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Conserved domains on  [gi|1213499690|gb|ASG92056|]
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cytochrome oxidase subunit II, partial (mitochondrion) [Sphenarium adelinae]

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
 1-154 5.39e-95

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 273.63  E-value: 5.39e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499690   1 IMITIIVGYSLNYIMLIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNDTLITIKSIGRQWYWSYEYS 80
Cdd:MTH00154   32 IMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYS 111

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1213499690  81 DFINIEFDAYML-TEEEQKNNFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSM 154
Cdd:MTH00154  112 DFKNIEFDSYMIpTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLI 186
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-154 5.39e-95

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 273.63  E-value: 5.39e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499690   1 IMITIIVGYSLNYIMLIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNDTLITIKSIGRQWYWSYEYS 80
Cdd:MTH00154   32 IMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYS 111

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1213499690  81 DFINIEFDAYML-TEEEQKNNFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSM 154
Cdd:MTH00154  112 DFKNIEFDSYMIpTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLI 186
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 64-154 1.14e-54

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: 168.13  E-value: 1.14e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499690  64 ITIKSIGRQWYWSYEYSDFINIEFDAYMLTEEE-QKNNFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDA 142
Cdd:cd13912     3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDlEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                          90
                  ....*....|..
gi 1213499690 143 TPGRLNQSTFSM 154
Cdd:cd13912    83 VPGRLNQTSFFI 94
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
64-153 3.02e-49

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 154.10  E-value: 3.02e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499690  64 ITIKSIGRQWYWSYEYSDFINIEFDAYMLTEEE-QKNNFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDA 142
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDlEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90
                  ....*....|.
gi 1213499690 143 TPGRLNQSTFS 153
Cdd:pfam00116  81 VPGRLNQTSFS 91
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
26-152 1.20e-26

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 99.90  E-value: 1.20e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499690  26 HGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNDTLITIKSIGRQWYWSYEYsdfiniefdaymlteEEQKNnfrllD 105
Cdd:COG1622    75 HNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY---------------PDQGI-----A 134

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1213499690 106 VDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTF 152
Cdd:COG1622   135 TVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWF 181
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 1-152 1.43e-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: 88.59  E-value: 1.43e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499690   1 IMITIIVGYSLNYIMLiKFKNRN------MLHGH-LIETIWTMIPA-ITLIFIALPSLRLLYMLDDSNDTLITIKSIGRQ 72
Cdd:TIGR02866  21 TLISLLVAALLAYVVW-KFRRKGdeekpsQIHGNrRLEYVWTVIPLiIVVGLFAATAKGLLYLERPIPKDALKVKVTGYQ 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499690  73 WYWSYEYSDFiniefdaymlteeeqknnfrLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTF 152
Cdd:TIGR02866 100 WWWDFEYPES--------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWF 159
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-154 5.39e-95

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 273.63  E-value: 5.39e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499690   1 IMITIIVGYSLNYIMLIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNDTLITIKSIGRQWYWSYEYS 80
Cdd:MTH00154   32 IMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYS 111

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1213499690  81 DFINIEFDAYML-TEEEQKNNFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSM 154
Cdd:MTH00154  112 DFKNIEFDSYMIpTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLI 186
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-152 2.66e-72

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 216.34  E-value: 2.66e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499690   1 IMITIIVGYSLNYIMLIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNDTLITIKSIGRQWYWSYEYS 80
Cdd:MTH00140   32 VLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYLLDETNNPLLTVKAIGHQWYWSYEYS 111

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1213499690  81 DFINIEFDAYMLTEEEQKN-NFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTF 152
Cdd:MTH00140  112 DFSVIEFDSYMVPENELELgDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSF 184
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-153 1.20e-71

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 214.78  E-value: 1.20e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499690   1 IMITIIVGYSLNYIMLIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNDTLITIKSIGRQWYWSYEYS 80
Cdd:MTH00117   32 LLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYLMDEINNPHLTIKAIGHQWYWSYEYT 111

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1213499690  81 DFINIEFDAYML-TEEEQKNNFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFS 153
Cdd:MTH00117  112 DYKDLSFDSYMIpTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFI 185
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-154 1.99e-70

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 211.50  E-value: 1.99e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499690   1 IMITIIVGYSLNYIMLIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNDTLITIKSIGRQWYWSYEYS 80
Cdd:MTH00139   32 IMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLYLMDEVSDPYLTFKAVGHQWYWSYEYS 111

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1213499690  81 DFINIEFDAYMLTEEE-QKNNFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSM 154
Cdd:MTH00139  112 DFKNLSFDSYMIPTEDlSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPGRLNQVGFFI 186
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-153 1.75e-68

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 206.76  E-value: 1.75e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499690   1 IMITIIVGYSLNYIMLIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNDTLITIKSIGRQWYWSYEYS 80
Cdd:MTH00168   32 VLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLYLMDEIDKPDLTIKAVGHQWYWSYEYT 111

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1213499690  81 DFINIEFDAYML-TEEEQKNNFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFS 153
Cdd:MTH00168  112 DYNDLEFDSYMVpTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGRLNQLAFL 185
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-153 6.87e-67

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 202.78  E-value: 6.87e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499690   1 IMITIIVGYSLNYIMLIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNDTLITIKSIGRQWYWSYEYS 80
Cdd:MTH00008   32 TLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLYLMDEVSNPSITLKTIGHQWYWSYEYS 111

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1213499690  81 DFINIEFDAYML-TEEEQKNNFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFS 153
Cdd:MTH00008  112 DFSNLEFDSYMLpTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFT 185
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-152 8.89e-67

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 202.62  E-value: 8.89e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499690   1 IMITIIVGYSLNYIMLIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNDTLITIKSIGRQWYWSYEYS 80
Cdd:MTH00038   32 TLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQLLYLMDEVNNPFLTIKAIGHQWYWSYEYT 111

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1213499690  81 DFINIEFDAYML-TEEEQKNNFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTF 152
Cdd:MTH00038  112 DYNDLEFDSYMVpTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTF 184
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-152 1.89e-60

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 186.52  E-value: 1.89e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499690   1 IMITIIVGYSLNYIMLIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNDTLITIKSIGRQWYWSYEYS 80
Cdd:MTH00076   32 FLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYLMDEINDPHLTVKAIGHQWYWSYEYT 111

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1213499690  81 DFINIEFDAYML-TEEEQKNNFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTF 152
Cdd:MTH00076  112 DYEDLSFDSYMIpTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSF 184
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 2-152 5.81e-60

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 185.30  E-value: 5.81e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499690   2 MITIIVGYSLNYIMLIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNDTLITIKSIGRQWYWSYEYSD 81
Cdd:MTH00129   33 LISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTD 112

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1213499690  82 FINIEFDAYML-TEEEQKNNFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTF 152
Cdd:MTH00129  113 YEDLGFDSYMIpTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQTAF 184
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 2-152 6.27e-60

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 185.09  E-value: 6.27e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499690   2 MITIIVGYSLNYIMLIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNDTLITIKSIGRQWYWSYEYSD 81
Cdd:MTH00185   33 LISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTD 112

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1213499690  82 FINIEFDAYML-TEEEQKNNFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTF 152
Cdd:MTH00185  113 YEQLEFDSYMTpTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQATF 184
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 2-152 8.63e-60

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 184.54  E-value: 8.63e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499690   2 MITIIVGYSLNYIMLIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNDTLITIKSIGRQWYWSYEYSD 81
Cdd:MTH00098   33 LISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTD 112

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1213499690  82 FINIEFDAYML-TEEEQKNNFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTF 152
Cdd:MTH00098  113 YEDLSFDSYMIpTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTL 184
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 1-152 2.22e-58

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 181.49  E-value: 2.22e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499690   1 IMITIIVGYSLNYIMLIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNDTLITIKSIGRQWYWSYEYS 80
Cdd:MTH00023   41 IIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYS 120

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1213499690  81 DFI--NIEFDAYML-TEEEQKNNFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTF 152
Cdd:MTH00023  121 DYEgeTLEFDSYMVpTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGF 195
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 1-152 2.67e-56

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 176.12  E-value: 2.67e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499690   1 IMITIIVGYSLNYIMLIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNDTLITIKSIGRQWYWSYEYS 80
Cdd:MTH00051   34 TIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYS 113

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1213499690  81 DF--INIEFDAYML-TEEEQKNNFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTF 152
Cdd:MTH00051  114 DYgtDTIEFDSYMIpTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSF 188
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 64-154 1.14e-54

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: 168.13  E-value: 1.14e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499690  64 ITIKSIGRQWYWSYEYSDFINIEFDAYMLTEEE-QKNNFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDA 142
Cdd:cd13912     3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDlEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                          90
                  ....*....|..
gi 1213499690 143 TPGRLNQSTFSM 154
Cdd:cd13912    83 VPGRLNQTSFFI 94
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
64-153 3.02e-49

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 154.10  E-value: 3.02e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499690  64 ITIKSIGRQWYWSYEYSDFINIEFDAYMLTEEE-QKNNFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDA 142
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDlEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90
                  ....*....|.
gi 1213499690 143 TPGRLNQSTFS 153
Cdd:pfam00116  81 VPGRLNQTSFS 91
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 2-152 7.11e-45

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 147.86  E-value: 7.11e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499690   2 MITIIVGYSLNYIMLIKFKNR------NMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNDTL-ITIKSIGRQWY 74
Cdd:MTH00027   58 ILTIIVGVVLWLIIRILLGNNyysyywNKLDGSLIEVIWTLIPAFILILIAFPSLRLLYIMDECGFSAnITIKVTGHQWY 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499690  75 WSYEYSDF--INIEFDAYML-TEEEQKNNFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQST 151
Cdd:MTH00027  138 WSYSYEDYgeKNIEFDSYMIpTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRINETG 217


                  .
gi 1213499690 152 F 152
Cdd:MTH00027  218 F 218
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 13-153 1.03e-41

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 138.60  E-value: 1.03e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499690  13 YIMLIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSN-DTLITIKSIGRQWYWSYEYSDFINIEFDAYM 91
Cdd:MTH00080   46 LISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNlDSNLTVKVTGHQWYWSYEFSDIPGLEFDSYM 125

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1213499690  92 -LTEEEQKNNFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFS 153
Cdd:MTH00080  126 kSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTLCYS 188
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
26-152 1.20e-26

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 99.90  E-value: 1.20e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499690  26 HGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNDTLITIKSIGRQWYWSYEYsdfiniefdaymlteEEQKNnfrllD 105
Cdd:COG1622    75 HNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY---------------PDQGI-----A 134

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1213499690 106 VDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTF 152
Cdd:COG1622   135 TVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWF 181
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 1-154 1.43e-25

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 96.18  E-value: 1.43e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499690   1 IMITIIVGYSL-NYIMLIKFKNRNmlhgHLIETIWTMIPaiTLIFIALPSLRLLYMLDDSND-TLITIKSIGRQWYWSYE 78
Cdd:MTH00047   23 CWVYIMLCWQVvSGNGSVNFGSEN----QVLELLWTVVP--TLLVLVLCFLNLNFITSDLDCfSSETIKVIGHQWYWSYE 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1213499690  79 YSDfiNIEFDAYMlteeeqkNNFRLLdVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSM 154
Cdd:MTH00047   97 YSF--GGSYDSFM-------TDDIFG-VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCP 162
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 1-152 1.43e-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: 88.59  E-value: 1.43e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499690   1 IMITIIVGYSLNYIMLiKFKNRN------MLHGH-LIETIWTMIPA-ITLIFIALPSLRLLYMLDDSNDTLITIKSIGRQ 72
Cdd:TIGR02866  21 TLISLLVAALLAYVVW-KFRRKGdeekpsQIHGNrRLEYVWTVIPLiIVVGLFAATAKGLLYLERPIPKDALKVKVTGYQ 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499690  73 WYWSYEYSDFiniefdaymlteeeqknnfrLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTF 152
Cdd:TIGR02866 100 WWWDFEYPES--------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWF 159
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 87-152 3.55e-18

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 76.01  E-value: 3.55e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1213499690  87 FDAYMLTEEE-QKNNFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQ-STF 152
Cdd:PTZ00047   51 FQSNLVTDEDlKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKiNTF 118
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 64-152 2.35e-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: 59.18  E-value: 2.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499690  64 ITIKSIGRQWYWSYEYsdfiniefdaymlteeeqKNNFRlldVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDAT 143
Cdd:cd13915     2 LEIQVTGRQWMWEFTY------------------PNGKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVV 60


                  ....*....
gi 1213499690 144 PGRLNQSTF 152
Cdd:cd13915    61 PGRYTYLWF 69
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 64-152 6.52e-12

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: 58.08  E-value: 6.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499690  64 ITIKSIGRQWYWSYEYSDfiniefdaymlteeeqknnfrlLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDAT 143
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDAV 58


                  ....*....
gi 1213499690 144 PGRLNQSTF 152
Cdd:cd13842    59 PGYTSELWF 67
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 64-152 3.63e-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: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 53.80  E-value: 3.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499690  64 ITIKSIGRQWYWSYEYSDfiniefdaymlteEEQKNNFRLLDVDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDAT 143
Cdd:cd13919     2 LVVEVTAQQWAWTFRYPG-------------GDGKLGTDDDVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAV 68


                  ....*....
gi 1213499690 144 PGRLNQSTF 152
Cdd:cd13919    69 PGRTTRLWF 77
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-52 6.05e-10

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: 52.72  E-value: 6.05e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1213499690   1 IMITIIVGYSLnYIMLIKFK-------NRNMLHGHLIETIWTMIPAITLIFIALPSLRL 52
Cdd:pfam02790  32 TLILILVLYIL-VTCLIRFNrrknpitARYTTHGQTIEIIWTIIPAVILILIALPSFKL 89
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 64-148 2.14e-08

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: 49.16  E-value: 2.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499690  64 ITIKSIGRQWYWSYEYsdfiniefdaymltEEEQKNNFRLLdvdNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDAT 143
Cdd:cd04213     2 LTIEVTGHQWWWEFRY--------------PDEPGRGIVTA---NELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMI 64


                  ....*
gi 1213499690 144 PGRLN 148
Cdd:cd04213    65 PGRTN 69
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 64-148 2.88e-08

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: 48.94  E-value: 2.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499690  64 ITIKSIGRQWYWSYEYSDfiniefdaymlteeeqKNNFRlldvDNRTLVPMNSEIRMLTSASDVLHSWTIPSMGIKVDAT 143
Cdd:cd13914     1 VEIEVEAYQWGWEFSYPE----------------ANVTT----SEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAF 60


                  ....*
gi 1213499690 144 PGRLN 148
Cdd:cd13914    61 PGQYN 65
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 52-152 2.16e-06

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: 44.37  E-value: 2.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213499690  52 LLYMLD---DSNDTLITIKSIGRQWYWSYEYSDfiniefdaymltEEEQKNNFRlldvdnrtlVPMNSEIRMLTSASDVL 128
Cdd:cd13918    18 LLYVEDppdEADEDALEVEVEGFQFGWQFEYPN------------GVTTGNTLR---------VPADTPIALRVTSTDVF 76

                          90       100
                  ....*....|....*....|....
gi 1213499690 129 HSWTIPSMGIKVDATPGRLNQSTF 152
Cdd:cd13918    77 HTFGIPELRVKADAIPGEYTSTWF 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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