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Conserved domains on  [gi|1063639071|gb|AOO35127|]
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cytochrome oxidase subunit II, partial (mitochondrion) [Stethophyma grossum]

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
 1-171 5.52e-102

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 292.12  E-value: 5.52e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071   1 QLSFFHDHTMIVLILITTVVGYSLTFMFLMNFTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMITIK 80
Cdd:MTH00154   19 QLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLK 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071  81 TIGRQWYWSYEYSDFMNVEFDTYMKPEKELEIESFRLLDVDNRMILPMNTEVRILTSASDVLHSWAIPALGIKIDATPGR 160
Cdd:MTH00154   99 TIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGR 178

                         170
                  ....*....|.
gi 1063639071 161 LNQGTFTINCP 171
Cdd:MTH00154  179 LNQLNFLINRP 189
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-171 5.52e-102

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 292.12  E-value: 5.52e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071   1 QLSFFHDHTMIVLILITTVVGYSLTFMFLMNFTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMITIK 80
Cdd:MTH00154   19 QLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLK 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071  81 TIGRQWYWSYEYSDFMNVEFDTYMKPEKELEIESFRLLDVDNRMILPMNTEVRILTSASDVLHSWAIPALGIKIDATPGR 160
Cdd:MTH00154   99 TIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGR 178

                         170
                  ....*....|.
gi 1063639071 161 LNQGTFTINCP 171
Cdd:MTH00154  179 LNQLNFLINRP 189
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 77-171 2.52e-60

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: 183.16  E-value: 2.52e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071  77 ITIKTIGRQWYWSYEYSDFMNVEFDTYMKPEKELEIESFRLLDVDNRMILPMNTEVRILTSASDVLHSWAIPALGIKIDA 156
Cdd:cd13912     3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                          90
                  ....*....|....*
gi 1063639071 157 TPGRLNQGTFTINCP 171
Cdd:cd13912    83 VPGRLNQTSFFIERP 97
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
77-171 2.25e-52

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 162.96  E-value: 2.25e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071  77 ITIKTIGRQWYWSYEYSDFMNVEFDTYMKPEKELEIESFRLLDVDNRMILPMNTEVRILTSASDVLHSWAIPALGIKIDA 156
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90
                  ....*....|....*
gi 1063639071 157 TPGRLNQGTFTINCP 171
Cdd:pfam00116  81 VPGRLNQTSFSIDRE 95
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
7-169 4.35e-28

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 104.14  E-value: 4.35e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071   7 DHTMIVLILITTVVG---YSLTFMFLMNFTNRN-------MLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSVDAM 76
Cdd:COG1622    33 DDLFWVSLIIMLVIFvlvFGLLLYFAIRYRRRKgdadpaqFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDP 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071  77 ITIKTIGRQWYWSYEYsdfmnvefdtymkPEKELEiesfrlldVDNRMILPMNTEVRILTSASDVLHSWAIPALGIKIDA 156
Cdd:COG1622   113 LTVEVTGYQWKWLFRY-------------PDQGIA--------TVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDA 171

                         170
                  ....*....|...
gi 1063639071 157 TPGRLNQGTFTIN 169
Cdd:COG1622   172 IPGRVTELWFTAD 184
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 1-171 3.43e-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: 88.21  E-value: 3.43e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071   1 QLSFFHDHTMIVLILITTVVgYSLTFMFLMNFTNRN------MLHGH-LIETIWTALPAI--TLIFIALPSLRLLYLLDD 71
Cdd:TIGR02866   8 QIAFLFLFVLAVSTLISLLV-AALLAYVVWKFRRKGdeekpsQIHGNrRLEYVWTVIPLIivVGLFAATAKGLLYLERPI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071  72 SVDAMiTIKTIGRQWYWSYEYSDFmnvefdtymkpekeleiesfrLLDVDNRMILPMNTEVRILTSASDVLHSWAIPALG 151
Cdd:TIGR02866  87 PKDAL-KVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELG 144

                         170       180
                  ....*....|....*....|
gi 1063639071 152 IKIDATPGRLNQGTFTINCP 171
Cdd:TIGR02866 145 GKIDAIPGQTNALWFNADEP 164
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-171 5.52e-102

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 292.12  E-value: 5.52e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071   1 QLSFFHDHTMIVLILITTVVGYSLTFMFLMNFTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMITIK 80
Cdd:MTH00154   19 QLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLK 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071  81 TIGRQWYWSYEYSDFMNVEFDTYMKPEKELEIESFRLLDVDNRMILPMNTEVRILTSASDVLHSWAIPALGIKIDATPGR 160
Cdd:MTH00154   99 TIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGR 178

                         170
                  ....*....|.
gi 1063639071 161 LNQGTFTINCP 171
Cdd:MTH00154  179 LNQLNFLINRP 189
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-171 5.26e-76

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 226.52  E-value: 5.26e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071   1 QLSFFHDHTMIVLILITTVVGYSLTFMFLMNFTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMITIK 80
Cdd:MTH00139   19 QLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLYLMDEVSDPYLTFK 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071  81 TIGRQWYWSYEYSDFMNVEFDTYMKPEKELEIESFRLLDVDNRMILPMNTEVRILTSASDVLHSWAIPALGIKIDATPGR 160
Cdd:MTH00139   99 AVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPGR 178

                         170
                  ....*....|.
gi 1063639071 161 LNQGTFTINCP 171
Cdd:MTH00139  179 LNQVGFFINRP 189
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-171 7.09e-76

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 226.36  E-value: 7.09e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071   1 QLSFFHDHTMIVLILITTVVGYSLTfMFLMN-FTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMITI 79
Cdd:MTH00140   19 ELIFFHDHAMVVLVLIFSFVMYMLV-LLLFNkFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYLLDETNNPLLTV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071  80 KTIGRQWYWSYEYSDFMNVEFDTYMKPEKELEIESFRLLDVDNRMILPMNTEVRILTSASDVLHSWAIPALGIKIDATPG 159
Cdd:MTH00140   98 KAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPG 177

                         170
                  ....*....|..
gi 1063639071 160 RLNQGTFTINCP 171
Cdd:MTH00140  178 RLNQLSFEPKRP 189
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-171 2.20e-75

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 224.79  E-value: 2.20e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071   1 QLSFFHDHTMIVLILITTVVGYSLTFMFLMNFTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMITIK 80
Cdd:MTH00117   19 ELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYLMDEINNPHLTIK 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071  81 TIGRQWYWSYEYSDFMNVEFDTYMKPEKELEIESFRLLDVDNRMILPMNTEVRILTSASDVLHSWAIPALGIKIDATPGR 160
Cdd:MTH00117   99 AIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGR 178

                         170
                  ....*....|.
gi 1063639071 161 LNQGTFTINCP 171
Cdd:MTH00117  179 LNQTSFITTRP 189
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-171 7.30e-73

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 218.57  E-value: 7.30e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071   1 QLSFFHDHTMIVLILITTVVGYSLTFMFLMNFTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMITIK 80
Cdd:MTH00008   19 QLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLYLMDEVSNPSITLK 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071  81 TIGRQWYWSYEYSDFMNVEFDTYMKPEKELEIESFRLLDVDNRMILPMNTEVRILTSASDVLHSWAIPALGIKIDATPGR 160
Cdd:MTH00008   99 TIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGR 178

                         170
                  ....*....|.
gi 1063639071 161 LNQGTFTINCP 171
Cdd:MTH00008  179 LNQIGFTITRP 189
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-166 3.64e-70

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 211.76  E-value: 3.64e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071   1 QLSFFHDHTMIVLILITTVVGYSLTFMFLMNFTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMITIK 80
Cdd:MTH00168   19 ELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLYLMDEIDKPDLTIK 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071  81 TIGRQWYWSYEYSDFMNVEFDTYMKPEKELEIESFRLLDVDNRMILPMNTEVRILTSASDVLHSWAIPALGIKIDATPGR 160
Cdd:MTH00168   99 AVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGR 178


                  ....*.
gi 1063639071 161 LNQGTF 166
Cdd:MTH00168  179 LNQLAF 184
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-169 6.94e-69

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 208.40  E-value: 6.94e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071   1 QLSFFHDHTMIVLILITTVVGYSLTFMFLMNFTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMITIK 80
Cdd:MTH00038   19 ELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQLLYLMDEVNNPFLTIK 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071  81 TIGRQWYWSYEYSDFMNVEFDTYMKPEKELEIESFRLLDVDNRMILPMNTEVRILTSASDVLHSWAIPALGIKIDATPGR 160
Cdd:MTH00038   99 AIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGR 178


                  ....*....
gi 1063639071 161 LNQGTFTIN 169
Cdd:MTH00038  179 LNQTTFFIS 187
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-171 2.07e-63

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 194.61  E-value: 2.07e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071   1 QLSFFHDHTMIVLILITTVVGYSLTFMFLMNFTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMITIK 80
Cdd:MTH00076   19 ELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYLMDEINDPHLTVK 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071  81 TIGRQWYWSYEYSDFMNVEFDTYMKPEKELEIESFRLLDVDNRMILPMNTEVRILTSASDVLHSWAIPALGIKIDATPGR 160
Cdd:MTH00076   99 AIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGR 178

                         170
                  ....*....|.
gi 1063639071 161 LNQGTFTINCP 171
Cdd:MTH00076  179 LNQTSFIASRP 189
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-171 6.37e-63

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 193.40  E-value: 6.37e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071   1 QLSFFHDHTMIVLILITTVVGYSLTFMFLMNFTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMITIK 80
Cdd:MTH00098   19 ELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEINNPSLTVK 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071  81 TIGRQWYWSYEYSDFMNVEFDTYMKPEKELEIESFRLLDVDNRMILPMNTEVRILTSASDVLHSWAIPALGIKIDATPGR 160
Cdd:MTH00098   99 TMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGR 178

                         170
                  ....*....|.
gi 1063639071 161 LNQGTFTINCP 171
Cdd:MTH00098  179 LNQTTLMSTRP 189
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-171 1.31e-62

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 192.79  E-value: 1.31e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071   1 QLSFFHDHTMIVLILITTVVGYSLTFMFLMNFTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMITIK 80
Cdd:MTH00185   19 ELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYLMDEINDPHLTIK 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071  81 TIGRQWYWSYEYSDFMNVEFDTYMKPEKELEIESFRLLDVDNRMILPMNTEVRILTSASDVLHSWAIPALGIKIDATPGR 160
Cdd:MTH00185   99 AMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGR 178

                         170
                  ....*....|.
gi 1063639071 161 LNQGTFTINCP 171
Cdd:MTH00185  179 LNQATFIISRP 189
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 1-171 2.56e-62

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 192.27  E-value: 2.56e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071   1 QLSFFHDHTMIVLILITTVVGYSLTFMFLMNFTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMITIK 80
Cdd:MTH00023   28 EIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMDEVVSPALTIK 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071  81 TIGRQWYWSYEYSDFM--NVEFDTYMKPEKELEIESFRLLDVDNRMILPMNTEVRILTSASDVLHSWAIPALGIKIDATP 158
Cdd:MTH00023  108 AIGHQWYWSYEYSDYEgeTLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVP 187

                         170
                  ....*....|...
gi 1063639071 159 GRLNQGTFTINCP 171
Cdd:MTH00023  188 GRLNQTGFFIKRP 200
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-171 3.87e-61

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 188.77  E-value: 3.87e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071   1 QLSFFHDHTMIVLILITTVVGYSLTFMFLMNFTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMITIK 80
Cdd:MTH00129   19 ELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMDEINDPHLTIK 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071  81 TIGRQWYWSYEYSDFMNVEFDTYMKPEKELEIESFRLLDVDNRMILPMNTEVRILTSASDVLHSWAIPALGIKIDATPGR 160
Cdd:MTH00129   99 AMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGR 178

                         170
                  ....*....|.
gi 1063639071 161 LNQGTFTINCP 171
Cdd:MTH00129  179 LNQTAFIASRP 189
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 77-171 2.52e-60

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: 183.16  E-value: 2.52e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071  77 ITIKTIGRQWYWSYEYSDFMNVEFDTYMKPEKELEIESFRLLDVDNRMILPMNTEVRILTSASDVLHSWAIPALGIKIDA 156
Cdd:cd13912     3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                          90
                  ....*....|....*
gi 1063639071 157 TPGRLNQGTFTINCP 171
Cdd:cd13912    83 VPGRLNQTSFFIERP 97
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 1-171 5.82e-59

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 183.44  E-value: 5.82e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071   1 QLSFFHDHTMIVLILITTVVGYSLTFMFLMNFTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMITIK 80
Cdd:MTH00051   21 EIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMDEVIDPALTIK 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071  81 TIGRQWYWSYEYSDF--MNVEFDTYMKPEKELEIESFRLLDVDNRMILPMNTEVRILTSASDVLHSWAIPALGIKIDATP 158
Cdd:MTH00051  101 AIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVP 180

                         170
                  ....*....|...
gi 1063639071 159 GRLNQGTFTINCP 171
Cdd:MTH00051  181 GRLNQTSFFIKRP 193
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
77-171 2.25e-52

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 162.96  E-value: 2.25e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071  77 ITIKTIGRQWYWSYEYSDFMNVEFDTYMKPEKELEIESFRLLDVDNRMILPMNTEVRILTSASDVLHSWAIPALGIKIDA 156
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90
                  ....*....|....*
gi 1063639071 157 TPGRLNQGTFTINCP 171
Cdd:pfam00116  81 VPGRLNQTSFSIDRE 95
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 1-171 1.44e-43

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 145.17  E-value: 1.44e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071   1 QLSFFHDHTMIVLILITTVVGYSLTFMFLMNFTNR---NMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSV-DAM 76
Cdd:MTH00027   47 EIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSyywNKLDGSLIEVIWTLIPAFILILIAFPSLRLLYIMDECGfSAN 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071  77 ITIKTIGRQWYWSYEYSDF--MNVEFDTYMKPEKELEIESFRLLDVDNRMILPMNTEVRILTSASDVLHSWAIPALGIKI 154
Cdd:MTH00027  127 ITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKM 206

                         170
                  ....*....|....*..
gi 1063639071 155 DATPGRLNQGTFTINCP 171
Cdd:MTH00027  207 DAVPGRINETGFLIKRP 223
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 5-171 2.01e-43

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 143.61  E-value: 2.01e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071   5 FHDHTM-IVLILITTVVGYSLTFMFLMNFTNrNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLD-DSVDAMITIKTI 82
Cdd:MTH00080   25 FNCSLLfGEFVLAFVVFLFLYLISNNFYFKS-KKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGlMNLDSNLTVKVT 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071  83 GRQWYWSYEYSDFMNVEFDTYMKPEKELEIESFRLLDVDNRMILPMNTEVRILTSASDVLHSWAIPALGIKIDATPGRLN 162
Cdd:MTH00080  104 GHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILS 183


                  ....*....
gi 1063639071 163 QGTFTINCP 171
Cdd:MTH00080  184 TLCYSFPMP 192
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
7-169 4.35e-28

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 104.14  E-value: 4.35e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071   7 DHTMIVLILITTVVG---YSLTFMFLMNFTNRN-------MLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSVDAM 76
Cdd:COG1622    33 DDLFWVSLIIMLVIFvlvFGLLLYFAIRYRRRKgdadpaqFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDP 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071  77 ITIKTIGRQWYWSYEYsdfmnvefdtymkPEKELEiesfrlldVDNRMILPMNTEVRILTSASDVLHSWAIPALGIKIDA 156
Cdd:COG1622   113 LTVEVTGYQWKWLFRY-------------PDQGIA--------TVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDA 171

                         170
                  ....*....|...
gi 1063639071 157 TPGRLNQGTFTIN 169
Cdd:COG1622   172 IPGRVTELWFTAD 184
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 1-171 3.43e-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: 88.21  E-value: 3.43e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071   1 QLSFFHDHTMIVLILITTVVgYSLTFMFLMNFTNRN------MLHGH-LIETIWTALPAI--TLIFIALPSLRLLYLLDD 71
Cdd:TIGR02866   8 QIAFLFLFVLAVSTLISLLV-AALLAYVVWKFRRKGdeekpsQIHGNrRLEYVWTVIPLIivVGLFAATAKGLLYLERPI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071  72 SVDAMiTIKTIGRQWYWSYEYSDFmnvefdtymkpekeleiesfrLLDVDNRMILPMNTEVRILTSASDVLHSWAIPALG 151
Cdd:TIGR02866  87 PKDAL-KVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELG 144

                         170       180
                  ....*....|....*....|
gi 1063639071 152 IKIDATPGRLNQGTFTINCP 171
Cdd:TIGR02866 145 GKIDAIPGQTNALWFNADEP 164
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 42-163 4.35e-22

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 87.70  E-value: 4.35e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071  42 LIETIWTALPaiTLIFIALPSLRLLYLLDDSVDAMI-TIKTIGRQWYWSYEYSDfmNVEFDTYMkpekeleieSFRLLDV 120
Cdd:MTH00047   48 VLELLWTVVP--TLLVLVLCFLNLNFITSDLDCFSSeTIKVIGHQWYWSYEYSF--GGSYDSFM---------TDDIFGV 114

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1063639071 121 DNRMILPMNTEVRILTSASDVLHSWAIPALGIKIDATPGRLNQ 163
Cdd:MTH00047  115 DKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINH 157
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 100-161 4.28e-18

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 76.40  E-value: 4.28e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063639071 100 FDTYMKPEKELEIESFRLLDVDNRMILPMNTEVRILTSASDVLHSWAIPALGIKIDATPGRL 161
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRL 112
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 77-171 7.58e-15

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: 66.17  E-value: 7.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071  77 ITIKTIGRQWYWSYEYSDfmnvefdtymkpekeleiesfrlLDVDNRMILPMNTEVRILTSASDVLHSWAIPALGIKIDA 156
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90
                  ....*....|....*
gi 1063639071 157 TPGRLNQGTFTINCP 171
Cdd:cd13842    58 VPGYTSELWFVADKP 72
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 77-169 1.62e-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: 60.34  E-value: 1.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071  77 ITIKTIGRQWYWSYEYsdfmnvefdtymkPEKELEIesfrlldvdNRMILPMNTEVRILTSASDVLHSWAIPALGIKIDA 156
Cdd:cd13915     2 LEIQVTGRQWMWEFTY-------------PNGKREI---------NELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                          90
                  ....*....|...
gi 1063639071 157 TPGRLNQGTFTIN 169
Cdd:cd13915    60 VPGRYTYLWFEAT 72
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 77-162 4.83e-12

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: 59.17  E-value: 4.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071  77 ITIKTIGRQWYWSYEYSDFMNVEFDTymkpekeleiesfrlldvDNRMILPMNTEVRILTSASDVLHSWAIPALGIKIDA 156
Cdd:cd04213     2 LTIEVTGHQWWWEFRYPDEPGRGIVT------------------ANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63


                  ....*.
gi 1063639071 157 TPGRLN 162
Cdd:cd04213    64 IPGRTN 69
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-59 1.08e-11

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: 57.73  E-value: 1.08e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063639071   1 QLSFFHDHTMIVLILITTVVGYSLTFMfLMNF-------TNRNMLHGHLIETIWTALPAITLIFIA 59
Cdd:pfam02790  19 GLLELHDYIMFILTLILILVLYILVTC-LIRFnrrknpiTARYTTHGQTIEIIWTIIPAVILILIA 83
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 77-169 1.13e-11

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: 58.42  E-value: 1.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071  77 ITIKTIGRQWYWSYEYsdfmnvefdtymkpEKELEIESFRLLDVDNRMILPMNTEVRILTSASDVLHSWAIPALGIKIDA 156
Cdd:cd13919     2 LVVEVTAQQWAWTFRY--------------PGGDGKLGTDDDVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                          90
                  ....*....|...
gi 1063639071 157 TPGRLNQGTFTIN 169
Cdd:cd13919    68 VPGRTTRLWFTPT 80
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 77-170 5.22e-11

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: 56.65  E-value: 5.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071  77 ITIKTIGRQWYWSYEYSDfMNVefdtymkpekeleiesfrllDVDNRMILPMNTEVRILTSASDVLHSWAIPALGIKIDA 156
Cdd:cd13914     1 VEIEVEAYQWGWEFSYPE-ANV--------------------TTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDA 59

                          90       100
                  ....*....|....*....|..
gi 1063639071 157 TPGRLN--------QGTFTINC 170
Cdd:cd13914    60 FPGQYNtikteateEGEYQLYC 81
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 70-170 1.51e-07

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: 48.22  E-value: 1.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063639071  70 DDSVDAMITIKTIGRQWYWSYEYSDfmnvefdtymkpekelEIESFrlldvdNRMILPMNTEVRILTSASDVLHSWAIPA 149
Cdd:cd13918    26 DEADEDALEVEVEGFQFGWQFEYPN----------------GVTTG------NTLRVPADTPIALRVTSTDVFHTFGIPE 83

                          90       100
                  ....*....|....*....|....*....
gi 1063639071 150 LGIKIDATPGRLNQ--------GTFTINC 170
Cdd:cd13918    84 LRVKADAIPGEYTStwfeadepGTYEAKC 112
 
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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