|
Name |
Accession |
Description |
Interval |
E-value |
| TRX_reduct |
TIGR01292 |
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ... |
86-391 |
1.38e-151 |
|
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: 435.52 E-value: 1.38e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 86 VVIIGSGPAGYTAAIYAARANLKPVVFEGYQmggvPGGQLMTTTEVENFPGFPDGITGPDLMEKMRKQAERWGAELYPED 165
Cdd:TIGR01292 2 VIIIGAGPAGLTAAIYAARANLKPLLIEGME----PGGQLTTTTEVENYPGFPEGISGPELMEKMKEQAVKFGAEIIYEE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 166 VESLSVTTAPFTVQTSERK-VKCHSIIYATGATARRLRLPREEEFWSRGISACAICDGasPLFKGQVLAVVGGGDTATEE 244
Cdd:TIGR01292 78 VIKVDKSDRPFKVYTGDGKeYTAKAVIIATGASARKLGIPGEDEFWGRGVSYCATCDG--PFFKNKEVAVVGGGDSAIEE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 245 ALYLTKYARHVHLLVRRDQLRASKAMQDRVINNPNITVHYNTETVDVLSNTKgqMSGILLRRLDTGEETELEAKGLFYGI 324
Cdd:TIGR01292 156 ALYLTRIAKKVTLVHRRDKFRAEKILLDRLKKNPKIEFLWNSTVEEIVGDNK--VEGVKIKNTVTGEEEELEVDGVFIAI 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18405775 325 GHSPNSQLLEGQVELDSSGYVLVREGTSnTSVEGVFAAGDVQDHEWRQAVTAAGSGCIAALSAERYL 391
Cdd:TIGR01292 234 GHEPNTELLKGLLELDENGYIVTDEGMR-TSVPGVFAAGDVRDKGYRQAVTAAGDGCIAALSAERYL 299
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
86-391 |
3.94e-150 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 431.85 E-value: 3.94e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 86 VVIIGSGPAGYTAAIYAARANLKPVVFEGyqmgGVPGGQLMTTTEVENFPGFPDGITGPDLMEKMRKQAERWGAELYPED 165
Cdd:COG0492 3 VVIIGAGPAGLTAAIYAARAGLKTLVIEG----GEPGGQLATTKEIENYPGFPEGISGPELAERLREQAERFGAEILLEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 166 VESLSVTTAPFTVQTSERK-VKCHSIIYATGATARRLRLPREEEFWSRGISACAICDGAspLFKGQVLAVVGGGDTATEE 244
Cdd:COG0492 79 VTSVDKDDGPFRVTTDDGTeYEAKAVIIATGAGPRKLGLPGEEEFEGRGVSYCATCDGF--FFRGKDVVVVGGGDSALEE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 245 ALYLTKYARHVHLLVRRDQLRASKAMQDRVINNPNITVHYNTETVDVLSNtkGQMSGILLRRLDTGEETELEAKGLFYGI 324
Cdd:COG0492 157 ALYLTKFASKVTLIHRRDELRASKILVERLRANPKIEVLWNTEVTEIEGD--GRVEGVTLKNVKTGEEKELEVDGVFVAI 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18405775 325 GHSPNSQLLEGQ-VELDSSGYVLVREGTSnTSVEGVFAAGDVQDHEWRQAVTAAGSGCIAALSAERYL 391
Cdd:COG0492 235 GLKPNTELLKGLgLELDEDGYIVVDEDME-TSVPGVFAAGDVRDYKYRQAATAAGEGAIAALSAARYL 301
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
86-391 |
4.74e-90 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 278.87 E-value: 4.74e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 86 VVIIGSGPAGYTAAIYAARANLKPVVFEGYQmggvPGGQLMTTTEVENFPGFPDGITGPDLMEKMRKQAERWGAELYPED 165
Cdd:PRK10262 9 LLILGSGPAGYTAAVYAARANLQPVLITGME----KGGQLTTTTEVENWPGDPNDLTGPLLMERMHEHATKFETEIIFDH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 166 VESLSVTTAPFTVQTSERKVKCHSIIYATGATARRLRLPREEEFWSRGISACAICDGAspLFKGQVLAVVGGGDTATEEA 245
Cdd:PRK10262 85 INKVDLQNRPFRLTGDSGEYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGF--FYRNQKVAVIGGGNTAVEEA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 246 LYLTKYARHVHLLVRRDQLRASKAMQDRVIN---NPNITVHYNTETVDVLSNTKGqMSGILLRRLDTGEETE-LEAKGLF 321
Cdd:PRK10262 163 LYLSNIASEVHLIHRRDGFRAEKILIKRLMDkveNGNIILHTNRTLEEVTGDQMG-VTGVRLRDTQNSDNIEsLDVAGLF 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18405775 322 YGIGHSPNSQLLEGQVELDsSGYVLVREG----TSNTSVEGVFAAGDVQDHEWRQAVTAAGSGCIAALSAERYL 391
Cdd:PRK10262 242 VAIGHSPNTAIFEGQLELE-NGYIKVQSGihgnATQTSIPGVFAAGDVMDHIYRQAITSAGTGCMAALDAERYL 314
|
|
| TRX_NTR |
cd02949 |
TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found ... |
430-526 |
1.34e-66 |
|
TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found only in oxygenic photosynthetic organisms containing both TRX and NTR domains. The TRX domain functions as a protein disulfide reductase via the reversible oxidation of an active center dithiol present in a CXXC motif, while the NTR domain functions as a reductant to oxidized TRX. The fusion protein is bifunctional, showing both TRX and NTR activities, but it is not an independent NTR/TRX system. In plants, the protein is found exclusively in shoots and mature leaves and is localized in the chloroplast. It is involved in plant protection against oxidative stress.
Pssm-ID: 239247 [Multi-domain] Cd Length: 97 Bit Score: 210.05 E-value: 1.34e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 430 GQYALRKLYHESPRVILVLYTSPTCGPCRTLKPILNKVVDEYNHDVHFVEIDIEEDQEIAEAAGIMGTPCVQFFKNKEML 509
Cdd:cd02949 1 GSYALRKLYHESDRLILVLYTSPTCGPCRTLKPILNKVIDEFDGAVHFVEIDIDEDQEIAEAAGIMGTPTVQFFKDKELV 80
|
90
....*....|....*..
gi 18405775 510 RTISGVKMKKEYREFIE 526
Cdd:cd02949 81 KEISGVKMKSEYREFIE 97
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
86-391 |
5.42e-61 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 209.24 E-value: 5.42e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 86 VVIIGSGPAGYTAAIYAARANLKP-VVFEGYqmggvpGGQLMTTTEVENFPGFPDgITGPDLMEKMRKQAERwgaelYPE 164
Cdd:PRK15317 214 VLVVGGGPAGAAAAIYAARKGIRTgIVAERF------GGQVLDTMGIENFISVPE-TEGPKLAAALEEHVKE-----YDV 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 165 DV------ESLSVTTAPFTVQT-SERKVKCHSIIYATGATARRLRLPREEEFWSRGISACAICDGasPLFKGQVLAVVGG 237
Cdd:PRK15317 282 DImnlqraSKLEPAAGLIEVELaNGAVLKAKTVILATGARWRNMNVPGEDEYRNKGVAYCPHCDG--PLFKGKRVAVIGG 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 238 GDTATEEALYLTKYARHVHLLVRRDQLRASKAMQDRVINNPNITVHYNTETVDVLSNTKgQMSGILLRRLDTGEETELEA 317
Cdd:PRK15317 360 GNSGVEAAIDLAGIVKHVTVLEFAPELKADQVLQDKLRSLPNVTIITNAQTTEVTGDGD-KVTGLTYKDRTTGEEHHLEL 438
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18405775 318 KGLFYGIGHSPNSQLLEGQVELDSSGYVLVREgTSNTSVEGVFAAGDVQDHEWRQAVTAAGSGCIAALSAERYL 391
Cdd:PRK15317 439 EGVFVQIGLVPNTEWLKGTVELNRRGEIIVDA-RGATSVPGVFAAGDCTTVPYKQIIIAMGEGAKAALSAFDYL 511
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
85-380 |
9.29e-55 |
|
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: 186.37 E-value: 9.29e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 85 NVVIIGSGPAGYTAAIYAARANLKPVVFEgyqMGGV-PGGQLMTTTEVENFPGFPDGI-TGPDLMEKMRKQAERWGAE-- 160
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGGKVTLIE---DEGTcPYGGCVLSKALLGAAEAPEIAsLWADLYKRKEEVVKKLNNGie 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 161 -LYPEDVESLSVTTAPF----TVQTSERKVKCHSIIYATGATARRLRLPREEEFWSRGISACAICDGASPLFKGQVLAVV 235
Cdd:pfam07992 79 vLLGTEVVSIDPGAKKVvleeLVDGDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKLLPKRVVVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 236 GGGDTATEEALYLTKYARHVHLLVRRDQL------RASKAMQDRVINNpNITVHYNTETVDVLSNTKGQmsgillrRLDT 309
Cdd:pfam07992 159 GGGYIGVELAAALAKLGKEVTLIEALDRLlrafdeEISAALEKALEKN-GVEVRLGTSVKEIIGDGDGV-------EVIL 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18405775 310 GEETELEAKGLFYGIGHSPNSQLLE-GQVELDSSGYVLVREgTSNTSVEGVFAAGDVQDHEWRQAVTAAGSG 380
Cdd:pfam07992 231 KDGTEIDADLVVVAIGRRPNTELLEaAGLELDERGGIVVDE-YLRTSVPGIYAAGDCRVGGPELAQNAVAQG 301
|
|
| CnoX |
COG3118 |
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ... |
440-528 |
3.09e-25 |
|
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442352 [Multi-domain] Cd Length: 105 Bit Score: 99.89 E-value: 3.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 440 ESPRVILVLYTSPTCGPCRTLKPILNKVVDEYNHDVHFVEIDIEEDQEIAEAAGIMGTPCVQFFKNKEMLRTISGVKMKK 519
Cdd:COG3118 16 ESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLFKDGQPVDRFVGALPKE 95
|
....*....
gi 18405775 520 EYREFIEAN 528
Cdd:COG3118 96 QLREFLDKV 104
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
86-390 |
4.11e-24 |
|
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: 104.83 E-value: 4.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 86 VVIIGSGPAGYTAAIYAARANLKPVVFEGYQmggVPGGQLMTttevenfpgfpdGITG----PDLMEKMRKQAERWGAEL 161
Cdd:COG0493 124 VAVVGSGPAGLAAAYQLARAGHEVTVFEALD---KPGGLLRY------------GIPEfrlpKDVLDREIELIEALGVEF 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 162 YPEdveslsvTTAPFTVQTSERKVKCHSIIYATGAT-ARRLRLPREEefwSRGI--------SACAICDGASPLFKGQVL 232
Cdd:COG0493 189 RTN-------VEVGKDITLDELLEEFDAVFLATGAGkPRDLGIPGED---LKGVhsamdfltAVNLGEAPDTILAVGKRV 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 233 AVVGGGDTATE---EALYLTkyARHVHLLVRRDQLRaSKAMQDRVIN--NPNITVHYNTETVDVLSNTKGQMSGILLRRL 307
Cdd:COG0493 259 VVIGGGNTAMDcarTALRLG--AESVTIVYRRTREE-MPASKEEVEEalEEGVEFLFLVAPVEIIGDENGRVTGLECVRM 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 308 D---------------TGEETELEAKGLFYGIGHSPNSQLLEGQ--VELDSSGYVLVREGTSNTSVEGVFAAGDVQdhew 370
Cdd:COG0493 336 ElgepdesgrrrpvpiEGSEFTLPADLVILAIGQTPDPSGLEEElgLELDKRGTIVVDEETYQTSLPGVFAGGDAV---- 411
|
330 340
....*....|....*....|...
gi 18405775 371 RQA---VTAAGSGCIAALSAERY 390
Cdd:COG0493 412 RGPslvVWAIAEGRKAARAIDRY 434
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
86-365 |
9.59e-24 |
|
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: 104.01 E-value: 9.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 86 VVIIGSGPAGYTAAIYAARANLKPVVFEGYQMGG-------VP------GGQLMttTEVENFPGFpdGITG-------PD 145
Cdd:COG1249 6 LVVIGAGPGGYVAAIRAAQLGLKVALVEKGRLGGtclnvgcIPskallhAAEVA--HEARHAAEF--GISAgapsvdwAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 146 LMEKMRKQAERWgAELYPEDVESLSVT--------TAPFTVQ-TSERKVKCHSIIYATGATARRLRLP--REEEFW-SRG 213
Cdd:COG1249 82 LMARKDKVVDRL-RGGVEELLKKNGVDvirgrarfVDPHTVEvTGGETLTADHIVIATGSRPRVPPIPglDEVRVLtSDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 214 IsacaicdgaspLFKGQV---LAVVGGGDTATEEAlylTKYAR---HVHLLVRRDQL------RASKAMQDRVINNpNIT 281
Cdd:COG1249 161 A-----------LELEELpksLVVIGGGYIGLEFA---QIFARlgsEVTLVERGDRLlpgedpEISEALEKALEKE-GID 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 282 VHYNTETVDVlSNTKGqmsGILLRRLDTGEETELEAKGLFYGIGHSPNSQLL---EGQVELDSSGYVLVREgTSNTSVEG 358
Cdd:COG1249 226 ILTGAKVTSV-EKTGD---GVTVTLEDGGGEEAVEADKVLVATGRRPNTDGLgleAAGVELDERGGIKVDE-YLRTSVPG 300
|
....*..
gi 18405775 359 VFAAGDV 365
Cdd:COG1249 301 IYAIGDV 307
|
|
| TRX_family |
cd02947 |
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ... |
440-526 |
1.57e-23 |
|
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a TRX domain; and Group II, which are composed of fusion proteins of TRX and additional domains. Group I TRX is a small ancient protein that alter the redox state of target proteins via the reversible oxidation of an active site dithiol, present in a CXXC motif, partially exposed at the protein's surface. TRX reduces protein disulfide bonds, resulting in a disulfide bond at its active site. Oxidized TRX is converted to the active form by TRX reductase, using reducing equivalents derived from either NADPH or ferredoxins. By altering their redox state, TRX regulates the functions of at least 30 target proteins, some of which are enzymes and transcription factors. It also plays an important role in the defense against oxidative stress by directly reducing hydrogen peroxide and certain radicals, and by serving as a reductant for peroxiredoxins. At least two major types of functional TRXs have been reported in most organisms; in eukaryotes, they are located in the cytoplasm and the mitochondria. Higher plants contain more types (at least 20 TRX genes have been detected in the genome of Arabidopsis thaliana), two of which (types f amd m) are located in the same compartment, the chloroplast. Also included in the alignment are TRX-like domains which show sequence homology to TRX but do not contain the redox active CXXC motif. Group II proteins, in addition to either a redox active TRX or a TRX-like domain, also contain additional domains, which may or may not possess homology to known proteins.
Pssm-ID: 239245 [Multi-domain] Cd Length: 93 Bit Score: 94.55 E-value: 1.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 440 ESPRVILVLYTSPTCGPCRTLKPILNKVVDEYNhDVHFVEIDIEEDQEIAEAAGIMGTPCVQFFKNKEMLRTISGVKMKK 519
Cdd:cd02947 8 KSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYP-KVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRVVGADPKE 86
|
....*..
gi 18405775 520 EYREFIE 526
Cdd:cd02947 87 ELEEFLE 93
|
|
| thioredoxin |
TIGR01068 |
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ... |
440-529 |
3.57e-19 |
|
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of a domain closely related to thioredoxin. This model is designed to recognize authentic thioredoxin, a small protein that should be hit exactly once by this model. Any protein that hits once with a score greater than the second (per domain) trusted cutoff may be taken as thioredoxin. [Energy metabolism, Electron transport]
Pssm-ID: 200072 [Multi-domain] Cd Length: 101 Bit Score: 82.72 E-value: 3.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 440 ESPRVILVLYTSPTCGPCRTLKPILNKVVDEYNHDVHFVEIDIEEDQEIAEAAGIMGTPCVQFFKNKEMLRTISGVKMKK 519
Cdd:TIGR01068 12 SSDKPVLVDFWAPWCGPCKMIAPILEELAKEYEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNGKEVDRSVGALPKA 91
|
90
....*....|
gi 18405775 520 EYREFIEANK 529
Cdd:TIGR01068 92 ALKQLINKNL 101
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
86-365 |
8.90e-18 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 86.00 E-value: 8.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 86 VVIIGSGPAGYTAAIYAARANLKPVVFEGYQMGG-------VPGGQLMTTTEV----ENFPGF---PDGIT--GPDLMEK 149
Cdd:PRK06292 6 VIVIGAGPAGYVAARRAAKLGKKVALIEKGPLGGtclnvgcIPSKALIAAAEAfheaKHAEEFgihADGPKidFKKVMAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 150 MRKQAERWgAELYPEDVESLSVTT---------APFTVQTSERKVKCHSIIYATGatARRLRLPREEEFWSRGI--Saca 218
Cdd:PRK06292 86 VRRERDRF-VGGVVEGLEKKPKIDkikgtarfvDPNTVEVNGERIEAKNIVIATG--SRVPPIPGVWLILGDRLltS--- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 219 icDGAsplFKGQVL----AVVGGGDTATEEALYLTKYARHVHLLVRRDQL----------RASKAMQDRvinnpnITVHY 284
Cdd:PRK06292 160 --DDA---FELDKLpkslAVIGGGVIGLELGQALSRLGVKVTVFERGDRIlpledpevskQAQKILSKE------FKIKL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 285 NTETVDVlsnTKGQMSGILLRRLDtGEETELEAKGLFYGIGHSPNSQLL---EGQVELDSSGYVLVREGTSnTSVEGVFA 361
Cdd:PRK06292 229 GAKVTSV---EKSGDEKVEELEKG-GKTETIEADYVLVATGRRPNTDGLgleNTGIELDERGRPVVDEHTQ-TSVPGIYA 303
|
....
gi 18405775 362 AGDV 365
Cdd:PRK06292 304 AGDV 307
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
86-394 |
1.07e-15 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 79.45 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 86 VVIIGSGPAGYTAAIYAARANLKPVVFEGYQmggVPGGQLMTtteveNFPGF--PDGItgpdlmekMRKQAERwgaelyp 163
Cdd:PRK11749 143 VAVIGAGPAGLTAAHRLARKGYDVTIFEARD---KAGGLLRY-----GIPEFrlPKDI--------VDREVER------- 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 164 edVESLSVTtapF--------TVQTSERKVKCHSIIYATGATA-RRLRLPREE--------EFWSRGISACAicdgASPL 226
Cdd:PRK11749 200 --LLKLGVE---IrtntevgrDITLDELRAGYDAVFIGTGAGLpRFLGIPGENlggvysavDFLTRVNQAVA----DYDL 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 227 FKGQVLAVVGGGDTA-----TeeALYLTkyARHVHLLVRRDQ--LRASKAMQDRVINNpNITVHYNTETVDVLSNtKGQM 299
Cdd:PRK11749 271 PVGKRVVVIGGGNTAmdaarT--AKRLG--AESVTIVYRRGReeMPASEEEVEHAKEE-GVEFEWLAAPVEILGD-EGRV 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 300 SGILLRR--------------LDTGEETELEAKGLFYGIGHSPNSQLLEGQ--VELDSSGYVLVREGTSNTSVEGVFAAG 363
Cdd:PRK11749 345 TGVEFVRmelgepdasgrrrvPIEGSEFTLPADLVIKAIGQTPNPLILSTTpgLELNRWGTIIADDETGRTSLPGVFAGG 424
|
330 340 350
....*....|....*....|....*....|....
gi 18405775 364 DVQdhewRQA---VTAAGSGCIAALSAERYLTSN 394
Cdd:PRK11749 425 DIV----TGAatvVWAVGDGKDAAEAIHEYLEGA 454
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
86-392 |
7.29e-15 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 76.74 E-value: 7.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 86 VVIIGSGPAGYTAAIYAARANLKPVVFEGY-QMGGvpggqLMTTtevenfpGFPDGITGPDLMEKMRKQAERWGAELYPE 164
Cdd:PRK12810 146 VAVVGSGPAGLAAADQLARAGHKVTVFERAdRIGG-----LLRY-------GIPDFKLEKEVIDRRIELMEAEGIEFRTN 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 165 dveslsvTTAPFTVQTSERKVKCHSIIYATGAT-ARRLRLPREE--------EFWSRGISACAICDGASPL-FKGQVLAV 234
Cdd:PRK12810 214 -------VEVGKDITAEELLAEYDAVFLGTGAYkPRDLGIPGRDldgvhfamDFLIQNTRRVLGDETEPFIsAKGKHVVV 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 235 VGGGDTATE---EALYLTkyARHVHllvRRDQlrASKAMQDRVINNPNITV----------------HYNTETVDVLsNT 295
Cdd:PRK12810 287 IGGGDTGMDcvgTAIRQG--AKSVT---QRDI--MPMPPSRRNKNNPWPYWpmklevsnaheegverEFNVQTKEFE-GE 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 296 KGQMSGILLRRLD---------TGEETELEAKGLFYGIG--HSPNSQLLEGQVELDSSGYVLVREGTSNTSVEGVFAAGD 364
Cdd:PRK12810 359 NGKVTGVKVVRTElgegdfepvEGSEFVLPADLVLLAMGftGPEAGLLAQFGVELDERGRVAAPDNAYQTSNPKVFAAGD 438
|
330 340 350
....*....|....*....|....*....|.
gi 18405775 365 V---QDhewrQAVTAAGSGCIAALSAERYLT 392
Cdd:PRK12810 439 MrrgQS----LVVWAIAEGRQAARAIDAYLM 465
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
84-394 |
1.63e-14 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 75.82 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 84 ENVVIIGSGPAGYTAAIYAARANLKPVVFEGYQMggvPGGQLmttteVENFPGF---PDGITGPDLmEKMRKQaerwGAE 160
Cdd:PRK12831 141 KKVAVIGSGPAGLTCAGDLAKMGYDVTIFEALHE---PGGVL-----VYGIPEFrlpKETVVKKEI-ENIKKL----GVK 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 161 LYPEDVESLSVTtapftVQTSERKVKCHSIIYATGA-TARRLRLPRE--------EEFWSRGISACAICDG-ASPLFKGQ 230
Cdd:PRK12831 208 IETNVVVGKTVT-----IDELLEEEGFDAVFIGSGAgLPKFMGIPGEnlngvfsaNEFLTRVNLMKAYKPEyDTPIKVGK 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 231 VLAVVGGGDTATEEALYLTKYARHVHLLVRR--DQLRASK-----AMQDRVInnpnitVHYNTETVDVLSNTKGQMSGIL 303
Cdd:PRK12831 283 KVAVVGGGNVAMDAARTALRLGAEVHIVYRRseEELPARVeevhhAKEEGVI------FDLLTNPVEILGDENGWVKGMK 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 304 LRRLD---------------TGEETELEAKGLFYGIGHSPNSQLLEGQ--VELDSSGYVLVREGTSNTSVEGVFAAGDvq 366
Cdd:PRK12831 357 CIKMElgepdasgrrrpveiEGSEFVLEVDTVIMSLGTSPNPLISSTTkgLKINKRGCIVADEETGLTSKEGVFAGGD-- 434
|
330 340 350
....*....|....*....|....*....|....*
gi 18405775 367 dhewrqAVTAA-------GSGCIAALSAERYLTSN 394
Cdd:PRK12831 435 ------AVTGAatvilamGAGKKAAKAIDEYLSKK 463
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
137-365 |
8.48e-13 |
|
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: 69.45 E-value: 8.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 137 FPDGITGPD-LMEKMRKQAERWGAELYPED-VESlsvttapftVQTSERKVKCHS--------IIYATGATARRLRLPre 206
Cdd:COG0446 28 VGGGIKDPEdLLVRTPESFERKGIDVRTGTeVTA---------IDPEAKTVTLRDgetlsydkLVLATGARPRPPPIP-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 207 eefwsrGISACAIC-----DGASPL------FKGQVLAVVGGGDTATEEALYLTKYARHVHLLVRRDQL--RASKAMQDR 273
Cdd:COG0446 97 ------GLDLPGVFtlrtlDDADALrealkeFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLlgVLDPEMAAL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 274 VINN---PNITVHYNTETVDVLSNTKGQMsgillrRLDTGEEteLEAKGLFYGIGHSPNSQLLEG-QVELDSSGYVLVRE 349
Cdd:COG0446 171 LEEElreHGVELRLGETVVAIDGDDKVAV------TLTDGEE--IPADLVVVAPGVRPNTELAKDaGLALGERGWIKVDE 242
|
250
....*....|....*.
gi 18405775 350 gTSNTSVEGVFAAGDV 365
Cdd:COG0446 243 -TLQTSDPDVYAAGDC 257
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
93-363 |
9.69e-13 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 68.79 E-value: 9.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 93 PAGYTAAIYAARANLKP-VVFEGyqmgGVPG---------GQLMTTTEVENFPGFPD-----------------GITGPD 145
Cdd:pfam13738 1 PAGIGCAIALKKAGLEDyLILEK----GNIGnsfyrypthMTFFSPSFTSNGFGIPDlnaispgtspaftfnreHPSGNE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 146 LMEKMRKQAERWgaEL---YPEDVESLSVTTAPFTVQTSERKVKCHSIIYATGatarRLRLPREEEFWSRGISACAICDG 222
Cdd:pfam13738 77 YAEYLRRVADHF--ELpinLFEEVTSVKKEDDGFVVTTSKGTYQARYVIIATG----EFDFPNKLGVPELPKHYSYVKDF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 223 ASplFKGQVLAVVGGGDTATEEALYLTKYARHVHLLVRRDQLRASKAMQ------------DRVINNPNITVHYNTETVD 290
Cdd:pfam13738 151 HP--YAGQKVVVIGGYNSAVDAALELVRKGARVTVLYRGSEWEDRDSDPsyslspdtlnrlEELVKNGKIKAHFNAEVKE 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18405775 291 VlsntkGQMSGILLRRLDTGEETELEAKGLFYGIGHSPNSQLLEGQVELDSSGYVLVREGTSNTSVEGVFAAG 363
Cdd:pfam13738 229 I-----TEVDVSYKVHTEDGRKVTSNDDPILATGYHPDLSFLKKGLFELDEDGRPVLTEETESTNVPGLFLAG 296
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
233-368 |
5.71e-12 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 67.87 E-value: 5.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 233 AVVGGGDTATEEALYLTKYARHVHLLVRRDQ-LRA-----SKAMQDrVINNPNITVHYNTETVDVLSNTKGQmsgiLLRR 306
Cdd:PRK06116 171 AVVGAGYIAVEFAGVLNGLGSETHLFVRGDApLRGfdpdiRETLVE-EMEKKGIRLHTNAVPKAVEKNADGS----LTLT 245
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18405775 307 LDTGEEteLEAKGLFYGIGHSPNSQ---LLEGQVELDSSGYVLVREgTSNTSVEGVFAAGDVQDH 368
Cdd:PRK06116 246 LEDGET--LTVDCLIWAIGREPNTDglgLENAGVKLNEKGYIIVDE-YQNTNVPGIYAVGDVTGR 307
|
|
| trxA |
PRK09381 |
thioredoxin TrxA; |
444-528 |
7.83e-12 |
|
thioredoxin TrxA;
Pssm-ID: 181812 [Multi-domain] Cd Length: 109 Bit Score: 62.00 E-value: 7.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 444 VILVLYTSPTCGPCRTLKPILNKVVDEYNHDVHFVEIDIEEDQEIAEAAGIMGTPCVQFFKNKEMLRTISGVKMKKEYRE 523
Cdd:PRK09381 23 AILVDFWAEWCGPCKMIAPILDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKNGEVAATKVGALSKGQLKE 102
|
....*
gi 18405775 524 FIEAN 528
Cdd:PRK09381 103 FLDAN 107
|
|
| Thioredoxin |
pfam00085 |
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ... |
445-527 |
1.00e-11 |
|
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond. Some members with only the active site are not separated from the noise.
Pssm-ID: 395038 [Multi-domain] Cd Length: 103 Bit Score: 61.48 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 445 ILVLYTSPTCGPCRTLKPILNKVVDEYNHDVHFVEIDIEEDQEIAEAAGIMGTPCVQFFKNKEMLRTISGVKMKKEYREF 524
Cdd:pfam00085 21 VLVDFYAPWCGPCKMLAPEYEELAQEYKGNVVFAKVDVDENPDLASKYGVRGYPTLIFFKNGQPVDDYVGARPKDALAAF 100
|
...
gi 18405775 525 IEA 527
Cdd:pfam00085 101 LKA 103
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
232-299 |
1.12e-11 |
|
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: 60.68 E-value: 1.12e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18405775 232 LAVVGGGDTATEEALYLTKYARHVHLLVRRDQLR------ASKAMQDRVINNpNITVHYNTETVDVLSNTKGQM 299
Cdd:pfam00070 2 VVVVGGGYIGLELAGALARLGSKVTVVERRDRLLpgfdpeIAKILQEKLEKN-GIEFLLNTTVEAIEGNGDGVV 74
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
86-393 |
1.11e-10 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 63.08 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 86 VVIIGSGPAGYTAAIYAARANLKPVVfegYQMGGVPGGQLMTTtevenFPGF--PDgitgpdlmEKMR---KQAERWGAE 160
Cdd:PRK12770 21 VAIIGAGPAGLAAAGYLACLGYEVHV---YDKLPEPGGLMLFG-----IPEFriPI--------ERVRegvKELEEAGVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 161 LYP-------------------EDVESLsvttapftvqtsERKVKCH-SIIYATGA-TARRLRLPREEE----------F 209
Cdd:PRK12770 85 FHTrtkvccgeplheeegdefvERIVSL------------EELVKKYdAVLIATGTwKSRKLGIPGEDLpgvysaleylF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 210 WSRGISACAICDGASPLFKGQVLAVVGGGDTA---TEEALYLtkYARHVHLLVRR--DQLRASKAMQDRVINNpNITVHY 284
Cdd:PRK12770 153 RIRAAKLGYLPWEKVPPVEGKKVVVVGAGLTAvdaALEAVLL--GAEKVYLAYRRtiNEAPAGKYEIERLIAR-GVEFLE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 285 NTETVDVLSntKGQMSGILLRRLD---------------TGEETELEAKGLFYGIGHSPNS--QLLEGQVELDSSGYVLV 347
Cdd:PRK12770 230 LVTPVRIIG--EGRVEGVELAKMRlgepdesgrprpvpiPGSEFVLEADTVVFAIGEIPTPpfAKECLGIELNRKGEIVV 307
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 18405775 348 REgTSNTSVEGVFAAGDVQdHEWRQAVTAAGSGCIAALSAERYLTS 393
Cdd:PRK12770 308 DE-KHMTSREGVFAAGDVV-TGPSKIGKAIKSGLRAAQSIHEWLDL 351
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
85-365 |
2.02e-10 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 62.91 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 85 NVVIIGSGPAGYTAAIYAARANLKPVVFEGYQMGG--VPGGQLMTTTEVE-----------NFPGFP-DGITGPDL---M 147
Cdd:PRK06370 7 DAIVIGAGQAGPPLAARAAGLGMKVALIERGLLGGtcVNTGCVPTKTLIAsaraahlarraAEYGVSvGGPVSVDFkavM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 148 EKMRK--QAERWGAELYPEDVESLSVT------TAPFTVQTSERKVKCHSIIYATGATARRLRLPreeefwsrGISACAI 219
Cdd:PRK06370 87 ARKRRirARSRHGSEQWLRGLEGVDVFrgharfESPNTVRVGGETLRAKRIFINTGARAAIPPIP--------GLDEVGY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 220 CDGASPLFKGQV---LAVVGGGDTATEEAlylTKYAR---HVHLLVRRDQL------RASKAMQDrVINNPNITVHYNTE 287
Cdd:PRK06370 159 LTNETIFSLDELpehLVIIGGGYIGLEFA---QMFRRfgsEVTVIERGPRLlpredeDVAAAVRE-ILEREGIDVRLNAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 288 TVDVlsntKGQMSGILLRRLDTGEETELEAKGLFYGIGHSPNSQLL---EGQVELDSSGYVLVREgTSNTSVEGVFAAGD 364
Cdd:PRK06370 235 CIRV----ERDGDGIAVGLDCNGGAPEITGSHILVAVGRVPNTDDLgleAAGVETDARGYIKVDD-QLRTTNPGIYAAGD 309
|
.
gi 18405775 365 V 365
Cdd:PRK06370 310 C 310
|
|
| SoxW |
COG2143 |
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ... |
440-526 |
3.18e-10 |
|
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 441746 [Multi-domain] Cd Length: 146 Bit Score: 58.38 E-value: 3.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 440 ESPRVILVLYTSPTCGPCRTL-KPILN--KVVDEYNHDVHFVEIDIEEDQEI-------------AEAAGIMGTPCVQFF 503
Cdd:COG2143 38 AEGKPILLFFESDWCPYCKKLhKEVFSdpEVAAYLKENFVVVQLDAEGDKEVtdfdgetltekelARKYGVRGTPTLVFF 117
|
90 100
....*....|....*....|....*
gi 18405775 504 --KNKEMLRtISGVKMKKEYREFIE 526
Cdd:COG2143 118 daEGKEIAR-IPGYLKPETFLALLK 141
|
|
| PDI_a_family |
cd02961 |
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ... |
441-525 |
3.28e-10 |
|
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic proteins involved in oxidative protein folding in the endoplasmic reticulum (ER) by acting as catalysts and folding assistants. Members of this family include PDI and PDI-related proteins like ERp72, ERp57 (or ERp60), ERp44, P5, PDIR, ERp46 and the transmembrane PDIs. PDI, ERp57, ERp72, P5, PDIR and ERp46 are all oxidases, catalyzing the formation of disulfide bonds of newly synthesized polypeptides in the ER. They also exhibit reductase activity in acting as isomerases to correct any non-native disulfide bonds, as well as chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. These proteins usually contain multiple copies of a redox active TRX (a) domain containing a CXXC motif, and may also contain one or more redox inactive TRX-like (b) domains. Only one a domain is required for the oxidase function but multiple copies are necessary for the isomerase function. The different types of PDIs may show different substrate specificities and tissue-specific expression, or may be induced by stress. PDIs are in their reduced form at steady state and are oxidized to the active form by Ero1, which is localized in the ER through ERp44. Some members of this family also contain a DnaJ domain in addition to the redox active a domains; examples are ERdj5 and Pfj2. Also included in the family is the redox inactive N-terminal TRX-like domain of ERp29.
Pssm-ID: 239259 [Multi-domain] Cd Length: 101 Bit Score: 57.24 E-value: 3.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 441 SPRVILVLYTSPTCGPCRTLKPILNKVVDEYNHD--VHFVEIDIEEDQEIAEAAGIMGTPCVQFFKN-KEMLRTISGVKM 517
Cdd:cd02961 14 DSKDVLVEFYAPWCGHCKALAPEYEKLAKELKGDgkVVVAKVDCTANNDLCSEYGVRGYPTIKLFPNgSKEPVKYEGPRT 93
|
....*...
gi 18405775 518 KKEYREFI 525
Cdd:cd02961 94 LESLVEFI 101
|
|
| GrxC |
COG0695 |
Glutaredoxin [Posttranslational modification, protein turnover, chaperones]; |
446-500 |
1.10e-09 |
|
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440459 [Multi-domain] Cd Length: 74 Bit Score: 54.82 E-value: 1.10e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 18405775 446 LVLYTSPTCGPCRTLKPILNKvvdeynHDVHFVEIDIEED----QEIAEAAGIMGTPCV 500
Cdd:COG0695 2 VTLYTTPGCPYCARAKRLLDE------KGIPYEEIDVDEDpearEELRERSGRRTVPVI 54
|
|
| PRK10996 |
PRK10996 |
thioredoxin 2; Provisional |
445-514 |
1.34e-09 |
|
thioredoxin 2; Provisional
Pssm-ID: 182889 [Multi-domain] Cd Length: 139 Bit Score: 56.62 E-value: 1.34e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 445 ILVLYTSPTCGPCRTLKPILNKVVDEYNHDVHFVEIDIEEDQEIAEAAGIMGTPCVQFFKNKEMLRTISG 514
Cdd:PRK10996 55 VVIDFWAPWCGPCRNFAPIFEDVAAERSGKVRFVKVNTEAERELSARFRIRSIPTIMIFKNGQVVDMLNG 124
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
86-394 |
1.69e-09 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 60.53 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 86 VVIIGSGPAGYTAAIYAARANLKPVVFEGYQMggvPGGQLmttteVENFPGF--PDGITGPDLmekmrkqaerwgaelyp 163
Cdd:PRK12778 434 VAVIGSGPAGLSFAGDLAKRGYDVTVFEALHE---IGGVL-----KYGIPEFrlPKKIVDVEI----------------- 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 164 EDVESLSVT-----TAPFTVQTSE-RKVKCHSIIYATGA-TARRLRLPRE--------EEFWSR-GISACAICDGASPLF 227
Cdd:PRK12778 489 ENLKKLGVKfetdvIVGKTITIEElEEEGFKGIFIASGAgLPNFMNIPGEnsngvmssNEYLTRvNLMDAASPDSDTPIK 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 228 KGQVLAVVGGGDTATEE---ALYLTkyARHVHLLVRRDQLRASkAMQDRVINNPNITVHYNTET--VDVLSNTKGQMSGI 302
Cdd:PRK12778 569 FGKKVAVVGGGNTAMDSartAKRLG--AERVTIVYRRSEEEMP-ARLEEVKHAKEEGIEFLTLHnpIEYLADEKGWVKQV 645
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 303 LLRRLDTGE---------------ETELEAKGLFYGIGHSPNSQLLEG--QVELDSSGYVLVREGTSnTSVEGVFAAGDV 365
Cdd:PRK12778 646 VLQKMELGEpdasgrrrpvaipgsTFTVDVDLVIVSVGVSPNPLVPSSipGLELNRKGTIVVDEEMQ-SSIPGIYAGGDI 724
|
330 340 350
....*....|....*....|....*....|..
gi 18405775 366 QdhewRQAVT---AAGSGCIAALSAERYLTSN 394
Cdd:PRK12778 725 V----RGGATvilAMGDGKRAAAAIDEYLSSK 752
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
85-385 |
3.84e-09 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 59.01 E-value: 3.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 85 NVVIIGSGPAGYTAAIYAARANLKPVVFEGYQMGG-------VPGGQLMTTTEV----ENFPgFPDGI--TGPDLM-EKM 150
Cdd:PRK13748 100 HVAVIGSGGAAMAAALKAVEQGARVTLIERGTIGGtcvnvgcVPSKIMIRAAHIahlrRESP-FDGGIaaTVPTIDrSRL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 151 RKQAERWGAELYPEDVESLSVTTAPFTV----------QT--------SERKVKCHSIIYATGATARRLRLP--REEEFW 210
Cdd:PRK13748 179 LAQQQARVDELRHAKYEGILDGNPAITVlhgearfkddQTlivrlndgGERVVAFDRCLIATGASPAVPPIPglKETPYW 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 211 SrgiSACAICDGASPlfkgQVLAVVGGGDTATEEALYLTKYARHVHLLVRRDQL-RASKAMQDRVinnpniTVHYNTETV 289
Cdd:PRK13748 259 T---STEALVSDTIP----ERLAVIGSSVVALELAQAFARLGSKVTILARSTLFfREDPAIGEAV------TAAFRAEGI 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 290 DVLSNTKG----QMSGILLrrLDTGEeTELEAKGLFYGIGHSPNSQLLE---GQVELDSSGYVLVREGTsNTSVEGVFAA 362
Cdd:PRK13748 326 EVLEHTQAsqvaHVDGEFV--LTTGH-GELRADKLLVATGRAPNTRSLAldaAGVTVNAQGAIVIDQGM-RTSVPHIYAA 401
|
330 340
....*....|....*....|....
gi 18405775 363 GDVQDHEwrQAV-TAAGSGCIAAL 385
Cdd:PRK13748 402 GDCTDQP--QFVyVAAAAGTRAAI 423
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
86-391 |
5.00e-09 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 58.73 E-value: 5.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 86 VVIIGSGPAGYTAAIYAARANLKPVVFEGYQMggvPGGQLMTttevenfpgfpdGITGpdlmekMRKQAERWGAELypED 165
Cdd:PRK12771 140 VAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPK---LGGMMRY------------GIPA------YRLPREVLDAEI--QR 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 166 VESLSVTTAPFT-----VQTSERKVKCHSIIYATGA-TARRLRLPREEEfwSRGISAC----AICDGASPlFKGQVLAVV 235
Cdd:PRK12771 197 ILDLGVEVRLGVrvgedITLEQLEGEFDAVFVAIGAqLGKRLPIPGEDA--AGVLDAVdflrAVGEGEPP-FLGKRVVVI 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 236 GGGDTA-----------TEEALYLtkYARhvhllvRRDQLRASK-----AMQDRVinnpniTVHYNTETVDVLSNTKGQM 299
Cdd:PRK12771 274 GGGNTAmdaartarrlgAEEVTIV--YRR------TREDMPAHDeeieeALREGV------EINWLRTPVEIEGDENGAT 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 300 SGILLR----RLD--------TGEETELEAKGLFYGIGHSPNSQLLEGQVELDSS-GYVLVREGTSNTSVEGVFAAGDVQ 366
Cdd:PRK12771 340 GLRVITvekmELDedgrpspvTGEEETLEADLVVLAIGQDIDSAGLESVPGVEVGrGVVQVDPNFMMTGRPGVFAGGDMV 419
|
330 340
....*....|....*....|....*
gi 18405775 367 DHEwRQAVTAAGSGCIAALSAERYL 391
Cdd:PRK12771 420 PGP-RTVTTAIGHGKKAARNIDAFL 443
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
83-384 |
8.94e-09 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 58.11 E-value: 8.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 83 IENVVIIGSGPAGYTAAIYAARANLKPVVFE------GYQMGGVPGGQLMTTTEVENFPGFPD-------------GITG 143
Cdd:PRK12809 310 SEKVAVIGAGPAGLGCADILARAGVQVDVFDrhpeigGMLTFGIPPFKLDKTVLSQRREIFTAmgidfhlnceigrDITF 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 144 PDLMEKMrkQAERWGAELYPEDVESLSVTTAPFTVQtserkvkchSIIYATGATARRLRLPREEEFwsrgisacaicdga 223
Cdd:PRK12809 390 SDLTSEY--DAVFIGVGTYGMMRADLPHEDAPGVIQ---------ALPFLTAHTRQLMGLPESEEY-------------- 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 224 sPL--FKGQVLAVVGGGDTATE-EALYLTKYARHVHLLVRRDQLRASKAMQDrVIN--NPNITVHYNTETVDVLSNTKGQ 298
Cdd:PRK12809 445 -PLtdVEGKRVVVLGGGDTTMDcLRTSIRLNAASVTCAYRRDEVSMPGSRKE-VVNarEEGVEFQFNVQPQYIACDEDGR 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 299 MSGILLRRLDTGE---------------ETELEAKGLFYGIGHSPNSQ-LLEGQ-VELDSSGYVL---VREGTSNTSVEG 358
Cdd:PRK12809 523 LTAVGLIRTAMGEpgpdgrrrprpvagsEFELPADVLIMAFGFQAHAMpWLQGSgIKLDKWGLIQtgdVGYLPTQTHLKK 602
|
330 340
....*....|....*....|....*.
gi 18405775 359 VFAAGDVQdHEWRQAVTAAGSGCIAA 384
Cdd:PRK12809 603 VFAGGDAV-HGADLVVTAMAAGRQAA 627
|
|
| TRX_PICOT |
cd02984 |
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ... |
440-515 |
9.32e-09 |
|
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that interacts with protein kinase C (PKC) theta, a calcium independent PKC isoform selectively expressed in skeletal muscle and T lymphocytes. PICOT contains an N-terminal TRX-like domain, which does not contain the catalytic CXXC motif, followed by one to three glutaredoxin domains. The TRX-like domain is required for interaction with PKC theta. PICOT inhibits the activation of c-Jun N-terminal kinase and the transcription factors, AP-1 and NF-kB, induced by PKC theta or T-cell activating stimuli.
Pssm-ID: 239282 [Multi-domain] Cd Length: 97 Bit Score: 52.66 E-value: 9.32e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18405775 440 ESPRVILVLYTSPTCGPCRTLKPILNKVVDEYNHDVHFVEIDIEEDQEIAEAAGIMGTPCVQFFKNKEMLRTISGV 515
Cdd:cd02984 12 DASKLLVLHFWAPWAEPCKQMNQVFEELAKEAFPSVLFLSIEAEELPEISEKFEITAVPTFVFFRNGTIVDRVSGA 87
|
|
| TRX_superfamily |
cd01659 |
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ... |
446-510 |
9.82e-09 |
|
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include TRX, protein disulfide isomerase (PDI), tlpA-like, glutaredoxin, NrdH redoxin, and the bacterial Dsb (DsbA, DsbC, DsbG, DsbE, DsbDgamma) protein families. Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins and glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.
Pssm-ID: 238829 [Multi-domain] Cd Length: 69 Bit Score: 51.93 E-value: 9.82e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18405775 446 LVLYTSPTCGPCRTLKPILNKVVDEyNHDVHFVEIDIEEDQEIAEAA---GIMGTPCVQFFKNKEMLR 510
Cdd:cd01659 1 LVLFYAPWCPFCQALRPVLAELALL-NKGVKFEAVDVDEDPALEKELkryGVGGVPTLVVFGPGIGVK 67
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
84-365 |
1.00e-08 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 57.46 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 84 ENVVIIGSGPAGYTAAIYAARANlkpvvfegyqmggvPGGQLMTTTEvENFPGF-----PDGITGPDLMEKMRKQAERW- 157
Cdd:COG1251 2 MRIVIIGAGMAGVRAAEELRKLD--------------PDGEITVIGA-EPHPPYnrpplSKVLAGETDEEDLLLRPADFy 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 158 ---GAELYPED-VESLSvttapftvqTSERKVKCHS--------IIYATGATARRLRLP---REEEFWSRGISAC-AICD 221
Cdd:COG1251 67 eenGIDLRLGTrVTAID---------RAARTVTLADgetlpydkLVLATGSRPRVPPIPgadLPGVFTLRTLDDAdALRA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 222 GASPlfkGQVLAVVGGGDTATEEALYLTKYARHVHLLVRRDQL-------RASKAMQDRVINNpNITVHYNTETVDVLSN 294
Cdd:COG1251 138 ALAP---GKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLlprqldeEAGALLQRLLEAL-GVEVRLGTGVTEIEGD 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18405775 295 TKGqmSGIllrRLDTGEEteLEAKGLFYGIGHSPNSQLLEGqVELDSSGYVLVREgTSNTSVEGVFAAGDV 365
Cdd:COG1251 214 DRV--TGV---RLADGEE--LPADLVVVAIGVRPNTELARA-AGLAVDRGIVVDD-YLRTSDPDIYAAGDC 275
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
86-365 |
1.10e-08 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 57.56 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 86 VVIIGSGPAGYTAAIYAARANLKPVVFEGYQMGG-------VPGGQLMTTTEVEN-FPGFPD-GITGPD----------- 145
Cdd:PRK07845 4 IVIIGGGPGGYEAALVAAQLGADVTVIERDGLGGaavltdcVPSKTLIATAEVRTeLRRAAElGIRFIDdgearvdlpav 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 146 ---LMEKMRKQAERWGAELYPEDVESLS-------VTTAPFTVQT-----SERKVKCHSIIYATGATARRLrlpreeefw 210
Cdd:PRK07845 84 narVKALAAAQSADIRARLEREGVRVIAgrgrlidPGLGPHRVKVttadgGEETLDADVVLIATGASPRIL--------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 211 srgisACAICDGASPLFKGQV---------LAVVGGGDTATEEALYLTKYARHVHLLVRRDQ-LRASKAMQDRVINNPni 280
Cdd:PRK07845 155 -----PTAEPDGERILTWRQLydldelpehLIVVGSGVTGAEFASAYTELGVKVTLVSSRDRvLPGEDADAAEVLEEV-- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 281 tvhYNTETVDVLSNTKGQMsgilLRRLDTGEETELEAKGLFYG------IGHSPNSQ---LLEGQVELDSSGYVLVrEGT 351
Cdd:PRK07845 228 ---FARRGMTVLKRSRAES----VERTGDGVVVTLTDGRTVEGshalmaVGSVPNTAglgLEEAGVELTPSGHITV-DRV 299
|
330
....*....|....
gi 18405775 352 SNTSVEGVFAAGDV 365
Cdd:PRK07845 300 SRTSVPGIYAAGDC 313
|
|
| TrxA |
COG0526 |
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ... |
422-527 |
1.24e-08 |
|
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440292 [Multi-domain] Cd Length: 139 Bit Score: 53.54 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 422 DITLTKHKGQ-YALRKLyheSPRVILVLYTSPTCGPCRTLKPILNKVVDEYnHDVHFVEIDIEEDQE------------- 487
Cdd:COG0526 10 DFTLTDLDGKpLSLADL---KGKPVLVNFWATWCPPCRAEMPVLKELAEEY-GGVVFVGVDVDENPEavkaflkelglpy 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 18405775 488 ---------IAEAAGIMGTPCVQFF-KNKEMLRTISGVKMKKEYREFIEA 527
Cdd:COG0526 86 pvlldpdgeLAKAYGVRGIPTTVLIdKDGKIVARHVGPLSPEELEEALEK 135
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
86-261 |
1.41e-08 |
|
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: 56.79 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 86 VVIIGSGPAGYTAAIYAARANLKPVVFE-GYQMGGV------PGGQLMTTTEVENFPGFPDGITGPDLMEK------MRK 152
Cdd:COG2072 9 VVVIGAGQAGLAAAYHLRRAGIDFVVLEkADDVGGTwrdnryPGLRLDTPSHLYSLPFFPNWSDDPDFPTGdeilayLEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 153 QAERWGAE---LYPEDVESLSV--TTAPFTVQTSE-RKVKCHSIIYATGA--TARRLRLPREEEF---------Wsrgis 215
Cdd:COG2072 89 YADKFGLRrpiRFGTEVTSARWdeADGRWTVTTDDgETLTARFVVVATGPlsRPKIPDIPGLEDFageqlhsadW----- 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 18405775 216 acaicDGASPlFKGQVLAVVGGGDTATEEALYLTKYARHVHLLVRR 261
Cdd:COG2072 164 -----RNPVD-LAGKRVLVVGTGASAVQIAPELARVAAHVTVFQRT 203
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
81-394 |
1.86e-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: 57.26 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 81 EIIENVVIIGSGPAGYTAAIYAARANLKPVVFEGYQmggVPGGQLMTttevenfpGFPDGITGPDLMEKMRKQAERWGAE 160
Cdd:PRK12775 428 KKLGKVAICGSGPAGLAAAADLVKYGVDVTVYEALH---VVGGVLQY--------GIPSFRLPRDIIDREVQRLVDIGVK 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 161 lypedVESLSVTTAPFTVQTSERKVKCHSIIYATGATARR-LRLPRE--------EEFWSR----GISACAICDgaSPLF 227
Cdd:PRK12775 497 -----IETNKVIGKTFTVPQLMNDKGFDAVFLGVGAGAPTfLGIPGEfagqvysaNEFLTRvnlmGGDKFPFLD--TPIS 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 228 KGQVLAVVGGGDTATEeALYLTKY--ARHVHLLVRRDQLRASKAMQD-RVINNPNITVHYNTETVDVLSNTKGQMSGILL 304
Cdd:PRK12775 570 LGKSVVVIGAGNTAMD-CLRVAKRlgAPTVRCVYRRSEAEAPARIEEiRHAKEEGIDFFFLHSPVEIYVDAEGSVRGMKV 648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 305 RRLD--------------TGEETELEAKGLFYGIGHSPN---SQLLEGqVELDSSGYVLVREG----TSNTSVEGVFAAG 363
Cdd:PRK12775 649 EEMElgepdekgrrkpmpTGEFKDLECDTVIYALGTKANpiiTQSTPG-LALNKWGNIAADDGklesTQSTNLPGVFAGG 727
|
330 340 350
....*....|....*....|....*....|.
gi 18405775 364 DVQDHEwRQAVTAAGSGCIAALSAERYLTSN 394
Cdd:PRK12775 728 DIVTGG-ATVILAMGAGRRAARSIATYLRLG 757
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
86-365 |
2.23e-08 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 56.32 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 86 VVIIGSGPAGYTAAIYAARANLKPVVFEGYQM-GGV-------PGGQLMTTteVENFPGF-----------PDGITGPDL 146
Cdd:PRK05249 8 LVVIGSGPAGEGAAMQAAKLGKRVAVIERYRNvGGGcthtgtiPSKALREA--VLRLIGFnqnplyssyrvKLRITFADL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 147 M-----------EKMRKQAERWGAELYP-----EDVESLSVTTAPFTVQTserkVKCHSIIYATGATARRlrlPREEEFw 210
Cdd:PRK05249 86 LaradhvinkqvEVRRGQYERNRVDLIQgrarfVDPHTVEVECPDGEVET----LTADKIVIATGSRPYR---PPDVDF- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 211 srgiSACAICDGASPL---FKGQVLAVVGGGDTATEealyltkYAR-------HVHLLVRRDQLRA------SKAMQDRV 274
Cdd:PRK05249 158 ----DHPRIYDSDSILsldHLPRSLIIYGAGVIGCE-------YASifaalgvKVTLINTRDRLLSflddeiSDALSYHL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 275 INNpNITVHYNTETVDVlsntKGQMSGILLrRLDTGeeTELEAKGLFYGIGHSPNSQLLE----GqVELDSSGYVLVREg 350
Cdd:PRK05249 227 RDS-GVTIRHNEEVEKV----EGGDDGVIV-HLKSG--KKIKADCLLYANGRTGNTDGLNlenaG-LEADSRGQLKVNE- 296
|
330
....*....|....*
gi 18405775 351 TSNTSVEGVFAAGDV 365
Cdd:PRK05249 297 NYQTAVPHIYAVGDV 311
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
190-365 |
7.27e-08 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 54.82 E-value: 7.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 190 IIYATGATARRLRLPREEefwsRGISAcaicDGASPLFKGQVLAVV-GGGDTATEEALYLTKYARHVHLLVRR------- 261
Cdd:PLN02507 171 ILIATGSRAQRPNIPGKE----LAITS----DEALSLEELPKRAVVlGGGYIAVEFASIWRGMGATVDLFFRKelplrgf 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 262 -DQLRASKAmqdRVINNPNITVHYNTeTVDVLSNTKGqmsGILLRrLDTGEEteLEAKGLFYGIGHSPNSQLL---EGQV 337
Cdd:PLN02507 243 dDEMRAVVA---RNLEGRGINLHPRT-NLTQLTKTEG---GIKVI-TDHGEE--FVADVVLFATGRAPNTKRLnleAVGV 312
|
170 180
....*....|....*....|....*...
gi 18405775 338 ELDSSGYVLVREgTSNTSVEGVFAAGDV 365
Cdd:PLN02507 313 ELDKAGAVKVDE-YSRTNIPSIWAIGDV 339
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
85-377 |
8.82e-08 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 54.37 E-value: 8.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 85 NVVIIGSGPAGYTAAIYAARANLKPV-----------VF--EGYQmggVPGGQLMtttevenfpgfPDGITgPDLmekmR 151
Cdd:COG1252 3 RIVIVGGGFAGLEAARRLRKKLGGDAevtlidpnpyhLFqpLLPE---VAAGTLS-----------PDDIA-IPL----R 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 152 KQAERWGAELYPEDVESlsvttapftVQTSERKVKCHS---------IIyATGATARRLRLP--RE-----------EEF 209
Cdd:COG1252 64 ELLRRAGVRFIQGEVTG---------IDPEARTVTLADgrtlsydylVI-ATGSVTNFFGIPglAEhalplktledaLAL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 210 WSRGISACAICDGASPLfkgqVLAVVGGGDTATEEALYLTKYARHVHLL--VRRDQLR---------------------A 266
Cdd:COG1252 134 RERLLAAFERAERRRLL----TIVVVGGGPTGVELAGELAELLRKLLRYpgIDPDKVRitlveagprilpglgeklseaA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 267 SKAMQDRvinnpNITVHYNTETVDVlsnTKGQMsgillrRLDTGEEteLEAKGLFYGIGHSPNSQLLEGQVELDSSGYVL 346
Cdd:COG1252 210 EKELEKR-----GVEVHTGTRVTEV---DADGV------TLEDGEE--IPADTVIWAAGVKAPPLLADLGLPTDRRGRVL 273
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 18405775 347 VREGTSNTSVEGVFAAGD---VQDHE-----------WRQAVTAA 377
Cdd:COG1252 274 VDPTLQVPGHPNVFAIGDcaaVPDPDgkpvpktaqaaVQQAKVLA 318
|
|
| Glutaredoxin |
pfam00462 |
Glutaredoxin; |
447-506 |
2.93e-07 |
|
Glutaredoxin;
Pssm-ID: 425695 [Multi-domain] Cd Length: 60 Bit Score: 47.50 E-value: 2.93e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18405775 447 VLYTSPTCGPCRTLKPILNKvvdeynHDVHFVEIDIEED----QEIAEAAGIMGTPCVqFFKNK 506
Cdd:pfam00462 2 VLYTKPTCPFCKRAKRLLKS------LGVDFEEIDVDEDpeirEELKELSGWPTVPQV-FIDGE 58
|
|
| PTZ00051 |
PTZ00051 |
thioredoxin; Provisional |
444-514 |
5.39e-07 |
|
thioredoxin; Provisional
Pssm-ID: 173347 [Multi-domain] Cd Length: 98 Bit Score: 47.95 E-value: 5.39e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18405775 444 VILVLYTSPTCGPCRTLKPILNKVVDEYNhDVHFVEIDIEEDQEIAEAAGIMGTPCVQFFKNKEMLRTISG 514
Cdd:PTZ00051 20 LVIVDFYAEWCGPCKRIAPFYEECSKEYT-KMVFVKVDVDELSEVAEKENITSMPTFKVFKNGSVVDTLLG 89
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
86-392 |
8.19e-07 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 51.65 E-value: 8.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 86 VVIIGSGPAGYTAAIYAARANLKPVVFEGYQMggvPGGQLMtttevENFPGF--PDGITGPDL--MEKMrkqaerwGAEL 161
Cdd:PRK12814 196 VAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQ---AGGMMR-----YGIPRFrlPESVIDADIapLRAM-------GAEF 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 162 YPEDVESLSVTTApftvqtsERKVKCHSIIYATGAT-ARRLRLPREE-EFWSRGISACA-ICDGASPLFKGQVLaVVGGG 238
Cdd:PRK12814 261 RFNTVFGRDITLE-------ELQKEFDAVLLAVGAQkASKMGIPGEElPGVISGIDFLRnVALGTALHPGKKVV-VIGGG 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 239 DTATE---EALYLTkyARHVHLLVRR--DQLRASKAMQDRVINNpNITVHYNTETVDVLSNTKG-QMSGILL-------- 304
Cdd:PRK12814 333 NTAIDaarTALRLG--AESVTILYRRtrEEMPANRAEIEEALAE-GVSLRELAAPVSIERSEGGlELTAIKMqqgepdes 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 305 -RRLDT---GEETELEAKGLFYGIGHSPNSQLLEGQ-VELDSSGYVLVREGTSNTSVEGVFAAGDV---QDhewrQAVTA 376
Cdd:PRK12814 410 gRRRPVpveGSEFTLQADTVISAIGQQVDPPIAEAAgIGTSRNGTVKVDPETLQTSVAGVFAGGDCvtgAD----IAINA 485
|
330
....*....|....*.
gi 18405775 377 AGSGCIAALSAERYLT 392
Cdd:PRK12814 486 VEQGKRAAHAIDLFLN 501
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
232-365 |
2.72e-06 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 49.95 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 232 LAVVGGGDTATEEALYLTKYARHVHLLVRRDQL----------RASKAMQDRVinnpniTVHYNTETVDVlsNTKGqmSG 301
Cdd:PRK07846 169 LVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRLlrhldddiseRFTELASKRW------DVRLGRNVVGV--SQDG--SG 238
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18405775 302 ILLRrLDTGeeTELEAKGLFYGIGHSPNSQLLE---GQVELDSSGYVLVREgTSNTSVEGVFAAGDV 365
Cdd:PRK07846 239 VTLR-LDDG--STVEADVLLVATGRVPNGDLLDaaaAGVDVDEDGRVVVDE-YQRTSAEGVFALGDV 301
|
|
| PTZ00102 |
PTZ00102 |
disulphide isomerase; Provisional |
444-507 |
2.76e-06 |
|
disulphide isomerase; Provisional
Pssm-ID: 240266 [Multi-domain] Cd Length: 477 Bit Score: 49.75 E-value: 2.76e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18405775 444 VILVLYTSPTCGPCRTLKPILNKV---VDEYNHDVHFVEIDIEEDQEIAEAAGIMGTPCVQFFKNKE 507
Cdd:PTZ00102 51 IVLVKFYAPWCGHCKRLAPEYKKAakmLKEKKSEIVLASVDATEEMELAQEFGVRGYPTIKFFNKGN 117
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
221-364 |
3.28e-06 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 49.61 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 221 DGASPLFKGQVLAVVGGGDTATEEALYLTKYARHVHLLVRR-------DQLRASKAMQDRVINNPNITVHYNTETVdvls 293
Cdd:PTZ00058 229 DDFFKIKEAKRIGIAGSGYIAVELINVVNRLGAESYIFARGnrllrkfDETIINELENDMKKNNINIITHANVEEI---- 304
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18405775 294 nTKGQMSGILLRRLDTGEETELEAkgLFYGIGHSPNSQLL--EGQVELDSSGYVLVrEGTSNTSVEGVFAAGD 364
Cdd:PTZ00058 305 -EKVKEKNLTIYLSDGRKYEHFDY--VIYCVGRSPNTEDLnlKALNIKTPKGYIKV-DDNQRTSVKHIYAVGD 373
|
|
| ybbN |
cd02956 |
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ... |
445-505 |
3.48e-06 |
|
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like domain. Its gene has been sequenced from several gammaproteobacteria and actinobacteria.
Pssm-ID: 239254 [Multi-domain] Cd Length: 96 Bit Score: 45.34 E-value: 3.48e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18405775 445 ILVLYTSPTCGPCRTLKPILNKVVDEYNHDVHFVEIDIEEDQEIAEAAGIMGTPCVQFFKN 505
Cdd:cd02956 15 VVVDFWAPRSPPSKELLPLLERLAEEYQGQFVLAKVNCDAQPQIAQQFGVQALPTVYLFAA 75
|
|
| TRX_GRX_like |
cd02973 |
Thioredoxin (TRX)-Glutaredoxin (GRX)-like family; composed of archaeal and bacterial proteins ... |
444-502 |
7.19e-06 |
|
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: 43.71 E-value: 7.19e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 18405775 444 VILVLYTSPTCGPCRTLKPILNKVVdEYNHDVHFVEIDIEEDQEIAEAAGIMGTPCVQF 502
Cdd:cd02973 1 VNIEVFVSPTCPYCPDAVQAANRIA-ALNPNISAEMIDAAEFPDLADEYGVMSVPAIVI 58
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
86-365 |
1.29e-05 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 47.83 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 86 VVIIGSGPAGYTAAIYAARANLKPVVFEGYQMGGV-------P-------GGQLMTTTEVENFpgfpdGIT----GPDlM 147
Cdd:PRK06416 7 VIVIGAGPGGYVAAIRAAQLGLKVAIVEKEKLGGTclnrgciPskallhaAERADEARHSEDF-----GIKaenvGID-F 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 148 EKMRKQAERWGAELYpEDVESL----SVT--------TAPFTVQ----TSERKVKCHSIIYATGATARRL---------- 201
Cdd:PRK06416 81 KKVQEWKNGVVNRLT-GGVEGLlkknKVDiirgeaklVDPNTVRvmteDGEQTYTAKNIILATGSRPRELpgieidgrvi 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 202 ----------RLPREeefwsrgisacaicdgasplfkgqvLAVVGGGDTATEEALYLTKYARHV-------HLL------ 258
Cdd:PRK06416 160 wtsdealnldEVPKS-------------------------LVVIGGGYIGVEFASAYASLGAEVtivealpRILpgedke 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 259 ----VRRdQLRA------SKAMQDRVI-NNPNITVHYNtetvdvlsntkgqmsgillrrlDTGEETELEAKGLFYGIGHS 327
Cdd:PRK06416 215 isklAER-ALKKrgikikTGAKAKKVEqTDDGVTVTLE----------------------DGGKEETLEADYVLVAVGRR 271
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 18405775 328 PNSQL--LEGQ-VELDsSGYVLVREgTSNTSVEGVFAAGDV 365
Cdd:PRK06416 272 PNTENlgLEELgVKTD-RGFIEVDE-QLRTNVPNIYAIGDI 310
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
86-137 |
2.56e-05 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 46.77 E-value: 2.56e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 18405775 86 VVIIGSGPAGYTAAIYAARANLKPVVFEgyqMGGVPGGqLMTTTEvenFPGF 137
Cdd:COG1233 6 VVVIGAGIGGLAAAALLARAGYRVTVLE---KNDTPGG-RARTFE---RPGF 50
|
|
| COG2509 |
COG2509 |
FAD-dependent dehydrogenase [General function prediction only]; |
86-113 |
2.82e-05 |
|
FAD-dependent dehydrogenase [General function prediction only];
Pssm-ID: 441999 [Multi-domain] Cd Length: 466 Bit Score: 46.64 E-value: 2.82e-05
10 20
....*....|....*....|....*...
gi 18405775 86 VVIIGSGPAGYTAAIYAARANLKPVVFE 113
Cdd:COG2509 33 VVIVGAGPAGLFAALELAEAGLKPLVLE 60
|
|
| NrdH |
cd02976 |
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ... |
446-498 |
4.48e-05 |
|
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active CXXC motif within a TRX fold, characterized by a glutaredoxin (GRX)-like sequence and TRX-like activity profile. In vitro, it displays protein disulfide reductase activity that is dependent on TRX reductase, not glutathione (GSH). It is part of the NrdHIEF operon, where NrdEF codes for class Ib ribonucleotide reductase (RNR-Ib), an efficient enzyme at low oxygen levels. Under these conditions when GSH is mostly conjugated to spermidine, NrdH can still function and act as a hydrogen donor for RNR-Ib. It has been suggested that the NrdHEF system may be the oldest RNR reducing system, capable of functioning in a microaerophilic environment, where GSH was not yet available. NrdH from Corynebacterium ammoniagenes can form domain-swapped dimers, although it is unknown if this happens in vivo. Domain-swapped dimerization, which results in the blocking of the TRX reductase binding site, could be a mechanism for regulating the oxidation state of the protein.
Pssm-ID: 239274 [Multi-domain] Cd Length: 73 Bit Score: 41.83 E-value: 4.48e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 18405775 446 LVLYTSPTCGPCRTLKPILNKvvdeynHDVHFVEIDIEEDQEIAEA----AGIMGTP 498
Cdd:cd02976 2 VTVYTKPDCPYCKATKRFLDE------RGIPFEEVDVDEDPEALEElkklNGYRSVP 52
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
86-365 |
4.73e-05 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 46.07 E-value: 4.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 86 VVIIGSGPAGYTAAIYAARANLKPVVFEGY-------QMGG-------VPGGQLMTTTE-VEN----FPGFpdGITGPDL 146
Cdd:PRK06327 7 VVVIGAGPGGYVAAIRAAQLGLKVACIEAWknpkgkpALGGtclnvgcIPSKALLASSEeFENaghhFADH--GIHVDGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 147 ---MEKM--RK----QAERWG----------------AELYPEDVESLSVTTApftvQTSERKVKCHSIIYATGATARRL 201
Cdd:PRK06327 85 kidVAKMiaRKdkvvKKMTGGieglfkknkitvlkgrGSFVGKTDAGYEIKVT----GEDETVITAKHVIIATGSEPRHL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 202 R-LPREEEfwsrgisacAICDGASPLFKGQV---LAVVGGG--------------------------------DTATEEA 245
Cdd:PRK06327 161 PgVPFDNK---------IILDNTGALNFTEVpkkLAVIGAGviglelgsvwrrlgaevtilealpaflaaadeQVAKEAA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 246 LYLTKYARHVHLLVRRDQLRASKAmqdrvinnpNITVHYNTetvdvlsntkgqmsgillrrlDTGEETELEAKGLFYGIG 325
Cdd:PRK06327 232 KAFTKQGLDIHLGVKIGEIKTGGK---------GVSVAYTD---------------------ADGEAQTLEVDKLIVSIG 281
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 18405775 326 HSPNSQLLEGQ---VELDSSGYVLVrEGTSNTSVEGVFAAGDV 365
Cdd:PRK06327 282 RVPNTDGLGLEavgLKLDERGFIPV-DDHCRTNVPNVYAIGDV 323
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
86-125 |
4.90e-05 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 45.68 E-value: 4.90e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 18405775 86 VVIIGSGPAGYTAAIYAARANLKPVVFEGYqmgGVPGGQL 125
Cdd:pfam12831 2 VVVVGGGPAGVAAAIAAARAGAKVLLVERR---GFLGGML 38
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
85-135 |
5.93e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 45.65 E-value: 5.93e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 18405775 85 NVVIIGSGPAGYTAAIYAARANLKPVVFEGyqmGGVPGGqLMTTTEVENFP 135
Cdd:PRK07233 1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEA---DDQLGG-LAASFEFGGLP 47
|
|
| GlrX_YruB |
TIGR02196 |
Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the ... |
447-500 |
6.60e-05 |
|
Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the conserved CxxC motif and includes the Clostridium pasteurianum protein YruB which has been cloned from a rubredoxin operon. Somewhat related to NrdH, it is unknown whether this protein actually interacts with glutathione/glutathione reducatase, or, like NrdH, some other reductant system.
Pssm-ID: 274027 [Multi-domain] Cd Length: 74 Bit Score: 41.21 E-value: 6.60e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 18405775 447 VLYTSPTCGPCRTLKPILNKvvdeynHDVHFVEIDIEED----QEIAEAAGIMGTPCV 500
Cdd:TIGR02196 3 KVYTTPWCPPCVKAKEYLTS------KGVAFEEIDVEKDaaarEELLKVYGQRGVPVI 54
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
86-195 |
6.62e-05 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 45.26 E-value: 6.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 86 VVIIGSGPAGYTAAIYAARANLKPVVFEGyqmGGVPGGQLMTT-----------TEVENF----PG-------------- 136
Cdd:pfam03486 3 VIVIGGGAAGLMAAISAAKRGRRVLLIEK---GKKLGRKILISgggrcnvtnlsEEPDNFlsryPGnpkflksalsrftp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 137 ----------------------FPDGITGPDLMEKMRKQAERWGAELYPE-DVESLSVTT-APFTVQTSERKVKCHSIIY 192
Cdd:pfam03486 80 wdfiaffeslgvplkeedhgrlFPDSDKASDIVDALLNELKELGVKIRLRtRVLSVEKDDdGRFRVKTGGEELEADSLVL 159
|
...
gi 18405775 193 ATG 195
Cdd:pfam03486 160 ATG 162
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
86-148 |
7.62e-05 |
|
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 440845 [Multi-domain] Cd Length: 443 Bit Score: 45.21 E-value: 7.62e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18405775 86 VVIIGSGPAGYTAAIYAARANLKPVVFEGyqmGGVPGGqLMTTTEVENFP--GFPDGI--TGPDLME 148
Cdd:COG1232 4 VAVIGGGIAGLTAAYRLAKAGHEVTVLEA---SDRVGG-LIRTVEVDGFRidRGPHSFltRDPEVLE 66
|
|
| PDI_a_PDIR |
cd02997 |
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ... |
419-525 |
9.87e-05 |
|
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide Isomerase Related). PDIR is composed of three redox active TRX (a) domains and an N-terminal redox inactive TRX-like (b) domain. Similar to PDI, it is involved in oxidative protein folding in the endoplasmic reticulum (ER) through its isomerase and chaperone activities. These activities are lower compared to PDI, probably due to PDIR acting only on a subset of proteins. PDIR is preferentially expressed in cells actively secreting proteins and its expression is induced by stress. Similar to PDI, the isomerase and chaperone activities of PDIR are independent; CXXC mutants lacking isomerase activity retain chaperone activity.
Pssm-ID: 239295 [Multi-domain] Cd Length: 104 Bit Score: 41.53 E-value: 9.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 419 EKFDITLTKHKGqyalrklyhesprvILVLYTSPTCGPCRTLKPILNKVVDEYNHDVHFV--EIDIEEDQE--IAEAAGI 494
Cdd:cd02997 8 EDFRKFLKKEKH--------------VLVMFYAPWCGHCKKMKPEFTKAATELKEDGKGVlaAVDCTKPEHdaLKEEYNV 73
|
90 100 110
....*....|....*....|....*....|.
gi 18405775 495 MGTPCVQFFKNKEMLRTISGVKMKKEYREFI 525
Cdd:cd02997 74 KGFPTFKYFENGKFVEKYEGERTAEDIIEFM 104
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
228-367 |
1.29e-04 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 44.48 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 228 KGQVLAVVGGGDTATEEALYLTKYARHVHLLVRRDQ-LRA-SKAMQDRVINNPN---ITVHYNTETVDVLSNTKGQMSgi 302
Cdd:PLN02546 251 KPEKIAIVGGGYIALEFAGIFNGLKSDVHVFIRQKKvLRGfDEEVRDFVAEQMSlrgIEFHTEESPQAIIKSADGSLS-- 328
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18405775 303 llrrLDTGEETELEAKGLFYGIGHSPNSQ---LLEGQVELDSSGYVLVREgTSNTSVEGVFAAGDVQD 367
Cdd:PLN02546 329 ----LKTNKGTVEGFSHVMFATGRKPNTKnlgLEEVGVKMDKNGAIEVDE-YSRTSVPSIWAVGDVTD 391
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
86-175 |
1.51e-04 |
|
FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.
Pssm-ID: 395718 [Multi-domain] Cd Length: 398 Bit Score: 44.20 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 86 VVIIGSGPAGYTAAIYAARANLKPVVFEGyqmGGVPGGQL------MttteveNFPGF-PDGitGPDLMEKMRKQAERWG 158
Cdd:pfam00890 2 VLVIGGGLAGLAAALAAAEAGLKVAVVEK---GQPFGGATawssggI------DALGNpPQG--GIDSPELHPTDTLKGL 70
|
90
....*....|....*..
gi 18405775 159 AELYPEDVESLSVTTAP 175
Cdd:pfam00890 71 DELADHPYVEAFVEAAP 87
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
86-119 |
1.79e-04 |
|
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: 44.05 E-value: 1.79e-04
10 20 30
....*....|....*....|....*....|....*
gi 18405775 86 VVIIGSGPAGYTAAIYAARANLKPVVFE-GYQMGG 119
Cdd:COG1053 6 VVVVGSGGAGLRAALEAAEAGLKVLVLEkVPPRGG 40
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
234-371 |
2.12e-04 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 43.62 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 234 VVGGGDTATEEALYLTKYARHVHLLVRRDQLraSKAMqDRVINNP--------NITVHYNTETVDVLSNTKGQMSGILlr 305
Cdd:PRK13512 153 VVGAGYISLEVLENLYERGLHPTLIHRSDKI--NKLM-DADMNQPildeldkrEIPYRLNEEIDAINGNEVTFKSGKV-- 227
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18405775 306 rldtgEETELeakgLFYGIGHSPNSQLLEG-QVELDSSGYVLVREgTSNTSVEGVFAAGDVQDHEWR 371
Cdd:PRK13512 228 -----EHYDM----IIEGVGTHPNSKFIESsNIKLDDKGFIPVND-KFETNVPNIYAIGDIITSHYR 284
|
|
| ER_PDI_fam |
TIGR01130 |
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ... |
419-505 |
3.48e-04 |
|
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide isomerases retained in the endoplasmic reticulum (ER) and closely related forms. Some members have been assigned alternative or additional functions such as prolyl 4-hydroxylase and dolichyl-diphosphooligosaccharide-protein glycotransferase. Members of this family have at least two protein-disulfide domains, each similar to thioredoxin but with the redox-active disulfide in the motif PWCGHCK, and an ER retention signal at the extreme C-terminus (KDEL, HDEL, and similar motifs).
Pssm-ID: 273457 [Multi-domain] Cd Length: 462 Bit Score: 43.12 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 419 EKFDITLTKHKgqyalrklyhesprVILVLYTSPTCGPCRTLKPILNKVVDEY---NHDVHFVEIDIEEDQEIAEAAGIM 495
Cdd:TIGR01130 9 DNFDDFIKSHE--------------FVLVEFYAPWCGHCKSLAPEYEKAADELkkkGPPIKLAKVDATEEKDLAQKYGVS 74
|
90
....*....|
gi 18405775 496 GTPCVQFFKN 505
Cdd:TIGR01130 75 GYPTLKIFRN 84
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
88-135 |
3.79e-04 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 38.67 E-value: 3.79e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 18405775 88 IIGSGPAGYTAAIYAARANLKPVVFEgyqMGGVPGGQlMTTTEVENFP 135
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLE---KRDRLGGN-AYSYRVPGYV 44
|
|
| GRX_family |
cd02066 |
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ... |
447-507 |
5.39e-04 |
|
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, as well as E. coli GRX1 and GRX3, which are members of this family. E. coli GRX2, however, is a 24-kDa protein that belongs to the GSH S-transferase (GST) family.
Pssm-ID: 239017 [Multi-domain] Cd Length: 72 Bit Score: 38.60 E-value: 5.39e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18405775 447 VLYTSPTCGPCRTLKPILNKvvdeynHDVHFVEIDIEEDQEI-AEAAGIMGTPCV-QFFKNKE 507
Cdd:cd02066 3 VVFSKSTCPYCKRAKRLLES------LGIEFEEIDILEDGELrEELKELSGWPTVpQIFINGE 59
|
|
| PDI_a_ERdj5_C |
cd03004 |
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ... |
446-507 |
5.56e-04 |
|
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a protein containing an N-terminal DnaJ domain and four redox active TRX domains. This subfamily is composed of the three TRX domains located at the C-terminal half of the protein. ERdj5 is a ubiquitous protein localized in the endoplasmic reticulum (ER) and is abundant in secretory cells. It's transcription is induced during ER stress. It interacts with BiP through its DnaJ domain in an ATP-dependent manner. BiP, an ER-resident member of the Hsp70 chaperone family, functions in ER-associated degradation and protein translocation. Also included in the alignment is the single complete TRX domain of an uncharacterized protein from Tetraodon nigroviridis, which also contains a DnaJ domain at its N-terminus.
Pssm-ID: 239302 [Multi-domain] Cd Length: 104 Bit Score: 39.58 E-value: 5.56e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18405775 446 LVLYTSPTCGPCRTLKPILNKVVDEYNHDVHFVEIDIEEDQEIAEAAGIMGTPCVQFFKNKE 507
Cdd:cd03004 23 LVDFYAPWCGPCQALLPELRKAARALKGKVKVGSVDCQKYESLCQQANIRAYPTIRLYPGNA 84
|
|
| TIGR00275 |
TIGR00275 |
flavoprotein, HI0933 family; The model when searched with a partial length search brings in ... |
87-195 |
7.10e-04 |
|
flavoprotein, HI0933 family; The model when searched with a partial length search brings in proteins with a dinucleotide-binding motif (Rossman fold) over the initial 40 residues of the model, including oxidoreductases and dehydrogenases. Partially characterized members include an FAD-binding protein from Bacillus cereus and flavoprotein HI0933 from Haemophilus influenzae. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 272992 [Multi-domain] Cd Length: 400 Bit Score: 42.20 E-value: 7.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 87 VIIGSGPAGYTAAIYAARANLKPVVFEGYQMGG----VPGG-------QLMTTTEVENFPGfpdgitGPDLMEKMRKQ-- 153
Cdd:TIGR00275 1 IIIGGGAAGLMAAITAARAGLSVLLLEKNKKIGkkllISGGgrcnltnSCPTPEFVAYYPR------NGKFLRSALSRfs 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 154 -------AERWGAELYPED----------------------------------VESLSVTTAPFTVQTSERKVKCHSIIY 192
Cdd:TIGR00275 75 nkdlidfFESLGLELKVEEdgrvfpcsdsaadvldallnelkelgveiltnskVKSIEKEDGGFGVETSGGEYEADKVII 154
|
...
gi 18405775 193 ATG 195
Cdd:TIGR00275 155 ATG 157
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
86-206 |
9.48e-04 |
|
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: 41.15 E-value: 9.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 86 VVIIGSGPAGYTAAIYAARANLKPVVFE-----GYQM--GGVPGGQLM-----------------------TTTEVENFP 135
Cdd:TIGR02032 3 VVVVGAGPAGASAAYRLADKGLRVLLLEkksfpRYKPcgGALSPRALEeldlpgelivnlvrgarffspngDSVEIPIET 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18405775 136 GFPDGITGPDLMEKMRKQAERWGAELYpEDVESLSVT----TAPFTVQTSERKVKCHSIIYATGA---TARRLRLPRE 206
Cdd:TIGR02032 83 ELAYVIDRDAFDEQLAERAQEAGAELR-LGTRVLDVEihddRVVVIVRGSEGTVTAKIVIGADGSrsiVAKKLGLKKE 159
|
|
| PDI_a_TMX3 |
cd03000 |
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ... |
446-524 |
1.01e-03 |
|
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX related transmembrane protein containing one redox active TRX domain at the N-terminus and a classical ER retrieval sequence for type I transmembrane proteins at the C-terminus. The TMX3 transcript is found in a variety of tissues with the highest levels detected in skeletal muscle and the heart. In vitro, TMX3 showed oxidase activity albeit slightly lower than that of protein disulfide isomerase.
Pssm-ID: 239298 [Multi-domain] Cd Length: 104 Bit Score: 38.59 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 446 LVLYTSPTCGPCRTLKPILNKVVDE---YNHDVHFVEIDIEEDQEIAEAAGIMGTPCVQFFKNkEMLRTISGVKMKKEYR 522
Cdd:cd03000 19 LVDFYAPWCGHCKKLEPVWNEVGAElksSGSPVRVGKLDATAYSSIASEFGVRGYPTIKLLKG-DLAYNYRGPRTKDDIV 97
|
..
gi 18405775 523 EF 524
Cdd:cd03000 98 EF 99
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
85-114 |
1.26e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 41.41 E-value: 1.26e-03
10 20 30
....*....|....*....|....*....|
gi 18405775 85 NVVIIGSGPAGYTAAIYAARANLKPVVFEG 114
Cdd:PRK07208 6 SVVIIGAGPAGLTAAYELLKRGYPVTVLEA 35
|
|
| PDI_a_ERp46 |
cd03005 |
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ... |
446-507 |
2.03e-03 |
|
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident protein containing three redox active TRX domains. Yeast complementation studies show that ERp46 can substitute for protein disulfide isomerase (PDI) function in vivo. It has been detected in many tissues, however, transcript and protein levels do not correlate in all tissues, suggesting regulation at a posttranscriptional level. An identical protein, named endoPDI, has been identified as an endothelial PDI that is highly expressed in the endothelium of tumors and hypoxic lesions. It has a protective effect on cells exposed to hypoxia.
Pssm-ID: 239303 [Multi-domain] Cd Length: 102 Bit Score: 37.65 E-value: 2.03e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18405775 446 LVLYTSPTCGPCRTLKPILNKVVDEYNH---DVHFVEIDIEEDQEIAEAAGIMGTPCVQFFKNKE 507
Cdd:cd03005 20 FVKFFAPWCGHCKRLAPTWEQLAKKFNNenpSVKIAKVDCTQHRELCSEFQVRGYPTLLLFKDGE 84
|
|
| PDI_a_P5 |
cd03001 |
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ... |
440-507 |
2.75e-03 |
|
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related protein with a domain structure of aa'b (where a and a' are redox active TRX domains and b is a redox inactive TRX-like domain). Like PDI, P5 is located in the endoplasmic reticulum (ER) and displays both isomerase and chaperone activities, which are independent of each other. Compared to PDI, the isomerase and chaperone activities of P5 are lower. The first cysteine in the CXXC motif of both redox active domains in P5 is necessary for isomerase activity. The P5 gene was first isolated as an amplified gene from a hydroxyurea-resistant hamster cell line. The zebrafish P5 homolog has been implicated to play a critical role in establishing left/right asymmetries in the embryonic midline. Some members of this subfamily are P5-like proteins containing only one redox active TRX domain.
Pssm-ID: 239299 [Multi-domain] Cd Length: 103 Bit Score: 37.27 E-value: 2.75e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18405775 440 ESPRVILVLYTSPTCGPCRTLKPILNKVVDEYNHDVHFVEIDIEEDQEIAEAAGIMGTPCVQFF-KNKE 507
Cdd:cd03001 16 NSDDVWLVEFYAPWCGHCKNLAPEWKKAAKALKGIVKVGAVDADVHQSLAQQYGVRGFPTIKVFgAGKN 84
|
|
| DsbG |
COG1651 |
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ... |
444-492 |
2.97e-03 |
|
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 441257 [Multi-domain] Cd Length: 152 Bit Score: 38.44 E-value: 2.97e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 18405775 444 VILVLYTSPTCGPCRTLKPILNKVVDEY-NHDVHFVEIDI----EEDQEIAEAA 492
Cdd:COG1651 2 VTVVEFFDYQCPYCARFHPELPELLKKYvDGKVRVVYRPFpllhPDSLRAARAA 55
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
189-365 |
3.35e-03 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 40.12 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 189 SIIYATGATARRLRLP----REEEFWSRGISACAicdgASPlfkgQVLAVVGGGDTATEEA-LY------LTKYARHVHL 257
Cdd:PRK07251 121 TIVINTGAVSNVLPIPgladSKHVYDSTGIQSLE----TLP----ERLGIIGGGNIGLEFAgLYnklgskVTVLDAASTI 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18405775 258 LVRRDQLRAskAMQDRVINNPNITVHYNTeTVDVLSNTKGQMsgillrrLDTGEETELEAKGLFYGIGHSPNS---QLLE 334
Cdd:PRK07251 193 LPREEPSVA--ALAKQYMEEDGITFLLNA-HTTEVKNDGDQV-------LVVTEDETYRFDALLYATGRKPNTeplGLEN 262
|
170 180 190
....*....|....*....|....*....|.
gi 18405775 335 GQVELDSSGYVLVREgTSNTSVEGVFAAGDV 365
Cdd:PRK07251 263 TDIELTERGAIKVDD-YCQTSVPGVFAVGDV 292
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
86-127 |
6.04e-03 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 39.12 E-value: 6.04e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 18405775 86 VVIIGSGPAGYTAAIYAARANLKPVVFEGYQMG----GVPGGQLMT 127
Cdd:COG0665 5 VVVIGGGIAGLSTAYHLARRGLDVTVLERGRPGsgasGRNAGQLRP 50
|
|
| Thi4 |
pfam01946 |
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme. |
85-132 |
6.49e-03 |
|
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.
Pssm-ID: 460393 Cd Length: 232 Bit Score: 38.22 E-value: 6.49e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 18405775 85 NVVIIGSGPAGYTAAIYAARA-NLKPVVFE-----GYQMGGvpGGQLMTTTEVE 132
Cdd:pfam01946 19 DVVIVGAGSSGLTAAYYLAKNrGLKVAIIErsvspGGGAWL--GGQLFSAMVVR 70
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
86-113 |
9.28e-03 |
|
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 440419 [Multi-domain] Cd Length: 326 Bit Score: 38.38 E-value: 9.28e-03
10 20
....*....|....*....|....*...
gi 18405775 86 VVIIGSGPAGYTAAIYAARANLKPVVFE 113
Cdd:COG0654 6 VLIVGGGPAGLALALALARAGIRVTVVE 33
|
|
| |
