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Conserved domains on  [gi|51036596|ref|NP_079130|]
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pyridine nucleotide-disulfide oxidoreductase domain-containing protein 1 isoform 1 [Homo sapiens]

Protein Classification

NAD(P)/FAD-dependent oxidoreductase( domain architecture ID 1001407)

NAD(P)/FAD-dependent oxidoreductase catalyzes the transfer of electrons from one molecule, the electron donor or reductant, to another molecule, the electron acceptor or oxidant; similar to nitrite reductase large subunit NirB

CATH:  3.30.390.30
EC:  1.-.-.-
Gene Ontology:  GO:0016491
PubMed:  2445993
SCOP:  4000121

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NirB super family cl34210
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
24-497 3.71e-33

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


The actual alignment was detected with superfamily member COG1251:

Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 129.88  E-value: 3.71e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596  24 TCAEQLATHFPSEDILLVTA-----------SPVIKAVTNFKQIS----KILEEFDVEeqssTMLGKRfpnikviesgVK 88
Cdd:COG1251  15 RAAEELRKLDPDGEITVIGAephppynrpplSKVLAGETDEEDLLlrpaDFYEENGID----LRLGTR----------VT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596  89 QLKSEEHCIVTEDGNQHVYKKLCLCAGAKP-KLICEGN--PYVLGIRDTDSAQEFQKQLTKAKRIMIIGNGGIALELVYE 165
Cdd:COG1251  81 AIDRAARTVTLADGETLPYDKLVLATGSRPrVPPIPGAdlPGVFTLRTLDDADALRAALAPGKRVVVIGGGLIGLEAAAA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596 166 I--EGCEVIWAIKDKAIGNTFFDAGAAEFLTskliaekseakiahkrtryttegrkkearskskadnvgsalgpDWHEGL 243
Cdd:COG1251 161 LrkRGLEVTVVERAPRLLPRQLDEEAGALLQ-------------------------------------------RLLEAL 197

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596 244 NLKgtkefshkIHLETmcEVKKIyLQDEfrilkkksftfprdhkSVTAdtemwpvyVELTNEKIYGCDFIVSATGVTPNV 323
Cdd:COG1251 198 GVE--------VRLGT--GVTEI-EGDD----------------RVTG--------VRLADGEELPADLVVVAIGVRPNT 242

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596 324 EpFLHGNSFDLgeDGGLKVDDHMHTSLPDIYAAGDICttSWQlSPVWQQ--MRLWTQARQMGWYAAKCMAAAssgdsiDM 401
Cdd:COG1251 243 E-LARAAGLAV--DRGIVVDDYLRTSDPDIYAAGDCA--EHP-GPVYGRrvLELVAPAYEQARVAAANLAGG------PA 310

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596 402 DFSFELFAHVTKFFNYKVVLLGKYNaqglGSDHELMLRCTKGREYIKVVMQNGRMMGAVLIGETDLEETFENLILNQMNL 481
Cdd:COG1251 311 AYEGSVPSTKLKVFGVDVASAGDAE----GDEEVVVRGDPARGVYKKLVLRDGRLVGAVLVGDTSDAGALRQLIKNGRPL 386

                       490
                ....*....|....*.
gi 51036596 482 SsyGEDLLDPNIDIED 497
Cdd:COG1251 387 P--PRALLDAALPLKE 400
 
Name Accession Description Interval E-value
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
24-497 3.71e-33

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 129.88  E-value: 3.71e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596  24 TCAEQLATHFPSEDILLVTA-----------SPVIKAVTNFKQIS----KILEEFDVEeqssTMLGKRfpnikviesgVK 88
Cdd:COG1251  15 RAAEELRKLDPDGEITVIGAephppynrpplSKVLAGETDEEDLLlrpaDFYEENGID----LRLGTR----------VT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596  89 QLKSEEHCIVTEDGNQHVYKKLCLCAGAKP-KLICEGN--PYVLGIRDTDSAQEFQKQLTKAKRIMIIGNGGIALELVYE 165
Cdd:COG1251  81 AIDRAARTVTLADGETLPYDKLVLATGSRPrVPPIPGAdlPGVFTLRTLDDADALRAALAPGKRVVVIGGGLIGLEAAAA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596 166 I--EGCEVIWAIKDKAIGNTFFDAGAAEFLTskliaekseakiahkrtryttegrkkearskskadnvgsalgpDWHEGL 243
Cdd:COG1251 161 LrkRGLEVTVVERAPRLLPRQLDEEAGALLQ-------------------------------------------RLLEAL 197

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596 244 NLKgtkefshkIHLETmcEVKKIyLQDEfrilkkksftfprdhkSVTAdtemwpvyVELTNEKIYGCDFIVSATGVTPNV 323
Cdd:COG1251 198 GVE--------VRLGT--GVTEI-EGDD----------------RVTG--------VRLADGEELPADLVVVAIGVRPNT 242

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596 324 EpFLHGNSFDLgeDGGLKVDDHMHTSLPDIYAAGDICttSWQlSPVWQQ--MRLWTQARQMGWYAAKCMAAAssgdsiDM 401
Cdd:COG1251 243 E-LARAAGLAV--DRGIVVDDYLRTSDPDIYAAGDCA--EHP-GPVYGRrvLELVAPAYEQARVAAANLAGG------PA 310

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596 402 DFSFELFAHVTKFFNYKVVLLGKYNaqglGSDHELMLRCTKGREYIKVVMQNGRMMGAVLIGETDLEETFENLILNQMNL 481
Cdd:COG1251 311 AYEGSVPSTKLKVFGVDVASAGDAE----GDEEVVVRGDPARGVYKKLVLRDGRLVGAVLVGDTSDAGALRQLIKNGRPL 386

                       490
                ....*....|....*.
gi 51036596 482 SsyGEDLLDPNIDIED 497
Cdd:COG1251 387 P--PRALLDAALPLKE 400
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 24-373 1.34e-15

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: 77.36  E-value: 1.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596    24 TCAEQLATHfpSEDILLVTASPVI--------KAVTNFKQISKILEEF-DVEEQSSTMLGKRFPNIKV--------IESG 86
Cdd:pfam07992  14 AAALTLAQL--GGKVTLIEDEGTCpyggcvlsKALLGAAEAPEIASLWaDLYKRKEEVVKKLNNGIEVllgtevvsIDPG 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596    87 VKQLKSEEhcIVTEDGNQHVYKKLCLCAGAKPKLI-CEG--NPYVLGIRDTDSAQEFQKQLtKAKRIMIIGNGGIALELV 163
Cdd:pfam07992  92 AKKVVLEE--LVDGDGETITYDRLVIATGARPRLPpIPGveLNVGFLVRTLDSAEALRLKL-LPKRVVVVGGGYIGVELA 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596   164 YEIE--GCEVIWaIKDKAIGNTFFDAGAAEFLTSKLiaekseakiahkrtryttegrkkearsksKADNVgsalgpdwhe 241
Cdd:pfam07992 169 AALAklGKEVTL-IEALDRLLRAFDEEISAALEKAL-----------------------------EKNGV---------- 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596   242 glnlkgtkefshKIHLETMceVKKIYlqdefrilkkksftfpRDHKSVTadtemwpvyVELTNEKIYGCDFIVSATGVTP 321
Cdd:pfam07992 209 ------------EVRLGTS--VKEII----------------GDGDGVE---------VILKDGTEIDADLVVVAIGRRP 249

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 51036596   322 NVEPFLHGNsFDLGEDGGLKVDDHMHTSLPDIYAAGDICTTSWQLSPVWQQM 373
Cdd:pfam07992 250 NTELLEAAG-LELDERGGIVVDEYLRTSVPGIYAAGDCRVGGPELAQNAVAQ 300
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 298-366 2.33e-08

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 56.20  E-value: 2.33e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 51036596  298 VYVELTNEKIYGCDFIVSATGVTPNVEpFLHGNSFDLGEDGGLKVDDHMHTSLPDIYAAGDiCTTSWQL 366
Cdd:PRK09564 223 VEGVVTDKGEYEADVVIVATGVKPNTE-FLEDTGLKTLKNGAIIVDEYGETSIENIYAAGD-CATIYNI 289
MerA TIGR02053
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ...
 311-369 2.79e-08

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: 55.89  E-value: 2.79e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596   311 DFIVSATGVTPNVEPF-LHGNSFDLGEDGGLKVDDHMHTSLPDIYAAGDiCTTSWQLSPV 369
Cdd:TIGR02053 256 DELLVATGRRPNTDGLgLEKAGVKLDERGGILVDETLRTSNPGIYAAGD-VTGGLQLEYV 314
PBP1_ABC_ligand_binding-like cd19980
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
 107-204 3.57e-03

type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids, peptides, or inorganic ions; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally.


Pssm-ID: 380635 [Multi-domain]  Cd Length: 334  Bit Score: 39.51  E-value: 3.57e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596 107 YKKLCLCAGAK-PKLICEGNPYVLGIRDTDS--AQEFQKQL---TKAKRIMII------GNGGIALelvYEiegcEVIWA 174
Cdd:cd19980  90 AKVPLVVEISSaPKITEGGNPYVFRLNPTNSmlAKAFAKYLadkGKPKKVAFLaenddyGRGAAEA---FK----KALKA 162

                        90       100       110
                ....*....|....*....|....*....|..
gi 51036596 175 IKDKAIGNTFFDAGAAEFLT--SKLIAEKSEA 204
Cdd:cd19980 163 KGVKVVATEYFDQGQTDFTTqlTKLKAANPDA 194
 
Name Accession Description Interval E-value
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
24-497 3.71e-33

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 129.88  E-value: 3.71e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596  24 TCAEQLATHFPSEDILLVTA-----------SPVIKAVTNFKQIS----KILEEFDVEeqssTMLGKRfpnikviesgVK 88
Cdd:COG1251  15 RAAEELRKLDPDGEITVIGAephppynrpplSKVLAGETDEEDLLlrpaDFYEENGID----LRLGTR----------VT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596  89 QLKSEEHCIVTEDGNQHVYKKLCLCAGAKP-KLICEGN--PYVLGIRDTDSAQEFQKQLTKAKRIMIIGNGGIALELVYE 165
Cdd:COG1251  81 AIDRAARTVTLADGETLPYDKLVLATGSRPrVPPIPGAdlPGVFTLRTLDDADALRAALAPGKRVVVIGGGLIGLEAAAA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596 166 I--EGCEVIWAIKDKAIGNTFFDAGAAEFLTskliaekseakiahkrtryttegrkkearskskadnvgsalgpDWHEGL 243
Cdd:COG1251 161 LrkRGLEVTVVERAPRLLPRQLDEEAGALLQ-------------------------------------------RLLEAL 197

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596 244 NLKgtkefshkIHLETmcEVKKIyLQDEfrilkkksftfprdhkSVTAdtemwpvyVELTNEKIYGCDFIVSATGVTPNV 323
Cdd:COG1251 198 GVE--------VRLGT--GVTEI-EGDD----------------RVTG--------VRLADGEELPADLVVVAIGVRPNT 242

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596 324 EpFLHGNSFDLgeDGGLKVDDHMHTSLPDIYAAGDICttSWQlSPVWQQ--MRLWTQARQMGWYAAKCMAAAssgdsiDM 401
Cdd:COG1251 243 E-LARAAGLAV--DRGIVVDDYLRTSDPDIYAAGDCA--EHP-GPVYGRrvLELVAPAYEQARVAAANLAGG------PA 310

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596 402 DFSFELFAHVTKFFNYKVVLLGKYNaqglGSDHELMLRCTKGREYIKVVMQNGRMMGAVLIGETDLEETFENLILNQMNL 481
Cdd:COG1251 311 AYEGSVPSTKLKVFGVDVASAGDAE----GDEEVVVRGDPARGVYKKLVLRDGRLVGAVLVGDTSDAGALRQLIKNGRPL 386

                       490
                ....*....|....*.
gi 51036596 482 SsyGEDLLDPNIDIED 497
Cdd:COG1251 387 P--PRALLDAALPLKE 400
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 78-391 1.45e-20

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: 92.57  E-value: 1.45e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596  78 PNIKVI-ESGVKQLKSEEHCIVTEDGNQHVYKKLCLCAGAKPKLI-CEG--NPYVLGIRDTDSAQEFQKQLT--KAKRIM 151
Cdd:COG0446  49 KGIDVRtGTEVTAIDPEAKTVTLRDGETLSYDKLVLATGARPRPPpIPGldLPGVFTLRTLDDADALREALKefKGKRAV 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596 152 IIGNGGIALELVYE----------IEGCEVIWAIKDKAIgntffdagaaefltskliaekseAKIAHKRTRyttegrkke 221
Cdd:COG0446 129 VIGGGPIGLELAEAlrkrglkvtlVERAPRLLGVLDPEM-----------------------AALLEEELR--------- 176

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596 222 arskskadnvgsalgpdwheglnlkgtkefSHKIHLETMCEVKKIylqdefrilkkksftfpRDHKSVTadtemwpvyVE 301
Cdd:COG0446 177 ------------------------------EHGVELRLGETVVAI-----------------DGDDKVA---------VT 200

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596 302 LTNEKIYGCDFIVSATGVTPNVEpFLHGNSFDLGEDGGLKVDDHMHTSLPDIYAAGDICTTSWQLSPVWQQMRLWTQARQ 381
Cdd:COG0446 201 LTDGEEIPADLVVVAPGVRPNTE-LAKDAGLALGERGWIKVDETLQTSDPDVYAAGDCAEVPHPVTGKTVYIPLASAANK 279

                       330
                ....*....|
gi 51036596 382 MGWYAAKCMA 391
Cdd:COG0446 280 QGRVAAENIL 289
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 24-373 1.34e-15

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: 77.36  E-value: 1.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596    24 TCAEQLATHfpSEDILLVTASPVI--------KAVTNFKQISKILEEF-DVEEQSSTMLGKRFPNIKV--------IESG 86
Cdd:pfam07992  14 AAALTLAQL--GGKVTLIEDEGTCpyggcvlsKALLGAAEAPEIASLWaDLYKRKEEVVKKLNNGIEVllgtevvsIDPG 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596    87 VKQLKSEEhcIVTEDGNQHVYKKLCLCAGAKPKLI-CEG--NPYVLGIRDTDSAQEFQKQLtKAKRIMIIGNGGIALELV 163
Cdd:pfam07992  92 AKKVVLEE--LVDGDGETITYDRLVIATGARPRLPpIPGveLNVGFLVRTLDSAEALRLKL-LPKRVVVVGGGYIGVELA 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596   164 YEIE--GCEVIWaIKDKAIGNTFFDAGAAEFLTSKLiaekseakiahkrtryttegrkkearsksKADNVgsalgpdwhe 241
Cdd:pfam07992 169 AALAklGKEVTL-IEALDRLLRAFDEEISAALEKAL-----------------------------EKNGV---------- 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596   242 glnlkgtkefshKIHLETMceVKKIYlqdefrilkkksftfpRDHKSVTadtemwpvyVELTNEKIYGCDFIVSATGVTP 321
Cdd:pfam07992 209 ------------EVRLGTS--VKEII----------------GDGDGVE---------VILKDGTEIDADLVVVAIGRRP 249

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 51036596   322 NVEPFLHGNsFDLGEDGGLKVDDHMHTSLPDIYAAGDICTTSWQLSPVWQQM 373
Cdd:pfam07992 250 NTELLEAAG-LELDERGGIVVDEYLRTSVPGIYAAGDCRVGGPELAQNAVAQ 300
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
76-396 4.72e-12

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 67.47  E-value: 4.72e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596  76 RFPNIKVIESGVKQLKSEEHCIVTEDGNQHVYKKLCLCAGAKPKLicEGNP----YVLGIRDTDSAQEFQKQL------- 144
Cdd:COG1252  67 RRAGVRFIQGEVTGIDPEARTVTLADGRTLSYDYLVIATGSVTNF--FGIPglaeHALPLKTLEDALALRERLlaafera 144

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596 145 --TKAKRIMIIGNGGIALELVYEIegceviwaikdkaigntffdagaAEFLTSKLiaekSEAKIAHKRTRYT-TEGrkke 221
Cdd:COG1252 145 erRRLLTIVVVGGGPTGVELAGEL-----------------------AELLRKLL----RYPGIDPDKVRITlVEA---- 193

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596 222 arskskADNVGSALGPDwhegLNLKGTKEFSH---KIHLETMCevkkiylqdefrilkkksftfprdhKSVTADTemwpv 298
Cdd:COG1252 194 ------GPRILPGLGEK----LSEAAEKELEKrgvEVHTGTRV-------------------------TEVDADG----- 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596 299 yVELTNEKIYGCDFIVSATGVTPNvePFLHGNSFDLGEDGGLKVDDHM-HTSLPDIYAAGDICTTSWQlSPVWQ----QM 373
Cdd:COG1252 234 -VTLEDGEEIPADTVIWAAGVKAP--PLLADLGLPTDRRGRVLVDPTLqVPGHPNVFAIGDCAAVPDP-DGKPVpktaQA 309

                       330       340
                ....*....|....*....|...
gi 51036596 374 rlwtqARQMGWYAAKCMAAASSG 396
Cdd:COG1252 310 -----AVQQAKVLAKNIAALLRG 327
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 273-464 3.63e-10

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: 62.03  E-value: 3.63e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596 273 RILKKKSFTFPRDHK--SVTADTEmwPVYVELTN---EKIYGCDFIVSATGVTPNVEpflhgnsfDLG---------EDG 338
Cdd:COG1249 217 KALEKEGIDILTGAKvtSVEKTGD--GVTVTLEDgggEEAVEADKVLVATGRRPNTD--------GLGleaagveldERG 286

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596 339 GLKVDDHMHTSLPDIYAAGDiCTTSWQLSPVwqqmrlwtqARQMGWYAAKcMAAASSGDSIDMD------FSF-ELfAHV 411
Cdd:COG1249 287 GIKVDEYLRTSVPGIYAIGD-VTGGPQLAHV---------ASAEGRVAAE-NILGKKPRPVDYRaipsvvFTDpEI-ASV 354

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51036596 412 --------TKFFNYKVvllGKYNAQGLGsdHELMLRCTKGreYIKVV--MQNGRMMGAVLIGE 464
Cdd:COG1249 355 glteeearEAGIDVKV---GKFPFAANG--RALALGETEG--FVKLIadAETGRILGAHIVGP 410
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
300-366 1.80e-09

Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 58.98  E-value: 1.80e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 51036596 300 VELTN-----EKIYGCDFIVSATGVTPNVEPFlHGNSFDLGEDGGLKVDDHMHTSLPDIYAAGDICTTSWQL 366
Cdd:COG0492 212 VTLKNvktgeEKELEVDGVFVAIGLKPNTELL-KGLGLELDEDGYIVVDEDMETSVPGVFAAGDVRDYKYRQ 282
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 298-366 2.33e-08

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 56.20  E-value: 2.33e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 51036596  298 VYVELTNEKIYGCDFIVSATGVTPNVEpFLHGNSFDLGEDGGLKVDDHMHTSLPDIYAAGDiCTTSWQL 366
Cdd:PRK09564 223 VEGVVTDKGEYEADVVIVATGVKPNTE-FLEDTGLKTLKNGAIIVDEYGETSIENIYAAGD-CATIYNI 289
MerA TIGR02053
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ...
 311-369 2.79e-08

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: 55.89  E-value: 2.79e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596   311 DFIVSATGVTPNVEPF-LHGNSFDLGEDGGLKVDDHMHTSLPDIYAAGDiCTTSWQLSPV 369
Cdd:TIGR02053 256 DELLVATGRRPNTDGLgLEKAGVKLDERGGILVDETLRTSNPGIYAAGD-VTGGLQLEYV 314
PRK09754 PRK09754
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
 87-390 6.99e-08

phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional


Pssm-ID: 170080 [Multi-domain]  Cd Length: 396  Bit Score: 54.55  E-value: 6.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596   87 VKQLKSEEHCIVTEDGNQHVYKKLCLCAGAKPK---LICEGNPYVLGIRDTDSAQEFQKQLTKAKRIMIIGNGGIALELV 163
Cdd:PRK09754  81 IKTLGRDTRELVLTNGESWHWDQLFIATGAAARplpLLDALGERCFTLRHAGDAARLREVLQPERSVVIVGAGTIGLELA 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596  164 yeiegceviwaikdkaigntffdAGAAEFLTSKLIAEkseakiahkrtryttegrkkearsksKADNVGSALGPDWHEGL 243
Cdd:PRK09754 161 -----------------------ASATQRRCKVTVIE--------------------------LAATVMGRNAPPPVQRY 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596  244 NLKGTKEFSHKIHLETMCEvkkiylqdefrilkkksftfprdhkSVTADTEMwpVYVELTNEKIYGcDFIVSATGVTPNV 323
Cdd:PRK09754 192 LLQRHQQAGVRILLNNAIE-------------------------HVVDGEKV--ELTLQSGETLQA-DVVIYGIGISAND 243

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51036596  324 EPFLHGNsfdLGEDGGLKVDDHMHTSLPDIYAAGDICTTSWQLSPVwQQMRLWTQARQMGWYAAKCM 390
Cdd:PRK09754 244 QLAREAN---LDTANGIVIDEACRTCDPAIFAGGDVAITRLDNGAL-HRCESWENANNQAQIAAAAM 306
PRK06370 PRK06370
FAD-containing oxidoreductase;
310-360 6.32e-07

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 51.74  E-value: 6.32e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596  310 CDFIVSATGVTPNVEpflhgnsfDLG---------EDGGLKVDDHMHTSLPDIYAAGDIC 360
Cdd:PRK06370 260 GSHILVAVGRVPNTD--------DLGleaagvetdARGYIKVDDQLRTTNPGIYAAGDCN 311
PRK07251 PRK07251
FAD-containing oxidoreductase;
303-359 1.17e-06

FAD-containing oxidoreductase;


Pssm-ID: 180907 [Multi-domain]  Cd Length: 438  Bit Score: 50.90  E-value: 1.17e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 51036596  303 TNEKIYGCDFIVSATGVTPNVEPF-LHGNSFDLGEDGGLKVDDHMHTSLPDIYAAGDI 359
Cdd:PRK07251 235 TEDETYRFDALLYATGRKPNTEPLgLENTDIELTERGAIKVDDYCQTSVPGVFAVGDV 292
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 297-359 1.40e-06

NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 440259 [Multi-domain]  Cd Length: 434  Bit Score: 50.52  E-value: 1.40e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51036596 297 PVYVELTnEKIYGCDFIVSATGVTPNVEPFLHGNSFDLGEDGGLKVD-DHMHTSLPDIYAAGDI 359
Cdd:COG0493 348 PVPIEGS-EFTLPADLVILAIGQTPDPSGLEEELGLELDKRGTIVVDeETYQTSLPGVFAGGDA 410
PRK13512 PRK13512
coenzyme A disulfide reductase; Provisional
 311-423 1.81e-06

coenzyme A disulfide reductase; Provisional


Pssm-ID: 184103 [Multi-domain]  Cd Length: 438  Bit Score: 50.17  E-value: 1.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596  311 DFIVSATGVTPNVEpFLHGNSFDLGEDGGLKVDDHMHTSLPDIYAAGDICTTSWQLSPVWQQMRL-WTQARqmgwyAAKC 389
Cdd:PRK13512 231 DMIIEGVGTHPNSK-FIESSNIKLDDKGFIPVNDKFETNVPNIYAIGDIITSHYRHVDLPASVPLaWGAHR-----AASI 304

                         90       100       110
                 ....*....|....*....|....*....|....
gi 51036596  390 MAAASSGDSiDMDFSFELFAHVTKFFNYKVVLLG 423
Cdd:PRK13512 305 VAEQIAGND-TIEFKGFLGNNIVKFFDYTFASVG 337
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 305-361 1.90e-06

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 50.18  E-value: 1.90e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 51036596  305 EKIYGCDFIVSATGVTPNVEPFLHGNSFDLGEDGGLKVDD-HMHTSLPDIYAAGDICT 361
Cdd:PRK11749 371 EFTLPADLVIKAIGQTPNPLILSTTPGLELNRWGTIIADDeTGRTSLPGVFAGGDIVT 428
PRK13748 PRK13748
putative mercuric reductase; Provisional
 303-366 7.91e-06

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 48.22  E-value: 7.91e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 51036596  303 TNEKIYGCDFIVSATGVTPNVEPF-LHGNSFDLGEDGGLKVDDHMHTSLPDIYAAGDiCTTSWQL 366
Cdd:PRK13748 347 TGHGELRADKLLVATGRAPNTRSLaLDAAGVTVNAQGAIVIDQGMRTSVPHIYAAGD-CTDQPQF 410
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
87-358 9.17e-06

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 47.99  E-value: 9.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596   87 VKQLKSEEHCIVTeDGNQHVYKKLCLCAGAK---PKLicEGNPYVLGIrdtDSAQEF---QKQLTKAKRIMIIGNGGIAL 160
Cdd:PRK04965  81 VTDIDAEAQVVKS-QGNQWQYDKLVLATGASafvPPI--PGRELMLTL---NSQQEYraaETQLRDAQRVLVVGGGLIGT 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596  161 ELVYEIegceviwAIKDKAIgnTFFDAgaAEFLTSKLIAEKSEAKIAHKRTRyttegrkkearskskadnvgsalgpdwh 240
Cdd:PRK04965 155 ELAMDL-------CRAGKAV--TLVDN--AASLLASLMPPEVSSRLQHRLTE---------------------------- 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596  241 eglnlKGtkefshkIHLETMCEVKKI-YLQDEFRilkkksftfprdhksvtadtemwpvyVELTNEKIYGCDFIVSATGV 319
Cdd:PRK04965 196 -----MG-------VHLLLKSQLQGLeKTDSGIR--------------------------ATLDSGRSIEVDAVIAAAGL 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 51036596  320 TPNVEpflhgnsfdLGEDGGLK------VDDHMHTSLPDIYAAGD 358
Cdd:PRK04965 238 RPNTA---------LARRAGLAvnrgivVDSYLQTSAPDIYALGD 273
PTZ00058 PTZ00058
glutathione reductase; Provisional
 100-360 1.81e-05

glutathione reductase; Provisional


Pssm-ID: 185420 [Multi-domain]  Cd Length: 561  Bit Score: 47.30  E-value: 1.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596  100 EDGNQHVYKKLCLCAGAKPKLicegnPYVLGIRDTDSAQEFqKQLTKAKRIMIIGNGGIALELVyeiegceviwaikdka 179
Cdd:PTZ00058 196 DDGQVIEGKNILIAVGNKPIF-----PDVKGKEFTISSDDF-FKIKEAKRIGIAGSGYIAVELI---------------- 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596  180 igNTFFDAGAAEFLTSKliaekseakiAHKRTRYTTEGRKKEARSKSKADNvgsalgpdwheglnlkgtkefshkIHLET 259
Cdd:PTZ00058 254 --NVVNRLGAESYIFAR----------GNRLLRKFDETIINELENDMKKNN------------------------INIIT 297

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596  260 MCEVKKIYLQDEFRILkkksftfprdhksvtadtemwpVYVELTNEKIYGcDFIVSATGVTPNVEPFLHGNSFDLGEDGG 339
Cdd:PTZ00058 298 HANVEEIEKVKEKNLT----------------------IYLSDGRKYEHF-DYVIYCVGRSPNTEDLNLKALNIKTPKGY 354

                        250       260
                 ....*....|....*....|.
gi 51036596  340 LKVDDHMHTSLPDIYAAGDIC 360
Cdd:PTZ00058 355 IKVDDNQRTSVKHIYAVGDCC 375
PRK06116 PRK06116
glutathione reductase; Validated
 300-369 2.38e-05

glutathione reductase; Validated


Pssm-ID: 235701 [Multi-domain]  Cd Length: 450  Bit Score: 46.69  E-value: 2.38e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51036596  300 VELTNEKIYGCDFIVSATGVTPNVEPF-LHGNSFDLGEDGGLKVDDHMHTSLPDIYAAGDiCTTSWQLSPV 369
Cdd:PRK06116 244 LTLEDGETLTVDCLIWAIGREPNTDGLgLENAGVKLNEKGYIIVDEYQNTNVPGIYAVGD-VTGRVELTPV 313
PRK14989 PRK14989
nitrite reductase subunit NirD; Provisional
 311-491 2.61e-05

nitrite reductase subunit NirD; Provisional


Pssm-ID: 184951 [Multi-domain]  Cd Length: 847  Bit Score: 47.04  E-value: 2.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596  311 DFIVSATGVTPNvEPFLHGNSFDLGEDGGLKVDDHMHTSLPDIYAAGDiCtTSWqlspvwqqmrlwtQARQMGWYAAKCM 390
Cdd:PRK14989 235 DFIVFSTGIRPQ-DKLATQCGLAVAPRGGIVINDSCQTSDPDIYAIGE-C-ASW-------------NNRVFGLVAPGYK 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596  391 AAASSGDsidmdfsfELFAHVTKF----FNYKVVLLGkYNAQGLGSDHElmlRCTKGREY------------IKVVMQNG 454
Cdd:PRK14989 299 MAQVAVD--------HLLGSENAFegadLSAKLKLLG-VDVGGIGDAHG---RTPGARSYvyldeskeiykrLIVSEDNK 366

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 51036596  455 RMMGAVLIGETDLEETFENLILNQMNLSSYGEDLLDP 491
Cdd:PRK14989 367 TLLGAVLVGDTSDYGNLLQLVLNAIELPENPDSLILP 403
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 311-359 3.19e-05

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 46.29  E-value: 3.19e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 51036596  311 DFIVSATGVTPNVEpflhgnsfDLG-EDGGLK-------VDDHMHTSLPDIYAAGDI 359
Cdd:PRK06416 262 DYVLVAVGRRPNTE--------NLGlEELGVKtdrgfieVDEQLRTNVPNIYAIGDI 310
PRK06327 PRK06327
dihydrolipoamide dehydrogenase; Validated
 304-366 1.10e-04

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235779 [Multi-domain]  Cd Length: 475  Bit Score: 44.53  E-value: 1.10e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51036596  304 NEKIYGCDFIVSATGVTPNVEPF-LHGNSFDLGEDGGLKVDDHMHTSLPDIYAAGDIcTTSWQL 366
Cdd:PRK06327 267 EAQTLEVDKLIVSIGRVPNTDGLgLEAVGLKLDERGFIPVDDHCRTNVPNVYAIGDV-VRGPML 329
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 268-359 1.31e-04

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 44.40  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596  268 LQDEFRILKKKSFTFPRDHK--SVTADTEMWPVYVELTNEKIY-GCDFIVSATGVTPNVEPF-LHGNSFDLGEDGGLKVD 343
Cdd:PRK06292 212 VSKQAQKILSKEFKIKLGAKvtSVEKSGDEKVEELEKGGKTETiEADYVLVATGRRPNTDGLgLENTGIELDERGRPVVD 291

                         90
                 ....*....|....*.
gi 51036596  344 DHMHTSLPDIYAAGDI 359
Cdd:PRK06292 292 EHTQTSVPGIYAAGDV 307
PRK07846 PRK07846
mycothione reductase; Reviewed
 298-369 1.33e-04

mycothione reductase; Reviewed


Pssm-ID: 181142 [Multi-domain]  Cd Length: 451  Bit Score: 44.17  E-value: 1.33e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51036596  298 VYVELTNEKIYGCDFIVSATGVTPNVEPF-LHGNSFDLGEDGGLKVDDHMHTSLPDIYAAGDICtTSWQLSPV 369
Cdd:PRK07846 239 VTLRLDDGSTVEADVLLVATGRVPNGDLLdAAAAGVDVDEDGRVVVDEYQRTSAEGVFALGDVS-SPYQLKHV 310
PLN02507 PLN02507
glutathione reductase
 311-369 6.31e-04

glutathione reductase


Pssm-ID: 215281 [Multi-domain]  Cd Length: 499  Bit Score: 42.11  E-value: 6.31e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596  311 DFIVSATGVTPNVEPF-LHGNSFDLGEDGGLKVDDHMHTSLPDIYAAGDIcTTSWQLSPV 369
Cdd:PLN02507 290 DVVLFATGRAPNTKRLnLEAVGVELDKAGAVKVDEYSRTNIPSIWAIGDV-TNRINLTPV 348
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
 284-406 7.89e-04

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 41.68  E-value: 7.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596  284 RDHKSVTADTEMwpvYVELTNEKIYGCDFIVSATGVTPNvePFLHGNSFDLGEDGGLKVDDHMHTS-LPDIYAAGDICTT 362
Cdd:PTZ00318 246 RTKTAVKEVLDK---EVVLKDGEVIPTGLVVWSTGVGPG--PLTKQLKVDKTSRGRISVDDHLRVKpIPNVFALGDCAAN 320

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 51036596  363 SWQLSPVWQQMrlwtqARQMGWYAAKCMAAASSGDSIDMDFSFE 406
Cdd:PTZ00318 321 EERPLPTLAQV-----ASQQGVYLAKEFNNELKGKPMSKPFVYR 359
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
 297-361 8.10e-04

bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 42.04  E-value: 8.10e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51036596  297 PVYVELTNEKIyGCDFIVSATGVTPNvePFLhGNSF---DLGEDGGLKVDDHMHTSLPDIYAAGDICT 361
Cdd:PRK12778 663 PVAIPGSTFTV-DVDLVIVSVGVSPN--PLV-PSSIpglELNRKGTIVVDEEMQSSIPGIYAGGDIVR 726
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
298-359 1.54e-03

Si-specific NAD(P)(+) transhydrogenase;


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 40.91  E-value: 1.54e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51036596  298 VYVELTNEKIYGCDFIVSATGVTPNVEPfLHGNSFDLGED--GGLKVDDHMHTSLPDIYAAGDI 359
Cdd:PRK05249 249 VIVHLKSGKKIKADCLLYANGRTGNTDG-LNLENAGLEADsrGQLKVNENYQTAVPHIYAVGDV 311
PRK15317 PRK15317
alkyl hydroperoxide reductase subunit F; Provisional
 318-363 1.66e-03

alkyl hydroperoxide reductase subunit F; Provisional


Pssm-ID: 237942 [Multi-domain]  Cd Length: 517  Bit Score: 40.91  E-value: 1.66e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 51036596  318 GVTPNVEpFLHGnSFDLGEDGGLKVDDHMHTSLPDIYAAGDiCTTS 363
Cdd:PRK15317 446 GLVPNTE-WLKG-TVELNRRGEIIVDARGATSVPGVFAAGD-CTTV 488
PBP1_ABC_ligand_binding-like cd19980
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
 107-204 3.57e-03

type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids, peptides, or inorganic ions; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally.


Pssm-ID: 380635 [Multi-domain]  Cd Length: 334  Bit Score: 39.51  E-value: 3.57e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51036596 107 YKKLCLCAGAK-PKLICEGNPYVLGIRDTDS--AQEFQKQL---TKAKRIMII------GNGGIALelvYEiegcEVIWA 174
Cdd:cd19980  90 AKVPLVVEISSaPKITEGGNPYVFRLNPTNSmlAKAFAKYLadkGKPKKVAFLaenddyGRGAAEA---FK----KALKA 162

                        90       100       110
                ....*....|....*....|....*....|..
gi 51036596 175 IKDKAIGNTFFDAGAAEFLT--SKLIAEKSEA 204
Cdd:cd19980 163 KGVKVVATEYFDQGQTDFTTqlTKLKAANPDA 194
 
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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