|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
1-519 |
0e+00 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 1079.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 1 MLDANLKAQLKSYLERVTQPIEIVASLDDGAKSREMLDLLKDIASLSHQITLIDSGDDARKPSFSINRPGADISLRFAGI 80
Cdd:PRK15317 1 MLDANLKTQLKQYLELLERPIELVASLDDSEKSAELKELLEEIASLSDKITVEEDSLDVRKPSFSITRPGEDTGVRFAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 81 PMGHEFTSLVLALLQVGGHPSKASVEVIEQIRSLKGEFNFETYFSLSCQNCPDVVQALNLMAVLNPNIRHVAIDGALFQD 160
Cdd:PRK15317 81 PMGHEFTSLVLALLQVGGHPPKLDQEVIEQIKALDGDFHFETYVSLSCHNCPDVVQALNLMAVLNPNITHTMIDGALFQD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 161 EVNDRKIMAVPSIYLNGENFGQGRMGLEEILAKLDTGAIERQAEKISAKQAFDVLVVGGGPAGASAAIYAARKGIRTGVA 240
Cdd:PRK15317 161 EVEARNIMAVPTVFLNGEEFGQGRMTLEEILAKLDTGAAARAAEELNAKDPYDVLVVGGGPAGAAAAIYAARKGIRTGIV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 241 AERFGGQVLDTMAIENFISVQETEGPKLATALEEHVKQYDVDIMNLQRADKLIPGKngELHEVRFASGATLKAKSVILAT 320
Cdd:PRK15317 241 AERFGGQVLDTMGIENFISVPETEGPKLAAALEEHVKEYDVDIMNLQRASKLEPAA--GLIEVELANGAVLKAKTVILAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 321 GARWREMNVPGEQEYRNKGVAYCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVSHVTLLEFDVQLRADAVLQRKLHS 400
Cdd:PRK15317 319 GARWRNMNVPGEDEYRNKGVAYCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVKHVTVLEFAPELKADQVLQDKLRS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 401 LPNVTVITSALTTEVTGDGQKVNGLRYKDRNTDELRTVELEGIFVQIGLLPNTDWLKGTIELSPRGEIIVDNRGETSIPG 480
Cdd:PRK15317 399 LPNVTIITNAQTTEVTGDGDKVTGLTYKDRTTGEEHHLELEGVFVQIGLVPNTEWLKGTVELNRRGEIIVDARGATSVPG 478
|
490 500 510
....*....|....*....|....*....|....*....
gi 499653597 481 IFAAGDVTTVPYKQIVIAVGEGAKASLSAFDHLIRTSAP 519
Cdd:PRK15317 479 VFAAGDCTTVPYKQIIIAMGEGAKAALSAFDYLIRNSAA 517
|
|
| AhpF |
TIGR03140 |
alkyl hydroperoxide reductase subunit F; This enzyme is the partner of the peroxiredoxin ... |
1-515 |
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: 822.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 1 MLDANLKAQLKSYLERVTQPIEIVASLDDGAKSREMLDLLKDIASLSHQITLI-DSGDDARKPSFSINRPGADISLRFAG 79
Cdd:TIGR03140 1 MLDQSLLAQLKSYLASLENPVTLVLSAGSHEKSKELLELLDEIASLSDKISLTqNTADTLRKPSFTILRDGADTGIRFAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 80 IPMGHEFTSLVLALLQVGGHPSKASVEVIEQIRSLKGEFNFETYFSLSCQNCPDVVQALNLMAVLNPNIRHVAIDGALFQ 159
Cdd:TIGR03140 81 IPGGHEFTSLVLAILQVGGHGPKLDEGIIDRIRRLNGPLHFETYVSLTCQNCPDVVQALNQMALLNPNISHTMIDGALFQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 160 DEVNDRKIMAVPSIYLNGENFGQGRMGLEEILAKLDTGAIERQAEKISAKQAFDVLVVGGGPAGASAAIYAARKGIRTGV 239
Cdd:TIGR03140 161 DEVEALGIQGVPAVFLNGEEFHNGRMDLAELLEKLEETAGVEAASALEQLDPYDVLVVGGGPAGAAAAIYAARKGLRTAM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 240 AAERFGGQVLDTMAIENFISVQETEGPKLATALEEHVKQYDVDIMNLQRADKLIpgKNGELHEVRFASGATLKAKSVILA 319
Cdd:TIGR03140 241 VAERIGGQVKDTVGIENLISVPYTTGSQLAANLEEHIKQYPIDLMENQRAKKIE--TEDGLIVVTLESGEVLKAKSVIVA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 320 TGARWREMNVPGEQEYRNKGVAYCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVSHVTLLEFDVQLRADAVLQRKLH 399
Cdd:TIGR03140 319 TGARWRKLGVPGEKEYIGKGVAYCPHCDGPFFKGKDVAVIGGGNSGIEAAIDLAGIVRHVTVLEFADELKADKVLQDKLK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 400 SLPNVTVITSALTTEVTGDGQKVNGLRYKDRNTDELRTVELEGIFVQIGLLPNTDWLKGTIELSPRGEIIVDNRGETSIP 479
Cdd:TIGR03140 399 SLPNVDILTSAQTTEIVGDGDKVTGIRYQDRNSGEEKQLDLDGVFVQIGLVPNTEWLKDAVELNRRGEIVIDERGRTSVP 478
|
490 500 510
....*....|....*....|....*....|....*.
gi 499653597 480 GIFAAGDVTTVPYKQIVIAVGEGAKASLSAFDHLIR 515
Cdd:TIGR03140 479 GIFAAGDVTTVPYKQIIIAMGEGAKAALSAFDYLIR 514
|
|
| AhpF |
COG3634 |
Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms]; |
1-196 |
2.46e-116 |
|
Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms];
Pssm-ID: 442851 [Multi-domain] Cd Length: 200 Bit Score: 341.34 E-value: 2.46e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 1 MLDANLKAQLKSYLERVTQPIEIVASLDDGAKSREMLDLLKDIASLSHQITL--IDSGDDARKPSFSINRPGADISLRFA 78
Cdd:COG3634 3 MLDDELKAQLKEYLEKLKNPVELVLFLDDCEKSEELRELLEEIASLSDKISLevYDKDDVERAPSFAILRDGEDTGIRFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 79 GIPMGHEFTSLVLALLQVGGHPSKASVEVIEQIRSLKGEFNFETYFSLSCQNCPDVVQALNLMAVLNPNIRHVAIDGALF 158
Cdd:COG3634 83 GIPSGHEFTSLVLALLQVSGHPPKLSEETIEQIKALDGPVHFEVFVSLSCPNCPDVVQALNLMAVLNPNITHEMIDGAEF 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 499653597 159 QDEVNDRKIMAVPSIYLNGENFGQGRMGLEEILAKLDT 196
Cdd:COG3634 163 PDEAEKYGVMSVPTVVLNGEVFFVGRMPEEEILEKLDT 200
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
232-513 |
5.78e-95 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 290.48 E-value: 5.78e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 232 RKGIRTGV-AAERFGGQVLDTMAIENFISVQE-TEGPKLATALEEHVKQYDVDIMnLQRADKLIpgKNGELHEVRFASGA 309
Cdd:COG0492 21 RAGLKTLViEGGEPGGQLATTKEIENYPGFPEgISGPELAERLREQAERFGAEIL-LEEVTSVD--KDDGPFRVTTDDGT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 310 TLKAKSVILATGARWREMNVPGEQEYRNKGVAYCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVSHVTLLEFDVQLR 389
Cdd:COG0492 98 EYEAKAVIIATGAGPRKLGLPGEEEFEGRGVSYCATCDGFFFRGKDVVVVGGGDSALEEALYLTKFASKVTLIHRRDELR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 390 ADAVLQRKLHSLPNVTVITSALTTEVTGDGqKVNGLRYKDRNTDELRTVELEGIFVQIGLLPNTDWLKGT-IELSPRGEI 468
Cdd:COG0492 178 ASKILVERLRANPKIEVLWNTEVTEIEGDG-RVEGVTLKNVKTGEEKELEVDGVFVAIGLKPNTELLKGLgLELDEDGYI 256
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 499653597 469 IVDNRGETSIPGIFAAGDVTTVPYKQIVIAVGEGAKASLSAFDHL 513
Cdd:COG0492 257 VVDEDMETSVPGVFAAGDVRDYKYRQAATAAGEGAIAALSAARYL 301
|
|
| TRX_reduct |
TIGR01292 |
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ... |
244-513 |
1.10e-78 |
|
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: 248.70 E-value: 1.10e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 244 FGGQVLDTMAIENFISVQET-EGPKLATALEEHVKQYDVDIM--NLQRADKlipgkNGELHEVRFASGATLKAKSVILAT 320
Cdd:TIGR01292 33 PGGQLTTTTEVENYPGFPEGiSGPELMEKMKEQAVKFGAEIIyeEVIKVDK-----SDRPFKVYTGDGKEYTAKAVIIAT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 321 GARWREMNVPGEQEYRNKGVAYCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVSHVTLLEFDVQLRADAVLQRKLHS 400
Cdd:TIGR01292 108 GASARKLGIPGEDEFWGRGVSYCATCDGPFFKNKEVAVVGGGDSAIEEALYLTRIAKKVTLVHRRDKFRAEKILLDRLKK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 401 LPNVTVITSALTTEVTGDgQKVNGLRYKDRNTDELRTVELEGIFVQIGLLPNTDWLKGTIELSPRGEIIVDNRGETSIPG 480
Cdd:TIGR01292 188 NPKIEFLWNSTVEEIVGD-NKVEGVKIKNTVTGEEEELEVDGVFIAIGHEPNTELLKGLLELDENGYIVTDEGMRTSVPG 266
|
250 260 270
....*....|....*....|....*....|...
gi 499653597 481 IFAAGDVTTVPYKQIVIAVGEGAKASLSAFDHL 513
Cdd:TIGR01292 267 VFAAGDVRDKGYRQAVTAAGDGCIAALSAERYL 299
|
|
| AhpF_NTD_C |
cd03026 |
TRX-GRX-like family, Alkyl hydroperoxide reductase F subunit (AhpF) N-terminal domain (NTD) ... |
106-193 |
1.40e-53 |
|
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: 175.56 E-value: 1.40e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 106 EVIEQIRSLKGEFNFETYFSLSCQNCPDVVQALNLMAVLNPNIRHVAIDGALFQDEVNDRKIMAVPSIYLNGENFGQGRM 185
Cdd:cd03026 2 DLLEQIRRLNGPINFETYVSLSCHNCPDVVQALNLMAVLNPNIEHEMIDGALFQDEVEERGIMSVPAIFLNGELFGFGRM 81
|
....*...
gi 499653597 186 GLEEILAK 193
Cdd:cd03026 82 TLEEILAK 89
|
|
| AhpF_NTD_N |
cd02974 |
Alkyl hydroperoxide reductase F subunit (AhpF) N-terminal domain (NTD) family, N-terminal ... |
1-94 |
1.89e-48 |
|
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: 162.36 E-value: 1.89e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 1 MLDANLKAQLKSYLERVTQPIEIVASLDDGAKSREMLDLLKDIASLSHQITLIDSGDDARKPSFSINRPGADISLRFAGI 80
Cdd:cd02974 1 MLDANLKQQLKAYLERLENPVELVASLDDSEKSAELLELLEEIASLSDKITLEEDNDDERKPSFSINRPGEDTGIRFAGI 80
|
90
....*....|....
gi 499653597 81 PMGHEFTSLVLALL 94
Cdd:cd02974 81 PMGHEFTSLVLALL 94
|
|
| AhpF_homolog |
TIGR03143 |
putative alkyl hydroperoxide reductase F subunit; This family of thioredoxin reductase ... |
242-509 |
3.14e-45 |
|
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: 166.88 E-value: 3.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 242 ERFGGQVLDTMAIENFISVQETEGPKLATALEEHVKQYDVDIMNLQRADKLIPGKngeLHEVRFASGaTLKAKSVILATG 321
Cdd:TIGR03143 36 DDFGGQITITSEVVNYPGILNTTGPELMQEMRQQAQDFGVKFLQAEVLDVDFDGD---IKTIKTARG-DYKTLAVLIATG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 322 ARWREMNVPGEQEYRNKGVAYCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVSHVTLLEFDVQLRADAVLQRKLHSL 401
Cdd:TIGR03143 112 ASPRKLGFPGEEEFTGRGVAYCATCDGEFFTGMDVFVIGGGFAAAEEAVFLTRYASKVTVIVREPDFTCAKLIAEKVKNH 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 402 PNVTVITSALTTEVTGDGqKVNGLRYKDRNTDELRTVELE------GIFVQIGLLPNTDWLKGTIELSPRGEIIVDNRGE 475
Cdd:TIGR03143 192 PKIEVKFNTELKEATGDD-GLRYAKFVNNVTGEITEYKAPkdagtfGVFVFVGYAPSSELFKGVVELDKRGYIPTNEDME 270
|
250 260 270
....*....|....*....|....*....|....
gi 499653597 476 TSIPGIFAAGDVTTVPYKQIVIAVGEGAKASLSA 509
Cdd:TIGR03143 271 TNVPGVYAAGDLRPKELRQVVTAVADGAIAATSA 304
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
238-502 |
8.33e-44 |
|
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: 157.09 E-value: 8.33e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 238 GVAAERFGGQVLDTMAIENFISVQET--EGPKLATALEEHVKQYDVDIMNLQR--ADKLIPGKnGELH--EVRFASGATL 311
Cdd:pfam07992 30 EDEGTCPYGGCVLSKALLGAAEAPEIasLWADLYKRKEEVVKKLNNGIEVLLGteVVSIDPGA-KKVVleELVDGDGETI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 312 KAKSVILATGARWREMNVPGEQEYRNKGVAYCPHCDGPLFK--GKRVAVIGGGNSGVEAAIDLAGIVSHVTLLE------ 383
Cdd:pfam07992 109 TYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKllPKRVVVVGGGYIGVELAAALAKLGKEVTLIEaldrll 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 384 --FDVQLRAdavLQRKLHSLPNVTVITSALTTEVTGDGQKVnglrykDRNTDELRTVELEGIFVQIGLLPNTDWLKGT-I 460
Cdd:pfam07992 189 raFDEEISA---ALEKALEKNGVEVRLGTSVKEIIGDGDGV------EVILKDGTEIDADLVVVAIGRRPNTELLEAAgL 259
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 499653597 461 ELSPRGEIIVDNRGETSIPGIFAAGDVTTVPYKQIVIAVGEG 502
Cdd:pfam07992 260 ELDERGGIVVDEYLRTSVPGIYAAGDCRVGGPELAQNAVAQG 301
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
245-513 |
1.14e-41 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 151.75 E-value: 1.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 245 GGQVLDTMAIENFI-SVQETEGPKLATALEEHVKQYDVDIM-------NLQRADKLIPGKNGELhevrfasgatlKAKSV 316
Cdd:PRK10262 41 GGQLTTTTEVENWPgDPNDLTGPLLMERMHEHATKFETEIIfdhinkvDLQNRPFRLTGDSGEY-----------TCDAL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 317 ILATGARWREMNVPGEQEYRNKGVAYCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVSHVTLLEFDVQLRADAVLQR 396
Cdd:PRK10262 110 IIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDGFRAEKILIK 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 397 KLH---SLPNVTVITSALTTEVTGDGQKVNGLRYKD-RNTDELRTVELEGIFVQIGLLPNTDWLKGTIELSpRGEIIVD- 471
Cdd:PRK10262 190 RLMdkvENGNIILHTNRTLEEVTGDQMGVTGVRLRDtQNSDNIESLDVAGLFVAIGHSPNTAIFEGQLELE-NGYIKVQs 268
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 499653597 472 ----NRGETSIPGIFAAGDVTTVPYKQIVIAVGEGAKASLSAFDHL 513
Cdd:PRK10262 269 gihgNATQTSIPGVFAAGDVMDHIYRQAITSAGTGCMAALDAERYL 314
|
|
| TRX_GRX_like |
cd02973 |
Thioredoxin (TRX)-Glutaredoxin (GRX)-like family; composed of archaeal and bacterial proteins ... |
118-184 |
1.67e-31 |
|
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: 115.74 E-value: 1.67e-31
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499653597 118 FNFETYFSLSCQNCPDVVQALNLMAVLNPNIRHVAIDGALFQDEVNDRKIMAVPSIYLNGENFGQGR 184
Cdd:cd02973 1 VNIEVFVSPTCPYCPDAVQAANRIAALNPNISAEMIDAAEFPDLADEYGVMSVPAIVINGKVEFVGR 67
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
257-492 |
4.03e-24 |
|
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: 102.97 E-value: 4.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 257 FISVQETEGPKLATALEEHVKQYDVDIMNLQRADKLIPGKNgelhEVRFASGATLKAKSVILATGARWREMNVPGEQE-- 334
Cdd:COG0446 27 YVGGGIKDPEDLLVRTPESFERKGIDVRTGTEVTAIDPEAK----TVTLRDGETLSYDKLVLATGARPRPPPIPGLDLpg 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 335 -YRNKGVAYCPHCDGPL--FKGKRVAVIGGGNSGVEAAIDL--AGIvsHVTLLEfdvqlRADAVLQR----------KLH 399
Cdd:COG0446 103 vFTLRTLDDADALREALkeFKGKRAVVIGGGPIGLELAEALrkRGL--KVTLVE-----RAPRLLGVldpemaalleEEL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 400 SLPNVTVITSALTTEVTGDGQKvnGLRYKDRntdelRTVELEGIFVQIGLLPNTDWLKGT-IELSPRGEIIVDNRGETSI 478
Cdd:COG0446 176 REHGVELRLGETVVAIDGDDKV--AVTLTDG-----EEIPADLVVVAPGVRPNTELAKDAgLALGERGWIKVDETLQTSD 248
|
250
....*....|....
gi 499653597 479 PGIFAAGDVTTVPY 492
Cdd:COG0446 249 PDVYAAGDCAEVPH 262
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
262-491 |
1.16e-22 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 99.83 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 262 ETEGPKLATALEEHVKQYDVDIMNLQRADKLIPGKngelHEVRFASGATLKAKSVILATGARWREMNVPGEQE-----YR 336
Cdd:COG1251 52 ETDEEDLLLRPADFYEENGIDLRLGTRVTAIDRAA----RTVTLADGETLPYDKLVLATGSRPRVPPIPGADLpgvftLR 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 337 NKG-----VAYCPhcdgplfKGKRVAVIGGGNSGVEAAIDLAGIVSHVTLLEF-----DVQLRADA--VLQRKLHSLpNV 404
Cdd:COG1251 128 TLDdadalRAALA-------PGKRVVVIGGGLIGLEAAAALRKRGLEVTVVERaprllPRQLDEEAgaLLQRLLEAL-GV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 405 TVITSALTTEVTGDGqKVNGLRYKDRntdelRTVELEGIFVQIGLLPNTDWLKGT-IELSpRGeIIVDNRGETSIPGIFA 483
Cdd:COG1251 200 EVRLGTGVTEIEGDD-RVTGVRLADG-----EELPADLVVVAIGVRPNTELARAAgLAVD-RG-IVVDDYLRTSDPDIYA 271
|
....*...
gi 499653597 484 AGDVTTVP 491
Cdd:COG1251 272 AGDCAEHP 279
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
301-488 |
1.17e-22 |
|
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: 100.55 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 301 HEVRFASGATLKAKSVILATGARWREMNVPGEQEYR---NKGV---AYCPhcdgplfkgKRVAVIGGGNSGVEAAIDLAG 374
Cdd:COG1249 119 HTVEVTGGETLTADHIVIATGSRPRVPPIPGLDEVRvltSDEAlelEELP---------KSLVVIGGGYIGLEFAQIFAR 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 375 IVSHVTLLEFDVQL--RAD----AVLQRKLHSLpNVTVITSALTTEVTGDGQKVNgLRYKDRntDELRTVELEGIFVQIG 448
Cdd:COG1249 190 LGSEVTLVERGDRLlpGEDpeisEALEKALEKE-GIDILTGAKVTSVEKTGDGVT-VTLEDG--GGEEAVEADKVLVATG 265
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499653597 449 LLPNTDWL---KGTIELSPRGEIIVDNRGETSIPGIFAAGDVT 488
Cdd:COG1249 266 RRPNTDGLgleAAGVELDERGGIKVDEYLRTSVPGIYAIGDVT 308
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
316-505 |
5.82e-21 |
|
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: 95.20 E-value: 5.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 316 VILATGA-RWREMNVPGEQ--------EY---RNKGVAYcphcDGPLFKGKRVAVIGGGNSgveaAIDLAGI-----VSH 378
Cdd:COG0493 210 VFLATGAgKPRDLGIPGEDlkgvhsamDFltaVNLGEAP----DTILAVGKRVVVIGGGNT----AMDCARTalrlgAES 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 379 VTLLEFDVQLRADAVLQRKLHSL-PNVTVITSALTTEVTGDGQ-KVNGLRYKD---RNTDE---LRTVELEG-------- 442
Cdd:COG0493 282 VTIVYRRTREEMPASKEEVEEALeEGVEFLFLVAPVEIIGDENgRVTGLECVRmelGEPDEsgrRRPVPIEGseftlpad 361
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499653597 443 -IFVQIGLLPNTDWLKGT--IELSPRGEIIVD-NRGETSIPGIFAAGDVTTVPyKQIVIAVGEGAKA 505
Cdd:COG0493 362 lVILAIGQTPDPSGLEEElgLELDKRGTIVVDeETYQTSLPGVFAGGDAVRGP-SLVVWAIAEGRKA 427
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
314-505 |
9.88e-20 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 91.78 E-value: 9.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 314 KSVILATGA-RWREMNVPGEQeyrNKGVAYC---------PHCDGPLFKGKRVAVIGGGNSgveaAIDLAGI-----VSH 378
Cdd:PRK11749 227 DAVFIGTGAgLPRFLGIPGEN---LGGVYSAvdfltrvnqAVADYDLPVGKRVVVIGGGNT----AMDAARTakrlgAES 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 379 VTLL-----------EFDVQL-RADAvlqrklhslpnVTVITSALTTEVTGDGQKVNGLRY-KDRNTDE----LRTVELE 441
Cdd:PRK11749 300 VTIVyrrgreempasEEEVEHaKEEG-----------VEFEWLAAPVEILGDEGRVTGVEFvRMELGEPdasgRRRVPIE 368
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499653597 442 G---------IFVQIGLLPNTDWLKGT--IELSPRGEIIVDNR-GETSIPGIFAAGDVTTvPYKQIVIAVGEGAKA 505
Cdd:PRK11749 369 GseftlpadlVIKAIGQTPNPLILSTTpgLELNRWGTIIADDEtGRTSLPGVFAGGDIVT-GAATVVWAVGDGKDA 443
|
|
| GlrX_arch |
TIGR02187 |
Glutaredoxin-like domain protein; This family of archaeal proteins contains a C-terminal ... |
7-177 |
5.20e-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: 85.57 E-value: 5.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 7 KAQLK-SYLERVTQPIEIVASLDDGAKS----REMLDLLKDIASLSHQITL----IDSGDDA---------RKPSFSINR 68
Cdd:TIGR02187 6 REILKeLFLKELKNPVEIVVFTDNDKEGcqycKETEQLLEELSEVSPKLKLeiydFDTPEDKeeaekygveRVPTTIILE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 69 PGADISLRFAGIPMGHEFTSLVLALLQVGGHPSKASVEVIEQIRSLKGEFNFETYFSLSCQNCPDVVQALNLMAVLNPNI 148
Cdd:TIGR02187 86 EGKDGGIRYTGIPAGYEFAALIEDIVRVSQGEPGLSEKTVELLQSLDEPVRIEVFVTPTCPYCPYAVLMAHKFALANDKI 165
|
170 180
....*....|....*....|....*....
gi 499653597 149 RHVAIDGALFQDEVNDRKIMAVPSIYLNG 177
Cdd:TIGR02187 166 LGEMIEANENPDLAEKYGVMSVPKIVINK 194
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
308-491 |
9.56e-17 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 82.53 E-value: 9.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 308 GATLKAKSVILATGARWRemNVPGEQE------YRNKGVAYCPHCdgPlfkgKRVAVIGGGNSGVEAAIDLAGIVSHVTL 381
Cdd:PRK06292 126 GERIEAKNIVIATGSRVP--PIPGVWLilgdrlLTSDDAFELDKL--P----KSLAVIGGGVIGLELGQALSRLGVKVTV 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 382 LEF----------DVQLRADAVLQRKLHslpnvtVITSALTTEVTGDGQKVNGLRYKDrntDELRTVELEGIFVQIGLLP 451
Cdd:PRK06292 198 FERgdrilpledpEVSKQAQKILSKEFK------IKLGAKVTSVEKSGDEKVEELEKG---GKTETIEADYVLVATGRRP 268
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 499653597 452 NTDWL---KGTIELSPRGEIIVDNRGETSIPGIFAAGDVTTVP 491
Cdd:PRK06292 269 NTDGLgleNTGIELDERGRPVVDEHTQTSVPGIYAAGDVNGKP 311
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
296-485 |
2.13e-16 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 79.58 E-value: 2.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 296 KNGELHEVRfASGATLKAKSVILATGarwrEMNVPgeqeYRNKGVAYCPHC----DGPLFKGKRVAVIGGGNSGVEAAID 371
Cdd:pfam13738 103 KEDDGFVVT-TSKGTYQARYVIIATG----EFDFP----NKLGVPELPKHYsyvkDFHPYAGQKVVVIGGYNSAVDAALE 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 372 LAGIVSHVTLL-----------EFDVQLRADaVLQRkLHSLPNVTVITSALTTEVTGDgqKVNGLRYKDrNTDELRTVEL 440
Cdd:pfam13738 174 LVRKGARVTVLyrgsewedrdsDPSYSLSPD-TLNR-LEELVKNGKIKAHFNAEVKEI--TEVDVSYKV-HTEDGRKVTS 248
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499653597 441 EGIFV-QIGLLPNTDWLK-GTIELSPRGEIIVDNRG-ETSIPGIFAAG 485
Cdd:pfam13738 249 NDDPIlATGYHPDLSFLKkGLFELDEDGRPVLTEETeSTNVPGLFLAG 296
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
316-506 |
6.03e-16 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 79.26 E-value: 6.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 316 VILATGA-RWREMNVPGEQEyrnKGV---------------AYCPHCDGPLFKGKRVAVIGGGNSGVEAAID--LAGiVS 377
Cdd:PRK12770 122 VLIATGTwKSRKLGIPGEDL---PGVysaleylfriraaklGYLPWEKVPPVEGKKVVVVGAGLTAVDAALEavLLG-AE 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 378 HVTLL-------------EFDvQLRADAVLQRKLhSLP-------NVTVITSALTTEVTGDGqkvNGLRYKDRNTDELRT 437
Cdd:PRK12770 198 KVYLAyrrtineapagkyEIE-RLIARGVEFLEL-VTPvriigegRVEGVELAKMRLGEPDE---SGRPRPVPIPGSEFV 272
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499653597 438 VELEGIFVQIGLLPNTDWLKGT--IELSPRGEIIVDNRGETSIPGIFAAGDVTTVPYKqIVIAVGEGAKAS 506
Cdd:PRK12770 273 LEADTVVFAIGEIPTPPFAKEClgIELNRKGEIVVDEKHMTSREGVFAAGDVVTGPSK-IGKAIKSGLRAA 342
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
302-488 |
6.07e-16 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 80.19 E-value: 6.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 302 EVRFASGA-TLKAKSVILATGARWREMnvPGeQEYRNKGVAYCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVSHVT 380
Cdd:PRK06416 123 RVMTEDGEqTYTAKNIILATGSRPREL--PG-IEIDGRVIWTSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVT 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 381 LLE--------FDVQLraDAVLQRKLHSlPNVTVITSALTTEVTgdgQKVNGLRYKDRNTDELRTVELEGIFVQIGLLPN 452
Cdd:PRK06416 200 IVEalprilpgEDKEI--SKLAERALKK-RGIKIKTGAKAKKVE---QTDDGVTVTLEDGGKEETLEADYVLVAVGRRPN 273
|
170 180 190
....*....|....*....|....*....|....*....
gi 499653597 453 TDWL---KGTIELSpRGEIIVDNRGETSIPGIFAAGDVT 488
Cdd:PRK06416 274 TENLgleELGVKTD-RGFIEVDEQLRTNVPNIYAIGDIV 311
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
301-498 |
3.89e-15 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 77.55 E-value: 3.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 301 HEVRfASGATLKAKSVILATGARWREMNVPGEQE---YRNKGV---AYCPhcdgplfkgKRVAVIGGGNSGVEAAIDLAG 374
Cdd:PRK06370 123 NTVR-VGGETLRAKRIFINTGARAAIPPIPGLDEvgyLTNETIfslDELP---------EHLVIIGGGYIGLEFAQMFRR 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 375 IVSHVTLLEFDVQL--RAD----AVLQRKLHSLpNVTVITSALTTEVTGDGqkvNGLRYKDRNTDELRTVELEGIFVQIG 448
Cdd:PRK06370 193 FGSEVTVIERGPRLlpREDedvaAAVREILERE-GIDVRLNAECIRVERDG---DGIAVGLDCNGGAPEITGSHILVAVG 268
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499653597 449 LLPNTDWL---KGTIELSPRGEIIVDNRGETSIPGIFAAGDV------TTVPYK--QIVIA 498
Cdd:PRK06370 269 RVPNTDDLgleAAGVETDARGYIKVDDQLRTTNPGIYAAGDCngrgafTHTAYNdaRIVAA 329
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
314-505 |
3.63e-13 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 71.59 E-value: 3.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 314 KSVILATGARW-REMNVPGEQ--------EY--R-NKGVAYCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVSHVTL 381
Cdd:PRK12831 230 DAVFIGSGAGLpKFMGIPGENlngvfsanEFltRvNLMKAYKPEYDTPIKVGKKVAVVGGGNVAMDAARTALRLGAEVHI 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 382 L----EFDVQLRADAVlqrklHSLPNVTVITSALT--TEVTGDGQ-KVNGLRYKDRNTDE------LRTVELEG------ 442
Cdd:PRK12831 310 VyrrsEEELPARVEEV-----HHAKEEGVIFDLLTnpVEILGDENgWVKGMKCIKMELGEpdasgrRRPVEIEGsefvle 384
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499653597 443 ---IFVQIGLLPNTDWLKGT--IELSPRGEIIVD-NRGETSIPGIFAAGD-VT---TVpykqiVIAVGEGAKA 505
Cdd:PRK12831 385 vdtVIMSLGTSPNPLISSTTkgLKINKRGCIVADeETGLTSKEGVFAGGDaVTgaaTV-----ILAMGAGKKA 452
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
354-490 |
2.69e-12 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 68.53 E-value: 2.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 354 KRVAVIGGGNSGVEAAIDLAGIVSHVTLLEFDVQLRADA-------VLQRKLHSlPNVTVITSALTTEVTGDgQKVNGLR 426
Cdd:PRK09564 150 KNIVIIGAGFIGLEAVEAAKHLGKNVRIIQLEDRILPDSfdkeitdVMEEELRE-NGVELHLNEFVKSLIGE-DKVEGVV 227
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499653597 427 ykdrnTDElRTVELEGIFVQIGLLPNTDWLKGT-IELSPRGEIIVDNRGETSIPGIFAAGDVTTV 490
Cdd:PRK09564 228 -----TDK-GEYEADVVIVATGVKPNTEFLEDTgLKTLKNGAIIVDEYGETSIENIYAAGDCATI 286
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
311-488 |
3.92e-12 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 68.24 E-value: 3.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 311 LKAKSVILATGARWREMNVPGEQE----YRNKGVAYCPHcdgplfKGKRVAVIGGGNSGVEAAIDLAGIVSHVTLLEfdv 386
Cdd:PRK07251 117 LTAETIVINTGAVSNVLPIPGLADskhvYDSTGIQSLET------LPERLGIIGGGNIGLEFAGLYNKLGSKVTVLD--- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 387 qlRADAVLQRKLHSLPN----------VTVITSALTTEVTGDGQKVnglrykdRNTDELRTVELEGIFVQIGLLPNTD-- 454
Cdd:PRK07251 188 --AASTILPREEPSVAAlakqymeedgITFLLNAHTTEVKNDGDQV-------LVVTEDETYRFDALLYATGRKPNTEpl 258
|
170 180 190
....*....|....*....|....*....|....*
gi 499653597 455 WLKGT-IELSPRGEIIVDNRGETSIPGIFAAGDVT 488
Cdd:PRK07251 259 GLENTdIELTERGAIKVDDYCQTSVPGVFAVGDVN 293
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
308-488 |
2.71e-11 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 65.56 E-value: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 308 GATLKAKSVILATGARWREMNVPGEQeyrnkgvaYCPHCDG-------PlfkgKRVAVIGGGNSGVEaaidLAGIV---- 376
Cdd:PRK06116 127 GERYTADHILIATGGRPSIPDIPGAE--------YGITSDGffaleelP----KRVAVVGAGYIAVE----FAGVLnglg 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 377 SHVTLLefdvqLRADAVLQRKLHSL----------PNVTVITSALTTEV--TGDGQKVngLRYKDRntdelRTVELEGIF 444
Cdd:PRK06116 191 SETHLF-----VRGDAPLRGFDPDIretlveemekKGIRLHTNAVPKAVekNADGSLT--LTLEDG-----ETLTVDCLI 258
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499653597 445 VQIGLLPNTDWL---KGTIELSPRGEIIVDNRGETSIPGIFAAGDVT 488
Cdd:PRK06116 259 WAIGREPNTDGLgleNAGVKLNEKGYIIVDEYQNTNVPGIYAVGDVT 305
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
302-382 |
1.47e-10 |
|
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: 62.96 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 302 EVRFASGATLKAKSVILATGArWREMNVP---------GEQ----EYRNkgvaycphcdgPL-FKGKRVAVIGGGNSGVE 367
Cdd:COG2072 118 TVTTDDGETLTARFVVVATGP-LSRPKIPdipgledfaGEQlhsaDWRN-----------PVdLAGKRVLVVGTGASAVQ 185
|
90
....*....|....*
gi 499653597 368 AAIDLAGIVSHVTLL 382
Cdd:COG2072 186 IAPELARVAAHVTVF 200
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
302-488 |
1.75e-10 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 63.30 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 302 EVRFASGATLK--AKSVILATGARWREMNVPGEQEYRNKGVAYCPHcDGPlfkgKRVAVIGGGNSGVEAAIDLAGIVSHV 379
Cdd:PLN02507 155 EVTQLDGTKLRytAKHILIATGSRAQRPNIPGKELAITSDEALSLE-ELP----KRAVVLGGGYIAVEFASIWRGMGATV 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 380 TLL--------EFDVQLRadAVLQR-------KLHSLPNVTVITSalttevTGDGQKVnglrykdrNTDELRTVELEGIF 444
Cdd:PLN02507 230 DLFfrkelplrGFDDEMR--AVVARnlegrgiNLHPRTNLTQLTK------TEGGIKV--------ITDHGEEFVADVVL 293
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 499653597 445 VQIGLLPNTDWLK---GTIELSPRGEIIVDNRGETSIPGIFAAGDVT 488
Cdd:PLN02507 294 FATGRAPNTKRLNleaVGVELDKAGAVKVDEYSRTNIPSIWAIGDVT 340
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
314-513 |
1.04e-09 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 61.30 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 314 KSVILATGARW-REMNVPGEQ--------EY---RNKGVAYCPHCDGPLFKGKRVAVIGGGNSGVEA---AIDLAGivSH 378
Cdd:PRK12778 519 KGIFIASGAGLpNFMNIPGENsngvmssnEYltrVNLMDAASPDSDTPIKFGKKVAVVGGGNTAMDSartAKRLGA--ER 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 379 VTLL----EFDVQLRADAVLQRKLHSLPNVTVITSaltTEVTGDGQ-KVNGLRYKDRNTDE------LRTVELEG----- 442
Cdd:PRK12778 597 VTIVyrrsEEEMPARLEEVKHAKEEGIEFLTLHNP---IEYLADEKgWVKQVVLQKMELGEpdasgrRRPVAIPGstftv 673
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499653597 443 ----IFVQIGLLPNTDWLKGT--IELSPRGEIIVDNRGETSIPGIFAAGDVTTvPYKQIVIAVGEGAKASLSAFDHL 513
Cdd:PRK12778 674 dvdlVIVSVGVSPNPLVPSSIpgLELNRKGTIVVDEEMQSSIPGIYAGGDIVR-GGATVILAMGDGKRAAAAIDEYL 749
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
317-486 |
1.21e-09 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 59.93 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 317 ILATGARWREMNVPGE---------QEYRNkgvaycphCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVSHVTLLEFDVQ 387
Cdd:PRK04965 104 VLATGASAFVPPIPGRelmltlnsqQEYRA--------AETQLRDAQRVLVVGGGLIGTELAMDLCRAGKAVTLVDNAAS 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 388 LRA----DAVLQRKLHSLPNVTViTSALTTEVTGDGQKVNGLRYKdrnTDELRTVELEGIFVQIGLLPNTDWLKGTIELS 463
Cdd:PRK04965 176 LLAslmpPEVSSRLQHRLTEMGV-HLLLKSQLQGLEKTDSGIRAT---LDSGRSIEVDAVIAAAGLRPNTALARRAGLAV 251
|
170 180
....*....|....*....|...
gi 499653597 464 PRGeIIVDNRGETSIPGIFAAGD 486
Cdd:PRK04965 252 NRG-IVVDSYLQTSAPDIYALGD 273
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
354-487 |
1.38e-09 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 60.61 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 354 KRVAVIGGGNSGVEAAIDLA--GIVSHVT-----LLEFDVQLRADAVLQRKLHSLpNVTVITSALTTEVTGDGqKVNGLR 426
Cdd:TIGR02374 141 KKAAVIGGGLLGLEAAVGLQnlGMDVSVIhhapgLMAKQLDQTAGRLLQRELEQK-GLTFLLEKDTVEIVGAT-KADRIR 218
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499653597 427 YKDRNtdelrTVELEGIFVQIGLLPNTDwLKGTIELSPRGEIIVDNRGETSIPGIFAAGDV 487
Cdd:TIGR02374 219 FKDGS-----SLEADLIVMAAGIRPNDE-LAVSAGIKVNRGIIVNDSMQTSDPDIYAVGEC 273
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
301-493 |
2.62e-09 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 59.20 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 301 HEVRFASGATLKAKSVILATGARWREMNVPGEQeyrnkGVAYcpHCDGPLFK----GKRVAVIGGGNSGVEAAIDLAGIV 376
Cdd:PRK07846 117 KTLRTGDGEEITADQVVIAAGSRPVIPPVIADS-----GVRY--HTSDTIMRlpelPESLVIVGGGFIAAEFAHVFSALG 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 377 SHVTLLE-FDVQLRA--DAVLQRklhslpnVTVITSA-----LTTEVTGDGQKVNGLRYkdrNTDELRTVELEGIFVQIG 448
Cdd:PRK07846 190 VRVTVVNrSGRLLRHldDDISER-------FTELASKrwdvrLGRNVVGVSQDGSGVTL---RLDDGSTVEADVLLVATG 259
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 499653597 449 LLPNTDWL---KGTIELSPRGEIIVDNRGETSIPGIFAAGDVTTvPYK 493
Cdd:PRK07846 260 RVPNGDLLdaaAAGVDVDEDGRVVVDEYQRTSAEGVFALGDVSS-PYQ 306
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
310-487 |
2.95e-09 |
|
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: 59.10 E-value: 2.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 310 TLKAKSVILATGARWREMNVPGEQEYRNKG-----VAYCPhcdgplfkGKRVaVIGGGNSGVEAAIDLAGIVSHVTLLEF 384
Cdd:TIGR01438 141 IYSAERFLIATGERPRYPGIPGAKELCITSddlfsLPYCP--------GKTL-VVGASYVALECAGFLAGIGLDVTVMVR 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 385 DVQLRA---DAVLQRKLH-SLPNVTVITSALTTEVTGDGQKVnglRYKDRNTDELRTVELEGIFVQIGLLPNTDWLK--- 457
Cdd:TIGR01438 212 SILLRGfdqDCANKVGEHmEEHGVKFKRQFVPIKVEQIEAKV---LVEFTDSTNGIEEEYDTVLLAIGRDACTRKLNlen 288
|
170 180 190
....*....|....*....|....*....|.
gi 499653597 458 -GTIELSPRGEIIVDNRGETSIPGIFAAGDV 487
Cdd:TIGR01438 289 vGVKINKKTGKIPADEEEQTNVPYIYAVGDI 319
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
355-422 |
8.42e-09 |
|
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: 52.21 E-value: 8.42e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499653597 355 RVAVIGGGNSGVEAAIDLAGIVSHVTLLEFDVQLR------ADAVLQRKLHSLpNVTVITSALTTEVTGDGQKV 422
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLpgfdpeIAKILQEKLEKN-GIEFLLNTTVEAIEGNGDGV 73
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
352-514 |
1.71e-08 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 57.44 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 352 KGKRVAVIGGGNSGVEAAIDLA--GIVSHVtlLEFDVQLRADAV-------LQRKLHSLpNVTVITSALTTEVTGDGQKV 422
Cdd:PRK14989 144 RSKRGAVVGGGLLGLEAAGALKnlGVETHV--IEFAPMLMAEQLdqmggeqLRRKIESM-GVRVHTSKNTLEIVQEGVEA 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 423 -NGLRYKDRNtdelrTVELEGIFVQIGLLPNtDWLKGTIELS--PRGEIIVDNRGETSIPGIFAAGDVTTvpYKQIVIA- 498
Cdd:PRK14989 221 rKTMRFADGS-----ELEVDFIVFSTGIRPQ-DKLATQCGLAvaPRGGIVINDSCQTSDPDIYAIGECAS--WNNRVFGl 292
|
170
....*....|....*.
gi 499653597 499 VGEGAKASLSAFDHLI 514
Cdd:PRK14989 293 VAPGYKMAQVAVDHLL 308
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
354-507 |
2.55e-08 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 56.31 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 354 KRVAVIGGGNSGVEAAIDLAGIVSHVTLLEFDVQL-RADAVLQRKLHS---LPNVTVITSALTTEVT-GDGQKVnglryK 428
Cdd:PRK13748 271 ERLAVIGSSVVALELAQAFARLGSKVTILARSTLFfREDPAIGEAVTAafrAEGIEVLEHTQASQVAhVDGEFV-----L 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 429 DRNTDELRTVELegiFVQIGLLPNTDWL---KGTIELSPRGEIIVDNRGETSIPGIFAAGDVTTVPykQIV-IAVGEGAK 504
Cdd:PRK13748 346 TTGHGELRADKL---LVATGRAPNTRSLaldAAGVTVNAQGAIVIDQGMRTSVPHIYAAGDCTDQP--QFVyVAAAAGTR 420
|
...
gi 499653597 505 ASL 507
Cdd:PRK13748 421 AAI 423
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
308-494 |
5.17e-08 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 55.39 E-value: 5.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 308 GATLKAKSVILATGarwremnvpGEQEYRN-KGVAYCPHCDG--PLFKGKRVAVIGGGNSGVEaaidLAGIVS------- 377
Cdd:PTZ00058 198 GQVIEGKNILIAVG---------NKPIFPDvKGKEFTISSDDffKIKEAKRIGIAGSGYIAVE----LINVVNrlgaesy 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 378 -----HVTLLEFDVQLRADAVLQRKLHslpNVTVITSALTTEVTGDGQKvNGLRYKdrnTDELRTVELEGIFVQIGLLPN 452
Cdd:PTZ00058 265 ifargNRLLRKFDETIINELENDMKKN---NINIITHANVEEIEKVKEK-NLTIYL---SDGRKYEHFDYVIYCVGRSPN 337
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 499653597 453 TDWL--KGTIELSPRGEIIVDNRGETSIPGIFAAGDVTTVPYKQ 494
Cdd:PTZ00058 338 TEDLnlKALNIKTPKGYIKVDDNQRTSVKHIYAVGDCCMVKKNQ 381
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
302-490 |
5.58e-08 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 55.25 E-value: 5.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 302 EVRFASGA--TLKAKSVILATGARWREMnvPGEQeyrnkgvaycphCDG---------------PlfkgKRVAVIGGGNS 364
Cdd:PRK07845 127 KVTTADGGeeTLDADVVLIATGASPRIL--PTAE------------PDGeriltwrqlydldelP----EHLIVVGSGVT 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 365 GVEAAIDLAGIVSHVTLlefdVQLR--------ADA------VLQRKlhslpNVTVI--TSALTTEVTGDGQKVnglryk 428
Cdd:PRK07845 189 GAEFASAYTELGVKVTL----VSSRdrvlpgedADAaevleeVFARR-----GMTVLkrSRAESVERTGDGVVV------ 253
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499653597 429 dRNTDElRTVELEGIFVQIGLLPNTDWL---KGTIELSPRGEIIVDNRGETSIPGIFAAGDVTTV 490
Cdd:PRK07845 254 -TLTDG-RTVEGSHALMAVGSVPNTAGLgleEAGVELTPSGHITVDRVSRTSVPGIYAAGDCTGV 316
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
310-503 |
6.16e-08 |
|
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: 54.98 E-value: 6.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 310 TLKAKSVILATGArWREM-NVPGEQEYRNKGVAYcpHCDGPlfkGKRVAVIGGGNSGVEAA------------IDLAgIV 376
Cdd:TIGR01423 149 RLQAEHILLATGS-WPQMlGIPGIEHCISSNEAF--YLDEP---PRRVLTVGGGFISVEFAgifnaykprggkVTLC-YR 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 377 SHVTLLEFDVQLRADAVLQRKLHSLpNVTVITSALTTEVTGDGQKvnglrykDRNTDELRTVELEGIFVQIGLLPNTDWL 456
Cdd:TIGR01423 222 NNMILRGFDSTLRKELTKQLRANGI-NIMTNENPAKVTLNADGSK-------HVTFESGKTLDVDVVMMAIGRVPRTQTL 293
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 499653597 457 ---KGTIELSPRGEIIVDNRGETSIPGIFAAGDVT----TVPykqivIAVGEGA 503
Cdd:TIGR01423 294 qldKVGVELTKKGAIQVDEFSRTNVPNIYAIGDVTdrvmLTP-----VAINEGA 342
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
316-486 |
9.98e-08 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 54.40 E-value: 9.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 316 VILATGA-RWREMNVPGEQ--------EY---RNKGVAYCPHCDGPLFKGKRVAVIGGGNSGVEAAidlagivshVTlle 383
Cdd:PRK12810 232 VFLGTGAyKPRDLGIPGRDldgvhfamDFliqNTRRVLGDETEPFISAKGKHVVVIGGGDTGMDCV---------GT--- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 384 fdvQLR--ADAVLQRKLHSLP-------------------------NVTVITSALTTEVTGDGQKVNGLRYKDRNTDELR 436
Cdd:PRK12810 300 ---AIRqgAKSVTQRDIMPMPpsrrnknnpwpywpmklevsnaheeGVEREFNVQTKEFEGENGKVTGVKVVRTELGEGD 376
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499653597 437 TVELEG---------IFVQIGLL-PNTDWLK-GTIELSPRGEIIVDNRG-ETSIPGIFAAGD 486
Cdd:PRK12810 377 FEPVEGsefvlpadlVLLAMGFTgPEAGLLAqFGVELDERGRVAAPDNAyQTSNPKVFAAGD 438
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
266-487 |
2.03e-07 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 53.39 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 266 PKLATALEEHVKQYD-VDIMNLQRADKLIPGKngelHEVRFASGATLKAKSVILATGARWRE---MNVPGEQEYRNKGVA 341
Cdd:PRK09754 57 PQLQQVLPANWWQENnVHLHSGVTIKTLGRDT----RELVLTNGESWHWDQLFIATGAAARPlplLDALGERCFTLRHAG 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 342 YCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVSHVTLLEF--DVQLR-ADAVLQRKL---HSLPNVTVITSALTTEV 415
Cdd:PRK09754 133 DAARLREVLQPERSVVIVGAGTIGLELAASATQRRCKVTVIELaaTVMGRnAPPPVQRYLlqrHQQAGVRILLNNAIEHV 212
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499653597 416 TgDGQKVnglrYKDRNTDElrTVELEGIFVQIGLLPNtDWLKGTIELSPRGEIIVDNRGETSIPGIFAAGDV 487
Cdd:PRK09754 213 V-DGEKV----ELTLQSGE--TLQADVVIYGIGISAN-DQLAREANLDTANGIVIDEACRTCDPAIFAGGDV 276
|
|
| Thioredoxin_3 |
pfam13192 |
Thioredoxin domain; |
124-194 |
2.53e-07 |
|
Thioredoxin domain;
Pssm-ID: 433026 [Multi-domain] Cd Length: 71 Bit Score: 47.98 E-value: 2.53e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499653597 124 FSLSCQNCPDVVQALNlMAVLNPNIRHVAIDGALFQdEVNDRKIMAVPSIYLNGENFGQGRMGLEEILAKL 194
Cdd:pfam13192 1 LGPGCPKCPQLEKAVK-EAAAELGIDAEVEKVTDFP-EIAKYGVMSTPALVINGKVVSSGKVPSEEEIRKL 69
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
347-505 |
4.78e-07 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 52.57 E-value: 4.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 347 DGPLFKGKRVAVIGGGNSGVEAA-------IDLAGIVSHVTL-----LEFDVQlraDAVLQrklhslpNVTVITSALTTE 414
Cdd:PRK12771 261 GEPPFLGKRVVVIGGGNTAMDAArtarrlgAEEVTIVYRRTRedmpaHDEEIE---EALRE-------GVEINWLRTPVE 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 415 VTGDGQKVNGLRY----------KDRN---TDELRTVELEGIFVQIGllpntdwlkGTIELSP----------RGEIIVD 471
Cdd:PRK12771 331 IEGDENGATGLRVitvekmeldeDGRPspvTGEEETLEADLVVLAIG---------QDIDSAGlesvpgvevgRGVVQVD 401
|
170 180 190
....*....|....*....|....*....|....*
gi 499653597 472 -NRGETSIPGIFAAGDVTTVPyKQIVIAVGEGAKA 505
Cdd:PRK12771 402 pNFMMTGRPGVFAGGDMVPGP-RTVTTAIGHGKKA 435
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
354-506 |
8.84e-07 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 51.69 E-value: 8.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 354 KRVAVIGGGNsgveAAIDLAGIVSHVTLLEF---DVQLRAdavLQRKLHSLP-NVTVITSALT-----------TEVTGD 418
Cdd:PRK13984 419 RSLVVIGGGN----VAMDIARSMARLQKMEYgevNVKVTS---LERTFEEMPaDMEEIEEGLEegvviypgwgpMEVVIE 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 419 GQKVNGLRYK------DRNT------DE--LRTVELEGIFVQIGLLPNTDWL----KGTIELSpRGEIIVDNRGETSIPG 480
Cdd:PRK13984 492 NDKVKGVKFKkcvevfDEEGrfnpkfDEsdQIIVEADMVVEAIGQAPDYSYLpeelKSKLEFV-RGRILTNEYGQTSIPW 570
|
170 180
....*....|....*....|....*.
gi 499653597 481 IFAAGDVTTVPykQIVIAVGEGAKAS 506
Cdd:PRK13984 571 LFAGGDIVHGP--DIIHGVADGYWAA 594
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
301-491 |
1.72e-06 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 50.13 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 301 HEVRFASGATLKAKSVILATGARWREMNVPGEQEYrnkGVAYCPHCDGPLF--------------KGKRVAVIGGGNSGV 366
Cdd:COG1252 86 RTVTLADGRTLSYDYLVIATGSVTNFFGIPGLAEH---ALPLKTLEDALALrerllaaferaerrRLLTIVVVGGGPTGV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 367 EaaidLAGIVSH-----------------VTLLE--------FDVQLRADAvlQRKLHSLpNVTVITSALTTEVTGDGqk 421
Cdd:COG1252 163 E----LAGELAEllrkllrypgidpdkvrITLVEagprilpgLGEKLSEAA--EKELEKR-GVEVHTGTRVTEVDADG-- 233
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499653597 422 vngLRYKDRNTDELRTVelegIFVqIGLLPNtDWLKGT-IELSPRGEIIVDNRGET-SIPGIFAAGDVTTVP 491
Cdd:COG1252 234 ---VTLEDGEEIPADTV----IWA-AGVKAP-PLLADLgLPTDRRGRVLVDPTLQVpGHPNVFAIGDCAAVP 296
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
302-487 |
1.92e-05 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 47.07 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 302 EVRFASGA--TLKAKSVILATGARwremnvPgeqeYRNKGVAycphcdgplFKGKRV----------------AVIGGGN 363
Cdd:PRK05249 125 EVECPDGEveTLTADKIVIATGSR------P----YRPPDVD---------FDHPRIydsdsilsldhlprslIIYGAGV 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 364 SGVEAAIDLAGIVSHVTL-------LEF------DV---QLRADAVLQR------KLHSLPNVTVITSAlttevtgDGQK 421
Cdd:PRK05249 186 IGCEYASIFAALGVKVTLintrdrlLSFlddeisDAlsyHLRDSGVTIRhneeveKVEGGDDGVIVHLK-------SGKK 258
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499653597 422 V--------NGlrykdR--NTDELrtvELEgifvQIGLlpntdwlkgtiELSPRGEIIVDNRGETSIPGIFAAGDV 487
Cdd:PRK05249 259 IkadcllyaNG-----RtgNTDGL---NLE----NAGL-----------EADSRGQLKVNENYQTAVPHIYAVGDV 311
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
295-488 |
3.13e-05 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 46.41 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 295 GKNGELHEVRfASGATLKAKSVILATGARWREMNVPGEQEYRNKGVAYcphcDGPlFKGKRVAVIGGGNSGVEAAIDLAG 374
Cdd:PLN02546 200 GKIVDPHTVD-VDGKLYTARNILIAVGGRPFIPDIPGIEHAIDSDAAL----DLP-SKPEKIAIVGGGYIALEFAGIFNG 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 375 IVSHV--------TLLEFDVQLRaDAVLQRKlhSLPNVTVITSALTTEVTGDGqkvNGLRYKDRNTDelrTVE-LEGIFV 445
Cdd:PLN02546 274 LKSDVhvfirqkkVLRGFDEEVR-DFVAEQM--SLRGIEFHTEESPQAIIKSA---DGSLSLKTNKG---TVEgFSHVMF 344
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 499653597 446 QIGLLPNTDWL---KGTIELSPRGEIIVDNRGETSIPGIFAAGDVT 488
Cdd:PLN02546 345 ATGRKPNTKNLgleEVGVKMDKNGAIEVDEYSRTSVPSIWAVGDVT 390
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
210-488 |
3.17e-05 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 46.46 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 210 QAFDVLVVGGGPAGASAAIYAARKGIRTGVAAE--------RFGGQVLDTMAI---------ENFISVQEtegpklatAL 272
Cdd:PRK06327 3 KQFDVVVIGAGPGGYVAAIRAAQLGLKVACIEAwknpkgkpALGGTCLNVGCIpskallassEEFENAGH--------HF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 273 EEH---VKQYDVDI--MnLQRADKLIP-------------------------GKNGELHEVRFA--SGATLKAKSVILAT 320
Cdd:PRK06327 75 ADHgihVDGVKIDVakM-IARKDKVVKkmtggieglfkknkitvlkgrgsfvGKTDAGYEIKVTgeDETVITAKHVIIAT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 321 GARWREM-NVPgeqeYRNKGVaycpHC-DGPL-FKG--KRVAVIGGGNSGVEAAIDLAGIVSHVTLLEF--------DVQ 387
Cdd:PRK06327 154 GSEPRHLpGVP----FDNKII----LDnTGALnFTEvpKKLAVIGAGVIGLELGSVWRRLGAEVTILEAlpaflaaaDEQ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 388 LRADAVLQRKLHSLpnvTVITSALTTEVTGDGQKVNgLRYKDRNTDElRTVELEGIFVQIGLLPNTDWL---KGTIELSP 464
Cdd:PRK06327 226 VAKEAAKAFTKQGL---DIHLGVKIGEIKTGGKGVS-VAYTDADGEA-QTLEVDKLIVSIGRVPNTDGLgleAVGLKLDE 300
|
330 340
....*....|....*....|....
gi 499653597 465 RGEIIVDNRGETSIPGIFAAGDVT 488
Cdd:PRK06327 301 RGFIPVDDHCRTNVPNVYAIGDVV 324
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
352-495 |
3.81e-05 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 46.31 E-value: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 352 KGKRVAVIGGGNSGVEAAIDLAGIVSHVTLLEFDVQLRA--DAVLQRKLHSLPNVTVITSALTTEVTgdgqKVNG--LRY 427
Cdd:PRK13512 147 QVDKALVVGAGYISLEVLENLYERGLHPTLIHRSDKINKlmDADMNQPILDELDKREIPYRLNEEID----AINGneVTF 222
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499653597 428 KDRNTDELRTVeLEGIfvqiGLLPNTDWLKGT-IELSPRGEIIVDNRGETSIPGIFAAGDVTTVPYKQI 495
Cdd:PRK13512 223 KSGKVEHYDMI-IEGV----GTHPNSKFIESSnIKLDDKGFIPVNDKFETNVPNIYAIGDIITSHYRHV 286
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
306-488 |
6.02e-05 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 45.98 E-value: 6.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 306 ASGATLKAKS---VILATGARW-REMNVPGEQ--------EYR---NKGVAYCPHCDGPL--FKGKRVAVIGGGNSGVEA 368
Cdd:PRK12779 383 ATLEDLKAAGfwkIFVGTGAGLpTFMNVPGEHllgvmsanEFLtrvNLMRGLDDDYETPLpeVKGKEVFVIGGGNTAMDA 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 369 AIDLAGIVSHVTLLEFDVQLRADAVLQRKLHSLP---NVTVITSAltTEVTGDGQK---------VNGL-------RYKD 429
Cdd:PRK12779 463 ARTAKRLGGNVTIVYRRTKSEMPARVEELHHALEegiNLAVLRAP--REFIGDDHThfvthalldVNELgepdksgRRSP 540
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499653597 430 RNTDELRTVELEGIFVQIGLLPN------------TDWlkGTIELSPrgeiivdNRGETSIPGIFAAGDVT 488
Cdd:PRK12779 541 KPTGEIERVPVDLVIMALGNTANpimkdaepglktNKW--GTIEVEK-------GSQRTSIKGVYSGGDAA 602
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
308-417 |
8.16e-05 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 45.24 E-value: 8.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 308 GATLKAKSVILATGARWREMNVPgeQEYRNKGVaycphcdgplfkgKRVAVIGGGNSGVEAAIDLA--GIvsHVTLLE-- 383
Cdd:COG1148 110 AATEKAKDLVRMAVAKAKLLEPL--EPIKVPVN-------------KRALVIGGGIAGMTAALELAeqGY--EVYLVEke 172
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 499653597 384 -------------FDVQLRADAVLQRKLHSL---PNVTVITSALTTEVTG 417
Cdd:COG1148 173 pelggraaqlhktFPGLDCPQCILEPLIAEVeanPNITVYTGAEVEEVSG 222
|
|
| PRK08275 |
PRK08275 |
putative oxidoreductase; Provisional |
470-520 |
3.61e-04 |
|
putative oxidoreductase; Provisional
Pssm-ID: 181346 [Multi-domain] Cd Length: 554 Bit Score: 43.12 E-value: 3.61e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 499653597 470 VDNRGETSIPGIFAAGDVTTVPYKQIVIAVGEGAKASLSAFDHLIRTSAPA 520
Cdd:PRK08275 361 VNEKAETTVPGLYAAGDMASVPHNYMLGAFTYGWFAGENAAEYVAGRDLPE 411
|
|
| PfPDO_like_N |
cd02975 |
Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO)-like family, N-terminal TRX-fold ... |
20-97 |
2.33e-03 |
|
Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO)-like family, N-terminal TRX-fold subdomain; composed of proteins with similarity to PfPDO, a redox active thermostable protein believed to be the archaeal counterpart of bacterial DsbA and eukaryotic protein disulfide isomerase (PDI), which are both involved in oxidative protein folding. PfPDO contains two redox active CXXC motifs in two contiguous TRX-fold subdomains. The active site in the N-terminal TRX-fold subdomain is required for isomerase but not for reductase activity of PfPDO. The exclusive presence of PfPDO-like proteins in extremophiles may suggest that they have a special role in adaptation to extreme conditions.
Pssm-ID: 239273 [Multi-domain] Cd Length: 113 Bit Score: 37.75 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499653597 20 PIEIV--ASLDDGAKSREMLDLLKDIASLSHQITL----IDSGDDA-------RKPSFSINR-PGADISLRFAGIPMGHE 85
Cdd:cd02975 22 PVDLVvfSSKEGCQYCEVTKQLLEELSELSDKLKLeiydFDEDKEKaekygveRVPTTIFLQdGGKDGGIRYYGLPAGYE 101
|
90
....*....|..
gi 499653597 86 FTSLVLALLQVG 97
Cdd:cd02975 102 FASLIEDIVRVS 113
|
|
| |
