NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1194587582|gb|ARR97098|]
View 

cytochrome oxidase subunit I, partial (mitochondrion) [Hyperolius nasutus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Heme_Cu_Oxidase_I super family cl00275
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-275 0e+00

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: 552.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582   1 LSLPVLAAGITMLLTDRNLNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSNKKEPFGYMGMVWA 80
Cdd:MTH00153  195 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYA 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582  81 MLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGVIKWEAPMFWALGFIFLFTVGGLTGI 160
Cdd:MTH00153  275 MLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGV 354

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582 161 VLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHDSWVKIHFIIMFVGVNLTFFPQHFLGLAGM 240
Cdd:MTH00153  355 VLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGM 434

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1194587582 241 PRRYSDYPDAYTLWNSVSSIGSLISLIAVIM*MFI 275
Cdd:MTH00153  435 PRRYSDYPDAYTSWNVISSIGSTISLISILFFIFI 469
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-275 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 552.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582   1 LSLPVLAAGITMLLTDRNLNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSNKKEPFGYMGMVWA 80
Cdd:MTH00153  195 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYA 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582  81 MLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGVIKWEAPMFWALGFIFLFTVGGLTGI 160
Cdd:MTH00153  275 MLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGV 354

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582 161 VLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHDSWVKIHFIIMFVGVNLTFFPQHFLGLAGM 240
Cdd:MTH00153  355 VLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGM 434

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1194587582 241 PRRYSDYPDAYTLWNSVSSIGSLISLIAVIM*MFI 275
Cdd:MTH00153  435 PRRYSDYPDAYTSWNVISSIGSTISLISILFFIFI 469
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-275 0e+00

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: 539.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582   1 LSLPVLAAGITMLLTDRNLNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSNKKEPFGYMGMVWA 80
Cdd:cd01663   188 LSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYA 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582  81 MLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGVIKWEAPMFWALGFIFLFTVGGLTGI 160
Cdd:cd01663   268 MLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGV 347

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582 161 VLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHDSWVKIHFIIMFVGVNLTFFPQHFLGLAGM 240
Cdd:cd01663   348 VLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGM 427

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1194587582 241 PRRYSDYPDAYTLWNSVSSIGSLISLIAVIM*MFI 275
Cdd:cd01663   428 PRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFI 462
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-275 1.34e-124

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 365.22  E-value: 1.34e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582   1 LSLPVLAAGITMLLTDRNLNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSnKKEPFGYMGMVWA 80
Cdd:COG0843   199 LAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFS-RKPLFGYKAMVLA 277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582  81 MLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGVIKWEAPMFWALGFIFLFTVGGLTGI 160
Cdd:COG0843   278 TVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGV 357

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582 161 VLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHDSWVKIHFIIMFVGVNLTFFPQHFLGLAGM 240
Cdd:COG0843   358 MLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGM 437

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1194587582 241 PRRYSDYP--DAYTLWNSVSSIGSLISLIAVIM*MFI 275
Cdd:COG0843   438 PRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLIN 474
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-274 4.80e-120

cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) of cytochrome c oxidases of bacterial origin. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits I-III form the functional core of the enzyme complex. Subunit I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit II and heme a of subunit I to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. In the bacilli an apparent split (paralogism) has created a sister clade (TIGR02882) encoding subunits (QoxA) of the aa3-type quinone oxidase complex which reacts directly with quinones, bypassing the interaction with soluble cytochrome c. This model attempts to exclude these sequences, placing them between the trusted and noise cutoffs. These families, as well as archaeal and eukaryotic cytochrome c subunit I's are included within the superfamily model, pfam00115. [Energy metabolism, Electron transport]


Pssm-ID: 213748  Cd Length: 499  Bit Score: 352.30  E-value: 4.80e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582   1 LSLPVLAAGITMLLTDRNLNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSnKKEPFGYMGMVWA 80
Cdd:TIGR02891 190 LAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFA-RKPIFGYRAMVYA 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582  81 MLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGVIKWEAPMFWALGFIFLFTVGGLTGI 160
Cdd:TIGR02891 269 TVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGV 348

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582 161 VLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHDSWVKIHFIIMFVGVNLTFFPQHFLGLAGM 240
Cdd:TIGR02891 349 MLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGM 428

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1194587582 241 PRRYSDYPDA--YTLWNSVSSIGSLISLIAVIM*MF 274
Cdd:TIGR02891 429 PRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLW 464
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-264 3.38e-83

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: 255.96  E-value: 3.38e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582   1 LSLPVLAAGITMLLTDRNLNTtffdptGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSNKKePFGYMGMVWA 80
Cdd:pfam00115 171 LAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLA 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582  81 MLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGVIKW-EAPMFWALGFIFLFTVGGLTG 159
Cdd:pfam00115 244 FWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFFLGFAFLFIIGGLTG 323

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582 160 IVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHDSWVKIHFIIMFVGVNLTFFPQHFLGLAG 239
Cdd:pfam00115 324 VMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLG 403

                         250       260
                  ....*....|....*....|....*....
gi 1194587582 240 MPRRYS----DYPDAYTLWNSVSSIGSLI 264
Cdd:pfam00115 404 MPRRYAppfiETVPAFQPLNWIRTIGGVL 432
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-275 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 552.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582   1 LSLPVLAAGITMLLTDRNLNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSNKKEPFGYMGMVWA 80
Cdd:MTH00153  195 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYA 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582  81 MLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGVIKWEAPMFWALGFIFLFTVGGLTGI 160
Cdd:MTH00153  275 MLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGV 354

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582 161 VLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHDSWVKIHFIIMFVGVNLTFFPQHFLGLAGM 240
Cdd:MTH00153  355 VLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGM 434

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1194587582 241 PRRYSDYPDAYTLWNSVSSIGSLISLIAVIM*MFI 275
Cdd:MTH00153  435 PRRYSDYPDAYTSWNVISSIGSTISLISILFFIFI 469
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-275 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 542.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582   1 LSLPVLAAGITMLLTDRNLNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSNKKEPFGYMGMVWA 80
Cdd:MTH00116  197 LSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWA 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582  81 MLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGVIKWEAPMFWALGFIFLFTVGGLTGI 160
Cdd:MTH00116  277 MLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGI 356

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582 161 VLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHDSWVKIHFIIMFVGVNLTFFPQHFLGLAGM 240
Cdd:MTH00116  357 VLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGM 436

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1194587582 241 PRRYSDYPDAYTLWNSVSSIGSLISLIAVIM*MFI 275
Cdd:MTH00116  437 PRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFI 471
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-275 0e+00

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: 539.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582   1 LSLPVLAAGITMLLTDRNLNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSNKKEPFGYMGMVWA 80
Cdd:cd01663   188 LSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYA 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582  81 MLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGVIKWEAPMFWALGFIFLFTVGGLTGI 160
Cdd:cd01663   268 MLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGV 347

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582 161 VLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHDSWVKIHFIIMFVGVNLTFFPQHFLGLAGM 240
Cdd:cd01663   348 VLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGM 427

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1194587582 241 PRRYSDYPDAYTLWNSVSSIGSLISLIAVIM*MFI 275
Cdd:cd01663   428 PRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFI 462
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-275 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 527.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582   1 LSLPVLAAGITMLLTDRNLNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSNKKEPFGYMGMVWA 80
Cdd:MTH00167  197 LSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWA 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582  81 MLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGVIKWEAPMFWALGFIFLFTVGGLTGI 160
Cdd:MTH00167  277 MMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGI 356

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582 161 VLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHDSWVKIHFIIMFVGVNLTFFPQHFLGLAGM 240
Cdd:MTH00167  357 VLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGM 436

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1194587582 241 PRRYSDYPDAYTLWNSVSSIGSLISLIAVIM*MFI 275
Cdd:MTH00167  437 PRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFI 471
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-275 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 509.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582   1 LSLPVLAAGITMLLTDRNLNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSNKKEPFGYMGMVWA 80
Cdd:MTH00077  197 LSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWA 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582  81 MLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGVIKWEAPMFWALGFIFLFTVGGLTGI 160
Cdd:MTH00077  277 MMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGI 356

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582 161 VLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHDSWVKIHFIIMFVGVNLTFFPQHFLGLAGM 240
Cdd:MTH00077  357 VLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGM 436

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1194587582 241 PRRYSDYPDAYTLWNSVSSIGSLISLIAVIM*MFI 275
Cdd:MTH00077  437 PRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFI 471
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-275 2.81e-177

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 498.35  E-value: 2.81e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582   1 LSLPVLAAGITMLLTDRNLNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSNKKEPFGYMGMVWA 80
Cdd:MTH00223  194 LSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYA 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582  81 MLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGVIKWEAPMFWALGFIFLFTVGGLTGI 160
Cdd:MTH00223  274 MLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGI 353

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582 161 VLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHDSWVKIHFIIMFVGVNLTFFPQHFLGLAGM 240
Cdd:MTH00223  354 ILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGM 433

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1194587582 241 PRRYSDYPDAYTLWNSVSSIGSLISLIAVIM*MFI 275
Cdd:MTH00223  434 PRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFI 468
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-275 2.12e-174

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 491.36  E-value: 2.12e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582   1 LSLPVLAAGITMLLTDRNLNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSNKKEPFGYMGMVWA 80
Cdd:MTH00183  197 LSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWA 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582  81 MLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGVIKWEAPMFWALGFIFLFTVGGLTGI 160
Cdd:MTH00183  277 MMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGI 356

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582 161 VLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHDSWVKIHFIIMFVGVNLTFFPQHFLGLAGM 240
Cdd:MTH00183  357 VLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGM 436

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1194587582 241 PRRYSDYPDAYTLWNSVSSIGSLISLIAVIM*MFI 275
Cdd:MTH00183  437 PRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFI 471
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-275 9.43e-173

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 486.92  E-value: 9.43e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582   1 LSLPVLAAGITMLLTDRNLNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSNKKEPFGYMGMVWA 80
Cdd:MTH00142  195 LSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYA 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582  81 MLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGVIKWEAPMFWALGFIFLFTVGGLTGI 160
Cdd:MTH00142  275 MLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGI 354

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582 161 VLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHDSWVKIHFIIMFVGVNLTFFPQHFLGLAGM 240
Cdd:MTH00142  355 VLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGM 434

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1194587582 241 PRRYSDYPDAYTLWNSVSSIGSLISLIAVIM*MFI 275
Cdd:MTH00142  435 PRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFI 469
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-275 6.33e-171

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 482.46  E-value: 6.33e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582   1 LSLPVLAAGITMLLTDRNLNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSNKKEPFGYMGMVWA 80
Cdd:MTH00103  197 LSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWA 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582  81 MLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGVIKWEAPMFWALGFIFLFTVGGLTGI 160
Cdd:MTH00103  277 MMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGI 356

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582 161 VLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHDSWVKIHFIIMFVGVNLTFFPQHFLGLAGM 240
Cdd:MTH00103  357 VLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGM 436

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1194587582 241 PRRYSDYPDAYTLWNSVSSIGSLISLIAVIM*MFI 275
Cdd:MTH00103  437 PRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFM 471
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-275 2.37e-159

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 453.13  E-value: 2.37e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582   1 LSLPVLAAGITMLLTDRNLNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSNKKEPFGYMGMVWA 80
Cdd:MTH00037  197 LSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYA 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582  81 MLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGVIKWEAPMFWALGFIFLFTVGGLTGI 160
Cdd:MTH00037  277 MIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGI 356

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582 161 VLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHDSWVKIHFIIMFVGVNLTFFPQHFLGLAGM 240
Cdd:MTH00037  357 VLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGM 436

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1194587582 241 PRRYSDYPDAYTLWNSVSSIGSLISLIAVIM*MFI 275
Cdd:MTH00037  437 PRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFL 471
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-275 9.80e-156

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 443.57  E-value: 9.80e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582   1 LSLPVLAAGITMLLTDRNLNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSNKKEPFGYMGMVWA 80
Cdd:MTH00007  194 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYA 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582  81 MLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGVIKWEAPMFWALGFIFLFTVGGLTGI 160
Cdd:MTH00007  274 MLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGI 353

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582 161 VLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHDSWVKIHFIIMFVGVNLTFFPQHFLGLAGM 240
Cdd:MTH00007  354 VLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGM 433

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1194587582 241 PRRYSDYPDAYTLWNSVSSIGSLISLIAVIM*MFI 275
Cdd:MTH00007  434 PRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFI 468
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-275 1.12e-139

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 402.91  E-value: 1.12e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582   1 LSLPVLAAGITMLLTDRNLNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSNKKEPFGYMGMVWA 80
Cdd:MTH00079  197 LSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYA 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582  81 MLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGVIKWEAPMFWALGFIFLFTVGGLTGI 160
Cdd:MTH00079  277 ILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGV 356

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582 161 VLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHDSWVKIHFIIMFVGVNLTFFPQHFLGLAGM 240
Cdd:MTH00079  357 ILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGM 436

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1194587582 241 PRRYSDYPDAYTLWNSVSSIGSLISLIAVIM*MFI 275
Cdd:MTH00079  437 PRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYV 471
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-275 1.72e-139

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 403.05  E-value: 1.72e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582   1 LSLPVLAAGITMLLTDRNLNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSNKKEPFGYMGMVWA 80
Cdd:MTH00182  199 LSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYA 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582  81 MLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGVIKWEAPMFWALGFIFLFTVGGLTGI 160
Cdd:MTH00182  279 MLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGV 358

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582 161 VLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHDSWVKIHFIIMFVGVNLTFFPQHFLGLAGM 240
Cdd:MTH00182  359 VLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGF 438

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1194587582 241 PRRYSDYPDAYTLWNSVSSIGSLISLIAVIM*MFI 275
Cdd:MTH00182  439 PRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYI 473
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-275 1.10e-136

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 395.35  E-value: 1.10e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582   1 LSLPVLAAGITMLLTDRNLNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSNKKEPFGYMGMVWA 80
Cdd:MTH00184  199 LSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYA 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582  81 MLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGVIKWEAPMFWALGFIFLFTVGGLTGI 160
Cdd:MTH00184  279 MVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGI 358

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582 161 VLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHDSWVKIHFIIMFVGVNLTFFPQHFLGLAGM 240
Cdd:MTH00184  359 VLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGL 438

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1194587582 241 PRRYSDYPDAYTLWNSVSSIGSLISLIAVIM*MFI 275
Cdd:MTH00184  439 PRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYI 473
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-275 2.87e-129

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: 374.56  E-value: 2.87e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582   1 LSLPVLAAGITMLLTDRNLNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSNKKePFGYMGMVWA 80
Cdd:cd00919   185 LALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGKP-LFGYKLMVYA 263

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582  81 MLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGVIKWEAPMFWALGFIFLFTVGGLTGI 160
Cdd:cd00919   264 FLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGV 343

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582 161 VLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHDSWVKIHFIIMFVGVNLTFFPQHFLGLAGM 240
Cdd:cd00919   344 VLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGFNLTFFPMHFLGLLGM 423

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1194587582 241 PRRYSDYPDAYTLWNSVSSIGSLISLIAVIM*MFI 275
Cdd:cd00919   424 PRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGN 458
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-275 1.34e-124

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 365.22  E-value: 1.34e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582   1 LSLPVLAAGITMLLTDRNLNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSnKKEPFGYMGMVWA 80
Cdd:COG0843   199 LAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFS-RKPLFGYKAMVLA 277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582  81 MLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGVIKWEAPMFWALGFIFLFTVGGLTGI 160
Cdd:COG0843   278 TVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGV 357

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582 161 VLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHDSWVKIHFIIMFVGVNLTFFPQHFLGLAGM 240
Cdd:COG0843   358 MLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGM 437

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1194587582 241 PRRYSDYP--DAYTLWNSVSSIGSLISLIAVIM*MFI 275
Cdd:COG0843   438 PRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLIN 474
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-274 4.80e-120

cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) of cytochrome c oxidases of bacterial origin. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits I-III form the functional core of the enzyme complex. Subunit I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit II and heme a of subunit I to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. In the bacilli an apparent split (paralogism) has created a sister clade (TIGR02882) encoding subunits (QoxA) of the aa3-type quinone oxidase complex which reacts directly with quinones, bypassing the interaction with soluble cytochrome c. This model attempts to exclude these sequences, placing them between the trusted and noise cutoffs. These families, as well as archaeal and eukaryotic cytochrome c subunit I's are included within the superfamily model, pfam00115. [Energy metabolism, Electron transport]


Pssm-ID: 213748  Cd Length: 499  Bit Score: 352.30  E-value: 4.80e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582   1 LSLPVLAAGITMLLTDRNLNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSnKKEPFGYMGMVWA 80
Cdd:TIGR02891 190 LAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFA-RKPIFGYRAMVYA 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582  81 MLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGVIKWEAPMFWALGFIFLFTVGGLTGI 160
Cdd:TIGR02891 269 TVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGV 348

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582 161 VLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHDSWVKIHFIIMFVGVNLTFFPQHFLGLAGM 240
Cdd:TIGR02891 349 MLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGM 428

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1194587582 241 PRRYSDYPDA--YTLWNSVSSIGSLISLIAVIM*MF 274
Cdd:TIGR02891 429 PRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLW 464
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-275 2.01e-118

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 349.70  E-value: 2.01e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582   1 LSLPVLAAGITMLLTDRNLNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSNKKEPFGYMGMVWA 80
Cdd:MTH00026  198 LSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYA 277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582  81 MLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGG--VIKWEAPMFWALGFIFLFTVGGLT 158
Cdd:MTH00026  278 MLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLT 357

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582 159 GIVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHDSWVKIHFIIMFVGVNLTFFPQHFLGLA 238
Cdd:MTH00026  358 GIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLA 437

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1194587582 239 GMPRRYSDYPDAYTLWNSVSSIGSLISLIAVIM*MFI 275
Cdd:MTH00026  438 GLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVV 474
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-275 1.62e-113

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 336.26  E-value: 1.62e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582   1 LSLPVLAAGITMLLTDRNLNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSNKKEPFGYMGMVWA 80
Cdd:MTH00048  195 LSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFA 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582  81 MLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHG-GVIKWEAPMFWALGFIFLFTVGGLTG 159
Cdd:MTH00048  275 MFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNsRVRKSDPVVWWVVSFIVLFTIGGVTG 354

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582 160 IVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHDSWVKIHFIIMFVGVNLTFFPQHFLGLAG 239
Cdd:MTH00048  355 IVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCG 434

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1194587582 240 MPRRYSDYPDAYTLWNSVSSIGSLISLIAVIM*MFI 275
Cdd:MTH00048  435 LPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFI 470
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-271 1.07e-110

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: 328.39  E-value: 1.07e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582   1 LSLPVLAAGITMLLTDRNLNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSnKKEPFGYMGMVWA 80
Cdd:cd01662   191 FAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFS-RKPLFGYRSMVYA 269

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582  81 MLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGVIKWEAPMFWALGFIFLFTVGGLTGI 160
Cdd:cd01662   270 TVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGV 349

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582 161 VLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHDSWVKIHFIIMFVGVNLTFFPQHFLGLAGM 240
Cdd:cd01662   350 MLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFNLTFFPMHILGLMGM 429

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1194587582 241 PRRYSDYP--DAYTLWNSVSSIGSLISLIAVIM 271
Cdd:cd01662   430 PRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLL 462
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-264 3.38e-83

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: 255.96  E-value: 3.38e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582   1 LSLPVLAAGITMLLTDRNLNTtffdptGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSNKKePFGYMGMVWA 80
Cdd:pfam00115 171 LAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLA 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582  81 MLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGVIKW-EAPMFWALGFIFLFTVGGLTG 159
Cdd:pfam00115 244 FWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFFLGFAFLFIIGGLTG 323

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582 160 IVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHDSWVKIHFIIMFVGVNLTFFPQHFLGLAG 239
Cdd:pfam00115 324 VMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLG 403

                         250       260
                  ....*....|....*....|....*....
gi 1194587582 240 MPRRYS----DYPDAYTLWNSVSSIGSLI 264
Cdd:pfam00115 404 MPRRYAppfiETVPAFQPLNWIRTIGGVL 432
CyoB TIGR02843
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ...
 2-269 3.09e-77

cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain which reacts with oxygen, reducing it to water with the concomitant transport of 4 protons across the membrane. Also known as the cytochrome bo complex, cytochrome o ubiquinol oxidase contains four subunits, two heme b cofactors and a copper atom which is believed to be the oxygen active site. This complex is structurally related to the cytochrome caa3 oxidases which utilize cytochrome c as the reductant and contain heme a cofactors, as well as the intermediate form aa3 oxidases which also react directly with quinones as the reductant. [Energy metabolism, Electron transport]


Pssm-ID: 131890  Cd Length: 646  Bit Score: 246.51  E-value: 3.09e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582   2 SLPVLAAGITMLLTDRNLNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSnKKEPFGYMGMVWAM 81
Cdd:TIGR02843 241 SFPILTVTLALLTLDRYLGMHFFTNEAGGNPMMYVNLIWAWGHPEVYILILPAFGIFSEVVATFS-RKRLFGYTSMVWAT 319

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582  82 LSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGVIKWEAPMFWALGFIFLFTVGGLTGIV 161
Cdd:TIGR02843 320 IAITVLSFIVWLHHFFTMGAGANVNAFFGIATMIIAIPTGVKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVL 399

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582 162 LANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHDSWVKIHFIIMFVGVNLTFFPQHFLGLAGMP 241
Cdd:TIGR02843 400 LAVPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWFPKAFGFKLNEKLGKRSFWCWFIGFYLAFMPLYILGFMGMT 479

                         250       260
                  ....*....|....*....|....*....
gi 1194587582 242 RRYSDYPD-AYTLWNSVSSIGSLISLIAV 269
Cdd:TIGR02843 480 RRLNHYDNpEWHPMLIIAAFGAFLIACGI 508
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 2-249 1.47e-65

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 215.96  E-value: 1.47e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582   2 SLPVLAAGITMLLTDRNLNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSnKKEPFGYMGMVWAM 81
Cdd:PRK15017  242 SFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWAT 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582  82 LSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATIHGGVIKWEAPMFWALGFIFLFTVGGLTGIV 161
Cdd:PRK15017  321 VCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVL 400

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582 162 LANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLTLHDSWVKIHFIIMFVGVNLTFFPQHFLGLAGMP 241
Cdd:PRK15017  401 LAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMT 480


                  ....*...
gi 1194587582 242 RRYSDYPD 249
Cdd:PRK15017  481 RRLSQQID 488
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 31-275 4.89e-17

ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively. For general information on the heme-copper oxidase superfamily, please see cd00919.


Pssm-ID: 238830  Cd Length: 473  Bit Score: 80.41  E-value: 4.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582  31 DPILYQHLFWFFGHPEVYILILPGFGIISHVVAYYSNKKEPFGYMGMVWAMLSIgLLGFIVWAHHMFTtDLNVDTRAYF- 109
Cdd:cd01660   200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARLAFILFL-LFSTPVGFHHQFA-DPGIGPGWKFi 277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582 110 -TSATMIIAIPTGVKVFSWLATI-HGGVIK-------------WEAPMFWALGF-IFLFTVGGLTGIVLANSSIDIVLHD 173
Cdd:cd01660   278 hMVLTFMVALPSLLTAFTVFASLeIAGRLRggkglfgwiralpWGDPMFLALFLaMLMFIPGGAGGIINASYQLNYVVHN 357

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587582 174 TYYVVAHFHyvLSMGAVFAIMA-GFVHWF-PLFTGLTLHDSWV-KIHFIIMFVGVNLTFFPQHFLGLAGMPRR--YSDYP 248
Cdd:cd01660   358 TAWVPGHFH--LTVGGAVALTFmAVAYWLvPHLTGRELAAKRLaLAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYG 435

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1194587582 249 DAY-----TLWNSVSSIGSLISLIAVIM*MFI 275
Cdd:cd01660   436 GLPaagewAPYQQLMAIGGTILFVSGALFLYI 467
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH