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Conserved domains on  [gi|1187525992|gb|ARM53245|]
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cytochrome c oxidase 1, partial (mitochondrion) [Pseudagrion acaciae]

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 ...
 1-168 6.39e-110

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: 322.20  E-value: 6.39e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992   1 HGSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGTTMSN 80
Cdd:MTH00153  326 HGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNP 405

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992  81 QMLKAQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDSYTAWNILSTLGSSISMMGVIMLLFIIWEAMASQRQVLSTSA 160
Cdd:MTH00153  406 KWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLN 485


                  ....*...
gi 1187525992 161 MNTSIEWY 168
Cdd:MTH00153  486 LSSSIEWL 493
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-168 6.39e-110

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 322.20  E-value: 6.39e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992   1 HGSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGTTMSN 80
Cdd:MTH00153  326 HGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNP 405

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992  81 QMLKAQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDSYTAWNILSTLGSSISMMGVIMLLFIIWEAMASQRQVLSTSA 160
Cdd:MTH00153  406 KWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLN 485


                  ....*...
gi 1187525992 161 MNTSIEWY 168
Cdd:MTH00153  486 LSSSIEWL 493
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-167 2.49e-89

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: 268.97  E-value: 2.49e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992   1 HGSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGTTMSN 80
Cdd:cd01663   319 WGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNE 398

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992  81 QMLKAQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDSYTAWNILSTLGSSISMMGVIMLLFIIWEAMASQRQVLS-TS 159
Cdd:cd01663   399 TLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFnVG 478


                  ....*...
gi 1187525992 160 AMNTSIEW 167
Cdd:cd01663   479 EGSTSLEW 486
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-146 3.00e-52

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 173.77  E-value: 3.00e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992   2 GSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGTTMSNQ 81
Cdd:COG0843   330 RGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNER 409

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1187525992  82 MLKAQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DSYTAWNILSTLGSSISMMGVIMLLFIIW 146
Cdd:COG0843   410 LGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLV 476
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 2-167 8.71e-51

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: 169.33  E-value: 8.71e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992   2 GSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGTTMSNQ 81
Cdd:TIGR02891 321 GGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNER 400

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992  82 MLKAQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDS--YTAWNILSTLGSSISMMGVIMLLFIIWEAMASQRQVLSTS 159
Cdd:TIGR02891 401 LGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGANP 480


                  ....*...
gi 1187525992 160 AMNTSIEW 167
Cdd:TIGR02891 481 WGATTLEW 488
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 11-133 1.02e-35

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


Pssm-ID: 459678  Cd Length: 432  Bit Score: 128.46  E-value: 1.02e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992  11 LLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGTTMSNQMLKAQFLTM 90
Cdd:pfam00115 306 MLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLL 385

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1187525992  91 FIGVNLTFFPQHFLGLAGMPRRYS----DYPDSYTAWNILSTLGSSI 133
Cdd:pfam00115 386 FIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-168 6.39e-110

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 322.20  E-value: 6.39e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992   1 HGSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGTTMSN 80
Cdd:MTH00153  326 HGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNP 405

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992  81 QMLKAQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDSYTAWNILSTLGSSISMMGVIMLLFIIWEAMASQRQVLSTSA 160
Cdd:MTH00153  406 KWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLN 485


                  ....*...
gi 1187525992 161 MNTSIEWY 168
Cdd:MTH00153  486 LSSSIEWL 493
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-168 3.04e-91

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 274.66  E-value: 3.04e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992   1 HGSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGTTMSN 80
Cdd:MTH00116  328 HGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQ 407

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992  81 QMLKAQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDSYTAWNILSTLGSSISMMGVIMLLFIIWEAMASQRQVLSTSA 160
Cdd:MTH00116  408 TWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVLQPEL 487


                  ....*...
gi 1187525992 161 MNTSIEWY 168
Cdd:MTH00116  488 TTTNIEWI 495
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-167 2.49e-89

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: 268.97  E-value: 2.49e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992   1 HGSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGTTMSN 80
Cdd:cd01663   319 WGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNE 398

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992  81 QMLKAQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDSYTAWNILSTLGSSISMMGVIMLLFIIWEAMASQRQVLS-TS 159
Cdd:cd01663   399 TLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFnVG 478


                  ....*...
gi 1187525992 160 AMNTSIEW 167
Cdd:cd01663   479 EGSTSLEW 486
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-167 4.77e-87

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 263.85  E-value: 4.77e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992   1 HGSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGTTMSN 80
Cdd:MTH00167  328 HGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNE 407

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992  81 QMLKAQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDSYTAWNILSTLGSSISMMGVIMLLFIIWEAMASQRQVLSTSA 160
Cdd:MTH00167  408 TWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLLPVEL 487


                  ....*..
gi 1187525992 161 MNTSIEW 167
Cdd:MTH00167  488 TSTNVEW 494
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-168 1.59e-86

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 262.35  E-value: 1.59e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992   1 HGSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGTTMSN 80
Cdd:MTH00142  326 HGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNP 405

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992  81 QMLKAQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDSYTAWNILSTLGSSISMMGVIMLLFIIWEAMASQRQVLSTSA 160
Cdd:MTH00142  406 RWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVMWSSH 485


                  ....*...
gi 1187525992 161 MNTSIEWY 168
Cdd:MTH00142  486 LSTSLEWS 493
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-167 6.43e-85

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 258.37  E-value: 6.43e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992   1 HGSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGTTMSN 80
Cdd:MTH00223  325 YGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHR 404

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992  81 QMLKAQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDSYTAWNILSTLGSSISMMGVIMLLFIIWEAMASQRQVLSTSA 160
Cdd:MTH00223  405 RWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVWSGH 484


                  ....*..
gi 1187525992 161 MNTSIEW 167
Cdd:MTH00223  485 LSTSLEW 491
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-167 4.31e-81

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 248.64  E-value: 4.31e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992   1 HGSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGTTMSN 80
Cdd:MTH00103  328 HGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLND 407

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992  81 QMLKAQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDSYTAWNILSTLGSSISMMGVIMLLFIIWEAMASQRQVLSTSA 160
Cdd:MTH00103  408 TWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVLTVEL 487


                  ....*..
gi 1187525992 161 MNTSIEW 167
Cdd:MTH00103  488 TTTNLEW 494
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-167 4.97e-78

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 240.60  E-value: 4.97e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992   1 HGSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGTTMSN 80
Cdd:MTH00183  328 HGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHS 407

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992  81 QMLKAQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDSYTAWNILSTLGSSISMMGVIMLLFIIWEAMASQRQVLSTSA 160
Cdd:MTH00183  408 TWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLSVEL 487


                  ....*..
gi 1187525992 161 MNTSIEW 167
Cdd:MTH00183  488 TSTNVEW 494
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-167 5.73e-78

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 240.61  E-value: 5.73e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992   1 HGSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGTTMSN 80
Cdd:MTH00077  328 HGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHS 407

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992  81 QMLKAQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDSYTAWNILSTLGSSISMMGVIMLLFIIWEAMASQRQVLSTSA 160
Cdd:MTH00077  408 TWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREVLTTEL 487


                  ....*..
gi 1187525992 161 MNTSIEW 167
Cdd:MTH00077  488 TSTNIEW 494
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 2-167 6.61e-76

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 235.11  E-value: 6.61e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992   2 GSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGTTMSNQ 81
Cdd:MTH00037  329 GSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPL 408

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992  82 MLKAQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDSYTAWNILSTLGSSISMMGVIMLLFIIWEAMASQRQVLSTSAM 161
Cdd:MTH00037  409 WSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVISPEFS 488


                  ....*.
gi 1187525992 162 NTSIEW 167
Cdd:MTH00037  489 SSSLEW 494
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-167 2.35e-75

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 233.64  E-value: 2.35e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992   1 HGSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGTTMSN 80
Cdd:MTH00007  325 HGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHD 404

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992  81 QMLKAQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDSYTAWNILSTLGSSISMMGVIMLLFIIWEAMASQRQVLSTSA 160
Cdd:MTH00007  405 RWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIASPH 484


                  ....*..
gi 1187525992 161 MNTSIEW 167
Cdd:MTH00007  485 MSSSLEW 491
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-167 1.07e-61

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 198.37  E-value: 1.07e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992   1 HGSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGTTMSN 80
Cdd:MTH00079  328 FGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDK 407

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992  81 QMLKAQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDSYTAWNILSTLGSSISMMGVIMLLFIIWEAMASQRQVLSTSA 160
Cdd:MTH00079  408 LMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLHDNY 487


                  ....*..
gi 1187525992 161 MNTSIEW 167
Cdd:MTH00079  488 INSSPEY 494
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-167 5.61e-60

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 194.27  E-value: 5.61e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992   1 HGSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGTTMSN 80
Cdd:MTH00182  330 YGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNE 409

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992  81 QMLKAQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDSYTAWNILSTLGSSISMMGVIMLLFIIWEAMASQRQVLS--- 157
Cdd:MTH00182  410 LYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKFIGwke 489

                         170
                  ....*....|.
gi 1187525992 158 -TSAMNTSIEW 167
Cdd:MTH00182  490 gTGESWASLEW 500
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-149 2.49e-58

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: 188.12  E-value: 2.49e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992   1 HGSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGTTMSN 80
Cdd:cd00919   315 WGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSE 394

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1187525992  81 QMLKAQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDSYTAWNILSTLGSSISMMGVIMLLFIIWEAM 149
Cdd:cd00919   395 KLGKIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 2-167 1.37e-57

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 187.73  E-value: 1.37e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992   2 GSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGTTMSNQ 81
Cdd:MTH00184  331 GGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEV 410

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992  82 MLKAQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDSYTAWNILSTLGSSISMMGVIMLLFIIWEAMASQRQVL---ST 158
Cdd:MTH00184  411 YGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVREIKFVgwvED 490


                  ....*....
gi 1187525992 159 SAMNTSIEW 167
Cdd:MTH00184  491 SGHYPSLEW 499
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-146 3.00e-52

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 173.77  E-value: 3.00e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992   2 GSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGTTMSNQ 81
Cdd:COG0843   330 RGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNER 409

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1187525992  82 MLKAQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DSYTAWNILSTLGSSISMMGVIMLLFIIW 146
Cdd:COG0843   410 LGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLV 476
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 2-167 8.71e-51

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: 169.33  E-value: 8.71e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992   2 GSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGTTMSNQ 81
Cdd:TIGR02891 321 GGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNER 400

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992  82 MLKAQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDS--YTAWNILSTLGSSISMMGVIMLLFIIWEAMASQRQVLSTS 159
Cdd:TIGR02891 401 LGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGANP 480


                  ....*...
gi 1187525992 160 AMNTSIEW 167
Cdd:TIGR02891 481 WGATTLEW 488
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 2-148 1.68e-46

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 158.64  E-value: 1.68e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992   2 GSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGTTMSNQ 81
Cdd:MTH00026  332 GRNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDI 411

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1187525992  82 MLKAQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDSYTAWNILSTLGSSISMMGVIMLLFIIWEA 148
Cdd:MTH00026  412 YGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDA 478
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 4-146 3.94e-45

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: 154.66  E-value: 3.94e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992   4 QLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGTTMSNQML 83
Cdd:cd01662   324 RIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLG 403

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1187525992  84 KAQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DSYTAWNILSTLGSSISMMGVIMLLFIIW 146
Cdd:cd01662   404 KWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLINVI 468
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 2-156 3.05e-43

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 149.83  E-value: 3.05e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992   2 GSQLNYS-PSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGTTMSN 80
Cdd:MTH00048  327 NSRVRKSdPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNK 406

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1187525992  81 QMLKAQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDSYTAWNILSTLGSSISMMGVIMLLFIIWEAMASQRQVL 156
Cdd:MTH00048  407 YLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEVL 482
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 11-133 1.02e-35

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


Pssm-ID: 459678  Cd Length: 432  Bit Score: 128.46  E-value: 1.02e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992  11 LLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGTTMSNQMLKAQFLTM 90
Cdd:pfam00115 306 MLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLL 385

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1187525992  91 FIGVNLTFFPQHFLGLAGMPRRYS----DYPDSYTAWNILSTLGSSI 133
Cdd:pfam00115 386 FIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
CyoB TIGR02843
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ...
 7-146 9.00e-26

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


Pssm-ID: 131890  Cd Length: 646  Bit Score: 102.44  E-value: 9.00e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992   7 YSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGTTMSNQMLKAQ 86
Cdd:TIGR02843 376 FETPMLWTIGFMVTFSIGGMTGVLLAVPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWFPKAFGFKLNEKLGKRS 455

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1187525992  87 FLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPD-SYTAWNILSTLGSSISMMGVIMLLFIIW 146
Cdd:TIGR02843 456 FWCWFIGFYLAFMPLYILGFMGMTRRLNHYDNpEWHPMLIIAAFGAFLIACGILCQIIQIF 516
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 4-154 1.71e-20

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 87.30  E-value: 1.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992   4 QLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGTTMSNQML 83
Cdd:PRK15017  374 RIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWG 453

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1187525992  84 KAQFLTMFIGVNLTFFPQHFLGLAGMPRRYSDYPD-SYTAWNILSTLGSSISMMGVIMLLFIIWEAMASQRQ 154
Cdd:PRK15017  454 KRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDpQFHTMLMIAASGAALIALGILCQVIQMYVSIRDRDQ 525
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 14-145 5.73e-13

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: 65.39  E-value: 5.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1187525992  14 ALGFVFlFTVGGLTGVVLANSSIDISMHDTYYVVAHFHyvLSMGAVFAIMG-GLIHWF-PLFTGTTM-SNQMLKAQFLTM 90
Cdd:cd01660   330 FLAMLM-FIPGGAGGIINASYQLNYVVHNTAWVPGHFH--LTVGGAVALTFmAVAYWLvPHLTGRELaAKRLALAQPWLW 406

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1187525992  91 FIGVNLTFFPQHFLGLAGMPRR--YSDYPDSY-----TAWNILSTLGSSISMMGVIMLLFII 145
Cdd:cd01660   407 FVGMTIMSTAMHVAGLLGAPRRtaEAQYGGLPaagewAPYQQLMAIGGTILFVSGALFLYIL 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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