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Conserved domains on  [gi|2177158292|gb|UIR90812|]
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cytochrome c oxidase subunit I, partial (mitochondrion) [Pterocladiella capillacea]

Protein Classification

cytochrome c oxidase subunit 1( domain architecture ID 10108859)

cytochrome c oxidase subunit 1 is the catalytic subunit of cytochrome c oxidase, which is the component of the respiratory chain that catalyzes the reduction of oxygen to water

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-459 0e+00

Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, may play a role in assembly or oxygen delivery to the active site. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center.


:

Pssm-ID: 238833  Cd Length: 488  Bit Score: 833.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292   1 GGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:cd01663    21 GTSLSLLIRLELSQPGS--QLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPP 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292  81 SLCLLLTSALVEVGVGTGWTIYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWS 160
Cdd:cd01663    99 SLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWS 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 161 IFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFS-RKPV 239
Cdd:cd01663   179 VLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSgKKPV 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 240 FGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIGFIFL 319
Cdd:cd01663   259 FGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFL 338

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 320 FTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEVLGQIHFWSTFIGVNLTFMP 399
Cdd:cd01663   339 FTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFP 418

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 400 MHFLGLAGMPRRIPDYPDAYTGWNLVASYGSYVSAFSTLFFFYLVFVSLTSNNTCIDSPW 459
Cdd:cd01663   419 QHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVG 478
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-459 0e+00

Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, may play a role in assembly or oxygen delivery to the active site. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center.


Pssm-ID: 238833  Cd Length: 488  Bit Score: 833.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292   1 GGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:cd01663    21 GTSLSLLIRLELSQPGS--QLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPP 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292  81 SLCLLLTSALVEVGVGTGWTIYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWS 160
Cdd:cd01663    99 SLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWS 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 161 IFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFS-RKPV 239
Cdd:cd01663   179 VLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSgKKPV 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 240 FGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIGFIFL 319
Cdd:cd01663   259 FGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFL 338

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 320 FTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEVLGQIHFWSTFIGVNLTFMP 399
Cdd:cd01663   339 FTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFP 418

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 400 MHFLGLAGMPRRIPDYPDAYTGWNLVASYGSYVSAFSTLFFFYLVFVSLTSNNTCIDSPW 459
Cdd:cd01663   419 QHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVG 478
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-451 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 749.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292   1 GGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:MTH00153   28 GTSLSLLIRAELGQPGS--LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292  81 SLCLLLTSALVEVGVGTGWTIYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWS 160
Cdd:MTH00153  106 SLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWS 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 161 IFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFS-RKPV 239
Cdd:MTH00153  186 VLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESgKKET 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 240 FGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIGFIFL 319
Cdd:MTH00153  266 FGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFL 345

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 320 FTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEVLGQIHFWSTFIGVNLTFMP 399
Cdd:MTH00153  346 FTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFP 425

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2177158292 400 MHFLGLAGMPRRIPDYPDAYTGWNLVASYGSYVSAFSTLFFFYLVFVSLTSN 451
Cdd:MTH00153  426 QHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISK 477
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-460 0e+00

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: 597.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292   1 GGCMSILIRMELAQPGNHLLlgNHQVYNVLITAHAFLMIFFMVMPVLiGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:TIGR02891  24 GGVLALLMRAQLATPGNTFM--DAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYLF 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292  81 SLCLLLTSALVEVGVGTGWTIYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWS 160
Cdd:TIGR02891 101 GGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWG 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 161 IFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFSRKPVF 240
Cdd:TIGR02891 181 ILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKPIF 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 241 GYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIGFIFLF 320
Cdd:TIGR02891 261 GYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLF 340

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 321 TIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEVLGQIHFWSTFIGVNLTFMPM 400
Cdd:TIGR02891 341 VIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPM 420

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2177158292 401 HFLGLAGMPRRIPDYPDA--YTGWNLVASYGSYVSAFSTLFFFYLVFVSLTSNNTCIDSPWD 460
Cdd:TIGR02891 421 HLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGANPWG 482
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-460 0e+00

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 587.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292   1 GGCMSILIRMELAQPGNHLLLGNHqvYNVLITAHAFLMIFFMVMPvLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:COG0843    33 GGLLALLMRLQLAGPGLGLLSPET--YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLF 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292  81 SLCLLLTSALVEVGVGTGWTIYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWS 160
Cdd:COG0843   110 GGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWA 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 161 IFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFSRKPVF 240
Cdd:COG0843   190 ALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKPLF 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 241 GYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIGFIFLF 320
Cdd:COG0843   270 GYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILF 349

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 321 TIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEVLGQIHFWSTFIGVNLTFMPM 400
Cdd:COG0843   350 VIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPM 429

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2177158292 401 HFLGLAGMPRRIPDYP--DAYTGWNLVASYGSYVSAFSTLFFFYLVFVSLTSNNTCIDSPWD 460
Cdd:COG0843   430 HILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPKAGGNPWG 491
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-432 1.97e-139

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: 407.34  E-value: 1.97e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292   1 GGCMSILIRMELAQPGNHLLlgNHQVYNVLITAHAFLMIFFMVMPVlIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:pfam00115  17 GGLLGLLIRLQLAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFWLVVL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292  81 SLCLLLTSALvevGVGTGWTIYPPLssiqshsgGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMyRMPLFVWS 160
Cdd:pfam00115  94 GAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 161 IFVTAFLLLLAVPVLAGAITMLLTDRNFNtsffdpAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFSRKPVF 240
Cdd:pfam00115 162 ILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRPLF 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 241 GYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHF-KTPMLFTIGFIFL 319
Cdd:pfam00115 236 GYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFFLGFAFL 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 320 FTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEVLGQIHFWSTFIGVNLTFMP 399
Cdd:pfam00115 316 FIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFP 395

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 2177158292 400 MHFLGLAGMPRRIP----DYPDAYTGWNLVASYGSYV 432
Cdd:pfam00115 396 MHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-459 0e+00

Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, may play a role in assembly or oxygen delivery to the active site. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center.


Pssm-ID: 238833  Cd Length: 488  Bit Score: 833.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292   1 GGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:cd01663    21 GTSLSLLIRLELSQPGS--QLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPP 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292  81 SLCLLLTSALVEVGVGTGWTIYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWS 160
Cdd:cd01663    99 SLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWS 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 161 IFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFS-RKPV 239
Cdd:cd01663   179 VLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSgKKPV 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 240 FGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIGFIFL 319
Cdd:cd01663   259 FGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFL 338

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 320 FTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEVLGQIHFWSTFIGVNLTFMP 399
Cdd:cd01663   339 FTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFP 418

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 400 MHFLGLAGMPRRIPDYPDAYTGWNLVASYGSYVSAFSTLFFFYLVFVSLTSNNTCIDSPW 459
Cdd:cd01663   419 QHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVG 478
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-451 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 749.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292   1 GGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:MTH00153   28 GTSLSLLIRAELGQPGS--LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292  81 SLCLLLTSALVEVGVGTGWTIYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWS 160
Cdd:MTH00153  106 SLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWS 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 161 IFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFS-RKPV 239
Cdd:MTH00153  186 VLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESgKKET 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 240 FGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIGFIFL 319
Cdd:MTH00153  266 FGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFL 345

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 320 FTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEVLGQIHFWSTFIGVNLTFMP 399
Cdd:MTH00153  346 FTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFP 425

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2177158292 400 MHFLGLAGMPRRIPDYPDAYTGWNLVASYGSYVSAFSTLFFFYLVFVSLTSN 451
Cdd:MTH00153  426 QHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISK 477
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-451 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 703.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292   1 GGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:MTH00167   30 GTALSLLIRAELSQPGS--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292  81 SLCLLLTSALVEVGVGTGWTIYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWS 160
Cdd:MTH00167  108 SLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWS 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 161 IFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFS-RKPV 239
Cdd:MTH00167  188 ILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSgKKEP 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 240 FGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIGFIFL 319
Cdd:MTH00167  268 FGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFL 347

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 320 FTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEVLGQIHFWSTFIGVNLTFMP 399
Cdd:MTH00167  348 FTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFIGVNLTFFP 427

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2177158292 400 MHFLGLAGMPRRIPDYPDAYTGWNLVASYGSYVSAFSTLFFFYLVFVSLTSN 451
Cdd:MTH00167  428 QHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSK 479
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-450 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 692.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292   1 GGCMSILIRMELAQPGnhLLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:MTH00223   27 GTSLSLLIRAELGQPG--ALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPP 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292  81 SLCLLLTSALVEVGVGTGWTIYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWS 160
Cdd:MTH00223  105 SLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWS 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 161 IFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFSRK-PV 239
Cdd:MTH00223  185 VKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKkEV 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 240 FGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIGFIFL 319
Cdd:MTH00223  265 FGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFL 344

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 320 FTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEVLGQIHFWSTFIGVNLTFMP 399
Cdd:MTH00223  345 FTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFLMFLGVNLTFFP 424

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2177158292 400 MHFLGLAGMPRRIPDYPDAYTGWNLVASYGSYVSAFSTLFFFYLVFVSLTS 450
Cdd:MTH00223  425 QHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVS 475
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-450 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 672.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292   1 GGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:MTH00116   30 GTALSLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292  81 SLCLLLTSALVEVGVGTGWTIYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWS 160
Cdd:MTH00116  108 SFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWS 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 161 IFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFS-RKPV 239
Cdd:MTH00116  188 VLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAgKKEP 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 240 FGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIGFIFL 319
Cdd:MTH00116  268 FGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFL 347

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 320 FTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEVLGQIHFWSTFIGVNLTFMP 399
Cdd:MTH00116  348 FTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFP 427

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2177158292 400 MHFLGLAGMPRRIPDYPDAYTGWNLVASYGSYVSAFSTLFFFYLVFVSLTS 450
Cdd:MTH00116  428 QHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSS 478
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-459 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 667.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292   1 GGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:MTH00142   28 GTGLSLLIRAELGQPGS--LLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292  81 SLCLLLTSALVEVGVGTGWTIYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWS 160
Cdd:MTH00142  106 ALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWS 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 161 IFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFS-RKPV 239
Cdd:MTH00142  186 VKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSgKKEV 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 240 FGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIGFIFL 319
Cdd:MTH00142  266 FGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFL 345

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 320 FTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEVLGQIHFWSTFIGVNLTFMP 399
Cdd:MTH00142  346 FTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYTMFIGVNLTFFP 425

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 400 MHFLGLAGMPRRIPDYPDAYTGWNLVASYGSYVSAFSTLFFFYLVFVSLTSNNTCIDSPW 459
Cdd:MTH00142  426 QHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVMWSSH 485
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-445 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 634.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292   1 GGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:MTH00182   32 GTAFSMLIRLELSAPGA--MLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPP 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292  81 SLCLLLTSALVEVGVGTGWTIYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWS 160
Cdd:MTH00182  110 ALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWS 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 161 IFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFS-RKPV 239
Cdd:MTH00182  190 ILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVaKKQI 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 240 FGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIGFIFL 319
Cdd:MTH00182  270 FGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFL 349

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 320 FTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEVLGQIHFWSTFIGVNLTFMP 399
Cdd:MTH00182  350 FTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWLMFIGVNLTFFP 429

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 2177158292 400 MHFLGLAGMPRRIPDYPDAYTGWNLVASYGSYVSAFSTLFFFYLVF 445
Cdd:MTH00182  430 QHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIY 475
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-445 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 632.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292   1 GGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:MTH00184   32 GTAFSMLIRLELSAPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPP 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292  81 SLCLLLTSALVEVGVGTGWTIYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWS 160
Cdd:MTH00184  110 ALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWS 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 161 IFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFS-RKPV 239
Cdd:MTH00184  190 ILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAaKKQI 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 240 FGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIGFIFL 319
Cdd:MTH00184  270 FGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFL 349

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 320 FTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEVLGQIHFWSTFIGVNLTFMP 399
Cdd:MTH00184  350 FTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMFIGVNLTFFP 429

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 2177158292 400 MHFLGLAGMPRRIPDYPDAYTGWNLVASYGSYVSAFSTLFFFYLVF 445
Cdd:MTH00184  430 QHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVY 475
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-455 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 617.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292   1 GGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:MTH00037   30 GTAMSVIIRTELAQPGS--LLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPP 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292  81 SLCLLLTSALVEVGVGTGWTIYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWS 160
Cdd:MTH00037  108 SFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWS 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 161 IFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFSRK-PV 239
Cdd:MTH00037  188 VFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKqEP 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 240 FGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIGFIFL 319
Cdd:MTH00037  268 FGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFL 347

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 320 FTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEVLGQIHFWSTFIGVNLTFMP 399
Cdd:MTH00037  348 FTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFLMFIGVNLTFFP 427

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2177158292 400 MHFLGLAGMPRRIPDYPDAYTGWNLVASYGSYVSAFSTLFFFYLVFVSLTSNNTCI 455
Cdd:MTH00037  428 QHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVI 483
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-458 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 600.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292   1 GGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:MTH00007   27 GTSMSLLIRIELGQPGA--FLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPP 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292  81 SLCLLLTSALVEVGVGTGWTIYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWS 160
Cdd:MTH00007  105 ALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWA 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 161 IFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFSRKP-V 239
Cdd:MTH00007  185 VVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLeP 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 240 FGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIGFIFL 319
Cdd:MTH00007  265 FGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFL 344

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 320 FTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEVLGQIHFWSTFIGVNLTFMP 399
Cdd:MTH00007  345 FTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFLMFLGVNLTFFP 424

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2177158292 400 MHFLGLAGMPRRIPDYPDAYTGWNLVASYGSYVSAFSTLFFFYLVFVSLTSNNTCIDSP 458
Cdd:MTH00007  425 QHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIASP 483
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-460 0e+00

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: 597.28  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292   1 GGCMSILIRMELAQPGNHLLlgNHQVYNVLITAHAFLMIFFMVMPVLiGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:TIGR02891  24 GGVLALLMRAQLATPGNTFM--DAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYLF 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292  81 SLCLLLTSALVEVGVGTGWTIYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWS 160
Cdd:TIGR02891 101 GGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWG 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 161 IFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFSRKPVF 240
Cdd:TIGR02891 181 ILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKPIF 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 241 GYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIGFIFLF 320
Cdd:TIGR02891 261 GYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLF 340

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 321 TIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEVLGQIHFWSTFIGVNLTFMPM 400
Cdd:TIGR02891 341 VIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPM 420

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2177158292 401 HFLGLAGMPRRIPDYPDA--YTGWNLVASYGSYVSAFSTLFFFYLVFVSLTSNNTCIDSPWD 460
Cdd:TIGR02891 421 HLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGANPWG 482
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-450 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 595.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292   1 GGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:MTH00183   30 GTALSLLIRAELSQPGA--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPP 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292  81 SLCLLLTSALVEVGVGTGWTIYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWS 160
Cdd:MTH00183  108 SFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWA 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 161 IFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFS-RKPV 239
Cdd:MTH00183  188 VLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSgKKEP 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 240 FGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIGFIFL 319
Cdd:MTH00183  268 FGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFL 347

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 320 FTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEVLGQIHFWSTFIGVNLTFMP 399
Cdd:MTH00183  348 FTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVMFVGVNLTFFP 427

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2177158292 400 MHFLGLAGMPRRIPDYPDAYTGWNLVASYGSYVSAFSTLFFFYLVFVSLTS 450
Cdd:MTH00183  428 QHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAA 478
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-450 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 594.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292   1 GGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:MTH00103   30 GTALSLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292  81 SLCLLLTSALVEVGVGTGWTIYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWS 160
Cdd:MTH00103  108 SFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWS 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 161 IFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFS-RKPV 239
Cdd:MTH00103  188 VLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSgKKEP 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 240 FGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIGFIFL 319
Cdd:MTH00103  268 FGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFL 347

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 320 FTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEVLGQIHFWSTFIGVNLTFMP 399
Cdd:MTH00103  348 FTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIMFVGVNMTFFP 427

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2177158292 400 MHFLGLAGMPRRIPDYPDAYTGWNLVASYGSYVSAFSTLFFFYLVFVSLTS 450
Cdd:MTH00103  428 QHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFAS 478
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-450 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 591.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292   1 GGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:MTH00077   30 GTALSLLIRAELSQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292  81 SLCLLLTSALVEVGVGTGWTIYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWS 160
Cdd:MTH00077  108 SFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWS 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 161 IFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFS-RKPV 239
Cdd:MTH00077  188 VLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSaKKEP 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 240 FGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIGFIFL 319
Cdd:MTH00077  268 FGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFL 347

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 320 FTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEVLGQIHFWSTFIGVNLTFMP 399
Cdd:MTH00077  348 FTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVMFIGVNLTFFP 427

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2177158292 400 MHFLGLAGMPRRIPDYPDAYTGWNLVASYGSYVSAFSTLFFFYLVFVSLTS 450
Cdd:MTH00077  428 QHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSS 478
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-448 0e+00

Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. Membership in the superfamily is defined by subunit I, which contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons to the binuclear center. Only subunit I is common to the entire superfamily. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from the electron donor on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I of cytochrome c oxidase (CcO) and ubiquinol oxidase. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electron transfer occurs in two segments: from the electron donor to the low-spin heme, and from the low-spin heme to the binuclear center. The first segment can be a multi-step process and varies among the different families, while the second segment, a direct transfer, is consistent throughout the superfamily.


Pssm-ID: 238461  Cd Length: 463  Bit Score: 588.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292   1 GGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPiMIGSPDMAFPRLNNISFWLLPP 80
Cdd:cd00919    19 GGLLALLIRLELATPGS--LFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPP 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292  81 SLCLLLTSALVEVGVGTGWTIYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWS 160
Cdd:cd00919    96 GLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWS 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 161 IFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFSRKPVF 240
Cdd:cd00919   176 VLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGKPLF 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 241 GYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIGFIFLF 320
Cdd:cd00919   256 GYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLF 335

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 321 TIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEVLGQIHFWSTFIGVNLTFMPM 400
Cdd:cd00919   336 TIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGFNLTFFPM 415

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 2177158292 401 HFLGLAGMPRRIPDYPDAYTGWNLVASYGSYVSAFSTLFFFYLVFVSL 448
Cdd:cd00919   416 HFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-460 0e+00

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 587.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292   1 GGCMSILIRMELAQPGNHLLLGNHqvYNVLITAHAFLMIFFMVMPvLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:COG0843    33 GGLLALLMRLQLAGPGLGLLSPET--YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLF 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292  81 SLCLLLTSALVEVGVGTGWTIYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWS 160
Cdd:COG0843   110 GGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWA 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 161 IFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFSRKPVF 240
Cdd:COG0843   190 ALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKPLF 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 241 GYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIGFIFLF 320
Cdd:COG0843   270 GYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILF 349

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 321 TIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEVLGQIHFWSTFIGVNLTFMPM 400
Cdd:COG0843   350 VIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPM 429

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2177158292 401 HFLGLAGMPRRIPDYP--DAYTGWNLVASYGSYVSAFSTLFFFYLVFVSLTSNNTCIDSPWD 460
Cdd:COG0843   430 HILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPKAGGNPWG 491
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-452 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 587.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292   1 GGCMSILIRMELAQPGnhLLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:MTH00079   31 GTSLSLIIRLELSKPG--LLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPT 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292  81 SLCLLLTSALVEVGVGTGWTIYPPLSSiQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWS 160
Cdd:MTH00079  109 SLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWT 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 161 IFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFS-RKPV 239
Cdd:MTH00079  188 VFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTgKKEV 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 240 FGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIGFIFL 319
Cdd:MTH00079  268 FGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFL 347

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 320 FTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEVLGQIHFWSTFIGVNLTFMP 399
Cdd:MTH00079  348 FTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFVGVNLTFFP 427

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2177158292 400 MHFLGLAGMPRRIPDYPDAYTGWNLVASYGSYVSAFSTLFFFYLVFVSLTSNN 452
Cdd:MTH00079  428 LHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYR 480
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-445 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 554.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292   1 GGCMSILIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:MTH00026   31 GTAFSMLIRLELSSPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPP 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292  81 SLCLLLTSALVEVGVGTGWTIYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWS 160
Cdd:MTH00026  109 ALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWS 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 161 IFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFS-RKPV 239
Cdd:MTH00026  189 VFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSyKKQI 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 240 FGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEG--SIHFKTPMLFTIGFI 317
Cdd:MTH00026  269 FGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSgrNLIFTTPMAWALGFI 348

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 318 FLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEVLGQIHFWSTFIGVNLTF 397
Cdd:MTH00026  349 FLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLMFIGVNITF 428

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 2177158292 398 MPMHFLGLAGMPRRIPDYPDAYTGWNLVASYGSYVSAFSTLFFFYLVF 445
Cdd:MTH00026  429 FPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIF 476
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-460 0e+00

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: 529.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292   1 GGCMSILIRMELAQPGNHLLLGNHqvYNVLITAHAFLMIFFMVMPVLIGgFGNWLVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:cd01662    25 GGVDALLMRTQLALPGNDFLSPEH--YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLF 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292  81 SLCLLLTSALVEVGVGTGWTIYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWS 160
Cdd:cd01662   102 GGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWT 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 161 IFVTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFSRKPVF 240
Cdd:cd01662   182 TLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRKPLF 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 241 GYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIGFIFLF 320
Cdd:cd01662   262 GYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTF 341

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 321 TIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEVLGQIHFWSTFIGVNLTFMPM 400
Cdd:cd01662   342 VIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFNLTFFPM 421

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2177158292 401 HFLGLAGMPRRIPDYP--DAYTGWNLVASYGSYVSAFSTLFFFYLVFVSL-TSNNTCIDSPWD 460
Cdd:cd01662   422 HILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLINVIVSIrKGKRDATGDPWG 484
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 4-452 2.18e-151

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 440.65  E-value: 2.18e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292   4 MSILIRMELAQPGNHLLlgNHQVYNVLITAHAFLMIFFMVMPVLIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSLC 83
Cdd:MTH00048   34 LSLLIRLNFLDPYYNVI--SLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIV 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292  84 LLLTSALVevGVGTGWTIYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPgQTMYRMPLFVWSIFV 163
Cdd:MTH00048  112 FLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMT-NVFSRTSIILWSYLF 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 164 TAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFSRKP-VFGY 242
Cdd:MTH00048  189 TSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDdPFGY 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 243 IGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPML-FTIGFIFLFT 321
Cdd:MTH00048  269 YGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSDPVVwWVVSFIVLFT 348

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 322 IGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEVLGQIHFWSTFIGVNLTFMPMH 401
Cdd:MTH00048  349 IGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIGFNLCFFPMH 428

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2177158292 402 FLGLAGMPRRIPDYPDAYTGWNLVASYGSYVSAFSTLFFFYLVFVSLTSNN 452
Cdd:MTH00048  429 YFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKN 479
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-432 1.97e-139

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: 407.34  E-value: 1.97e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292   1 GGCMSILIRMELAQPGNHLLlgNHQVYNVLITAHAFLMIFFMVMPVlIGGFGNWLVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:pfam00115  17 GGLLGLLIRLQLAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFWLVVL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292  81 SLCLLLTSALvevGVGTGWTIYPPLssiqshsgGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMyRMPLFVWS 160
Cdd:pfam00115  94 GAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 161 IFVTAFLLLLAVPVLAGAITMLLTDRNFNtsffdpAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFSRKPVF 240
Cdd:pfam00115 162 ILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRPLF 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 241 GYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHF-KTPMLFTIGFIFL 319
Cdd:pfam00115 236 GYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFFLGFAFL 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 320 FTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEVLGQIHFWSTFIGVNLTFMP 399
Cdd:pfam00115 316 FIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFP 395

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 2177158292 400 MHFLGLAGMPRRIP----DYPDAYTGWNLVASYGSYV 432
Cdd:pfam00115 396 MHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
CyoB TIGR02843
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ...
 6-460 3.66e-133

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: 398.66  E-value: 3.66e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292   6 ILIRME--LAQPGNHLLLGNHQvYNVLITAHAFLMIFFMVMPVLIGGFgNWLVPIMIGSPDMAFPRLNNISFWLLPPSLC 83
Cdd:TIGR02843  76 IMMRTQqaLASGGSAGYLPPHH-YDQIFTAHGVIMIFFVAMPFVFGLM-NLVVPLQIGARDVAFPFLNSLSFWLTVVGAI 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292  84 LLLTSALVEVGVGTGWTIYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWSIFV 163
Cdd:TIGR02843 154 LVNVSLGVGEFAQTGWLAYPPLSELQYSPGVGVDYYIWALQISGIGTLLTGINFFVTIIKMRAPGMTLMKMPVFTWTSLC 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 164 TAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFSRKPVFGYI 243
Cdd:TIGR02843 234 SNVLIIASFPILTVTLALLTLDRYLGMHFFTNEAGGNPMMYVNLIWAWGHPEVYILILPAFGIFSEVVATFSRKRLFGYT 313

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 244 GMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIGFIFLFTIG 323
Cdd:TIGR02843 314 SMVWATIAITVLSFIVWLHHFFTMGAGANVNAFFGIATMIIAIPTGVKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIG 393

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 324 GLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEVLGQIHFWSTFIGVNLTFMPMHFL 403
Cdd:TIGR02843 394 GMTGVLLAVPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWFPKAFGFKLNEKLGKRSFWCWFIGFYLAFMPLYIL 473

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2177158292 404 GLAGMPRRIPDYPD-AYTGWNLVASYGSYVSAFSTLFFFYLVFVSLTSNNTCIDS---PWD 460
Cdd:TIGR02843 474 GFMGMTRRLNHYDNpEWHPMLIIAAFGAFLIACGILCQIIQIFVSIRDRDQNRDTtgdPWG 534
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 5-459 3.36e-109

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 337.29  E-value: 3.36e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292   5 SILIRME--LAQPGNHLLLGNHQvYNVLITAHAFLMIFFMVMPVLIGgFGNWLVPIMIGSPDMAFPRLNNISFWLLPPSL 82
Cdd:PRK15017   76 AIMMRSQqaLASAGEAGFLPPHH-YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGV 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292  83 CLLLTSALVEVGVGTGWTIYPPLSSIQSHSGGAVDLAIFSLHISGASSILGAVNFISTILNMRNPGQTMYRMPLFVWSIF 162
Cdd:PRK15017  154 ILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASL 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 163 VTAFLLLLAVPVLAGAITMLLTDRNFNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFSRKPVFGY 242
Cdd:PRK15017  234 CANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGY 313

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 243 IGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIHFKTPMLFTIGFIFLFTI 322
Cdd:PRK15017  314 TSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSV 393

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 323 GGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYPEVLGQIHFWSTFIGVNLTFMPMHF 402
Cdd:PRK15017  394 GGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYA 473

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2177158292 403 LGLAGMPRRIPDYPD-AYTGWNLVASYGSYVSAFSTLFFFYLVFVSLTS---NNTCIDSPW 459
Cdd:PRK15017  474 LGFMGMTRRLSQQIDpQFHTMLMIAASGAALIALGILCQVIQMYVSIRDrdqNRDLTGDPW 534
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 16-449 1.12e-20

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: 94.28  E-value: 1.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292  16 GNHLLLGNHQVYNVLITAHAFLMIFfmVMPVL-IGGFGNWLVPIMIGSPDMAfPRLNNISFWLLPPSlcllltSALVEVG 94
Cdd:cd01660    33 GVFPLPSSGILYYQGLTLHGVLLAI--VFTTFfIMGFFYAIVARALLRSLFN-RRLAWAGFWLMVIG------TVMAAVP 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292  95 VGTG-----WTIYPPLssiQSHSGGAVDLAIFSLhisgASSILGAVNFI-STILNMRNPGQtmyRMPLFVWSIFVTAFLL 168
Cdd:cd01660   104 ILLGqasvlYTFYPPL---QAHPLFYIGAALVVV----GSWISGFAMFVtLWRWKKANPGK---KVPLATFMVVTTMILW 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 169 LLAVPVLagAITMLLtdrnfntsFFDPAGGG-----DPVLYQHLFWFFGHPEVYILILPGFGMVSHIVSTFSRKPVFGYI 243
Cdd:cd01660   174 LVASLGV--ALEVLF--------QLLPWSLGlvdtvDVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDP 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 244 GMVYAMVSIGVLGFIVWAHHMYT-VGLDVDTRAYFTAATMIIAVPTGIKIFSWIATM--------------WEGSIHFKT 308
Cdd:cd01660   244 LARLAFILFLLFSTPVGFHHQFAdPGIGPGWKFIHMVLTFMVALPSLLTAFTVFASLeiagrlrggkglfgWIRALPWGD 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177158292 309 PMLFTIGF-IFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHyvLSMGAVFAI-FAGFYYWF-GKITGLQYPEV-LGQI 384
Cdd:cd01660   324 PMFLALFLaMLMFIPGGAGGIINASYQLNYVVHNTAWVPGHFH--LTVGGAVALtFMAVAYWLvPHLTGRELAAKrLALA 401

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2177158292 385 HFWSTFIGVNLTFMPMHFLGLAGMPRR--IPDYPDAY-----TGWNLVASYGSYVSAFSTLFFFYLVFVSLT 449
Cdd:cd01660   402 QPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGGLPaagewAPYQQLMAIGGTILFVSGALFLYILFRTLL 473
 
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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