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Conserved domains on  [gi|1186518001|ref|NP_001337841|]
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pyridine nucleotide-disulfide oxidoreductase domain-containing protein 1 isoform 2 [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];
16-426 9.52e-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: 127.57  E-value: 9.52e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001  16 VKQLKSEEHCIVTEDGNQHVYKKLCLCAGAKP-KLICEGN--PYVLGIRDTDSAQEFQKQLTKAKRIMIIGNGGIALELV 92
Cdd:COG1251    79 VTAIDRAARTVTLADGETLPYDKLVLATGSRPrVPPIPGAdlPGVFTLRTLDDADALRAALAPGKRVVVIGGGLIGLEAA 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001  93 YEI--EGCEVIWAIKDKAIGNTFFDAGAAEFLTskliaekseakiahkrtryttegrkkearskskadnvgsalgpDWHE 170
Cdd:COG1251   159 AALrkRGLEVTVVERAPRLLPRQLDEEAGALLQ-------------------------------------------RLLE 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001 171 GLNLKgtkefshkIHLETmcEVKKIyLQDEfrilkkksftfprdhkSVTAdtemwpvyVELTNEKIYGCDFIVSATGVTP 250
Cdd:COG1251   196 ALGVE--------VRLGT--GVTEI-EGDD----------------RVTG--------VRLADGEELPADLVVVAIGVRP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001 251 NVEpFLHGNSFDLgeDGGLKVDDHMHTSLPDIYAAGDICttSWQlSPVWQQ--MRLWTQARQMGWYAAKCMAAAssgdsi 328
Cdd:COG1251   241 NTE-LARAAGLAV--DRGIVVDDYLRTSDPDIYAAGDCA--EHP-GPVYGRrvLELVAPAYEQARVAAANLAGG------ 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001 329 DMDFSFELFAHVTKFFNYKVVLLGKYNaqglGSDHELMLRCTKGREYIKVVMQNGRMMGAVLIGETDLEETFENLILNQM 408
Cdd:COG1251   309 PAAYEGSVPSTKLKVFGVDVASAGDAE----GDEEVVVRGDPARGVYKKLVLRDGRLVGAVLVGDTSDAGALRQLIKNGR 384

                         410
                  ....*....|....*...
gi 1186518001 409 NLSsyGEDLLDPNIDIED 426
Cdd:COG1251   385 PLP--PRALLDAALPLKE 400
 
Name Accession Description Interval E-value
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
16-426 9.52e-33

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 127.57  E-value: 9.52e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001  16 VKQLKSEEHCIVTEDGNQHVYKKLCLCAGAKP-KLICEGN--PYVLGIRDTDSAQEFQKQLTKAKRIMIIGNGGIALELV 92
Cdd:COG1251    79 VTAIDRAARTVTLADGETLPYDKLVLATGSRPrVPPIPGAdlPGVFTLRTLDDADALRAALAPGKRVVVIGGGLIGLEAA 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001  93 YEI--EGCEVIWAIKDKAIGNTFFDAGAAEFLTskliaekseakiahkrtryttegrkkearskskadnvgsalgpDWHE 170
Cdd:COG1251   159 AALrkRGLEVTVVERAPRLLPRQLDEEAGALLQ-------------------------------------------RLLE 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001 171 GLNLKgtkefshkIHLETmcEVKKIyLQDEfrilkkksftfprdhkSVTAdtemwpvyVELTNEKIYGCDFIVSATGVTP 250
Cdd:COG1251   196 ALGVE--------VRLGT--GVTEI-EGDD----------------RVTG--------VRLADGEELPADLVVVAIGVRP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001 251 NVEpFLHGNSFDLgeDGGLKVDDHMHTSLPDIYAAGDICttSWQlSPVWQQ--MRLWTQARQMGWYAAKCMAAAssgdsi 328
Cdd:COG1251   241 NTE-LARAAGLAV--DRGIVVDDYLRTSDPDIYAAGDCA--EHP-GPVYGRrvLELVAPAYEQARVAAANLAGG------ 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001 329 DMDFSFELFAHVTKFFNYKVVLLGKYNaqglGSDHELMLRCTKGREYIKVVMQNGRMMGAVLIGETDLEETFENLILNQM 408
Cdd:COG1251   309 PAAYEGSVPSTKLKVFGVDVASAGDAE----GDEEVVVRGDPARGVYKKLVLRDGRLVGAVLVGDTSDAGALRQLIKNGR 384

                         410
                  ....*....|....*...
gi 1186518001 409 NLSsyGEDLLDPNIDIED 426
Cdd:COG1251   385 PLP--PRALLDAALPLKE 400
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 12-302 2.88e-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: 75.82  E-value: 2.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001  12 IESGVKQLKSEEhcIVTEDGNQHVYKKLCLCAGAKPKLI-CEG--NPYVLGIRDTDSAQEFQKQLtKAKRIMIIGNGGIA 88
Cdd:pfam07992  88 IDPGAKKVVLEE--LVDGDGETITYDRLVIATGARPRLPpIPGveLNVGFLVRTLDSAEALRLKL-LPKRVVVVGGGYIG 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001  89 LELVYEIE--GCEVIWaIKDKAIGNTFFDAGAAEFLTSKLiaekseakiahkrtryttegrkkearsksKADNVgsalgp 166
Cdd:pfam07992 165 VELAAALAklGKEVTL-IEALDRLLRAFDEEISAALEKAL-----------------------------EKNGV------ 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001 167 dwheglnlkgtkefshKIHLETMceVKKIYlqdefrilkkksftfpRDHKSVTadtemwpvyVELTNEKIYGCDFIVSAT 246
Cdd:pfam07992 209 ----------------EVRLGTS--VKEII----------------GDGDGVE---------VILKDGTEIDADLVVVAI 245

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1186518001 247 GVTPNVEPFLHGNsFDLGEDGGLKVDDHMHTSLPDIYAAGDICTTSWQLSPVWQQM 302
Cdd:pfam07992 246 GRRPNTELLEAAG-LELDERGGIVVDEYLRTSVPGIYAAGDCRVGGPELAQNAVAQ 300
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 227-295 1.88e-08

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 56.20  E-value: 1.88e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1186518001 227 VYVELTNEKIYGCDFIVSATGVTPNVEpFLHGNSFDLGEDGGLKVDDHMHTSLPDIYAAGDiCTTSWQL 295
Cdd:PRK09564  223 VEGVVTDKGEYEADVVIVATGVKPNTE-FLEDTGLKTLKNGAIIVDEYGETSIENIYAAGD-CATIYNI 289
MerA TIGR02053
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ...
 240-298 2.11e-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: 2.11e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001 240 DFIVSATGVTPNVEPF-LHGNSFDLGEDGGLKVDDHMHTSLPDIYAAGDiCTTSWQLSPV 298
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 ...
 36-133 2.33e-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: 39.90  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001  36 YKKLCLCAGAK-PKLICEGNPYVLGIRDTDS--AQEFQKQL---TKAKRIMII------GNGGIALelvYEiegcEVIWA 103
Cdd:cd19980    90 AKVPLVVEISSaPKITEGGNPYVFRLNPTNSmlAKAFAKYLadkGKPKKVAFLaenddyGRGAAEA---FK----KALKA 162

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1186518001 104 IKDKAIGNTFFDAGAAEFLT--SKLIAEKSEA 133
Cdd:cd19980   163 KGVKVVATEYFDQGQTDFTTqlTKLKAANPDA 194
 
Name Accession Description Interval E-value
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
16-426 9.52e-33

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 127.57  E-value: 9.52e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001  16 VKQLKSEEHCIVTEDGNQHVYKKLCLCAGAKP-KLICEGN--PYVLGIRDTDSAQEFQKQLTKAKRIMIIGNGGIALELV 92
Cdd:COG1251    79 VTAIDRAARTVTLADGETLPYDKLVLATGSRPrVPPIPGAdlPGVFTLRTLDDADALRAALAPGKRVVVIGGGLIGLEAA 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001  93 YEI--EGCEVIWAIKDKAIGNTFFDAGAAEFLTskliaekseakiahkrtryttegrkkearskskadnvgsalgpDWHE 170
Cdd:COG1251   159 AALrkRGLEVTVVERAPRLLPRQLDEEAGALLQ-------------------------------------------RLLE 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001 171 GLNLKgtkefshkIHLETmcEVKKIyLQDEfrilkkksftfprdhkSVTAdtemwpvyVELTNEKIYGCDFIVSATGVTP 250
Cdd:COG1251   196 ALGVE--------VRLGT--GVTEI-EGDD----------------RVTG--------VRLADGEELPADLVVVAIGVRP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001 251 NVEpFLHGNSFDLgeDGGLKVDDHMHTSLPDIYAAGDICttSWQlSPVWQQ--MRLWTQARQMGWYAAKCMAAAssgdsi 328
Cdd:COG1251   241 NTE-LARAAGLAV--DRGIVVDDYLRTSDPDIYAAGDCA--EHP-GPVYGRrvLELVAPAYEQARVAAANLAGG------ 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001 329 DMDFSFELFAHVTKFFNYKVVLLGKYNaqglGSDHELMLRCTKGREYIKVVMQNGRMMGAVLIGETDLEETFENLILNQM 408
Cdd:COG1251   309 PAAYEGSVPSTKLKVFGVDVASAGDAE----GDEEVVVRGDPARGVYKKLVLRDGRLVGAVLVGDTSDAGALRQLIKNGR 384

                         410
                  ....*....|....*...
gi 1186518001 409 NLSsyGEDLLDPNIDIED 426
Cdd:COG1251   385 PLP--PRALLDAALPLKE 400
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 7-320 8.87e-21

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: 8.87e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001   7 PNIKVI-ESGVKQLKSEEHCIVTEDGNQHVYKKLCLCAGAKPKLI-CEG--NPYVLGIRDTDSAQEFQKQLT--KAKRIM 80
Cdd:COG0446    49 KGIDVRtGTEVTAIDPEAKTVTLRDGETLSYDKLVLATGARPRPPpIPGldLPGVFTLRTLDDADALREALKefKGKRAV 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001  81 IIGNGGIALELVYE----------IEGCEVIWAIKDKAIgntffdagaaefltskliaekseAKIAHKRTRyttegrkke 150
Cdd:COG0446   129 VIGGGPIGLELAEAlrkrglkvtlVERAPRLLGVLDPEM-----------------------AALLEEELR--------- 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001 151 arskskadnvgsalgpdwheglnlkgtkefSHKIHLETMCEVKKIylqdefrilkkksftfpRDHKSVTadtemwpvyVE 230
Cdd:COG0446   177 ------------------------------EHGVELRLGETVVAI-----------------DGDDKVA---------VT 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001 231 LTNEKIYGCDFIVSATGVTPNVEpFLHGNSFDLGEDGGLKVDDHMHTSLPDIYAAGDICTTSWQLSPVWQQMRLWTQARQ 310
Cdd:COG0446   201 LTDGEEIPADLVVVAPGVRPNTE-LAKDAGLALGERGWIKVDETLQTSDPDVYAAGDCAEVPHPVTGKTVYIPLASAANK 279

                         330
                  ....*....|
gi 1186518001 311 MGWYAAKCMA 320
Cdd:COG0446   280 QGRVAAENIL 289
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 12-302 2.88e-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: 75.82  E-value: 2.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001  12 IESGVKQLKSEEhcIVTEDGNQHVYKKLCLCAGAKPKLI-CEG--NPYVLGIRDTDSAQEFQKQLtKAKRIMIIGNGGIA 88
Cdd:pfam07992  88 IDPGAKKVVLEE--LVDGDGETITYDRLVIATGARPRLPpIPGveLNVGFLVRTLDSAEALRLKL-LPKRVVVVGGGYIG 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001  89 LELVYEIE--GCEVIWaIKDKAIGNTFFDAGAAEFLTSKLiaekseakiahkrtryttegrkkearsksKADNVgsalgp 166
Cdd:pfam07992 165 VELAAALAklGKEVTL-IEALDRLLRAFDEEISAALEKAL-----------------------------EKNGV------ 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001 167 dwheglnlkgtkefshKIHLETMceVKKIYlqdefrilkkksftfpRDHKSVTadtemwpvyVELTNEKIYGCDFIVSAT 246
Cdd:pfam07992 209 ----------------EVRLGTS--VKEII----------------GDGDGVE---------VILKDGTEIDADLVVVAI 245

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1186518001 247 GVTPNVEPFLHGNsFDLGEDGGLKVDDHMHTSLPDIYAAGDICTTSWQLSPVWQQM 302
Cdd:pfam07992 246 GRRPNTELLEAAG-LELDERGGIVVDEYLRTSVPGIYAAGDCRVGGPELAQNAVAQ 300
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
5-325 3.45e-12

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 67.47  E-value: 3.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001   5 RFPNIKVIESGVKQLKSEEHCIVTEDGNQHVYKKLCLCAGAKPKLicEGNP----YVLGIRDTDSAQEFQKQL------- 73
Cdd:COG1252    67 RRAGVRFIQGEVTGIDPEARTVTLADGRTLSYDYLVIATGSVTNF--FGIPglaeHALPLKTLEDALALRERLlaafera 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001  74 --TKAKRIMIIGNGGIALELVYEIegceviwaikdkaigntffdagaAEFLTSKLiaekSEAKIAHKRTRYT-TEGrkke 150
Cdd:COG1252   145 erRRLLTIVVVGGGPTGVELAGEL-----------------------AELLRKLL----RYPGIDPDKVRITlVEA---- 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001 151 arskskADNVGSALGPDwhegLNLKGTKEFSH---KIHLETMCevkkiylqdefrilkkksftfprdhKSVTADTemwpv 227
Cdd:COG1252   194 ------GPRILPGLGEK----LSEAAEKELEKrgvEVHTGTRV-------------------------TEVDADG----- 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001 228 yVELTNEKIYGCDFIVSATGVTPNvePFLHGNSFDLGEDGGLKVDDHM-HTSLPDIYAAGDICTTSWQlSPVWQ----QM 302
Cdd:COG1252   234 -VTLEDGEEIPADTVIWAAGVKAP--PLLADLGLPTDRRGRVLVDPTLqVPGHPNVFAIGDCAAVPDP-DGKPVpktaQA 309

                         330       340
                  ....*....|....*....|...
gi 1186518001 303 rlwtqARQMGWYAAKCMAAASSG 325
Cdd:COG1252   310 -----AVQQAKVLAKNIAALLRG 327
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 202-393 2.48e-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: 2.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001 202 RILKKKSFTFPRDHK--SVTADTEmwPVYVELTN---EKIYGCDFIVSATGVTPNVEpflhgnsfDLG---------EDG 267
Cdd:COG1249   217 KALEKEGIDILTGAKvtSVEKTGD--GVTVTLEDgggEEAVEADKVLVATGRRPNTD--------GLGleaagveldERG 286

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001 268 GLKVDDHMHTSLPDIYAAGDiCTTSWQLSPVwqqmrlwtqARQMGWYAAKcMAAASSGDSIDMD------FSF-ELfAHV 340
Cdd:COG1249   287 GIKVDEYLRTSVPGIYAIGD-VTGGPQLAHV---------ASAEGRVAAE-NILGKKPRPVDYRaipsvvFTDpEI-ASV 354

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1186518001 341 --------TKFFNYKVvllGKYNAQGLGsdHELMLRCTKGreYIKVV--MQNGRMMGAVLIGE 393
Cdd:COG1249   355 glteeearEAGIDVKV---GKFPFAANG--RALALGETEG--FVKLIadAETGRILGAHIVGP 410
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
229-295 1.50e-09

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 58.98  E-value: 1.50e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1186518001 229 VELTN-----EKIYGCDFIVSATGVTPNVEPFlHGNSFDLGEDGGLKVDDHMHTSLPDIYAAGDICTTSWQL 295
Cdd:COG0492   212 VTLKNvktgeEKELEVDGVFVAIGLKPNTELL-KGLGLELDEDGYIVVDEDMETSVPGVFAAGDVRDYKYRQ 282
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 227-295 1.88e-08

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 56.20  E-value: 1.88e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1186518001 227 VYVELTNEKIYGCDFIVSATGVTPNVEpFLHGNSFDLGEDGGLKVDDHMHTSLPDIYAAGDiCTTSWQL 295
Cdd:PRK09564  223 VEGVVTDKGEYEADVVIVATGVKPNTE-FLEDTGLKTLKNGAIIVDEYGETSIENIYAAGD-CATIYNI 289
MerA TIGR02053
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ...
 240-298 2.11e-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: 2.11e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001 240 DFIVSATGVTPNVEPF-LHGNSFDLGEDGGLKVDDHMHTSLPDIYAAGDiCTTSWQLSPV 298
Cdd:TIGR02053 256 DELLVATGRRPNTDGLgLEKAGVKLDERGGILVDETLRTSNPGIYAAGD-VTGGLQLEYV 314
PRK09754 PRK09754
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
 16-319 5.36e-08

phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional


Pssm-ID: 170080 [Multi-domain]  Cd Length: 396  Bit Score: 54.55  E-value: 5.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001  16 VKQLKSEEHCIVTEDGNQHVYKKLCLCAGAKPK---LICEGNPYVLGIRDTDSAQEFQKQLTKAKRIMIIGNGGIALELV 92
Cdd:PRK09754   81 IKTLGRDTRELVLTNGESWHWDQLFIATGAAARplpLLDALGERCFTLRHAGDAARLREVLQPERSVVIVGAGTIGLELA 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001  93 yeiegceviwaikdkaigntffdAGAAEFLTSKLIAEkseakiahkrtryttegrkkearsksKADNVGSALGPDWHEGL 172
Cdd:PRK09754  161 -----------------------ASATQRRCKVTVIE--------------------------LAATVMGRNAPPPVQRY 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001 173 NLKGTKEFSHKIHLETMCEvkkiylqdefrilkkksftfprdhkSVTADTEMwpVYVELTNEKIYGcDFIVSATGVTPNV 252
Cdd:PRK09754  192 LLQRHQQAGVRILLNNAIE-------------------------HVVDGEKV--ELTLQSGETLQA-DVVIYGIGISAND 243

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1186518001 253 EPFLHGNsfdLGEDGGLKVDDHMHTSLPDIYAAGDICTTSWQLSPVwQQMRLWTQARQMGWYAAKCM 319
Cdd:PRK09754  244 QLAREAN---LDTANGIVIDEACRTCDPAIFAGGDVAITRLDNGAL-HRCESWENANNQAQIAAAAM 306
PRK06370 PRK06370
FAD-containing oxidoreductase;
239-289 4.86e-07

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 51.74  E-value: 4.86e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001 239 CDFIVSATGVTPNVEpflhgnsfDLG---------EDGGLKVDDHMHTSLPDIYAAGDIC 289
Cdd:PRK06370  260 GSHILVAVGRVPNTD--------DLGleaagvetdARGYIKVDDQLRTTNPGIYAAGDCN 311
PRK07251 PRK07251
FAD-containing oxidoreductase;
232-288 8.27e-07

FAD-containing oxidoreductase;


Pssm-ID: 180907 [Multi-domain]  Cd Length: 438  Bit Score: 50.90  E-value: 8.27e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1186518001 232 TNEKIYGCDFIVSATGVTPNVEPF-LHGNSFDLGEDGGLKVDDHMHTSLPDIYAAGDI 288
Cdd:PRK07251  235 TEDETYRFDALLYATGRKPNTEPLgLENTDIELTERGAIKVDDYCQTSVPGVFAVGDV 292
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 226-288 1.08e-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: 1.08e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1186518001 226 PVYVELTnEKIYGCDFIVSATGVTPNVEPFLHGNSFDLGEDGGLKVD-DHMHTSLPDIYAAGDI 288
Cdd:COG0493   348 PVPIEGS-EFTLPADLVILAIGQTPDPSGLEEELGLELDKRGTIVVDeETYQTSLPGVFAGGDA 410
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 234-290 1.47e-06

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 50.18  E-value: 1.47e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1186518001 234 EKIYGCDFIVSATGVTPNVEPFLHGNSFDLGEDGGLKVDD-HMHTSLPDIYAAGDICT 290
Cdd:PRK11749  371 EFTLPADLVIKAIGQTPNPLILSTTPGLELNRWGTIIADDeTGRTSLPGVFAGGDIVT 428
PRK13512 PRK13512
coenzyme A disulfide reductase; Provisional
 240-352 1.62e-06

coenzyme A disulfide reductase; Provisional


Pssm-ID: 184103 [Multi-domain]  Cd Length: 438  Bit Score: 50.17  E-value: 1.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001 240 DFIVSATGVTPNVEpFLHGNSFDLGEDGGLKVDDHMHTSLPDIYAAGDICTTSWQLSPVWQQMRL-WTQARqmgwyAAKC 318
Cdd:PRK13512  231 DMIIEGVGTHPNSK-FIESSNIKLDDKGFIPVNDKFETNVPNIYAIGDIITSHYRHVDLPASVPLaWGAHR-----AASI 304

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1186518001 319 MAAASSGDSiDMDFSFELFAHVTKFFNYKVVLLG 352
Cdd:PRK13512  305 VAEQIAGND-TIEFKGFLGNNIVKFFDYTFASVG 337
PRK13748 PRK13748
putative mercuric reductase; Provisional
 232-295 6.15e-06

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 48.22  E-value: 6.15e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1186518001 232 TNEKIYGCDFIVSATGVTPNVEPF-LHGNSFDLGEDGGLKVDDHMHTSLPDIYAAGDiCTTSWQL 295
Cdd:PRK13748  347 TGHGELRADKLLVATGRAPNTRSLaLDAAGVTVNAQGAIVIDQGMRTSVPHIYAAGD-CTDQPQF 410
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
16-287 7.21e-06

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 47.99  E-value: 7.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001  16 VKQLKSEEHCIVTeDGNQHVYKKLCLCAGAK---PKLicEGNPYVLGIrdtDSAQEF---QKQLTKAKRIMIIGNGGIAL 89
Cdd:PRK04965   81 VTDIDAEAQVVKS-QGNQWQYDKLVLATGASafvPPI--PGRELMLTL---NSQQEYraaETQLRDAQRVLVVGGGLIGT 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001  90 ELVYEIegceviwAIKDKAIgnTFFDAgaAEFLTSKLIAEKSEAKIAHKRTRyttegrkkearskskadnvgsalgpdwh 169
Cdd:PRK04965  155 ELAMDL-------CRAGKAV--TLVDN--AASLLASLMPPEVSSRLQHRLTE---------------------------- 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001 170 eglnlKGtkefshkIHLETMCEVKKI-YLQDEFRilkkksftfprdhksvtadtemwpvyVELTNEKIYGCDFIVSATGV 248
Cdd:PRK04965  196 -----MG-------VHLLLKSQLQGLeKTDSGIR--------------------------ATLDSGRSIEVDAVIAAAGL 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1186518001 249 TPNVEpflhgnsfdLGEDGGLK------VDDHMHTSLPDIYAAGD 287
Cdd:PRK04965  238 RPNTA---------LARRAGLAvnrgivVDSYLQTSAPDIYALGD 273
PTZ00058 PTZ00058
glutathione reductase; Provisional
 29-289 1.41e-05

glutathione reductase; Provisional


Pssm-ID: 185420 [Multi-domain]  Cd Length: 561  Bit Score: 47.30  E-value: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001  29 EDGNQHVYKKLCLCAGAKPKLicegnPYVLGIRDTDSAQEFqKQLTKAKRIMIIGNGGIALELVyeiegceviwaikdka 108
Cdd:PTZ00058  196 DDGQVIEGKNILIAVGNKPIF-----PDVKGKEFTISSDDF-FKIKEAKRIGIAGSGYIAVELI---------------- 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001 109 igNTFFDAGAAEFLTSKliaekseakiAHKRTRYTTEGRKKEARSKSKADNvgsalgpdwheglnlkgtkefshkIHLET 188
Cdd:PTZ00058  254 --NVVNRLGAESYIFAR----------GNRLLRKFDETIINELENDMKKNN------------------------INIIT 297

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001 189 MCEVKKIYLQDEFRILkkksftfprdhksvtadtemwpVYVELTNEKIYGcDFIVSATGVTPNVEPFLHGNSFDLGEDGG 268
Cdd:PTZ00058  298 HANVEEIEKVKEKNLT----------------------IYLSDGRKYEHF-DYVIYCVGRSPNTEDLNLKALNIKTPKGY 354

                         250       260
                  ....*....|....*....|.
gi 1186518001 269 LKVDDHMHTSLPDIYAAGDIC 289
Cdd:PTZ00058  355 IKVDDNQRTSVKHIYAVGDCC 375
PRK06116 PRK06116
glutathione reductase; Validated
 229-298 1.91e-05

glutathione reductase; Validated


Pssm-ID: 235701 [Multi-domain]  Cd Length: 450  Bit Score: 46.69  E-value: 1.91e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1186518001 229 VELTNEKIYGCDFIVSATGVTPNVEPF-LHGNSFDLGEDGGLKVDDHMHTSLPDIYAAGDiCTTSWQLSPV 298
Cdd:PRK06116  244 LTLEDGETLTVDCLIWAIGREPNTDGLgLENAGVKLNEKGYIIVDEYQNTNVPGIYAVGD-VTGRVELTPV 313
PRK14989 PRK14989
nitrite reductase subunit NirD; Provisional
 240-420 2.36e-05

nitrite reductase subunit NirD; Provisional


Pssm-ID: 184951 [Multi-domain]  Cd Length: 847  Bit Score: 46.65  E-value: 2.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001 240 DFIVSATGVTPNvEPFLHGNSFDLGEDGGLKVDDHMHTSLPDIYAAGDiCtTSWqlspvwqqmrlwtQARQMGWYAAKCM 319
Cdd:PRK14989  235 DFIVFSTGIRPQ-DKLATQCGLAVAPRGGIVINDSCQTSDPDIYAIGE-C-ASW-------------NNRVFGLVAPGYK 298

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001 320 AAASSGDsidmdfsfELFAHVTKF----FNYKVVLLGkYNAQGLGSDHElmlRCTKGREY------------IKVVMQNG 383
Cdd:PRK14989  299 MAQVAVD--------HLLGSENAFegadLSAKLKLLG-VDVGGIGDAHG---RTPGARSYvyldeskeiykrLIVSEDNK 366

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1186518001 384 RMMGAVLIGETDLEETFENLILNQMNLSSYGEDLLDP 420
Cdd:PRK14989  367 TLLGAVLVGDTSDYGNLLQLVLNAIELPENPDSLILP 403
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 240-288 2.50e-05

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 46.29  E-value: 2.50e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1186518001 240 DFIVSATGVTPNVEpflhgnsfDLG-EDGGLK-------VDDHMHTSLPDIYAAGDI 288
Cdd:PRK06416  262 DYVLVAVGRRPNTE--------NLGlEELGVKtdrgfieVDEQLRTNVPNIYAIGDI 310
PRK06327 PRK06327
dihydrolipoamide dehydrogenase; Validated
 233-295 8.41e-05

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235779 [Multi-domain]  Cd Length: 475  Bit Score: 44.53  E-value: 8.41e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1186518001 233 NEKIYGCDFIVSATGVTPNVEPF-LHGNSFDLGEDGGLKVDDHMHTSLPDIYAAGDIcTTSWQL 295
Cdd:PRK06327  267 EAQTLEVDKLIVSIGRVPNTDGLgLEAVGLKLDERGFIPVDDHCRTNVPNVYAIGDV-VRGPML 329
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 197-288 1.04e-04

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 44.40  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001 197 LQDEFRILKKKSFTFPRDHK--SVTADTEMWPVYVELTNEKIY-GCDFIVSATGVTPNVEPF-LHGNSFDLGEDGGLKVD 272
Cdd:PRK06292  212 VSKQAQKILSKEFKIKLGAKvtSVEKSGDEKVEELEKGGKTETiEADYVLVATGRRPNTDGLgLENTGIELDERGRPVVD 291

                          90
                  ....*....|....*.
gi 1186518001 273 DHMHTSLPDIYAAGDI 288
Cdd:PRK06292  292 EHTQTSVPGIYAAGDV 307
PRK07846 PRK07846
mycothione reductase; Reviewed
 227-298 1.05e-04

mycothione reductase; Reviewed


Pssm-ID: 181142 [Multi-domain]  Cd Length: 451  Bit Score: 44.17  E-value: 1.05e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1186518001 227 VYVELTNEKIYGCDFIVSATGVTPNVEPF-LHGNSFDLGEDGGLKVDDHMHTSLPDIYAAGDICtTSWQLSPV 298
Cdd:PRK07846  239 VTLRLDDGSTVEADVLLVATGRVPNGDLLdAAAAGVDVDEDGRVVVDEYQRTSAEGVFALGDVS-SPYQLKHV 310
PLN02507 PLN02507
glutathione reductase
 240-298 5.02e-04

glutathione reductase


Pssm-ID: 215281 [Multi-domain]  Cd Length: 499  Bit Score: 42.11  E-value: 5.02e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001 240 DFIVSATGVTPNVEPF-LHGNSFDLGEDGGLKVDDHMHTSLPDIYAAGDIcTTSWQLSPV 298
Cdd:PLN02507  290 DVVLFATGRAPNTKRLnLEAVGVELDKAGAVKVDEYSRTNIPSIWAIGDV-TNRINLTPV 348
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
 226-290 5.64e-04

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


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 42.42  E-value: 5.64e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1186518001 226 PVYVELTNEKIyGCDFIVSATGVTPNvePFLhGNSF---DLGEDGGLKVDDHMHTSLPDIYAAGDICT 290
Cdd:PRK12778  663 PVAIPGSTFTV-DVDLVIVSVGVSPN--PLV-PSSIpglELNRKGTIVVDEEMQSSIPGIYAGGDIVR 726
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
 213-335 6.30e-04

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 41.68  E-value: 6.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001 213 RDHKSVTADTEMwpvYVELTNEKIYGCDFIVSATGVTPNvePFLHGNSFDLGEDGGLKVDDHMHTS-LPDIYAAGDICTT 291
Cdd:PTZ00318  246 RTKTAVKEVLDK---EVVLKDGEVIPTGLVVWSTGVGPG--PLTKQLKVDKTSRGRISVDDHLRVKpIPNVFALGDCAAN 320

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1186518001 292 SWQLSPVWQQMrlwtqARQMGWYAAKCMAAASSGDSIDMDFSFE 335
Cdd:PTZ00318  321 EERPLPTLAQV-----ASQQGVYLAKEFNNELKGKPMSKPFVYR 359
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
227-288 1.23e-03

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


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 40.91  E-value: 1.23e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1186518001 227 VYVELTNEKIYGCDFIVSATGVTPNVEPfLHGNSFDLGED--GGLKVDDHMHTSLPDIYAAGDI 288
Cdd:PRK05249  249 VIVHLKSGKKIKADCLLYANGRTGNTDG-LNLENAGLEADsrGQLKVNENYQTAVPHIYAVGDV 311
PRK15317 PRK15317
alkyl hydroperoxide reductase subunit F; Provisional
 247-292 1.25e-03

alkyl hydroperoxide reductase subunit F; Provisional


Pssm-ID: 237942 [Multi-domain]  Cd Length: 517  Bit Score: 40.91  E-value: 1.25e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1186518001 247 GVTPNVEpFLHGnSFDLGEDGGLKVDDHMHTSLPDIYAAGDiCTTS 292
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 ...
 36-133 2.33e-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: 39.90  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1186518001  36 YKKLCLCAGAK-PKLICEGNPYVLGIRDTDS--AQEFQKQL---TKAKRIMII------GNGGIALelvYEiegcEVIWA 103
Cdd:cd19980    90 AKVPLVVEISSaPKITEGGNPYVFRLNPTNSmlAKAFAKYLadkGKPKKVAFLaenddyGRGAAEA---FK----KALKA 162

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1186518001 104 IKDKAIGNTFFDAGAAEFLT--SKLIAEKSEA 133
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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