGVPGEAefkNKGVAYC---------PHCDGPLFIGKDVAVIGGGNSgieaAIDLAGI-----VKH 372
Cdd:PRK11749 227 DAVFIGTGAgLPRFLGIPGEN---LGGVYSAvdfltrvnqAVADYDLPVGKRVVVIGGGNT----AMDAARTakrlgAES 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 373 VTVL-----EFMPelkadAVLQERLNSLPN-VTVLKNVQTKEITGTDKVN-GISYI----------DRETEEVHH----V 431
Cdd:PRK11749 300 VTIVyrrgrEEMP-----ASEEEVEHAKEEgVEFEWLAAPVEILGDEGRVtGVEFVrmelgepdasGRRRVPIEGseftL 374
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488053536 432 ELQGVFVQIGLVPNTDWL----GETVERVRGEIVTDKHGATNVPGVFGAGDCTN 481
Cdd:PRK11749 375 PADLVIKAIGQTPNPLILsttpGLELNRWGTIIADDETGRTSLPGVFAGGDIVT 428
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
295-483 |
3.52e-11 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 65.20 E-value: 3.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 295 IEVeleNGAILKSKSVIVSTGARWRNVgvPGEAEFKNKGVAYCphcDGPLFI---GKDVAVIGGGNSGIEAAIDLAGIVK 371
Cdd:PRK06292 122 VEV---NGERIEAKNIVIATGSRVPPI--PGVWLILGDRLLTS---DDAFELdklPKSLAVIGGGVIGLELGQALSRLGV 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 372 HVTVLEFMPEL----------KADAVLQERLNSLPNVTVlknvqtKEITGTDKVNGISYIDRETEEVHHVELqgVFVQIG 441
Cdd:PRK06292 194 KVTVFERGDRIlpledpevskQAQKILSKEFKIKLGAKV------TSVEKSGDEKVEELEKGGKTETIEADY--VLVATG 265
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488053536 442 LVPNTDWLG------ETVERvrGEIVTDKHGATNVPGVFGAGDCTNNP 483
Cdd:PRK06292 266 RRPNTDGLGlentgiELDER--GRPVVDEHTQTSVPGIYAAGDVNGKP 311
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
306-498 |
3.03e-10 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 61.93 E-value: 3.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 306 KSKSVIVSTGA-RWRNVGVPGEA------------EFKNKGVAYCPHCDGPLFIGKDVAVIGGGNSGIEAAID--LAGiV 370
Cdd:PRK12770 118 KYDAVLIATGTwKSRKLGIPGEDlpgvysaleylfRIRAAKLGYLPWEKVPPVEGKKVVVVGAGLTAVDAALEavLLG-A 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 371 KHVTVL--EFMPELKADAVLQERLNSLpNVTVLKNVQTKEITGTDKVNGISYIDRE---------------TEEVHHVEL 433
Cdd:PRK12770 197 EKVYLAyrRTINEAPAGKYEIERLIAR-GVEFLELVTPVRIIGEGRVEGVELAKMRlgepdesgrprpvpiPGSEFVLEA 275
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488053536 434 QGVFVQIGLVP----NTDWLGETVERvRGEIVTDKHGATNVPGVFGAGDCTNNPYKqIIISMGSGANAA 498
Cdd:PRK12770 276 DTVVFAIGEIPtppfAKECLGIELNR-KGEIVVDEKHMTSREGVFAAGDVVTGPSK-IGKAIKSGLRAA 342
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
348-496 |
5.22e-10 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 61.59 E-value: 5.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 348 KDVAVIGGGNSGIEAAIDLAGIVKHVTVLE---------FMPELKAdaVLQERLNSlPNVTVLKNVQTKEITGTDKVNGI 418
Cdd:PRK09564 150 KNIVIIGAGFIGLEAVEAAKHLGKNVRIIQledrilpdsFDKEITD--VMEEELRE-NGVELHLNEFVKSLIGEDKVEGV 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 419 SYIDREteevhhVELQGVFVQIGLVPNTDWLGET-VERVR-GEIVTDKHGATNVPGVFGAGDC-------TNnpyKQIII 489
Cdd:PRK09564 227 VTDKGE------YEADVVIVATGVKPNTEFLEDTgLKTLKnGAIIVDEYGETSIENIYAAGDCatiynivSN---KNVYV 297
|
....*..
gi 488053536 490 SMGSGAN 496
Cdd:PRK09564 298 PLATTAN 304
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
350-418 |
6.05e-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: 6.05e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488053536 350 VAVIGGGNSGIEAAIDLAGIVKHVTVLEFMPELK------ADAVLQERLNSLpNVTVLKNVQTKEITGTDKVNGI 418
Cdd:pfam00070 2 VVVVGGGYIGLELAGALARLGSKVTVVERRDRLLpgfdpeIAKILQEKLEKN-GIEFLLNTTVEAIEGNGDGVVV 75
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
348-479 |
1.67e-09 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 60.23 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 348 KDVAVIGGGNSGIEAAIDLAGIVKHVTVLEFMPELKAD-------AVLQERLNSLpNVTVLKNVQTKEITGTDKVNGISY 420
Cdd:TIGR02374 141 KKAAVIGGGLLGLEAAVGLQNLGMDVSVIHHAPGLMAKqldqtagRLLQRELEQK-GLTFLLEKDTVEIVGATKADRIRF 219
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 488053536 421 IDRETEEVHHVelqgVFVqIGLVPNTDWLGETVERVRGEIVTDKHGATNVPGVFGAGDC 479
Cdd:TIGR02374 220 KDGSSLEADLI----VMA-AGIRPNDELAVSAGIKVNRGIIVNDSMQTSDPDIYAVGEC 273
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
310-479 |
2.40e-09 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 59.41 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 310 VIVSTGA-RWRNVGVPGEaEFK------------NKGVAYCPHCDGPLFIGKDVAVIGGGNSGIEA---AIDL-AgivKH 372
Cdd:PRK12810 232 VFLGTGAyKPRDLGIPGR-DLDgvhfamdfliqnTRRVLGDETEPFISAKGKHVVVIGGGDTGMDCvgtAIRQgA---KS 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 373 VTVLEFMPELKAdavlqERLNSLPNVTVLK----------------NVQTKEITGTD-KVNGISYIDRETEEVHHVELQG 435
Cdd:PRK12810 308 VTQRDIMPMPPS-----RRNKNNPWPYWPMklevsnaheegverefNVQTKEFEGENgKVTGVKVVRTELGEGDFEPVEG 382
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488053536 436 ---------VFVQIGLV-PNTDWLGE-TVERV-RGEIVTDKHG-ATNVPGVFGAGDC 479
Cdd:PRK12810 383 sefvlpadlVLLAMGFTgPEAGLLAQfGVELDeRGRVAAPDNAyQTSNPKVFAAGDM 439
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
262-376 |
4.22e-09 |
|
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: 58.34 E-value: 4.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 262 GPKLVASLEEHVKEYDIDV-----MNLQRAKRLEKKELIEVELENGAILKSKSVIVSTGARWR-NV-GVPGEAEFKnkGV 334
Cdd:COG2072 79 GDEILAYLEAYADKFGLRRpirfgTEVTSARWDEADGRWTVTTDDGETLTARFVVVATGPLSRpKIpDIPGLEDFA--GE 156
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 488053536 335 AYcpHC---DGPL-FIGKDVAVIGGGNSGIEAAIDLAGIVKHVTVL 376
Cdd:COG2072 157 QL--HSadwRNPVdLAGKRVLVVGTGASAVQIAPELARVAAHVTVF 200
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
296-483 |
2.08e-08 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 56.30 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 296 EVELENGA---ILKSKSVIVSTGARWRNVGVPGEAEFKN----KGVAYCPHcdgplfIGKDVAVIGGGNSGIEAAIDLAG 368
Cdd:PRK07251 105 VIEVQAGDekiELTAETIVINTGAVSNVLPIPGLADSKHvydsTGIQSLET------LPERLGIIGGGNIGLEFAGLYNK 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 369 IVKHVTVLEFMPEL--KADAVLQERLNSL---PNVTVLKNVQTKEITGT-DKVngISYIDRETEEvhhveLQGVFVQIGL 442
Cdd:PRK07251 179 LGSKVTVLDAASTIlpREEPSVAALAKQYmeeDGITFLLNAHTTEVKNDgDQV--LVVTEDETYR-----FDALLYATGR 251
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488053536 443 VPNTDWLG------ETVERvrGEIVTDKHGATNVPGVFGAGDCTNNP 483
Cdd:PRK07251 252 KPNTEPLGlentdiELTER--GAIKVDDYCQTSVPGVFAVGDVNGGP 296
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
209-505 |
3.06e-08 |
|
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: 56.11 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 209 YDVLVVGGGPAGASAAIYAARKGIRTGIV-AERFGG-----------------QVMDT------MGIE------NFISV- 257
Cdd:TIGR01350 2 YDVIVIGGGPGGYVAAIRAAQLGLKVALVeKEYLGGtclnvgciptkallhsaEVYDEikhakdLGIEvenvsvDWEKMq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 258 KRTEG--PKLVASLEEHVKEYDIDVMNlQRAKRLEKKElIEVELENGA-ILKSKSVIVSTGARWRnvGVPGEAEFKNKGV 334
Cdd:TIGR01350 82 KRKNKvvKKLVGGVSGLLKKNKVTVIK-GEAKFLDPGT-VSVTGENGEeTLEAKNIIIATGSRPR--SLPGPFDFDGKVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 335 aycpHC-DGPLF---IGKDVAVIGGGNSGIEAAIDLAGIVKHVTVLEFMPELKA--DA----VLQERLNSLpNVTVLKNV 404
Cdd:TIGR01350 158 ----ITsTGALNleeVPESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRILPgeDAevskVLQKALKKK-GVKILTNT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 405 QTKEITGTDkvNGISYiDRETEEVHHVELQGVFVQIGLVPNTDWLGetVERV------RGEIVTDKHGATNVPGVFGAGD 478
Cdd:TIGR01350 233 KVTAVEKND--DQVTY-ENKGGETETLTGEKVLVAVGRKPNTEGLG--LEKLgveldeRGRIVVDEYMRTNVPGIYAIGD 307
|
330 340 350
....*....|....*....|....*....|...
gi 488053536 479 CTNNP------YKQIIISMGSGANAALGAFDYL 505
Cdd:TIGR01350 308 VIGGPmlahvaSHEGIVAAENIAGKEPAHIDYD 340
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
341-505 |
4.49e-08 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 55.54 E-value: 4.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 341 DGP-LFIGKDVAVIGGGNSGIEAAIDLAGIVK--------HVTVLEF-MPELKAD-----AVLQERLNSLPN---VTVLk 402
Cdd:PRK13984 411 EGPkPKIPRSLVVIGGGNVAMDIARSMARLQKmeygevnvKVTSLERtFEEMPADmeeieEGLEEGVVIYPGwgpMEVV- 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 403 nVQTKEITGTDKVNGISYIDR---------ETEEVHHvELQGVFVQIGLVPNTDWLGETV----ERVRGEIVTDKHGATN 469
Cdd:PRK13984 490 -IENDKVKGVKFKKCVEVFDEegrfnpkfdESDQIIV-EADMVVEAIGQAPDYSYLPEELksklEFVRGRILTNEYGQTS 567
|
170 180 190
....*....|....*....|....*....|....*.
gi 488053536 470 VPGVFGAGDCTNNPykQIIISMGSGANAALGAFDYL 505
Cdd:PRK13984 568 IPWLFAGGDIVHGP--DIIHGVADGYWAAEGIDMYL 601
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
346-483 |
6.00e-08 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 55.16 E-value: 6.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 346 IGKDVAVIGGGNSGIEAAIDLAGIVKHVTVLE----FMPElkaDAVLQERLNS---LPNVTVLKNVQTKEItgtdkvngi 418
Cdd:PRK13748 269 IPERLAVIGSSVVALELAQAFARLGSKVTILArstlFFRE---DPAIGEAVTAafrAEGIEVLEHTQASQV--------- 336
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488053536 419 SYIDRE-TEEVHHVELQG--VFVQIGLVPNT-----DWLGETVERvRGEIVTDKHGATNVPGVFGAGDCTNNP 483
Cdd:PRK13748 337 AHVDGEfVLTTGHGELRAdkLLVATGRAPNTrslalDAAGVTVNA-QGAIVIDQGMRTSVPHIYAAGDCTDQP 408
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
292-505 |
6.99e-08 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 54.64 E-value: 6.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 292 KELIEVElengailKSKSVIVSTGARW-RNVGVPGEA--------EF---KNKGVAYCPHCDGPLFIGKDVAVIGGGNSG 359
Cdd:PRK12831 221 DELLEEE-------GFDAVFIGSGAGLpKFMGIPGENlngvfsanEFltrVNLMKAYKPEYDTPIKVGKKVAVVGGGNVA 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 360 IEAAIDLAGIVKHVTVLEFMPELKADAVLQERLNSLPN-VTVLKNVQTKEITGTDK--VNGISYIDRETEEVHH------ 430
Cdd:PRK12831 294 MDAARTALRLGAEVHIVYRRSEEELPARVEEVHHAKEEgVIFDLLTNPVEILGDENgwVKGMKCIKMELGEPDAsgrrrp 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 431 VELQG---------VFVQIGLVPNTDWLGETVE---RVRGEIVTDK-HGATNVPGVFGAGDCTNNPyKQIIISMGSGANA 497
Cdd:PRK12831 374 VEIEGsefvlevdtVIMSLGTSPNPLISSTTKGlkiNKRGCIVADEeTGLTSKEGVFAGGDAVTGA-ATVILAMGAGKKA 452
|
....*...
gi 488053536 498 ALGAFDYL 505
Cdd:PRK12831 453 AKAIDEYL 460
|
|
| PfPDO_like_N |
cd02975 |
Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO)-like family, N-terminal TRX-fold ... |
1-97 |
8.77e-08 |
|
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: 50.47 E-value: 8.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 1 MILDADIKTQLSQYLQLMENDILLKVSAGDDNV--SKDMLSLVDELATMSSKITVEKVEL----ERTPSFSVNR------ 68
Cdd:cd02975 2 LLSDEDRKALKEEFFKEMKNPVDLVVFSSKEGCqyCEVTKQLLEELSELSDKLKLEIYDFdedkEKAEKYGVERvpttif 81
|
90 100 110
....*....|....*....|....*....|..
gi 488053536 69 ---PGEDTGVVFAGIPLGHEFTSLVLALLQVS 97
Cdd:cd02975 82 lqdGGKDGGIRYYGLPAGYEFASLIEDIVRVS 113
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
253-482 |
5.00e-07 |
|
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member of the pyridine nucleotide disulfide oxidoreductase family contains a C-terminal motif Cys-SeCys-Gly, where SeCys is selenocysteine encoded by TGA (in some sequence reports interpreted as a stop codon). In some members of this subfamily, Cys-SeCys-Gly is replaced by Cys-Cys-Gly. The reach of the selenium atom at the C-term arm of the protein is proposed to allow broad substrate specificity.
Pssm-ID: 273624 [Multi-domain] Cd Length: 484 Bit Score: 52.16 E-value: 5.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 253 NFISVKRTEGPKLVASLEEHVKEYDIDVMNLQRAKR---------LEKKELIEVELENGA--ILKSKSVIVSTGARWRNV 321
Cdd:TIGR01438 79 KVEETVKHDWKRLVEAVQNHIGSLNWGYRVALREKKvkyenayaeFVDKHRIKATNKKGKekIYSAERFLIATGERPRYP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 322 GVPGEAEFKNKG-----VAYCPhcdgplfiGKDVaVIGGGNSGIEAAIDLAGIVKHVTVLEFMPELKA---DAV------ 387
Cdd:TIGR01438 159 GIPGAKELCITSddlfsLPYCP--------GKTL-VVGASYVALECAGFLAGIGLDVTVMVRSILLRGfdqDCAnkvgeh 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 388 LQERLNSLPNVTVLKNVQTKE----ITGTDKVNGISYidreteevhhvELQGVFVQIGLVPNTDWL-----GETVERVRG 458
Cdd:TIGR01438 230 MEEHGVKFKRQFVPIKVEQIEakvlVEFTDSTNGIEE-----------EYDTVLLAIGRDACTRKLnlenvGVKINKKTG 298
|
250 260
....*....|....*....|....
gi 488053536 459 EIVTDKHGATNVPGVFGAGDCTNN 482
Cdd:TIGR01438 299 KIPADEEEQTNVPYIYAVGDILED 322
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
340-479 |
1.11e-06 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 50.69 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 340 CDGPLFIGKDVAVIGGGNSGIEAAIDLAGIVKHVTVLE--------FMPELKAdAVLQERLNSLpNVTVLKNVQTKEITG 411
Cdd:PRK04965 134 AETQLRDAQRVLVVGGGLIGTELAMDLCRAGKAVTLVDnaasllasLMPPEVS-SRLQHRLTEM-GVHLLLKSQLQGLEK 211
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488053536 412 TDKVNGISYIDRETEEVhhvelQGVFVQIGLVPNTDWLGETVERVRGEIVTDKHGATNVPGVFGAGDC 479
Cdd:PRK04965 212 TDSGIRATLDSGRSIEV-----DAVIAAAGLRPNTALARRAGLAVNRGIVVDSYLQTSAPDIYALGDC 274
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
348-481 |
2.39e-06 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 49.77 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 348 KDVAVIGGGNSGIEaaidLAGIV------------KHVTVLEFMPELKAdaVLQERLNSlPNVTVLKNVQTKEITGTDkv 415
Cdd:PRK06116 168 KRVAVVGAGYIAVE----FAGVLnglgsethlfvrGDAPLRGFDPDIRE--TLVEEMEK-KGIRLHTNAVPKAVEKNA-- 238
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488053536 416 NGISYIDRETEEVHHVELqgVFVQIGLVPNTDWLG------ETVERvrGEIVTDKHGATNVPGVFGAGDCTN 481
Cdd:PRK06116 239 DGSLTLTLEDGETLTVDC--LIWAIGREPNTDGLGlenagvKLNEK--GYIIVDEYQNTNVPGIYAVGDVTG 306
|
|
| Thioredoxin_3 |
pfam13192 |
Thioredoxin domain; |
124-194 |
2.56e-06 |
|
Thioredoxin domain;
Pssm-ID: 433026 [Multi-domain] Cd Length: 71 Bit Score: 44.90 E-value: 2.56e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488053536 124 ISLSCHNCPDVVQALNvMSVLNSGITHTMIDGAAFKEeVESKDIMAVPTVYLNGESFGSGRMTLEEILAKM 194
Cdd:pfam13192 1 LGPGCPKCPQLEKAVK-EAAAELGIDAEVEKVTDFPE-IAKYGVMSTPALVINGKVVSSGKVPSEEEIRKL 69
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
301-485 |
4.42e-06 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 49.05 E-value: 4.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 301 NGAILKSKSVIVSTGARWRNVGVPGEAE---FKNKGV---AYCPhcdgplfigKDVAVIGGGNSGIEAAIDLAGIVKHVT 374
Cdd:PRK06370 128 GGETLRAKRIFINTGARAAIPPIPGLDEvgyLTNETIfslDELP---------EHLVIIGGGYIGLEFAQMFRRFGSEVT 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 375 VLEFMPEL------KADAVLQERLNSLpNVTVLKNVQTKEITGTDkvNGISYIDRETEEVHHVELQGVFVQIGLVPNTDW 448
Cdd:PRK06370 199 VIERGPRLlpredeDVAAAVREILERE-GIDVRLNAECIRVERDG--DGIAVGLDCNGGAPEITGSHILVAVGRVPNTDD 275
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488053536 449 LGetVERV------RGEIVTDKHGATNVPGVFGAGDCtNNPYK 485
Cdd:PRK06370 276 LG--LEAAgvetdaRGYIKVDDQLRTTNPGIYAAGDC-NGRGA 315
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
308-505 |
2.53e-05 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 47.04 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 308 KSVIVSTGARWRN-VGVPGE--------AEF---KNKGVAYCPHCDGPLFIGKDVAVIGGGNSGIEA---AIDLAGivKH 372
Cdd:PRK12778 519 KGIFIASGAGLPNfMNIPGEnsngvmssNEYltrVNLMDAASPDSDTPIKFGKKVAVVGGGNTAMDSartAKRLGA--ER 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 373 VTVLEFMPELKADAVLQErlnslpnvtvLKNVQTKEITGTDKVNGISYIDRETEEVHHVELQG----------------- 435
Cdd:PRK12778 597 VTIVYRRSEEEMPARLEE----------VKHAKEEGIEFLTLHNPIEYLADEKGWVKQVVLQKmelgepdasgrrrpvai 666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 436 -----------VFVQIGLVPNTdWLGETVERV----RGEIVTDKHGATNVPGVFGAGDCTNNPyKQIIISMGSGANAALG 500
Cdd:PRK12778 667 pgstftvdvdlVIVSVGVSPNP-LVPSSIPGLelnrKGTIVVDEEMQSSIPGIYAGGDIVRGG-ATVILAMGDGKRAAAA 744
|
....*
gi 488053536 501 AFDYL 505
Cdd:PRK12778 745 IDEYL 749
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
352-480 |
6.59e-05 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 45.24 E-value: 6.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 352 VIGGGNSGIEAAIDLAGIVKHVTVL----EFMPELKADA------VLQERlnslpNVTVLKN--VQTKEITGTDKVNGIS 419
Cdd:PRK07845 182 VVGSGVTGAEFASAYTELGVKVTLVssrdRVLPGEDADAaevleeVFARR-----GMTVLKRsrAESVERTGDGVVVTLT 256
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488053536 420 yiD-RETEEVHhvelqgVFVQIGLVPNTDWLGetVERV------RGEIVTDKHGATNVPGVFGAGDCT 480
Cdd:PRK07845 257 --DgRTVEGSH------ALMAVGSVPNTAGLG--LEEAgveltpSGHITVDRVSRTSVPGIYAAGDCT 314
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
265-479 |
6.81e-05 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 45.12 E-value: 6.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 265 LVASLEEHVKEYDIDVMnLQRAKRL--EKKElieVELENGAILKSKSVIVSTGARWRNVGVPGEAEFknkGVAYCP---- 338
Cdd:COG1252 58 IAIPLRELLRRAGVRFI-QGEVTGIdpEART---VTLADGRTLSYDYLVIATGSVTNFFGIPGLAEH---ALPLKTleda 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 339 --------------HCDGPLfigkDVAVIGGGNSGIEAAIDLAGIVKH-------------VTVLEFMPEL------KAD 385
Cdd:COG1252 131 lalrerllaaferaERRRLL----TIVVVGGGPTGVELAGELAELLRKllrypgidpdkvrITLVEAGPRIlpglgeKLS 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 386 AVLQERLNSLpNVTVLKNVQTKEITGtdkvNGISYIDRETEEVHHVelqgVFVqIGLVPN--TDWLGETVERvRGEIVTD 463
Cdd:COG1252 207 EAAEKELEKR-GVEVHTGTRVTEVDA----DGVTLEDGEEIPADTV----IWA-AGVKAPplLADLGLPTDR-RGRVLVD 275
|
250
....*....|....*..
gi 488053536 464 KHG-ATNVPGVFGAGDC 479
Cdd:COG1252 276 PTLqVPGHPNVFAIGDC 292
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
348-430 |
2.43e-04 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 43.70 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 348 KDVAVIGGGNSGIEAAIDLAGIVKHVTVLEFMPEL---------------KADAVLQERLNSL---PNVTVLKNVQTKEI 409
Cdd:COG1148 141 KRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELggraaqlhktfpgldCPQCILEPLIAEVeanPNITVYTGAEVEEV 220
|
90 100
....*....|....*....|....
gi 488053536 410 TGTD---KVNgISYIDRETEEVHH 430
Cdd:COG1148 221 SGYVgnfTVT-IKKGPREEIEIEV 243
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
298-488 |
3.48e-04 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 43.07 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 298 ELENGAILKSKSVIVSTGarwrnvgvpGEAEFKN-KGVAYCPHCDGPLFI--GKDVAVIGGGnsgiEAAIDLAGIVKHVT 374
Cdd:PTZ00058 194 QLDDGQVIEGKNILIAVG---------NKPIFPDvKGKEFTISSDDFFKIkeAKRIGIAGSG----YIAVELINVVNRLG 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 375 VLEFMPELKADA-------VLQERLNSLP--NVTVLKNVQTKEITGTDKVNGISYIDRETEEVHhveLQGVFVQIGLVPN 445
Cdd:PTZ00058 261 AESYIFARGNRLlrkfdetIINELENDMKknNINIITHANVEEIEKVKEKNLTIYLSDGRKYEH---FDYVIYCVGRSPN 337
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488053536 446 TDWL---GETVERVRGEIVTDKHGATNVPGVFGAGDCTNNPYKQII 488
Cdd:PTZ00058 338 TEDLnlkALNIKTPKGYIKVDDNQRTSVKHIYAVGDCCMVKKNQEI 383
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
347-479 |
1.10e-03 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 41.64 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 347 GKDVAVIGGGNSGIEAAIDLA--GIVKHvtVLEFMPELKADAV-------LQERLNSLpNVTVLKNVQTKEIT--GTDKV 415
Cdd:PRK14989 145 SKRGAVVGGGLLGLEAAGALKnlGVETH--VIEFAPMLMAEQLdqmggeqLRRKIESM-GVRVHTSKNTLEIVqeGVEAR 221
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488053536 416 NGISYIDRETEEVHHVelqgVFvQIGLVPNtDWLGETVERV---RGEIVTDKHGATNVPGVFGAGDC 479
Cdd:PRK14989 222 KTMRFADGSELEVDFI----VF-STGIRPQ-DKLATQCGLAvapRGGIVINDSCQTSDPDIYAIGEC 282
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
298-485 |
1.98e-03 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 40.71 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 298 ELENGAILKSKSVIVSTGARWRNVGVPGEAefknkGVAYcpHCDGPLF----IGKDVAVIGGGNSGIEAAIDLAGIVKHV 373
Cdd:PRK07846 120 RTGDGEEITADQVVIAAGSRPVIPPVIADS-----GVRY--HTSDTIMrlpeLPESLVIVGGGFIAAEFAHVFSALGVRV 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488053536 374 TVLEFMPEL--KADAVLQERLNSLPNV--TVLKNVQTKEITGTDKVNGISYIDRETeevhhVELQGVFVQIGLVPNTDWL 449
Cdd:PRK07846 193 TVVNRSGRLlrHLDDDISERFTELASKrwDVRLGRNVVGVSQDGSGVTLRLDDGST-----VEADVLLVATGRVPNGDLL 267
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488053536 450 G------ETVERvrGEIVTDKHGATNVPGVFGAGDCTnNPYK 485
Cdd:PRK07846 268 DaaaagvDVDED--GRVVVDEYQRTSAEGVFALGDVS-SPYQ 306
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
348-382 |
7.72e-03 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 38.72 E-value: 7.72e-03
10 20 30
....*....|....*....|....*....|....*
gi 488053536 348 KDVAVIGGGNSGIEAAIDLAGIVKHVTVLEFMPEL 382
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKL 35
|
|
| |
