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Conserved domains on  [gi|78103085|gb|ABB21732|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Ornithomya fringillina]

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 ...
 1-252 1.01e-173

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: 488.22  E-value: 1.01e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085    1 GFGMISHIISHESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00153 248 GFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 327

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085   81 TQLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIY 160
Cdd:MTH00153 328 SQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKW 407

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085  161 LKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNIISSIGSTISFLGILYFFFIIWESIMSQRLVMYPIQLN 240
Cdd:MTH00153 408 LKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLS 487

                        250
                 ....*....|..
gi 78103085  241 SSIEWFQNTPPA 252
Cdd:MTH00153 488 SSIEWLQNLPPA 499
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-252 1.01e-173

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 488.22  E-value: 1.01e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085    1 GFGMISHIISHESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00153 248 GFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 327

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085   81 TQLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIY 160
Cdd:MTH00153 328 SQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKW 407

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085  161 LKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNIISSIGSTISFLGILYFFFIIWESIMSQRLVMYPIQLN 240
Cdd:MTH00153 408 LKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLS 487

                        250
                 ....*....|..
gi 78103085  241 SSIEWFQNTPPA 252
Cdd:MTH00153 488 SSIEWLQNLPPA 499
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-245 5.06e-144

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: 411.88  E-value: 5.06e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085   1 GFGMISHIISHESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:cd01663 241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085  81 TQLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIY 160
Cdd:cd01663 321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085 161 LKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNIISSIGSTISFLGILYFFFIIWESIMSQRLVMYPI-QL 239
Cdd:cd01663 401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVgEG 480


                ....*.
gi 78103085 240 NSSIEW 245
Cdd:cd01663 481 STSLEW 486
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-251 1.96e-79

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 248.50  E-value: 1.96e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085   1 GFGMISHIISHESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:COG0843 252 AFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWR 330

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085  81 TQLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIY 160
Cdd:COG0843 331 GRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERL 410

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085 161 LKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTSWNIISSIGSTISFLGILYFFFIIWESIMSQRLV-MYPI 237
Cdd:COG0843 411 GKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPKAgGNPW 490

                       250
                ....*....|....
gi 78103085 238 QLNsSIEWFQNTPP 251
Cdd:COG0843 491 GAR-TLEWATPSPP 503
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-251 3.63e-78

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: 244.05  E-value: 3.63e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085     1 GFGMISHIISHESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:TIGR02891 243 AFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWG 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085    81 TQLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIY 160
Cdd:TIGR02891 322 GSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERL 401

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085   161 LKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTSWNIISSIGSTISFLGILYFFFIIWESIMSQRLVMYPIQ 238
Cdd:TIGR02891 402 GRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGANPW 481

                         250
                  ....*....|...
gi 78103085   239 LNSSIEWFQNTPP 251
Cdd:TIGR02891 482 GATTLEWTTSSPP 494
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-193 2.59e-54

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: 180.46  E-value: 2.59e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085     1 GFGMISHIISHESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:pfam00115 218 AFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWG 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085    81 TQL-IYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSI 159
Cdd:pfam00115 297 GWIrFRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEK 376

                         170       180       190
                  ....*....|....*....|....*....|....
gi 78103085   160 YLKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSD 193
Cdd:pfam00115 377 LGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAP 410
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-252 1.01e-173

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 488.22  E-value: 1.01e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085    1 GFGMISHIISHESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00153 248 GFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 327

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085   81 TQLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIY 160
Cdd:MTH00153 328 SQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKW 407

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085  161 LKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNIISSIGSTISFLGILYFFFIIWESIMSQRLVMYPIQLN 240
Cdd:MTH00153 408 LKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLS 487

                        250
                 ....*....|..
gi 78103085  241 SSIEWFQNTPPA 252
Cdd:MTH00153 488 SSIEWLQNLPPA 499
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-245 5.06e-144

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: 411.88  E-value: 5.06e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085   1 GFGMISHIISHESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:cd01663 241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085  81 TQLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIY 160
Cdd:cd01663 321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085 161 LKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNIISSIGSTISFLGILYFFFIIWESIMSQRLVMYPI-QL 239
Cdd:cd01663 401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVgEG 480


                ....*.
gi 78103085 240 NSSIEW 245
Cdd:cd01663 481 STSLEW 486
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-252 9.74e-138

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 396.74  E-value: 9.74e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085    1 GFGMISHIISHESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00167 250 GFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHG 329

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085   81 TQLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIY 160
Cdd:MTH00167 330 GKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETW 409

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085  161 LKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNIISSIGSTISFLGILYFFFIIWESIMSQRLVMYPIQLN 240
Cdd:MTH00167 410 TKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLLPVELTS 489

                        250
                 ....*....|..
gi 78103085  241 SSIEWFQNTPPA 252
Cdd:MTH00167 490 TNVEWLHGCPPP 501
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-252 1.46e-137

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 396.40  E-value: 1.46e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085    1 GFGMISHIISHESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00142 248 GFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHG 327

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085   81 TQLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIY 160
Cdd:MTH00142 328 SKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRW 407

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085  161 LKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNIISSIGSTISFLGILYFFFIIWESIMSQRLVMYPIQLN 240
Cdd:MTH00142 408 LKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVMWSSHLS 487

                        250
                 ....*....|..
gi 78103085  241 SSIEWFQNTPPA 252
Cdd:MTH00142 488 TSLEWSHRLPPD 499
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-252 2.99e-136

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 393.19  E-value: 2.99e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085    1 GFGMISHIISHESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00223 247 GFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYG 326

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085   81 TQLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIY 160
Cdd:MTH00223 327 SKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRW 406

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085  161 LKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNIISSIGSTISFLGILYFFFIIWESIMSQRLVMYPIQLN 240
Cdd:MTH00223 407 AKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVWSGHLS 486

                        250
                 ....*....|..
gi 78103085  241 SSIEWFQNTPPA 252
Cdd:MTH00223 487 TSLEWDNLLPAD 498
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-251 5.41e-136

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 392.53  E-value: 5.41e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085    1 GFGMISHIISHESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00116 250 GFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHG 329

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085   81 TQLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIY 160
Cdd:MTH00116 330 GTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTW 409

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085  161 LKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNIISSIGSTISFLGILYFFFIIWESIMSQRLVMYPIQLN 240
Cdd:MTH00116 410 TKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVLQPELTT 489

                        250
                 ....*....|.
gi 78103085  241 SSIEWFQNTPP 251
Cdd:MTH00116 490 TNIEWIHGCPP 500
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-251 2.63e-121

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 355.34  E-value: 2.63e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085    1 GFGMISHIISHESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00103 250 GFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHG 329

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085   81 TQLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIY 160
Cdd:MTH00103 330 GNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTW 409

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085  161 LKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNIISSIGSTISFLGILYFFFIIWESIMSQRLVMYPIQLN 240
Cdd:MTH00103 410 AKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVLTVELTT 489

                        250
                 ....*....|.
gi 78103085  241 SSIEWFQNTPP 251
Cdd:MTH00103 490 TNLEWLHGCPP 500
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-251 2.80e-120

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 352.59  E-value: 2.80e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085    1 GFGMISHIISHESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00037 250 GFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQG 329

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085   81 TQLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIY 160
Cdd:MTH00037 330 SNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLW 409

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085  161 LKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNIISSIGSTISFLGILYFFFIIWESIMSQRLVMYPIQLN 240
Cdd:MTH00037 410 SKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVISPEFSS 489

                        250
                 ....*....|.
gi 78103085  241 SSIEWFQNTPP 251
Cdd:MTH00037 490 SSLEWQYSSFP 500
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-250 5.72e-119

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 349.20  E-value: 5.72e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085    1 GFGMISHIISHESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00007 247 GFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHG 326

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085   81 TQLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIY 160
Cdd:MTH00007 327 SPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRW 406

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085  161 LKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNIISSIGSTISFLGILYFFFIIWESIMSQRLVMYPIQLN 240
Cdd:MTH00007 407 AKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIASPHMS 486

                        250
                 ....*....|
gi 78103085  241 SSIEWFQNTP 250
Cdd:MTH00007 487 SSLEWQDTLP 496
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-251 9.08e-119

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 348.84  E-value: 9.08e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085    1 GFGMISHIISHESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00183 250 GFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHG 329

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085   81 TQLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIY 160
Cdd:MTH00183 330 GSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTW 409

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085  161 LKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNIISSIGSTISFLGILYFFFIIWESIMSQRLVMYPIQLN 240
Cdd:MTH00183 410 TKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLSVELTS 489

                        250
                 ....*....|.
gi 78103085  241 SSIEWFQNTPP 251
Cdd:MTH00183 490 TNVEWLHGCPP 500
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-251 2.82e-116

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 342.31  E-value: 2.82e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085    1 GFGMISHIISHESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00077 250 GFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHG 329

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085   81 TQLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIY 160
Cdd:MTH00077 330 GAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTW 409

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085  161 LKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNIISSIGSTISFLGILYFFFIIWESIMSQRLVMYPIQLN 240
Cdd:MTH00077 410 SKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREVLTTELTS 489

                        250
                 ....*....|.
gi 78103085  241 SSIEWFQNTPP 251
Cdd:MTH00077 490 TNIEWLHGCPP 500
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 2-251 7.96e-105

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 312.77  E-value: 7.96e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085    2 FGMISHIISHESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 81
Cdd:MTH00079 251 FGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGM 330

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085   82 QLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIYL 161
Cdd:MTH00079 331 KMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMM 410

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085  162 KTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNIISSIGSTISFLGILYFFFIIWESIMSQRLVMYPIQLNS 241
Cdd:MTH00079 411 SAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLHDNYINS 490

                        250
                 ....*....|
gi 78103085  242 SIEWFQNTPP 251
Cdd:MTH00079 491 SPEYSLSSYV 500
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-252 1.45e-101

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 305.21  E-value: 1.45e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085    1 GFGMISHIISHESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00182 252 GFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYG 331

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085   81 TQLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIY 160
Cdd:MTH00182 332 GTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELY 411

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085  161 LKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNIISSIGSTISFLGILYFFFIIWESIMSQRLVMYPIQLN 240
Cdd:MTH00182 412 GKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKFIGWKEGT 491

                        250
                 ....*....|....*.
gi 78103085  241 ----SSIEWFQNTPPA 252
Cdd:MTH00182 492 geswASLEWVHSSPPL 507
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-252 1.87e-98

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 296.74  E-value: 1.87e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085    1 GFGMISHIISHESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00184 252 GFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFG 331

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085   81 TQLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIY 160
Cdd:MTH00184 332 GSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVY 411

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085  161 LKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNIISSIGSTISFLGILYFFFIIWESIMSQRLV---MYPI 237
Cdd:MTH00184 412 GKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVREIKFvgwVEDS 491

                        250
                 ....*....|....*
gi 78103085  238 QLNSSIEWFQNTPPA 252
Cdd:MTH00184 492 GHYPSLEWAQTSPPA 506
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-227 1.38e-89

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: 272.48  E-value: 1.38e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085   1 GFGMISHIISHESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:cd00919 238 AFGAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWG 316

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085  81 TQLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIY 160
Cdd:cd00919 317 GRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKL 396

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 78103085 161 LKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNIISSIGSTISFLGILYFFFIIWESI 227
Cdd:cd00919 397 GKIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-226 3.33e-83

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 258.02  E-value: 3.33e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085    1 GFGMISHIISHESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00026 251 GFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSG 330

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085   81 T--QLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNS 158
Cdd:MTH00026 331 SgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKD 410

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 78103085  159 IYLKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNIISSIGSTISFLGILYFFFIIWES 226
Cdd:MTH00026 411 IYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDA 478
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-251 1.96e-79

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 248.50  E-value: 1.96e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085   1 GFGMISHIISHESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:COG0843 252 AFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWR 330

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085  81 TQLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIY 160
Cdd:COG0843 331 GRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERL 410

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085 161 LKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTSWNIISSIGSTISFLGILYFFFIIWESIMSQRLV-MYPI 237
Cdd:COG0843 411 GKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPKAgGNPW 490

                       250
                ....*....|....
gi 78103085 238 QLNsSIEWFQNTPP 251
Cdd:COG0843 491 GAR-TLEWATPSPP 503
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-251 3.63e-78

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: 244.05  E-value: 3.63e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085     1 GFGMISHIISHESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:TIGR02891 243 AFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWG 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085    81 TQLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIY 160
Cdd:TIGR02891 322 GSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERL 401

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085   161 LKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTSWNIISSIGSTISFLGILYFFFIIWESIMSQRLVMYPIQ 238
Cdd:TIGR02891 402 GRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGANPW 481

                         250
                  ....*....|...
gi 78103085   239 LNSSIEWFQNTPP 251
Cdd:TIGR02891 482 GATTLEWTTSSPP 494
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-234 1.07e-73

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 233.03  E-value: 1.07e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085    1 GFGMISHIISHESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:MTH00048 248 GFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLN 327

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085   81 TQL-IYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSI 159
Cdd:MTH00048 328 SRVrKSDPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKY 407

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 78103085  160 YLKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNIISSIGSTISFLGILYFFFIIWESIMSQRLVM 234
Cdd:MTH00048 408 LLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEVL 482
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 2-227 9.42e-71

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: 225.15  E-value: 9.42e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085   2 FGMISHIISHESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 81
Cdd:cd01662 245 FGIFSEIVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRG 323

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085  82 QLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIYL 161
Cdd:cd01662 324 RIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLG 403

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 78103085 162 KTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTSWNIISSIGSTISFLGILYFFFIIWESI 227
Cdd:cd01662 404 KWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLINVIVSI 471
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-193 2.59e-54

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: 180.46  E-value: 2.59e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085     1 GFGMISHIISHESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHG 80
Cdd:pfam00115 218 AFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWG 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085    81 TQL-IYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSI 159
Cdd:pfam00115 297 GWIrFRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEK 376

                         170       180       190
                  ....*....|....*....|....*....|....
gi 78103085   160 YLKTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSD 193
Cdd:pfam00115 377 LGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAP 410
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 2-196 8.02e-43

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 153.94  E-value: 8.02e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085    2 FGMISHIISHESgKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGT 81
Cdd:PRK15017 295 FGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQG 373

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085   82 QLIYSPSTMWALGFIFLFTVGGLTGVVLANSSIDIMLHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTLNSIYL 161
Cdd:PRK15017 374 RIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWG 453

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 78103085  162 KTQFLIMFMGVNLTFFPQHFLGLAGMPRRYSDYPD 196
Cdd:PRK15017 454 KRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQID 488
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 60-223 1.24e-08

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: 54.98  E-value: 1.24e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085  60 TMIIAVPTGIKIFSWLATL-------HGTQLIYSPSTMW---------ALGFIFlFTVGGLTGVVLANSSIDIMLHDTYY 123
Cdd:cd01660 282 TFMVALPSLLTAFTVFASLeiagrlrGGKGLFGWIRALPwgdpmflalFLAMLM-FIPGGAGGIINASYQLNYVVHNTAW 360

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78103085 124 VVAHFHyvLSMGAVFAIMAGFIHWY--SLFTGLTLNSIYL-KTQFLIMFMGVNLTFFPQHFLGLAGMPRR--YSDYPDAY 198
Cdd:cd01660 361 VPGHFH--LTVGGAVALTFMAVAYWlvPHLTGRELAAKRLaLAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGGLP 438

                       170       180       190
                ....*....|....*....|....*....|
gi 78103085 199 -----TSWNIISSIGSTISFLGILYFFFII 223
Cdd:cd01660 439 aagewAPYQQLMAIGGTILFVSGALFLYIL 468
 
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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