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Conserved domains on  [gi|970839881|gb|ALU66374|]
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cytochrome c oxidase subunit II, partial (mitochondrion) [Sphenacris crassicornis]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475927)

cytochrome c oxidase subunit II, part of the functional core of the enzyme, transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit I

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-153 3.70e-96

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 276.71  E-value: 3.70e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839881   1 IMITMIVGYSLSYIMFINFKNRNMLHGHLIETIWTMMPAFTLIFIALPSLRLLYMLDDSNDAMITIKTIGRQWYWSYEYS 80
Cdd:MTH00154  32 IMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYS 111

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 970839881  81 DFINVEFDTYIHPEKELNQDSFRLLDVDNRTIVPMNSEVRMLTSASDVLHSWTMPALGIKVDAMPGRLNQGTF 153
Cdd:MTH00154 112 DFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNF 184
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-153 3.70e-96

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 276.71  E-value: 3.70e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839881   1 IMITMIVGYSLSYIMFINFKNRNMLHGHLIETIWTMMPAFTLIFIALPSLRLLYMLDDSNDAMITIKTIGRQWYWSYEYS 80
Cdd:MTH00154  32 IMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYS 111

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 970839881  81 DFINVEFDTYIHPEKELNQDSFRLLDVDNRTIVPMNSEVRMLTSASDVLHSWTMPALGIKVDAMPGRLNQGTF 153
Cdd:MTH00154 112 DFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNF 184
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 64-153 2.81e-53

C-terminal domain of Cytochrome c Oxidase subunit II; 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. It 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. 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 II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 164.67  E-value: 2.81e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839881  64 ITIKTIGRQWYWSYEYSDFINVEFDTYIHPEKELNQDSFRLLDVDNRTIVPMNSEVRMLTSASDVLHSWTMPALGIKVDA 143
Cdd:cd13912    3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                         90
                 ....*....|
gi 970839881 144 MPGRLNQGTF 153
Cdd:cd13912   83 VPGRLNQTSF 92
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
64-153 2.67e-49

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 154.49  E-value: 2.67e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839881   64 ITIKTIGRQWYWSYEYSDFINVEFDTYIHPEKELNQDSFRLLDVDNRTIVPMNSEVRMLTSASDVLHSWTMPALGIKVDA 143
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90
                  ....*....|
gi 970839881  144 MPGRLNQGTF 153
Cdd:pfam00116  81 VPGRLNQTSF 90
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
26-150 3.27e-28

Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 103.75  E-value: 3.27e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839881  26 HGHLIETIWTMMPAFTLIFIALPSLRLLYMLDDSNDAMITIKTIGRQWYWSYEYsdfinvefdtyihpekeLNQDSfrll 105
Cdd:COG1622   75 HNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY-----------------PDQGI---- 133

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 970839881 106 DVDNRTIVPMNSEVRMLTSASDVLHSWTMPALGIKVDAMPGRLNQ 150
Cdd:COG1622  134 ATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTE 178
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 1-153 9.33e-22

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 86.28  E-value: 9.33e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839881    1 IMITMIVgyslsYIMFINFKNRN--------MLHGH-LIETIWTMMPA-FTLIFIALPSLRLLYMLDDSNDAMITIKTIG 70
Cdd:TIGR02866  23 ISLLVAA-----LLAYVVWKFRRkgdeekpsQIHGNrRLEYVWTVIPLiIVVGLFAATAKGLLYLERPIPKDALKVKVTG 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839881   71 RQWYWSYEYSDFinvefdtyihpekelnqdsfrLLDVDNRTIVPMNSEVRMLTSASDVLHSWTMPALGIKVDAMPGRLNQ 150
Cdd:TIGR02866  98 YQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNA 156


                  ...
gi 970839881  151 GTF 153
Cdd:TIGR02866 157 LWF 159
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-153 3.70e-96

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 276.71  E-value: 3.70e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839881   1 IMITMIVGYSLSYIMFINFKNRNMLHGHLIETIWTMMPAFTLIFIALPSLRLLYMLDDSNDAMITIKTIGRQWYWSYEYS 80
Cdd:MTH00154  32 IMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYS 111

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 970839881  81 DFINVEFDTYIHPEKELNQDSFRLLDVDNRTIVPMNSEVRMLTSASDVLHSWTMPALGIKVDAMPGRLNQGTF 153
Cdd:MTH00154 112 DFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNF 184
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-153 4.07e-73

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 218.27  E-value: 4.07e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839881   1 IMITMIVGYSLSYIMFINFKNRNMLHGHLIETIWTMMPAFTLIFIALPSLRLLYMLDDSNDAMITIKTIGRQWYWSYEYS 80
Cdd:MTH00140  32 VLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYLLDETNNPLLTVKAIGHQWYWSYEYS 111

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 970839881  81 DFINVEFDTYIHPEKELNQDSFRLLDVDNRTIVPMNSEVRMLTSASDVLHSWTMPALGIKVDAMPGRLNQGTF 153
Cdd:MTH00140 112 DFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSF 184
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-153 9.34e-72

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 214.78  E-value: 9.34e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839881   1 IMITMIVGYSLSYIMFINFKNRNMLHGHLIETIWTMMPAFTLIFIALPSLRLLYMLDDSNDAMITIKTIGRQWYWSYEYS 80
Cdd:MTH00117  32 LLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYLMDEINNPHLTIKAIGHQWYWSYEYT 111

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 970839881  81 DFINVEFDTYIHPEKELNQDSFRLLDVDNRTIVPMNSEVRMLTSASDVLHSWTMPALGIKVDAMPGRLNQGTF 153
Cdd:MTH00117 112 DYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSF 184
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-150 2.59e-70

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 211.11  E-value: 2.59e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839881   1 IMITMIVGYSLSYIMFINFKNRNMLHGHLIETIWTMMPAFTLIFIALPSLRLLYMLDDSNDAMITIKTIGRQWYWSYEYS 80
Cdd:MTH00139  32 IMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLYLMDEVSDPYLTFKAVGHQWYWSYEYS 111

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839881  81 DFINVEFDTYIHPEKELNQDSFRLLDVDNRTIVPMNSEVRMLTSASDVLHSWTMPALGIKVDAMPGRLNQ 150
Cdd:MTH00139 112 DFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPGRLNQ 181
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-153 1.28e-67

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 204.70  E-value: 1.28e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839881   1 IMITMIVGYSLSYIMFINFKNRNMLHGHLIETIWTMMPAFTLIFIALPSLRLLYMLDDSNDAMITIKTIGRQWYWSYEYS 80
Cdd:MTH00008  32 TLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLYLMDEVSNPSITLKTIGHQWYWSYEYS 111

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 970839881  81 DFINVEFDTYIHPEKELNQDSFRLLDVDNRTIVPMNSEVRMLTSASDVLHSWTMPALGIKVDAMPGRLNQGTF 153
Cdd:MTH00008 112 DFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGF 184
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-153 1.12e-66

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 202.24  E-value: 1.12e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839881   1 IMITMIVGYSLSYIMFINFKNRNMLHGHLIETIWTMMPAFTLIFIALPSLRLLYMLDDSNDAMITIKTIGRQWYWSYEYS 80
Cdd:MTH00038  32 TLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQLLYLMDEVNNPFLTIKAIGHQWYWSYEYT 111

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 970839881  81 DFINVEFDTYIHPEKELNQDSFRLLDVDNRTIVPMNSEVRMLTSASDVLHSWTMPALGIKVDAMPGRLNQGTF 153
Cdd:MTH00038 112 DYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTF 184
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-153 1.88e-66

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 201.36  E-value: 1.88e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839881   1 IMITMIVGYSLSYIMFINFKNRNMLHGHLIETIWTMMPAFTLIFIALPSLRLLYMLDDSNDAMITIKTIGRQWYWSYEYS 80
Cdd:MTH00168  32 VLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLYLMDEIDKPDLTIKAVGHQWYWSYEYT 111

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 970839881  81 DFINVEFDTYIHPEKELNQDSFRLLDVDNRTIVPMNSEVRMLTSASDVLHSWTMPALGIKVDAMPGRLNQGTF 153
Cdd:MTH00168 112 DYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGRLNQLAF 184
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-153 2.06e-63

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 193.84  E-value: 2.06e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839881   1 IMITMIVGYSLSYIMFINFKNRNMLHGHLIETIWTMMPAFTLIFIALPSLRLLYMLDDSNDAMITIKTIGRQWYWSYEYS 80
Cdd:MTH00076  32 FLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYLMDEINDPHLTVKAIGHQWYWSYEYT 111

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 970839881  81 DFINVEFDTYIHPEKELNQDSFRLLDVDNRTIVPMNSEVRMLTSASDVLHSWTMPALGIKVDAMPGRLNQGTF 153
Cdd:MTH00076 112 DYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSF 184
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 2-153 6.13e-61

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 187.62  E-value: 6.13e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839881   2 MITMIVGYSLSYIMFINFKNRNMLHGHLIETIWTMMPAFTLIFIALPSLRLLYMLDDSNDAMITIKTIGRQWYWSYEYSD 81
Cdd:MTH00098  33 LISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTD 112

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 970839881  82 FINVEFDTYIHPEKELNQDSFRLLDVDNRTIVPMNSEVRMLTSASDVLHSWTMPALGIKVDAMPGRLNQGTF 153
Cdd:MTH00098 113 YEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTL 184
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 2-153 1.92e-60

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 186.24  E-value: 1.92e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839881   2 MITMIVGYSLSYIMFINFKNRNMLHGHLIETIWTMMPAFTLIFIALPSLRLLYMLDDSNDAMITIKTIGRQWYWSYEYSD 81
Cdd:MTH00185  33 LISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTD 112

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 970839881  82 FINVEFDTYIHPEKELNQDSFRLLDVDNRTIVPMNSEVRMLTSASDVLHSWTMPALGIKVDAMPGRLNQGTF 153
Cdd:MTH00185 113 YEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQATF 184
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 2-153 4.29e-59

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 182.99  E-value: 4.29e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839881   2 MITMIVGYSLSYIMFINFKNRNMLHGHLIETIWTMMPAFTLIFIALPSLRLLYMLDDSNDAMITIKTIGRQWYWSYEYSD 81
Cdd:MTH00129  33 LISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTD 112

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 970839881  82 FINVEFDTYIHPEKELNQDSFRLLDVDNRTIVPMNSEVRMLTSASDVLHSWTMPALGIKVDAMPGRLNQGTF 153
Cdd:MTH00129 113 YEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQTAF 184
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 1-153 4.79e-58

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 180.72  E-value: 4.79e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839881   1 IMITMIVGYSLSYIMFINFKNRNMLHGHLIETIWTMMPAFTLIFIALPSLRLLYMLDDSNDAMITIKTIGRQWYWSYEYS 80
Cdd:MTH00023  41 IIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYS 120

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 970839881  81 DFI--NVEFDTYIHPEKELNQDSFRLLDVDNRTIVPMNSEVRMLTSASDVLHSWTMPALGIKVDAMPGRLNQGTF 153
Cdd:MTH00023 121 DYEgeTLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGF 195
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 1-153 5.30e-55

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 172.66  E-value: 5.30e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839881   1 IMITMIVGYSLSYIMFINFKNRNMLHGHLIETIWTMMPAFTLIFIALPSLRLLYMLDDSNDAMITIKTIGRQWYWSYEYS 80
Cdd:MTH00051  34 TIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYS 113

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 970839881  81 DF--INVEFDTYIHPEKELNQDSFRLLDVDNRTIVPMNSEVRMLTSASDVLHSWTMPALGIKVDAMPGRLNQGTF 153
Cdd:MTH00051 114 DYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSF 188
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 64-153 2.81e-53

C-terminal domain of Cytochrome c Oxidase subunit II; 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. It 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. 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 II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 164.67  E-value: 2.81e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839881  64 ITIKTIGRQWYWSYEYSDFINVEFDTYIHPEKELNQDSFRLLDVDNRTIVPMNSEVRMLTSASDVLHSWTMPALGIKVDA 143
Cdd:cd13912    3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                         90
                 ....*....|
gi 970839881 144 MPGRLNQGTF 153
Cdd:cd13912   83 VPGRLNQTSF 92
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
64-153 2.67e-49

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 154.49  E-value: 2.67e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839881   64 ITIKTIGRQWYWSYEYSDFINVEFDTYIHPEKELNQDSFRLLDVDNRTIVPMNSEVRMLTSASDVLHSWTMPALGIKVDA 143
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90
                  ....*....|
gi 970839881  144 MPGRLNQGTF 153
Cdd:pfam00116  81 VPGRLNQTSF 90
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 2-153 5.49e-47

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 153.26  E-value: 5.49e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839881   2 MITMIVGYSLSYIMFINFKNR------NMLHGHLIETIWTMMPAFTLIFIALPSLRLLYMLDDSN-DAMITIKTIGRQWY 74
Cdd:MTH00027  58 ILTIIVGVVLWLIIRILLGNNyysyywNKLDGSLIEVIWTLIPAFILILIAFPSLRLLYIMDECGfSANITIKVTGHQWY 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839881  75 WSYEYSDF--INVEFDTYIHPEKELNQDSFRLLDVDNRTIVPMNSEVRMLTSASDVLHSWTMPALGIKVDAMPGRLNQGT 152
Cdd:MTH00027 138 WSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRINETG 217


                 .
gi 970839881 153 F 153
Cdd:MTH00027 218 F 218
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 3-149 5.43e-43

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 142.07  E-value: 5.43e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839881   3 ITMIVGYSLSYIMFINFK-NRNMLHGHLIETIWTMMPAFTLIFIALPSLRLLYMLDDSN-DAMITIKTIGRQWYWSYEYS 80
Cdd:MTH00080  35 VLAFVVFLFLYLISNNFYfKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNlDSNLTVKVTGHQWYWSYEFS 114

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 970839881  81 DFINVEFDTYIHPEKELNQDSFRLLDVDNRTIVPMNSEVRMLTSASDVLHSWTMPALGIKVDAMPGRLN 149
Cdd:MTH00080 115 DIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILS 183
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
26-150 3.27e-28

Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 103.75  E-value: 3.27e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839881  26 HGHLIETIWTMMPAFTLIFIALPSLRLLYMLDDSNDAMITIKTIGRQWYWSYEYsdfinvefdtyihpekeLNQDSfrll 105
Cdd:COG1622   75 HNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY-----------------PDQGI---- 133

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 970839881 106 DVDNRTIVPMNSEVRMLTSASDVLHSWTMPALGIKVDAMPGRLNQ 150
Cdd:COG1622  134 ATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTE 178
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 12-150 8.24e-24

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 91.55  E-value: 8.24e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839881  12 SYIMFINFKNRNmlhgHLIETIWTMMPafTLIFIALPSLRLLYMLDDSNDAMI-TIKTIGRQWYWSYEYSDfiNVEFDTY 90
Cdd:MTH00047  35 SGNGSVNFGSEN----QVLELLWTVVP--TLLVLVLCFLNLNFITSDLDCFSSeTIKVIGHQWYWSYEYSF--GGSYDSF 106

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839881  91 ihpekeLNQDSFrllDVDNRTIVPMNSEVRMLTSASDVLHSWTMPALGIKVDAMPGRLNQ 150
Cdd:MTH00047 107 ------MTDDIF---GVDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINH 157
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 1-153 9.33e-22

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 86.28  E-value: 9.33e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839881    1 IMITMIVgyslsYIMFINFKNRN--------MLHGH-LIETIWTMMPA-FTLIFIALPSLRLLYMLDDSNDAMITIKTIG 70
Cdd:TIGR02866  23 ISLLVAA-----LLAYVVWKFRRkgdeekpsQIHGNrRLEYVWTVIPLiIVVGLFAATAKGLLYLERPIPKDALKVKVTG 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839881   71 RQWYWSYEYSDFinvefdtyihpekelnqdsfrLLDVDNRTIVPMNSEVRMLTSASDVLHSWTMPALGIKVDAMPGRLNQ 150
Cdd:TIGR02866  98 YQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNA 156


                  ...
gi 970839881  151 GTF 153
Cdd:TIGR02866 157 LWF 159
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 103-148 2.86e-15

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 68.69  E-value: 2.86e-15
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 970839881 103 RLLDVDNRTIVPMNSEVRMLTSASDVLHSWTMPALGIKVDAMPGRL 148
Cdd:PTZ00047  67 RQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRL 112
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 64-153 3.76e-13

Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259911 [Multi-domain]  Cd Length: 95  Bit Score: 61.16  E-value: 3.76e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839881  64 ITIKTIGRQWYWSYEYSDfinvefdtyihpekelnqdsfrlLDVDNRTIVPMNSEVRMLTSASDVLHSWTMPALGIKVDA 143
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                         90
                 ....*....|
gi 970839881 144 MPGRLNQGTF 153
Cdd:cd13842   58 VPGYTSELWF 67
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 64-153 8.32e-12

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 58.02  E-value: 8.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839881  64 ITIKTIGRQWYWSYEYSDfinvefdtyihPEKElnqdsfrlldvDNRTIVPMNSEVRMLTSASDVLHSWTMPALGIKVDA 143
Cdd:cd13915    2 LEIQVTGRQWMWEFTYPN-----------GKRE-----------INELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                         90
                 ....*....|
gi 970839881 144 MPGRLNQGTF 153
Cdd:cd13915   60 VPGRYTYLWF 69
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 64-149 6.48e-10

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 53.18  E-value: 6.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839881  64 ITIKTIGRQWYWSYEYsdfinvefdtyihPEKELNQDsfrlldvdNRTIVPMNSEVRMLTSASDVLHSWTMPALGIKVDA 143
Cdd:cd13914    1 VEIEVEAYQWGWEFSY-------------PEANVTTS--------EQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDA 59


                 ....*.
gi 970839881 144 MPGRLN 149
Cdd:cd13914   60 FPGQYN 65
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 64-149 6.75e-10

The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of most bacteria, is a multi-chain transmembrane protein located in the inner membrane the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. Caa3 type of CcO Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the cytochromes a, a3 and CuB active site in subunit I.


Pssm-ID: 259875 [Multi-domain]  Cd Length: 103  Bit Score: 53.01  E-value: 6.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839881  64 ITIKTIGRQWYWSYEYSDFINVEFDTyihpekelnqdsfrlldvDNRTIVPMNSEVRMLTSASDVLHSWTMPALGIKVDA 143
Cdd:cd04213    2 LTIEVTGHQWWWEFRYPDEPGRGIVT------------------ANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63


                 ....*.
gi 970839881 144 MPGRLN 149
Cdd:cd04213   64 IPGRTN 69
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 64-150 3.32e-09

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 51.49  E-value: 3.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839881  64 ITIKTIGRQWYWSYEYSDFinvefDTYIHPEKELNQDSFRLldvdnrtivPMNSEVRMLTSASDVLHSWTMPALGIKVDA 143
Cdd:cd13919    2 LVVEVTAQQWAWTFRYPGG-----DGKLGTDDDVTSPELHL---------PVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67


                 ....*..
gi 970839881 144 MPGRLNQ 150
Cdd:cd13919   68 VPGRTTR 74
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-52 8.96e-09

Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C oxidase contains two transmembrane alpha-helices.


Pssm-ID: 397083 [Multi-domain]  Cd Length: 89  Bit Score: 49.64  E-value: 8.96e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 970839881    1 IMITMIVGYSLSYIM--FINFKN----RNMLHGHLIETIWTMMPAFTLIFIALPSLRL 52
Cdd:pfam02790  32 TLILILVLYILVTCLirFNRRKNpitaRYTTHGQTIEIIWTIIPAVILILIALPSFKL 89
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 52-153 2.56e-04

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 38.98  E-value: 2.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839881  52 LLYMLD---DSNDAMITIKTIGRQWYWSYEYSDFINVEfdtyihpekelnqdsfrlldvdNRTIVPMNSEVRMLTSASDV 128
Cdd:cd13918   18 LLYVEDppdEADEDALEVEVEGFQFGWQFEYPNGVTTG----------------------NTLRVPADTPIALRVTSTDV 75

                         90       100
                 ....*....|....*....|....*
gi 970839881 129 LHSWTMPALGIKVDAMPGRLNQGTF 153
Cdd:cd13918   76 FHTFGIPELRVKADAIPGEYTSTWF 100
 
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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