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Conserved domains on  [gi|1443087326|ref|XP_025882304|]
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external alternative NAD(P)H-ubiquinone oxidoreductase B1, mitochondrial [Oryza sativa Japonica Group]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTZ00318 super family cl33177
NADH dehydrogenase-like protein; Provisional
 61-588 4.88e-138

NADH dehydrogenase-like protein; Provisional


The actual alignment was detected with superfamily member PTZ00318:

Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 408.00  E-value: 4.88e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326  61 RKKKVVVLGTGWAGTSFLKDLDCSKYEVKVISPRNYFAFTPLLPSVTCGTVEARSIVEPIRKMLEKKrkDVAFYEAECFK 140
Cdd:PTZ00318    9 KKPNVVVLGTGWAGAYFVRNLDPKKYNITVISPRNHMLFTPLLPQTTTGTLEFRSICEPVRPALAKL--PNRYLRAVVYD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 141 IDASKKAVHCRSAVGTNFDGNGDFMVDYDYLVVALGATVNTFNTPGVMENCYFLKEVEDAQKIRRNVIDCFEKASLPNIS 220
Cdd:PTZ00318   87 VDFEEKRVKCGVVSKSNNANVNTFSVPYDKLVVAHGARPNTFNIPGVEERAFFLKEVNHARGIRKRIVQCIERASLPTTS 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 221 EEEKRKILHFVIIGGGPTGVEFAAEMHDFLVEDLVKLYPAIQDFVKITIIQSGEHILNMFDQRIATFAEMKFQRDGIEVN 300
Cdd:PTZ00318  167 VEERKRLLHFVVVGGGPTGVEFAAELADFFRDDVRNLNPELVEECKVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVDIR 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 301 TGFRVVKVSDDLITMKSkslGEVsVPYGMAVWSAGIGTRPVIMDFmqQIGQTNRRVLATNEWLRVHECDNIYAIGDCASI 380
Cdd:PTZ00318  247 TKTAVKEVLDKEVVLKD---GEV-IPTGLVVWSTGVGPGPLTKQL--KVDKTSRGRISVDDHLRVKPIPNVFALGDCAAN 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 381 TQRkimddistvfkmadkdnsgtltlkeindvledicirypqvelymksmhmldirdlikdaigdshkesmvvnieefkk 460
Cdd:PTZ00318  321 EER----------------------------------------------------------------------------- 323

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 461 alshvdsqvkSIPATAQVAAQQGHYLAECFNKMDQCKEHPegplrmtgtgsgrhnfRPFRYKHLGQFAPLGGEQAAAELp 540
Cdd:PTZ00318  324 ----------PLPTLAQVASQQGVYLAKEFNNELKGKPMS----------------KPFVYRSLGSLAYLGNYSAIVQL- 376

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 1443087326 541 GDWVSMGHSTQWLWYSVYASKQVSWRTRMLVVSDWTRRFIFGRDSSRI 588
Cdd:PTZ00318  377 GAFDLSGFKALLFWRSAYLTILGSWRSKLYVLVNWAGTAIFGRDITRF 424
EF-hand_7 pfam13499
EF-hand domain pair;
386-463 4.20e-04

EF-hand domain pair;


:

Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 38.77  E-value: 4.20e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1443087326 386 MDDISTVFKMADKDNSGTLTLKEINDVLEDICIrypqvelyMKSMHMLDIRDLIKDAigDSHKESmVVNIEEFKKALS 463
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEE--------GEPLSDEEVEELFKEF--DLDKDG-RISFEEFLELYS 67
 
Name Accession Description Interval E-value
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
 61-588 4.88e-138

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 408.00  E-value: 4.88e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326  61 RKKKVVVLGTGWAGTSFLKDLDCSKYEVKVISPRNYFAFTPLLPSVTCGTVEARSIVEPIRKMLEKKrkDVAFYEAECFK 140
Cdd:PTZ00318    9 KKPNVVVLGTGWAGAYFVRNLDPKKYNITVISPRNHMLFTPLLPQTTTGTLEFRSICEPVRPALAKL--PNRYLRAVVYD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 141 IDASKKAVHCRSAVGTNFDGNGDFMVDYDYLVVALGATVNTFNTPGVMENCYFLKEVEDAQKIRRNVIDCFEKASLPNIS 220
Cdd:PTZ00318   87 VDFEEKRVKCGVVSKSNNANVNTFSVPYDKLVVAHGARPNTFNIPGVEERAFFLKEVNHARGIRKRIVQCIERASLPTTS 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 221 EEEKRKILHFVIIGGGPTGVEFAAEMHDFLVEDLVKLYPAIQDFVKITIIQSGEHILNMFDQRIATFAEMKFQRDGIEVN 300
Cdd:PTZ00318  167 VEERKRLLHFVVVGGGPTGVEFAAELADFFRDDVRNLNPELVEECKVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVDIR 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 301 TGFRVVKVSDDLITMKSkslGEVsVPYGMAVWSAGIGTRPVIMDFmqQIGQTNRRVLATNEWLRVHECDNIYAIGDCASI 380
Cdd:PTZ00318  247 TKTAVKEVLDKEVVLKD---GEV-IPTGLVVWSTGVGPGPLTKQL--KVDKTSRGRISVDDHLRVKPIPNVFALGDCAAN 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 381 TQRkimddistvfkmadkdnsgtltlkeindvledicirypqvelymksmhmldirdlikdaigdshkesmvvnieefkk 460
Cdd:PTZ00318  321 EER----------------------------------------------------------------------------- 323

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 461 alshvdsqvkSIPATAQVAAQQGHYLAECFNKMDQCKEHPegplrmtgtgsgrhnfRPFRYKHLGQFAPLGGEQAAAELp 540
Cdd:PTZ00318  324 ----------PLPTLAQVASQQGVYLAKEFNNELKGKPMS----------------KPFVYRSLGSLAYLGNYSAIVQL- 376

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 1443087326 541 GDWVSMGHSTQWLWYSVYASKQVSWRTRMLVVSDWTRRFIFGRDSSRI 588
Cdd:PTZ00318  377 GAFDLSGFKALLFWRSAYLTILGSWRSKLYVLVNWAGTAIFGRDITRF 424
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
62-572 8.67e-82

NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 261.61  E-value: 8.67e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326  62 KKKVVVLGTGWAGTSF---LKDLDCSKYEVKVISPRNYFAFTPLLPSVTCGTVEARSIVEPIRKMLEKKRkdVAFYEAEC 138
Cdd:COG1252     1 MKRIVIVGGGFAGLEAarrLRKKLGGDAEVTLIDPNPYHLFQPLLPEVAAGTLSPDDIAIPLRELLRRAG--VRFIQGEV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 139 FKIDASKKAVHCRSavGTNfdgngdfmVDYDYLVVALGATVNTFNTPGVMENCYFLKEVEDAQKIRRNVIDCFEKAslpn 218
Cdd:COG1252    79 TGIDPEARTVTLAD--GRT--------LSYDYLVIATGSVTNFFGIPGLAEHALPLKTLEDALALRERLLAAFERA---- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 219 iseeEKRKILHFVIIGGGPTGVEFAAEMHDFLvEDLVKLYPAIQDFVKITIIQSGEHILNMFDQRIATFAEMKFQRDGIE 298
Cdd:COG1252   145 ----ERRRLLTIVVVGGGPTGVELAGELAELL-RKLLRYPGIDPDKVRITLVEAGPRILPGLGEKLSEAAEKELEKRGVE 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 299 VNTGFRVVKVSDDLITMKSkslGEvSVPYGMAVWSAGIgtRPVimDFMQQIG-QTNRRV-LATNEWLRVHECDNIYAIGD 376
Cdd:COG1252   220 VHTGTRVTEVDADGVTLED---GE-EIPADTVIWAAGV--KAP--PLLADLGlPTDRRGrVLVDPTLQVPGHPNVFAIGD 291

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 377 CASItqrkimddistvfkmadkdnsgtltlkeindvledicirypqvelymksmhmldirdlikdaigdshkesmvvnie 456
Cdd:COG1252   292 CAAV---------------------------------------------------------------------------- 295

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 457 efkkalshVDSQVKSIPATAQVAAQQGHYLAEcfNKMDQCKEHPEgplrmtgtgsgrhnfRPFRYKHLGQFAPLGGEQAA 536
Cdd:COG1252   296 --------PDPDGKPVPKTAQAAVQQAKVLAK--NIAALLRGKPL---------------KPFRYRDKGCLASLGRGAAV 350

                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 1443087326 537 AELPGDWVSmGHSTQWLWYSVYASKQVSWRTRMLVV 572
Cdd:COG1252   351 ADVGGLKLS-GFLAWLLKRAIHLYFLPGFRGRLRVL 385
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 63-377 1.14e-43

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 157.87  E-value: 1.14e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326  63 KKVVVLGTGWAGTSFLKDLDCSKYEVKVIS-PRNYFAFTPLLPSVTCGTVEARSI-------VEPIRKMLEKKRKDVAFY 134
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEdEGTCPYGGCVLSKALLGAAEAPEIaslwadlYKRKEEVVKKLNNGIEVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 135 -EAECFKIDASKKAVHCRSAVgtnfDGNGdFMVDYDYLVVALGATVNTFNTPGVMENCYFL-KEVEDAQKIRRNVIDCfe 212
Cdd:pfam07992  81 lGTEVVSIDPGAKKVVLEELV----DGDG-ETITYDRLVIATGARPRLPPIPGVELNVGFLvRTLDSAEALRLKLLPK-- 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 213 kaslpniseeekrkilHFVIIGGGPTGVEFAAEMHDFLVEdlvklypaiqdfvkITIIQSGEHILNMFDQRIATFAEMKF 292
Cdd:pfam07992 154 ----------------RVVVVGGGYIGVELAAALAKLGKE--------------VTLIEALDRLLRAFDEEISAALEKAL 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 293 QRDGIEVNTGFRVVKVSDDLITMKSKSLGEVSVPYGMAVWsaGIGTRPVImDFMQQIG--QTNRRVLATNEWLRVhECDN 370
Cdd:pfam07992 204 EKNGVEVRLGTSVKEIIGDGDGVEVILKDGTEIDADLVVV--AIGRRPNT-ELLEAAGleLDERGGIVVDEYLRT-SVPG 279


                  ....*..
gi 1443087326 371 IYAIGDC 377
Cdd:pfam07992 280 IYAAGDC 286
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
 159-377 1.22e-14

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: 76.53  E-value: 1.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 159 DGNGDFMVDYDYLVVALGATVNTFntPGVMEncyflkevEDAQKirrnVIDCFEKASLPNISEeekrkilHFVIIGGGPT 238
Cdd:TIGR01350 123 GENGEETLEAKNIIIATGSRPRSL--PGPFD--------FDGKV----VITSTGALNLEEVPE-------SLVIIGGGVI 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 239 GVEFAAEMHDFlvedlvklypaiqdFVKITIIQSGEHILNMFDQRIATFAEMKFQRDGIEVNTGFRVVKVS--DDLITMK 316
Cdd:TIGR01350 182 GIEFASIFASL--------------GSKVTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILTNTKVTAVEknDDQVTYE 247

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1443087326 317 SKSlGEVSVPYGMAVWSAgIGTRPVIMDF-MQQIG--QTNRRVLATNEWLRVHEcDNIYAIGDC 377
Cdd:TIGR01350 248 NKG-GETETLTGEKVLVA-VGRKPNTEGLgLEKLGveLDERGRIVVDEYMRTNV-PGIYAIGDV 308
EF-hand_7 pfam13499
EF-hand domain pair;
386-463 4.20e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 38.77  E-value: 4.20e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1443087326 386 MDDISTVFKMADKDNSGTLTLKEINDVLEDICIrypqvelyMKSMHMLDIRDLIKDAigDSHKESmVVNIEEFKKALS 463
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEE--------GEPLSDEEVEELFKEF--DLDKDG-RISFEEFLELYS 67
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
 389-458 3.40e-03

EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta isozymes represent a class of metazoan PI-PLCs that are some of the most sensitive to calcium among all PLCs. Their activation is modulated by intracellular calcium ion concentration, phospholipids, polyamines, and other proteins, such as RhoAGAP. Like other PI-PLC isozymes, PI-PLC-delta isozymes contain a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C-terminal C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There are three PI-PLC-delta isozymes (1, 3 and 4). PI-PLC-delta1 is relatively well characterized. It is activated by high calcium levels generated by other PI-PLC family members, and therefore functions as a calcium amplifier within the cell. Different PI-PLC-delta isozymes have different tissue distribution and different subcellular locations. PI-PLC-delta1 is mostly a cytoplasmic protein, PI-PLC-delta3 is located in the membrane, and PI-PLC-delta4 is predominantly detected in the cell nucleus. PI-PLC-delta isozymes is evolutionarily conserved even in non-mammalian species, such as yeast, slime molds and plants.


Pssm-ID: 320032 [Multi-domain]  Cd Length: 140  Bit Score: 37.98  E-value: 3.40e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 389 ISTVFKMADKDNSGTLTLKEINDVLEDICIRypqvelyMKSMHmldIRDLIKDAIgdsHKESMVVNIEEF 458
Cdd:cd16202     2 LKDQFRKADKNGDGKLSFKECKKLLKKLNVK-------VDKDY---AKKLFQEAD---TSGEDVLDEEEF 58
 
Name Accession Description Interval E-value
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
 61-588 4.88e-138

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 408.00  E-value: 4.88e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326  61 RKKKVVVLGTGWAGTSFLKDLDCSKYEVKVISPRNYFAFTPLLPSVTCGTVEARSIVEPIRKMLEKKrkDVAFYEAECFK 140
Cdd:PTZ00318    9 KKPNVVVLGTGWAGAYFVRNLDPKKYNITVISPRNHMLFTPLLPQTTTGTLEFRSICEPVRPALAKL--PNRYLRAVVYD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 141 IDASKKAVHCRSAVGTNFDGNGDFMVDYDYLVVALGATVNTFNTPGVMENCYFLKEVEDAQKIRRNVIDCFEKASLPNIS 220
Cdd:PTZ00318   87 VDFEEKRVKCGVVSKSNNANVNTFSVPYDKLVVAHGARPNTFNIPGVEERAFFLKEVNHARGIRKRIVQCIERASLPTTS 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 221 EEEKRKILHFVIIGGGPTGVEFAAEMHDFLVEDLVKLYPAIQDFVKITIIQSGEHILNMFDQRIATFAEMKFQRDGIEVN 300
Cdd:PTZ00318  167 VEERKRLLHFVVVGGGPTGVEFAAELADFFRDDVRNLNPELVEECKVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVDIR 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 301 TGFRVVKVSDDLITMKSkslGEVsVPYGMAVWSAGIGTRPVIMDFmqQIGQTNRRVLATNEWLRVHECDNIYAIGDCASI 380
Cdd:PTZ00318  247 TKTAVKEVLDKEVVLKD---GEV-IPTGLVVWSTGVGPGPLTKQL--KVDKTSRGRISVDDHLRVKPIPNVFALGDCAAN 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 381 TQRkimddistvfkmadkdnsgtltlkeindvledicirypqvelymksmhmldirdlikdaigdshkesmvvnieefkk 460
Cdd:PTZ00318  321 EER----------------------------------------------------------------------------- 323

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 461 alshvdsqvkSIPATAQVAAQQGHYLAECFNKMDQCKEHPegplrmtgtgsgrhnfRPFRYKHLGQFAPLGGEQAAAELp 540
Cdd:PTZ00318  324 ----------PLPTLAQVASQQGVYLAKEFNNELKGKPMS----------------KPFVYRSLGSLAYLGNYSAIVQL- 376

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 1443087326 541 GDWVSMGHSTQWLWYSVYASKQVSWRTRMLVVSDWTRRFIFGRDSSRI 588
Cdd:PTZ00318  377 GAFDLSGFKALLFWRSAYLTILGSWRSKLYVLVNWAGTAIFGRDITRF 424
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
62-572 8.67e-82

NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 261.61  E-value: 8.67e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326  62 KKKVVVLGTGWAGTSF---LKDLDCSKYEVKVISPRNYFAFTPLLPSVTCGTVEARSIVEPIRKMLEKKRkdVAFYEAEC 138
Cdd:COG1252     1 MKRIVIVGGGFAGLEAarrLRKKLGGDAEVTLIDPNPYHLFQPLLPEVAAGTLSPDDIAIPLRELLRRAG--VRFIQGEV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 139 FKIDASKKAVHCRSavGTNfdgngdfmVDYDYLVVALGATVNTFNTPGVMENCYFLKEVEDAQKIRRNVIDCFEKAslpn 218
Cdd:COG1252    79 TGIDPEARTVTLAD--GRT--------LSYDYLVIATGSVTNFFGIPGLAEHALPLKTLEDALALRERLLAAFERA---- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 219 iseeEKRKILHFVIIGGGPTGVEFAAEMHDFLvEDLVKLYPAIQDFVKITIIQSGEHILNMFDQRIATFAEMKFQRDGIE 298
Cdd:COG1252   145 ----ERRRLLTIVVVGGGPTGVELAGELAELL-RKLLRYPGIDPDKVRITLVEAGPRILPGLGEKLSEAAEKELEKRGVE 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 299 VNTGFRVVKVSDDLITMKSkslGEvSVPYGMAVWSAGIgtRPVimDFMQQIG-QTNRRV-LATNEWLRVHECDNIYAIGD 376
Cdd:COG1252   220 VHTGTRVTEVDADGVTLED---GE-EIPADTVIWAAGV--KAP--PLLADLGlPTDRRGrVLVDPTLQVPGHPNVFAIGD 291

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 377 CASItqrkimddistvfkmadkdnsgtltlkeindvledicirypqvelymksmhmldirdlikdaigdshkesmvvnie 456
Cdd:COG1252   292 CAAV---------------------------------------------------------------------------- 295

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 457 efkkalshVDSQVKSIPATAQVAAQQGHYLAEcfNKMDQCKEHPEgplrmtgtgsgrhnfRPFRYKHLGQFAPLGGEQAA 536
Cdd:COG1252   296 --------PDPDGKPVPKTAQAAVQQAKVLAK--NIAALLRGKPL---------------KPFRYRDKGCLASLGRGAAV 350

                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 1443087326 537 AELPGDWVSmGHSTQWLWYSVYASKQVSWRTRMLVV 572
Cdd:COG1252   351 ADVGGLKLS-GFLAWLLKRAIHLYFLPGFRGRLRVL 385
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 63-377 1.14e-43

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 157.87  E-value: 1.14e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326  63 KKVVVLGTGWAGTSFLKDLDCSKYEVKVIS-PRNYFAFTPLLPSVTCGTVEARSI-------VEPIRKMLEKKRKDVAFY 134
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEdEGTCPYGGCVLSKALLGAAEAPEIaslwadlYKRKEEVVKKLNNGIEVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 135 -EAECFKIDASKKAVHCRSAVgtnfDGNGdFMVDYDYLVVALGATVNTFNTPGVMENCYFL-KEVEDAQKIRRNVIDCfe 212
Cdd:pfam07992  81 lGTEVVSIDPGAKKVVLEELV----DGDG-ETITYDRLVIATGARPRLPPIPGVELNVGFLvRTLDSAEALRLKLLPK-- 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 213 kaslpniseeekrkilHFVIIGGGPTGVEFAAEMHDFLVEdlvklypaiqdfvkITIIQSGEHILNMFDQRIATFAEMKF 292
Cdd:pfam07992 154 ----------------RVVVVGGGYIGVELAAALAKLGKE--------------VTLIEALDRLLRAFDEEISAALEKAL 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 293 QRDGIEVNTGFRVVKVSDDLITMKSKSLGEVSVPYGMAVWsaGIGTRPVImDFMQQIG--QTNRRVLATNEWLRVhECDN 370
Cdd:pfam07992 204 EKNGVEVRLGTSVKEIIGDGDGVEVILKDGTEIDADLVVV--AIGRRPNT-ELLEAAGleLDERGGIVVDEYLRT-SVPG 279


                  ....*..
gi 1443087326 371 IYAIGDC 377
Cdd:pfam07992 280 IYAAGDC 286
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 140-381 2.78e-27

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: 112.60  E-value: 2.78e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 140 KIDASKKAVHCRSavGTNfdgngdfmVDYDYLVVALGATVNTFNTPGV-MENCYFLKEVEDAQKIRRNVidcfekaslpn 218
Cdd:COG0446    61 AIDPEAKTVTLRD--GET--------LSYDKLVLATGARPRPPPIPGLdLPGVFTLRTLDDADALREAL----------- 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 219 iseeEKRKILHFVIIGGGPTGVEFAaemhdflvEDLVKLYpaiqdfVKITIIQSGEHILNMFDQRIATFAEMKFQRDGIE 298
Cdd:COG0446   120 ----KEFKGKRAVVIGGGPIGLELA--------EALRKRG------LKVTLVERAPRLLGVLDPEMAALLEEELREHGVE 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 299 VNTGFRVVKV-SDDLITMKSKSlGEVsVPYGMAVwsAGIGTRPVImDFMQQIG-QTNRRV-LATNEWLRvHECDNIYAIG 375
Cdd:COG0446   182 LRLGETVVAIdGDDKVAVTLTD-GEE-IPADLVV--VAPGVRPNT-ELAKDAGlALGERGwIKVDETLQ-TSDPDVYAAG 255


                  ....*.
gi 1443087326 376 DCASIT 381
Cdd:COG0446   256 DCAEVP 261
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
62-380 4.07e-23

NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 101.76  E-value: 4.07e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326  62 KKKVVVLGTGWAGTSF---LKDLDcSKYEVKVISPRNYFAFT-PLLPSVTCGTVEARSIVEPIRKMLEKKRKDVaFYEAE 137
Cdd:COG1251     1 KMRIVIIGAGMAGVRAaeeLRKLD-PDGEITVIGAEPHPPYNrPPLSKVLAGETDEEDLLLRPADFYEENGIDL-RLGTR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 138 CFKIDASKKAVHcrsavgtnfDGNGDfMVDYDYLVVALGATVNTFNTPGV-MENCYFLKEVEDAQKIRRNVidcfekasl 216
Cdd:COG1251    79 VTAIDRAARTVT---------LADGE-TLPYDKLVLATGSRPRVPPIPGAdLPGVFTLRTLDDADALRAAL--------- 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 217 pniseEEKRKIlhfVIIGGGPTGVEFAAemhdflveDLVKLYpaiqdfVKITIIQSGEHILN-MFDQRIATFAEMKFQRD 295
Cdd:COG1251   140 -----APGKRV---VVIGGGLIGLEAAA--------ALRKRG------LEVTVVERAPRLLPrQLDEEAGALLQRLLEAL 197

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 296 GIEVNTGFRVVKV--SDDLITMKSKSlGEVsVPYGMAVwsAGIGTRPVImDFMQQIG-QTNRRVLaTNEWLRVHEcDNIY 372
Cdd:COG1251   198 GVEVRLGTGVTEIegDDRVTGVRLAD-GEE-LPADLVV--VAIGVRPNT-ELARAAGlAVDRGIV-VDDYLRTSD-PDIY 270


                  ....*...
gi 1443087326 373 AIGDCASI 380
Cdd:COG1251   271 AAGDCAEH 278
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 229-378 3.66e-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: 3.66e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 229 HFVIIGGGPTGVEFAAEMHDFlvedlvklypaiqdFVKITIIQSGEHILNMFDQRIATFAEMKFQRDGIEVNTGFRVVKV 308
Cdd:COG1249   170 SLVVIGGGYIGLEFAQIFARL--------------GSEVTLVERGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTSV 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 309 SDD----LITMKSKSlGEVSVPYGMAVWSAGIgtRPVImdfmQQIG------QTNRR-VLATNEWLRVhECDNIYAIGDC 377
Cdd:COG1249   236 EKTgdgvTVTLEDGG-GEEAVEADKVLVATGR--RPNT----DGLGleaagvELDERgGIKVDEYLRT-SVPGIYAIGDV 307


                  .
gi 1443087326 378 A 378
Cdd:COG1249   308 T 308
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
 159-377 1.22e-14

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: 76.53  E-value: 1.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 159 DGNGDFMVDYDYLVVALGATVNTFntPGVMEncyflkevEDAQKirrnVIDCFEKASLPNISEeekrkilHFVIIGGGPT 238
Cdd:TIGR01350 123 GENGEETLEAKNIIIATGSRPRSL--PGPFD--------FDGKV----VITSTGALNLEEVPE-------SLVIIGGGVI 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 239 GVEFAAEMHDFlvedlvklypaiqdFVKITIIQSGEHILNMFDQRIATFAEMKFQRDGIEVNTGFRVVKVS--DDLITMK 316
Cdd:TIGR01350 182 GIEFASIFASL--------------GSKVTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILTNTKVTAVEknDDQVTYE 247

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1443087326 317 SKSlGEVSVPYGMAVWSAgIGTRPVIMDF-MQQIG--QTNRRVLATNEWLRVHEcDNIYAIGDC 377
Cdd:TIGR01350 248 NKG-GETETLTGEKVLVA-VGRKPNTEGLgLEKLGveLDERGRIVVDEYMRTNV-PGIYAIGDV 308
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 205-376 1.69e-14

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 75.95  E-value: 1.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 205 RNVIDCFEKASLPNISEeekrkilHFVIIGGGPTGVEFAAEMHDFLVEdlvklypaiqdfvkITIIQSGEHILNMFDQRI 284
Cdd:PRK06416  157 RVIWTSDEALNLDEVPK-------SLVVIGGGYIGVEFASAYASLGAE--------------VTIVEALPRILPGEDKEI 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 285 ATFAEMKFQRDGIEVNTGFRVVKVS--DDLITMKSKSLGEVSVPYGMAVWSAgIGTRPVIMDF-MQQIG-QTNRRVLATN 360
Cdd:PRK06416  216 SKLAERALKKRGIKIKTGAKAKKVEqtDDGVTVTLEDGGKEETLEADYVLVA-VGRRPNTENLgLEELGvKTDRGFIEVD 294

                         170
                  ....*....|....*...
gi 1443087326 361 EWLR--VhecDNIYAIGD 376
Cdd:PRK06416  295 EQLRtnV---PNIYAIGD 309
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 63-383 3.32e-13

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 72.00  E-value: 3.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326  63 KKVVVLGTGWAGTSF---LKDLDcSKYEVKVISPRNYFAFTPL-LPSVTCGTV-EARSIVEPIRKMLEKKRKDVaFYEAE 137
Cdd:PRK09564    1 MKIIIIGGTAAGMSAaakAKRLN-KELEITVYEKTDIVSFGACgLPYFVGGFFdDPNTMIARTPEEFIKSGIDV-KTEHE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 138 CFKIDASKKAVHCRsavgtNFDGNGDFMVDYDYLVVALGATVNTFNTPGV-MENCYFLKEVEDAQKIRRNVIDcfekasl 216
Cdd:PRK09564   79 VVKVDAKNKTITVK-----NLKTGSIFNDTYDKLMIATGARPIIPPIKNInLENVYTLKSMEDGLALKELLKD------- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 217 pniseEEKRKIlhfVIIGGGPTGVEfaaemhdfLVEDLVKLYPaiqdfvKITIIQSGEHILN-MFDQRIATFAEMKFQRD 295
Cdd:PRK09564  147 -----EEIKNI---VIIGAGFIGLE--------AVEAAKHLGK------NVRIIQLEDRILPdSFDKEITDVMEEELREN 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 296 GIEVNTGFRVVKV-SDDLITMKSKSLGEVSVPYgmAVWSAGIgtRPViMDFM--QQIGQTNRRVLATNEWLRVhECDNIY 372
Cdd:PRK09564  205 GVELHLNEFVKSLiGEDKVEGVVTDKGEYEADV--VIVATGV--KPN-TEFLedTGLKTLKNGAIIVDEYGET-SIENIY 278

                         330
                  ....*....|.
gi 1443087326 373 AIGDCASITQR 383
Cdd:PRK09564  279 AAGDCATIYNI 289
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 229-311 1.70e-09

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 425450 [Multi-domain]  Cd Length: 80  Bit Score: 54.52  E-value: 1.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 229 HFVIIGGGPTGVEFAAEMHDFLVedlvklypaiqdfvKITIIQSGEHILNMFDQRIATFAEMKFQRDGIEVNTGFRVVKV 308
Cdd:pfam00070   1 RVVVVGGGYIGLELAGALARLGS--------------KVTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAI 66


                  ...
gi 1443087326 309 SDD 311
Cdd:pfam00070  67 EGN 69
PRK06370 PRK06370
FAD-containing oxidoreductase;
229-311 5.30e-07

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 52.51  E-value: 5.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 229 HFVIIGGGPTGVEFAaemhdflvedlvklypaiQDF----VKITIIQSGEHILNMFDQRIATFAEMKFQRDGIEVNTGFR 304
Cdd:PRK06370  173 HLVIIGGGYIGLEFA------------------QMFrrfgSEVTVIERGPRLLPREDEDVAAAVREILEREGIDVRLNAE 234


                  ....*..
gi 1443087326 305 VVKVSDD 311
Cdd:PRK06370  235 CIRVERD 241
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 229-377 8.09e-07

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 51.72  E-value: 8.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 229 HFVIIGGGPTGVEFAAEMHDFlvedlvklypaiqdFVKITIIQSGEHILNMFDQRIATFAEMKFQRDgIEVNTGFRVVKV 308
Cdd:PRK06292  171 SLAVIGGGVIGLELGQALSRL--------------GVKVTVFERGDRILPLEDPEVSKQAQKILSKE-FKIKLGAKVTSV 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 309 ---SDDLITMKSKSLGEVSV------------PY--GMAVWSAGIGT----RPVIMDFMQQigqtnrrvlatnewlrvhE 367
Cdd:PRK06292  236 eksGDEKVEELEKGGKTETIeadyvlvatgrrPNtdGLGLENTGIELdergRPVVDEHTQT------------------S 297

                         170
                  ....*....|
gi 1443087326 368 CDNIYAIGDC 377
Cdd:PRK06292  298 VPGIYAAGDV 307
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
 65-383 2.71e-05

nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 47.13  E-value: 2.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326  65 VVVLGTGWAGTSFLKDL---DCSKYEVKVISPRNYFAFTP-LLPSVTCGTVEARSIVEPIRKMLEKKRkdVAFYEAE-CF 139
Cdd:TIGR02374   1 LVLVGNGMAGHRCIEEVlklNRHMFEITIFGEEPHPNYNRiLLSSVLQGEADLDDITLNSKDWYEKHG--ITLYTGEtVI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 140 KIDASKKAVHCrsavgtnfdgNGDFMVDYDYLVVALGATVNTFNTPGV-MENCYFLKEVEDAQKIRrnvidcfekaslpN 218
Cdd:TIGR02374  79 QIDTDQKQVIT----------DAGRTLSYDKLILATGSYPFILPIPGAdKKGVYVFRTIEDLDAIM-------------A 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 219 ISEEEKRKilhfVIIGGGPTGVEFAAEMHDFLVE-DLVKLYPAIQDfvkitiiqsgehilNMFDQRIATFAEMKFQRDGI 297
Cdd:TIGR02374 136 MAQRFKKA----AVIGGGLLGLEAAVGLQNLGMDvSVIHHAPGLMA--------------KQLDQTAGRLLQRELEQKGL 197

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 298 EVNTGFRVVKVSDDLI--TMKSKSlGEvSVPYGMAVWSAGIgtRPVImDFMQQIGQTNRRVLATNEWLRVHEcDNIYAIG 375
Cdd:TIGR02374 198 TFLLEKDTVEIVGATKadRIRFKD-GS-SLEADLIVMAAGI--RPND-ELAVSAGIKVNRGIIVNDSMQTSD-PDIYAVG 271


                  ....*...
gi 1443087326 376 DCASITQR 383
Cdd:TIGR02374 272 ECAEHNGR 279
PRK13512 PRK13512
coenzyme A disulfide reductase; Provisional
 103-385 5.46e-05

coenzyme A disulfide reductase; Provisional


Pssm-ID: 184103 [Multi-domain]  Cd Length: 438  Bit Score: 45.93  E-value: 5.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 103 LPSVTCGTVEARSIVEPI--RKMLEKKRKDVAFYEaECFKIDASKKAVHCRsavgtNFDGNGDFMVDYDYLVVALGATVN 180
Cdd:PRK13512   45 LPYYIGEVVEDRKYALAYtpEKFYDRKQITVKTYH-EVIAINDERQTVTVL-----NRKTNEQFEESYDKLILSPGASAN 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 181 TFNTPGVMenCYFLKEVEDAQKirrnvIDCFekaslpnISEEEKRKILhfvIIGGGPTGVEFAAEMHdflvedlvklypa 260
Cdd:PRK13512  119 SLGFESDI--TFTLRNLEDTDA-----IDQF-------IKANQVDKAL---VVGAGYISLEVLENLY------------- 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 261 iQDFVKITIIQSGEHILNMFDQRI--ATFAEMkfQRDGIEVNTGFRVVKVSDDLITMKSkslGEVSvPYGMAVwsAGIGT 338
Cdd:PRK13512  169 -ERGLHPTLIHRSDKINKLMDADMnqPILDEL--DKREIPYRLNEEIDAINGNEVTFKS---GKVE-HYDMII--EGVGT 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1443087326 339 RPViMDFMQ--QIGQTNRRVLATNEWLRVHeCDNIYAIGDCASITQRKI 385
Cdd:PRK13512  240 HPN-SKFIEssNIKLDDKGFIPVNDKFETN-VPNIYAIGDIITSHYRHV 286
MerA TIGR02053
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ...
 222-377 8.51e-05

mercury(II) reductase; This model represents the mercuric reductase found in the mer operon for the detoxification of mercury compounds. MerA is a FAD-containing flavoprotein which reduces Hg(II) to Hg(0) utilizing NADPH. [Cellular processes, Detoxification]


Pssm-ID: 273944 [Multi-domain]  Cd Length: 463  Bit Score: 45.49  E-value: 8.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 222 EEKRKILHFVIIGGGPTGVEFAAEMHDFLVEdlvklypaiqdfvkITIIQSGEHILNMFDQRIATFAEMKFQRDGIEVNT 301
Cdd:TIGR02053 161 ALDRIPESLAVIGGGAIGVELAQAFARLGSE--------------VTILQRSDRLLPREEPEISAAVEEALAEEGIEVVT 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 302 GFRVVKVSDDlitmKSKSLGEVSVPYGMAVWSA-----GIGTRPVIMDF-MQQIG-QTNRR-VLATNEWLRVhECDNIYA 373
Cdd:TIGR02053 227 SAQVKAVSVR----GGGKIITVEKPGGQGEVEAdellvATGRRPNTDGLgLEKAGvKLDERgGILVDETLRT-SNPGIYA 301


                  ....
gi 1443087326 374 IGDC 377
Cdd:TIGR02053 302 AGDV 305
PRK06116 PRK06116
glutathione reductase; Validated
 231-377 1.41e-04

glutathione reductase; Validated


Pssm-ID: 235701 [Multi-domain]  Cd Length: 450  Bit Score: 44.38  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 231 VIIGGGPTGVEFAAEMHDFLVEdlvklypaiqdfvkITIIQSGEHILNMFDQRIATF--AEMkfQRDGIEVNTGF---RV 305
Cdd:PRK06116  171 AVVGAGYIAVEFAGVLNGLGSE--------------THLFVRGDAPLRGFDPDIRETlvEEM--EKKGIRLHTNAvpkAV 234

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1443087326 306 VKVSDDLITMKSKSLGEVSVpyGMAVWSagIGTRPVIMDF-MQQIG-QTN-RRVLATNEWLRVHEcDNIYAIGDC 377
Cdd:PRK06116  235 EKNADGSLTLTLEDGETLTV--DCLIWA--IGREPNTDGLgLENAGvKLNeKGYIIVDEYQNTNV-PGIYAVGDV 304
EF-hand_7 pfam13499
EF-hand domain pair;
386-463 4.20e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 38.77  E-value: 4.20e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1443087326 386 MDDISTVFKMADKDNSGTLTLKEINDVLEDICIrypqvelyMKSMHMLDIRDLIKDAigDSHKESmVVNIEEFKKALS 463
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEE--------GEPLSDEEVEELFKEF--DLDKDG-RISFEEFLELYS 67
PRK06327 PRK06327
dihydrolipoamide dehydrogenase; Validated
 229-379 7.21e-04

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235779 [Multi-domain]  Cd Length: 475  Bit Score: 42.22  E-value: 7.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 229 HFVIIGGGPTGVEFAAEMHDFLVEdlvklypaiqdfvkITIIQSGEHILNMFDQRIATFAEMKFQRDGIEVNTGfrvVKV 308
Cdd:PRK06327  185 KLAVIGAGVIGLELGSVWRRLGAE--------------VTILEALPAFLAAADEQVAKEAAKAFTKQGLDIHLG---VKI 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 309 SDdlITMKSKSlgeVSVPYGMAVWSA----------GIGTRP-----------VIMDfmqqigqtNRRVLATNEWLRVHe 367
Cdd:PRK06327  248 GE--IKTGGKG---VSVAYTDADGEAqtlevdklivSIGRVPntdglgleavgLKLD--------ERGFIPVDDHCRTN- 313

                         170
                  ....*....|..
gi 1443087326 368 CDNIYAIGDCAS 379
Cdd:PRK06327  314 VPNVYAIGDVVR 325
PRK07251 PRK07251
FAD-containing oxidoreductase;
169-376 7.97e-04

FAD-containing oxidoreductase;


Pssm-ID: 180907 [Multi-domain]  Cd Length: 438  Bit Score: 42.04  E-value: 7.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 169 DYLVVALGATVNTFNTPGVMENcyflKEVEDAQKIRrnvidcfekaslpNISEEEKRkilhFVIIGGGPTGVEFAAemhd 248
Cdd:PRK07251  120 ETIVINTGAVSNVLPIPGLADS----KHVYDSTGIQ-------------SLETLPER----LGIIGGGNIGLEFAG---- 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 249 flvedlvkLYPAIQDfvKITIIQSGEHILNMFDQRIATFAEMKFQRDGIEVNTGFRVVKVSDD----LITMKSKSLGEVS 324
Cdd:PRK07251  175 --------LYNKLGS--KVTVLDAASTILPREEPSVAALAKQYMEEDGITFLLNAHTTEVKNDgdqvLVVTEDETYRFDA 244

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1443087326 325 VPYGMavwsagiGTRPVIMDFMQQ---IGQTNRRVLATNEWLRVhECDNIYAIGD 376
Cdd:PRK07251  245 LLYAT-------GRKPNTEPLGLEntdIELTERGAIKVDDYCQT-SVPGVFAVGD 291
PRK09754 PRK09754
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
 161-244 1.13e-03

phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional


Pssm-ID: 170080 [Multi-domain]  Cd Length: 396  Bit Score: 41.45  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 161 NGDfMVDYDYLVVALGATVNTFNTPGVM-ENCYFLKEVEDAQKIRRNVidcfekaslpnisEEEKRkilhFVIIGGGPTG 239
Cdd:PRK09754   95 NGE-SWHWDQLFIATGAAARPLPLLDALgERCFTLRHAGDAARLREVL-------------QPERS----VVIVGAGTIG 156


                  ....*
gi 1443087326 240 VEFAA 244
Cdd:PRK09754  157 LELAA 161
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
 389-458 3.40e-03

EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta isozymes represent a class of metazoan PI-PLCs that are some of the most sensitive to calcium among all PLCs. Their activation is modulated by intracellular calcium ion concentration, phospholipids, polyamines, and other proteins, such as RhoAGAP. Like other PI-PLC isozymes, PI-PLC-delta isozymes contain a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C-terminal C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There are three PI-PLC-delta isozymes (1, 3 and 4). PI-PLC-delta1 is relatively well characterized. It is activated by high calcium levels generated by other PI-PLC family members, and therefore functions as a calcium amplifier within the cell. Different PI-PLC-delta isozymes have different tissue distribution and different subcellular locations. PI-PLC-delta1 is mostly a cytoplasmic protein, PI-PLC-delta3 is located in the membrane, and PI-PLC-delta4 is predominantly detected in the cell nucleus. PI-PLC-delta isozymes is evolutionarily conserved even in non-mammalian species, such as yeast, slime molds and plants.


Pssm-ID: 320032 [Multi-domain]  Cd Length: 140  Bit Score: 37.98  E-value: 3.40e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1443087326 389 ISTVFKMADKDNSGTLTLKEINDVLEDICIRypqvelyMKSMHmldIRDLIKDAIgdsHKESMVVNIEEF 458
Cdd:cd16202     2 LKDQFRKADKNGDGKLSFKECKKLLKKLNVK-------VDKDY---AKKLFQEAD---TSGEDVLDEEEF 58
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 392-463 5.95e-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: 35.60  E-value: 5.95e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1443087326 392 VFKMADKDNSGTLTLKEINDVLEDICIRYPQVELyMKSMHMLDirdliKDAIGdshkesmVVNIEEFKKALS 463
Cdd:cd00051     5 AFRLFDKDGDGTISADELKAALKSLGEGLSEEEI-DEMIREVD-----KDGDG-------KIDFEEFLELMA 63
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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