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Conserved domains on  [gi|166165013|gb|ABY83857|]
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cytochrome oxidase subunit 1, partial (mitochondrion) [Sibthorpia peregrina]

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 ...
 1-344 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 cd01663:

Pssm-ID: 469701  Cd Length: 488  Bit Score: 644.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013   1 ILGSINFITTISNMRGPGMTMHRLPLFVWSVLVTAFPLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWF 80
Cdd:cd01663  149 ILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWF 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013  81 FGHPEVYILILPGSGIISHIVSTFSG-KPVFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTG 159
Cdd:cd01663  229 FGHPEVYILILPGFGIISHIISTFSGkKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTG 308

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 160 IKIFSWIATMWGGSIQYKTPMLFAVGFIFLFTIGGLTGIVLANSGLDIALHDTYYVVAHFHYVLSMGAVFALFAGFHYWV 239
Cdd:cd01663  309 IKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWF 388

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 240 GKIFGRTYPETLGKIHFWITFIGVNLTFFPMHFLGLSGMPRRIPDYPDAYAGWNALSSFGSYISVVGICRFFVVVTITSS 319
Cdd:cd01663  389 PKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFV 468

                        330       340
                 ....*....|....*....|....*
gi 166165013 320 SGknkRCAPSPWavEQNPPHPEWMV 344
Cdd:cd01663  469 SG---RKVIFNV--GEGSTSLEWTL 488
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-344 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: 644.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013   1 ILGSINFITTISNMRGPGMTMHRLPLFVWSVLVTAFPLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWF 80
Cdd:cd01663  149 ILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWF 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013  81 FGHPEVYILILPGSGIISHIVSTFSG-KPVFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTG 159
Cdd:cd01663  229 FGHPEVYILILPGFGIISHIISTFSGkKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTG 308

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 160 IKIFSWIATMWGGSIQYKTPMLFAVGFIFLFTIGGLTGIVLANSGLDIALHDTYYVVAHFHYVLSMGAVFALFAGFHYWV 239
Cdd:cd01663  309 IKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWF 388

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 240 GKIFGRTYPETLGKIHFWITFIGVNLTFFPMHFLGLSGMPRRIPDYPDAYAGWNALSSFGSYISVVGICRFFVVVTITSS 319
Cdd:cd01663  389 PKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFV 468

                        330       340
                 ....*....|....*....|....*
gi 166165013 320 SGknkRCAPSPWavEQNPPHPEWMV 344
Cdd:cd01663  469 SG---RKVIFNV--GEGSTSLEWTL 488
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-352 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 579.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013   1 ILGSINFITTISNMRGPGMTMHRLPLFVWSVLVTAFPLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWF 80
Cdd:MTH00153 156 ILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013  81 FGHPEVYILILPGSGIISHIVSTFSGKP-VFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTG 159
Cdd:MTH00153 236 FGHPEVYILILPGFGMISHIISQESGKKeTFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTG 315

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 160 IKIFSWIATMWGGSIQYKTPMLFAVGFIFLFTIGGLTGIVLANSGLDIALHDTYYVVAHFHYVLSMGAVFALFAGFHYWV 239
Cdd:MTH00153 316 IKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWF 395

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 240 GKIFGRTYPETLGKIHFWITFIGVNLTFFPMHFLGLSGMPRRIPDYPDAYAGWNALSSFGSYISVVGICRFFVVVTITSS 319
Cdd:MTH00153 396 PLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMI 475

                        330       340       350
                 ....*....|....*....|....*....|...
gi 166165013 320 SgknKRCAPSPwavEQNPPHPEWMVQSPPAFHT 352
Cdd:MTH00153 476 S---KRPVLFS---LNLSSSIEWLQNLPPAEHS 502
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-351 5.01e-169

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: 480.18  E-value: 5.01e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013    1 ILGSINFITTISNMRGPGMTMHRLPLFVWSVLVTAFPLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWF 80
Cdd:TIGR02891 151 ILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWF 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013   81 FGHPEVYILILPGSGIISHIVSTFSGKPVFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGI 160
Cdd:TIGR02891 231 FGHPEVYIIFLPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGV 310

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013  161 KIFSWIATMWGGSIQYKTPMLFAVGFIFLFTIGGLTGIVLANSGLDIALHDTYYVVAHFHYVLSMGAVFALFAGFHYWVG 240
Cdd:TIGR02891 311 KVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFP 390

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013  241 KIFGRTYPETLGKIHFWITFIGVNLTFFPMHFLGLSGMPRRIPDYPDA--YAGWNALSSFGSYISVVGICRFFVVVTITS 318
Cdd:TIGR02891 391 KVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSL 470

                         330       340       350
                  ....*....|....*....|....*....|...
gi 166165013  319 SSGknKRCAPSPWAVEQnpphPEWMVQSPPAFH 351
Cdd:TIGR02891 471 RKG--PKAGANPWGATT----LEWTTSSPPPAH 497
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-351 6.27e-168

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 478.85  E-value: 6.27e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013   1 ILGSINFITTISNMRGPGMTMHRLPLFVWSVLVTAFPLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWF 80
Cdd:COG0843  160 ILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWF 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013  81 FGHPEVYILILPGSGIISHIVSTFSGKPVFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGI 160
Cdd:COG0843  240 FGHPEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGV 319

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 161 KIFSWIATMWGGSIQYKTPMLFAVGFIFLFTIGGLTGIVLANSGLDIALHDTYYVVAHFHYVLSMGAVFALFAGFHYWVG 240
Cdd:COG0843  320 KVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFP 399

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 241 KIFGRTYPETLGKIHFWITFIGVNLTFFPMHFLGLSGMPRRIPDYP--DAYAGWNALSSFGSYISVVGICRFFVVVTIts 318
Cdd:COG0843  400 KMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVV-- 477

                        330       340       350
                 ....*....|....*....|....*....|...
gi 166165013 319 SSGKNKRCAPSPWaveqNPPHPEWMVQSPPAFH 351
Cdd:COG0843  478 SLRKGPKAGGNPW----GARTLEWATPSPPPLY 506
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-302 5.36e-115

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: 340.32  E-value: 5.36e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013    1 ILGSINFITTISNMRGPGMTMhRLPLFVWSVLVTAFPLLLSLPVLAGAITMLLTDRNFNttffdpAGGGDPILYQHLFWF 80
Cdd:pfam00115 133 LLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWW 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013   81 FGHPEVYILILPGSGIISHIVSTFSGKPVFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGI 160
Cdd:pfam00115 206 FGHPEVYILILPAFGIIYYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGV 285

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013  161 KIFSWIATMWGGSIQ-YKTPMLFAVGFIFLFTIGGLTGIVLANSGLDIALHDTYYVVAHFHYVLSMGAVFALFAGFHYWV 239
Cdd:pfam00115 286 KVFNWLATLWGGWIRfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWL 365

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 166165013  240 GKIFGRTYPETLGKIHFWITFIGVNLTFFPMHFLGLSGMPRRIP----DYPDAYAGWNALSSFGSYI 302
Cdd:pfam00115 366 PKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-344 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: 644.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013   1 ILGSINFITTISNMRGPGMTMHRLPLFVWSVLVTAFPLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWF 80
Cdd:cd01663  149 ILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWF 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013  81 FGHPEVYILILPGSGIISHIVSTFSG-KPVFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTG 159
Cdd:cd01663  229 FGHPEVYILILPGFGIISHIISTFSGkKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTG 308

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 160 IKIFSWIATMWGGSIQYKTPMLFAVGFIFLFTIGGLTGIVLANSGLDIALHDTYYVVAHFHYVLSMGAVFALFAGFHYWV 239
Cdd:cd01663  309 IKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWF 388

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 240 GKIFGRTYPETLGKIHFWITFIGVNLTFFPMHFLGLSGMPRRIPDYPDAYAGWNALSSFGSYISVVGICRFFVVVTITSS 319
Cdd:cd01663  389 PKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFV 468

                        330       340
                 ....*....|....*....|....*
gi 166165013 320 SGknkRCAPSPWavEQNPPHPEWMV 344
Cdd:cd01663  469 SG---RKVIFNV--GEGSTSLEWTL 488
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-352 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 579.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013   1 ILGSINFITTISNMRGPGMTMHRLPLFVWSVLVTAFPLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWF 80
Cdd:MTH00153 156 ILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013  81 FGHPEVYILILPGSGIISHIVSTFSGKP-VFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTG 159
Cdd:MTH00153 236 FGHPEVYILILPGFGMISHIISQESGKKeTFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTG 315

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 160 IKIFSWIATMWGGSIQYKTPMLFAVGFIFLFTIGGLTGIVLANSGLDIALHDTYYVVAHFHYVLSMGAVFALFAGFHYWV 239
Cdd:MTH00153 316 IKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWF 395

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 240 GKIFGRTYPETLGKIHFWITFIGVNLTFFPMHFLGLSGMPRRIPDYPDAYAGWNALSSFGSYISVVGICRFFVVVTITSS 319
Cdd:MTH00153 396 PLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMI 475

                        330       340       350
                 ....*....|....*....|....*....|...
gi 166165013 320 SgknKRCAPSPwavEQNPPHPEWMVQSPPAFHT 352
Cdd:MTH00153 476 S---KRPVLFS---LNLSSSIEWLQNLPPAEHS 502
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-352 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 547.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013   1 ILGSINFITTISNMRGPGMTMHRLPLFVWSVLVTAFPLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWF 80
Cdd:MTH00167 158 ILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWF 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013  81 FGHPEVYILILPGSGIISHIVSTFSGKP-VFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTG 159
Cdd:MTH00167 238 FGHPEVYILILPGFGMISHIVVYYSGKKePFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTG 317

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 160 IKIFSWIATMWGGSIQYKTPMLFAVGFIFLFTIGGLTGIVLANSGLDIALHDTYYVVAHFHYVLSMGAVFALFAGFHYWV 239
Cdd:MTH00167 318 IKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWF 397

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 240 GKIFGRTYPETLGKIHFWITFIGVNLTFFPMHFLGLSGMPRRIPDYPDAYAGWNALSSFGSYISVVGICRFFVVVTITSS 319
Cdd:MTH00167 398 PLFTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFS 477

                        330       340       350
                 ....*....|....*....|....*....|...
gi 166165013 320 SGKnkrcapSPWAVEQNPPHPEWMVQSPPAFHT 352
Cdd:MTH00167 478 SKR------KLLPVELTSTNVEWLHGCPPPHHT 504
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-352 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 543.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013   1 ILGSINFITTISNMRGPGMTMHRLPLFVWSVLVTAFPLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWF 80
Cdd:MTH00223 155 ILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWF 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013  81 FGHPEVYILILPGSGIISHIVSTFSGK-PVFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTG 159
Cdd:MTH00223 235 FGHPEVYILILPGFGMISHIVSHYSSKkEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 314

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 160 IKIFSWIATMWGGSIQYKTPMLFAVGFIFLFTIGGLTGIVLANSGLDIALHDTYYVVAHFHYVLSMGAVFALFAGFHYWV 239
Cdd:MTH00223 315 IKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWF 394

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 240 GKIFGRTYPETLGKIHFWITFIGVNLTFFPMHFLGLSGMPRRIPDYPDAYAGWNALSSFGSYISVVGICRFFVVVTITSS 319
Cdd:MTH00223 395 PLFTGVTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFV 474

                        330       340       350
                 ....*....|....*....|....*....|...
gi 166165013 320 SGKnkrcapSPWAVEQNPPHPEWMVQSPPAFHT 352
Cdd:MTH00223 475 SQR------SVVWSGHLSTSLEWDNLLPADFHN 501
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-352 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 521.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013   1 ILGSINFITTISNMRGPGMTMHRLPLFVWSVLVTAFPLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWF 80
Cdd:MTH00116 158 ILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWF 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013  81 FGHPEVYILILPGSGIISHIVSTFSGKP-VFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTG 159
Cdd:MTH00116 238 FGHPEVYILILPGFGIISHIVTYYAGKKePFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTG 317

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 160 IKIFSWIATMWGGSIQYKTPMLFAVGFIFLFTIGGLTGIVLANSGLDIALHDTYYVVAHFHYVLSMGAVFALFAGFHYWV 239
Cdd:MTH00116 318 IKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWF 397

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 240 GKIFGRTYPETLGKIHFWITFIGVNLTFFPMHFLGLSGMPRRIPDYPDAYAGWNALSSFGSYISVVGIcrfFVVVTITSS 319
Cdd:MTH00116 398 PLFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAV---IMLMFIIWE 474

                        330       340       350
                 ....*....|....*....|....*....|...
gi 166165013 320 SGKNKRCAPSPWAVEQNpphPEWMVQSPPAFHT 352
Cdd:MTH00116 475 AFSSKRKVLQPELTTTN---IEWIHGCPPPYHT 504
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-352 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 513.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013   1 ILGSINFITTISNMRGPGMTMHRLPLFVWSVLVTAFPLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWF 80
Cdd:MTH00142 156 ILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWF 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013  81 FGHPEVYILILPGSGIISHIVSTFSGKP-VFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTG 159
Cdd:MTH00142 236 FGHPEVYILILPGFGMISHIINHYSGKKeVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTG 315

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 160 IKIFSWIATMWGGSIQYKTPMLFAVGFIFLFTIGGLTGIVLANSGLDIALHDTYYVVAHFHYVLSMGAVFALFAGFHYWV 239
Cdd:MTH00142 316 IKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWF 395

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 240 GKIFGRTYPETLGKIHFWITFIGVNLTFFPMHFLGLSGMPRRIPDYPDAYAGWNALSSFGSYISVVGICRFfvVVTITSS 319
Cdd:MTH00142 396 PLFTGLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMF--VFIVWES 473

                        330       340       350
                 ....*....|....*....|....*....|...
gi 166165013 320 SGKNKRCAPSPWAVEQNpphpEWMVQSPPAFHT 352
Cdd:MTH00142 474 FVSQRLVMWSSHLSTSL----EWSHRLPPDFHT 502
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-352 2.77e-176

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 499.73  E-value: 2.77e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013   1 ILGSINFITTISNMRGPGMTMHRLPLFVWSVLVTAFPLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWF 80
Cdd:MTH00182 160 ILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWF 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013  81 FGHPEVYILILPGSGIISHIVSTFSGK-PVFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTG 159
Cdd:MTH00182 240 FGHPEVYILILPGFGMISQIIPTFVAKkQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 319

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 160 IKIFSWIATMWGGSIQYKTPMLFAVGFIFLFTIGGLTGIVLANSGLDIALHDTYYVVAHFHYVLSMGAVFALFAGFHYWV 239
Cdd:MTH00182 320 IKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWF 399

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 240 GKIFGRTYPETLGKIHFWITFIGVNLTFFPMHFLGLSGMPRRIPDYPDAYAGWNALSSFGSYISVVGICRFFVVvtITSS 319
Cdd:MTH00182 400 GKITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYI--IYDA 477

                        330       340       350
                 ....*....|....*....|....*....|...
gi 166165013 320 SGKNKRCAPSPWAVEQNPPHPEWMVQSPPAFHT 352
Cdd:MTH00182 478 YVREEKFIGWKEGTGESWASLEWVHSSPPLFHT 510
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-352 1.61e-174

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 495.12  E-value: 1.61e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013   1 ILGSINFITTISNMRGPGMTMHRLPLFVWSVLVTAFPLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWF 80
Cdd:MTH00184 160 ILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWF 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013  81 FGHPEVYILILPGSGIISHIVSTFSGKP-VFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTG 159
Cdd:MTH00184 240 FGHPEVYILILPGFGIISQIIPTFAAKKqIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 319

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 160 IKIFSWIATMWGGSIQYKTPMLFAVGFIFLFTIGGLTGIVLANSGLDIALHDTYYVVAHFHYVLSMGAVFALFAGFHYWV 239
Cdd:MTH00184 320 IKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWF 399

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 240 GKIFGRTYPETLGKIHFWITFIGVNLTFFPMHFLGLSGMPRRIPDYPDAYAGWNALSSFGSYISVVGICRFFVVVTitss 319
Cdd:MTH00184 400 GKITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVY---- 475

                        330       340       350
                 ....*....|....*....|....*....|....
gi 166165013 320 SGKNKRCAPSPWAVEQNP-PHPEWMVQSPPAFHT 352
Cdd:MTH00184 476 DAYVREIKFVGWVEDSGHyPSLEWAQTSPPAHHT 509
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-351 5.01e-169

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: 480.18  E-value: 5.01e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013    1 ILGSINFITTISNMRGPGMTMHRLPLFVWSVLVTAFPLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWF 80
Cdd:TIGR02891 151 ILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWF 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013   81 FGHPEVYILILPGSGIISHIVSTFSGKPVFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGI 160
Cdd:TIGR02891 231 FGHPEVYIIFLPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGV 310

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013  161 KIFSWIATMWGGSIQYKTPMLFAVGFIFLFTIGGLTGIVLANSGLDIALHDTYYVVAHFHYVLSMGAVFALFAGFHYWVG 240
Cdd:TIGR02891 311 KVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFP 390

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013  241 KIFGRTYPETLGKIHFWITFIGVNLTFFPMHFLGLSGMPRRIPDYPDA--YAGWNALSSFGSYISVVGICRFFVVVTITS 318
Cdd:TIGR02891 391 KVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSL 470

                         330       340       350
                  ....*....|....*....|....*....|...
gi 166165013  319 SSGknKRCAPSPWAVEQnpphPEWMVQSPPAFH 351
Cdd:TIGR02891 471 RKG--PKAGANPWGATT----LEWTTSSPPPAH 497
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-351 6.27e-168

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 478.85  E-value: 6.27e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013   1 ILGSINFITTISNMRGPGMTMHRLPLFVWSVLVTAFPLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWF 80
Cdd:COG0843  160 ILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWF 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013  81 FGHPEVYILILPGSGIISHIVSTFSGKPVFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGI 160
Cdd:COG0843  240 FGHPEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGV 319

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 161 KIFSWIATMWGGSIQYKTPMLFAVGFIFLFTIGGLTGIVLANSGLDIALHDTYYVVAHFHYVLSMGAVFALFAGFHYWVG 240
Cdd:COG0843  320 KVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFP 399

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 241 KIFGRTYPETLGKIHFWITFIGVNLTFFPMHFLGLSGMPRRIPDYP--DAYAGWNALSSFGSYISVVGICRFFVVVTIts 318
Cdd:COG0843  400 KMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVV-- 477

                        330       340       350
                 ....*....|....*....|....*....|...
gi 166165013 319 SSGKNKRCAPSPWaveqNPPHPEWMVQSPPAFH 351
Cdd:COG0843  478 SLRKGPKAGGNPW----GARTLEWATPSPPPLY 506
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-314 5.31e-166

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: 471.24  E-value: 5.31e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013   1 ILGSINFITTISNMRGPGMTMHRLPLFVWSVLVTAFPLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWF 80
Cdd:cd00919  146 ILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWF 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013  81 FGHPEVYILILPGSGIISHIVSTFSGKPVFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGI 160
Cdd:cd00919  226 FGHPEVYILILPAFGAISEIIPTFSGKPLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGI 305

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 161 KIFSWIATMWGGSIQYKTPMLFAVGFIFLFTIGGLTGIVLANSGLDIALHDTYYVVAHFHYVLSMGAVFALFAGFHYWVG 240
Cdd:cd00919  306 KVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFP 385

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 166165013 241 KIFGRTYPETLGKIHFWITFIGVNLTFFPMHFLGLSGMPRRIPDYPDAYAGWNALSSFGSYISVVGICRFFVVV 314
Cdd:cd00919  386 KMTGRMLSEKLGKIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNL 459
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-352 4.66e-165

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 470.85  E-value: 4.66e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013   1 ILGSINFITTISNMRGPGMTMHRLPLFVWSVLVTAFPLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWF 80
Cdd:MTH00037 158 ILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWF 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013  81 FGHPEVYILILPGSGIISHIVSTFSGKP-VFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTG 159
Cdd:MTH00037 238 FGHPEVYILILPGFGMISHVIAHYSGKQePFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 317

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 160 IKIFSWIATMWGGSIQYKTPMLFAVGFIFLFTIGGLTGIVLANSGLDIALHDTYYVVAHFHYVLSMGAVFALFAGFHYWV 239
Cdd:MTH00037 318 IKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWF 397

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 240 GKIFGRTYPETLGKIHFWITFIGVNLTFFPMHFLGLSGMPRRIPDYPDAYAGWNALSSFGSYISVVGICRFFVVVTITSS 319
Cdd:MTH00037 398 PLFSGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFA 477

                        330       340       350
                 ....*....|....*....|....*....|....
gi 166165013 320 SgknKRCAPSPWAVEQNpphPEWMVQS-PPAFHT 352
Cdd:MTH00037 478 S---QREVISPEFSSSS---LEWQYSSfPPSHHT 505
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-352 1.19e-161

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 462.04  E-value: 1.19e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013   1 ILGSINFITTISNMRGPGMTMHRLPLFVWSVLVTAFPLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWF 80
Cdd:MTH00103 158 ILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWF 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013  81 FGHPEVYILILPGSGIISHIVSTFSGKP-VFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTG 159
Cdd:MTH00103 238 FGHPEVYILILPGFGMISHIVTYYSGKKePFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTG 317

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 160 IKIFSWIATMWGGSIQYKTPMLFAVGFIFLFTIGGLTGIVLANSGLDIALHDTYYVVAHFHYVLSMGAVFALFAGFHYWV 239
Cdd:MTH00103 318 VKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWF 397

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 240 GKIFGRTYPETLGKIHFWITFIGVNLTFFPMHFLGLSGMPRRIPDYPDAYAGWNALSSFGSYISVVGIcrfFVVVTITSS 319
Cdd:MTH00103 398 PLFSGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAV---MLMIFMIWE 474

                        330       340       350
                 ....*....|....*....|....*....|...
gi 166165013 320 SGKNKRcapSPWAVEQNPPHPEWMVQSPPAFHT 352
Cdd:MTH00103 475 AFASKR---EVLTVELTTTNLEWLHGCPPPYHT 504
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-352 3.89e-161

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 460.93  E-value: 3.89e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013   1 ILGSINFITTISNMRGPGMTMHRLPLFVWSVLVTAFPLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWF 80
Cdd:MTH00183 158 ILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWF 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013  81 FGHPEVYILILPGSGIISHIVSTFSGKP-VFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTG 159
Cdd:MTH00183 238 FGHPEVYILILPGFGMISHIVAYYSGKKePFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTG 317

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 160 IKIFSWIATMWGGSIQYKTPMLFAVGFIFLFTIGGLTGIVLANSGLDIALHDTYYVVAHFHYVLSMGAVFALFAGFHYWV 239
Cdd:MTH00183 318 VKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWF 397

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 240 GKIFGRTYPETLGKIHFWITFIGVNLTFFPMHFLGLSGMPRRIPDYPDAYAGWNALSSFGSYISVVGICRFFVVVTITSS 319
Cdd:MTH00183 398 PLFSGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFA 477

                        330       340       350
                 ....*....|....*....|....*....|...
gi 166165013 320 SGKNKRcapspwAVEQNPPHPEWMVQSPPAFHT 352
Cdd:MTH00183 478 AKREVL------SVELTSTNVEWLHGCPPPYHT 504
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-352 7.71e-160

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 457.48  E-value: 7.71e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013   1 ILGSINFITTISNMRGPGMTMHRLPLFVWSVLVTAFPLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWF 80
Cdd:MTH00077 158 ILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWF 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013  81 FGHPEVYILILPGSGIISHIVSTFSGKP-VFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTG 159
Cdd:MTH00077 238 FGHPEVYILILPGFGMISHIVTYYSAKKePFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTG 317

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 160 IKIFSWIATMWGGSIQYKTPMLFAVGFIFLFTIGGLTGIVLANSGLDIALHDTYYVVAHFHYVLSMGAVFALFAGFHYWV 239
Cdd:MTH00077 318 VKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWF 397

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 240 GKIFGRTYPETLGKIHFWITFIGVNLTFFPMHFLGLSGMPRRIPDYPDAYAGWNALSSFGSYISVVGICRFFVVVTITSS 319
Cdd:MTH00077 398 PLFSGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFS 477

                        330       340       350
                 ....*....|....*....|....*....|...
gi 166165013 320 SgknKRCAPSPwavEQNPPHPEWMVQSPPAFHT 352
Cdd:MTH00077 478 S---KREVLTT---ELTSTNIEWLHGCPPPYHT 504
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-314 3.19e-159

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 455.68  E-value: 3.19e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013   1 ILGSINFITTISNMRGPGMTMHRLPLFVWSVLVTAFPLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWF 80
Cdd:MTH00079 158 ILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWF 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013  81 FGHPEVYILILPGSGIISHIVSTFSGKP-VFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTG 159
Cdd:MTH00079 238 FGHPEVYILILPAFGIISQSTLYLTGKKeVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTG 317

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 160 IKIFSWIATMWGGSIQYKTPMLFAVGFIFLFTIGGLTGIVLANSGLDIALHDTYYVVAHFHYVLSMGAVFALFAGFHYWV 239
Cdd:MTH00079 318 VKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWW 397

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 166165013 240 GKIFGRTYPETLGKIHFWITFIGVNLTFFPMHFLGLSGMPRRIPDYPDAYAGWNALSSFGSYISVVGICRFFVVV 314
Cdd:MTH00079 398 PFMTGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVL 472
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-314 1.03e-157

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 452.05  E-value: 1.03e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013   1 ILGSINFITTISNMRGPGMTMHRLPLFVWSVLVTAFPLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWF 80
Cdd:MTH00007 155 ILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013  81 FGHPEVYILILPGSGIISHIVSTFSGKP-VFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTG 159
Cdd:MTH00007 235 FGHPEVYILILPGFGAISHIVTHYAGKLePFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 314

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 160 IKIFSWIATMWGGSIQYKTPMLFAVGFIFLFTIGGLTGIVLANSGLDIALHDTYYVVAHFHYVLSMGAVFALFAGFHYWV 239
Cdd:MTH00007 315 IKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWF 394

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 166165013 240 GKIFGRTYPETLGKIHFWITFIGVNLTFFPMHFLGLSGMPRRIPDYPDAYAGWNALSSFGSYISVVGICRFFVVV 314
Cdd:MTH00007 395 PLFTGLTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFIL 469
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-351 3.16e-150

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: 432.39  E-value: 3.16e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013   1 ILGSINFITTISNMRGPGMTMHRLPLFVWSVLVTAFPLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWF 80
Cdd:cd01662  152 LLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWI 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013  81 FGHPEVYILILPGSGIISHIVSTFSGKPVFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGI 160
Cdd:cd01662  232 FGHPEVYILILPAFGIFSEIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGV 311

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 161 KIFSWIATMWGGSIQYKTPMLFAVGFIFLFTIGGLTGIVLANSGLDIALHDTYYVVAHFHYVLSMGAVFALFAGFHYWVG 240
Cdd:cd01662  312 KIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFP 391

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 241 KIFGRTYPETLGKIHFWITFIGVNLTFFPMHFLGLSGMPRRIPDYP--DAYAGWNALSSFGSYISVVGICRFFVVVTITS 318
Cdd:cd01662  392 KMFGRMLNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLINVIVSI 471

                        330       340       350
                 ....*....|....*....|....*....|...
gi 166165013 319 SSGKnKRCAPSPWaveqNPPHPEWMVQSPPAFH 351
Cdd:cd01662  472 RKGK-RDATGDPW----GARTLEWATSSPPPAY 499
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-314 4.25e-145

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 420.96  E-value: 4.25e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013   1 ILGSINFITTISNMRGPGMTMHRLPLFVWSVLVTAFPLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWF 80
Cdd:MTH00026 159 ILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWF 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013  81 FGHPEVYILILPGSGIISHIVSTFS-GKPVFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTG 159
Cdd:MTH00026 239 FGHPEVYILILPGFGIISQILSLFSyKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTG 318

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 160 IKIFSWIATMWGG--SIQYKTPMLFAVGFIFLFTIGGLTGIVLANSGLDIALHDTYYVVAHFHYVLSMGAVFALFAGFHY 237
Cdd:MTH00026 319 IKIFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYL 398

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 166165013 238 WVGKIFGRTYPETLGKIHFWITFIGVNLTFFPMHFLGLSGMPRRIPDYPDAYAGWNALSSFGSYISVVGICRFFVVV 314
Cdd:MTH00026 399 WFGKITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVI 475
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-324 9.92e-116

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 345.12  E-value: 9.92e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013   1 ILGSINFITTISNMRGPGMTmHRLPLFVWSVLVTAFPLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWF 80
Cdd:MTH00048 157 LFGSINFICTIYSAFMTNVF-SRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWF 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013  81 FGHPEVYILILPGSGIISHIVSTFSGKP-VFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTG 159
Cdd:MTH00048 236 FGHPEVYVLILPGFGIISHICLSLSNNDdPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTG 315

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 160 IKIFSWIATMWGGSIQYKTPML-FAVGFIFLFTIGGLTGIVLANSGLDIALHDTYYVVAHFHYVLSMGAVFALFAGFHYW 238
Cdd:MTH00048 316 IKVFSWLYMLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWW 395

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 239 VGKIFGRTYPETLGKIHFWITFIGVNLTFFPMHFLGLSGMPRRIPDYPDAYAGWNALSSFGSYISVVGICrFFVVVTITS 318
Cdd:MTH00048 396 WPLITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGC-FFVFILWES 474


                 ....*.
gi 166165013 319 SSGKNK 324
Cdd:MTH00048 475 LVVKNE 480
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-302 5.36e-115

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: 340.32  E-value: 5.36e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013    1 ILGSINFITTISNMRGPGMTMhRLPLFVWSVLVTAFPLLLSLPVLAGAITMLLTDRNFNttffdpAGGGDPILYQHLFWF 80
Cdd:pfam00115 133 LLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWW 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013   81 FGHPEVYILILPGSGIISHIVSTFSGKPVFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGI 160
Cdd:pfam00115 206 FGHPEVYILILPAFGIIYYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGV 285

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013  161 KIFSWIATMWGGSIQ-YKTPMLFAVGFIFLFTIGGLTGIVLANSGLDIALHDTYYVVAHFHYVLSMGAVFALFAGFHYWV 239
Cdd:pfam00115 286 KVFNWLATLWGGWIRfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWL 365

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 166165013  240 GKIFGRTYPETLGKIHFWITFIGVNLTFFPMHFLGLSGMPRRIP----DYPDAYAGWNALSSFGSYI 302
Cdd:pfam00115 366 PKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 2-351 4.00e-86

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 272.96  E-value: 4.00e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013   2 LGSINFITTISNMRGPGMTMHRLPLFVWSVLVTAFPLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFF 81
Cdd:PRK15017 203 LTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAW 282

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013  82 GHPEVYILILPGSGIISHIVSTFSGKPVFGYLGMVYAMISIGVLGFLVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIK 161
Cdd:PRK15017 283 GHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVK 362

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 162 IFSWIATMWGGSIQYKTPMLFAVGFIFLFTIGGLTGIVLANSGLDIALHDTYYVVAHFHYVLSMGAVFALFAGFHYWVGK 241
Cdd:PRK15017 363 IFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPK 442

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 242 IFGRTYPETLGKIHFWITFIGVNLTFFPMHFLGLSGMPRRIPDYPD-AYAGWNALSSFGSYISVVGI-CRFFVVVTITSS 319
Cdd:PRK15017 443 AFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDpQFHTMLMIAASGAALIALGIlCQVIQMYVSIRD 522

                        330       340       350
                 ....*....|....*....|....*....|..
gi 166165013 320 SGKNKRCAPSPWAVEQnpphPEWMVQSPPAFH 351
Cdd:PRK15017 523 RDQNRDLTGDPWGGRT----LEWATSSPPPFY 550
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 70-317 4.92e-24

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: 102.36  E-value: 4.92e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013  70 DPILYQHLFWFFGHPEVYILILPGSGIISHIVSTFSGKPVFGYLGMVYAMISIGVLGFLVWAHHMFT-VGLDVDTRAYFT 148
Cdd:cd01660  200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARLAFILFLLFSTPVGFHHQFAdPGIGPGWKFIHM 279

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 149 AATMIIAVPTGIKIFSWIATM--------------WGGSIQYKTPMLFAVGF-IFLFTIGGLTGIVLANSGLDIALHDTY 213
Cdd:cd01660  280 VLTFMVALPSLLTAFTVFASLeiagrlrggkglfgWIRALPWGDPMFLALFLaMLMFIPGGAGGIINASYQLNYVVHNTA 359

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166165013 214 YVVAHFHyvLSMGAVFAL-FAGFHYW-VGKIFGRTYP-ETLGKIHFWITFIGVNLTFFPMHFLGLSGMPRR--IPDYPDA 288
Cdd:cd01660  360 WVPGHFH--LTVGGAVALtFMAVAYWlVPHLTGRELAaKRLALAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGGL 437

                        250       260       270
                 ....*....|....*....|....*....|....
gi 166165013 289 Y-----AGWNALSSFGSYISVVGICRFFVVVTIT 317
Cdd:cd01660  438 PaagewAPYQQLMAIGGTILFVSGALFLYILFRT 471
 
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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