NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1931720864|ref|XP_037490993|]
View 

cytochrome c oxidase subunit 3 (mitochondrion) [Plasmodium vinckei vinckei]

Protein Classification

cytochrome c oxidase subunit 3( domain architecture ID 10086888)

cytochrome c oxidase subunit 3 is a component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 1-183 5.02e-29

Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. This group additionally contains proteins which are fusions between subunits I and III, such as Sulfolobus acidocaldarius SoxM, a subunit of the SoxM terminal oxidase complex. It also includes NorE which has been speculated to be a subunit of nitric oxide reductase. Some archaebacterial cytochrome oxidases lack subunit III. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria.


:

Pssm-ID: 238227  Cd Length: 183  Bit Score: 105.75  E-value: 5.02e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864   1 MLAIIISEALLFITYFWGILHFCLSPYPLYNEGIIItSSRMLILTITFILASASCMTACLQFLIEKGMSFEISSIVCIIY 80
Cdd:cd00386    13 MWLFILSEVMLFGSFFWAYFHSRLSPPVEFGAGLDP-LDLPLLNTNTLLLSGSSVTWAHASLAARRGNRKKARLWLLLTI 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864  81 LLGECFASLQTTEYLHLSYYINDAVLGTLFYCVTGLHFTHVIVGLILLLIYFIRIvdqydvnteWSYSYIGISYVILTht 160
Cdd:cd00386    92 LLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRL---------RRGHFTPRHHLGLE-- 160

                         170       180
                  ....*....|....*....|...
gi 1931720864 161 dqMTLLYWHFVEIVWLFIEFFFY 183
Cdd:cd00386   161 --AAALYWHFVDVVWLFLFPLVY 181
 
Name Accession Description Interval E-value
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 1-183 5.02e-29

Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. This group additionally contains proteins which are fusions between subunits I and III, such as Sulfolobus acidocaldarius SoxM, a subunit of the SoxM terminal oxidase complex. It also includes NorE which has been speculated to be a subunit of nitric oxide reductase. Some archaebacterial cytochrome oxidases lack subunit III. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria.


Pssm-ID: 238227  Cd Length: 183  Bit Score: 105.75  E-value: 5.02e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864   1 MLAIIISEALLFITYFWGILHFCLSPYPLYNEGIIItSSRMLILTITFILASASCMTACLQFLIEKGMSFEISSIVCIIY 80
Cdd:cd00386    13 MWLFILSEVMLFGSFFWAYFHSRLSPPVEFGAGLDP-LDLPLLNTNTLLLSGSSVTWAHASLAARRGNRKKARLWLLLTI 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864  81 LLGECFASLQTTEYLHLSYYINDAVLGTLFYCVTGLHFTHVIVGLILLLIYFIRIvdqydvnteWSYSYIGISYVILTht 160
Cdd:cd00386    92 LLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRL---------RRGHFTPRHHLGLE-- 160

                         170       180
                  ....*....|....*....|...
gi 1931720864 161 dqMTLLYWHFVEIVWLFIEFFFY 183
Cdd:cd00386   161 --AAALYWHFVDVVWLFLFPLVY 181
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 1-183 2.95e-18

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 79.45  E-value: 2.95e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864   1 MLAIIISEALLFITYFWGILHFCLSP-------YPLYneGIIITSSRMLILTITFIL-ASASCMTACLQFLIEKGMSFEI 72
Cdd:MTH00155   81 MILFIVSEVFFFISFFWAFFHSSLSPnielgmiWPPK--GIIPFNPFQIPLLNTIILlSSGVTVTWAHHSLMENNYKQAT 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864  73 SS-IVCIIylLGECFASLQTTEYLHLSYYINDAVLGTLFYCVTGLHFTHVIVGLILLLIYFIRIvdqyDVNTEWSYSYIG 151
Cdd:MTH00155  159 QSlFFTII--LGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRH----LNNHFSSNHHFG 232

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1931720864 152 ISYVIlthtdqmtlLYWHFVEIVWLFIEFFFY 183
Cdd:MTH00155  233 FEAAA---------WYWHFVDVVWLFLYISIY 255
COX3 pfam00510
Cytochrome c oxidase subunit III;
1-183 1.17e-16

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 75.14  E-value: 1.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864   1 MLAIIISEALLFITYFWGILHFCLSPYPLYNE-----GI-IITSSRMLILTITFILASASCMTACLQFLIEKGMSFEISS 74
Cdd:pfam00510  80 MILFIISEVFFFLGIFWAFFHSALSPTVELGAqwppvGIhPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQG 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864  75 IVCIIyLLGECFASLQTTEYLHLSYYINDAVLGTLFYCVTGLHFTHVIVGLILLLIYFIRIVdQYDVNTEWSYSYigisy 154
Cdd:pfam00510 160 LILTI-LLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLL-KYHLTDNHHFGF----- 232

                         170       180
                  ....*....|....*....|....*....
gi 1931720864 155 vilthtdQMTLLYWHFVEIVWLFIEFFFY 183
Cdd:pfam00510 233 -------EAAILYWHFVDVVWLFLYVSVY 254
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
1-183 8.26e-12

Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];


Pssm-ID: 441450  Cd Length: 192  Bit Score: 61.02  E-value: 8.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864   1 MLAIIISEALLFITYFWGILHFCLSpYPLYNEGIIITSsRMLILTITFILASASCMTACLQFLIEKGMSFEISSIVCIIY 80
Cdd:COG1845    20 MWLFLASEVMLFAALFAAYFVLRAS-APDWPAGAELLD-LPLPLINTLLLLLSSFTVALAVRAARRGDRKGLRLWLLLTL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864  81 LLGECFASLQTTEYLHLS---YYINDAVLGTLFYCVTGLHFTHVIVGLILLLIYFIRIvdqydvnteWSYSYIGISYVIL 157
Cdd:COG1845    98 LLGLAFLGLQAYEYSHLIaegLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRA---------LRGGFTPENHTGV 168

                         170       180
                  ....*....|....*....|....*.
gi 1931720864 158 thtdQMTLLYWHFVEIVWLFIEFFFY 183
Cdd:COG1845   169 ----EAAALYWHFVDVVWIFLFALVY 190
 
Name Accession Description Interval E-value
Heme_Cu_Oxidase_III_like cd00386
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ...
 1-183 5.02e-29

Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. This group additionally contains proteins which are fusions between subunits I and III, such as Sulfolobus acidocaldarius SoxM, a subunit of the SoxM terminal oxidase complex. It also includes NorE which has been speculated to be a subunit of nitric oxide reductase. Some archaebacterial cytochrome oxidases lack subunit III. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria.


Pssm-ID: 238227  Cd Length: 183  Bit Score: 105.75  E-value: 5.02e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864   1 MLAIIISEALLFITYFWGILHFCLSPYPLYNEGIIItSSRMLILTITFILASASCMTACLQFLIEKGMSFEISSIVCIIY 80
Cdd:cd00386    13 MWLFILSEVMLFGSFFWAYFHSRLSPPVEFGAGLDP-LDLPLLNTNTLLLSGSSVTWAHASLAARRGNRKKARLWLLLTI 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864  81 LLGECFASLQTTEYLHLSYYINDAVLGTLFYCVTGLHFTHVIVGLILLLIYFIRIvdqydvnteWSYSYIGISYVILTht 160
Cdd:cd00386    92 LLGLAFLGLQAYEYSHLIFTISDSVFGSTFFLLTGFHGLHVIIGLIFLLVVLIRL---------RRGHFTPRHHLGLE-- 160

                         170       180
                  ....*....|....*....|...
gi 1931720864 161 dqMTLLYWHFVEIVWLFIEFFFY 183
Cdd:cd00386   161 --AAALYWHFVDVVWLFLFPLVY 181
Cyt_c_Oxidase_III cd01665
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-183 7.43e-20

Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. CcO catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit III contains bound phospholipids in several crystal structures and is proposed to contain a "lipid pool." These phospholipids are believed to intrinsic constituents similar to cofactors of the enzyme.


Pssm-ID: 238834  Cd Length: 243  Bit Score: 83.33  E-value: 7.43e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864   1 MLAIIISEALLFITYFWGILHFCLSP-------YPLYNEGIIITSSRMLILTITFILASASCMTACLQFLIEKGMSFEIS 73
Cdd:cd01665    67 MILFILSEVMFFFSFFWAFFHSSLSPsvelggtWPPVGIEPLNPFGIPLLNTIILLSSGATVTWAHHALLLGNRKKAILG 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864  74 SIVCIiyLLGECFASLQTTEYLHLSYYINDAVLGTLFYCVTGLHFTHVIVGLILLLIYFIRIVdQYDVNTEWSYSYigis 153
Cdd:cd01665   147 LILTI--LLGVYFTGLQAYEYYEASFTISDSVYGSTFFMLTGFHGLHVIIGTIFLTVCLIRLL-KGHFSSNHHLGF---- 219

                         170       180       190
                  ....*....|....*....|....*....|
gi 1931720864 154 yvilthtdQMTLLYWHFVEIVWLFIEFFFY 183
Cdd:cd01665   220 --------EAAIWYWHFVDVVWLFLFVFVY 241
COX3 MTH00155
cytochrome c oxidase subunit III; Provisional
 1-183 2.95e-18

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214439  Cd Length: 255  Bit Score: 79.45  E-value: 2.95e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864   1 MLAIIISEALLFITYFWGILHFCLSP-------YPLYneGIIITSSRMLILTITFIL-ASASCMTACLQFLIEKGMSFEI 72
Cdd:MTH00155   81 MILFIVSEVFFFISFFWAFFHSSLSPnielgmiWPPK--GIIPFNPFQIPLLNTIILlSSGVTVTWAHHSLMENNYKQAT 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864  73 SS-IVCIIylLGECFASLQTTEYLHLSYYINDAVLGTLFYCVTGLHFTHVIVGLILLLIYFIRIvdqyDVNTEWSYSYIG 151
Cdd:MTH00155  159 QSlFFTII--LGIYFTMLQAYEYYEAPFTIADSVYGSTFFMATGFHGLHVIIGTTFLLVCLIRH----LNNHFSSNHHFG 232

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1931720864 152 ISYVIlthtdqmtlLYWHFVEIVWLFIEFFFY 183
Cdd:MTH00155  233 FEAAA---------WYWHFVDVVWLFLYISIY 255
COX3 pfam00510
Cytochrome c oxidase subunit III;
1-183 1.17e-16

Cytochrome c oxidase subunit III;


Pssm-ID: 395410  Cd Length: 258  Bit Score: 75.14  E-value: 1.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864   1 MLAIIISEALLFITYFWGILHFCLSPYPLYNE-----GI-IITSSRMLILTITFILASASCMTACLQFLIEKGMSFEISS 74
Cdd:pfam00510  80 MILFIISEVFFFLGIFWAFFHSALSPTVELGAqwppvGIhPVNPFEVPLLNTIILLSSGVTVTYAHHSLIEGNRKQALQG 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864  75 IVCIIyLLGECFASLQTTEYLHLSYYINDAVLGTLFYCVTGLHFTHVIVGLILLLIYFIRIVdQYDVNTEWSYSYigisy 154
Cdd:pfam00510 160 LILTI-LLAVYFTGLQAMEYTEASFTISDGVYGSTFYFATGFHGLHVIIGTAFLAVCFLRLL-KYHLTDNHHFGF----- 232

                         170       180
                  ....*....|....*....|....*....
gi 1931720864 155 vilthtdQMTLLYWHFVEIVWLFIEFFFY 183
Cdd:pfam00510 233 -------EAAILYWHFVDVVWLFLYVSVY 254
COX3 MTH00028
cytochrome c oxidase subunit III; Provisional
 1-183 1.24e-15

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214406  Cd Length: 297  Bit Score: 72.79  E-value: 1.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864   1 MLAIIISEALLFITYFWGILHFCLSP--------------------YPLYNEGIIITSSRMLILTITFILASASCMTACL 60
Cdd:MTH00028   83 MLLFILSEVCLFFAFFWAFFHSSLAPsvelgsvwppkgiealdpfaVPLLNTTILLSSGATVTWAHHAIIGTGNPASLEK 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864  61 --------------QFLIEKGMSFEISSI-------VCIIYLLGECFASLQTTEYLHLSYYINDAVLGTLFYCVTGLHFT 119
Cdd:MTH00028  163 gtqgiegpnpsngaPPDPQKGPTFLLSDFrtnavigLLMTILLGIIFTGLQAFEYKEASFAISDSVYGSTFFMLTGTHGL 242

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1931720864 120 HVIVGLILLLIYFIRIVDQYDVNTEwsysYIGISYVILthtdqmtllYWHFVEIVWLFIEFFFY 183
Cdd:MTH00028  243 HVLVGTTFLIVCFIRLLSNQFTNSH----HLGLEAAIW---------YWHFVDVVWLFLYVFVY 293
COX3 MTH00130
cytochrome c oxidase subunit III; Provisional
 1-183 2.55e-14

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177188  Cd Length: 261  Bit Score: 68.64  E-value: 2.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864   1 MLAIIISEALLFITYFWGILHFCLSPYPLYN-----EGII-ITSSRMLILTITFILASASCMTACLQFLIEKGMSFEISS 74
Cdd:MTH00130   83 MILFITSEVFFFLGFFWAFYHSSLAPTPELGgcwppTGITtLDPFEVPLLNTAVLLASGVTVTWAHHSIMEGERKQAIQS 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864  75 IVCIIyLLGECFASLQTTEYLHLSYYINDAVLGTLFYCVTGLHFTHVIVGLILLLIYFIRIVdQYDVNTEWSYSYIGISY 154
Cdd:MTH00130  163 LTLTI-LLGFYFTFLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSTFLAVCLLRQI-QYHFTSEHHFGFEAAAW 240

                         170       180
                  ....*....|....*....|....*....
gi 1931720864 155 vilthtdqmtllYWHFVEIVWLFIEFFFY 183
Cdd:MTH00130  241 ------------YWHFVDVVWLFLYISIY 257
COX3 MTH00118
cytochrome c oxidase subunit III; Provisional
 1-178 8.35e-14

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177179  Cd Length: 261  Bit Score: 67.28  E-value: 8.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864   1 MLAIIISEALLFITYFWGILHFCLSPYP-LYNE----GII-ITSSRMLILTITFILASASCMTACLQFLIEkGMSFEISS 74
Cdd:MTH00118   83 MILFITSEVFFFLGFFWAFYHSSLAPTPeLGGQwpptGIKpLNPFEVPLLNTAVLLASGVTVTWAHHSIME-GNRKQAIQ 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864  75 IVCIIYLLGECFASLQTTEYLHLSYYINDAVLGTLFYCVTGLHFTHVIVGLILLLIYFIRIVdQYDVNTEWSYSYigisy 154
Cdd:MTH00118  162 ALTLTILLGLYFTALQAMEYYEAPFTISDSVYGSTFFVATGFHGLHVIIGSTFLIVCLLRLI-KFHFTTNHHFGF----- 235

                         170       180
                  ....*....|....*....|....
gi 1931720864 155 vilthtdQMTLLYWHFVEIVWLFI 178
Cdd:MTH00118  236 -------EAAAWYWHFVDVVWLFL 252
COX3 MTH00141
cytochrome c oxidase subunit III; Provisional
 1-183 1.08e-13

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177199  Cd Length: 259  Bit Score: 66.84  E-value: 1.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864   1 MLAIIISEALLFITYFWGILHFCLSP-------------YPLYNEGIIITSSRMLILTITFILASASCMTAclqfliEKG 67
Cdd:MTH00141   81 FILFIVSEVCFFFAFFWAYFHSSLAPsveigccwppvgiEPLNPFQVPLLNTAVLLASGVTVTWAHHSLME------GDY 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864  68 MSFEISSIVCIIylLGECFASLQTTEYLHLSYYINDAVLGTLFYCVTGLHFTHVIVGLILLLIYFIRIvdqydVNTEWSY 147
Cdd:MTH00141  155 KSALQGLGLTII--LGVYFTFLQAGEYYEASFSIADGVYGSTFFVLTGFHGLHVIIGTTFLLVCLVRL-----LLGHFST 227

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1931720864 148 S-YIGISYVIlthtdqmtlLYWHFVEIVWLFIEFFFY 183
Cdd:MTH00141  228 NhHFGFEAAA---------WYWHFVDVVWLFLYLSIY 255
COX3 MTH00099
cytochrome c oxidase subunit III; Validated
 1-178 1.53e-13

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177161  Cd Length: 261  Bit Score: 66.67  E-value: 1.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864   1 MLAIIISEALLFITYFWGILHFCLSPYPLYN-----EGII-ITSSRMLILTITFILASASCMTACLQFLIEKGMSFEISS 74
Cdd:MTH00099   83 MILFIISEVFFFAGFFWAFYHSSLAPTPELGgcwppTGITpLNPLEVPLLNTSVLLASGVSITWAHHSLMEGNRKHMLQA 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864  75 IVCIIyLLGECFASLQTTEYLHLSYYINDAVLGTLFYCVTGLHFTHVIVGLILLLIYFIRIVdQYDVNTEWSYSYIGISY 154
Cdd:MTH00099  163 LFITI-LLGLYFTLLQASEYYEAPFTISDGIYGSTFFMATGFHGLHVIIGSTFLIVCFLRQL-KFHFTSNHHFGFEAAAW 240

                         170       180
                  ....*....|....*....|....
gi 1931720864 155 vilthtdqmtllYWHFVEIVWLFI 178
Cdd:MTH00099  241 ------------YWHFVDVVWLFL 252
COX3 MTH00039
cytochrome c oxidase subunit III; Validated
 1-183 1.57e-13

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177114  Cd Length: 260  Bit Score: 66.67  E-value: 1.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864   1 MLAIIISEALLFITYFWGILHFCLSPYPLYN-----EGII-ITSSRMLILTITFILASASCMTACLQFLIEKGMSFEISS 74
Cdd:MTH00039   82 MILFITSEVCFFFAFFWAFFHSSLAPTVEIGvswppTGINpINPFLVPLLNTAVLLSSGVTITWSHHSILEGNRTEAIQA 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864  75 IVCIIyLLGECFASLQTTEYLHLSYYINDAVLGTLFYCVTGLHFTHVIVGLILLLIYFIRIVDQYDVNtewsYSYIGISY 154
Cdd:MTH00039  162 LFLTV-LLGLYFTALQAWEYYDAPFTIADSVYGSTFFVATGFHGLHVIIGTTFLAVCLFRLINHHFSN----NHHFGFEA 236

                         170       180
                  ....*....|....*....|....*....
gi 1931720864 155 VILthtdqmtllYWHFVEIVWLFIEFFFY 183
Cdd:MTH00039  237 AAW---------YWHFVDVVWLFLYVCIY 256
COX3 MTH00219
cytochrome c oxidase subunit III; Provisional
 1-183 2.08e-13

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 214464  Cd Length: 262  Bit Score: 66.35  E-value: 2.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864   1 MLAIIISEALLFITYFWGILHFCLSPYPLYNE-----GI-IITSSRMLILTITFILASASCMTACLQFLIEKGMSFEISS 74
Cdd:MTH00219   84 MILFIVSEILFFFAFFWAFFHSSLAPTIELGScwpptGInPLNPFQVPLLNTAVLLASGVTVTWAHHSLMESNHKEAQQG 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864  75 IVCIIyLLGECFASLQTTEYLHLSYYINDAVLGTLFYCVTGLHFTHVIVGLILLLIYFIRIVdqydVNTEWSYSYIGIsy 154
Cdd:MTH00219  164 LLFTI-LLGLYFTMLQGMEYLEASFSISDSVYGTTFFVATGFHGLHVIIGTIFLFVCFMRGL----MLHFSKNHHFGF-- 236

                         170       180
                  ....*....|....*....|....*....
gi 1931720864 155 vilthtdQMTLLYWHFVEIVWLFIEFFFY 183
Cdd:MTH00219  237 -------EAAAWYWHFVDVVWLFLYVSIY 258
COX3 MTH00052
cytochrome c oxidase subunit III; Provisional
 1-183 3.17e-13

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 164623  Cd Length: 262  Bit Score: 65.97  E-value: 3.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864   1 MLAIIISEALLFITYFWGILHFCLSP-------YPlyNEGIIITSSRMLILTITFILASASCMTACLQFLIEKGMSFEIS 73
Cdd:MTH00052   84 MILFIVSEVCLFFSFFWAFFHSSLAPtieigavWP--PRGVDPLNPFSVPLLNTAVLLSSGATVTWAHHGIISGKRKEAI 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864  74 SIVCIIYLLGECFASLQTTEYLHLSYYINDAVLGTLFYCVTGLHFTHVIVGLILLLIYFIRIvdqydvntewsysyigIS 153
Cdd:MTH00052  162 IGLALTVALGLLFTGLQAMEYYEAPFTISDSVYGSTFFVTTGAHGGHVLIGSSFLLVCLFRL----------------IN 225

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1931720864 154 YVILTHTD---QMTLLYWHFVEIVWLFIEFFFY 183
Cdd:MTH00052  226 HQFTRHHHfgfEAAAWYWHFVDVVWLFLFIFMY 258
COX3 MTH00075
cytochrome c oxidase subunit III; Provisional
 1-178 5.80e-13

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177146  Cd Length: 261  Bit Score: 65.15  E-value: 5.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864   1 MLAIIISEALLFITYFWGILHFCLSPYPLYNE-----GII-ITSSRMLILTITFILASASCMTACLQFLIEKGMSFEISS 74
Cdd:MTH00075   83 MILFITSEVFFFLGFFWAFYNSSLAPTPELGEcwpptGITpLDPFEVPLLNTAVLLASGVTVTWAHHSIMQGNRKEAIQS 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864  75 IVCIIyLLGECFASLQTTEYLHLSYYINDAVLGTLFYCVTGLHFTHVIVGLILLLIYFIRIVdQYDVNTEWSYSYIGISY 154
Cdd:MTH00075  163 LALTI-ILGLYFTLLQAMEYYEAPFTIADGVYGSTFFVATGFHGLHVIIGSLFLLVCLLRQI-NFHFTSQHHFGFEAAAW 240

                         170       180
                  ....*....|....*....|....
gi 1931720864 155 vilthtdqmtllYWHFVEIVWLFI 178
Cdd:MTH00075  241 ------------YWHFVDVVWLFL 252
COX3 MTH00083
cytochrome c oxidase subunit III; Provisional
 1-183 2.20e-12

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177150  Cd Length: 256  Bit Score: 63.44  E-value: 2.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864   1 MLAIIISEALLFITYFWGILHFCLSPYPLYNE-----GIIITSSRMLILTITFILASASC-MTACLQFLIEKGMSFEISS 74
Cdd:MTH00083   79 MILFIFSEFMFFFSIFWTFFDAALVPVHELGGvwspiGIHLVNYLGVPLLNTIILLSSGVsVTWSHHSLCLSNKSCTNSL 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864  75 IVCIIylLGECFASLQTTEYLHLSYYINDAVLGTLFYCVTGLHFTHVIVGLILLLIYFIRIVdQYDVNTEWSYSYigisy 154
Cdd:MTH00083  159 LLTCF--LGLYFTSFQLMEYKEASFSISDSIYGSIFYLGTGFHGIHVLCGGLFLLFNLLRLL-KSHFNYNHHLGL----- 230

                         170       180
                  ....*....|....*....|....*....
gi 1931720864 155 vilthtdQMTLLYWHFVEIVWLFIEFFFY 183
Cdd:MTH00083  231 -------EFAILYWHFVDVVWLFLFVFVY 252
COX3 MTH00009
cytochrome c oxidase subunit III; Validated
 1-183 2.40e-12

cytochrome c oxidase subunit III; Validated


Pssm-ID: 177101  Cd Length: 259  Bit Score: 63.32  E-value: 2.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864   1 MLAIIISEALLFITYFWGILHFCLSPYPLYN-----EGI-IITSSRMLILTITFILASASCMTACLQFLIEkGMSFEISS 74
Cdd:MTH00009   81 MILFIASEVMFFFAFFWAFFHSSLAPTPELGcswppTGIePLNPFSVPLLNTAVLLASGVTVTWAHHSLIE-GDRPEATQ 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864  75 IVCIIYLLGECFASLQTTEYLHLSYYINDAVLGTLFYCVTGLHFTHVIVGLILLLIYFIRIvdqydvnteWSYSYIGISY 154
Cdd:MTH00009  160 ALILTVLLGAYFTFLQAGEYIEAPFTIADSVYGSTFFVATGFHGLHVLIGSSFLFVCLLRT---------WSHHFSTGHH 230

                         170       180
                  ....*....|....*....|....*....
gi 1931720864 155 VILthtdQMTLLYWHFVEIVWLFIEFFFY 183
Cdd:MTH00009  231 FGF----EAAAWYWHFVDVVWIFLYLCIY 255
COX3 MTH00189
cytochrome c oxidase subunit III; Provisional
 1-183 2.99e-12

cytochrome c oxidase subunit III; Provisional


Pssm-ID: 177238  Cd Length: 260  Bit Score: 63.07  E-value: 2.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864   1 MLAIIISEALLFITYFWGILHFCLSPYPLYNE-----GII-ITSSRMLILTITFILASASCMTACLQFLIEKGMSFEISS 74
Cdd:MTH00189   82 MILFITSEVFFFLGFFWAFFHSSLAPTVELGMcwpptGIEpLNPFEVPLLNTAVLLSSGVTVTWAHHSLMEGNRKEAIQA 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864  75 IVCIIyLLGECFASLQTTEYLHLSYYINDAVLGTLFYCVTGLHFTHVIVGLILLLIYFIRIVdQYDVNTEWSYSYigisy 154
Cdd:MTH00189  162 LTLTV-ILGVYFTLLQAMEYYEAPFTIADSVYGSTFFVATGFHGLHVIIGSTFLLVCLLRQI-QGHFTSSHHFGF----- 234

                         170       180
                  ....*....|....*....|....*....
gi 1931720864 155 vilthtdQMTLLYWHFVEIVWLFIEFFFY 183
Cdd:MTH00189  235 -------EAAAWYWHFVDVVWLFLYVSIY 256
CyoC COG1845
Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];
1-183 8.26e-12

Heme/copper-type cytochrome/quinol oxidase, subunit 3 [Energy production and conversion];


Pssm-ID: 441450  Cd Length: 192  Bit Score: 61.02  E-value: 8.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864   1 MLAIIISEALLFITYFWGILHFCLSpYPLYNEGIIITSsRMLILTITFILASASCMTACLQFLIEKGMSFEISSIVCIIY 80
Cdd:COG1845    20 MWLFLASEVMLFAALFAAYFVLRAS-APDWPAGAELLD-LPLPLINTLLLLLSSFTVALAVRAARRGDRKGLRLWLLLTL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864  81 LLGECFASLQTTEYLHLS---YYINDAVLGTLFYCVTGLHFTHVIVGLILLLIYFIRIvdqydvnteWSYSYIGISYVIL 157
Cdd:COG1845    98 LLGLAFLGLQAYEYSHLIaegLTPTSNAFGSFFFLLTGFHGLHVIIGLIWLLVVLVRA---------LRGGFTPENHTGV 168

                         170       180
                  ....*....|....*....|....*.
gi 1931720864 158 thtdQMTLLYWHFVEIVWLFIEFFFY 183
Cdd:COG1845   169 ----EAAALYWHFVDVVWIFLFALVY 190
PLN02194 PLN02194
cytochrome-c oxidase
 5-183 2.71e-09

cytochrome-c oxidase


Pssm-ID: 177845  Cd Length: 265  Bit Score: 55.05  E-value: 2.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864   5 IISEALLFITYFWGILHFCLSPYPLYN-----EGIIITSSRMLILTITFILASASCMTACLQFLIEKGMSFEISSIVCII 79
Cdd:PLN02194   90 IVSEVMFFFAFFWASSHSSLAPAVEIGgiwppKGIEVLDPWEIPFLNTPILPSSGAAVTWAHHAILAGKEKRAVYALVAT 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864  80 YLLGECFASLQTTEYLHLSYYINDAVLGTLFYCVTGLHFTHVIVGLILLLIYFIRivdqydvntewsySYIGISYVILTH 159
Cdd:PLN02194  170 VLLALVFTGFQGMEYYQAPFTISDSIYGSTFFLATGFHGFHVIIGTLFLIICGIR-------------QYLGHLTKEHHV 236

                         170       180
                  ....*....|....*....|....
gi 1931720864 160 TDQMTLLYWHFVEIVWLFIEFFFY 183
Cdd:PLN02194  237 GFEAAAWYWHFVDVVWLFLFVSIY 260
Heme_Cu_Oxidase_III_1 cd02864
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 41-183 7.63e-09

Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria.


Pssm-ID: 239215  Cd Length: 202  Bit Score: 52.89  E-value: 7.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864  41 MLILTITFILASASCMTACLQFLIEKGMSFEISSIVCIIYLLGECFASLQTTEYLHLSYYIND---------AVLGTLFY 111
Cdd:cd02864    61 VLIAIMTFILITSSGTMAMAVNFGYRGNRKAAARLMLATALLGATFVGMQAFEWTKLIVEEGVrpwgnpwgaAQFGASFF 140

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1931720864 112 CVTGLHFTHVIVGLILLLIYFiRIVDQYDVNTEWSYSYIGISYvilthtdqmtlLYWHFVEIVWLFIEFFFY 183
Cdd:cd02864   141 MITGFHGTHVTIGVIYLIIIA-RKVWRGKYQRIGRYEIVEIAG-----------LYWHFVDLVWVFIFAFFY 200
NorE_like cd02862
NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include ...
 108-183 6.72e-06

NorE_like subfamily of heme-copper oxidase subunit III. Heme-copper oxidases include cytochrome c and ubiquinol oxidases. Alcaligenes faecalis norE is found in a gene cluster containing norCB. norCB encodes the cytochrome c and cytochrome b subunits of nitric oxide reductase (NOR). Based on this and on its similarity to subunit III of cytochrome c oxidase (CcO) and ubiquinol oxidase, NorE has been speculated to be a subunit of NOR.


Pssm-ID: 239213  Cd Length: 186  Bit Score: 44.53  E-value: 6.72e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1931720864 108 TLFYCVTGLHFTHVIVGLILLLIYFIRIvdqydvnteWSYSYIGISYVILthtdQMTLLYWHFVEIVWLFIEFFFY 183
Cdd:cd02862   122 TLYFLLTGFHLLHVLIGLGILLWVAWRA---------RRGRYSARDYEGV----EAAALYWHMVDLVWIVLFPLLY 184
Heme_Cu_Oxidase_III_2 cd02865
Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein ...
 107-183 1.56e-04

Heme-copper oxidase subunit III subfamily. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria.


Pssm-ID: 239216  Cd Length: 184  Bit Score: 40.43  E-value: 1.56e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1931720864 107 GTLFYCVTGLHFTHVIVGLILLLI-YFIRIVDQYDVNTEWSYSyigisyvilthtdqMTLLYWHFVEIVWLFIEFFFY 183
Cdd:cd02865   119 GSFFYLLTGLHGLHVIGGLVALAIvLAGLIRGHYGPRRRLPVE--------------LCALYWHFLLLVWLVLLALLY 182
Ubiquinol_oxidase_III cd02863
Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the ...
 9-183 4.31e-04

Ubiquinol oxidase subunit III subfamily. Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. Ubiquinol oxidases feature four subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of bovine CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in bovine CcO. Although not required for catalytic activity, subunit III appears to be involved in assembly of the multimer complex.


Pssm-ID: 239214  Cd Length: 186  Bit Score: 39.15  E-value: 4.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864   9 ALLFITYFwgILHFCLSPYPLYNEgiIITSSRMLILTITFILASASCMTACLQflIEKGMSFEISSIVCIIYLLGECFAS 88
Cdd:cd02863    25 ATLFATYA--VLSGNTAGGPPGHE--LFELPLVFIETFLLLLSSFTCGLAMIA--MNKNNKKKVILWLIITFLLGLGFVG 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720864  89 LQTTEYLHL---SYYINDAVLGTLFYCVTGLHFTHVIVGLILLLIYFIRIVdqydvntewsysYIGISyvILTHTDQMTL 165
Cdd:cd02863    99 MEIYEFHHLiaeGAGPDRSAFLSAFFTLVGTHGLHVTFGLIWILVMIIQLK------------KRGLT--PDTARRLFCL 164

                         170
                  ....*....|....*....
gi 1931720864 166 -LYWHFVEIVWLFIEFFFY 183
Cdd:cd02863   165 sLFWHFLDIVWIFVFTVVY 183
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH