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Conserved domains on  [gi|893665423|gb|AKQ95945|]
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cytochrome oxidase subunit 1, partial (mitochondrion) [Ichneumonidae sp. BOLD:AAH1870]

Protein Classification

heme-copper oxidase family protein( domain architecture ID 14)

heme-copper oxidase family protein may catalyze the transfer of electrons from an electron donor onto molecular oxygen

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Heme_Cu_Oxidase_I super family cl00275
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-212 1.68e-116

Heme-copper oxidase subunit I. 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 three to five in bacteria and up to 13 in mammalian mitochondria. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. Membership in the superfamily is defined by subunit I, which contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons to the binuclear center. Only subunit I is common to the entire superfamily. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from the electron donor on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I of cytochrome c oxidase (CcO) and ubiquinol oxidase. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electron transfer occurs in two segments: from the electron donor to the low-spin heme, and from the low-spin heme to the binuclear center. The first segment can be a multi-step process and varies among the different families, while the second segment, a direct transfer, is consistent throughout the superfamily.


The actual alignment was detected with superfamily member MTH00153:

Pssm-ID: 469701  Cd Length: 511  Bit Score: 341.08  E-value: 1.68e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423   1 MWAGMIGTSMSMIIRMELSKPGIFINNDQIYNSMITSHAFIMIFFMIMPLMIGGFGNWLIPLMMGAPDMAFPRMNNMSFW 80
Cdd:MTH00153  22 AWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423  81 LLPPSLILLIYSNLINQGIGTGWTIYPPLSLNLNHEGMSIDLSIFSLHLAGSSSIMGAINFITTIMNMMSKKIKLEQLTL 160
Cdd:MTH00153 102 LLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPL 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 893665423 161 FTWSIFITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 212
Cdd:MTH00153 182 FVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-212 1.68e-116

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 341.08  E-value: 1.68e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423   1 MWAGMIGTSMSMIIRMELSKPGIFINNDQIYNSMITSHAFIMIFFMIMPLMIGGFGNWLIPLMMGAPDMAFPRMNNMSFW 80
Cdd:MTH00153  22 AWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423  81 LLPPSLILLIYSNLINQGIGTGWTIYPPLSLNLNHEGMSIDLSIFSLHLAGSSSIMGAINFITTIMNMMSKKIKLEQLTL 160
Cdd:MTH00153 102 LLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPL 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 893665423 161 FTWSIFITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 212
Cdd:MTH00153 182 FVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-212 1.51e-112

Cytochrome C oxidase subunit I. 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, but subunit III, which is also conserved, may play a role in assembly or oxygen delivery to the active site. 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 I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center.


Pssm-ID: 238833  Cd Length: 488  Bit Score: 330.21  E-value: 1.51e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423   1 MWAGMIGTSMSMIIRMELSKPGIFINNDQIYNSMITSHAFIMIFFMIMPLMIGGFGNWLIPLMMGAPDMAFPRMNNMSFW 80
Cdd:cd01663   15 LWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFW 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423  81 LLPPSLILLIYSNLINQGIGTGWTIYPPLSLNLNHEGMSIDLSIFSLHLAGSSSIMGAINFITTIMNMMSKKIKLEQLTL 160
Cdd:cd01663   95 LLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPL 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 893665423 161 FTWSIFITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 212
Cdd:cd01663  175 FVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
3-212 6.17e-61

Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];


Pssm-ID: 440605  Cd Length: 535  Bit Score: 198.43  E-value: 6.17e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423   3 AGMIGTSMSMIIRMELSKPGI-FINNDQiYNSMITSHAFIMIFFMIMPlMIGGFGNWLIPLMMGAPDMAFPRMNNMSFWL 81
Cdd:COG0843   29 FLLIGGLLALLMRLQLAGPGLgLLSPET-YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423  82 LPPSLILLIYSNLINQGIGTGWTIYPPLSLNLNHEGMSIDLSIFSLHLAGSSSIMGAINFITTIMNMMSKKIKLEQLTLF 161
Cdd:COG0843  107 YLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLF 186

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 893665423 162 TWSIFITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 212
Cdd:COG0843  187 TWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-212 1.49e-35

Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key enzyme in aerobic metabolism. Proton pumping haem-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-haem a3 (or haem o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxidases (E.C:1.10.3.11), is directly involved in the coupling between dioxygen reduction and proton pumping. Some terminal oxidases generate a transmembrane proton gradient across the plasma membrane (prokaryotes) or the mitochondrial inner membrane (eukaryotes). The enzyme complex consists of 3-4 subunits (prokaryotes) up to 13 polypeptides (mammals) of which only the catalytic subunit (equivalent to mammalian subunit I (COXI) is found in all haem-copper respiratory oxidases. The presence of a bimetallic centre (formed by a high-spin haem and copper B) as well as a low-spin haem, both ligated to six conserved histidine residues near the outer side of four transmembrane spans within CO I is common to all family members.


Pssm-ID: 459678  Cd Length: 432  Bit Score: 129.62  E-value: 1.49e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423    1 MWAGMIGTSMSMIIRMELSKPGIFINNDQIYNSMITSHAFIMIFFMIMPlMIGGFGNWLIPLMMGAPDMAFPRMNNMSFW 80
Cdd:pfam00115  11 LVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFW 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423   81 LLPPSLILLiysNLINQGIGTGWTIYPPLslnlnhegMSIDLSIFSLHLAGSSSIMGAINFITTIMNMMSKKIKLeQLTL 160
Cdd:pfam00115  90 LVVLGAVLL---LASFGGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPL 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 893665423  161 FTWSIFITTILLLLAVPVLAGAITMLLTDRNLNTsffdpsGGGDPILYQHLF 212
Cdd:pfam00115 158 FVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLF 203
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 11-212 6.01e-33

cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]


Pssm-ID: 131928  Cd Length: 643  Bit Score: 124.58  E-value: 6.01e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423   11 SMIIRMELSKPGIFINNDQIYNSMITSHAFIMIFFMIMPLMIGgFGNWLIPLMMGAPDMAFPRMNNMSFWLLPPSLILLI 90
Cdd:TIGR02882  72 ALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFN 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423   91 YSNLINQGIGTGWTIYPPLSLNLNHEGMSIDLSIFSLHLAGSSSIMGAINFITTIMNMMSKKIKLEQLTLFTWSIFITTI 170
Cdd:TIGR02882 151 ISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTL 230

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 893665423  171 LLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 212
Cdd:TIGR02882 231 IIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLF 272
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-212 1.68e-116

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 341.08  E-value: 1.68e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423   1 MWAGMIGTSMSMIIRMELSKPGIFINNDQIYNSMITSHAFIMIFFMIMPLMIGGFGNWLIPLMMGAPDMAFPRMNNMSFW 80
Cdd:MTH00153  22 AWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFW 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423  81 LLPPSLILLIYSNLINQGIGTGWTIYPPLSLNLNHEGMSIDLSIFSLHLAGSSSIMGAINFITTIMNMMSKKIKLEQLTL 160
Cdd:MTH00153 102 LLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPL 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 893665423 161 FTWSIFITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 212
Cdd:MTH00153 182 FVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 233
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-212 1.51e-112

Cytochrome C oxidase subunit I. 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, but subunit III, which is also conserved, may play a role in assembly or oxygen delivery to the active site. 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 I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center.


Pssm-ID: 238833  Cd Length: 488  Bit Score: 330.21  E-value: 1.51e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423   1 MWAGMIGTSMSMIIRMELSKPGIFINNDQIYNSMITSHAFIMIFFMIMPLMIGGFGNWLIPLMMGAPDMAFPRMNNMSFW 80
Cdd:cd01663   15 LWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFW 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423  81 LLPPSLILLIYSNLINQGIGTGWTIYPPLSLNLNHEGMSIDLSIFSLHLAGSSSIMGAINFITTIMNMMSKKIKLEQLTL 160
Cdd:cd01663   95 LLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPL 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 893665423 161 FTWSIFITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 212
Cdd:cd01663  175 FVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 226
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-212 6.09e-107

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 316.62  E-value: 6.09e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423   1 MWAGMIGTSMSMIIRMELSKPGIFINNDQIYNSMITSHAFIMIFFMIMPLMIGGFGNWLIPLMMGAPDMAFPRMNNMSFW 80
Cdd:MTH00167  24 AWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423  81 LLPPSLILLIYSNLINQGIGTGWTIYPPLSLNLNHEGMSIDLSIFSLHLAGSSSIMGAINFITTIMNMMSKKIKLEQLTL 160
Cdd:MTH00167 104 LLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPL 183

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 893665423 161 FTWSIFITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 212
Cdd:MTH00167 184 FVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-212 8.56e-102

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 303.44  E-value: 8.56e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423   1 MWAGMIGTSMSMIIRMELSKPGIFINNDQIYNSMITSHAFIMIFFMIMPLMIGGFGNWLIPLMMGAPDMAFPRMNNMSFW 80
Cdd:MTH00223  21 MWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFW 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423  81 LLPPSLILLIYSNLINQGIGTGWTIYPPLSLNLNHEGMSIDLSIFSLHLAGSSSIMGAINFITTIMNMMSKKIKLEQLTL 160
Cdd:MTH00223 101 LLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPL 180

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 893665423 161 FTWSIFITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 212
Cdd:MTH00223 181 FVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 232
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-212 1.58e-100

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 300.47  E-value: 1.58e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423   1 MWAGMIGTSMSMIIRMELSKPGIFINNDQIYNSMITSHAFIMIFFMIMPLMIGGFGNWLIPLMMGAPDMAFPRMNNMSFW 80
Cdd:MTH00116  24 AWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFW 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423  81 LLPPSLILLIYSNLINQGIGTGWTIYPPLSLNLNHEGMSIDLSIFSLHLAGSSSIMGAINFITTIMNMMSKKIKLEQLTL 160
Cdd:MTH00116 104 LLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPL 183

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 893665423 161 FTWSIFITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 212
Cdd:MTH00116 184 FVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 2-212 3.25e-98

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 294.32  E-value: 3.25e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423   2 WAGMIGTSMSMIIRMELSKPGIFINNDQIYNSMITSHAFIMIFFMIMPLMIGGFGNWLIPLMMGAPDMAFPRMNNMSFWL 81
Cdd:MTH00142  23 WAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423  82 LPPSLILLIYSNLINQGIGTGWTIYPPLSLNLNHEGMSIDLSIFSLHLAGSSSIMGAINFITTIMNMMSKKIKLEQLTLF 161
Cdd:MTH00142 103 LPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLF 182

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 893665423 162 TWSIFITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 212
Cdd:MTH00142 183 VWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF 233
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 2-212 2.40e-94

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 284.49  E-value: 2.40e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423   2 WAGMIGTSMSMIIRMELSKPGIFINNDQIYNSMITSHAFIMIFFMIMPLMIGGFGNWLIPLMMGAPDMAFPRMNNMSFWL 81
Cdd:MTH00007  22 WGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWL 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423  82 LPPSLILLIYSNLINQGIGTGWTIYPPLSLNLNHEGMSIDLSIFSLHLAGSSSIMGAINFITTIMNMMSKKIKLEQLTLF 161
Cdd:MTH00007 102 LPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLF 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 893665423 162 TWSIFITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 212
Cdd:MTH00007 182 VWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF 232
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 2-212 9.46e-94

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 283.26  E-value: 9.46e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423   2 WAGMIGTSMSMIIRMELSKPGIFINNDQIYNSMITSHAFIMIFFMIMPLMIGGFGNWLIPLMMGAPDMAFPRMNNMSFWL 81
Cdd:MTH00037  25 WAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423  82 LPPSLILLIYSNLINQGIGTGWTIYPPLSLNLNHEGMSIDLSIFSLHLAGSSSIMGAINFITTIMNMMSKKIKLEQLTLF 161
Cdd:MTH00037 105 IPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLF 184

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 893665423 162 TWSIFITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 212
Cdd:MTH00037 185 VWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLF 235
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 2-212 6.86e-92

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 278.35  E-value: 6.86e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423   2 WAGMIGTSMSMIIRMELSKPGIFINNDQIYNSMITSHAFIMIFFMIMPLMIGGFGNWLIPLMMGAPDMAFPRMNNMSFWL 81
Cdd:MTH00183  25 WAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423  82 LPPSLILLIYSNLINQGIGTGWTIYPPLSLNLNHEGMSIDLSIFSLHLAGSSSIMGAINFITTIMNMMSKKIKLEQLTLF 161
Cdd:MTH00183 105 LPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLF 184

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 893665423 162 TWSIFITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 212
Cdd:MTH00183 185 VWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 2-212 8.57e-91

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 275.28  E-value: 8.57e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423   2 WAGMIGTSMSMIIRMELSKPGIFINNDQIYNSMITSHAFIMIFFMIMPLMIGGFGNWLIPLMMGAPDMAFPRMNNMSFWL 81
Cdd:MTH00077  25 WAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423  82 LPPSLILLIYSNLINQGIGTGWTIYPPLSLNLNHEGMSIDLSIFSLHLAGSSSIMGAINFITTIMNMMSKKIKLEQLTLF 161
Cdd:MTH00077 105 LPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLF 184

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 893665423 162 TWSIFITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 212
Cdd:MTH00077 185 VWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLF 235
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 2-212 8.67e-90

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 272.91  E-value: 8.67e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423   2 WAGMIGTSMSMIIRMELSKPGIFINNDQIYNSMITSHAFIMIFFMIMPLMIGGFGNWLIPLMMGAPDMAFPRMNNMSFWL 81
Cdd:MTH00103  25 WAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423  82 LPPSLILLIYSNLINQGIGTGWTIYPPLSLNLNHEGMSIDLSIFSLHLAGSSSIMGAINFITTIMNMMSKKIKLEQLTLF 161
Cdd:MTH00103 105 LPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLF 184

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 893665423 162 TWSIFITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 212
Cdd:MTH00103 185 VWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 235
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-212 1.34e-88

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 269.63  E-value: 1.34e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423   1 MWAGMIGTSMSMIIRMELSKPGIFINNDQIYNSMITSHAFIMIFFMIMPLMIGGFGNWLIPLMMGAPDMAFPRMNNMSFW 80
Cdd:MTH00079  25 LWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFW 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423  81 LLPPSLILLIYSNLINQGIGTGWTIYPPLSlNLNHEGMSIDLSIFSLHLAGSSSIMGAINFITTIMNMMSKKIKLEQLTL 160
Cdd:MTH00079 105 LLPTSLFLILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSL 183

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 893665423 161 FTWSIFITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 212
Cdd:MTH00079 184 FVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLF 235
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 3-212 1.44e-84

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 259.75  E-value: 1.44e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423   3 AGMIGTSMSMIIRMELSKPGIFINNDQIYNSMITSHAFIMIFFMIMPLMIGGFGNWLIPLMMGAPDMAFPRMNNMSFWLL 82
Cdd:MTH00182  28 AGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLL 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423  83 PPSLILLIYSNLINQGIGTGWTIYPPLSLNLNHEGMSIDLSIFSLHLAGSSSIMGAINFITTIMNMMSKKIKLEQLTLFT 162
Cdd:MTH00182 108 PPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFV 187

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 893665423 163 WSIFITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 212
Cdd:MTH00182 188 WSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLF 237
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 2-212 5.04e-84

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 258.22  E-value: 5.04e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423   2 WAGMIGTSMSMIIRMELSKPGIFINNDQIYNSMITSHAFIMIFFMIMPLMIGGFGNWLIPLMMGAPDMAFPRMNNMSFWL 81
Cdd:MTH00184  27 FAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423  82 LPPSLILLIYSNLINQGIGTGWTIYPPLSLNLNHEGMSIDLSIFSLHLAGSSSIMGAINFITTIMNMMSKKIKLEQLTLF 161
Cdd:MTH00184 107 LPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLF 186

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 893665423 162 TWSIFITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 212
Cdd:MTH00184 187 VWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 237
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 3-212 5.31e-77

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 240.69  E-value: 5.31e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423   3 AGMIGTSMSMIIRMELSKPGIFINNDQIYNSMITSHAFIMIFFMIMPLMIGGFGNWLIPLMMGAPDMAFPRMNNMSFWLL 82
Cdd:MTH00026  27 SGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423  83 PPSLILLIYSNLINQGIGTGWTIYPPLSLNLNHEGMSIDLSIFSLHLAGSSSIMGAINFITTIMNMMSKKIKLEQLTLFT 162
Cdd:MTH00026 107 PPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFV 186

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 893665423 163 WSIFITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 212
Cdd:MTH00026 187 WSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLF 236
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-212 3.63e-70

Heme-copper oxidase subunit I. 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 three to five in bacteria and up to 13 in mammalian mitochondria. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. Membership in the superfamily is defined by subunit I, which contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons to the binuclear center. Only subunit I is common to the entire superfamily. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from the electron donor on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I of cytochrome c oxidase (CcO) and ubiquinol oxidase. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electron transfer occurs in two segments: from the electron donor to the low-spin heme, and from the low-spin heme to the binuclear center. The first segment can be a multi-step process and varies among the different families, while the second segment, a direct transfer, is consistent throughout the superfamily.


Pssm-ID: 238461  Cd Length: 463  Bit Score: 220.87  E-value: 3.63e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423   1 MWAGMIGTSMSMIIRMELSKPGIFINNDQIYNSMITSHAFIMIFFMIMPLMIGGFGNWLIPlMMGAPDMAFPRMNNMSFW 80
Cdd:cd00919   13 FVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFW 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423  81 LLPPSLILLIYSNLINQGIGTGWTIYPPLSLNLNHEGMSIDLSIFSLHLAGSSSIMGAINFITTIMNMMSKKIKLEQLTL 160
Cdd:cd00919   92 LFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPL 171

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 893665423 161 FTWSIFITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 212
Cdd:cd00919  172 FVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLF 223
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
3-212 6.17e-61

Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];


Pssm-ID: 440605  Cd Length: 535  Bit Score: 198.43  E-value: 6.17e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423   3 AGMIGTSMSMIIRMELSKPGI-FINNDQiYNSMITSHAFIMIFFMIMPlMIGGFGNWLIPLMMGAPDMAFPRMNNMSFWL 81
Cdd:COG0843   29 FLLIGGLLALLMRLQLAGPGLgLLSPET-YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423  82 LPPSLILLIYSNLINQGIGTGWTIYPPLSLNLNHEGMSIDLSIFSLHLAGSSSIMGAINFITTIMNMMSKKIKLEQLTLF 161
Cdd:COG0843  107 YLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLF 186

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 893665423 162 TWSIFITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 212
Cdd:COG0843  187 TWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLF 237
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-212 7.35e-59

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 192.59  E-value: 7.35e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423   1 MWAGMIGTSMSMIIRMELSKPGIFINNDQIYNSMITSHAFIMIFFMIMPLMIGGFGNWLIPLMMGAPDMAFPRMNNMSFW 80
Cdd:MTH00048  25 VWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAW 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423  81 LLPPSLILLIYSNLInqGIGTGWTIYPPLSLNLNHEGMSIDLSIFSLHLAGSSSIMGAINFITTIMNMMSKKIkLEQLTL 160
Cdd:MTH00048 105 LLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNV-FSRTSI 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 893665423 161 FTWSIFITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 212
Cdd:MTH00048 182 ILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMF 233
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 6-212 1.66e-50

Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits in ubiquinol oxidase varies from two to five. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons from ubiquinol to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from ubiquinol on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. It is generally believed that the channels contain water molecules that act as 'proton wires' to transfer the protons. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are believed to be transferred directly from ubiquinol (the electron donor) to the low-spin heme, and directly from the low-spin heme to the binuclear center.


Pssm-ID: 238832  Cd Length: 501  Bit Score: 170.45  E-value: 1.66e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423   6 IGTSMSMIIRMELSKPGI-FINNDQiYNSMITSHAFIMIFFMIMPLMIGgFGNWLIPLMMGAPDMAFPRMNNMSFWLLPP 84
Cdd:cd01662   24 RGGVDALLMRTQLALPGNdFLSPEH-YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLF 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423  85 SLILLIYSNLINQGIGTGWTIYPPLSLNLNHEGMSIDLSIFSLHLAGSSSIMGAINFITTIMNMMSKKIKLEQLTLFTWS 164
Cdd:cd01662  102 GGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWT 181

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 893665423 165 IFITTILLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 212
Cdd:cd01662  182 TLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLF 229
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-212 1.49e-35

Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key enzyme in aerobic metabolism. Proton pumping haem-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-haem a3 (or haem o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxidases (E.C:1.10.3.11), is directly involved in the coupling between dioxygen reduction and proton pumping. Some terminal oxidases generate a transmembrane proton gradient across the plasma membrane (prokaryotes) or the mitochondrial inner membrane (eukaryotes). The enzyme complex consists of 3-4 subunits (prokaryotes) up to 13 polypeptides (mammals) of which only the catalytic subunit (equivalent to mammalian subunit I (COXI) is found in all haem-copper respiratory oxidases. The presence of a bimetallic centre (formed by a high-spin haem and copper B) as well as a low-spin haem, both ligated to six conserved histidine residues near the outer side of four transmembrane spans within CO I is common to all family members.


Pssm-ID: 459678  Cd Length: 432  Bit Score: 129.62  E-value: 1.49e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423    1 MWAGMIGTSMSMIIRMELSKPGIFINNDQIYNSMITSHAFIMIFFMIMPlMIGGFGNWLIPLMMGAPDMAFPRMNNMSFW 80
Cdd:pfam00115  11 LVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFW 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423   81 LLPPSLILLiysNLINQGIGTGWTIYPPLslnlnhegMSIDLSIFSLHLAGSSSIMGAINFITTIMNMMSKKIKLeQLTL 160
Cdd:pfam00115  90 LVVLGAVLL---LASFGGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPL 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 893665423  161 FTWSIFITTILLLLAVPVLAGAITMLLTDRNLNTsffdpsGGGDPILYQHLF 212
Cdd:pfam00115 158 FVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLF 203
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 11-212 6.01e-33

cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]


Pssm-ID: 131928  Cd Length: 643  Bit Score: 124.58  E-value: 6.01e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423   11 SMIIRMELSKPGIFINNDQIYNSMITSHAFIMIFFMIMPLMIGgFGNWLIPLMMGAPDMAFPRMNNMSFWLLPPSLILLI 90
Cdd:TIGR02882  72 ALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFN 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423   91 YSNLINQGIGTGWTIYPPLSLNLNHEGMSIDLSIFSLHLAGSSSIMGAINFITTIMNMMSKKIKLEQLTLFTWSIFITTI 170
Cdd:TIGR02882 151 ISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTL 230

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 893665423  171 LLLLAVPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF 212
Cdd:TIGR02882 231 IIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLF 272
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 31-211 3.19e-28

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 111.18  E-value: 3.19e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423  31 YNSMITSHAFIMIFFMIMPLMIGgFGNWLIPLMMGAPDMAFPRMNNMSFWLLPPSLILLIYSNLINQGIGTGWTIYPPLS 110
Cdd:PRK15017  99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893665423 111 LNLNHEGMSIDLSIFSLHLAGSSSIMGAINFITTIMNMMSKKIKLEQLTLFTWSIFITTILLLLAVPVLAGAITMLLTDR 190
Cdd:PRK15017 178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257

                        170       180
                 ....*....|....*....|.
gi 893665423 191 NLNTSFFDPSGGGDPILYQHL 211
Cdd:PRK15017 258 YLGTHFFTNDMGGNMMMYINL 278
 
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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