|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
54-579 |
3.30e-130 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 387.59 E-value: 3.30e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 54 RKRKVVLLGTGWAGASFLKTLNNSSYEVQVISPRNYFAFTPLLPSVTCGTVEARSVVEPIRNIARKNvEMSFLEAECFKI 133
Cdd:PTZ00318 9 KKPNVVVLGTGWAGAYFVRNLDPKKYNITVISPRNHMLFTPLLPQTTTGTLEFRSICEPVRPALAKL-PNRYLRAVVYDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 134 DPGSKKVYCRSKQGVNSKGKKEFDVDYDYLVIATGAQSNTFNIPGVEENCHFLKEVEDAQRIRSTVIDSFEKASLPGLNE 213
Cdd:PTZ00318 88 DFEEKRVKCGVVSKSNNANVNTFSVPYDKLVVAHGARPNTFNIPGVEERAFFLKEVNHARGIRKRIVQCIERASLPTTSV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 214 QERKRMLHFVVVGGGPTGVEFASELHDFVNEDLVKLYPKAKNLVQITLLEAADHILTMFDKRITEFAEEKFTRDGIDVKL 293
Cdd:PTZ00318 168 EERKRLLHFVVVGGGPTGVEFAAELADFFRDDVRNLNPELVEECKVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVDIRT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 294 GSMVVKVNDKEISakTKAGEVstIPYGMIVWSTGIGTRPVIKDFmkQIGQGNRRALATDEWLRVEGCDNIYALGDCATIN 373
Cdd:PTZ00318 248 KTAVKEVLDKEVV--LKDGEV--IPTGLVVWSTGVGPGPLTKQL--KVDKTSRGRISVDDHLRVKPIPNVFALGDCAANE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 374 QRKvmediaaifkkadkensgtltmkefhevmsdicdrypqvelylkskgmhgitdllkqaqaengsnksveldieelks 453
Cdd:PTZ00318 322 ERP----------------------------------------------------------------------------- 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 454 alcqvdsqvklLPATGQVAAQQGTYLAKCFDRMEvceknpegpirirgEGRHRFRPFRYRHLGQFAPLGGEQTAAQLpGD 533
Cdd:PTZ00318 325 -----------LPTLAQVASQQGVYLAKEFNNEL--------------KGKPMSKPFVYRSLGSLAYLGNYSAIVQL-GA 378
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1063724048 534 WVSIGHSSQWLWYSVYASKQVSWRTRVLVVSDWMRRFIFGRDSSRI 579
Cdd:PTZ00318 379 FDLSGFKALLFWRSAYLTILGSWRSKLYVLVNWAGTAIFGRDITRF 424
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
55-563 |
1.77e-75 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 244.66 E-value: 1.77e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 55 KRKVVLLGTGWAGASFLKTLNN---SSYEVQVISPRNYFAFTPLLPSVTCGTVEARSVVEPIRNIARK-NVEmsFLEAEC 130
Cdd:COG1252 1 MKRIVIVGGGFAGLEAARRLRKklgGDAEVTLIDPNPYHLFQPLLPEVAAGTLSPDDIAIPLRELLRRaGVR--FIQGEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 131 FKIDPGSKKVYCRSKQgvnskgkkefDVDYDYLVIATGAQSNTFNIPGVEENCHFLKEVEDAQRIRSTVIDSFEKAslpg 210
Cdd:COG1252 79 TGIDPEARTVTLADGR----------TLSYDYLVIATGSVTNFFGIPGLAEHALPLKTLEDALALRERLLAAFERA---- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 211 lneqERKRMLHFVVVGGGPTGVEFASELHDFVNEdLVKLYPKAKNLVQITLLEAADHILTMFDKRITEFAEEKFTRDGID 290
Cdd:COG1252 145 ----ERRRLLTIVVVGGGPTGVELAGELAELLRK-LLRYPGIDPDKVRITLVEAGPRILPGLGEKLSEAAEKELEKRGVE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 291 VKLGSMVVKVNDKEIsaKTKAGEvsTIPYGMIVWSTGIGTRPVIKDFMKQIGQGNRraLATDEWLRVEGCDNIYALGDCA 370
Cdd:COG1252 220 VHTGTRVTEVDADGV--TLEDGE--EIPADTVIWAAGVKAPPLLADLGLPTDRRGR--VLVDPTLQVPGHPNVFAIGDCA 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 371 TInqrkvmediaaifkkadkensgtltmkefhevmsdicdrypqvelylkskgmhgitdllkqaqaengsnksveldiee 450
Cdd:COG1252 294 AV------------------------------------------------------------------------------ 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 451 lksalcqVDSQVKLLPATGQVAAQQGTYLAKCFDRmevceknpegpiRIRGEGRhrfRPFRYRHLGQFAPLGGEQTAAQL 530
Cdd:COG1252 296 -------PDPDGKPVPKTAQAAVQQAKVLAKNIAA------------LLRGKPL---KPFRYRDKGCLASLGRGAAVADV 353
|
490 500 510
....*....|....*....|....*....|....*
gi 1063724048 531 PGDWVS--IGHssqWLWYSVYASKQVSWRTRVLVV 563
Cdd:COG1252 354 GGLKLSgfLAW---LLKRAIHLYFLPGFRGRLRVL 385
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
57-369 |
5.54e-53 |
|
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: 182.90 E-value: 5.54e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 57 KVVLLGTGWAGASFLKTLNNSSYEVQVIS-PRNYFAFTPLLPSVTCGTVEARS-------VVEPIRNIARK---NVEMsF 125
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGGKVTLIEdEGTCPYGGCVLSKALLGAAEAPEiaslwadLYKRKEEVVKKlnnGIEV-L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 126 LEAECFKIDPGSKKVYCRskqgvNSKGKKEFDVDYDYLVIATGAQSNTFNIPGVEENCHFL-KEVEDAQRIRSTVIDsfE 204
Cdd:pfam07992 81 LGTEVVSIDPGAKKVVLE-----ELVDGDGETITYDRLVIATGARPRLPPIPGVELNVGFLvRTLDSAEALRLKLLP--K 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 205 K-----ASLPGLneqerkrmlhfvvvgggptgvEFASELHDFVnedlvklypkaknlVQITLLEAADHILTMFDKRITEF 279
Cdd:pfam07992 154 RvvvvgGGYIGV---------------------ELAAALAKLG--------------KEVTLIEALDRLLRAFDEEISAA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 280 AEEKFTRDGIDVKLGSMVVKVNDKEISAKTKAGEVSTIPYGMIVWstGIGTRPVIkDFMKQIG--QGNRRALATDEWLRV 357
Cdd:pfam07992 199 LEKALEKNGVEVRLGTSVKEIIGDGDGVEVILKDGTEIDADLVVV--AIGRRPNT-ELLEAAGleLDERGGIVVDEYLRT 275
|
330
....*....|..
gi 1063724048 358 EgCDNIYALGDC 369
Cdd:pfam07992 276 S-VPGIYAAGDC 286
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
150-369 |
3.42e-11 |
|
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: 65.74 E-value: 3.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 150 SKGKKEFDVDYDYLVIATGAQSNTFNIPGVEEnchflkevedaqriRSTVIDSFEKASLPGLNEqerkrmlHFVVVGGGP 229
Cdd:TIGR01350 122 TGENGEETLEAKNIIIATGSRPRSLPGPFDFD--------------GKVVITSTGALNLEEVPE-------SLVIIGGGV 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 230 TGVEFASELHDFVnedlvklypkaknlVQITLLEAADHILTMFDKRITEFAEEKFTRDGIDVKLGSMVVKV--NDKEISA 307
Cdd:TIGR01350 181 IGIEFASIFASLG--------------SKVTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILTNTKVTAVekNDDQVTY 246
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063724048 308 KTKAGEVSTIPYGMIVWStgIGTRPVIKDF-MKQIG--QGNRRALATDEWLRVeGCDNIYALGDC 369
Cdd:TIGR01350 247 ENKGGETETLTGEKVLVA--VGRKPNTEGLgLEKLGveLDERGRIVVDEYMRT-NVPGIYAIGDV 308
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
372-406 |
2.46e-03 |
|
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.
Pssm-ID: 238008 [Multi-domain] Cd Length: 63 Bit Score: 36.37 E-value: 2.46e-03
10 20 30
....*....|....*....|....*....|....*
gi 1063724048 372 INQRKVMEDIAAIFKKADKENSGTLTMKEFHEVMS 406
Cdd:cd00051 29 LGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
|
|
| EF-hand_1 |
pfam00036 |
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ... |
380-408 |
6.85e-03 |
|
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.
Pssm-ID: 425435 [Multi-domain] Cd Length: 29 Bit Score: 34.30 E-value: 6.85e-03
10 20
....*....|....*....|....*....
gi 1063724048 380 DIAAIFKKADKENSGTLTMKEFHEVMSDI 408
Cdd:pfam00036 1 ELKEIFRLFDKDGDGKIDFEEFKELLKKL 29
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
54-579 |
3.30e-130 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 387.59 E-value: 3.30e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 54 RKRKVVLLGTGWAGASFLKTLNNSSYEVQVISPRNYFAFTPLLPSVTCGTVEARSVVEPIRNIARKNvEMSFLEAECFKI 133
Cdd:PTZ00318 9 KKPNVVVLGTGWAGAYFVRNLDPKKYNITVISPRNHMLFTPLLPQTTTGTLEFRSICEPVRPALAKL-PNRYLRAVVYDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 134 DPGSKKVYCRSKQGVNSKGKKEFDVDYDYLVIATGAQSNTFNIPGVEENCHFLKEVEDAQRIRSTVIDSFEKASLPGLNE 213
Cdd:PTZ00318 88 DFEEKRVKCGVVSKSNNANVNTFSVPYDKLVVAHGARPNTFNIPGVEERAFFLKEVNHARGIRKRIVQCIERASLPTTSV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 214 QERKRMLHFVVVGGGPTGVEFASELHDFVNEDLVKLYPKAKNLVQITLLEAADHILTMFDKRITEFAEEKFTRDGIDVKL 293
Cdd:PTZ00318 168 EERKRLLHFVVVGGGPTGVEFAAELADFFRDDVRNLNPELVEECKVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVDIRT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 294 GSMVVKVNDKEISakTKAGEVstIPYGMIVWSTGIGTRPVIKDFmkQIGQGNRRALATDEWLRVEGCDNIYALGDCATIN 373
Cdd:PTZ00318 248 KTAVKEVLDKEVV--LKDGEV--IPTGLVVWSTGVGPGPLTKQL--KVDKTSRGRISVDDHLRVKPIPNVFALGDCAANE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 374 QRKvmediaaifkkadkensgtltmkefhevmsdicdrypqvelylkskgmhgitdllkqaqaengsnksveldieelks 453
Cdd:PTZ00318 322 ERP----------------------------------------------------------------------------- 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 454 alcqvdsqvklLPATGQVAAQQGTYLAKCFDRMEvceknpegpirirgEGRHRFRPFRYRHLGQFAPLGGEQTAAQLpGD 533
Cdd:PTZ00318 325 -----------LPTLAQVASQQGVYLAKEFNNEL--------------KGKPMSKPFVYRSLGSLAYLGNYSAIVQL-GA 378
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1063724048 534 WVSIGHSSQWLWYSVYASKQVSWRTRVLVVSDWMRRFIFGRDSSRI 579
Cdd:PTZ00318 379 FDLSGFKALLFWRSAYLTILGSWRSKLYVLVNWAGTAIFGRDITRF 424
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
55-563 |
1.77e-75 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 244.66 E-value: 1.77e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 55 KRKVVLLGTGWAGASFLKTLNN---SSYEVQVISPRNYFAFTPLLPSVTCGTVEARSVVEPIRNIARK-NVEmsFLEAEC 130
Cdd:COG1252 1 MKRIVIVGGGFAGLEAARRLRKklgGDAEVTLIDPNPYHLFQPLLPEVAAGTLSPDDIAIPLRELLRRaGVR--FIQGEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 131 FKIDPGSKKVYCRSKQgvnskgkkefDVDYDYLVIATGAQSNTFNIPGVEENCHFLKEVEDAQRIRSTVIDSFEKAslpg 210
Cdd:COG1252 79 TGIDPEARTVTLADGR----------TLSYDYLVIATGSVTNFFGIPGLAEHALPLKTLEDALALRERLLAAFERA---- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 211 lneqERKRMLHFVVVGGGPTGVEFASELHDFVNEdLVKLYPKAKNLVQITLLEAADHILTMFDKRITEFAEEKFTRDGID 290
Cdd:COG1252 145 ----ERRRLLTIVVVGGGPTGVELAGELAELLRK-LLRYPGIDPDKVRITLVEAGPRILPGLGEKLSEAAEKELEKRGVE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 291 VKLGSMVVKVNDKEIsaKTKAGEvsTIPYGMIVWSTGIGTRPVIKDFMKQIGQGNRraLATDEWLRVEGCDNIYALGDCA 370
Cdd:COG1252 220 VHTGTRVTEVDADGV--TLEDGE--EIPADTVIWAAGVKAPPLLADLGLPTDRRGR--VLVDPTLQVPGHPNVFAIGDCA 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 371 TInqrkvmediaaifkkadkensgtltmkefhevmsdicdrypqvelylkskgmhgitdllkqaqaengsnksveldiee 450
Cdd:COG1252 294 AV------------------------------------------------------------------------------ 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 451 lksalcqVDSQVKLLPATGQVAAQQGTYLAKCFDRmevceknpegpiRIRGEGRhrfRPFRYRHLGQFAPLGGEQTAAQL 530
Cdd:COG1252 296 -------PDPDGKPVPKTAQAAVQQAKVLAKNIAA------------LLRGKPL---KPFRYRDKGCLASLGRGAAVADV 353
|
490 500 510
....*....|....*....|....*....|....*
gi 1063724048 531 PGDWVS--IGHssqWLWYSVYASKQVSWRTRVLVV 563
Cdd:COG1252 354 GGLKLSgfLAW---LLKRAIHLYFLPGFRGRLRVL 385
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
57-369 |
5.54e-53 |
|
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: 182.90 E-value: 5.54e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 57 KVVLLGTGWAGASFLKTLNNSSYEVQVIS-PRNYFAFTPLLPSVTCGTVEARS-------VVEPIRNIARK---NVEMsF 125
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGGKVTLIEdEGTCPYGGCVLSKALLGAAEAPEiaslwadLYKRKEEVVKKlnnGIEV-L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 126 LEAECFKIDPGSKKVYCRskqgvNSKGKKEFDVDYDYLVIATGAQSNTFNIPGVEENCHFL-KEVEDAQRIRSTVIDsfE 204
Cdd:pfam07992 81 LGTEVVSIDPGAKKVVLE-----ELVDGDGETITYDRLVIATGARPRLPPIPGVELNVGFLvRTLDSAEALRLKLLP--K 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 205 K-----ASLPGLneqerkrmlhfvvvgggptgvEFASELHDFVnedlvklypkaknlVQITLLEAADHILTMFDKRITEF 279
Cdd:pfam07992 154 RvvvvgGGYIGV---------------------ELAAALAKLG--------------KEVTLIEALDRLLRAFDEEISAA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 280 AEEKFTRDGIDVKLGSMVVKVNDKEISAKTKAGEVSTIPYGMIVWstGIGTRPVIkDFMKQIG--QGNRRALATDEWLRV 357
Cdd:pfam07992 199 LEKALEKNGVEVRLGTSVKEIIGDGDGVEVILKDGTEIDADLVVV--AIGRRPNT-ELLEAAGleLDERGGIVVDEYLRT 275
|
330
....*....|..
gi 1063724048 358 EgCDNIYALGDC 369
Cdd:pfam07992 276 S-VPGIYAAGDC 286
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
75-372 |
6.04e-31 |
|
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: 123.00 E-value: 6.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 75 NNSSYEVQVISPRNYFAFTPL-LPSVTCGTVEARS--VVEPIRNIARKNVEMsFLEAECFKIDPGSKKVYCRSKQgvnsk 151
Cdd:COG0446 2 LGPDAEITVIEKGPHHSYQPCgLPYYVGGGIKDPEdlLVRTPESFERKGIDV-RTGTEVTAIDPEAKTVTLRDGE----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 152 gkkefDVDYDYLVIATGAQSNTFNIPGVE-ENCHFLKEVEDAQRIRSTvidsfekaslpgLNEQERKR---------MLh 221
Cdd:COG0446 76 -----TLSYDKLVLATGARPRPPPIPGLDlPGVFTLRTLDDADALREA------------LKEFKGKRavvigggpiGL- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 222 fvvvgggptgvEFASELHdfvnedlvklypKAKnlVQITLLEAADHILTMFDKRITEFAEEKFTRDGIDVKLGSMVVKVN 301
Cdd:COG0446 138 -----------ELAEALR------------KRG--LKVTLVERAPRLLGVLDPEMAALLEEELREHGVELRLGETVVAID 192
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063724048 302 -DKEISAKTKAGEvsTIPYGMIVwsTGIGTRPVIkDFMKQIG--QGNRRALATDEWLRVeGCDNIYALGDCATI 372
Cdd:COG0446 193 gDDKVAVTLTDGE--EIPADLVV--VAPGVRPNT-ELAKDAGlaLGERGWIKVDETLQT-SDPDVYAAGDCAEV 260
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
55-375 |
5.17e-24 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 104.45 E-value: 5.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 55 KRKVVLLGTGWAGASFLKTL--NNSSYEVQVISPRNYFAFT-PLLPSVTCGTVEARSVV-EPIRNIARKNVEMsFLEAEC 130
Cdd:COG1251 1 KMRIVIIGAGMAGVRAAEELrkLDPDGEITVIGAEPHPPYNrPPLSKVLAGETDEEDLLlRPADFYEENGIDL-RLGTRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 131 FKIDPGSKKVYCRSKQgvnskgkkefDVDYDYLVIATGAQSNTFNIPGVE-ENCHFLKEVEDAQRIRS--------TVID 201
Cdd:COG1251 80 TAIDRAARTVTLADGE----------TLPYDKLVLATGSRPRVPPIPGADlPGVFTLRTLDDADALRAalapgkrvVVIG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 202 sfekASLPGLneqerkrmlhfvvvgggptgvEFASELhdfvnedlvklypkAKNLVQITLLEAADHIL-TMFDKRITEFA 280
Cdd:COG1251 150 ----GGLIGL---------------------EAAAAL--------------RKRGLEVTVVERAPRLLpRQLDEEAGALL 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 281 EEKFTRDGIDVKLGSMVVKV--NDKEISAKTKAGEvsTIPYGMIVWSTGIgtRPVIkDFMKQ----IGQGnrraLATDEW 354
Cdd:COG1251 191 QRLLEALGVEVRLGTGVTEIegDDRVTGVRLADGE--ELPADLVVVAIGV--RPNT-ELARAaglaVDRG----IVVDDY 261
|
330 340
....*....|....*....|.
gi 1063724048 355 LRVeGCDNIYALGDCATINQR 375
Cdd:COG1251 262 LRT-SDPDIYAAGDCAEHPGP 281
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
57-375 |
3.19e-19 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 90.48 E-value: 3.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 57 KVVLLGTGWAGASFLKTL--NNSSYEVQVISPRNYFAFTPL-LPSVTCGTVEarsvvEPIRNIAR------KNVEMSFLE 127
Cdd:PRK09564 2 KIIIIGGTAAGMSAAAKAkrLNKELEITVYEKTDIVSFGACgLPYFVGGFFD-----DPNTMIARtpeefiKSGIDVKTE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 128 AECFKIDPGSKKVYCRskqgvNSKGKKEFDVDYDYLVIATGAQSNTFNIPGVE-ENCHFLKEVEDAQRIRSTVIDSFEK- 205
Cdd:PRK09564 77 HEVVKVDAKNKTITVK-----NLKTGSIFNDTYDKLMIATGARPIIPPIKNINlENVYTLKSMEDGLALKELLKDEEIKn 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 206 -----ASLPGLneqerkrmlhfvvvgggptgvEFASELHDfvnedlvklypKAKNlvqITLLEAADHILT-MFDKRITEF 279
Cdd:PRK09564 152 iviigAGFIGL---------------------EAVEAAKH-----------LGKN---VRIIQLEDRILPdSFDKEITDV 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 280 AEEKFTRDGIDVKLGSMVVKV--NDKEISAKTKAGEVSTipyGMIVWSTGIgtRP---VIKD-FMKQIGQGnrrALATDE 353
Cdd:PRK09564 197 MEEELRENGVELHLNEFVKSLigEDKVEGVVTDKGEYEA---DVVIVATGV--KPnteFLEDtGLKTLKNG---AIIVDE 268
|
330 340
....*....|....*....|..
gi 1063724048 354 WLRVEgCDNIYALGDCATINQR 375
Cdd:PRK09564 269 YGETS-IENIYAAGDCATIYNI 289
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
161-370 |
3.40e-15 |
|
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: 78.20 E-value: 3.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 161 DYLVIATGAQSNTFNIPGVEENchflkevedaqrirsTVIDS---FEKASLPglneqerKRM---------Lhfvvvggg 228
Cdd:COG1249 132 DHIVIATGSRPRVPPIPGLDEV---------------RVLTSdeaLELEELP-------KSLvvigggyigL-------- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 229 ptgvEFASELHDFVnedlvklypkaknlVQITLLEAADHILTMFDKRITEFAEEKFTRDGIDVKLGSMVVKV--NDKEIS 306
Cdd:COG1249 182 ----EFAQIFARLG--------------SEVTLVERGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVekTGDGVT 243
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063724048 307 AKTKAGE-VSTIPYGMIVWSTGIgtRPVIKDF-MKQIG--QGNRRALATDEWLRVeGCDNIYALGDCA 370
Cdd:COG1249 244 VTLEDGGgEEAVEADKVLVATGR--RPNTDGLgLEAAGveLDERGGIKVDEYLRT-SVPGIYAIGDVT 308
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
257-368 |
2.19e-11 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 66.32 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 257 VQITLLEAADHILTMFDKRITEFAEEKFTRDGIDVKLGSMVVKV--NDKEISAKT-KAGEVSTIPYGMIVWSTGIgtRPV 333
Cdd:PRK06416 196 AEVTIVEALPRILPGEDKEISKLAERALKKRGIKIKTGAKAKKVeqTDDGVTVTLeDGGKEETLEADYVLVAVGR--RPN 273
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1063724048 334 IKDfmkqIG---QG---NRRALATDEWLRvEGCDNIYALGD 368
Cdd:PRK06416 274 TEN----LGleeLGvktDRGFIEVDEQLR-TNVPNIYAIGD 309
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
150-369 |
3.42e-11 |
|
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: 65.74 E-value: 3.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 150 SKGKKEFDVDYDYLVIATGAQSNTFNIPGVEEnchflkevedaqriRSTVIDSFEKASLPGLNEqerkrmlHFVVVGGGP 229
Cdd:TIGR01350 122 TGENGEETLEAKNIIIATGSRPRSLPGPFDFD--------------GKVVITSTGALNLEEVPE-------SLVIIGGGV 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 230 TGVEFASELHDFVnedlvklypkaknlVQITLLEAADHILTMFDKRITEFAEEKFTRDGIDVKLGSMVVKV--NDKEISA 307
Cdd:TIGR01350 181 IGIEFASIFASLG--------------SKVTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILTNTKVTAVekNDDQVTY 246
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063724048 308 KTKAGEVSTIPYGMIVWStgIGTRPVIKDF-MKQIG--QGNRRALATDEWLRVeGCDNIYALGDC 369
Cdd:TIGR01350 247 ENKGGETETLTGEKVLVA--VGRKPNTEGLgLEKLGveLDERGRIVVDEYMRT-NVPGIYAIGDV 308
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
96-377 |
1.76e-06 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 50.55 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 96 LPSVTCGTVEARSVVEPI--------RNIARKNVEmsfleaECFKIDPGSKKVYCRskqgvNSKGKKEFDVDYDYLVIAT 167
Cdd:PRK13512 45 LPYYIGEVVEDRKYALAYtpekfydrKQITVKTYH------EVIAINDERQTVTVL-----NRKTNEQFEESYDKLILSP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 168 GAQSNTfniPGVEENCHF-LKEVEDAQRirstvIDSFekaslpgLNEQERKRMLHFVVVGGGPtgvefaselhdfvnEDL 246
Cdd:PRK13512 114 GASANS---LGFESDITFtLRNLEDTDA-----IDQF-------IKANQVDKALVVGAGYISL--------------EVL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 247 VKLYPKAknlVQITLLEAADHILTMFDKRITEFAEEKFTRDGIDVKLGSMVVKVNDKEISAKTkaGEVSTipYGMIVwsT 326
Cdd:PRK13512 165 ENLYERG---LHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEIDAINGNEVTFKS--GKVEH--YDMII--E 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063724048 327 GIGTRPVIKdFMKqigqGNRRALATDEWLRVE-----GCDNIYALGDCATINQRKV 377
Cdd:PRK13512 236 GVGTHPNSK-FIE----SSNIKLDDKGFIPVNdkfetNVPNIYAIGDIITSHYRHV 286
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
161-369 |
2.52e-06 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 50.18 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 161 DYLVIATGaqSNTFNIPGVEEnchflkeVEDAQRIRSTviDSFEKASLPglneqerKRMLHFVVVgggPTGVEFASELHd 240
Cdd:PRK06292 132 KNIVIATG--SRVPPIPGVWL-------ILGDRLLTSD--DAFELDKLP-------KSLAVIGGG---VIGLELGQALS- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 241 fvnedlvklypkakNL-VQITLLEAADHILTMFDKRITEFAEEKFTRDgIDVKLGSMVVKV---NDKEISAKTKAGEVST 316
Cdd:PRK06292 190 --------------RLgVKVTVFERGDRILPLEDPEVSKQAQKILSKE-FKIKLGAKVTSVeksGDEKVEELEKGGKTET 254
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063724048 317 IPYGMIVWSTGIgtRPVIKDF-MKQIGqgnrraLATDEWLRVE-------GCDNIYALGDC 369
Cdd:PRK06292 255 IEADYVLVATGR--RPNTDGLgLENTG------IELDERGRPVvdehtqtSVPGIYAAGDV 307
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
257-370 |
4.46e-06 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 49.54 E-value: 4.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 257 VQITLLEAADHILTMFDKRITEFAEEKFTRDGIDVKLGsmvVKVNDKEISAK-------TKAGEVSTIPYGMIVWStgIG 329
Cdd:PRK06327 207 AEVTILEALPAFLAAADEQVAKEAAKAFTKQGLDIHLG---VKIGEIKTGGKgvsvaytDADGEAQTLEVDKLIVS--IG 281
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1063724048 330 TRPVIKDfmkqIGQGN-------RRALATDEWLRVeGCDNIYALGDCA 370
Cdd:PRK06327 282 RVPNTDG----LGLEAvglkldeRGFIPVDDHCRT-NVPNVYAIGDVV 324
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
161-368 |
8.13e-06 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 48.59 E-value: 8.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 161 DYLVIATGAQSNTFNIPGVEENCHFLKevedaqrirSTVIDSFEKasLPglneqerKRMlhfVVVGGGPTGVEFASelhd 240
Cdd:PRK07251 120 ETIVINTGAVSNVLPIPGLADSKHVYD---------STGIQSLET--LP-------ERL---GIIGGGNIGLEFAG---- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 241 fvnedlvkLYPKAKNlvQITLLEAADHILTMFDKRITEFAEEKFTRDGIDVKLGSMVVKV-NDKEISAKTKAGEvsTIPY 319
Cdd:PRK07251 175 --------LYNKLGS--KVTVLDAASTILPREEPSVAALAKQYMEEDGITFLLNAHTTEVkNDGDQVLVVTEDE--TYRF 242
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1063724048 320 GMIVWSTgiGTRPVIKDFMKQ---IGQGNRRALATDEWLR--VEGcdnIYALGD 368
Cdd:PRK07251 243 DALLYAT--GRKPNTEPLGLEntdIELTERGAIKVDDYCQtsVPG---VFAVGD 291
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
55-368 |
1.35e-05 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 47.70 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 55 KRKVVLLGTGWAGASFLKTLNNSSYEVQVISPRN-YFAFTpllpSVTCGTVEARSVVEP-------IRNIARKNVEMSFL 126
Cdd:PRK08010 3 KYQAVIIGFGKAGKTLAVTLAKAGWRVALIEQSNaMYGGT----CINIGCIPTKTLVHDaqqhtdfVRAIQRKNEVVNFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 127 EAECFK-----------------IDPGSKKVYcRSKQGVNSKGKKEFdvdydylvIATGAQSNTFNIPGVeenchflkev 189
Cdd:PRK08010 79 RNKNFHnladmpnidvidgqaefINNHSLRVH-RPEGNLEIHGEKIF--------INTGAQTVVPPIPGI---------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 190 edaqrirSTVIDSFEKASLPGLNEqerkRMLHFVVVGGGPTGVEFASELHDFVNedlvklypkaknlvQITLLEAADHIL 269
Cdd:PRK08010 140 -------TTTPGVYDSTGLLNLKE----LPGHLGILGGGYIGVEFASMFANFGS--------------KVTILEAASLFL 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 270 TMFDKRITEFAEEKFTRDGIDVKLGSMVVKVNDKEISAKTKAGEVSTIPYGMIVWStgiGTRPVIKDFMKQ---IGQGNR 346
Cdd:PRK08010 195 PREDRDIADNIATILRDQGVDIILNAHVERISHHENQVQVHSEHAQLAVDALLIAS---GRQPATASLHPEnagIAVNER 271
|
330 340
....*....|....*....|..
gi 1063724048 347 RALATDEWLRVEGcDNIYALGD 368
Cdd:PRK08010 272 GAIVVDKYLHTTA-DNIWAMGD 292
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
233-312 |
2.04e-05 |
|
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: 42.96 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 233 EFASELHDFVnedlvklypkaknlVQITLLEAADHILTMFDKRITEFAEEKFTRDGIDVKLGSMVVKV--NDKEISAKTK 310
Cdd:pfam00070 13 ELAGALARLG--------------SKVTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIegNGDGVVVVLT 78
|
..
gi 1063724048 311 AG 312
Cdd:pfam00070 79 DG 80
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
58-375 |
3.52e-05 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 46.74 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 58 VVLLGTGWAGASF---LKTLNNSSYEVQVISPRNYFAFTP-LLPSVTCGTVEARSVVEPIRNIARKNVEMSFLEAECFKI 133
Cdd:TIGR02374 1 LVLVGNGMAGHRCieeVLKLNRHMFEITIFGEEPHPNYNRiLLSSVLQGEADLDDITLNSKDWYEKHGITLYTGETVIQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 134 DPGSKKVycrskqgVNSKGKKEFdvdYDYLVIATGAQSNTFNIPGVE-ENCHFLKEVEDAQRIRSTViDSFEKASL--PG 210
Cdd:TIGR02374 81 DTDQKQV-------ITDAGRTLS---YDKLILATGSYPFILPIPGADkKGVYVFRTIEDLDAIMAMA-QRFKKAAVigGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 211 LNEQERKRMLhfvvvgggptgVEFASELHdfvnedLVKLYPKaknLVQITLLEAADHILtmfdkritefaEEKFTRDGID 290
Cdd:TIGR02374 150 LLGLEAAVGL-----------QNLGMDVS------VIHHAPG---LMAKQLDQTAGRLL-----------QRELEQKGLT 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 291 VKLGSmvvkvNDKEISAKTKAGEV-----STIPYGMIVWSTGIgtRPVIKdFMKQIGQGNRRALATDEWLRVEGcDNIYA 365
Cdd:TIGR02374 199 FLLEK-----DTVEIVGATKADRIrfkdgSSLEADLIVMAAGI--RPNDE-LAVSAGIKVNRGIIVNDSMQTSD-PDIYA 269
|
330
....*....|
gi 1063724048 366 LGDCATINQR 375
Cdd:TIGR02374 270 VGECAEHNGR 279
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
258-378 |
7.88e-05 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 45.29 E-value: 7.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 258 QITLLEAADHIL-TMFDKRITEFAEEKFTRDGIDVKLGSMVVKVN--DKEISAKTKAGEVSTIPygmIVWStGIGTRPVI 334
Cdd:PRK04965 166 AVTLVDNAASLLaSLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEktDSGIRATLDSGRSIEVD---AVIA-AAGLRPNT 241
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1063724048 335 KdFMKQIGQGNRRALATDEWLRVEGcDNIYALGDCATINQrKVM 378
Cdd:PRK04965 242 A-LARRAGLAVNRGIVVDSYLQTSA-PDIYALGDCAEING-QVL 282
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
372-406 |
2.46e-03 |
|
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.
Pssm-ID: 238008 [Multi-domain] Cd Length: 63 Bit Score: 36.37 E-value: 2.46e-03
10 20 30
....*....|....*....|....*....|....*
gi 1063724048 372 INQRKVMEDIAAIFKKADKENSGTLTMKEFHEVMS 406
Cdd:cd00051 29 LGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
161-369 |
3.25e-03 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 40.14 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 161 DYLVIATGAQSNTFNIPGVEencHflkevedaqrirstVIDS---FEKASLPglneqerKRMLhfvVVGGGPTGVEFASE 237
Cdd:PRK06116 133 DHILIATGGRPSIPDIPGAE---Y--------------GITSdgfFALEELP-------KRVA---VVGAGYIAVEFAGV 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724048 238 LHdfvnedlvklypkakNL-VQITLLEAADHILTMFDKRITEFAEEKFTRDGIDVKLGSM---VVKVNDKEISAKTKAGE 313
Cdd:PRK06116 186 LN---------------GLgSETHLFVRGDAPLRGFDPDIRETLVEEMEKKGIRLHTNAVpkaVEKNADGSLTLTLEDGE 250
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063724048 314 VSTIpyGMIVWStgIGTRPVIKDF-MKQIG--QGNRRALATDEWLR--VEGcdnIYALGDC 369
Cdd:PRK06116 251 TLTV--DCLIWA--IGREPNTDGLgLENAGvkLNEKGYIIVDEYQNtnVPG---IYAVGDV 304
|
|
| EF-hand_1 |
pfam00036 |
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ... |
380-408 |
6.85e-03 |
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EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.
Pssm-ID: 425435 [Multi-domain] Cd Length: 29 Bit Score: 34.30 E-value: 6.85e-03
10 20
....*....|....*....|....*....
gi 1063724048 380 DIAAIFKKADKENSGTLTMKEFHEVMSDI 408
Cdd:pfam00036 1 ELKEIFRLFDKDGDGKIDFEEFKELLKKL 29
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