|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
1-507 |
0e+00 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 931.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 1 MLNADLKQQLQQLLQLMEGDVEFRASIGSDDKSKELKDLLDEIAEMTDYITIVEKELK-RTPSFQVSKPEEDTGITFAGI 79
Cdd:PRK15317 1 MLDANLKTQLKQYLELLERPIELVASLDDSEKSAELKELLEEIASLSDKITVEEDSLDvRKPSFSITRPGEDTGVRFAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 80 PLGHEFNSLVLAILQVSGRAPKEKQSIIDQIKGLEGNYNFETYVSLTCQKCPDVVQALNLMSVINPNITHTMIDGAVFRE 159
Cdd:PRK15317 81 PMGHEFTSLVLALLQVGGHPPKLDQEVIEQIKALDGDFHFETYVSLSCHNCPDVVQALNLMAVLNPNITHTMIDGALFQD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 160 E--SKDIMAVPAVFLDGEEFGNGRMTISDILSKLGS---TQDASEYEDKDPYDVLIIGGGPASGSAAIYTARKGLRTGIV 234
Cdd:PRK15317 161 EveARNIMAVPTVFLNGEEFGQGRMTLEEILAKLDTgaaARAAEELNAKDPYDVLVVGGGPAGAAAAIYAARKGIRTGIV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 235 ADRIGGQVNDTAGIENFITVKQTTGSEFSSNLAAHIEEYDIDAMTGIRATKIEKTDKAIRVTLENDAVLESKTAIISTGA 314
Cdd:PRK15317 241 AERFGGQVLDTMGIENFISVPETEGPKLAAALEEHVKEYDVDIMNLQRASKLEPAAGLIEVELANGAVLKAKTVILATGA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 315 SWRKLNIPGEDRLINKGVAFCPHCDGPLFENKNVAVIGGGNSGVEAAIDLAGIVKHVTLFEFAPELKADTVLQERLRSFP 394
Cdd:PRK15317 321 RWRNMNVPGEDEYRNKGVAYCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVKHVTVLEFAPELKADQVLQDKLRSLP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 395 NVDIHTNARTAEVLGE-DHVTGLSYEDMSSGEMKELSLDGIFVQIGLVPNTKWIGDAVELNNRGEVVVDRENNTNVPGIF 473
Cdd:PRK15317 401 NVTIITNAQTTEVTGDgDKVTGLTYKDRTTGEEHHLELEGVFVQIGLVPNTEWLKGTVELNRRGEIIVDARGATSVPGVF 480
|
490 500 510
....*....|....*....|....*....|....
gi 515743079 474 AAGDVTDQKYKQIIISMGSGANAALSAFDYIIRN 507
Cdd:PRK15317 481 AAGDCTTVPYKQIIIAMGEGAKAALSAFDYLIRN 514
|
|
| AhpF |
TIGR03140 |
alkyl hydroperoxide reductase subunit F; This enzyme is the partner of the peroxiredoxin ... |
1-507 |
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: 816.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 1 MLNADLKQQLQQLLQLMEGDVEFRASIGSDDKSKELKDLLDEIAEMTDYITIVEKE--LKRTPSFQVSKPEEDTGITFAG 78
Cdd:TIGR03140 1 MLDQSLLAQLKSYLASLENPVTLVLSAGSHEKSKELLELLDEIASLSDKISLTQNTadTLRKPSFTILRDGADTGIRFAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 79 IPLGHEFNSLVLAILQVSGRAPKEKQSIIDQIKGLEGNYNFETYVSLTCQKCPDVVQALNLMSVINPNITHTMIDGAVFR 158
Cdd:TIGR03140 81 IPGGHEFTSLVLAILQVGGHGPKLDEGIIDRIRRLNGPLHFETYVSLTCQNCPDVVQALNQMALLNPNISHTMIDGALFQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 159 EE--SKDIMAVPAVFLDGEEFGNGRMTISDILSKLGST---QDASEYEDKDPYDVLIIGGGPASGSAAIYTARKGLRTGI 233
Cdd:TIGR03140 161 DEveALGIQGVPAVFLNGEEFHNGRMDLAELLEKLEETagvEAASALEQLDPYDVLVVGGGPAGAAAAIYAARKGLRTAM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 234 VADRIGGQVNDTAGIENFITVKQTTGSEFSSNLAAHIEEYDIDAMTGIRATKIEKTDKAIRVTLENDAVLESKTAIISTG 313
Cdd:TIGR03140 241 VAERIGGQVKDTVGIENLISVPYTTGSQLAANLEEHIKQYPIDLMENQRAKKIETEDGLIVVTLESGEVLKAKSVIVATG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 314 ASWRKLNIPGEDRLINKGVAFCPHCDGPLFENKNVAVIGGGNSGVEAAIDLAGIVKHVTLFEFAPELKADTVLQERLRSF 393
Cdd:TIGR03140 321 ARWRKLGVPGEKEYIGKGVAYCPHCDGPFFKGKDVAVIGGGNSGIEAAIDLAGIVRHVTVLEFADELKADKVLQDKLKSL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 394 PNVDIHTNARTAEVLGE-DHVTGLSYEDMSSGEMKELSLDGIFVQIGLVPNTKWIGDAVELNNRGEVVVDRENNTNVPGI 472
Cdd:TIGR03140 401 PNVDILTSAQTTEIVGDgDKVTGIRYQDRNSGEEKQLDLDGVFVQIGLVPNTEWLKDAVELNRRGEIVIDERGRTSVPGI 480
|
490 500 510
....*....|....*....|....*....|....*
gi 515743079 473 FAAGDVTDQKYKQIIISMGSGANAALSAFDYIIRN 507
Cdd:TIGR03140 481 FAAGDVTTVPYKQIIIAMGEGAKAALSAFDYLIRQ 515
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
206-504 |
1.06e-109 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 327.85 E-value: 1.06e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 206 YDVLIIGGGPASGSAAIYTARKGLRTGIV-ADRIGGQVNDTAGIENFITV-KQTTGSEFSSNLAAHIEEYDIDAMTGiRA 283
Cdd:COG0492 1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIeGGEPGGQLATTKEIENYPGFpEGISGPELAERLREQAERFGAEILLE-EV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 284 TKIEKTDKAIRVTLENDAVLESKTAIISTGASWRKLNIPGEDRLINKGVAFCPHCDGPLFENKNVAVIGGGNSGVEAAID 363
Cdd:COG0492 80 TSVDKDDGPFRVTTDDGTEYEAKAVIIATGAGPRKLGLPGEEEFEGRGVSYCATCDGFFFRGKDVVVVGGGDSALEEALY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 364 LAGIVKHVTLFEFAPELKADTVLQERLRSFPNVDIHTNARTAEVLGEDHVTGLSYEDMSSGEMKELSLDGIFVQIGLVPN 443
Cdd:COG0492 160 LTKFASKVTLIHRRDELRASKILVERLRANPKIEVLWNTEVTEIEGDGRVEGVTLKNVKTGEEKELEVDGVFVAIGLKPN 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515743079 444 TKWIGDA-VELNNRGEVVVDRENNTNVPGIFAAGDVTDQKYKQIIISMGSGANAALSAFDYI 504
Cdd:COG0492 240 TELLKGLgLELDEDGYIVVDEDMETSVPGVFAAGDVRDYKYRQAATAAGEGAIAALSAARYL 301
|
|
| AhpF |
COG3634 |
Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms]; |
17-193 |
8.10e-90 |
|
Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms];
Pssm-ID: 442851 [Multi-domain] Cd Length: 200 Bit Score: 273.16 E-value: 8.10e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 17 MEGDVEFRASIGSDDKSKELKDLLDEIAEMTDYITIVE---KELKRTPSFQVSKPEEDTGITFAGIPLGHEFNSLVLAIL 93
Cdd:COG3634 19 LKNPVELVLFLDDCEKSEELRELLEEIASLSDKISLEVydkDDVERAPSFAILRDGEDTGIRFAGIPSGHEFTSLVLALL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 94 QVSGRAPKEKQSIIDQIKGLEGNYNFETYVSLTCQKCPDVVQALNLMSVINPNITHTMIDGAVFREES--KDIMAVPAVF 171
Cdd:COG3634 99 QVSGHPPKLSEETIEQIKALDGPVHFEVFVSLSCPNCPDVVQALNLMAVLNPNITHEMIDGAEFPDEAekYGVMSVPTVV 178
|
170 180
....*....|....*....|..
gi 515743079 172 LDGEEFGNGRMTISDILSKLGS 193
Cdd:COG3634 179 LNGEVFFVGRMPEEEILEKLDT 200
|
|
| TRX_reduct |
TIGR01292 |
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ... |
207-504 |
6.36e-87 |
|
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: 269.50 E-value: 6.36e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 207 DVLIIGGGPASGSAAIYTARKGLRTGIVADRI-GGQVNDTAGIENFITVKQT-TGSEFSSNLAAHIEEYDidamTGIRAT 284
Cdd:TIGR01292 1 DVIIIGAGPAGLTAAIYAARANLKPLLIEGMEpGGQLTTTTEVENYPGFPEGiSGPELMEKMKEQAVKFG----AEIIYE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 285 KIEKTDKAIR---VTLENDAVLESKTAIISTGASWRKLNIPGEDRLINKGVAFCPHCDGPLFENKNVAVIGGGNSGVEAA 361
Cdd:TIGR01292 77 EVIKVDKSDRpfkVYTGDGKEYTAKAVIIATGASARKLGIPGEDEFWGRGVSYCATCDGPFFKNKEVAVVGGGDSAIEEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 362 IDLAGIVKHVTLFEFAPELKADTVLQERLRSFPNVDIHTNARTAEVLGEDHVTGLSYEDMSSGEMKELSLDGIFVQIGLV 441
Cdd:TIGR01292 157 LYLTRIAKKVTLVHRRDKFRAEKILLDRLKKNPKIEFLWNSTVEEIVGDNKVEGVKIKNTVTGEEEELEVDGVFIAIGHE 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515743079 442 PNTKWIGDAVELNNRGEVVVDRENNTNVPGIFAAGDVTDQKYKQIIISMGSGANAALSAFDYI 504
Cdd:TIGR01292 237 PNTELLKGLLELDENGYIVTDEGMRTSVPGVFAAGDVRDKGYRQAVTAAGDGCIAALSAERYL 299
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
206-493 |
3.55e-49 |
|
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: 170.96 E-value: 3.55e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 206 YDVLIIGGGPASGSAAIYTARKGLRTGIVADRiGGQVND----TAGIENFITVKQT--TGSEFSSNLAAHIEEY--DIDA 277
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDE-GTCPYGgcvlSKALLGAAEAPEIasLWADLYKRKEEVVKKLnnGIEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 278 MTGIRATKIEKTDKAIRVT---LENDAVLESKTAIISTGASWRKLNIPGEDRLINKGVAFCPHCDGPLFEN--KNVAVIG 352
Cdd:pfam07992 80 LLGTEVVSIDPGAKKVVLEelvDGDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKLlpKRVVVVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 353 GGNSGVEAAIDLAGIVKHVTLFEFAPEL------KADTVLQERLRSfPNVDIHTNARTAEVLGEDHvtGLSYEDmssGEM 426
Cdd:pfam07992 160 GGYIGVELAAALAKLGKEVTLIEALDRLlrafdeEISAALEKALEK-NGVEVRLGTSVKEIIGDGD--GVEVIL---KDG 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515743079 427 KELSLDGIFVQIGLVPNTKWIGDA-VELNNRGEVVVDRENNTNVPGIFAAGDVTDQKYKQIIISMGSG 493
Cdd:pfam07992 234 TEIDADLVVVAIGRRPNTELLEAAgLELDERGGIVVDEYLRTSVPGIYAAGDCRVGGPELAQNAVAQG 301
|
|
| AhpF_NTD_C |
cd03026 |
TRX-GRX-like family, Alkyl hydroperoxide reductase F subunit (AhpF) N-terminal domain (NTD) ... |
104-190 |
8.69e-47 |
|
TRX-GRX-like family, Alkyl hydroperoxide reductase F subunit (AhpF) N-terminal domain (NTD) subfamily, C-terminal TRX-fold subdomain; AhpF is a homodimeric flavoenzyme which catalyzes the NADH-dependent reduction of the peroxiredoxin AhpC, which then reduces hydrogen peroxide and organic hydroperoxides. AhpF contains an NTD containing two contiguous TRX-fold subdomains similar to Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO). It also contains a catalytic core similar to TRX reductase containing FAD and NADH binding domains with an active site disulfide. The proposed mechanism of action of AhpF is similar to a TRX/TRX reductase system. The flow of reducing equivalents goes from NADH -> catalytic core of AhpF -> NTD of AhpF -> AhpC -> peroxide substrates. The catalytic CXXC motif of the NTD of AhpF is contained in its C-terminal TRX subdomain.
Pssm-ID: 239324 [Multi-domain] Cd Length: 89 Bit Score: 157.46 E-value: 8.69e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 104 QSIIDQIKGLEGNYNFETYVSLTCQKCPDVVQALNLMSVINPNITHTMIDGAVFREE--SKDIMAVPAVFLDGEEFGNGR 181
Cdd:cd03026 1 EDLLEQIRRLNGPINFETYVSLSCHNCPDVVQALNLMAVLNPNIEHEMIDGALFQDEveERGIMSVPAIFLNGELFGFGR 80
|
....*....
gi 515743079 182 MTISDILSK 190
Cdd:cd03026 81 MTLEEILAK 89
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
208-504 |
2.40e-40 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 147.90 E-value: 2.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 208 VLIIGGGPASGSAAIYTARKGLRTGIVAD-RIGGQVNDTAGIENFI-TVKQTTGSEFSSNLAAHIEEYDIDAMTGiRATK 285
Cdd:PRK10262 9 LLILGSGPAGYTAAVYAARANLQPVLITGmEKGGQLTTTTEVENWPgDPNDLTGPLLMERMHEHATKFETEIIFD-HINK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 286 IEKTDKAIRVTlENDAVLESKTAIISTGASWRKLNIPGEDRLINKGVAFCPHCDGPLFENKNVAVIGGGNSGVEAAIDLA 365
Cdd:PRK10262 88 VDLQNRPFRLT-GDSGEYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEALYLS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 366 GIVKHVTLFEFAPELKADTVLQERLR---SFPNVDIHTNARTAEVLGEDH-VTGLSYEDMSSGE-MKELSLDGIFVQIGL 440
Cdd:PRK10262 167 NIASEVHLIHRRDGFRAEKILIKRLMdkvENGNIILHTNRTLEEVTGDQMgVTGVRLRDTQNSDnIESLDVAGLFVAIGH 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515743079 441 VPNTKWIGDAVELNNrGEVVVD-----RENNTNVPGIFAAGDVTDQKYKQIIISMGSGANAALSAFDYI 504
Cdd:PRK10262 247 SPNTAIFEGQLELEN-GYIKVQsgihgNATQTSIPGVFAAGDVMDHIYRQAITSAGTGCMAALDAERYL 314
|
|
| AhpF_NTD_N |
cd02974 |
Alkyl hydroperoxide reductase F subunit (AhpF) N-terminal domain (NTD) family, N-terminal ... |
1-93 |
1.36e-30 |
|
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: 114.21 E-value: 1.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 1 MLNADLKQQLQQLLQLMEGDVEFRASIGSDDKSKELKDLLDEIAEMTDYITIVEKELK-RTPSFQVSKPEEDTGITFAGI 79
Cdd:cd02974 1 MLDANLKQQLKAYLERLENPVELVASLDDSEKSAELLELLEEIASLSDKITLEEDNDDeRKPSFSINRPGEDTGIRFAGI 80
|
90
....*....|....
gi 515743079 80 PLGHEFNSLVLAIL 93
Cdd:cd02974 81 PMGHEFTSLVLALL 94
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
205-479 |
2.99e-28 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 116.01 E-value: 2.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 205 PYDVLIIGGGPASGSAAiytarKGLRtgivadRIGGQVNdtagienfITV-------------------KQTTGSEFSSN 265
Cdd:COG1251 1 KMRIVIIGAGMAGVRAA-----EELR------KLDPDGE--------ITVigaephppynrpplskvlaGETDEEDLLLR 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 266 LAAHIEEYDIDAMTGIRATKIEKTDKaiRVTLENDAVLESKTAIISTGASWRKLNIPGEDRlinKGV----------AFC 335
Cdd:COG1251 62 PADFYEENGIDLRLGTRVTAIDRAAR--TVTLADGETLPYDKLVLATGSRPRVPPIPGADL---PGVftlrtlddadALR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 336 PHCDGPlfenKNVAVIGGGNSGVEAAIDLAGIVKHVTLFEFAPEL-------KADTVLQERLRSFpNVDIHTNARTAEVL 408
Cdd:COG1251 137 AALAPG----KRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLlprqldeEAGALLQRLLEAL-GVEVRLGTGVTEIE 211
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515743079 409 GEDHVTGLSyedMSSGEmkELSLDGIFVQIGLVPNTKWIGDA-VELnNRGeVVVDRENNTNVPGIFAAGDVT 479
Cdd:COG1251 212 GDDRVTGVR---LADGE--ELPADLVVVAIGVRPNTELARAAgLAV-DRG-IVVDDYLRTSDPDIYAAGDCA 276
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
206-481 |
1.51e-27 |
|
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: 114.80 E-value: 1.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 206 YDVLIIGGGPASGSAAIYTARKGLRTGIV-ADRIGG---------------------QVNDTA--GIE-NFITV------ 254
Cdd:COG1249 4 YDLVVIGAGPGGYVAAIRAAQLGLKVALVeKGRLGGtclnvgcipskallhaaevahEARHAAefGISaGAPSVdwaalm 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 255 --KQTTGSEFSSNLAAHIEEYDIDAMTGiRATKIEKTdkaiRVTLENDAVLESKTAIISTGASWRKLNIPG--EDRLINk 330
Cdd:COG1249 84 arKDKVVDRLRGGVEELLKKNGVDVIRG-RARFVDPH----TVEVTGGETLTADHIVIATGSRPRVPPIPGldEVRVLT- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 331 gvafcphCDGpLFEN----KNVAVIGGGNSGVEAAIDLAGIVKHVTLFEFAPEL--KAD----TVLQERLRSfPNVDIHT 400
Cdd:COG1249 158 -------SDE-ALELeelpKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLlpGEDpeisEALEKALEK-EGIDILT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 401 NARTAEV-LGEDHVTgLSYEDmsSGEMKELSLDGIFVQIGLVPNTKWIG-DA--VELNNRGEVVVDRENNTNVPGIFAAG 476
Cdd:COG1249 229 GAKVTSVeKTGDGVT-VTLED--GGGEEAVEADKVLVATGRRPNTDGLGlEAagVELDERGGIKVDEYLRTSVPGIYAIG 305
|
....*
gi 515743079 477 DVTDQ 481
Cdd:COG1249 306 DVTGG 310
|
|
| TRX_GRX_like |
cd02973 |
Thioredoxin (TRX)-Glutaredoxin (GRX)-like family; composed of archaeal and bacterial proteins ... |
117-181 |
2.18e-27 |
|
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: 104.57 E-value: 2.18e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515743079 117 YNFETYVSLTCQKCPDVVQALNLMSVINPNITHTMIDGAVFREESK--DIMAVPAVFLDGEEFGNGR 181
Cdd:cd02973 1 VNIEVFVSPTCPYCPDAVQAANRIAALNPNISAEMIDAAEFPDLADeyGVMSVPAIVINGKVEFVGR 67
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
208-499 |
2.54e-26 |
|
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: 110.99 E-value: 2.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 208 VLIIGGGPASGSAAIYTARKGLRtgiV-----ADRIGGQVndTAGIENFITVKqttgsefssnlaaHIEEYDIDAMT--G 280
Cdd:COG0493 124 VAVVGSGPAGLAAAYQLARAGHE---VtvfeaLDKPGGLL--RYGIPEFRLPK-------------DVLDREIELIEalG 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 281 IRA---TKIEKTdkairVTLEN-----DAVlesktaIISTGAS-WRKLNIPGED-----------RLINKGVAFcphcDG 340
Cdd:COG0493 186 VEFrtnVEVGKD-----ITLDElleefDAV------FLATGAGkPRDLGIPGEDlkgvhsamdflTAVNLGEAP----DT 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 341 PLFENKNVAVIGGGNSgveaAIDLAGI-----VKHVTLFEFAPE-------LKADTVLQErlrsfpNVDIHTNARTAEVL 408
Cdd:COG0493 251 ILAVGKRVVVIGGGNT----AMDCARTalrlgAESVTIVYRRTReempaskEEVEEALEE------GVEFLFLVAPVEII 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 409 GED--HVTGLSYEDM---------------SSGEMKELSLDGIFVQIGLVPNTKWIGDA--VELNNRGEVVVDREN-NTN 468
Cdd:COG0493 321 GDEngRVTGLECVRMelgepdesgrrrpvpIEGSEFTLPADLVILAIGQTPDPSGLEEElgLELDKRGTIVVDEETyQTS 400
|
330 340 350
....*....|....*....|....*....|..
gi 515743079 469 VPGIFAAGD-VTDQkyKQIIISMGSGANAALS 499
Cdd:COG0493 401 LPGVFAGGDaVRGP--SLVVWAIAEGRKAARA 430
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
267-495 |
5.23e-25 |
|
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: 105.28 E-value: 5.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 267 AAHIEEYDIDAMTGIRATKIEKTDKaiRVTLENDAVLESKTAIISTGASWRKLNIPGEDrliNKGVAFCPHCDGPL---- 342
Cdd:COG0446 43 PESFERKGIDVRTGTEVTAIDPEAK--TVTLRDGETLSYDKLVLATGARPRPPPIPGLD---LPGVFTLRTLDDADalre 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 343 ----FENKNVAVIGGGNSGVEAAIDLAGIVKHVTLFEFAPEL--KAD----TVLQERLRSFpNVDIHTNARTAEVLGEDH 412
Cdd:COG0446 118 alkeFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLlgVLDpemaALLEEELREH-GVELRLGETVVAIDGDDK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 413 VTGLSyedmSSGEmkELSLDGIFVQIGLVPNTKWIGDA-VELNNRGEVVVDRENNTNVPGIFAAGDVTDQKY----KQII 487
Cdd:COG0446 197 VAVTL----TDGE--EIPADLVVVAPGVRPNTELAKDAgLALGERGWIKVDETLQTSDPDVYAAGDCAEVPHpvtgKTVY 270
|
....*...
gi 515743079 488 ISMGSGAN 495
Cdd:COG0446 271 IPLASAAN 278
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
206-503 |
8.62e-22 |
|
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide.
Pssm-ID: 273568 [Multi-domain] Cd Length: 460 Bit Score: 98.10 E-value: 8.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 206 YDVLIIGGGPASGSAAIYTARKGLRTGIV-ADRIGG-----------------QVNDTA------GIE------NFITV- 254
Cdd:TIGR01350 2 YDVIVIGGGPGGYVAAIRAAQLGLKVALVeKEYLGGtclnvgciptkallhsaEVYDEIkhakdlGIEvenvsvDWEKMq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 255 --KQTTGSEFSSNLAAHIEEYDIDAMTGIraTKIEKtDKAIRVTLENDA-VLESKTAIISTGASWRKLNIP---GEDRLI 328
Cdd:TIGR01350 82 krKNKVVKKLVGGVSGLLKKNKVTVIKGE--AKFLD-PGTVSVTGENGEeTLEAKNIIIATGSRPRSLPGPfdfDGKVVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 329 NKGVAFcphcdgPLFEN-KNVAVIGGGNSGVEAAIDLAGIVKHVTLFEFAPELKADT------VLQERLRSfPNVDIHTN 401
Cdd:TIGR01350 159 TSTGAL------NLEEVpESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRILPGEdaevskVLQKALKK-KGVKILTN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 402 ARTAEVLGEDhvTGLSYEdMSSGEMKELSLDGIFVQIGLVPNTKWIGDA---VELNNRGEVVVDRENNTNVPGIFAAGDV 478
Cdd:TIGR01350 232 TKVTAVEKND--DQVTYE-NKGGETETLTGEKVLVAVGRKPNTEGLGLEklgVELDERGRIVVDEYMRTNVPGIYAIGDV 308
|
330 340 350
....*....|....*....|....*....|.
gi 515743079 479 TDQK------YKQIIISMGSGANAALSAFDY 503
Cdd:TIGR01350 309 IGGPmlahvaSHEGIVAAENIAGKEPAHIDY 339
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
208-479 |
1.51e-20 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 94.09 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 208 VLIIGGGPASGSAAIYTARKGLRTGI--VADRIGGqVNdTAGIENFITVKqttgsEFSSNLAAHIEEYDIDAMTGiraTK 285
Cdd:PRK11749 143 VAVIGAGPAGLTAAHRLARKGYDVTIfeARDKAGG-LL-RYGIPEFRLPK-----DIVDREVERLLKLGVEIRTN---TE 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 286 IEKTdkairVTLE-----NDAVLesktaiISTGAS-WRKLNIPGEDRlinKGVAFC---------PHCDGPLFENKNVAV 350
Cdd:PRK11749 213 VGRD-----ITLDelragYDAVF------IGTGAGlPRFLGIPGENL---GGVYSAvdfltrvnqAVADYDLPVGKRVVV 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 351 IGGGNSgveaAIDLAGI-----VKHVTL---------------FEFAPELkadtvlqerlrsfpNVDIHTNARTAEVLGE 410
Cdd:PRK11749 279 IGGGNT----AMDAARTakrlgAESVTIvyrrgreempaseeeVEHAKEE--------------GVEFEWLAAPVEILGD 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 411 DH-VTGLSYEDMSSGEMKE--------------LSLDGIFVQIGLVPNTK--WIGDAVELNNRGEVVVDREN-NTNVPGI 472
Cdd:PRK11749 341 EGrVTGVEFVRMELGEPDAsgrrrvpiegseftLPADLVIKAIGQTPNPLilSTTPGLELNRWGTIIADDETgRTSLPGV 420
|
....*..
gi 515743079 473 FAAGDVT 479
Cdd:PRK11749 421 FAGGDIV 427
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
206-479 |
2.30e-19 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 90.76 E-value: 2.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 206 YDVLIIGGGPASGSAAIYTARKGLRTGIV--------ADRIGGQVNDT---------AGIENF-----------ITVKqt 257
Cdd:PRK06327 5 FDVVVIGAGPGGYVAAIRAAQLGLKVACIeawknpkgKPALGGTCLNVgcipskallASSEEFenaghhfadhgIHVD-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 258 tgsEFSSNLAAHIEEYD--IDAMTG-----IRATKI----------EKTDKA--IRVTLENDAVLESKTAIISTGASWRK 318
Cdd:PRK06327 83 ---GVKIDVAKMIARKDkvVKKMTGgieglFKKNKItvlkgrgsfvGKTDAGyeIKVTGEDETVITAKHVIIATGSEPRH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 319 L-NIPGEDRLInkgvafcpHC-DGPL-FEN--KNVAVIGGGNSGVEAAIDLAGIVKHVTLFEFAPELKA---DTVLQERL 390
Cdd:PRK06327 160 LpGVPFDNKII--------LDnTGALnFTEvpKKLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFLAaadEQVAKEAA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 391 RSFPN--VDIHTNARTAEV-LGEDHVTgLSYEDmSSGEMKELSLDGIFVQIGLVPNTKWIG-DAV--ELNNRGEVVVDRE 464
Cdd:PRK06327 232 KAFTKqgLDIHLGVKIGEIkTGGKGVS-VAYTD-ADGEAQTLEVDKLIVSIGRVPNTDGLGlEAVglKLDERGFIPVDDH 309
|
330
....*....|....*
gi 515743079 465 NNTNVPGIFAAGDVT 479
Cdd:PRK06327 310 CRTNVPNVYAIGDVV 324
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
206-479 |
2.40e-18 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 87.54 E-value: 2.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 206 YDVLIIGGGPASGSAAIYTARKGLRTGIV--------------------------------ADRIGGQVnDTAGIeNFIT 253
Cdd:PRK06292 4 YDVIVIGAGPAGYVAARRAAKLGKKVALIekgplggtclnvgcipskaliaaaeafheakhAEEFGIHA-DGPKI-DFKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 254 V---KQTTGSEFSSnlaaHIEEY--DIDAMTGIRATKIEKTDKAIRVtleNDAVLESKTAIISTGAswRKLNIPG----- 323
Cdd:PRK06292 82 VmarVRRERDRFVG----GVVEGleKKPKIDKIKGTARFVDPNTVEV---NGERIEAKNIVIATGS--RVPPIPGvwlil 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 324 EDRLI-NKGVAFCPHCdgPlfenKNVAVIGGGNSGVEAAIDLAGIVKHVTLFEFAPELKA--DTVLQERL-RSFP-NVDI 398
Cdd:PRK06292 153 GDRLLtSDDAFELDKL--P----KSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPleDPEVSKQAqKILSkEFKI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 399 HTNARTAEVLGEDHVTGLSYEDmsSGEMKELSLDGIFVQIGLVPNTKWIGDA---VELNNRGEVVVDRENNTNVPGIFAA 475
Cdd:PRK06292 227 KLGAKVTSVEKSGDEKVEELEK--GGKTETIEADYVLVATGRRPNTDGLGLEntgIELDERGRPVVDEHTQTSVPGIYAA 304
|
....
gi 515743079 476 GDVT 479
Cdd:PRK06292 305 GDVN 308
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
206-479 |
2.14e-17 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 84.43 E-value: 2.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 206 YDVLIIGGGPASGSAAIYTARKGLRTGIV-ADRIGG-----------------QVNDTA------GIEN-FITVKQTTGS 260
Cdd:PRK06416 5 YDVIVIGAGPGGYVAAIRAAQLGLKVAIVeKEKLGGtclnrgcipskallhaaERADEArhsedfGIKAeNVGIDFKKVQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 261 EFSSNLAAHI--------EEYDIDAMTGirATKIEKTDKaIRVTLENDA-VLESKTAIISTGASWRKL-NIPGEDRLI-- 328
Cdd:PRK06416 85 EWKNGVVNRLtggvegllKKNKVDIIRG--EAKLVDPNT-VRVMTEDGEqTYTAKNIILATGSRPRELpGIEIDGRVIwt 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 329 NKGVAFCPHCdgPlfenKNVAVIGGGNSGVEAAIDLAGIVKHVTLFEFAPELKA--D----TVLQERLRSfPNVDIHTNA 402
Cdd:PRK06416 162 SDEALNLDEV--P----KSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILPgeDkeisKLAERALKK-RGIKIKTGA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 403 RTAEVL-GEDHVTgLSYEDmsSGEMKELSLDGIFVQIGLVPNTKWIGDA---VELNnRGEVVVDRENNTNVPGIFAAGDV 478
Cdd:PRK06416 235 KAKKVEqTDDGVT-VTLED--GGKEETLEADYVLVAVGRRPNTENLGLEelgVKTD-RGFIEVDEQLRTNVPNIYAIGDI 310
|
.
gi 515743079 479 T 479
Cdd:PRK06416 311 V 311
|
|
| GlrX_arch |
TIGR02187 |
Glutaredoxin-like domain protein; This family of archaeal proteins contains a C-terminal ... |
17-177 |
2.74e-17 |
|
Glutaredoxin-like domain protein; This family of archaeal proteins contains a C-terminal domain with homology to bacterial and eukaryotic glutaredoxins, including a CPYC motif. There is an N-terminal domain which has even more distant homology to glutaredoxins. The name "glutaredoxin" may be inappropriate in the sense of working in tandem with glutathione and glutathione reductase which may not be present in the archaea. The overall domain structure appears to be related to bacterial alkylhydroperoxide reductases, but the homology may be distant enough that the function of this family is wholly different.
Pssm-ID: 274021 [Multi-domain] Cd Length: 215 Bit Score: 80.57 E-value: 2.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 17 MEGDVEFRASIGSDDKS----KELKDLLDEIAEMTDYI--------TIVEKEL------KRTPSFQVSKPEEDTGITFAG 78
Cdd:TIGR02187 17 LKNPVEIVVFTDNDKEGcqycKETEQLLEELSEVSPKLkleiydfdTPEDKEEaekygvERVPTTIILEEGKDGGIRYTG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 79 IPLGHEFNSLVLAILQVSGRAPKEKQSIIDQIKGLEGNYNFETYVSLTCQKCPDVVQALNLMSVINPNITHTMIDGAVFR 158
Cdd:TIGR02187 97 IPAGYEFAALIEDIVRVSQGEPGLSEKTVELLQSLDEPVRIEVFVTPTCPYCPYAVLMAHKFALANDKILGEMIEANENP 176
|
170 180
....*....|....*....|...
gi 515743079 159 EESKD--IMAVPAVFL--DGEEF 177
Cdd:TIGR02187 177 DLAEKygVMSVPKIVInkGVEEF 199
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
204-484 |
2.62e-16 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 81.02 E-value: 2.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 204 DPYDVLIIGGGPASGSAAIYTARKGLRTGIVA-DRIGGQ-----------------------------VNDTAGIE-NFI 252
Cdd:PRK06370 4 QRYDAIVIGAGQAGPPLAARAAGLGMKVALIErGLLGGTcvntgcvptktliasaraahlarraaeygVSVGGPVSvDFK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 253 TV---KQTTGSEFSSNLAAHIEEYDidAMTGIRATKIEKTDKAIRVtleNDAVLESKTAIISTGASWRKLNIPGEDR--- 326
Cdd:PRK06370 84 AVmarKRRIRARSRHGSEQWLRGLE--GVDVFRGHARFESPNTVRV---GGETLRAKRIFINTGARAAIPPIPGLDEvgy 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 327 LINKGV---AFCPhcdgplfenKNVAVIGGGNSGVEAAIDLAGIVKHVTLFEFAPEL------KADTVLQERLRSfPNVD 397
Cdd:PRK06370 159 LTNETIfslDELP---------EHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLlpredeDVAAAVREILER-EGID 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 398 IHTNARTAEVlgEDHVTGLSYEDMSSGEMKELSLDGIFVQIGLVPNTKWIG-DA--VELNNRGEVVVDRENNTNVPGIFA 474
Cdd:PRK06370 229 VRLNAECIRV--ERDGDGIAVGLDCNGGAPEITGSHILVAVGRVPNTDDLGlEAagVETDARGYIKVDDQLRTTNPGIYA 306
|
330
....*....|
gi 515743079 475 AGDVtDQKYK 484
Cdd:PRK06370 307 AGDC-NGRGA 315
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
208-497 |
7.28e-16 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 78.88 E-value: 7.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 208 VLIIGGGPASGSAAIYTARKG---------------LRTGIVADRI-------GGQVNDTAGIENFITVKQTTGSEFSSN 265
Cdd:PRK12770 21 VAIIGAGPAGLAAAGYLACLGyevhvydklpepgglMLFGIPEFRIpiervreGVKELEEAGVVFHTRTKVCCGEPLHEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 266 LAAHIEEYDIDamtgiratkIEKTDKairvtlENDAVLesktaiISTGaSW--RKLNIPGEDRlinKGV----------- 332
Cdd:PRK12770 101 EGDEFVERIVS---------LEELVK------KYDAVL------IATG-TWksRKLGIPGEDL---PGVysaleylfrir 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 333 ----AFCPHCDGPLFENKNVAVIGGGNSGVEAAID--LAGiVKHVTLF-----EFAPELKAD-TVLQERlrsfpNVDIHT 400
Cdd:PRK12770 156 aaklGYLPWEKVPPVEGKKVVVVGAGLTAVDAALEavLLG-AEKVYLAyrrtiNEAPAGKYEiERLIAR-----GVEFLE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 401 NARTAEVLGEDHVTGLSYEDMSSGEMKE---------------LSLDGIFVQIGLVP----NTKWIGdaVELNNRGEVVV 461
Cdd:PRK12770 230 LVTPVRIIGEGRVEGVELAKMRLGEPDEsgrprpvpipgsefvLEADTVVFAIGEIPtppfAKECLG--IELNRKGEIVV 307
|
330 340 350
....*....|....*....|....*....|....*.
gi 515743079 462 DRENNTNVPGIFAAGDVTDQKYKqIIISMGSGANAA 497
Cdd:PRK12770 308 DEKHMTSREGVFAAGDVVTGPSK-IGKAIKSGLRAA 342
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
344-495 |
2.01e-15 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 78.54 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 344 ENKNVAVIGGGNSGVEAAIDLAGIVKHVTLFE---------FAPELKAdtVLQERLRSfPNVDIHTNARTAEVLGEDHVT 414
Cdd:PRK09564 148 EIKNIVIIGAGFIGLEAVEAAKHLGKNVRIIQledrilpdsFDKEITD--VMEEELRE-NGVELHLNEFVKSLIGEDKVE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 415 GLSYEDmssgemKELSLDGIFVQIGLVPNTKWIGDA-VELNNRGEVVVDRENNTNVPGIFAAGD-------VTDqkyKQI 486
Cdd:PRK09564 225 GVVTDK------GEYEADVVIVATGVKPNTEFLEDTgLKTLKNGAIIVDEYGETSIENIYAAGDcatiyniVSN---KNV 295
|
....*....
gi 515743079 487 IISMGSGAN 495
Cdd:PRK09564 296 YVPLATTAN 304
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
309-480 |
3.29e-15 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 77.89 E-value: 3.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 309 IISTGASWRKLNIPGEDRLINKGVAF----CPhcdgplfenKNVAVIGGGNSGVEaaidLAGIVK----HVTLF------ 374
Cdd:PRK06116 136 LIATGGRPSIPDIPGAEYGITSDGFFaleeLP---------KRVAVVGAGYIAVE----FAGVLNglgsETHLFvrgdap 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 375 --EFAPELKaDTVLQERLRSfpNVDIHTNARTAEV-LGEDHVTGLSYEDmssGEmkELSLDGIFVQIGLVPNTKWIG--- 448
Cdd:PRK06116 203 lrGFDPDIR-ETLVEEMEKK--GIRLHTNAVPKAVeKNADGSLTLTLED---GE--TLTVDCLIWAIGREPNTDGLGlen 274
|
170 180 190
....*....|....*....|....*....|..
gi 515743079 449 DAVELNNRGEVVVDRENNTNVPGIFAAGDVTD 480
Cdd:PRK06116 275 AGVKLNEKGYIIVDEYQNTNVPGIYAVGDVTG 306
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
289-479 |
1.40e-14 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 75.56 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 289 TDKAIRVTLENDAV-LESKTAIISTGASWRKLNIPGEDRLIN----KGVAFCPHcdgplfENKNVAVIGGGNSGVEAAID 363
Cdd:PRK07251 102 SNKVIEVQAGDEKIeLTAETIVINTGAVSNVLPIPGLADSKHvydsTGIQSLET------LPERLGIIGGGNIGLEFAGL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 364 LAGIVKHVTLFEFAPEL--KADTVLQERLRSF---PNVDIHTNARTAEVLGEDHVTGLSYEDmssgemKELSLDGIFVQI 438
Cdd:PRK07251 176 YNKLGSKVTVLDAASTIlpREEPSVAALAKQYmeeDGITFLLNAHTTEVKNDGDQVLVVTED------ETYRFDALLYAT 249
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 515743079 439 GLVPNTKWIG---DAVELNNRGEVVVDRENNTNVPGIFAAGDVT 479
Cdd:PRK07251 250 GRKPNTEPLGlenTDIELTERGAIKVDDYCQTSVPGVFAVGDVN 293
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
208-477 |
1.47e-13 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 72.50 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 208 VLIIGGGPASGSAAIYTARKGLRtgiV-----ADRIGGQVndTAGIENFITVKQttgsefssnlaaHIEEyDIDAMT--G 280
Cdd:PRK12810 146 VAVVGSGPAGLAAADQLARAGHK---VtvferADRIGGLL--RYGIPDFKLEKE------------VIDR-RIELMEaeG 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 281 IR---ATKIEKTDKAIRVTLENDAVlesktaIISTGAS-WRKLNIPGEDR---------LI--NKGVAFCPHCDGPLFEN 345
Cdd:PRK12810 208 IEfrtNVEVGKDITAEELLAEYDAV------FLGTGAYkPRDLGIPGRDLdgvhfamdfLIqnTRRVLGDETEPFISAKG 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 346 KNVAVIGGGNSGVEA---AIDL-AgivKHVTLFEFAPELKADTVLQERLRSFPN-----------VDIHTNARTAEVLGE 410
Cdd:PRK12810 282 KHVVVIGGGDTGMDCvgtAIRQgA---KSVTQRDIMPMPPSRRNKNNPWPYWPMklevsnaheegVEREFNVQTKEFEGE 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 411 D-HVTGL--SYEDMSSGEMKE-------LSLDGIFVQIGLV-PNTKWIGD-AVELNNRGEVVVDREN-NTNVPGIFAAGD 477
Cdd:PRK12810 359 NgKVTGVkvVRTELGEGDFEPvegsefvLPADLVLLAMGFTgPEAGLLAQfGVELDERGRVAAPDNAyQTSNPKVFAAGD 438
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
258-476 |
2.37e-13 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 70.72 E-value: 2.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 258 TGSEFSSNLAAHIEEYDIDAMTGIRATKIEKTDKAIRVTLENDaVLESKTAIISTG--ASWRKLNIPGedrlinkgvaFC 335
Cdd:pfam13738 73 SGNEYAEYLRRVADHFELPINLFEEVTSVKKEDDGFVVTTSKG-TYQARYVIIATGefDFPNKLGVPE----------LP 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 336 PHC----DGPLFENKNVAVIGGGNSGVEAAIDLAGIVKHVTLF-----------EFAPELKADTvlQERLRSFPN---VD 397
Cdd:pfam13738 142 KHYsyvkDFHPYAGQKVVVIGGYNSAVDAALELVRKGARVTVLyrgsewedrdsDPSYSLSPDT--LNRLEELVKngkIK 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 398 IHTNARTAEVLGEDHVTGLSYEDmssgeMKELSLDGIFV-QIGLVPNTKWIGDAV-ELNNRGEVVVDRENN-TNVPGIFA 474
Cdd:pfam13738 220 AHFNAEVKEITEVDVSYKVHTED-----GRKVTSNDDPIlATGYHPDLSFLKKGLfELDEDGRPVLTEETEsTNVPGLFL 294
|
..
gi 515743079 475 AG 476
Cdd:pfam13738 295 AG 296
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
206-374 |
3.02e-13 |
|
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: 71.43 E-value: 3.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 206 YDVLIIGGGPAsG-SAAIYTARKGLRTGIV--ADRIGG--QVND----TAGIENFI---------TVKQT--TGSEFSSN 265
Cdd:COG2072 7 VDVVVIGAGQA-GlAAAYHLRRAGIDFVVLekADDVGGtwRDNRypglRLDTPSHLyslpffpnwSDDPDfpTGDEILAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 266 LAAHIEEYDI--DAMTGIRATKIE--KTDKAIRVTLENDAVLESKTAIISTGASWRKL--NIPGEDRliNKGVAFcpHC- 338
Cdd:COG2072 86 LEAYADKFGLrrPIRFGTEVTSARwdEADGRWTVTTDDGETLTARFVVVATGPLSRPKipDIPGLED--FAGEQL--HSa 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 515743079 339 --DGPL-FENKNVAVIGGGNSGVEAAIDLAGIVKHVTLF 374
Cdd:COG2072 162 dwRNPVdLAGKRVLVVGTGASAVQIAPELARVAAHVTVF 200
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
208-499 |
7.72e-12 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 67.59 E-value: 7.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 208 VLIIGGGPASGSAAIYTARKGLRTGI--VADRIGGQVNdtAGIENFITVKQTTGSEFSSNLAAHIE-EYDIDAMTGIRAT 284
Cdd:PRK12771 140 VAVIGGGPAGLSAAYHLRRMGHAVTIfeAGPKLGGMMR--YGIPAYRLPREVLDAEIQRILDLGVEvRLGVRVGEDITLE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 285 KIEKtdkairvtlENDAVLesktaiISTGA-SWRKLNIPGED--RLINkGVAFCpHC---DGPLFENKNVAVIGGGNSgv 358
Cdd:PRK12771 218 QLEG---------EFDAVF------VAIGAqLGKRLPIPGEDaaGVLD-AVDFL-RAvgeGEPPFLGKRVVVIGGGNT-- 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 359 eaAIDLAGIvkhvtlfefAPELKADTVL------QERLRSFPN---------VDIHTNARTAEVL-GEDHVTGLSYEDMs 422
Cdd:PRK12771 279 --AMDAART---------ARRLGAEEVTivyrrtREDMPAHDEeieealregVEINWLRTPVEIEgDENGATGLRVITV- 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 423 sgEMKELSLDGifvqiGLVPNTK------------WIGDAVEL----------NNRGEVVVDRENN-TNVPGIFAAGD-V 478
Cdd:PRK12771 347 --EKMELDEDG-----RPSPVTGeeetleadlvvlAIGQDIDSaglesvpgveVGRGVVQVDPNFMmTGRPGVFAGGDmV 419
|
330 340
....*....|....*....|.
gi 515743079 479 TDQkyKQIIISMGSGANAALS 499
Cdd:PRK12771 420 PGP--RTVTTAIGHGKKAARN 438
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
299-481 |
9.48e-12 |
|
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: 66.92 E-value: 9.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 299 NDAVLESKTA---IISTGASWRKLNIPGEDRLINKGVAFcpHCDGPlfeNKNVAVIGGGNSGVEAA------------ID 363
Cdd:TIGR01423 143 KSAVKERLQAehiLLATGSWPQMLGIPGIEHCISSNEAF--YLDEP---PRRVLTVGGGFISVEFAgifnaykprggkVT 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 364 LAgIVKHVTLFEFAPELKADtvLQERLRSfPNVDIHTNARTAEVL----GEDHVTglsyedMSSGemKELSLDGIFVQIG 439
Cdd:TIGR01423 218 LC-YRNNMILRGFDSTLRKE--LTKQLRA-NGINIMTNENPAKVTlnadGSKHVT------FESG--KTLDVDVVMMAIG 285
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 515743079 440 LVPNTKWI---GDAVELNNRGEVVVDRENNTNVPGIFAAGDVTDQ 481
Cdd:TIGR01423 286 RVPRTQTLqldKVGVELTKKGAIQVDEFSRTNVPNIYAIGDVTDR 330
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
271-478 |
8.35e-11 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 64.46 E-value: 8.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 271 EEYDIDAMTGIRATKIEKTDKAirVTLENDAVLESKTAIISTGASWRKLNIPGEDRlinKGV-AFCPHCDGPLFEN---- 345
Cdd:TIGR02374 65 EKHGITLYTGETVIQIDTDQKQ--VITDAGRTLSYDKLILATGSYPFILPIPGADK---KGVyVFRTIEDLDAIMAmaqr 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 346 -KNVAVIGGGNSGVEAAIDLAGIVKHVTLFEFAPELKADTV-------LQERLRSFpNVDIHTNARTAEVLGEDHVTGLS 417
Cdd:TIGR02374 140 fKKAAVIGGGLLGLEAAVGLQNLGMDVSVIHHAPGLMAKQLdqtagrlLQRELEQK-GLTFLLEKDTVEIVGATKADRIR 218
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515743079 418 YEDMSSgemkeLSLDGIFVQIGLVPNTKwIGDAVELNNRGEVVVDRENNTNVPGIFAAGDV 478
Cdd:TIGR02374 219 FKDGSS-----LEADLIVMAAGIRPNDE-LAVSAGIKVNRGIIVNDSMQTSDPDIYAVGEC 273
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
347-420 |
1.20e-10 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 425450 [Multi-domain] Cd Length: 80 Bit Score: 57.60 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 347 NVAVIGGGNSGVEAAIDLAGIVKHVTLFEFAPELK------ADTVLQERLRSFpNVDIHTNARTAEVLGEDHVTGLSYED 420
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLpgfdpeIAKILQEKLEKN-GIEFLLNTTVEAIEGNGDGVVVVLTD 79
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
265-478 |
1.41e-10 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 62.84 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 265 NLAAHIEEYDIDAMTGiRATKIEKTDKaiRVTLENDAVLESKTAIISTGASWRKLNIPGedrLINKGVAFCPHCDGPLFE 344
Cdd:COG1252 61 PLRELLRRAGVRFIQG-EVTGIDPEAR--TVTLADGRTLSYDYLVIATGSVTNFFGIPG---LAEHALPLKTLEDALALR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 345 NK--------------NVAVIGGGNSGVEAAIDLAGIVKH-------------VTLFEFAPEL------KADTVLQERLR 391
Cdd:COG1252 135 ERllaaferaerrrllTIVVVGGGPTGVELAGELAELLRKllrypgidpdkvrITLVEAGPRIlpglgeKLSEAAEKELE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 392 SFpNVDIHTNARTAEVlGEDHVTglsyedMSSGEmkELSLDGIFVQIGLVPNtKWIGDA-VELNNRGEVVVDREN-NTNV 469
Cdd:COG1252 215 KR-GVEVHTGTRVTEV-DADGVT------LEDGE--EIPADTVIWAAGVKAP-PLLADLgLPTDRRGRVLVDPTLqVPGH 283
|
....*....
gi 515743079 470 PGIFAAGDV 478
Cdd:COG1252 284 PNVFAIGDC 292
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
201-481 |
1.44e-10 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 63.63 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 201 EDKDPYDVLIIGGGPASGSAAIYTARKGLR-TGIVADRIGGQVNDTAGIENFITVK------QTTGSEFSSNLAAHIEEY 273
Cdd:PRK13748 94 GNERPLHVAVIGSGGAAMAAALKAVEQGARvTLIERGTIGGTCVNVGCVPSKIMIRaahiahLRRESPFDGGIAATVPTI 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 274 DIDAMTG--------IRATKIE------------------KTDKAIRVTLENDA--VLESKTAIISTGASWRKLNIPGEd 325
Cdd:PRK13748 174 DRSRLLAqqqarvdeLRHAKYEgildgnpaitvlhgearfKDDQTLIVRLNDGGerVVAFDRCLIATGASPAVPPIPGL- 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 326 rlinKGVAFCPHCDGpLFEN---KNVAVIGGGNSGVEAAIDLAGIVKHVTLFE----FAPElkaDTVLQERLrsfpnvdi 398
Cdd:PRK13748 253 ----KETPYWTSTEA-LVSDtipERLAVIGSSVVALELAQAFARLGSKVTILArstlFFRE---DPAIGEAV-------- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 399 hTNARTAE---VLGEDHVTGLSYED---MSSGEMKELSLDGIFVQIGLVPNTKWIG-DA--VELNNRGEVVVDRENNTNV 469
Cdd:PRK13748 317 -TAAFRAEgieVLEHTQASQVAHVDgefVLTTGHGELRADKLLVATGRAPNTRSLAlDAagVTVNAQGAIVIDQGMRTSV 395
|
330
....*....|..
gi 515743079 470 PGIFAAGDVTDQ 481
Cdd:PRK13748 396 PHIYAAGDCTDQ 407
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
179-504 |
4.44e-10 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 62.07 E-value: 4.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 179 NGRMTISDILSKLGSTqdaseyedkdpydVLIIGGGPASGSAAIYTARKGLRTGI--VADRIGGQVndTAGIENFitvkq 256
Cdd:PRK12778 418 SGNISVPEVAEKNGKK-------------VAVIGSGPAGLSFAGDLAKRGYDVTVfeALHEIGGVL--KYGIPEF----- 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 257 ttgsefssNLAAHIEEYDIDAMTGIrATKIEkTDKAIRVTLENDAVLES--KTAIISTGASW-RKLNIPGEDRL------ 327
Cdd:PRK12778 478 --------RLPKKIVDVEIENLKKL-GVKFE-TDVIVGKTITIEELEEEgfKGIFIASGAGLpNFMNIPGENSNgvmssn 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 328 -----INKGVAFCPHCDGPLFENKNVAVIGGGNSGVEAAidlagivkhvtlfEFAPELKADTVLQERLRSfpnvDIHTNA 402
Cdd:PRK12778 548 eyltrVNLMDAASPDSDTPIKFGKKVAVVGGGNTAMDSA-------------RTAKRLGAERVTIVYRRS----EEEMPA 610
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 403 RTAEV------------------------------------LGEDHVTGLSYEDMSSGEMKELSLDGIFVQIGLVPN--- 443
Cdd:PRK12778 611 RLEEVkhakeegiefltlhnpieyladekgwvkqvvlqkmeLGEPDASGRRRPVAIPGSTFTVDVDLVIVSVGVSPNplv 690
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515743079 444 TKWIgDAVELNNRGEVVVDRENNTNVPGIFAAGDVTdQKYKQIIISMGSGANAALSAFDYI 504
Cdd:PRK12778 691 PSSI-PGLELNRKGTIVVDEEMQSSIPGIYAGGDIV-RGGATVILAMGDGKRAAAAIDEYL 749
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
208-504 |
4.65e-10 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 61.57 E-value: 4.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 208 VLIIGGGPASGSAAIYTARKGLRTGI--VADRIGGQVndTAGIENFITVKQTtgsefssnlaahIEEYDIDAMTGIrATK 285
Cdd:PRK12831 143 VAVIGSGPAGLTCAGDLAKMGYDVTIfeALHEPGGVL--VYGIPEFRLPKET------------VVKKEIENIKKL-GVK 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 286 IEkTDKAIRVTLENDAVLES---KTAIISTGASWRK-LNIPGED------------RlINKGVAFCPHCDGPLFENKNVA 349
Cdd:PRK12831 208 IE-TNVVVGKTVTIDELLEEegfDAVFIGSGAGLPKfMGIPGENlngvfsanefltR-VNLMKAYKPEYDTPIKVGKKVA 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 350 VIGGGNSGVEAA---IDLAGIVkHVTLFEFAPELKADT-----VLQERLRsfpnVDIHTNArtAEVLGEDH--VTGLSYE 419
Cdd:PRK12831 286 VVGGGNVAMDAArtaLRLGAEV-HIVYRRSEEELPARVeevhhAKEEGVI----FDLLTNP--VEILGDENgwVKGMKCI 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 420 DMSSGEMKE---------------LSLDGIFVQIGLVPNtKWIGDAV---ELNNRGEVVVDRENN-TNVPGIFAAGD-VT 479
Cdd:PRK12831 359 KMELGEPDAsgrrrpveiegsefvLEVDTVIMSLGTSPN-PLISSTTkglKINKRGCIVADEETGlTSKEGVFAGGDaVT 437
|
330 340
....*....|....*....|....*
gi 515743079 480 DQkyKQIIISMGSGANAALSAFDYI 504
Cdd:PRK12831 438 GA--ATVILAMGAGKKAAKAIDEYL 460
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
258-477 |
8.11e-10 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 60.70 E-value: 8.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 258 TGSEFSsnlaahiEEYDIDAMTgirATKIEKTDKAIRVTLENDAVLESKTAIISTGASWRKLNIPGEDRLI--NKGVAFc 335
Cdd:PRK04965 63 SAGEFA-------EQFNLRLFP---HTWVTDIDAEAQVVKSQGNQWQYDKLVLATGASAFVPPIPGRELMLtlNSQQEY- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 336 PHCDGPLFENKNVAVIGGGNSGVEAAIDLAGIVKHVTLFEFAPELKADTV-------LQERLRSfPNVDIHTNARTAEVl 408
Cdd:PRK04965 132 RAAETQLRDAQRVLVVGGGLIGTELAMDLCRAGKAVTLVDNAASLLASLMppevssrLQHRLTE-MGVHLLLKSQLQGL- 209
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515743079 409 gEDHVTGLSYEdMSSGEmkELSLDGIFVQIGLVPNTKWIGDAVELNNRGeVVVDRENNTNVPGIFAAGD 477
Cdd:PRK04965 210 -EKTDSGIRAT-LDSGR--SIEVDAVIAAAGLRPNTALARRAGLAVNRG-IVVDSYLQTSAPDIYALGD 273
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
305-481 |
1.05e-09 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 60.60 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 305 SKTAIISTGASWRKLNIPGEDRLINKGVAFCPHcDGPlfenKNVAVIGGGNSGVEAAIDLAGIVKHVTLFeFAPELKadt 384
Cdd:PLN02507 168 AKHILIATGSRAQRPNIPGKELAITSDEALSLE-ELP----KRAVVLGGGYIAVEFASIWRGMGATVDLF-FRKELP--- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 385 vlqerLRSFPNVDIHTNARTAEVLG-----EDHVTGLSYED----MSSGEMKELSLDGIFVQIGLVPNTKWIG---DAVE 452
Cdd:PLN02507 239 -----LRGFDDEMRAVVARNLEGRGinlhpRTNLTQLTKTEggikVITDHGEEFVADVVLFATGRAPNTKRLNleaVGVE 313
|
170 180
....*....|....*....|....*....
gi 515743079 453 LNNRGEVVVDRENNTNVPGIFAAGDVTDQ 481
Cdd:PLN02507 314 LDKAGAVKVDEYSRTNIPSIWAIGDVTNR 342
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
192-507 |
1.17e-08 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 57.62 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 192 GSTQDASEYEDKdPYDVLIIGGGPASGSAAIYTARKGLRTGIVA---DRIGGQ-VN------------------------ 243
Cdd:PTZ00153 104 FATSQSMNFSDE-EYDVGIIGCGVGGHAAAINAMERGLKVIIFTgddDSIGGTcVNvgcipskallyatgkyrelknlak 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 244 -DTAGI---------ENFITVKQTTGSEFSSNLAAhIEEYD---IDAM-----TGIRATKIEKTDKAIRVTLENDAVLES 305
Cdd:PTZ00153 183 lYTYGIytnafkngkNDPVERNQLVADTVQIDITK-LKEYTqsvIDKLrggieNGLKSKKFCKNSEHVQVIYERGHIVDK 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 306 KTA--------------IISTGASwrkLNIPGEDRLINKGVAFCPHCDGPLFENKNVAVIGGGNSGVEAAIDLAGIVKHV 371
Cdd:PTZ00153 262 NTIkseksgkefkvkniIIATGST---PNIPDNIEVDQKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEV 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 372 TLFEFAPEL----KADTV-LQER--LRSFPnVDIHTNARTAEVL---GEDHVTgLSYEDMSSGE----------MKELSL 431
Cdd:PTZ00153 339 VSFEYSPQLlpllDADVAkYFERvfLKSKP-VRVHLNTLIEYVRagkGNQPVI-IGHSERQTGEsdgpkknmndIKETYV 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 432 DGIFVQIGLVPNTKWIG-DAVELN-NRGEVVVD------RENNTNVPGIFAAGDVTDqkyKQIIISMGSgaNAALSAFDY 503
Cdd:PTZ00153 417 DSCLVATGRKPNTNNLGlDKLKIQmKRGFVSVDehlrvlREDQEVYDNIFCIGDANG---KQMLAHTAS--HQALKVVDW 491
|
....
gi 515743079 504 IIRN 507
Cdd:PTZ00153 492 IEGK 495
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
206-493 |
2.24e-08 |
|
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member of the pyridine nucleotide disulfide oxidoreductase family contains a C-terminal motif Cys-SeCys-Gly, where SeCys is selenocysteine encoded by TGA (in some sequence reports interpreted as a stop codon). In some members of this subfamily, Cys-SeCys-Gly is replaced by Cys-Cys-Gly. The reach of the selenium atom at the C-term arm of the protein is proposed to allow broad substrate specificity.
Pssm-ID: 273624 [Multi-domain] Cd Length: 484 Bit Score: 56.40 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 206 YDVLIIGGGP----ASGSAAIYTAR-----------KGLRTGI----------------VADRIGGQVNDTAGIE-NFIT 253
Cdd:TIGR01438 3 YDLIVIGGGSgglaAAKEAAAYGAKvmlldfvtptpLGTRWGIggtcvnvgcipkklmhQAALLGQALKDSRNYGwKVEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 254 VKQTTGSEFSSNLAAHIEEYDIDAMTGIRATKI-------EKTDK-AIRVTLEN--DAVLESKTAIISTGASWRKLNIPG 323
Cdd:TIGR01438 83 TVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVkyenayaEFVDKhRIKATNKKgkEKIYSAERFLIATGERPRYPGIPG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 324 EDRL-INKGVAFC-PHCDGplfenkNVAVIGGGNSGVEAAIDLAGIVKHVTLFefapelkadtVLQERLRSFPN---VDI 398
Cdd:TIGR01438 163 AKELcITSDDLFSlPYCPG------KTLVVGASYVALECAGFLAGIGLDVTVM----------VRSILLRGFDQdcaNKV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 399 HTNARTAEVLGEDHVTGLSYEDMSSGEMKELS---------LDGIFVQIGLVPNTKWIG---DAVELNNR-GEVVVDREN 465
Cdd:TIGR01438 227 GEHMEEHGVKFKRQFVPIKVEQIEAKVLVEFTdstngieeeYDTVLLAIGRDACTRKLNlenVGVKINKKtGKIPADEEE 306
|
330 340
....*....|....*....|....*...
gi 515743079 466 NTNVPGIFAAGDVTDQKYKQIIISMGSG 493
Cdd:TIGR01438 307 QTNVPYIYAVGDILEDKPELTPVAIQAG 334
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
208-507 |
5.12e-08 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 55.72 E-value: 5.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 208 VLIIGGGPASGSAAIYTARKGLRTGI--VADRIGGQVNdtAGIENFitvkqttgsefssNLAAHIEEYDIDAMTGIrATK 285
Cdd:PRK12775 433 VAICGSGPAGLAAAADLVKYGVDVTVyeALHVVGGVLQ--YGIPSF-------------RLPRDIIDREVQRLVDI-GVK 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 286 IEkTDKAIRVTLENDAVLESK---TAIISTGASWRK-LNIPGE------------DRLINKGVAFCPHCDGPLFENKNVA 349
Cdd:PRK12775 497 IE-TNKVIGKTFTVPQLMNDKgfdAVFLGVGAGAPTfLGIPGEfagqvysaneflTRVNLMGGDKFPFLDTPISLGKSVV 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 350 VIGGGNSgveaAIDLAGIVKHVTlfefAP---------ELKADTVLQE-RLRSFPNVDIHTNARTAEVL--GEDHVTGLS 417
Cdd:PRK12775 576 VIGAGNT----AMDCLRVAKRLG----APtvrcvyrrsEAEAPARIEEiRHAKEEGIDFFFLHSPVEIYvdAEGSVRGMK 647
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 418 YEDM--------------SSGEMKELSLDGIFVQIGLVPNtKWIGDA---VELNNRGEVVVD-----RENNTNVPGIFAA 475
Cdd:PRK12775 648 VEEMelgepdekgrrkpmPTGEFKDLECDTVIYALGTKAN-PIITQStpgLALNKWGNIAADdgkleSTQSTNLPGVFAG 726
|
330 340 350
....*....|....*....|....*....|..
gi 515743079 476 GDVTDQKyKQIIISMGSGANAALSAFDYIIRN 507
Cdd:PRK12775 727 GDIVTGG-ATVILAMGAGRRAARSIATYLRLG 757
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
438-480 |
7.21e-08 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 54.87 E-value: 7.21e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 515743079 438 IGLVPNTKWIG--DA-VELNNRGEVVVDRENNTNVPGIFAAGDVTD 480
Cdd:PRK07845 270 VGSVPNTAGLGleEAgVELTPSGHITVDRVSRTSVPGIYAAGDCTG 315
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
206-487 |
1.82e-07 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 53.85 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 206 YDVLIIGGGPASGSAAIYTARKGLRTGIVA-DRIGGQVNDTAGIENFITVKQTTGSEFSSNlAAHI-----EEYDIDAMT 279
Cdd:PTZ00058 49 YDLIVIGGGSGGMAAARRAARNKAKVALVEkDYLGGTCVNVGCVPKKIMFNAASIHDILEN-SRHYgfdtqFSFNLPLLV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 280 GIRATKIEKTDKAIRVTLENDAV--LESKTAIISTGASWRK--------LNIPGEDRLINKGVAFCPHCDGPLFENKNVA 349
Cdd:PTZ00058 128 ERRDKYIRRLNDIYRQNLKKDNVeyFEGKGSLLSENQVLIKkvsqvdgeADESDDDEVTIVSAGVSQLDDGQVIEGKNIL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 350 VIGGGN------SGVEAAIDLAGIVK---------------HVTLFEFAPELKADTVLQER----LRSF----------- 393
Cdd:PTZ00058 208 IAVGNKpifpdvKGKEFTISSDDFFKikeakrigiagsgyiAVELINVVNRLGAESYIFARgnrlLRKFdetiinelend 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 394 ---PNVDIHTNARTAEVlGEDHVTGLSYEDMSSGemKELSLDGIFVQIGLVPNTKWIG--DAVELNNRGEVVVDRENNTN 468
Cdd:PTZ00058 288 mkkNNINIITHANVEEI-EKVKEKNLTIYLSDGR--KYEHFDYVIYCVGRSPNTEDLNlkALNIKTPKGYIKVDDNQRTS 364
|
330
....*....|....*....
gi 515743079 469 VPGIFAAGDVTDQKYKQII 487
Cdd:PTZ00058 365 VKHIYAVGDCCMVKKNQEI 383
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
305-496 |
1.98e-07 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 53.73 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 305 SKTAIISTGASWRKLNIPGEDRLINKGVAFcphcDGPlFENKNVAVIGGGNSGVEAAIDLAGIVKHVTLFefapeLKADT 384
Cdd:PLN02546 217 ARNILIAVGGRPFIPDIPGIEHAIDSDAAL----DLP-SKPEKIAIVGGGYIALEFAGIFNGLKSDVHVF-----IRQKK 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 385 VLQ---ERLRSF-------PNVDIHTNARTAEVLGEDhvTGLSYEDMSSGEMKELSldGIFVQIGLVPNTKWIG---DAV 451
Cdd:PLN02546 287 VLRgfdEEVRDFvaeqmslRGIEFHTEESPQAIIKSA--DGSLSLKTNKGTVEGFS--HVMFATGRKPNTKNLGleeVGV 362
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 515743079 452 ELNNRGEVVVDRENNTNVPGIFAAGDVTDQKYKQIIISMGSGANA 496
Cdd:PLN02546 363 KMDKNGAIEVDEYSRTSVPSIWAVGDVTDRINLTPVALMEGGALA 407
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
206-478 |
2.21e-07 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 53.24 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 206 YDVLIIGGGPASGSAAIYTARKGLRTGIV--ADRIGGQVNDTAGI------EnfiTVKQTTG----SEFSSN-------- 265
Cdd:PRK05249 6 YDLVVIGSGPAGEGAAMQAAKLGKRVAVIerYRNVGGGCTHTGTIpskalrE---AVLRLIGfnqnPLYSSYrvklritf 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 266 --LAAHIEE------------YD---IDAMTGiRATKIEKTDkaIRVTLENDAV--LESKTAIISTGASWRKlniPgedr 326
Cdd:PRK05249 83 adLLARADHvinkqvevrrgqYErnrVDLIQG-RARFVDPHT--VEVECPDGEVetLTADKIVIATGSRPYR---P---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 327 linKGVAFcphcDGP-----------LFENKNVAVIGGGNSGVEAAIDLAGIVKHVTLFEFAPELKA--DT----VLQER 389
Cdd:PRK05249 153 ---PDVDF----DHPriydsdsilslDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINTRDRLLSflDDeisdALSYH 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 390 LRSFpNVDIHTNARTAEVLGEDH--VTGLSyedmsSGemKELSLDGIFVQIGLVPNTKWIG-DAV--ELNNRGEVVVDRE 464
Cdd:PRK05249 226 LRDS-GVTIRHNEEVEKVEGGDDgvIVHLK-----SG--KKIKADCLLYANGRTGNTDGLNlENAglEADSRGQLKVNEN 297
|
330
....*....|....
gi 515743079 465 NNTNVPGIFAAGDV 478
Cdd:PRK05249 298 YQTAVPHIYAVGDV 311
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
199-477 |
1.68e-06 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 50.50 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 199 EYEDKDPYDVLIIGGGPASGSAAIYTARKGLRTGIV--ADRIGGQVNdtAGIENFitvkqttgsefssNLAAHIEEYDID 276
Cdd:PRK12814 187 ERAPKSGKKVAIIGAGPAGLTAAYYLLRKGHDVTIFdaNEQAGGMMR--YGIPRF-------------RLPESVIDADIA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 277 AMTGIRATKIEKTDKAIRVTLEN-----DAVLesktaiISTGASW-RKLNIPGED-----------RLINKGVAFCPhcd 339
Cdd:PRK12814 252 PLRAMGAEFRFNTVFGRDITLEElqkefDAVL------LAVGAQKaSKMGIPGEElpgvisgidflRNVALGTALHP--- 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 340 gplfeNKNVAVIGGGNSGVEAA-IDLAGIVKHVTLF------EF-APELKADTVLQE----RLRSFPnVDIHTNARTAEV 407
Cdd:PRK12814 323 -----GKKVVVIGGGNTAIDAArTALRLGAESVTILyrrtreEMpANRAEIEEALAEgvslRELAAP-VSIERSEGGLEL 396
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515743079 408 ------LGEDHVTGLSYEDMSSGEMKELSLDGIFVQIG-LVPNTKWIGDAVELNNRGEVVVDREN-NTNVPGIFAAGD 477
Cdd:PRK12814 397 taikmqQGEPDESGRRRPVPVEGSEFTLQADTVISAIGqQVDPPIAEAAGIGTSRNGTVKVDPETlQTSVAGVFAGGD 474
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
345-410 |
5.08e-06 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 49.09 E-value: 5.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 345 NKNVAVIGGGNSGVEAAIDLAGIVKHVTLFEFAPEL------------KADTV------LQERLRSFPNVDIHTNARTAE 406
Cdd:COG1148 140 NKRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELggraaqlhktfpGLDCPqcilepLIAEVEANPNITVYTGAEVEE 219
|
....
gi 515743079 407 VLGE 410
Cdd:COG1148 220 VSGY 223
|
|
| Thioredoxin_3 |
pfam13192 |
Thioredoxin domain; |
123-191 |
7.82e-06 |
|
Thioredoxin domain;
Pssm-ID: 433026 [Multi-domain] Cd Length: 71 Bit Score: 43.74 E-value: 7.82e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 123 VSLTCQKCPDVVQALNlMSVINPNITHTMIDGAVFREESK-DIMAVPAVFLDGEEFGNGRMTISDILSKL 191
Cdd:pfam13192 1 LGPGCPKCPQLEKAVK-EAAAELGIDAEVEKVTDFPEIAKyGVMSTPALVINGKVVSSGKVPSEEEIRKL 69
|
|
| PfPDO_like_N |
cd02975 |
Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO)-like family, N-terminal TRX-fold ... |
33-96 |
1.75e-05 |
|
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: 43.92 E-value: 1.75e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515743079 33 SKELKDLLDEIAEMTDYITIV------EKEL------KRTPSFQVSKPE-EDTGITFAGIPLGHEFNSLVLAILQVS 96
Cdd:cd02975 37 CEVTKQLLEELSELSDKLKLEiydfdeDKEKaekygvERVPTTIFLQDGgKDGGIRYYGLPAGYEFASLIEDIVRVS 113
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
206-259 |
1.84e-05 |
|
geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
Pssm-ID: 273936 [Multi-domain] Cd Length: 295 Bit Score: 46.54 E-value: 1.84e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 515743079 206 YDVLIIGGGPASGSAAIYTARKGLRTGIVaDRiggqvndtagiENFITVKQTTG 259
Cdd:TIGR02032 1 YDVVVVGAGPAGASAAYRLADKGLRVLLL-EK-----------KSFPRYKPCGG 42
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
432-486 |
2.48e-05 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 46.70 E-value: 2.48e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 515743079 432 DGIFVQIGLVPNTKWIGDA-VELNNRGEVVVDRENNTNVPGIFAAGDVTDQKYKQI 486
Cdd:PRK13512 231 DMIIEGVGTHPNSKFIESSnIKLDDKGFIPVNDKFETNVPNIYAIGDIITSHYRHV 286
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
206-479 |
4.12e-05 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 46.16 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 206 YDVLIIGGGPASGSAAIYTARKGLRTGIV---ADRIGGQ------------VNDTAGIENFITVKQTTGS--EFSSNLAA 268
Cdd:PRK08010 4 YQAVIIGFGKAGKTLAVTLAKAGWRVALIeqsNAMYGGTcinigciptktlVHDAQQHTDFVRAIQRKNEvvNFLRNKNF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 269 H--IEEYDIDAMTGiRATKIEktDKAIRV-TLENDAVLESKTAIISTGASWRKLNIPG----EDRLINKGVAFCPHCDGP 341
Cdd:PRK08010 84 HnlADMPNIDVIDG-QAEFIN--NHSLRVhRPEGNLEIHGEKIFINTGAQTVVPPIPGitttPGVYDSTGLLNLKELPGH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 342 LfenknvAVIGGGNSGVEAAIDLAGIVKHVTLFE----FAPELKAD------TVLQERlrsfpNVDIHTNArtaevlged 411
Cdd:PRK08010 161 L------GILGGGYIGVEFASMFANFGSKVTILEaaslFLPREDRDiadniaTILRDQ-----GVDIILNA--------- 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515743079 412 HVTGLSYEDMS---SGEMKELSLDGIFVQIGLVPNTKWI---GDAVELNNRGEVVVDRENNTNVPGIFAAGDVT 479
Cdd:PRK08010 221 HVERISHHENQvqvHSEHAQLAVDALLIASGRQPATASLhpeNAGIAVNERGAIVVDKYLHTTADNIWAMGDVT 294
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
272-482 |
4.69e-05 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 45.69 E-value: 4.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 272 EYDIDAMTGIRATKIEKTDKAirVTLENDAVLESKTAIISTGASWRKLniPGEDRLiNKGVAFCPHCDGP------LFEN 345
Cdd:PRK09754 70 ENNVHLHSGVTIKTLGRDTRE--LVLTNGESWHWDQLFIATGAAARPL--PLLDAL-GERCFTLRHAGDAarlrevLQPE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 346 KNVAVIGGGNSGVEAAIDLAGIVKHVTLFEFA--------PELKADTVLQERLRSFPNVDIHTNARTAeVLGEDHVTGLS 417
Cdd:PRK09754 145 RSVVIVGAGTIGLELAASATQRRCKVTVIELAatvmgrnaPPPVQRYLLQRHQQAGVRILLNNAIEHV-VDGEKVELTLQ 223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515743079 418 yedmsSGEmkELSLDGIFVQIGLVPNTKWIGDAvELNNRGEVVVDRENNTNVPGIFAAGDVTDQK 482
Cdd:PRK09754 224 -----SGE--TLQADVVIYGIGISANDQLAREA-NLDTANGIVIDEACRTCDPAIFAGGDVAITR 280
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
346-477 |
4.92e-05 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 46.26 E-value: 4.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 346 KNVAVIGGGNSGVEAAIDLA--GIVKHVtlFEFAPELKADTV-------LQERLRSFpNVDIHTNARTAEVL--GEDHVT 414
Cdd:PRK14989 146 KRGAVVGGGLLGLEAAGALKnlGVETHV--IEFAPMLMAEQLdqmggeqLRRKIESM-GVRVHTSKNTLEIVqeGVEARK 222
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515743079 415 GLSYEDMSsgemkELSLDGIFVQIGLVPNTKWIGD-AVELNNRGEVVVDRENNTNVPGIFAAGD 477
Cdd:PRK14989 223 TMRFADGS-----ELEVDFIVFSTGIRPQDKLATQcGLAVAPRGGIVINDSCQTSDPDIYAIGE 281
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
348-480 |
7.58e-05 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 45.33 E-value: 7.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 348 VAVIGGGNSGVEAAIDLAGIVKHVTLFEFAPEL--KADTVLQERLRSFPNV--DIHTNARTAEVLGEDHVTGLSYEDMSS 423
Cdd:PRK07846 169 LVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRLlrHLDDDISERFTELASKrwDVRLGRNVVGVSQDGSGVTLRLDDGST 248
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 424 gemkeLSLDGIFVQIGLVPNTKWIGDA---VELNNRGEVVVDRENNTNVPGIFAAGDVTD 480
Cdd:PRK07846 249 -----VEADVLLVATGRVPNGDLLDAAaagVDVDEDGRVVVDEYQRTSAEGVFALGDVSS 303
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
206-240 |
1.72e-04 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 44.07 E-value: 1.72e-04
10 20 30
....*....|....*....|....*....|....*..
gi 515743079 206 YDVLIIGGGPASGSAAIYTARKGLRTGIV--ADRIGG 240
Cdd:COG1233 4 YDVVVIGAGIGGLAAAALLARAGYRVTVLekNDTPGG 40
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
198-313 |
4.67e-04 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 42.21 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 198 SEYEDKDPY---DVLIIGGGPASGSAAIYTARKGLRTgIVADRiggqvndTAGIENFitvkqttGSEFSSNLAAHIEEY- 273
Cdd:pfam13738 145 SYVKDFHPYagqKVVVIGGYNSAVDAALELVRKGARV-TVLYR-------GSEWEDR-------DSDPSYSLSPDTLNRl 209
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 515743079 274 -------DIDAMTGIRATKIEKTDKAIRVTLENDAVLESKTA-IISTG 313
Cdd:pfam13738 210 eelvkngKIKAHFNAEVKEITEVDVSYKVHTEDGRKVTSNDDpILATG 257
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
310-479 |
4.75e-04 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 42.90 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 310 ISTGASW-RKLNIPGEDRL-----------INKGVAFCPHCDGPLFE--NKNVAVIGGGNSGVEAAIDLAGIVKHVTLF- 374
Cdd:PRK12779 398 VGTGAGLpTFMNVPGEHLLgvmsanefltrVNLMRGLDDDYETPLPEvkGKEVFVIGGGNTAMDAARTAKRLGGNVTIVy 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 375 ------------EFAPELKADTVLQErLRSfPNV---DIHTNARTAEVLGedhVTGLSYEDMS-------SGEMKELSLD 432
Cdd:PRK12779 478 rrtksemparveELHHALEEGINLAV-LRA-PREfigDDHTHFVTHALLD---VNELGEPDKSgrrspkpTGEIERVPVD 552
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 515743079 433 GIFVQIGLVPNtKWIGDA---VELNNRGEVVVDRENN-TNVPGIFAAGDVT 479
Cdd:PRK12779 553 LVIMALGNTAN-PIMKDAepgLKTNKWGTIEVEKGSQrTSIKGVYSGGDAA 602
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
207-247 |
6.10e-04 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 42.21 E-value: 6.10e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 515743079 207 DVLIIGGGPASGSAAIYTARKGLRTGIVADR--IGGQVndTAG 247
Cdd:pfam12831 1 DVVVVGGGPAGVAAAIAAARAGAKVLLVERRgfLGGML--TSG 41
|
|
| GlpB |
COG3075 |
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism]; |
206-235 |
1.35e-03 |
|
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 442309 Cd Length: 415 Bit Score: 40.93 E-value: 1.35e-03
10 20 30
....*....|....*....|....*....|
gi 515743079 206 YDVLIIGGGPASGSAAIYTARKGLRTGIVA 235
Cdd:COG3075 3 FDVVVIGGGLAGLTAAIRAAEAGLRVAIVS 32
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
201-313 |
1.43e-03 |
|
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: 40.95 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 201 EDKDPYDVLIIGGGPAsGSAAIYTARK-GLRTGIV--ADRIGGQVndtagienfitvkqttGSEFSSNLAAHIEEYDIDA 277
Cdd:COG0446 120 KEFKGKRAVVIGGGPI-GLELAEALRKrGLKVTLVerAPRLLGVL----------------DPEMAALLEEELREHGVEL 182
|
90 100 110
....*....|....*....|....*....|....*.
gi 515743079 278 MTGIRATKIEKTDKaIRVTLENDAVLESKTAIISTG 313
Cdd:COG0446 183 RLGETVVAIDGDDK-VAVTLTDGEEIPADLVVVAPG 217
|
|
| PRK07494 |
PRK07494 |
UbiH/UbiF family hydroxylase; |
201-235 |
1.78e-03 |
|
UbiH/UbiF family hydroxylase;
Pssm-ID: 181001 [Multi-domain] Cd Length: 388 Bit Score: 40.66 E-value: 1.78e-03
10 20 30
....*....|....*....|....*....|....*
gi 515743079 201 EDKDPYDVLIIGGGPASGSAAIYTARKGLRTGIVA 235
Cdd:PRK07494 3 MEKEHTDIAVIGGGPAGLAAAIALARAGASVALVA 37
|
|
| PRK05329 |
PRK05329 |
glycerol-3-phosphate dehydrogenase subunit GlpB; |
206-235 |
1.97e-03 |
|
glycerol-3-phosphate dehydrogenase subunit GlpB;
Pssm-ID: 235412 Cd Length: 422 Bit Score: 40.60 E-value: 1.97e-03
10 20 30
....*....|....*....|....*....|
gi 515743079 206 YDVLIIGGGPASGSAAIYTARKGLRTGIVA 235
Cdd:PRK05329 3 FDVLVIGGGLAGLTAALAAAEAGKRVALVA 32
|
|
| glycerol3P_GlpB |
TIGR03378 |
glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are ... |
206-235 |
3.05e-03 |
|
glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are the B subunit, product of the glpB gene, of a three-subunit, membrane-anchored, FAD-dependent anaerobic glycerol-3-phosphate dehydrogenase. [Energy metabolism, Anaerobic]
Pssm-ID: 213807 Cd Length: 419 Bit Score: 40.00 E-value: 3.05e-03
10 20 30
....*....|....*....|....*....|
gi 515743079 206 YDVLIIGGGPASGSAAIYTARKGLRTGIVA 235
Cdd:TIGR03378 1 FDVIIIGGGLAGLSCALRLAEAGKKCAIIA 30
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
207-506 |
3.05e-03 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 40.23 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 207 DVLIIGGGPASGSAAIYTARKGLRTGIV--ADRIGGQVndtAGIeNFITVKQTTGSEFSSNLAAHIEEYD-IDAMTGira 283
Cdd:COG1148 142 RALVIGGGIAGMTAALELAEQGYEVYLVekEPELGGRA---AQL-HKTFPGLDCPQCILEPLIAEVEANPnITVYTG--- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 284 TKIEKTDKAI---RVTLENDA----VLESKTAIISTGAS---WRKLN------IPG-----E-DRLINKGVAFCPHcDGP 341
Cdd:COG1148 215 AEVEEVSGYVgnfTVTIKKGPreeiEIEVGAIVLATGFKpydPTKLGeygygkYPNvitnlElERLLAAGKILRPS-DGK 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 342 lfENKNVAVI--------GGGN---SGV--EAAIDLAGIVKH------VTLF-----------EFAPELKADTVlqerlr 391
Cdd:COG1148 294 --EPKSVAFIqcvgsrdeENGLpycSRVccMYALKQALYLKEknpdadVYIFyrdirtygkyeEFYRRAREDGV------ 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743079 392 sfpnvdIHTNARTAEVL--GEDHVTgLSYEDMSSGEMKELSLDGIFVQIGLVPNTkwigDAVELNNRGEVVVDREN---- 465
Cdd:COG1148 366 ------RFIRGRVAEIEedEGGKLV-VTVEDTLLGEPVEIEADLVVLATGMVPSE----DNEELAKLLKLPLDQDGffle 434
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 515743079 466 --------NTNVPGIFAAGDVtdQKYKQIIISMGSGANAALSAFDYIIR 506
Cdd:COG1148 435 ahpklrpvETATDGIFLAGAA--HGPKDIPESIAQATAAAARAIQLLSK 481
|
|
| sdhA |
PRK07803 |
succinate dehydrogenase flavoprotein subunit; Reviewed |
198-234 |
8.35e-03 |
|
succinate dehydrogenase flavoprotein subunit; Reviewed
Pssm-ID: 236101 [Multi-domain] Cd Length: 626 Bit Score: 38.86 E-value: 8.35e-03
10 20 30
....*....|....*....|....*....|....*..
gi 515743079 198 SEYEDKDpYDVLIIGGGPASGSAAIYTARKGLRTGIV 234
Cdd:PRK07803 2 TEVERHS-YDVVVIGAGGAGLRAAIEARERGLRVAVV 37
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
206-240 |
9.84e-03 |
|
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440673 [Multi-domain] Cd Length: 443 Bit Score: 38.28 E-value: 9.84e-03
10 20 30
....*....|....*....|....*....|....*..
gi 515743079 206 YDVLIIGGGPASGSAAIYTARKGLRTGIV--ADRIGG 240
Cdd:COG1053 4 YDVVVVGSGGAGLRAALEAAEAGLKVLVLekVPPRGG 40
|
|
| |
