|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
1-521 |
0e+00 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 1027.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 1 MLDTNMKTQLKAYLEKLTKPVELIATLDDSAKSAEIKELLAEIAELSPKVTFKEDnSLNVRKPSFLITNPGSELGPRFAG 80
Cdd:PRK15317 1 MLDANLKTQLKQYLELLERPIELVASLDDSEKSAELKELLEEIASLSDKITVEED-SLDVRKPSFSITRPGEDTGVRFAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 81 SPLGHEFTSLVLALLWTGGHPSKEAQALLEQIRDIDGDFEFETYYSLSCHNCPDVVQALNLMSVLNPRIKHTAIDGGTFQ 160
Cdd:PRK15317 80 IPMGHEFTSLVLALLQVGGHPPKLDQEVIEQIKALDGDFHFETYVSLSCHNCPDVVQALNLMAVLNPNITHTMIDGALFQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 161 NEITDRNVMGVPAVYLNGQEFGQGRMTLTEIVAKVDTGAEKRAAEALNKRDAYDVLIVGSGPAGAAAAVYSARKGIRTGL 240
Cdd:PRK15317 160 DEVEARNIMAVPTVFLNGEEFGQGRMTLEEILAKLDTGAAARAAEELNAKDPYDVLVVGGGPAGAAAAIYAARKGIRTGI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 241 MGERFGGQVLDTVDIENYISVPKTEGQKLAGALKAHVSDYDVDVIDSQSASKLVPAAvegGLHQIETASGAVLKARSIII 320
Cdd:PRK15317 240 VAERFGGQVLDTMGIENFISVPETEGPKLAAALEEHVKEYDVDIMNLQRASKLEPAA---GLIEVELANGAVLKAKTVIL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 321 ATGAKWRNMNVPGEDQYRTKGVTYCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVEHVTLLEFAPEMKADQVLQDKV 400
Cdd:PRK15317 317 ATGARWRNMNVPGEDEYRNKGVAYCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVKHVTVLEFAPELKADQVLQDKL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 401 RSLKNVDIILNAQTTEVKGDGSKVTGLEYRDRVSGDVHSVQLSGIFVQIGLLPNTTWLEGAIERNRMGEIIIDAKCETSV 480
Cdd:PRK15317 397 RSLPNVTIITNAQTTEVTGDGDKVTGLTYKDRTTGEEHHLELEGVFVQIGLVPNTEWLKGTVELNRRGEIIVDARGATSV 476
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 798944333 481 KGVFAAGDCTTVPYKQIIIATGEGAKASLSAFDYLIRTKTA 521
Cdd:PRK15317 477 PGVFAAGDCTTVPYKQIIIAMGEGAKAALSAFDYLIRNSAA 517
|
|
| AhpF |
TIGR03140 |
alkyl hydroperoxide reductase subunit F; This enzyme is the partner of the peroxiredoxin ... |
1-517 |
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: 812.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 1 MLDTNMKTQLKAYLEKLTKPVELIATLDDSAKSAEIKELLAEIAELSPKVTFKEDNSLNVRKPSFLITNPGSELGPRFAG 80
Cdd:TIGR03140 1 MLDQSLLAQLKSYLASLENPVTLVLSAGSHEKSKELLELLDEIASLSDKISLTQNTADTLRKPSFTILRDGADTGIRFAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 81 SPLGHEFTSLVLALLWTGGHPSKEAQALLEQIRDIDGDFEFETYYSLSCHNCPDVVQALNLMSVLNPRIKHTAIDGGTFQ 160
Cdd:TIGR03140 81 IPGGHEFTSLVLAILQVGGHGPKLDEGIIDRIRRLNGPLHFETYVSLTCQNCPDVVQALNQMALLNPNISHTMIDGALFQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 161 NEITDRNVMGVPAVYLNGQEFGQGRMTLTEIVAKVDTGAEKRAAEALNKRDAYDVLIVGSGPAGAAAAVYSARKGIRTGL 240
Cdd:TIGR03140 161 DEVEALGIQGVPAVFLNGEEFHNGRMDLAELLEKLEETAGVEAASALEQLDPYDVLVVGGGPAGAAAAIYAARKGLRTAM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 241 MGERFGGQVLDTVDIENYISVPKTEGQKLAGALKAHVSDYDVDVIDSQSASKLvpaAVEGGLHQIETASGAVLKARSIII 320
Cdd:TIGR03140 241 VAERIGGQVKDTVGIENLISVPYTTGSQLAANLEEHIKQYPIDLMENQRAKKI---ETEDGLIVVTLESGEVLKAKSVIV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 321 ATGAKWRNMNVPGEDQYRTKGVTYCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVEHVTLLEFAPEMKADQVLQDKV 400
Cdd:TIGR03140 318 ATGARWRKLGVPGEKEYIGKGVAYCPHCDGPFFKGKDVAVIGGGNSGIEAAIDLAGIVRHVTVLEFADELKADKVLQDKL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 401 RSLKNVDIILNAQTTEVKGDGSKVTGLEYRDRVSGDVHSVQLSGIFVQIGLLPNTTWLEGAIERNRMGEIIIDAKCETSV 480
Cdd:TIGR03140 398 KSLPNVDILTSAQTTEIVGDGDKVTGIRYQDRNSGEEKQLDLDGVFVQIGLVPNTEWLKDAVELNRRGEIVIDERGRTSV 477
|
490 500 510
....*....|....*....|....*....|....*..
gi 798944333 481 KGVFAAGDCTTVPYKQIIIATGEGAKASLSAFDYLIR 517
Cdd:TIGR03140 478 PGIFAAGDVTTVPYKQIIIAMGEGAKAALSAFDYLIR 514
|
|
| AhpF |
COG3634 |
Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms]; |
1-197 |
4.03e-109 |
|
Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms];
Pssm-ID: 442851 [Multi-domain] Cd Length: 200 Bit Score: 322.85 E-value: 4.03e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 1 MLDTNMKTQLKAYLEKLTKPVELIATLDDSAKSAEIKELLAEIAELSPKVTFKEDNSLNV-RKPSFLITNPGSELGPRFA 79
Cdd:COG3634 3 MLDDELKAQLKEYLEKLKNPVELVLFLDDCEKSEELRELLEEIASLSDKISLEVYDKDDVeRAPSFAILRDGEDTGIRFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 80 GSPLGHEFTSLVLALLWTGGHPSKEAQALLEQIRDIDGDFEFETYYSLSCHNCPDVVQALNLMSVLNPRIKHTAIDGGTF 159
Cdd:COG3634 83 GIPSGHEFTSLVLALLQVSGHPPKLSEETIEQIKALDGPVHFEVFVSLSCPNCPDVVQALNLMAVLNPNITHEMIDGAEF 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 798944333 160 QNEITDRNVMGVPAVYLNGQEFGQGRMTLTEIVAKVDT 197
Cdd:COG3634 163 PDEAEKYGVMSVPTVVLNGEVFFVGRMPEEEILEKLDT 200
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
229-515 |
1.12e-91 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 282.39 E-value: 1.12e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 229 VYSARKGIRTGLM-GERFGGQVLDTVDIENYISVP-KTEGQKLAGALKAHVSDYDVDVIdSQSASKLVPaavEGGLHQIE 306
Cdd:COG0492 17 IYAARAGLKTLVIeGGEPGGQLATTKEIENYPGFPeGISGPELAERLREQAERFGAEIL-LEEVTSVDK---DDGPFRVT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 307 TASGAVLKARSIIIATGAKWRNMNVPGEDQYRTKGVTYCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVEHVTLLEF 386
Cdd:COG0492 93 TDDGTEYEAKAVIIATGAGPRKLGLPGEEEFEGRGVSYCATCDGFFFRGKDVVVVGGGDSALEEALYLTKFASKVTLIHR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 387 APEMKADQVLQDKVRSLKNVDIILNAQTTEVKGDGsKVTGLEYRDRVSGDVHSVQLSGIFVQIGLLPNTTWLEGA-IERN 465
Cdd:COG0492 173 RDELRASKILVERLRANPKIEVLWNTEVTEIEGDG-RVEGVTLKNVKTGEEKELEVDGVFVAIGLKPNTELLKGLgLELD 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 798944333 466 RMGEIIIDAKCETSVKGVFAAGDCTTVPYKQIIIATGEGAKASLSAFDYL 515
Cdd:COG0492 252 EDGYIVVDEDMETSVPGVFAAGDVRDYKYRQAATAAGEGAIAALSAARYL 301
|
|
| TRX_reduct |
TIGR01292 |
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ... |
214-515 |
2.90e-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: 242.15 E-value: 2.90e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 214 DVLIVGSGPAGAAAAVYSARKGIRTGLM-GERFGGQVLDTVDIENYISVPKT-EGQKLAGALKAHVSDYDVDVI--DSQS 289
Cdd:TIGR01292 1 DVIIIGAGPAGLTAAIYAARANLKPLLIeGMEPGGQLTTTTEVENYPGFPEGiSGPELMEKMKEQAVKFGAEIIyeEVIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 290 ASKLVPAAVegglhqIETASGAVLKARSIIIATGAKWRNMNVPGEDQYRTKGVTYCPHCDGPLFKGKRVAVIGGGNSGVE 369
Cdd:TIGR01292 81 VDKSDRPFK------VYTGDGKEYTAKAVIIATGASARKLGIPGEDEFWGRGVSYCATCDGPFFKNKEVAVVGGGDSAIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 370 AAIDLAGIVEHVTLLEFAPEMKADQVLQDKVRSLKNVDIILNAQTTEVKGDgSKVTGLEYRDRVSGDVHSVQLSGIFVQI 449
Cdd:TIGR01292 155 EALYLTRIAKKVTLVHRRDKFRAEKILLDRLKKNPKIEFLWNSTVEEIVGD-NKVEGVKIKNTVTGEEEELEVDGVFIAI 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 798944333 450 GLLPNTTWLEGAIERNRMGEIIIDAKCETSVKGVFAAGDCTTVPYKQIIIATGEGAKASLSAFDYL 515
Cdd:TIGR01292 234 GHEPNTELLKGLLELDENGYIVTDEGMRTSVPGVFAAGDVRDKGYRQAVTAAGDGCIAALSAERYL 299
|
|
| AhpF_NTD_C |
cd03026 |
TRX-GRX-like family, Alkyl hydroperoxide reductase F subunit (AhpF) N-terminal domain (NTD) ... |
106-194 |
1.86e-50 |
|
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: 167.47 E-value: 1.86e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 106 QALLEQIRDIDGDFEFETYYSLSCHNCPDVVQALNLMSVLNPRIKHTAIDGGTFQNEITDRNVMGVPAVYLNGQEFGQGR 185
Cdd:cd03026 1 EDLLEQIRRLNGPINFETYVSLSCHNCPDVVQALNLMAVLNPNIEHEMIDGALFQDEVEERGIMSVPAIFLNGELFGFGR 80
|
....*....
gi 798944333 186 MTLTEIVAK 194
Cdd:cd03026 81 MTLEEILAK 89
|
|
| AhpF_NTD_N |
cd02974 |
Alkyl hydroperoxide reductase F subunit (AhpF) N-terminal domain (NTD) family, N-terminal ... |
1-95 |
4.00e-46 |
|
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: 156.20 E-value: 4.00e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 1 MLDTNMKTQLKAYLEKLTKPVELIATLDDSAKSAEIKELLAEIAELSPKVTFKEDNSlNVRKPSFLITNPGSELGPRFAG 80
Cdd:cd02974 1 MLDANLKQQLKAYLERLENPVELVASLDDSEKSAELLELLEEIASLSDKITLEEDND-DERKPSFSINRPGEDTGIRFAG 79
|
90
....*....|....*
gi 798944333 81 SPLGHEFTSLVLALL 95
Cdd:cd02974 80 IPMGHEFTSLVLALL 94
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
230-504 |
1.76e-43 |
|
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: 156.32 E-value: 1.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 230 YSARKGIRTGLM---GERFGGQVLDTVDIENYISVPKT--EGQKLAGALKAHVSDY--DVDVIDSQSASKLVPAAVEGGL 302
Cdd:pfam07992 18 TLAQLGGKVTLIedeGTCPYGGCVLSKALLGAAEAPEIasLWADLYKRKEEVVKKLnnGIEVLLGTEVVSIDPGAKKVVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 303 HQIETASGAVLKARSIIIATGAKWRNMNVPGEDQYRTKGVTYCPHCDGPLFK--GKRVAVIGGGNSGVEAAIDLAGIVEH 380
Cdd:pfam07992 98 EELVDGDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKllPKRVVVVGGGYIGVELAAALAKLGKE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 381 VTLLEFAPEM------KADQVLQDKVRSlKNVDIILNAQTTEVKGDGSKVTGLEyrdrvsGDVHSVQLSGIFVQIGLLPN 454
Cdd:pfam07992 178 VTLIEALDRLlrafdeEISAALEKALEK-NGVEVRLGTSVKEIIGDGDGVEVIL------KDGTEIDADLVVVAIGRRPN 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 798944333 455 TTWLEGA-IERNRMGEIIIDAKCETSVKGVFAAGDCTTVPYKQIIIATGEG 504
Cdd:pfam07992 251 TELLEAAgLELDERGGIVVDEYLRTSVPGIYAAGDCRVGGPELAQNAVAQG 301
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
215-515 |
1.69e-36 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 137.89 E-value: 1.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 215 VLIVGSGPAGAAAAVYSARKGIRTGLM-GERFGGQVLDTVDIENYISVPKT-EGQKLAGALKAHVSDYDVDVIDSQSASk 292
Cdd:PRK10262 9 LLILGSGPAGYTAAVYAARANLQPVLItGMEKGGQLTTTTEVENWPGDPNDlTGPLLMERMHEHATKFETEIIFDHINK- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 293 lvpAAVEGGLHQIETASGAvLKARSIIIATGAKWRNMNVPGEDQYRTKGVTYCPHCDGPLFKGKRVAVIGGGNSGVEAAI 372
Cdd:PRK10262 88 ---VDLQNRPFRLTGDSGE-YTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 373 DLAGIVEHVTLLEFAPEMKADQVLQDKVR-SLKNVDIILNAQTT--EVKGDGSKVTGLEYRDRVSGD-VHSVQLSGIFVQ 448
Cdd:PRK10262 164 YLSNIASEVHLIHRRDGFRAEKILIKRLMdKVENGNIILHTNRTleEVTGDQMGVTGVRLRDTQNSDnIESLDVAGLFVA 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 798944333 449 IGLLPNTTWLEGAIERNRmGEIIIDA-----KCETSVKGVFAAGDCTTVPYKQIIIATGEGAKASLSAFDYL 515
Cdd:PRK10262 244 IGHSPNTAIFEGQLELEN-GYIKVQSgihgnATQTSIPGVFAAGDVMDHIYRQAITSAGTGCMAALDAERYL 314
|
|
| AhpF_homolog |
TIGR03143 |
putative alkyl hydroperoxide reductase F subunit; This family of thioredoxin reductase ... |
1-192 |
1.86e-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: 127.97 E-value: 1.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 1 MLDTNMKTQLKAYLEKLTKPVELIATLDDS-AKSAEIKELLAEIAELSPKVTF----KEDNSLNVRK------PSFLITN 69
Cdd:TIGR03143 348 LLDDSLRQQLVGIFGRLENPVTLLLFLDGSnEKSAELQSFLGEFASLSEKLNSeavnRGEEPESETLpkitklPTVALLD 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 70 P-GSELGPRFAGSPLGHEFTSLVLALLWTGGHPSKEAQALLEQIRDIDGDFEFETYYSLSCHNCPDVVQALNLMSVLNPR 148
Cdd:TIGR03143 428 DdGNYTGLKFHGVPSGHELNSFILALYNAAGPGQPLGEELLEKIKKITKPVNIKIGVSLSCTLCPDVVLAAQRIASLNPN 507
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 798944333 149 IKHTAIDGGTFQNEITDRNVMGVPAVYLNGQEFGQGRMTLTEIV 192
Cdd:TIGR03143 508 VEAEMIDVSHFPDLKDEYGIMSVPAIVVDDQQVYFGKKTIEEML 551
|
|
| TRX_GRX_like |
cd02973 |
Thioredoxin (TRX)-Glutaredoxin (GRX)-like family; composed of archaeal and bacterial proteins ... |
119-185 |
6.44e-29 |
|
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: 108.81 E-value: 6.44e-29
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 798944333 119 FEFETYYSLSCHNCPDVVQALNLMSVLNPRIKHTAIDGGTFQNEITDRNVMGVPAVYLNGQEFGQGR 185
Cdd:cd02973 1 VNIEVFVSPTCPYCPDAVQAANRIAALNPNISAEMIDAAEFPDLADEYGVMSVPAIVINGKVEFVGR 67
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
258-494 |
7.98e-26 |
|
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: 107.97 E-value: 7.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 258 YISVPKTEGQKLAGALKAHVSDYDVDVIDSQSASKLVPAAvegglHQIETASGAVLKARSIIIATGAKWRNMNVPGEDqy 337
Cdd:COG0446 27 YVGGGIKDPEDLLVRTPESFERKGIDVRTGTEVTAIDPEA-----KTVTLRDGETLSYDKLVLATGARPRPPPIPGLD-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 338 rTKGVTYCPHCDGPL--------FKGKRVAVIGGGNSGVEAAIDL--AGIveHVTLLEFAPEM--KAD----QVLQDKVR 401
Cdd:COG0446 100 -LPGVFTLRTLDDADalrealkeFKGKRAVVIGGGPIGLELAEALrkRGL--KVTLVERAPRLlgVLDpemaALLEEELR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 402 SlKNVDIILNAQTTEVKGDGSKVTGLEYRDRVSGDVhsvqlsgIFVQIGLLPNTTWLEGA-IERNRMGEIIIDAKCETSV 480
Cdd:COG0446 177 E-HGVELRLGETVVAIDGDDKVAVTLTDGEEIPADL-------VVVAPGVRPNTELAKDAgLALGERGWIKVDETLQTSD 248
|
250
....*....|....
gi 798944333 481 KGVFAAGDCTTVPY 494
Cdd:COG0446 249 PDVYAAGDCAEVPH 262
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
279-493 |
1.10e-25 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 109.08 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 279 DYDVDVIDSQSASKLVPAAvegglHQIETASGAVLKARSIIIATGAKWRNMNVPGEDQyrtKGVTYC---PHCD---GPL 352
Cdd:COG1251 68 ENGIDLRLGTRVTAIDRAA-----RTVTLADGETLPYDKLVLATGSRPRVPPIPGADL---PGVFTLrtlDDADalrAAL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 353 FKGKRVAVIGGGNSGVEAAIDLAGIVEHVTLLEFAPEMKADQV-------LQDKVRSlKNVDIILNAQTTEVKGDGsKVT 425
Cdd:COG1251 140 APGKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLLPRQLdeeagalLQRLLEA-LGVEVRLGTGVTEIEGDD-RVT 217
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 798944333 426 GLEYRDrvsGDVHSVQLsgIFVQIGLLPNTTWLEGA-IERNRmGeIIIDAKCETSVKGVFAAGDCTTVP 493
Cdd:COG1251 218 GVRLAD---GEELPADL--VVVAIGVRPNTELARAAgLAVDR-G-IVVDDYLRTSDPDIYAAGDCAEHP 279
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
318-507 |
3.22e-23 |
|
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: 102.14 E-value: 3.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 318 IIIATGA-KWRNMNVPGEDqyrTKGVTYC----------PHCDGPLFKGKRVAVIGGGNSgveaAIDLAGI-----VEHV 381
Cdd:COG0493 210 VFLATGAgKPRDLGIPGED---LKGVHSAmdfltavnlgEAPDTILAVGKRVVVIGGGNT----AMDCARTalrlgAESV 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 382 TLLEFAP--EMKADqvlQDKVRSLK--NVDIILNAQTTEVKGD-GSKVTGLEYRD------RVSGDVHSVQLSG------ 444
Cdd:COG0493 283 TIVYRRTreEMPAS---KEEVEEALeeGVEFLFLVAPVEIIGDeNGRVTGLECVRmelgepDESGRRRPVPIEGseftlp 359
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 798944333 445 ---IFVQIGLLPNTTWLEGA--IERNRMGEIIIDAKC-ETSVKGVFAAGDCTTVPyKQIIIATGEGAKA 507
Cdd:COG0493 360 adlVILAIGQTPDPSGLEEElgLELDKRGTIVVDEETyQTSLPGVFAGGDAVRGP-SLVVWAIAEGRKA 427
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
303-490 |
4.09e-20 |
|
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: 92.84 E-value: 4.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 303 HQIETASGAVLKARSIIIATGAKWRNMNVPGEDQYRtkGVTYcphcDG-------PlfkgKRVAVIGGGNSGVEaaidLA 375
Cdd:COG1249 119 HTVEVTGGETLTADHIVIATGSRPRVPPIPGLDEVR--VLTS----DEaleleelP----KSLVVIGGGYIGLE----FA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 376 GI-----VEhVTLLEFAPEM--KADQVLQDKV-RSLKN--VDIILNAQTTEVKGDGSKVTgLEYRDRvsGDVHSVQLSGI 445
Cdd:COG1249 185 QIfarlgSE-VTLVERGDRLlpGEDPEISEALeKALEKegIDILTGAKVTSVEKTGDGVT-VTLEDG--GGEEAVEADKV 260
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 798944333 446 FVQIGLLPNTTW--LEGA-IERNRMGEIIIDAKCETSVKGVFAAGDCT 490
Cdd:COG1249 261 LVATGRRPNTDGlgLEAAgVELDERGGIKVDEYLRTSVPGIYAIGDVT 308
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
317-491 |
2.31e-19 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 90.62 E-value: 2.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 317 SIIIATGA-KWRNMNVPGEDqyrTKGVTYC---------PHCDGPLFKGKRVAVIGGGNSgveaAIDLAGI-----VEHV 381
Cdd:PRK11749 228 AVFIGTGAgLPRFLGIPGEN---LGGVYSAvdfltrvnqAVADYDLPVGKRVVVIGGGNT----AMDAARTakrlgAESV 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 382 TLL---EFApEMKADQVLQDKVRSlKNVDIILNAQTTEVKGDGSKVTGLEY--------------RDRVSGDVHSVQLSG 444
Cdd:PRK11749 301 TIVyrrGRE-EMPASEEEVEHAKE-EGVEFEWLAAPVEILGDEGRVTGVEFvrmelgepdasgrrRVPIEGSEFTLPADL 378
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 798944333 445 IFVQIGLLPN--TTWLEGAIERNRMGEIIID-AKCETSVKGVFAAGDCTT 491
Cdd:PRK11749 379 VIKAIGQTPNplILSTTPGLELNRWGTIIADdETGRTSLPGVFAGGDIVT 428
|
|
| GlrX_arch |
TIGR02187 |
Glutaredoxin-like domain protein; This family of archaeal proteins contains a C-terminal ... |
7-178 |
2.85e-19 |
|
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: 86.34 E-value: 2.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 7 KTQLK-AYLEKLTKPVELIATLDDSAKSAE----IKELLAEIAELSPKVTFK-------EDNSL----NV-RKPSFLITN 69
Cdd:TIGR02187 6 REILKeLFLKELKNPVEIVVFTDNDKEGCQyckeTEQLLEELSEVSPKLKLEiydfdtpEDKEEaekyGVeRVPTTIILE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 70 PGSELGPRFAGSPLGHEFTSLVLALLWTGGHPSKEAQALLEQIRDIDGDFEFETYYSLSCHNCPDVVQALNLMSVLNPRI 149
Cdd:TIGR02187 86 EGKDGGIRYTGIPAGYEFAALIEDIVRVSQGEPGLSEKTVELLQSLDEPVRIEVFVTPTCPYCPYAVLMAHKFALANDKI 165
|
170 180
....*....|....*....|....*....
gi 798944333 150 KHTAIDGGTFQNEITDRNVMGVPAVYLNG 178
Cdd:TIGR02187 166 LGEMIEANENPDLAEKYGVMSVPKIVINK 194
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
268-488 |
1.55e-15 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 78.64 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 268 KLAGALKAHVSDYDVDVIDSQS---ASKLVpaAVEGGLHQIEtasgavLKARSIIIATGAKWRNMNVPGEDQ----YRTK 340
Cdd:PRK07251 77 RLRGKNYAMLAGSGVDLYDAEAhfvSNKVI--EVQAGDEKIE------LTAETIVINTGAVSNVLPIPGLADskhvYDST 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 341 GVTYCPHcdgplfKGKRVAVIGGGNSGVEAAIDLAGIVEHVTLLEFAPEMKADQvlQDKVRSLKN-------VDIILNAQ 413
Cdd:PRK07251 149 GIQSLET------LPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTILPRE--EPSVAALAKqymeedgITFLLNAH 220
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 798944333 414 TTEVKGDGSKVTgleyrdrVSGDVHSVQLSGIFVQIGLLPNTTWL---EGAIERNRMGEIIIDAKCETSVKGVFAAGD 488
Cdd:PRK07251 221 TTEVKNDGDQVL-------VVTEDETYRFDALLYATGRKPNTEPLgleNTDIELTERGAIKVDDYCQTSVPGVFAVGD 291
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
318-515 |
4.87e-15 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 76.57 E-value: 4.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 318 IIIATGA-KWRNMNVPGEDQ----------YRTKGVTYC--PHCDGPLFKGKRVAVIGGGNSGVEAAID--LAGiVEHVT 382
Cdd:PRK12770 122 VLIATGTwKSRKLGIPGEDLpgvysaleylFRIRAAKLGylPWEKVPPVEGKKVVVVGAGLTAVDAALEavLLG-AEKVY 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 383 L-----LEFAPEMKADqvlqdkVRSLKN--VDIILNAQTTEVKGDGsKVTGLEYRD------RVSGDVHSVQLSG----- 444
Cdd:PRK12770 201 LayrrtINEAPAGKYE------IERLIArgVEFLELVTPVRIIGEG-RVEGVELAKmrlgepDESGRPRPVPIPGsefvl 273
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 798944333 445 ----IFVQIGLLPnTTWLEGA---IERNRMGEIIIDAKCETSVKGVFAAGDCTTVPYKqIIIATGEGAKASLSAFDYL 515
Cdd:PRK12770 274 eadtVVFAIGEIP-TPPFAKEclgIELNRKGEIVVDEKHMTSREGVFAAGDVVTGPSK-IGKAIKSGLRAAQSIHEWL 349
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
303-493 |
1.49e-14 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 75.98 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 303 HQIEtASGAVLKARSIIIATGAkwRNMNVPGEDQ------YRTKGV---TYCPhcdgplfkgKRVAVIGGGNSGVEAAID 373
Cdd:PRK06292 120 NTVE-VNGERIEAKNIVIATGS--RVPPIPGVWLilgdrlLTSDDAfelDKLP---------KSLAVIGGGVIGLELGQA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 374 LAGIVEHVTLLE----FAPEMkaDQVLQDKVRSL--KNVDIILNAQTTEVKGDGSKVTGLEyrdRVSGDVHSVQLSGIFV 447
Cdd:PRK06292 188 LSRLGVKVTVFErgdrILPLE--DPEVSKQAQKIlsKEFKIKLGAKVTSVEKSGDEKVEEL---EKGGKTETIEADYVLV 262
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 798944333 448 QIGLLPNTTWL---EGAIERNRMGEIIIDAKCETSVKGVFAAGDCTTVP 493
Cdd:PRK06292 263 ATGRRPNTDGLgleNTGIELDERGRPVVDEHTQTSVPGIYAAGDVNGKP 311
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
299-487 |
5.98e-14 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 72.64 E-value: 5.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 299 EGGLHQIETaSGAVLKARSIIIATG--AKWRNMNVPGedqyrtkgvtYCPHC----DGPLFKGKRVAVIGGGNSGVEAAI 372
Cdd:pfam13738 104 EDDGFVVTT-SKGTYQARYVIIATGefDFPNKLGVPE----------LPKHYsyvkDFHPYAGQKVVVIGGYNSAVDAAL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 373 DLAGIVEHVTLLEFAPEMKADQvlQDKVRSLK--------------NVDIILNAQTTEVKGDGSKVtgleyrdRV-SGDV 437
Cdd:pfam13738 173 ELVRKGARVTVLYRGSEWEDRD--SDPSYSLSpdtlnrleelvkngKIKAHFNAEVKEITEVDVSY-------KVhTEDG 243
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 798944333 438 HSVQLSGIFV-QIGLLPNTTWLEGA-IERNRMGEIIIDAK-CETSVKGVFAAG 487
Cdd:pfam13738 244 RKVTSNDDPIlATGYHPDLSFLKKGlFELDEDGRPVLTEEtESTNVPGLFLAG 296
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
292-490 |
8.47e-14 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 73.42 E-value: 8.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 292 KLVPAAVEGGLHQIETASGAVLKARSIIIATGAKWRNMnvPGE--DQYRTkgvtycpHC-DGPL-FKG--KRVAVIGGGN 365
Cdd:PRK06327 123 SFVGKTDAGYEIKVTGEDETVITAKHVIIATGSEPRHL--PGVpfDNKII-------LDnTGALnFTEvpKKLAVIGAGV 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 366 SGVEAAIDLAGIVEHVTLLEFAPE---MKADQVLQD--KVRSLKNVDIILNAQTTEVKGDGSKVTgLEYRDRvSGDVHSV 440
Cdd:PRK06327 194 IGLELGSVWRRLGAEVTILEALPAflaAADEQVAKEaaKAFTKQGLDIHLGVKIGEIKTGGKGVS-VAYTDA-DGEAQTL 271
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 798944333 441 QLSGIFVQIGLLPNTTWL--EGA-IERNRMGEIIIDAKCETSVKGVFAAGDCT 490
Cdd:PRK06327 272 EVDKLIVSIGRVPNTDGLglEAVgLKLDERGFIPVDDHCRTNVPNVYAIGDVV 324
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
309-489 |
6.51e-13 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 70.62 E-value: 6.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 309 SGAVLKARSIIIATGAKWRNMNVPGEDQ--YRTK----GVTYCPhcdgplfkgKRVAVIGGGNSGVEAAIDLAGIVEHVT 382
Cdd:PRK06370 128 GGETLRAKRIFINTGARAAIPPIPGLDEvgYLTNetifSLDELP---------EHLVIIGGGYIGLEFAQMFRRFGSEVT 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 383 LLEFAPEM------KADQVLQDKVRSLkNVDIILNAQTTEVKGDGS-KVTGLEyrdrVSGDVHSVQLSGIFVQIGLLPNT 455
Cdd:PRK06370 199 VIERGPRLlpredeDVAAAVREILERE-GIDVRLNAECIRVERDGDgIAVGLD----CNGGAPEITGSHILVAVGRVPNT 273
|
170 180 190
....*....|....*....|....*....|....*..
gi 798944333 456 TW--LEGA-IERNRMGEIIIDAKCETSVKGVFAAGDC 489
Cdd:PRK06370 274 DDlgLEAAgVETDARGYIKVDDQLRTTNPGIYAAGDC 310
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
318-489 |
1.00e-12 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 70.19 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 318 IIIATGA-KWRNMNVPGEDqyrTKGVT----YCP----HCDG------PLFKGKRVAVIGGGNSGVEA---AIDL-Agiv 378
Cdd:PRK12810 232 VFLGTGAyKPRDLGIPGRD---LDGVHfamdFLIqntrRVLGdetepfISAKGKHVVVIGGGDTGMDCvgtAIRQgA--- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 379 EHVTLLEFAPeMKADQVLQDKVRSLKN------------VDIILNAQTTEVKGDGSKVTGLEYRDRVSGDVHSVQLSG-- 444
Cdd:PRK12810 306 KSVTQRDIMP-MPPSRRNKNNPWPYWPmklevsnaheegVEREFNVQTKEFEGENGKVTGVKVVRTELGEGDFEPVEGse 384
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 798944333 445 -------IFVQIGLL-PNTTWL-EGAIERNRMGEII-IDAKCETSVKGVFAAGDC 489
Cdd:PRK12810 385 fvlpadlVLLAMGFTgPEAGLLaQFGVELDERGRVAaPDNAYQTSNPKVFAAGDM 439
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
356-492 |
1.88e-12 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 69.30 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 356 KRVAVIGGGNSGVEAAIDLAGIVEHVTLLE---------FAPEMKadQVLQDKVRSlKNVDIILNAQTTEVKGDGsKVTG 426
Cdd:PRK09564 150 KNIVIIGAGFIGLEAVEAAKHLGKNVRIIQledrilpdsFDKEIT--DVMEEELRE-NGVELHLNEFVKSLIGED-KVEG 225
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 798944333 427 LEY-RDRVSGDVhsvqlsgIFVQIGLLPNTTWLEGA-IERNRMGEIIIDAKCETSVKGVFAAGDCTTV 492
Cdd:PRK09564 226 VVTdKGEYEADV-------VIVATGVKPNTEFLEDTgLKTLKNGAIIVDEYGETSIENIYAAGDCATI 286
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
357-425 |
2.70e-12 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 425450 [Multi-domain] Cd Length: 80 Bit Score: 62.22 E-value: 2.70e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 798944333 357 RVAVIGGGNSGVEAAIDLAGIVEHVTLLEFAPEMK------ADQVLQDKVRSlKNVDIILNAQTTEVKGDGSKVT 425
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLpgfdpeIAKILQEKLEK-NGIEFLLNTTVEAIEGNGDGVV 74
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
299-384 |
1.07e-11 |
|
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: 66.81 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 299 EGGLHQIETASGAVLKARSIIIATGAKWR-NM-NVPGEDQYrtKGVTYcpHC---DGPL-FKGKRVAVIGGGNSGVEAAI 372
Cdd:COG2072 113 ADGRWTVTTDDGETLTARFVVVATGPLSRpKIpDIPGLEDF--AGEQL--HSadwRNPVdLAGKRVLVVGTGASAVQIAP 188
|
90
....*....|..
gi 798944333 373 DLAGIVEHVTLL 384
Cdd:COG2072 189 ELARVAAHVTVF 200
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
316-515 |
2.03e-10 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 62.73 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 316 RSIIIATGAKW-RNMNVPGE--------DQYRTK---GVTYCPHCDGPLFKGKRVAVIGGGNSGVEAA---IDLAGIVeH 380
Cdd:PRK12831 230 DAVFIGSGAGLpKFMGIPGEnlngvfsaNEFLTRvnlMKAYKPEYDTPIKVGKKVAVVGGGNVAMDAArtaLRLGAEV-H 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 381 VTLLEFAPEMKADqvlQDKVRSLKNVDIILN--AQTTEVKGD-GSKVTG-------LEYRDR--------VSGDVHSVQL 442
Cdd:PRK12831 309 IVYRRSEEELPAR---VEEVHHAKEEGVIFDllTNPVEILGDeNGWVKGmkcikmeLGEPDAsgrrrpveIEGSEFVLEV 385
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 798944333 443 SGIFVQIGLLPNTTWLEGA--IERNRMGEIIID-AKCETSVKGVFAAGDCTTvPYKQIIIATGEGAKASLSAFDYL 515
Cdd:PRK12831 386 DTVIMSLGTSPNPLISSTTkgLKINKRGCIVADeETGLTSKEGVFAGGDAVT-GAATVILAMGAGKKAAKAIDEYL 460
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
303-490 |
4.91e-10 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 61.71 E-value: 4.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 303 HQIETaSGAVLKARSIIIATGAKWRNMNVPGEDqyrtkgvtYCPHCDG-------PlfkgKRVAVIGGGNSGVEaaidLA 375
Cdd:PRK06116 121 HTVEV-NGERYTADHILIATGGRPSIPDIPGAE--------YGITSDGffaleelP----KRVAVVGAGYIAVE----FA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 376 GI-----VEhVTLL--EFAPEMKADQVLQDKVR---SLKNVDIILNAQTTEVK--GDGSKVTGLEyrdrvSGDVHSVQLs 443
Cdd:PRK06116 184 GVlnglgSE-THLFvrGDAPLRGFDPDIRETLVeemEKKGIRLHTNAVPKAVEknADGSLTLTLE-----DGETLTVDC- 256
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 798944333 444 gIFVQIGLLPNTTW--LEGA-IERNRMGEIIIDAKCETSVKGVFAAGDCT 490
Cdd:PRK06116 257 -LIWAIGREPNTDGlgLENAgVKLNEKGYIIVDEYQNTNVPGIYAVGDVT 305
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
304-489 |
5.54e-10 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 62.15 E-value: 5.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 304 QIETASGAVLKARSIIIATGAKWRNMNVPGEDQ-----YRTkgVTYCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIV 378
Cdd:TIGR02374 86 QVITDAGRTLSYDKLILATGSYPFILPIPGADKkgvyvFRT--IEDLDAIMAMAQRFKKAAVIGGGLLGLEAAVGLQNLG 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 379 EHVTLLEFAPEMKADQVLQDKVRSLKN------VDIILNAQTTEVKGDGsKVTGLEYRDRVSGDVHSVQLSgifvqIGLL 452
Cdd:TIGR02374 164 MDVSVIHHAPGLMAKQLDQTAGRLLQReleqkgLTFLLEKDTVEIVGAT-KADRIRFKDGSSLEADLIVMA-----AGIR 237
|
170 180 190
....*....|....*....|....*....|....*...
gi 798944333 453 PNTTW-LEGAIERNRmgEIIIDAKCETSVKGVFAAGDC 489
Cdd:TIGR02374 238 PNDELaVSAGIKVNR--GIIVNDSMQTSDPDIYAVGEC 273
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
300-495 |
9.00e-10 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 60.74 E-value: 9.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 300 GGLHQIETASGAVLKARSIIIATGAKWRNMNVPGEDqyrtkGVTYcpHCDGPLFK----GKRVAVIGGGNSGVEAAIDLA 375
Cdd:PRK07846 114 IGPKTLRTGDGEEITADQVVIAAGSRPVIPPVIADS-----GVRY--HTSDTIMRlpelPESLVIVGGGFIAAEFAHVFS 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 376 GIVEHVTLLEFAPEM--KADQVLQDKVRSL--KNVDIILNAQTTEVKGDGSKVT-GLEYRDRVSGDVhsvqlsgIFVQIG 450
Cdd:PRK07846 187 ALGVRVTVVNRSGRLlrHLDDDISERFTELasKRWDVRLGRNVVGVSQDGSGVTlRLDDGSTVEADV-------LLVATG 259
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 798944333 451 LLPNTTWLE---GAIERNRMGEIIIDAKCETSVKGVFAAGDCTTvPYK 495
Cdd:PRK07846 260 RVPNGDLLDaaaAGVDVDEDGRVVVDEYQRTSAEGVFALGDVSS-PYQ 306
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
317-515 |
3.15e-09 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 59.76 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 317 SIIIATGAKWRN-MNVPGED--------QYRTKG---VTYCPHCDGPLFKGKRVAVIGGGNSGVEA---AIDLAGivEHV 381
Cdd:PRK12778 520 GIFIASGAGLPNfMNIPGENsngvmssnEYLTRVnlmDAASPDSDTPIKFGKKVAVVGGGNTAMDSartAKRLGA--ERV 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 382 TLL--EFAPEMKA--DQVLQDKVRSLK-----NVDIILNAQTTEVKGDGSKVTGLEYRDrVSGDVHSVQLSG-------- 444
Cdd:PRK12778 598 TIVyrRSEEEMPArlEEVKHAKEEGIEfltlhNPIEYLADEKGWVKQVVLQKMELGEPD-ASGRRRPVAIPGstftvdvd 676
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 798944333 445 -IFVQIGLLPN---TTWLEGaIERNRMGEIIIDAKCETSVKGVFAAGDCTTvPYKQIIIATGEGAKASLSAFDYL 515
Cdd:PRK12778 677 lVIVSVGVSPNplvPSSIPG-LELNRKGTIVVDEEMQSSIPGIYAGGDIVR-GGATVILAMGDGKRAAAAIDEYL 749
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
348-499 |
6.86e-09 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 57.62 E-value: 6.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 348 CDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVEHVTLLEFA--------PEMKADQvLQDKVRSlKNVDIILNA--QTTEV 417
Cdd:PRK04965 134 AETQLRDAQRVLVVGGGLIGTELAMDLCRAGKAVTLVDNAasllaslmPPEVSSR-LQHRLTE-MGVHLLLKSqlQGLEK 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 418 KGDGSKVTgleyrdRVSGdvHSVQLSGIFVQIGLLPNTTWLEGA-IERNRmGeIIIDAKCETSVKGVFAAGDCTTV---- 492
Cdd:PRK04965 212 TDSGIRAT------LDSG--RSIEVDAVIAAAGLRPNTALARRAgLAVNR-G-IVVDSYLQTSAPDIYALGDCAEIngqv 281
|
....*...
gi 798944333 493 -PYKQIII 499
Cdd:PRK04965 282 lPFLQPIQ 289
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
305-488 |
8.37e-09 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 57.85 E-value: 8.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 305 IETASGAVLKARSIIIATGAKWRNMnvPGEDQYRTKGVTYcphcDGPL---FKGKRVAVIGGGNSGVEAAIDLAGIVEHV 381
Cdd:PRK06416 125 MTEDGEQTYTAKNIILATGSRPREL--PGIEIDGRVIWTS----DEALnldEVPKSLVVIGGGYIGVEFASAYASLGAEV 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 382 TLLE--------FAPEMKadQVLQDKVRSlKNVDIILNAQTTEVK--GDGSKVTgleyrDRVSGDVHSVQLSGIFVQIGL 451
Cdd:PRK06416 199 TIVEalprilpgEDKEIS--KLAERALKK-RGIKIKTGAKAKKVEqtDDGVTVT-----LEDGGKEETLEADYVLVAVGR 270
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 798944333 452 LPNTTWL---EGAIERNRmGEIIIDAKCETSVKGVFAAGD 488
Cdd:PRK06416 271 RPNTENLgleELGVKTDR-GFIEVDEQLRTNVPNIYAIGD 309
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
273-493 |
1.40e-07 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 53.60 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 273 LKAHVSDYDVDVIdSQSASKLVPAAvegglHQIETASGAVLKARSIIIATGAKWRNMNVPGEDQYrtkGVTYCPHCDGPL 352
Cdd:COG1252 62 LRELLRRAGVRFI-QGEVTGIDPEA-----RTVTLADGRTLSYDYLVIATGSVTNFFGIPGLAEH---ALPLKTLEDALA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 353 F--------------KGKRVAVIGGGNSGVEaaidLAGIVEH-----------------VTLLEFAPEM--KADQVLQDK 399
Cdd:COG1252 133 LrerllaaferaerrRLLTIVVVGGGPTGVE----LAGELAEllrkllrypgidpdkvrITLVEAGPRIlpGLGEKLSEA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 400 VRSL---KNVDIILNAQTTEVKGDgskvtGLEYRDrvsGDVHS---------VQLSGIFVQIGLlpnttwlegaiERNRM 467
Cdd:COG1252 209 AEKElekRGVEVHTGTRVTEVDAD-----GVTLED---GEEIPadtviwaagVKAPPLLADLGL-----------PTDRR 269
|
250 260
....*....|....*....|....*..
gi 798944333 468 GEIIIDAKCET-SVKGVFAAGDCTTVP 493
Cdd:COG1252 270 GRVLVDPTLQVpGHPNVFAIGDCAAVP 296
|
|
| Thioredoxin_3 |
pfam13192 |
Thioredoxin domain; |
126-195 |
3.30e-07 |
|
Thioredoxin domain;
Pssm-ID: 433026 [Multi-domain] Cd Length: 71 Bit Score: 47.59 E-value: 3.30e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 126 SLSCHNCPDVVQALNlMSVLNPRIKHTAIDGGTFQnEITDRNVMGVPAVYLNGQEFGQGRMTLTEIVAKV 195
Cdd:pfam13192 2 GPGCPKCPQLEKAVK-EAAAELGIDAEVEKVTDFP-EIAKYGVMSTPALVINGKVVSSGKVPSEEEIRKL 69
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
305-489 |
4.71e-07 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 52.81 E-value: 4.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 305 IETASGAVLKARSIIIATGAKWRNMNVPGEDQ-----YRT----KGVTYCPHcdgplfKGKRVAVIGGGNSGVEAAIDLA 375
Cdd:PRK14989 92 IHSSAGRTVFYDKLIMATGSYPWIPPIKGSETqdcfvYRTiedlNAIEACAR------RSKRGAVVGGGLLGLEAAGALK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 376 --GIVEHVtlLEFAPEMKADQV-------LQDKVRSLkNVDIILNAQTTEVKGDGSkvtglEYRDRVS-GDVHSVQLSGI 445
Cdd:PRK14989 166 nlGVETHV--IEFAPMLMAEQLdqmggeqLRRKIESM-GVRVHTSKNTLEIVQEGV-----EARKTMRfADGSELEVDFI 237
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 798944333 446 FVQIGLLP-NTTWLEGAIERNRMGEIIIDAKCETSVKGVFAAGDC 489
Cdd:PRK14989 238 VFSTGIRPqDKLATQCGLAVAPRGGIVINDSCQTSDPDIYAIGEC 282
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
245-490 |
1.37e-06 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 50.97 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 245 FGGQVLDTVDIE--NYISVPKTEGQKLAGALKAHVSDYDVDVIdsQSASKLV-PAAVEgglhqIETASGAVLK--ARSII 319
Cdd:PLN02507 100 YGWEINEKVDFNwkKLLQKKTDEILRLNGIYKRLLANAGVKLY--EGEGKIVgPNEVE-----VTQLDGTKLRytAKHIL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 320 IATGAKWRNMNVPGEDQYRTKGVTYCPHcDGPlfkgKRVAVIGGGNSGVEAAIDLAGIVEHVTLL--------EFAPEMK 391
Cdd:PLN02507 173 IATGSRAQRPNIPGKELAITSDEALSLE-ELP----KRAVVLGGGYIAVEFASIWRGMGATVDLFfrkelplrGFDDEMR 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 392 AdqVLqdkVRSLKNVDIILNAQTTEVK----GDGSKVTgLEYRDRVSGDVhsvqlsgIFVQIGLLPNTTWL---EGAIER 464
Cdd:PLN02507 248 A--VV---ARNLEGRGINLHPRTNLTQltktEGGIKVI-TDHGEEFVADV-------VLFATGRAPNTKRLnleAVGVEL 314
|
250 260
....*....|....*....|....*.
gi 798944333 465 NRMGEIIIDAKCETSVKGVFAAGDCT 490
Cdd:PLN02507 315 DKAGAVKVDEYSRTNIPSIWAIGDVT 340
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
282-488 |
1.68e-06 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 50.31 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 282 VDVIDSQSASKLVPAAvegglHQIETASGAVLKARSIIIATGAKWRN---MNVPGEDQYRTKGVTYCPHCDGPLFKGKRV 358
Cdd:PRK09754 73 VHLHSGVTIKTLGRDT-----RELVLTNGESWHWDQLFIATGAAARPlplLDALGERCFTLRHAGDAARLREVLQPERSV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 359 AVIGGGNSGVEAAIDLAGIVEHVTLLEFAPEMK---ADQVLQDKV---RSLKNVDIILNAQTTEVKgDGSKVT-GLEYRD 431
Cdd:PRK09754 148 VIVGAGTIGLELAASATQRRCKVTVIELAATVMgrnAPPPVQRYLlqrHQQAGVRILLNNAIEHVV-DGEKVElTLQSGE 226
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 798944333 432 RVSGDVhsvqlsgIFVQIGLLPNTtwlEGAIERN--RMGEIIIDAKCETSVKGVFAAGD 488
Cdd:PRK09754 227 TLQADV-------VIYGIGISAND---QLAREANldTANGIVIDEACRTCDPAIFAGGD 275
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
356-509 |
2.16e-06 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 50.15 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 356 KRVAVIGGGNSGVEAAIDLAGIVEHVTLLE----FAPEmkaDQVLQDKVRS---LKNVDIILNAQTTEVKGDGSKVTgLE 428
Cdd:PRK13748 271 ERLAVIGSSVVALELAQAFARLGSKVTILArstlFFRE---DPAIGEAVTAafrAEGIEVLEHTQASQVAHVDGEFV-LT 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 429 YRdrvSGDVHSVQLsgiFVQIGLLPNTTWL--EGA-IERNRMGEIIIDAKCETSVKGVFAAGDCTTVPyKQIIIATGEGA 505
Cdd:PRK13748 347 TG---HGELRADKL---LVATGRAPNTRSLalDAAgVTVNAQGAIVIDQGMRTSVPHIYAAGDCTDQP-QFVYVAAAAGT 419
|
....
gi 798944333 506 KASL 509
Cdd:PRK13748 420 RAAI 423
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
354-497 |
1.27e-05 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 47.47 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 354 KGKRVAVIGGGNSGVEAAIDLAGIVEHVTLL----EFAPEMKAD--QVLQDKVRSlKNVDIILNAQTTEVkgDGSKVTgl 427
Cdd:PRK13512 147 QVDKALVVGAGYISLEVLENLYERGLHPTLIhrsdKINKLMDADmnQPILDELDK-REIPYRLNEEIDAI--NGNEVT-- 221
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 798944333 428 eyrdRVSGDVHSVQLsgIFVQIGLLPNTTWLEGA-IERNRMGEIIIDAKCETSVKGVFAAGDCTTVPYKQI 497
Cdd:PRK13512 222 ----FKSGKVEHYDM--IIEGVGTHPNSKFIESSnIKLDDKGFIPVNDKFETNVPNIYAIGDIITSHYRHV 286
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
357-490 |
1.62e-05 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 47.32 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 357 RVAVIGGGNSGVEAAIDLAGIVEHVTLLEFAPEM--KADQVLQDKVRSL---KNVDIILNAQTTEVKGDGSKVtgleyrd 431
Cdd:PRK08010 160 HLGILGGGYIGVEFASMFANFGSKVTILEAASLFlpREDRDIADNIATIlrdQGVDIILNAHVERISHHENQV------- 232
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 798944333 432 RVSGDVHSVQLSGIFVQIGLLPNTTWLE---GAIERNRMGEIIIDAKCETSVKGVFAAGDCT 490
Cdd:PRK08010 233 QVHSEHAQLAVDALLIASGRQPATASLHpenAGIAVNERGAIVVDKYLHTTADNIWAMGDVT 294
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
296-498 |
2.23e-05 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 46.92 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 296 AAVEGGLHQIEtaSGAVLKARSIIIATGAKWRNMNVpgedqyrtKGVTYCPHCDG--PLFKGKRVAVIGGGNSGVEaaid 373
Cdd:PTZ00058 186 TIVSAGVSQLD--DGQVIEGKNILIAVGNKPIFPDV--------KGKEFTISSDDffKIKEAKRIGIAGSGYIAVE---- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 374 LAGIVE------------HVTLLEFaPEMKADQVLQDKVRSlkNVDIILNAQTTEVKGDGSK-VTGL--EYRDRVSGDVh 438
Cdd:PTZ00058 252 LINVVNrlgaesyifargNRLLRKF-DETIINELENDMKKN--NINIITHANVEEIEKVKEKnLTIYlsDGRKYEHFDY- 327
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 798944333 439 svqlsgIFVQIGLLPNTTWL--EGAIERNRMGEIIIDAKCETSVKGVFAAGDCTTVPYKQII 498
Cdd:PTZ00058 328 ------VIYCVGRSPNTEDLnlKALNIKTPKGYIKVDDNQRTSVKHIYAVGDCCMVKKNQEI 383
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
356-419 |
7.38e-05 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 45.24 E-value: 7.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 356 KRVAVIGGGNSGVEAAIDLA--GIveHVTLLEFAPE---------------MKADQVLQDKVRSLK---NVDIILNAQTT 415
Cdd:COG1148 141 KRALVIGGGIAGMTAALELAeqGY--EVYLVEKEPElggraaqlhktfpglDCPQCILEPLIAEVEanpNITVYTGAEVE 218
|
....
gi 798944333 416 EVKG 419
Cdd:COG1148 219 EVSG 222
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
412-492 |
1.60e-04 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 44.08 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 412 AQTTEVKGDGSKVTgLEYRDRVSGdvhsvqlSGIFVQIGLLPNTT--WLEGA-IERNRMGEIIIDAKCETSVKGVFAAGD 488
Cdd:PRK07845 241 AESVERTGDGVVVT-LTDGRTVEG-------SHALMAVGSVPNTAglGLEEAgVELTPSGHITVDRVSRTSVPGIYAAGD 312
|
....
gi 798944333 489 CTTV 492
Cdd:PRK07845 313 CTGV 316
|
|
| PfPDO_like_N |
cd02975 |
Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO)-like family, N-terminal TRX-fold ... |
14-91 |
2.02e-04 |
|
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: 40.84 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 14 LEKLTKPVEL-IATLDDSAKSAEI-KELLAEIAELSPK-----VTFKEDNSL----NV-RKPSFLITNPGSE-LGPRFAG 80
Cdd:cd02975 16 FKEMKNPVDLvVFSSKEGCQYCEVtKQLLEELSELSDKlkleiYDFDEDKEKaekyGVeRVPTTIFLQDGGKdGGIRYYG 95
|
90
....*....|.
gi 798944333 81 SPLGHEFTSLV 91
Cdd:cd02975 96 LPAGYEFASLI 106
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
312-492 |
2.41e-04 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 43.60 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 312 VLKARSIIIATGAKWRNMNVPGEDQY----------RT--KGVTYC------PhcDGPLFKGKR---VAVIGGGNSGVEA 370
Cdd:PTZ00318 111 SVPYDKLVVAHGARPNTFNIPGVEERafflkevnhaRGirKRIVQCieraslP--TTSVEERKRllhFVVVGGGPTGVEF 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 371 AIDLAG------------IVEH--VTLLEFAPEMKA--DQVLQDK-VRSLKN--VDIILNAQTTEVKgDGSKVTGleyrd 431
Cdd:PTZ00318 189 AAELADffrddvrnlnpeLVEEckVTVLEAGSEVLGsfDQALRKYgQRRLRRlgVDIRTKTAVKEVL-DKEVVLK----- 262
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 798944333 432 rvSGDVHSVQLSGIFVQIGLLPNTTWLEgaIERNRMGEIIIDAKCEtsVKG---VFAAGDCTTV 492
Cdd:PTZ00318 263 --DGEVIPTGLVVWSTGVGPGPLTKQLK--VDKTSRGRISVDDHLR--VKPipnVFALGDCAAN 320
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
312-488 |
3.66e-04 |
|
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: 42.92 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 312 VLKARSIIIATGAKWRNMNVPGEDQYrtkGVT--------YCPhcdgplfkGKRVaVIGGGNSGVEAAIDLAGIVEHVTL 383
Cdd:TIGR01438 141 IYSAERFLIATGERPRYPGIPGAKEL---CITsddlfslpYCP--------GKTL-VVGASYVALECAGFLAGIGLDVTV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 384 LEFAPEMKA-DQVLQDKVRS-LKNVDIILNAQTTEVK----GDGSKVTGLEYRDRVSGDVHSVQLSgifvqIGLLPNTTW 457
Cdd:TIGR01438 209 MVRSILLRGfDQDCANKVGEhMEEHGVKFKRQFVPIKveqiEAKVLVEFTDSTNGIEEEYDTVLLA-----IGRDACTRK 283
|
170 180 190
....*....|....*....|....*....|....*
gi 798944333 458 LE----GAIERNRMGEIIIDAKCETSVKGVFAAGD 488
Cdd:TIGR01438 284 LNlenvGVKINKKTGKIPADEEEQTNVPYIYAVGD 318
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
313-490 |
6.75e-04 |
|
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of spermidine, is (in its reduced form) an important antioxidant found in trypanosomatids (Crithidia, Leishmania, Trypanosoma). This model describes trypanothione reductase, a possible antitrypanosomal drug target closely related to some forms of glutathione reductase.
Pssm-ID: 200098 [Multi-domain] Cd Length: 486 Bit Score: 42.27 E-value: 6.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 313 LKARSIIIATGAKWRNMNVPGEDQYRTKGVTYcpHCDGPlfkGKRVAVIGGGNSGVEAA------------IDLAgIVEH 380
Cdd:TIGR01423 150 LQAEHILLATGSWPQMLGIPGIEHCISSNEAF--YLDEP---PRRVLTVGGGFISVEFAgifnaykprggkVTLC-YRNN 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 798944333 381 VTLLEFAPEMKadQVLQDKVRSlKNVDIILNAQTTEVK--GDGSKVTGLEYRDRVSGDVhsvqlsgIFVQIGLLPNTTWL 458
Cdd:TIGR01423 224 MILRGFDSTLR--KELTKQLRA-NGINIMTNENPAKVTlnADGSKHVTFESGKTLDVDV-------VMMAIGRVPRTQTL 293
|
170 180 190
....*....|....*....|....*....|....*
gi 798944333 459 E---GAIERNRMGEIIIDAKCETSVKGVFAAGDCT 490
Cdd:TIGR01423 294 QldkVGVELTKKGAIQVDEFSRTNVPNIYAIGDVT 328
|
|
| PRK09231 |
PRK09231 |
fumarate reductase flavoprotein subunit; Validated |
467-492 |
8.07e-04 |
|
fumarate reductase flavoprotein subunit; Validated
Pssm-ID: 236421 [Multi-domain] Cd Length: 582 Bit Score: 41.93 E-value: 8.07e-04
10 20
....*....|....*....|....*.
gi 798944333 467 MGEIIIDAKCETSVKGVFAAGDCTTV 492
Cdd:PRK09231 358 MGGIETDQNCETRIKGLFAVGECSSV 383
|
|
| COG3349 |
COG3349 |
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ... |
355-388 |
7.38e-03 |
|
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function prediction only];
Pssm-ID: 442577 [Multi-domain] Cd Length: 445 Bit Score: 38.68 E-value: 7.38e-03
10 20 30
....*....|....*....|....*....|....
gi 798944333 355 GKRVAVIGGGNSGVEAAIDLAGIVEHVTLLEFAP 388
Cdd:COG3349 3 PPRVVVVGGGLAGLAAAVELAEAGFRVTLLEARP 36
|
|
| |
