|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
54-580 |
3.10e-129 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 384.89 E-value: 3.10e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 54 RKRKVVLLGTGWAGASFLKTLNNSSYEVQVISPRNYFAFTPLLPSVTCGTVEARSVVEPIRNIARKQnvEMSFLEAECFK 133
Cdd:PTZ00318 9 KKPNVVVLGTGWAGAYFVRNLDPKKYNITVISPRNHMLFTPLLPQTTTGTLEFRSICEPVRPALAKL--PNRYLRAVVYD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 134 IDPGSKKVYCRSKQGVNSKGKKEFDVDYDYLVIATGAQSNTFNIPGVEENCHFLKEVEDAQRIRSTVIDSFEKASLPGLN 213
Cdd:PTZ00318 87 VDFEEKRVKCGVVSKSNNANVNTFSVPYDKLVVAHGARPNTFNIPGVEERAFFLKEVNHARGIRKRIVQCIERASLPTTS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 214 EQERKRMLHFVVVGGGPTGVEFASELHDFVNEDLVKLYPKAKNLVQITLLEAADHILTMFDKRITEFAEEKFTRDGIDVK 293
Cdd:PTZ00318 167 VEERKRLLHFVVVGGGPTGVEFAAELADFFRDDVRNLNPELVEECKVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVDIR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 294 LGSMVVKVNDKEISakTKAGEVstIPYGMIVWSTGIGTRPVIKDFmkQIGQGNRRALATDEWLRVEGCDNIYALGDCATI 373
Cdd:PTZ00318 247 TKTAVKEVLDKEVV--LKDGEV--IPTGLVVWSTGVGPGPLTKQL--KVDKTSRGRISVDDHLRVKPIPNVFALGDCAAN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 374 NQRKvmediaaifkkadkensgtltmkefhevmsdicdrypqvelylkskgmhgitdllkqaqaengsnksveldieelk 453
Cdd:PTZ00318 321 EERP---------------------------------------------------------------------------- 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 454 salcqvdsqvklLPATGQVAAQQGTYLAKCFDRMEvceknpegpirirgEGRHRFRPFRYRHLGQFAPLGGEQTAAQLpG 533
Cdd:PTZ00318 325 ------------LPTLAQVASQQGVYLAKEFNNEL--------------KGKPMSKPFVYRSLGSLAYLGNYSAIVQL-G 377
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 240256027 534 DWVSIGHSSQWLWYSVYASKQVSWRTRVLVVSDWMRRFIFGRDSSRI 580
Cdd:PTZ00318 378 AFDLSGFKALLFWRSAYLTILGSWRSKLYVLVNWAGTAIFGRDITRF 424
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
55-564 |
1.45e-77 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 250.43 E-value: 1.45e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 55 KRKVVLLGTGWAGASFLKTLNN---SSYEVQVISPRNYFAFTPLLPSVTCGTVEARSVVEPIRNIARKQNVEmsFLEAEC 131
Cdd:COG1252 1 MKRIVIVGGGFAGLEAARRLRKklgGDAEVTLIDPNPYHLFQPLLPEVAAGTLSPDDIAIPLRELLRRAGVR--FIQGEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 132 FKIDPGSKKVYCRSKQgvnskgkkefDVDYDYLVIATGAQSNTFNIPGVEENCHFLKEVEDAQRIRSTVIDSFEKAslpg 211
Cdd:COG1252 79 TGIDPEARTVTLADGR----------TLSYDYLVIATGSVTNFFGIPGLAEHALPLKTLEDALALRERLLAAFERA---- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 212 lneqERKRMLHFvvvgggptgV---------EFASELHDFVNEdLVKLYPKAKNLVQITLLEAADHILTMFDKRITEFAE 282
Cdd:COG1252 145 ----ERRRLLTI---------VvvgggptgvELAGELAELLRK-LLRYPGIDPDKVRITLVEAGPRILPGLGEKLSEAAE 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 283 EKFTRDGIDVKLGSMVVKVNDKEIsaKTKAGEvsTIPYGMIVWSTGIGTRPVIKDFMKQIGQGNRraLATDEWLRVEGCD 362
Cdd:COG1252 211 KELEKRGVEVHTGTRVTEVDADGV--TLEDGE--EIPADTVIWAAGVKAPPLLADLGLPTDRRGR--VLVDPTLQVPGHP 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 363 NIYALGDCATInqrkvmediaaifkkadkensgtltmkefhevmsdicdrypqvelylkskgmhgitdllkqaqaengsn 442
Cdd:COG1252 285 NVFAIGDCAAV--------------------------------------------------------------------- 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 443 ksveldieelksalcqVDSQVKLLPATGQVAAQQGTYLAKCFDRmevceknpegpiRIRGEGRhrfRPFRYRHLGQFAPL 522
Cdd:COG1252 296 ----------------PDPDGKPVPKTAQAAVQQAKVLAKNIAA------------LLRGKPL---KPFRYRDKGCLASL 344
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 240256027 523 GGEQTAAQLPGDWVS--IGHssqWLWYSVYASKQVSWRTRVLVV 564
Cdd:COG1252 345 GRGAAVADVGGLKLSgfLAW---LLKRAIHLYFLPGFRGRLRVL 385
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
57-370 |
2.57e-54 |
|
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: 2.57e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 57 KVVLLGTGWAGASFLKTLNNSSYEVQVIS-PRNYFAFTPLLPSVTCGTVEARS-------VVEPIRNIARKQNVEMSF-L 127
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGGKVTLIEdEGTCPYGGCVLSKALLGAAEAPEiaslwadLYKRKEEVVKKLNNGIEVlL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 128 EAECFKIDPGSKKVYCRskqgvNSKGKKEFDVDYDYLVIATGAQSNTFNIPGVEENCHFL-KEVEDAQRIRSTVIDsfEK 206
Cdd:pfam07992 82 GTEVVSIDPGAKKVVLE-----ELVDGDGETITYDRLVIATGARPRLPPIPGVELNVGFLvRTLDSAEALRLKLLP--KR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 207 -----ASLPGLneqerkrmlhfvvvgggptgvEFASELHDFVnedlvklypkaknlVQITLLEAADHILTMFDKRITEFA 281
Cdd:pfam07992 155 vvvvgGGYIGV---------------------ELAAALAKLG--------------KEVTLIEALDRLLRAFDEEISAAL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 282 EEKFTRDGIDVKLGSMVVKVNDKEISAKTKAGEVSTIPYGMIVWstGIGTRPVIkDFMKQIG--QGNRRALATDEWLRVE 359
Cdd:pfam07992 200 EKALEKNGVEVRLGTSVKEIIGDGDGVEVILKDGTEIDADLVVV--AIGRRPNT-ELLEAAGleLDERGGIVVDEYLRTS 276
|
330
....*....|.
gi 240256027 360 gCDNIYALGDC 370
Cdd:pfam07992 277 -VPGIYAAGDC 286
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
151-370 |
3.25e-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: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 151 SKGKKEFDVDYDYLVIATGAQSNTFNIPGVEEnchflkevedaqriRSTVIDSFEKASLPGLNEqerkrmlHFVVVGGGP 230
Cdd:TIGR01350 122 TGENGEETLEAKNIIIATGSRPRSLPGPFDFD--------------GKVVITSTGALNLEEVPE-------SLVIIGGGV 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 231 TGVEFASELHDFVnedlvklypkaknlVQITLLEAADHILTMFDKRITEFAEEKFTRDGIDVKLGSMVVKV--NDKEISA 308
Cdd:TIGR01350 181 IGIEFASIFASLG--------------SKVTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILTNTKVTAVekNDDQVTY 246
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240256027 309 KTKAGEVSTIPYGMIVWStgIGTRPVIKDF-MKQIG--QGNRRALATDEWLRVeGCDNIYALGDC 370
Cdd:TIGR01350 247 ENKGGETETLTGEKVLVA--VGRKPNTEGLgLEKLGveLDERGRIVVDEYMRT-NVPGIYAIGDV 308
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
373-407 |
2.39e-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: 36.76 E-value: 2.39e-03
10 20 30
....*....|....*....|....*....|....*
gi 240256027 373 INQRKVMEDIAAIFKKADKENSGTLTMKEFHEVMS 407
Cdd:cd00051 29 LGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
|
|
| EF-hand_1 |
pfam00036 |
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ... |
381-409 |
6.60e-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: 6.60e-03
10 20
....*....|....*....|....*....
gi 240256027 381 DIAAIFKKADKENSGTLTMKEFHEVMSDI 409
Cdd:pfam00036 1 ELKEIFRLFDKDGDGKIDFEEFKELLKKL 29
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
54-580 |
3.10e-129 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 384.89 E-value: 3.10e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 54 RKRKVVLLGTGWAGASFLKTLNNSSYEVQVISPRNYFAFTPLLPSVTCGTVEARSVVEPIRNIARKQnvEMSFLEAECFK 133
Cdd:PTZ00318 9 KKPNVVVLGTGWAGAYFVRNLDPKKYNITVISPRNHMLFTPLLPQTTTGTLEFRSICEPVRPALAKL--PNRYLRAVVYD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 134 IDPGSKKVYCRSKQGVNSKGKKEFDVDYDYLVIATGAQSNTFNIPGVEENCHFLKEVEDAQRIRSTVIDSFEKASLPGLN 213
Cdd:PTZ00318 87 VDFEEKRVKCGVVSKSNNANVNTFSVPYDKLVVAHGARPNTFNIPGVEERAFFLKEVNHARGIRKRIVQCIERASLPTTS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 214 EQERKRMLHFVVVGGGPTGVEFASELHDFVNEDLVKLYPKAKNLVQITLLEAADHILTMFDKRITEFAEEKFTRDGIDVK 293
Cdd:PTZ00318 167 VEERKRLLHFVVVGGGPTGVEFAAELADFFRDDVRNLNPELVEECKVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVDIR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 294 LGSMVVKVNDKEISakTKAGEVstIPYGMIVWSTGIGTRPVIKDFmkQIGQGNRRALATDEWLRVEGCDNIYALGDCATI 373
Cdd:PTZ00318 247 TKTAVKEVLDKEVV--LKDGEV--IPTGLVVWSTGVGPGPLTKQL--KVDKTSRGRISVDDHLRVKPIPNVFALGDCAAN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 374 NQRKvmediaaifkkadkensgtltmkefhevmsdicdrypqvelylkskgmhgitdllkqaqaengsnksveldieelk 453
Cdd:PTZ00318 321 EERP---------------------------------------------------------------------------- 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 454 salcqvdsqvklLPATGQVAAQQGTYLAKCFDRMEvceknpegpirirgEGRHRFRPFRYRHLGQFAPLGGEQTAAQLpG 533
Cdd:PTZ00318 325 ------------LPTLAQVASQQGVYLAKEFNNEL--------------KGKPMSKPFVYRSLGSLAYLGNYSAIVQL-G 377
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 240256027 534 DWVSIGHSSQWLWYSVYASKQVSWRTRVLVVSDWMRRFIFGRDSSRI 580
Cdd:PTZ00318 378 AFDLSGFKALLFWRSAYLTILGSWRSKLYVLVNWAGTAIFGRDITRF 424
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
55-564 |
1.45e-77 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 250.43 E-value: 1.45e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 55 KRKVVLLGTGWAGASFLKTLNN---SSYEVQVISPRNYFAFTPLLPSVTCGTVEARSVVEPIRNIARKQNVEmsFLEAEC 131
Cdd:COG1252 1 MKRIVIVGGGFAGLEAARRLRKklgGDAEVTLIDPNPYHLFQPLLPEVAAGTLSPDDIAIPLRELLRRAGVR--FIQGEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 132 FKIDPGSKKVYCRSKQgvnskgkkefDVDYDYLVIATGAQSNTFNIPGVEENCHFLKEVEDAQRIRSTVIDSFEKAslpg 211
Cdd:COG1252 79 TGIDPEARTVTLADGR----------TLSYDYLVIATGSVTNFFGIPGLAEHALPLKTLEDALALRERLLAAFERA---- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 212 lneqERKRMLHFvvvgggptgV---------EFASELHDFVNEdLVKLYPKAKNLVQITLLEAADHILTMFDKRITEFAE 282
Cdd:COG1252 145 ----ERRRLLTI---------VvvgggptgvELAGELAELLRK-LLRYPGIDPDKVRITLVEAGPRILPGLGEKLSEAAE 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 283 EKFTRDGIDVKLGSMVVKVNDKEIsaKTKAGEvsTIPYGMIVWSTGIGTRPVIKDFMKQIGQGNRraLATDEWLRVEGCD 362
Cdd:COG1252 211 KELEKRGVEVHTGTRVTEVDADGV--TLEDGE--EIPADTVIWAAGVKAPPLLADLGLPTDRRGR--VLVDPTLQVPGHP 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 363 NIYALGDCATInqrkvmediaaifkkadkensgtltmkefhevmsdicdrypqvelylkskgmhgitdllkqaqaengsn 442
Cdd:COG1252 285 NVFAIGDCAAV--------------------------------------------------------------------- 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 443 ksveldieelksalcqVDSQVKLLPATGQVAAQQGTYLAKCFDRmevceknpegpiRIRGEGRhrfRPFRYRHLGQFAPL 522
Cdd:COG1252 296 ----------------PDPDGKPVPKTAQAAVQQAKVLAKNIAA------------LLRGKPL---KPFRYRDKGCLASL 344
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 240256027 523 GGEQTAAQLPGDWVS--IGHssqWLWYSVYASKQVSWRTRVLVV 564
Cdd:COG1252 345 GRGAAVADVGGLKLSgfLAW---LLKRAIHLYFLPGFRGRLRVL 385
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
57-370 |
2.57e-54 |
|
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: 2.57e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 57 KVVLLGTGWAGASFLKTLNNSSYEVQVIS-PRNYFAFTPLLPSVTCGTVEARS-------VVEPIRNIARKQNVEMSF-L 127
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGGKVTLIEdEGTCPYGGCVLSKALLGAAEAPEiaslwadLYKRKEEVVKKLNNGIEVlL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 128 EAECFKIDPGSKKVYCRskqgvNSKGKKEFDVDYDYLVIATGAQSNTFNIPGVEENCHFL-KEVEDAQRIRSTVIDsfEK 206
Cdd:pfam07992 82 GTEVVSIDPGAKKVVLE-----ELVDGDGETITYDRLVIATGARPRLPPIPGVELNVGFLvRTLDSAEALRLKLLP--KR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 207 -----ASLPGLneqerkrmlhfvvvgggptgvEFASELHDFVnedlvklypkaknlVQITLLEAADHILTMFDKRITEFA 281
Cdd:pfam07992 155 vvvvgGGYIGV---------------------ELAAALAKLG--------------KEVTLIEALDRLLRAFDEEISAAL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 282 EEKFTRDGIDVKLGSMVVKVNDKEISAKTKAGEVSTIPYGMIVWstGIGTRPVIkDFMKQIG--QGNRRALATDEWLRVE 359
Cdd:pfam07992 200 EKALEKNGVEVRLGTSVKEIIGDGDGVEVILKDGTEIDADLVVV--AIGRRPNT-ELLEAAGleLDERGGIVVDEYLRTS 276
|
330
....*....|.
gi 240256027 360 gCDNIYALGDC 370
Cdd:pfam07992 277 -VPGIYAAGDC 286
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
118-373 |
6.73e-30 |
|
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: 119.92 E-value: 6.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 118 RKQNVEMsFLEAECFKIDPGSKKVYCRSKQgvnskgkkefDVDYDYLVIATGAQSNTFNIPGVE-ENCHFLKEVEDAQRI 196
Cdd:COG0446 47 ERKGIDV-RTGTEVTAIDPEAKTVTLRDGE----------TLSYDKLVLATGARPRPPPIPGLDlPGVFTLRTLDDADAL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 197 RSTvidsfekaslpgLNEQERKR---------MLhfvvvgggptgvEFASELHdfvnedlvklypKAKnlVQITLLEAAD 267
Cdd:COG0446 116 REA------------LKEFKGKRavvigggpiGL------------ELAEALR------------KRG--LKVTLVERAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 268 HILTMFDKRITEFAEEKFTRDGIDVKLGSMVVKVN-DKEISAKTKAGEvsTIPYGMIVwsTGIGTRPVIkDFMKQIG--Q 344
Cdd:COG0446 158 RLLGVLDPEMAALLEEELREHGVELRLGETVVAIDgDDKVAVTLTDGE--EIPADLVV--VAPGVRPNT-ELAKDAGlaL 232
|
250 260
....*....|....*....|....*....
gi 240256027 345 GNRRALATDEWLRVeGCDNIYALGDCATI 373
Cdd:COG0446 233 GERGWIKVDETLQT-SDPDVYAAGDCAEV 260
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
55-376 |
8.58e-25 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 106.76 E-value: 8.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 55 KRKVVLLGTGWAGASFLKTL--NNSSYEVQVISPRNYFAFT-PLLPSVTCGTVEARSVVEPIRNIARKQNVEMsFLEAEC 131
Cdd:COG1251 1 KMRIVIIGAGMAGVRAAEELrkLDPDGEITVIGAEPHPPYNrPPLSKVLAGETDEEDLLLRPADFYEENGIDL-RLGTRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 132 FKIDPGSKKVYCRSKQgvnskgkkefDVDYDYLVIATGAQSNTFNIPGVE-ENCHFLKEVEDAQRIRS--------TVID 202
Cdd:COG1251 80 TAIDRAARTVTLADGE----------TLPYDKLVLATGSRPRVPPIPGADlPGVFTLRTLDDADALRAalapgkrvVVIG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 203 sfekASLPGLneqerkrmlhfvvvgggptgvEFASELhdfvnedlvklypkAKNLVQITLLEAADHIL-TMFDKRITEFA 281
Cdd:COG1251 150 ----GGLIGL---------------------EAAAAL--------------RKRGLEVTVVERAPRLLpRQLDEEAGALL 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 282 EEKFTRDGIDVKLGSMVVKV--NDKEISAKTKAGEvsTIPYGMIVWSTGIgtRPVIkDFMKQ----IGQGnrraLATDEW 355
Cdd:COG1251 191 QRLLEALGVEVRLGTGVTEIegDDRVTGVRLADGE--ELPADLVVVAIGV--RPNT-ELARAaglaVDRG----IVVDDY 261
|
330 340
....*....|....*....|.
gi 240256027 356 LRVeGCDNIYALGDCATINQR 376
Cdd:COG1251 262 LRT-SDPDIYAAGDCAEHPGP 281
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
57-376 |
6.94e-20 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 92.41 E-value: 6.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 57 KVVLLGTGWAGASFLKTL--NNSSYEVQVISPRNYFAFTPL-LPSVTCGTVEarsvvEPIRNIAR------KQNVEMsFL 127
Cdd:PRK09564 2 KIIIIGGTAAGMSAAAKAkrLNKELEITVYEKTDIVSFGACgLPYFVGGFFD-----DPNTMIARtpeefiKSGIDV-KT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 128 EAECFKIDPGSKKVYCRskqgvNSKGKKEFDVDYDYLVIATGAQSNTFNIPGVE-ENCHFLKEVEDAQRIRSTVIDSFEK 206
Cdd:PRK09564 76 EHEVVKVDAKNKTITVK-----NLKTGSIFNDTYDKLMIATGARPIIPPIKNINlENVYTLKSMEDGLALKELLKDEEIK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 207 ------ASLPGLneqerkrmlhfvvvgggptgvEFASELHDfvnedlvklypKAKNlvqITLLEAADHILT-MFDKRITE 279
Cdd:PRK09564 151 niviigAGFIGL---------------------EAVEAAKH-----------LGKN---VRIIQLEDRILPdSFDKEITD 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 280 FAEEKFTRDGIDVKLGSMVVKV--NDKEISAKTKAGEVSTipyGMIVWSTGIgtRP---VIKD-FMKQIGQGnrrALATD 353
Cdd:PRK09564 196 VMEEELRENGVELHLNEFVKSLigEDKVEGVVTDKGEYEA---DVVIVATGV--KPnteFLEDtGLKTLKNG---AIIVD 267
|
330 340
....*....|....*....|...
gi 240256027 354 EWLRVEgCDNIYALGDCATINQR 376
Cdd:PRK09564 268 EYGETS-IENIYAAGDCATIYNI 289
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
162-371 |
3.29e-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: 3.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 162 DYLVIATGAQSNTFNIPGVEENchflkevedaqrirsTVIDS---FEKASLPglneqerKRM---------Lhfvvvggg 229
Cdd:COG1249 132 DHIVIATGSRPRVPPIPGLDEV---------------RVLTSdeaLELEELP-------KSLvvigggyigL-------- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 230 ptgvEFASELHDFVnedlvklypkaknlVQITLLEAADHILTMFDKRITEFAEEKFTRDGIDVKLGSMVVKV--NDKEIS 307
Cdd:COG1249 182 ----EFAQIFARLG--------------SEVTLVERGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVekTGDGVT 243
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 240256027 308 AKTKAGE-VSTIPYGMIVWSTGIgtRPVIKDF-MKQIG--QGNRRALATDEWLRVeGCDNIYALGDCA 371
Cdd:COG1249 244 VTLEDGGgEEAVEADKVLVATGR--RPNTDGLgLEAAGveLDERGGIKVDEYLRT-SVPGIYAIGDVT 308
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
258-369 |
2.20e-11 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 66.32 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 258 VQITLLEAADHILTMFDKRITEFAEEKFTRDGIDVKLGSMVVKV--NDKEISAKT-KAGEVSTIPYGMIVWSTGIgtRPV 334
Cdd:PRK06416 196 AEVTIVEALPRILPGEDKEISKLAERALKKRGIKIKTGAKAKKVeqTDDGVTVTLeDGGKEETLEADYVLVAVGR--RPN 273
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 240256027 335 IKDfmkqIG---QG---NRRALATDEWLRvEGCDNIYALGD 369
Cdd:PRK06416 274 TEN----LGleeLGvktDRGFIEVDEQLR-TNVPNIYAIGD 309
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
151-370 |
3.25e-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: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 151 SKGKKEFDVDYDYLVIATGAQSNTFNIPGVEEnchflkevedaqriRSTVIDSFEKASLPGLNEqerkrmlHFVVVGGGP 230
Cdd:TIGR01350 122 TGENGEETLEAKNIIIATGSRPRSLPGPFDFD--------------GKVVITSTGALNLEEVPE-------SLVIIGGGV 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 231 TGVEFASELHDFVnedlvklypkaknlVQITLLEAADHILTMFDKRITEFAEEKFTRDGIDVKLGSMVVKV--NDKEISA 308
Cdd:TIGR01350 181 IGIEFASIFASLG--------------SKVTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILTNTKVTAVekNDDQVTY 246
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240256027 309 KTKAGEVSTIPYGMIVWStgIGTRPVIKDF-MKQIG--QGNRRALATDEWLRVeGCDNIYALGDC 370
Cdd:TIGR01350 247 ENKGGETETLTGEKVLVA--VGRKPNTEGLgLEKLGveLDERGRIVVDEYMRT-NVPGIYAIGDV 308
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
162-370 |
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 240256027 162 DYLVIATGaqSNTFNIPGVEEnchflkeVEDAQRIRSTviDSFEKASLPglneqerKRMLHFVVVgggPTGVEFASELHd 241
Cdd:PRK06292 132 KNIVIATG--SRVPPIPGVWL-------ILGDRLLTSD--DAFELDKLP-------KSLAVIGGG---VIGLELGQALS- 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 242 fvnedlvklypkakNL-VQITLLEAADHILTMFDKRITEFAEEKFTRDgIDVKLGSMVVKV---NDKEISAKTKAGEVST 317
Cdd:PRK06292 190 --------------RLgVKVTVFERGDRILPLEDPEVSKQAQKILSKE-FKIKLGAKVTSVeksGDEKVEELEKGGKTET 254
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240256027 318 IPYGMIVWSTGIgtRPVIKDF-MKQIGqgnrraLATDEWLRVE-------GCDNIYALGDC 370
Cdd:PRK06292 255 IEADYVLVATGR--RPNTDGLgLENTG------IELDERGRPVvdehtqtSVPGIYAAGDV 307
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
58-376 |
3.05e-06 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 50.21 E-value: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 58 VVLLGTGWAGASF---LKTLNNSSYEVQVISPRNYFAFTP-LLPSVTCGTVEARSVVEPIRNIARKQNVEMsFLEAECFK 133
Cdd:TIGR02374 1 LVLVGNGMAGHRCieeVLKLNRHMFEITIFGEEPHPNYNRiLLSSVLQGEADLDDITLNSKDWYEKHGITL-YTGETVIQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 134 IDPGSKKVycrskqgVNSKGKKEFdvdYDYLVIATGAQSNTFNIPGVE-ENCHFLKEVEDAQRIRSTViDSFEKASL--P 210
Cdd:TIGR02374 80 IDTDQKQV-------ITDAGRTLS---YDKLILATGSYPFILPIPGADkKGVYVFRTIEDLDAIMAMA-QRFKKAAVigG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 211 GLNEQERKRMLhfvvvgggptgVEFASELHdfvnedLVKLYPKaknLVQITLLEAADHILtmfdkritefaEEKFTRDGI 290
Cdd:TIGR02374 149 GLLGLEAAVGL-----------QNLGMDVS------VIHHAPG---LMAKQLDQTAGRLL-----------QRELEQKGL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 291 DVKLGSmvvkvNDKEISAKTKAGEV-----STIPYGMIVWSTGIgtRPVIKdFMKQIGQGNRRALATDEWLRVEGcDNIY 365
Cdd:TIGR02374 198 TFLLEK-----DTVEIVGATKADRIrfkdgSSLEADLIVMAAGI--RPNDE-LAVSAGIKVNRGIIVNDSMQTSD-PDIY 268
|
330
....*....|.
gi 240256027 366 ALGDCATINQR 376
Cdd:TIGR02374 269 AVGECAEHNGR 279
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
130-378 |
3.36e-06 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 49.78 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 130 ECFKIDPGSKKVYCRskqgvNSKGKKEFDVDYDYLVIATGAQSNTfniPGVEENCHF-LKEVEDAQRirstvIDSFekas 208
Cdd:PRK13512 80 EVIAINDERQTVTVL-----NRKTNEQFEESYDKLILSPGASANS---LGFESDITFtLRNLEDTDA-----IDQF---- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 209 lpgLNEQERKRMLHFVVVGGGPtgvefaselhdfvnEDLVKLYPKAknlVQITLLEAADHILTMFDKRITEFAEEKFTRD 288
Cdd:PRK13512 143 ---IKANQVDKALVVGAGYISL--------------EVLENLYERG---LHPTLIHRSDKINKLMDADMNQPILDELDKR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 289 GIDVKLGSMVVKVNDKEISAKTkaGEVSTipYGMIVwsTGIGTRPVIKdFMKqigqGNRRALATDEWLRVE-----GCDN 363
Cdd:PRK13512 203 EIPYRLNEEIDAINGNEVTFKS--GKVEH--YDMII--EGVGTHPNSK-FIE----SSNIKLDDKGFIPVNdkfetNVPN 271
|
250
....*....|....*
gi 240256027 364 IYALGDCATINQRKV 378
Cdd:PRK13512 272 IYAIGDIITSHYRHV 286
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
258-371 |
4.47e-06 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 49.54 E-value: 4.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 258 VQITLLEAADHILTMFDKRITEFAEEKFTRDGIDVKLGsmvVKVNDKEISAK-------TKAGEVSTIPYGMIVWStgIG 330
Cdd:PRK06327 207 AEVTILEALPAFLAAADEQVAKEAAKAFTKQGLDIHLG---VKIGEIKTGGKgvsvaytDADGEAQTLEVDKLIVS--IG 281
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 240256027 331 TRPVIKDfmkqIGQGN-------RRALATDEWLRVeGCDNIYALGDCA 371
Cdd:PRK06327 282 RVPNTDG----LGLEAvglkldeRGFIPVDDHCRT-NVPNVYAIGDVV 324
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
162-369 |
8.22e-06 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 48.59 E-value: 8.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 162 DYLVIATGAQSNTFNIPGVEENCHFLKevedaqrirSTVIDSFEKasLPglneqerKRMlhfVVVGGGPTGVEFASelhd 241
Cdd:PRK07251 120 ETIVINTGAVSNVLPIPGLADSKHVYD---------STGIQSLET--LP-------ERL---GIIGGGNIGLEFAG---- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 242 fvnedlvkLYPKAKNlvQITLLEAADHILTMFDKRITEFAEEKFTRDGIDVKLGSMVVKV-NDKEISAKTKAGEvsTIPY 320
Cdd:PRK07251 175 --------LYNKLGS--KVTVLDAASTILPREEPSVAALAKQYMEEDGITFLLNAHTTEVkNDGDQVLVVTEDE--TYRF 242
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 240256027 321 GMIVWSTgiGTRPVIKDFMKQ---IGQGNRRALATDEWLR--VEGcdnIYALGD 369
Cdd:PRK07251 243 DALLYAT--GRKPNTEPLGLEntdIELTERGAIKVDDYCQtsVPG---VFAVGD 291
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
234-313 |
2.02e-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: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 234 EFASELHDFVnedlvklypkaknlVQITLLEAADHILTMFDKRITEFAEEKFTRDGIDVKLGSMVVKV--NDKEISAKTK 311
Cdd:pfam00070 13 ELAGALARLG--------------SKVTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIegNGDGVVVVLT 78
|
..
gi 240256027 312 AG 313
Cdd:pfam00070 79 DG 80
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
259-379 |
7.90e-05 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 45.29 E-value: 7.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 259 QITLLEAADHIL-TMFDKRITEFAEEKFTRDGIDVKLGSMVVKVN--DKEISAKTKAGEVSTIPygmIVWStGIGTRPVI 335
Cdd:PRK04965 166 AVTLVDNAASLLaSLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEktDSGIRATLDSGRSIEVD---AVIA-AAGLRPNT 241
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 240256027 336 KdFMKQIGQGNRRALATDEWLRVEGcDNIYALGDCATINQrKVM 379
Cdd:PRK04965 242 A-LARRAGLAVNRGIVVDSYLQTSA-PDIYALGDCAEING-QVL 282
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
55-369 |
1.82e-04 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 44.23 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 55 KRKVVLLGTGWAGASFLKTLNNSSYEVQVISPRN-YFAFTpllpSVTCGTVEARSVVEP-------IRNIARKQNVeMSF 126
Cdd:PRK08010 3 KYQAVIIGFGKAGKTLAVTLAKAGWRVALIEQSNaMYGGT----CINIGCIPTKTLVHDaqqhtdfVRAIQRKNEV-VNF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 127 LEAECFK-----------------IDPGSKKVYcRSKQGVNSKGKKEFdvdydylvIATGAQSNTFNIPGVeenchflke 189
Cdd:PRK08010 78 LRNKNFHnladmpnidvidgqaefINNHSLRVH-RPEGNLEIHGEKIF--------INTGAQTVVPPIPGI--------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 190 vedaqrirSTVIDSFEKASLPGLNEqerkRMLHFVVVGGGPTGVEFASELHDFVNedlvklypkaknlvQITLLEAADHI 269
Cdd:PRK08010 140 --------TTTPGVYDSTGLLNLKE----LPGHLGILGGGYIGVEFASMFANFGS--------------KVTILEAASLF 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 270 LTMFDKRITEFAEEKFTRDGIDVKLGSMVVKVNDKEISAKTKAGEVSTIPYGMIVWStgiGTRPVIKDFMKQ---IGQGN 346
Cdd:PRK08010 194 LPREDRDIADNIATILRDQGVDIILNAHVERISHHENQVQVHSEHAQLAVDALLIAS---GRQPATASLHPEnagIAVNE 270
|
330 340
....*....|....*....|...
gi 240256027 347 RRALATDEWLRVEGcDNIYALGD 369
Cdd:PRK08010 271 RGAIVVDKYLHTTA-DNIWAMGD 292
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
373-407 |
2.39e-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: 36.76 E-value: 2.39e-03
10 20 30
....*....|....*....|....*....|....*
gi 240256027 373 INQRKVMEDIAAIFKKADKENSGTLTMKEFHEVMS 407
Cdd:cd00051 29 LGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
162-370 |
3.23e-03 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 40.14 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 162 DYLVIATGAQSNTFNIPGVEencHflkevedaqrirstVIDS---FEKASLPglneqerKRMLhfvVVGGGPTGVEFASE 238
Cdd:PRK06116 133 DHILIATGGRPSIPDIPGAE---Y--------------GITSdgfFALEELP-------KRVA---VVGAGYIAVEFAGV 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240256027 239 LHdfvnedlvklypkakNL-VQITLLEAADHILTMFDKRITEFAEEKFTRDGIDVKLGSM---VVKVNDKEISAKTKAGE 314
Cdd:PRK06116 186 LN---------------GLgSETHLFVRGDAPLRGFDPDIRETLVEEMEKKGIRLHTNAVpkaVEKNADGSLTLTLEDGE 250
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 240256027 315 VSTIpyGMIVWStgIGTRPVIKDF-MKQIG--QGNRRALATDEWLR--VEGcdnIYALGDC 370
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 ... |
381-409 |
6.60e-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: 6.60e-03
10 20
....*....|....*....|....*....
gi 240256027 381 DIAAIFKKADKENSGTLTMKEFHEVMSDI 409
Cdd:pfam00036 1 ELKEIFRLFDKDGDGKIDFEEFKELLKKL 29
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