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Conserved domains on  [gi|1820426294|gb|QIJ69677|]
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cytochrome c oxidase subunit I, partial (mitochondrion) [Staphylocystis furcata]

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 ...
 2-174 1.96e-103

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 MTH00048:

Pssm-ID: 469701  Cd Length: 511  Bit Score: 306.22  E-value: 1.96e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294   2 HICLSLSLIPDAFGFYGLLFAMFSIVCLGCSVWAHHMFTVGLDVKTAVFFSSVTMIIGIPTGIKVFTWLYMLLNSMANKS 81
Cdd:MTH00048  254 HICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKS 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294  82 DPVIWWIVSFIVLFSFGGVTGIILSACVLDNVLHDTWFVVAHFHYVMSLGSYISVIIMFIWWWPLVTGVALNKVLLQCQC 161
Cdd:MTH00048  334 DPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHC 413

                         170
                  ....*....|...
gi 1820426294 162 IISNVGFNLCFFP 174
Cdd:MTH00048  414 IISMIGFNLCFFP 426
 
Name Accession Description Interval E-value
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 2-174 1.96e-103

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 306.22  E-value: 1.96e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294   2 HICLSLSLIPDAFGFYGLLFAMFSIVCLGCSVWAHHMFTVGLDVKTAVFFSSVTMIIGIPTGIKVFTWLYMLLNSMANKS 81
Cdd:MTH00048  254 HICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKS 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294  82 DPVIWWIVSFIVLFSFGGVTGIILSACVLDNVLHDTWFVVAHFHYVMSLGSYISVIIMFIWWWPLVTGVALNKVLLQCQC 161
Cdd:MTH00048  334 DPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHC 413

                         170
                  ....*....|...
gi 1820426294 162 IISNVGFNLCFFP 174
Cdd:MTH00048  414 IISMIGFNLCFFP 426
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 2-174 4.87e-73

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: 227.37  E-value: 4.87e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294   2 HICLSLSLIPDAFGFYGLLFAMFSIVCLGCSVWAHHMFTVGLDVKTAVFFSSVTMIIGIPTGIKVFTWLYMLLNSmANKS 81
Cdd:cd01663   247 HIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGG-SIKF 325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294  82 DPVIWWIVSFIVLFSFGGVTGIILSACVLDNVLHDTWFVVAHFHYVMSLGSYISVIIMFIWWWPLVTGVALNKVLLQCQC 161
Cdd:cd01663   326 ETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHF 405

                         170
                  ....*....|...
gi 1820426294 162 IISNVGFNLCFFP 174
Cdd:cd01663   406 WLMFIGVNLTFFP 418
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 14-174 8.65e-40

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: 140.44  E-value: 8.65e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294  14 FGFYGLLFAMFSIVCLGCSVWAHHMFTVGLDVKTAVFFSSVTMIIGIPTGIKVFTWLYMLLNSMANKSDPvIWWIVSFIV 93
Cdd:TIGR02891 260 FGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTP-MLFALGFIF 338

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294  94 LFSFGGVTGIILSACVLDNVLHDTWFVVAHFHYVMSLGSYISVIIMFIWWWPLVTGVALNKVLLQCQCIISNVGFNLCFF 173
Cdd:TIGR02891 339 LFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFF 418


                  .
gi 1820426294 174 P 174
Cdd:TIGR02891 419 P 419
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
14-174 3.26e-39

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 139.49  E-value: 3.26e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294  14 FGFYGLLFAMFSIVCLGCSVWAHHMFTVGLDVKTAVFFSSVTMIIGIPTGIKVFTWLYMLLNSMANKSDPVIwWIVSFIV 93
Cdd:COG0843   269 FGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPML-FALGFII 347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294  94 LFSFGGVTGIILSACVLDNVLHDTWFVVAHFHYVMSLGSYISVIIMFIWWWPLVTGVALNKVLLQCQCIISNVGFNLCFF 173
Cdd:COG0843   348 LFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFF 427


                  .
gi 1820426294 174 P 174
Cdd:COG0843   428 P 428
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 14-175 2.99e-30

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: 113.82  E-value: 2.99e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294  14 FGFYGLLFAMFSIVCLGCSVWAHHMFTVGLDVKTAVFFSSVTMIIGIPTGIKVFTWLYMLLNSMANKSDPVIWWIVSFIV 93
Cdd:pfam00115 235 FGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFRTTPMLFFLGFAF 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294  94 LFSFGGVTGIILSACVLDNVLHDTWFVVAHFHYVMSLGSYISVIIMFIWWWPLVTGVALNKVLLQCQCIISNVGFNLCFF 173
Cdd:pfam00115 315 LFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFF 394


                  ..
gi 1820426294 174 PW 175
Cdd:pfam00115 395 PM 396
 
Name Accession Description Interval E-value
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 2-174 1.96e-103

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 306.22  E-value: 1.96e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294   2 HICLSLSLIPDAFGFYGLLFAMFSIVCLGCSVWAHHMFTVGLDVKTAVFFSSVTMIIGIPTGIKVFTWLYMLLNSMANKS 81
Cdd:MTH00048  254 HICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKS 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294  82 DPVIWWIVSFIVLFSFGGVTGIILSACVLDNVLHDTWFVVAHFHYVMSLGSYISVIIMFIWWWPLVTGVALNKVLLQCQC 161
Cdd:MTH00048  334 DPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHC 413

                         170
                  ....*....|...
gi 1820426294 162 IISNVGFNLCFFP 174
Cdd:MTH00048  414 IISMIGFNLCFFP 426
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 2-174 4.87e-73

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: 227.37  E-value: 4.87e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294   2 HICLSLSLIPDAFGFYGLLFAMFSIVCLGCSVWAHHMFTVGLDVKTAVFFSSVTMIIGIPTGIKVFTWLYMLLNSmANKS 81
Cdd:cd01663   247 HIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGG-SIKF 325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294  82 DPVIWWIVSFIVLFSFGGVTGIILSACVLDNVLHDTWFVVAHFHYVMSLGSYISVIIMFIWWWPLVTGVALNKVLLQCQC 161
Cdd:cd01663   326 ETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHF 405

                         170
                  ....*....|...
gi 1820426294 162 IISNVGFNLCFFP 174
Cdd:cd01663   406 WLMFIGVNLTFFP 418
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 2-174 1.28e-54

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 180.06  E-value: 1.28e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294   2 HICLSLSLIPDAFGFYGLLFAMFSIVCLGCSVWAHHMFTVGLDVKTAVFFSSVTMIIGIPTGIKVFTWLYMLLNSMANKS 81
Cdd:MTH00153  254 HIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYS 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294  82 dPVIWWIVSFIVLFSFGGVTGIILSACVLDNVLHDTWFVVAHFHYVMSLGSYISVIIMFIWWWPLVTGVALNKVLLQCQC 161
Cdd:MTH00153  334 -PSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQF 412

                         170
                  ....*....|...
gi 1820426294 162 IISNVGFNLCFFP 174
Cdd:MTH00153  413 FIMFIGVNLTFFP 425
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 14-174 2.85e-52

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 174.09  E-value: 2.85e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294  14 FGFYGLLFAMFSIVCLGCSVWAHHMFTVGLDVKTAVFFSSVTMIIGIPTGIKVFTWLYMLLNSMAnKSDPVIWWIVSFIV 93
Cdd:MTH00167  268 FGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKI-KWETPMLWALGFIF 346

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294  94 LFSFGGVTGIILSACVLDNVLHDTWFVVAHFHYVMSLGSYISVIIMFIWWWPLVTGVALNKVLLQCQCIISNVGFNLCFF 173
Cdd:MTH00167  347 LFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFIGVNLTFF 426


                  .
gi 1820426294 174 P 174
Cdd:MTH00167  427 P 427
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 2-174 1.46e-51

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 172.08  E-value: 1.46e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294   2 HICLSLSLIPDAFGFYGLLFAMFSIVCLGCSVWAHHMFTVGLDVKTAVFFSSVTMIIGIPTGIKVFTWLYMLLNSMAnKS 81
Cdd:MTH00223  253 HIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKI-KY 331

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294  82 DPVIWWIVSFIVLFSFGGVTGIILSACVLDNVLHDTWFVVAHFHYVMSLGSYISVIIMFIWWWPLVTGVALNKVLLQCQC 161
Cdd:MTH00223  332 EAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHF 411

                         170
                  ....*....|...
gi 1820426294 162 IISNVGFNLCFFP 174
Cdd:MTH00223  412 FLMFLGVNLTFFP 424
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 14-174 2.17e-51

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 171.81  E-value: 2.17e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294  14 FGFYGLLFAMFSIVCLGCSVWAHHMFTVGLDVKTAVFFSSVTMIIGIPTGIKVFTWLYMLLNSMAnKSDPVIWWIVSFIV 93
Cdd:MTH00116  268 FGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTI-KWDPPMLWALGFIF 346

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294  94 LFSFGGVTGIILSACVLDNVLHDTWFVVAHFHYVMSLGSYISVIIMFIWWWPLVTGVALNKVLLQCQCIISNVGFNLCFF 173
Cdd:MTH00116  347 LFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLTFF 426


                  .
gi 1820426294 174 P 174
Cdd:MTH00116  427 P 427
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 2-174 2.58e-50

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 168.75  E-value: 2.58e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294   2 HICLSLSLIPDAFGFYGLLFAMFSIVCLGCSVWAHHMFTVGLDVKTAVFFSSVTMIIGIPTGIKVFTWLYMLLNSmANKS 81
Cdd:MTH00142  254 HIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGS-KVKY 332

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294  82 DPVIWWIVSFIVLFSFGGVTGIILSACVLDNVLHDTWFVVAHFHYVMSLGSYISVIIMFIWWWPLVTGVALNKVLLQCQC 161
Cdd:MTH00142  333 EPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHF 412

                         170
                  ....*....|...
gi 1820426294 162 IISNVGFNLCFFP 174
Cdd:MTH00142  413 YTMFIGVNLTFFP 425
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 2-174 9.69e-50

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 167.16  E-value: 9.69e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294   2 HICLSLSLIPDAFGFYGLLFAMFSIVCLGCSVWAHHMFTVGLDVKTAVFFSSVTMIIGIPTGIKVFTWLYMLLnSMANKS 81
Cdd:MTH00079  256 QSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLF-GMKMKF 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294  82 DPVIWWIVSFIVLFSFGGVTGIILSACVLDNVLHDTWFVVAHFHYVMSLGSYISVIIMFIWWWPLVTGVALNKVLLQCQC 161
Cdd:MTH00079  335 QPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVF 414

                         170
                  ....*....|...
gi 1820426294 162 IISNVGFNLCFFP 174
Cdd:MTH00079  415 FLMFVGVNLTFFP 427
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 2-174 3.84e-46

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 157.74  E-value: 3.84e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294   2 HICLSLSLIPDAFGFYGLLFAMFSIVCLGCSVWAHHMFTVGLDVKTAVFFSSVTMIIGIPTGIKVFTWLYMLLNSMANKS 81
Cdd:MTH00103  256 HIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWS 335

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294  82 dPVIWWIVSFIVLFSFGGVTGIILSACVLDNVLHDTWFVVAHFHYVMSLGSYISVIIMFIWWWPLVTGVALNKVLLQCQC 161
Cdd:MTH00103  336 -PAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHF 414

                         170
                  ....*....|...
gi 1820426294 162 IISNVGFNLCFFP 174
Cdd:MTH00103  415 TIMFVGVNMTFFP 427
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 14-175 1.66e-45

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: 155.00  E-value: 1.66e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294  14 FGFYGLLFAMFSIVCLGCSVWAHHMFTVGLDVKTAVFFSSVTMIIGIPTGIKVFTWLYMLLNSmANKSDPVIWWIVSFIV 93
Cdd:cd00919   255 FGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGG-RIRFDPPMLFALGFLF 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294  94 LFSFGGVTGIILSACVLDNVLHDTWFVVAHFHYVMSLGSYISVIIMFIWWWPLVTGVALNKVLLQCQCIISNVGFNLCFF 173
Cdd:cd00919   334 LFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGFNLTFF 413


                  ..
gi 1820426294 174 PW 175
Cdd:cd00919   414 PM 415
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 2-174 2.73e-45

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 155.45  E-value: 2.73e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294   2 HICLSLSLIPDAFGFYGLLFAMFSIVCLGCSVWAHHMFTVGLDVKTAVFFSSVTMIIGIPTGIKVFTWLYMLLNSMAnKS 81
Cdd:MTH00007  253 HIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPI-KY 331

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294  82 DPVIWWIVSFIVLFSFGGVTGIILSACVLDNVLHDTWFVVAHFHYVMSLGSYISVIIMFIWWWPLVTGVALNKVLLQCQC 161
Cdd:MTH00007  332 ETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHF 411

                         170
                  ....*....|...
gi 1820426294 162 IISNVGFNLCFFP 174
Cdd:MTH00007  412 FLMFLGVNLTFFP 424
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 2-174 1.06e-43

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 151.25  E-value: 1.06e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294   2 HICLSLSLIPDAFGFYGLLFAMFSIVCLGCSVWAHHMFTVGLDVKTAVFFSSVTMIIGIPTGIKVFTWLyMLLNSMANKS 81
Cdd:MTH00077  256 HIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWL-ATMHGGAIKW 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294  82 DPVIWWIVSFIVLFSFGGVTGIILSACVLDNVLHDTWFVVAHFHYVMSLGSYISVIIMFIWWWPLVTGVALNKVLLQCQC 161
Cdd:MTH00077  335 DAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHF 414

                         170
                  ....*....|...
gi 1820426294 162 IISNVGFNLCFFP 174
Cdd:MTH00077  415 GVMFIGVNLTFFP 427
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 2-174 1.70e-43

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 150.75  E-value: 1.70e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294   2 HICLSLSLIPDAFGFYGLLFAMFSIVCLGCSVWAHHMFTVGLDVKTAVFFSSVTMIIGIPTGIKVFTWLYMLLNSMANkS 81
Cdd:MTH00037  256 HVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLR-W 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294  82 DPVIWWIVSFIVLFSFGGVTGIILSACVLDNVLHDTWFVVAHFHYVMSLGSYISVIIMFIWWWPLVTGVALNKVLLQCQC 161
Cdd:MTH00037  335 ETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHF 414

                         170
                  ....*....|...
gi 1820426294 162 IISNVGFNLCFFP 174
Cdd:MTH00037  415 FLMFIGVNLTFFP 427
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 2-174 1.78e-43

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 150.84  E-value: 1.78e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294   2 HICLSLSLIPDAFGFYGLLFAMFSIVCLGCSVWAHHMFTVGLDVKTAVFFSSVTMIIGIPTGIKVFTWLYMLLNSMANKS 81
Cdd:MTH00183  256 HIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWE 335

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294  82 DPVIWwIVSFIVLFSFGGVTGIILSACVLDNVLHDTWFVVAHFHYVMSLGSYISVIIMFIWWWPLVTGVALNKVLLQCQC 161
Cdd:MTH00183  336 TPLLW-ALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHF 414

                         170
                  ....*....|...
gi 1820426294 162 IISNVGFNLCFFP 174
Cdd:MTH00183  415 GVMFVGVNLTFFP 427
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 14-174 8.65e-40

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: 140.44  E-value: 8.65e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294  14 FGFYGLLFAMFSIVCLGCSVWAHHMFTVGLDVKTAVFFSSVTMIIGIPTGIKVFTWLYMLLNSMANKSDPvIWWIVSFIV 93
Cdd:TIGR02891 260 FGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTP-MLFALGFIF 338

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294  94 LFSFGGVTGIILSACVLDNVLHDTWFVVAHFHYVMSLGSYISVIIMFIWWWPLVTGVALNKVLLQCQCIISNVGFNLCFF 173
Cdd:TIGR02891 339 LFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFF 418


                  .
gi 1820426294 174 P 174
Cdd:TIGR02891 419 P 419
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
14-174 3.26e-39

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 139.49  E-value: 3.26e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294  14 FGFYGLLFAMFSIVCLGCSVWAHHMFTVGLDVKTAVFFSSVTMIIGIPTGIKVFTWLYMLLNSMANKSDPVIwWIVSFIV 93
Cdd:COG0843   269 FGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPML-FALGFII 347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294  94 LFSFGGVTGIILSACVLDNVLHDTWFVVAHFHYVMSLGSYISVIIMFIWWWPLVTGVALNKVLLQCQCIISNVGFNLCFF 173
Cdd:COG0843   348 LFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFF 427


                  .
gi 1820426294 174 P 174
Cdd:COG0843   428 P 428
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 14-174 3.29e-39

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 139.57  E-value: 3.29e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294  14 FGFYGLLFAMFSIVCLGCSVWAHHMFTVGLDVKTAVFFSSVTMIIGIPTGIKVFTWLYMLLNSMANKSDPVIWWIvSFIV 93
Cdd:MTH00182  270 FGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAM-GFVF 348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294  94 LFSFGGVTGIILSACVLDNVLHDTWFVVAHFHYVMSLGSYISVIIMFIWWWPLVTGVALNKVLLQCQCIISNVGFNLCFF 173
Cdd:MTH00182  349 LFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWLMFIGVNLTFF 428


                  .
gi 1820426294 174 P 174
Cdd:MTH00182  429 P 429
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 14-174 8.92e-39

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 138.04  E-value: 8.92e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294  14 FGFYGLLFAMFSIVCLGCSVWAHHMFTVGLDVKTAVFFSSVTMIIGIPTGIKVFTWLYMLLNSMANKSDPVIWwIVSFIV 93
Cdd:MTH00184  270 FGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLW-AIGFVF 348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294  94 LFSFGGVTGIILSACVLDNVLHDTWFVVAHFHYVMSLGSYISVIIMFIWWWPLVTGVALNKVLLQCQCIISNVGFNLCFF 173
Cdd:MTH00184  349 LFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMFIGVNLTFF 428


                  .
gi 1820426294 174 P 174
Cdd:MTH00184  429 P 429
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 14-174 1.15e-36

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: 132.32  E-value: 1.15e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294  14 FGFYGLLFAMFSIVCLGCSVWAHHMFTVGLDVKTAVFFSSVTMIIGIPTGIKVFTWLYMLLNSMANKSDPVIWwIVSFIV 93
Cdd:cd01662   261 FGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLW-AIGFLV 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294  94 LFSFGGVTGIILSACVLDNVLHDTWFVVAHFHYVMSLGSYISVIIMFIWWWPLVTGVALNKVLLQCQCIISNVGFNLCFF 173
Cdd:cd01662   340 TFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFNLTFF 419


                  .
gi 1820426294 174 P 174
Cdd:cd01662   420 P 420
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 14-174 2.55e-33

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 123.58  E-value: 2.55e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294  14 FGFYGLLFAMFSIVCLGCSVWAHHMFTVGLDVKTAVFFSSVTMIIGIPTGIKVFTWLYMLLNSMANK--SDPVIwWIVSF 91
Cdd:MTH00026  269 FGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSGRNLifTTPMA-WALGF 347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294  92 IVLFSFGGVTGIILSACVLDNVLHDTWFVVAHFHYVMSLGSYISVIIMFIWWWPLVTGVALNKVLLQCQCIISNVGFNLC 171
Cdd:MTH00026  348 IFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLMFIGVNIT 427


                  ...
gi 1820426294 172 FFP 174
Cdd:MTH00026  428 FFP 430
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 14-175 2.99e-30

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: 113.82  E-value: 2.99e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294  14 FGFYGLLFAMFSIVCLGCSVWAHHMFTVGLDVKTAVFFSSVTMIIGIPTGIKVFTWLYMLLNSMANKSDPVIWWIVSFIV 93
Cdd:pfam00115 235 FGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFRTTPMLFFLGFAF 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294  94 LFSFGGVTGIILSACVLDNVLHDTWFVVAHFHYVMSLGSYISVIIMFIWWWPLVTGVALNKVLLQCQCIISNVGFNLCFF 173
Cdd:pfam00115 315 LFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFF 394


                  ..
gi 1820426294 174 PW 175
Cdd:pfam00115 395 PM 396
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 14-174 1.16e-28

cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]


Pssm-ID: 131928  Cd Length: 643  Bit Score: 111.10  E-value: 1.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294  14 FGFYGLLFAMFSIVCLGCSVWAHHMFTVGLDVKTAVFFSSVTMIIGIPTGIKVFTWLYMLLNSMANKSDPVIWWIvSFIV 93
Cdd:TIGR02882 304 FGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPMLFSL-AFIP 382

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294  94 LFSFGGVTGIILSACVLDNVLHDTWFVVAHFHYVMSLGSYISVIIMFIWWWPLVTGVALNKVLLQCQCIISNVGFNLCFF 173
Cdd:TIGR02882 383 NFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLNERLGKWCFWFFMIGFNVCFF 462


                  .
gi 1820426294 174 P 174
Cdd:TIGR02882 463 P 463
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 14-174 2.49e-25

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 101.55  E-value: 2.49e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294  14 FGFYGLLFAMFSIVCLGCSVWAHHMFTVGLDVKTAVFFSSVTMIIGIPTGIKVFTWLYMLLNSMANKSDPVIwWIVSFIV 93
Cdd:PRK15017  311 FGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAML-WTIGFIV 389

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820426294  94 LFSFGGVTGIILSACVLDNVLHDTWFVVAHFHYVMSLGSYISVIIMFIWWWPLVTGVALNKVLLQCQCIISNVGFNLCFF 173
Cdd:PRK15017  390 TFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFM 469


                  .
gi 1820426294 174 P 174
Cdd:PRK15017  470 P 470
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 92-149 2.21e-03

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: 37.65  E-value: 2.21e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1820426294  92 IVLFSFGGVTGIILSACVLDNVLHDTWFVVAHFHYVMSLGSYISVIIMFIWWWPLVTG 149
Cdd:cd01660   333 MLMFIPGGAGGIINASYQLNYVVHNTAWVPGHFHLTVGGAVALTFMAVAYWLVPHLTG 390
 
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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