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Conserved domains on  [gi|926663203|gb|ALD51942|]
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cytochrome c oxidase subunit 1, partial (mitochondrion) [Psorodonotus fieberi]

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 ...
 1-370 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: 759.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203   1 SLVESGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGASSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLL 80
Cdd:MTH00153 114 SMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILL 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203  81 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIISQESGKKEAFGTLGMIY 160
Cdd:MTH00153 194 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIY 273

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 161 AMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTG 240
Cdd:MTH00153 274 AMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTG 353

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 241 VVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTLNPKWLKIQFTTMFVGVNLTFFPQHFLGLAG 320
Cdd:MTH00153 354 VVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAG 433

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 926663203 321 MPRRYSDYPDSYTSWNVVSSLGSTISFIGIIFLIFIIWESMISNRTVLFP 370
Cdd:MTH00153 434 MPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFS 483
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-370 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 759.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203   1 SLVESGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGASSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLL 80
Cdd:MTH00153 114 SMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILL 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203  81 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIISQESGKKEAFGTLGMIY 160
Cdd:MTH00153 194 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIY 273

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 161 AMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTG 240
Cdd:MTH00153 274 AMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTG 353

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 241 VVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTLNPKWLKIQFTTMFVGVNLTFFPQHFLGLAG 320
Cdd:MTH00153 354 VVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAG 433

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 926663203 321 MPRRYSDYPDSYTSWNVVSSLGSTISFIGIIFLIFIIWESMISNRTVLFP 370
Cdd:MTH00153 434 MPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFS 483
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-369 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: 666.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203   1 SLVESGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGASSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLL 80
Cdd:cd01663  107 ALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLL 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203  81 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIISQESGKKEAFGTLGMIY 160
Cdd:cd01663  187 LLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVY 266

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 161 AMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTG 240
Cdd:cd01663  267 AMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTG 346

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 241 VVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTLNPKWLKIQFTTMFVGVNLTFFPQHFLGLAG 320
Cdd:cd01663  347 VVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAG 426

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 926663203 321 MPRRYSDYPDSYTSWNVVSSLGSTISFIGIIFLIFIIWESMISNRTVLF 369
Cdd:cd01663  427 MPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIF 475
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-344 1.48e-151

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 438.02  E-value: 1.48e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203   2 LVESGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGASSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLLL 81
Cdd:COG0843  119 FVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILIL 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203  82 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIISQESGKKeAFGTLGMIYA 161
Cdd:COG0843  199 LAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLA 277

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 162 MMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTGV 241
Cdd:COG0843  278 TVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGV 357

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 242 VLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTLNPKWLKIQFTTMFVGVNLTFFPQHFLGLAGM 321
Cdd:COG0843  358 MLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGM 437

                        330       340
                 ....*....|....*....|....*
gi 926663203 322 PRRYSDYP--DSYTSWNVVSSLGST 344
Cdd:COG0843  438 PRRYATYPpePGWQPLNLISTIGAF 462
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 2-343 1.87e-148

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: 428.57  E-value: 1.87e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203    2 LVESGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGASSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLLL 81
Cdd:TIGR02891 110 FTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILIL 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203   82 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIISQESGKKeAFGTLGMIYA 161
Cdd:TIGR02891 190 LAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYA 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203  162 MMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTGV 241
Cdd:TIGR02891 269 TVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGV 348

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203  242 VLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTLNPKWLKIQFTTMFVGVNLTFFPQHFLGLAGM 321
Cdd:TIGR02891 349 MLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGM 428

                         330       340
                  ....*....|....*....|....
gi 926663203  322 PRRYSDYPDS--YTSWNVVSSLGS 343
Cdd:TIGR02891 429 PRRYYTYPPQmgFATLNLISTIGA 452
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 6-344 3.36e-102

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: 308.35  E-value: 3.36e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203    6 GAGTGWTVYPPLSAgiahagasVDLAIFSLHLAGASSILGAVNFITTTINMRAPGMSLdQTPLFVWAVAITALLLLLSLP 85
Cdd:pfam00115 104 GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFP 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203   86 VLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIISQESGKKeAFGTLGMIYAMMAI 165
Cdd:pfam00115 175 VLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLI 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203  166 GLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLT-YSPALLWVLGFVFLFTIGGLTGVVLA 244
Cdd:pfam00115 248 AFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRfRTTPMLFFLGFAFLFIIGGLTGVMLA 327

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203  245 NSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTLNPKWLKIQFTTMFVGVNLTFFPQHFLGLAGMPRR 324
Cdd:pfam00115 328 LPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRR 407

                         330       340
                  ....*....|....*....|....
gi 926663203  325 YS----DYPDSYTSWNVVSSLGST 344
Cdd:pfam00115 408 YAppfiETVPAFQPLNWIRTIGGV 431
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-370 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 759.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203   1 SLVESGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGASSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLL 80
Cdd:MTH00153 114 SMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILL 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203  81 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIISQESGKKEAFGTLGMIY 160
Cdd:MTH00153 194 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIY 273

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 161 AMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTG 240
Cdd:MTH00153 274 AMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTG 353

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 241 VVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTLNPKWLKIQFTTMFVGVNLTFFPQHFLGLAG 320
Cdd:MTH00153 354 VVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAG 433

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 926663203 321 MPRRYSDYPDSYTSWNVVSSLGSTISFIGIIFLIFIIWESMISNRTVLFP 370
Cdd:MTH00153 434 MPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFS 483
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-369 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: 666.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203   1 SLVESGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGASSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLL 80
Cdd:cd01663  107 ALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLL 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203  81 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIISQESGKKEAFGTLGMIY 160
Cdd:cd01663  187 LLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVY 266

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 161 AMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTG 240
Cdd:cd01663  267 AMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTG 346

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 241 VVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTLNPKWLKIQFTTMFVGVNLTFFPQHFLGLAG 320
Cdd:cd01663  347 VVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAG 426

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 926663203 321 MPRRYSDYPDSYTSWNVVSSLGSTISFIGIIFLIFIIWESMISNRTVLF 369
Cdd:cd01663  427 MPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIF 475
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-369 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 630.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203   1 SLVESGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGASSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLL 80
Cdd:MTH00167 116 SGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILL 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203  81 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIISQESGKKEAFGTLGMIY 160
Cdd:MTH00167 196 LLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVW 275

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 161 AMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTG 240
Cdd:MTH00167 276 AMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTG 355

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 241 VVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTLNPKWLKIQFTTMFVGVNLTFFPQHFLGLAG 320
Cdd:MTH00167 356 IVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAG 435

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 926663203 321 MPRRYSDYPDSYTSWNVVSSLGSTISFIGIIFLIFIIWESMISNRTVLF 369
Cdd:MTH00167 436 MPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLLP 484
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-370 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 624.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203   1 SLVESGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGASSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLL 80
Cdd:MTH00223 113 SAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLL 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203  81 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIISQESGKKEAFGTLGMIY 160
Cdd:MTH00223 193 LLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIY 272

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 161 AMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTG 240
Cdd:MTH00223 273 AMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTG 352

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 241 VVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTLNPKWLKIQFTTMFVGVNLTFFPQHFLGLAG 320
Cdd:MTH00223 353 IILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAG 432

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 926663203 321 MPRRYSDYPDSYTSWNVVSSLGSTISFIGIIFLIFIIWESMISNRTVLFP 370
Cdd:MTH00223 433 MPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVWS 482
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-370 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 619.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203   1 SLVESGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGASSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLL 80
Cdd:MTH00142 114 AAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILL 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203  81 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIISQESGKKEAFGTLGMIY 160
Cdd:MTH00142 194 LLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIY 273

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 161 AMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTG 240
Cdd:MTH00142 274 AMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTG 353

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 241 VVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTLNPKWLKIQFTTMFVGVNLTFFPQHFLGLAG 320
Cdd:MTH00142 354 IVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAG 433

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 926663203 321 MPRRYSDYPDSYTSWNVVSSLGSTISFIGIIFLIFIIWESMISNRTVLFP 370
Cdd:MTH00142 434 MPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVMWS 483
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-370 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 618.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203   1 SLVESGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGASSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLL 80
Cdd:MTH00116 116 STVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLL 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203  81 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIISQESGKKEAFGTLGMIY 160
Cdd:MTH00116 196 LLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVW 275

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 161 AMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTG 240
Cdd:MTH00116 276 AMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTG 355

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 241 VVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTLNPKWLKIQFTTMFVGVNLTFFPQHFLGLAG 320
Cdd:MTH00116 356 IVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAG 435

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 926663203 321 MPRRYSDYPDSYTSWNVVSSLGSTISFIGIIFLIFIIWESMISNRTVLFP 370
Cdd:MTH00116 436 MPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVLQP 485
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-369 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 558.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203   1 SLVESGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGASSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLL 80
Cdd:MTH00103 116 SMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLL 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203  81 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIISQESGKKEAFGTLGMIY 160
Cdd:MTH00103 196 LLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVW 275

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 161 AMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTG 240
Cdd:MTH00103 276 AMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTG 355

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 241 VVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTLNPKWLKIQFTTMFVGVNLTFFPQHFLGLAG 320
Cdd:MTH00103 356 IVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSG 435

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 926663203 321 MPRRYSDYPDSYTSWNVVSSLGSTISFIGIIFLIFIIWESMISNRTVLF 369
Cdd:MTH00103 436 MPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVLT 484
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 3-370 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 556.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203   3 VESGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGASSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLLLL 82
Cdd:MTH00037 118 VESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLL 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203  83 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIISQESGKKEAFGTLGMIYAM 162
Cdd:MTH00037 198 SLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAM 277

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 163 MAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTGVV 242
Cdd:MTH00037 278 IAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIV 357

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 243 LANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTLNPKWLKIQFTTMFVGVNLTFFPQHFLGLAGMP 322
Cdd:MTH00037 358 LANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMP 437

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 926663203 323 RRYSDYPDSYTSWNVVSSLGSTISFIGIIFLIFIIWESMISNRTVLFP 370
Cdd:MTH00037 438 RRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVISP 485
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-369 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 551.07  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203   1 SLVESGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGASSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLL 80
Cdd:MTH00183 116 SGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLL 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203  81 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIISQESGKKEAFGTLGMIY 160
Cdd:MTH00183 196 LLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVW 275

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 161 AMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTG 240
Cdd:MTH00183 276 AMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTG 355

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 241 VVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTLNPKWLKIQFTTMFVGVNLTFFPQHFLGLAG 320
Cdd:MTH00183 356 IVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAG 435

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 926663203 321 MPRRYSDYPDSYTSWNVVSSLGSTISFIGIIFLIFIIWESMISNRTVLF 369
Cdd:MTH00183 436 MPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLS 484
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-368 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 546.42  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203   1 SLVESGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGASSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLL 80
Cdd:MTH00007 113 AAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLL 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203  81 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIISQESGKKEAFGTLGMIY 160
Cdd:MTH00007 193 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIY 272

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 161 AMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTG 240
Cdd:MTH00007 273 AMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTG 352

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 241 VVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTLNPKWLKIQFTTMFVGVNLTFFPQHFLGLAG 320
Cdd:MTH00007 353 IVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSG 432

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 926663203 321 MPRRYSDYPDSYTSWNVVSSLGSTISFIGIIFLIFIIWESMISNRTVL 368
Cdd:MTH00007 433 MPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVI 480
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-368 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 541.07  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203   1 SLVESGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGASSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLL 80
Cdd:MTH00077 116 SGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLL 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203  81 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIISQESGKKEAFGTLGMIY 160
Cdd:MTH00077 196 LLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVW 275

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 161 AMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTG 240
Cdd:MTH00077 276 AMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTG 355

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 241 VVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTLNPKWLKIQFTTMFVGVNLTFFPQHFLGLAG 320
Cdd:MTH00077 356 IVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAG 435

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 926663203 321 MPRRYSDYPDSYTSWNVVSSLGSTISFIGIIFLIFIIWESMISNRTVL 368
Cdd:MTH00077 436 MPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREVL 483
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 2-368 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 518.08  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203   2 LVESGAGTGWTVYPPLSAgIAHAGASVDLAIFSLHLAGASSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLLL 81
Cdd:MTH00079 118 FVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLV 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203  82 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIISQESGKKEAFGTLGMIYA 161
Cdd:MTH00079 197 LSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYA 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 162 MMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTGV 241
Cdd:MTH00079 277 ILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGV 356

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 242 VLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTLNPKWLKIQFTTMFVGVNLTFFPQHFLGLAGM 321
Cdd:MTH00079 357 ILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGM 436

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 926663203 322 PRRYSDYPDSYTSWNVVSSLGSTISFIGIIFLIFIIWESMISNRTVL 368
Cdd:MTH00079 437 PRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVL 483
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-344 1.27e-177

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 503.97  E-value: 1.27e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203   1 SLVESGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGASSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLL 80
Cdd:MTH00182 118 AFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLL 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203  81 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIISQESGKKEAFGTLGMIY 160
Cdd:MTH00182 198 LLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVY 277

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 161 AMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTG 240
Cdd:MTH00182 278 AMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTG 357

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 241 VVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTLNPKWLKIQFTTMFVGVNLTFFPQHFLGLAG 320
Cdd:MTH00182 358 VVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAG 437

                        330       340
                 ....*....|....*....|....
gi 926663203 321 MPRRYSDYPDSYTSWNVVSSLGST 344
Cdd:MTH00182 438 FPRRYSDFADAFAGWNLVSSLGSI 461
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-343 5.67e-173

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 492.03  E-value: 5.67e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203   1 SLVESGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGASSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLL 80
Cdd:MTH00184 118 AFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLL 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203  81 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIISQESGKKEAFGTLGMIY 160
Cdd:MTH00184 198 LLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVY 277

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 161 AMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTG 240
Cdd:MTH00184 278 AMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTG 357

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 241 VVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTLNPKWLKIQFTTMFVGVNLTFFPQHFLGLAG 320
Cdd:MTH00184 358 IVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAG 437

                        330       340
                 ....*....|....*....|...
gi 926663203 321 MPRRYSDYPDSYTSWNVVSSLGS 343
Cdd:MTH00184 438 LPRRYSDFHDSFAGWNQISSLGS 460
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 2-361 2.09e-162

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: 462.77  E-value: 2.09e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203   2 LVESGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGASSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLLL 81
Cdd:cd00919  105 LVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLL 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203  82 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIISQESGKKeAFGTLGMIYA 161
Cdd:cd00919  185 LALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGKP-LFGYKLMVYA 263

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 162 MMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTGV 241
Cdd:cd00919  264 FLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGV 343

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 242 VLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTLNPKWLKIQFTTMFVGVNLTFFPQHFLGLAGM 321
Cdd:cd00919  344 VLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGFNLTFFPMHFLGLLGM 423

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 926663203 322 PRRYSDYPDSYTSWNVVSSLGSTISFIGIIFLIFIIWESM 361
Cdd:cd00919  424 PRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-343 1.67e-152

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 440.22  E-value: 1.67e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203   1 SLVESGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGASSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLL 80
Cdd:MTH00026 117 SLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILL 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203  81 LLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIISQESGKKEAFGTLGMIY 160
Cdd:MTH00026 197 LLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVY 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 161 AMMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGT--QLTYSPALLWVLGFVFLFTIGGL 238
Cdd:MTH00026 277 AMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGL 356

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 239 TGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTLNPKWLKIQFTTMFVGVNLTFFPQHFLGL 318
Cdd:MTH00026 357 TGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGL 436

                        330       340
                 ....*....|....*....|....*
gi 926663203 319 AGMPRRYSDYPDSYTSWNVVSSLGS 343
Cdd:MTH00026 437 AGLPRRYADYPDNFEDFNQISSFGS 461
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-344 1.48e-151

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 438.02  E-value: 1.48e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203   2 LVESGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGASSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLLL 81
Cdd:COG0843  119 FVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILIL 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203  82 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIISQESGKKeAFGTLGMIYA 161
Cdd:COG0843  199 LAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLA 277

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 162 MMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTGV 241
Cdd:COG0843  278 TVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGV 357

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 242 VLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTLNPKWLKIQFTTMFVGVNLTFFPQHFLGLAGM 321
Cdd:COG0843  358 MLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGM 437

                        330       340
                 ....*....|....*....|....*
gi 926663203 322 PRRYSDYP--DSYTSWNVVSSLGST 344
Cdd:COG0843  438 PRRYATYPpePGWQPLNLISTIGAF 462
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 2-343 1.87e-148

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: 428.57  E-value: 1.87e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203    2 LVESGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGASSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLLL 81
Cdd:TIGR02891 110 FTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILIL 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203   82 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIISQESGKKeAFGTLGMIYA 161
Cdd:TIGR02891 190 LAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYA 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203  162 MMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTGV 241
Cdd:TIGR02891 269 TVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGV 348

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203  242 VLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTLNPKWLKIQFTTMFVGVNLTFFPQHFLGLAGM 321
Cdd:TIGR02891 349 MLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGM 428

                         330       340
                  ....*....|....*....|....
gi 926663203  322 PRRYSDYPDS--YTSWNVVSSLGS 343
Cdd:TIGR02891 429 PRRYYTYPPQmgFATLNLISTIGA 452
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 6-368 3.55e-137

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 400.59  E-value: 3.55e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203   6 GAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGASSILGAVNFITTTINMRAPGMSLdQTPLFVWAVAITALLLLLSLP 85
Cdd:MTH00048 120 GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLP 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203  86 VLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIISQESGKKEAFGTLGMIYAMMAI 165
Cdd:MTH00048 199 VLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSI 278

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 166 GLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYS-PALLWVLGFVFLFTIGGLTGVVLA 244
Cdd:MTH00048 279 VCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSdPVVWWVVSFIVLFTIGGVTGIVLS 358

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 245 NSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTLNPKWLKIQFTTMFVGVNLTFFPQHFLGLAGMPRR 324
Cdd:MTH00048 359 ASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRR 438

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 926663203 325 YSDYPDSYTSWNVVSSLGSTISFIGIIFLIFIIWESMISNRTVL 368
Cdd:MTH00048 439 VCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEVL 482
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 2-343 1.66e-133

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: 390.79  E-value: 1.66e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203   2 LVESGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGASSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLLL 81
Cdd:cd01662  111 LIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILIL 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203  82 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIISQESGKKeAFGTLGMIYA 161
Cdd:cd01662  191 FAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRKP-LFGYRSMVYA 269

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 162 MMAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTGV 241
Cdd:cd01662  270 TVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGV 349

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 242 VLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTLNPKWLKIQFTTMFVGVNLTFFPQHFLGLAGM 321
Cdd:cd01662  350 MLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFNLTFFPMHILGLMGM 429

                        330       340
                 ....*....|....*....|....
gi 926663203 322 PRRYSDYP--DSYTSWNVVSSLGS 343
Cdd:cd01662  430 PRRVYTYLpgPGWDPLNLISTIGA 453
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 6-344 3.36e-102

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: 308.35  E-value: 3.36e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203    6 GAGTGWTVYPPLSAgiahagasVDLAIFSLHLAGASSILGAVNFITTTINMRAPGMSLdQTPLFVWAVAITALLLLLSLP 85
Cdd:pfam00115 104 GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFP 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203   86 VLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIISQESGKKeAFGTLGMIYAMMAI 165
Cdd:pfam00115 175 VLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLI 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203  166 GLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLT-YSPALLWVLGFVFLFTIGGLTGVVLA 244
Cdd:pfam00115 248 AFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRfRTTPMLFFLGFAFLFIIGGLTGVMLA 327

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203  245 NSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTLNPKWLKIQFTTMFVGVNLTFFPQHFLGLAGMPRR 324
Cdd:pfam00115 328 LPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRR 407

                         330       340
                  ....*....|....*....|....
gi 926663203  325 YS----DYPDSYTSWNVVSSLGST 344
Cdd:pfam00115 408 YAppfiETVPAFQPLNWIRTIGGV 431
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 10-343 1.72e-82

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: 263.64  E-value: 1.72e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203   10 GWTVYPPLSAGIAHAGASVDLAIFSLHLAGASSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLLLLSLPVLAG 89
Cdd:TIGR02882 162 GWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTV 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203   90 AITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIISQESgKKEAFGTLGMIYAMMAIGLLG 169
Cdd:TIGR02882 242 ALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIISTFA-QKRLFGYKSMVWSTVGIAFLS 320

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203  170 FVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTGVVLANSSLD 249
Cdd:TIGR02882 321 FLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASAD 400

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203  250 IILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTLNPKWLKIQFTTMFVGVNLTFFPQHFLGLAGMPRRYSDY- 328
Cdd:TIGR02882 401 YQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYs 480

                         330
                  ....*....|....*.
gi 926663203  329 -PDSYTSWNVVSSLGS 343
Cdd:TIGR02882 481 pSDGWFPLNLISTIGA 496
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 7-330 2.35e-80

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 258.71  E-value: 2.35e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203   7 AGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGASSILGAVNFITTTINMRAPGMSLDQTPLFVWAVAITALLLLLSLPV 86
Cdd:PRK15017 166 AQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPI 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203  87 LAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIISQESgKKEAFGTLGMIYAMMAIG 166
Cdd:PRK15017 246 LTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCIT 324

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 167 LLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLTYSPALLWVLGFVFLFTIGGLTGVVLANS 246
Cdd:PRK15017 325 VLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVP 404

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 247 SLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLTLNPKWLKIQFTTMFVGVNLTFFPQHFLGLAGMPRRYS 326
Cdd:PRK15017 405 GADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLS 484


                 ....
gi 926663203 327 DYPD 330
Cdd:PRK15017 485 QQID 488
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 11-344 5.52e-18

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: 85.03  E-value: 5.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203  11 WTVYPPLsagIAHAGASVDLAIFSLhlagASSILGAVNFITTTINMRA-PGmslDQTPLFVWAVAITALLLLLSLPVLAG 89
Cdd:cd01660  113 YTFYPPL---QAHPLFYIGAALVVV----GSWISGFAMFVTLWRWKKAnPG---KKVPLATFMVVTTMILWLVASLGVAL 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203  90 AITMLLtdrnLNTSFFDpAGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIISQESGKKEAFGTLGMIyAMMAIGLLG 169
Cdd:cd01660  183 EVLFQL----LPWSLGL-VDTVDVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARL-AFILFLLFS 256

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 170 FVVWAHHMFT-VGMDVDTRAYFTSATMIIAVPTGIKIFSWLATL-HGTQLTYSPALLW---------------VLGFVFl 232
Cdd:cd01660  257 TPVGFHHQFAdPGIGPGWKFIHMVLTFMVALPSLLTAFTVFASLeIAGRLRGGKGLFGwiralpwgdpmflalFLAMLM- 335

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926663203 233 FTIGGLTGVVLANSSLDIILHDTYYVVAHFHyvLSMGAVFAIMAGFIQWY--PLFTGLTLNPKWL-KIQFTTMFVGVNLT 309
Cdd:cd01660  336 FIPGGAGGIINASYQLNYVVHNTAWVPGHFH--LTVGGAVALTFMAVAYWlvPHLTGRELAAKRLaLAQPWLWFVGMTIM 413

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 926663203 310 FFPQHFLGLAGMPRR--YSDYPDSY-----TSWNVVSSLGST 344
Cdd:cd01660  414 STAMHVAGLLGAPRRtaEAQYGGLPaagewAPYQQLMAIGGT 455
 
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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