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Conserved domains on  [gi|1016561360|gb|AMX21981|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Halichrysis micans]

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 ...
 1-410 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: 745.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360   1 TLYLIFGAFSGILGGCMSVLIRMELAQPGNhlLLGNHQLYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAF 80
Cdd:cd01663     8 TLYLIFGLWSGLVGTSLSLLIRLELSQPGS--QLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAF 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360  81 PRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHVSGASSILGAINFISTIINMRNS 160
Cdd:cd01663    86 PRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAP 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 161 GQNMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMV 240
Cdd:cd01663   166 GMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGII 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 241 SHVVSTFS-RKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWDGSIHL 319
Cdd:cd01663   246 SHIISTFSgKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKF 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 320 KTPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYSELLGQIHF 399
Cdd:cd01663   326 ETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHF 405

                         410
                  ....*....|.
gi 1016561360 400 WSTFIGVNLTF 410
Cdd:cd01663   406 WLMFIGVNLTF 416
 
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 ...
 1-410 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: 745.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360   1 TLYLIFGAFSGILGGCMSVLIRMELAQPGNhlLLGNHQLYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAF 80
Cdd:cd01663     8 TLYLIFGLWSGLVGTSLSLLIRLELSQPGS--QLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAF 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360  81 PRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHVSGASSILGAINFISTIINMRNS 160
Cdd:cd01663    86 PRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAP 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 161 GQNMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMV 240
Cdd:cd01663   166 GMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGII 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 241 SHVVSTFS-RKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWDGSIHL 319
Cdd:cd01663   246 SHIISTFSgKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKF 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 320 KTPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYSELLGQIHF 399
Cdd:cd01663   326 ETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHF 405

                         410
                  ....*....|.
gi 1016561360 400 WSTFIGVNLTF 410
Cdd:cd01663   406 WLMFIGVNLTF 416
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-410 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 688.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360   1 TLYLIFGAFSGILGGCMSVLIRMELAQPGNhlLLGNHQLYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00153   15 TLYFIFGAWSGMVGTSLSLLIRAELGQPGS--LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAF 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360  81 PRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHVSGASSILGAINFISTIINMRNS 160
Cdd:MTH00153   93 PRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSK 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 161 GQNMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMV 240
Cdd:MTH00153  173 GMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 241 SHVVSTFS-RKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWDGSIHL 319
Cdd:MTH00153  253 SHIISQESgKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINY 332

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 320 KTPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYSELLGQIHF 399
Cdd:MTH00153  333 SPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQF 412

                         410
                  ....*....|.
gi 1016561360 400 WSTFIGVNLTF 410
Cdd:MTH00153  413 FIMFIGVNLTF 423
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-410 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: 531.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360   1 TLYLIFGAFSGILGGCMSVLIRMELAQPGNHLLlgNHQLYNVLITAHAFLMIFFMVMPvMIGGFGNWLVPIMIGSPDMAF 80
Cdd:TIGR02891  11 ILYLVTAFAFFLVGGVLALLMRAQLATPGNTFM--DAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIGARDMAF 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360  81 PRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHVSGASSILGAINFISTIINMRNS 160
Cdd:TIGR02891  88 PRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAP 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 161 GQNMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMV 240
Cdd:TIGR02891 168 GMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGII 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 241 SHVVSTFSRKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWDGSIHLK 320
Cdd:TIGR02891 248 SEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFT 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 321 TPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYSELLGQIHFW 400
Cdd:TIGR02891 328 TPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFW 407

                         410
                  ....*....|
gi 1016561360 401 STFIGVNLTF 410
Cdd:TIGR02891 408 LTFVGFNLTF 417
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-410 0e+00

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 519.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360   2 LYLIFGAFSGILGGCMSVLIRMELAQPGNHLLLGNHqlYNVLITAHAFLMIFFMVMPvMIGGFGNWLVPIMIGSPDMAFP 81
Cdd:COG0843    21 MYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPET--YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360  82 RLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHVSGASSILGAINFISTIINMRNSG 161
Cdd:COG0843    98 RLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPG 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 162 QNMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMVS 241
Cdd:COG0843   178 MTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVS 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 242 HVVSTFSRKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWDGSIHLKT 321
Cdd:COG0843   258 EIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTT 337

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 322 PMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYSELLGQIHFWS 401
Cdd:COG0843   338 PMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWL 417


                  ....*....
gi 1016561360 402 TFIGVNLTF 410
Cdd:COG0843   418 WFIGFNLTF 426
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 2-410 3.59e-125

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: 368.44  E-value: 3.59e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360   2 LYLIFGAFSGILGGCMSVLIRMELAQPGNHLLlgNHQLYNVLITAHAFLMIFFMVMPvMIGGFGNWLVPIMIGSPDMAFP 81
Cdd:pfam00115   5 LYLVTALVWFLVGGLLGLLIRLQLAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360  82 RLNNISFWLLPPSLCLLLTSALvevGVGTGWTVYPPLssiqshsgGAVDLAIFSLHVSGASSILGAINFISTIINMRNSG 161
Cdd:pfam00115  82 RLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPG 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 162 QNMyRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNttffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGMVS 241
Cdd:pfam00115 151 MTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIY 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 242 HVVSTFSRKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWDGSIHL-K 320
Cdd:pfam00115 224 YILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrT 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 321 TPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYSELLGQIHFW 400
Cdd:pfam00115 304 TPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFW 383

                         410
                  ....*....|
gi 1016561360 401 STFIGVNLTF 410
Cdd:pfam00115 384 LLFIGFNLTF 393
 
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 ...
 1-410 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: 745.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360   1 TLYLIFGAFSGILGGCMSVLIRMELAQPGNhlLLGNHQLYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAF 80
Cdd:cd01663     8 TLYLIFGLWSGLVGTSLSLLIRLELSQPGS--QLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAF 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360  81 PRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHVSGASSILGAINFISTIINMRNS 160
Cdd:cd01663    86 PRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAP 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 161 GQNMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMV 240
Cdd:cd01663   166 GMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGII 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 241 SHVVSTFS-RKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWDGSIHL 319
Cdd:cd01663   246 SHIISTFSgKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKF 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 320 KTPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYSELLGQIHF 399
Cdd:cd01663   326 ETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHF 405

                         410
                  ....*....|.
gi 1016561360 400 WSTFIGVNLTF 410
Cdd:cd01663   406 WLMFIGVNLTF 416
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-410 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 688.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360   1 TLYLIFGAFSGILGGCMSVLIRMELAQPGNhlLLGNHQLYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00153   15 TLYFIFGAWSGMVGTSLSLLIRAELGQPGS--LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAF 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360  81 PRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHVSGASSILGAINFISTIINMRNS 160
Cdd:MTH00153   93 PRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSK 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 161 GQNMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMV 240
Cdd:MTH00153  173 GMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 241 SHVVSTFS-RKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWDGSIHL 319
Cdd:MTH00153  253 SHIISQESgKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINY 332

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 320 KTPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYSELLGQIHF 399
Cdd:MTH00153  333 SPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQF 412

                         410
                  ....*....|.
gi 1016561360 400 WSTFIGVNLTF 410
Cdd:MTH00153  413 FIMFIGVNLTF 423
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-410 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 648.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360   1 TLYLIFGAFSGILGGCMSVLIRMELAQPGNhlLLGNHQLYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00167   17 TLYFIFGAWAGMVGTALSLLIRAELSQPGS--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360  81 PRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHVSGASSILGAINFISTIINMRNS 160
Cdd:MTH00167   95 PRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPP 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 161 GQNMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMV 240
Cdd:MTH00167  175 GITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 241 SHVVSTFS-RKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWDGSIHL 319
Cdd:MTH00167  255 SHIVVYYSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKW 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 320 KTPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYSELLGQIHF 399
Cdd:MTH00167  335 ETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHF 414

                         410
                  ....*....|.
gi 1016561360 400 WSTFIGVNLTF 410
Cdd:MTH00167  415 FVMFIGVNLTF 425
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-410 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 635.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360   1 TLYLIFGAFSGILGGCMSVLIRMELAQPGnhLLLGNHQLYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00223   14 TLYLIFGMWSGLVGTSLSLLIRAELGQPG--ALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAF 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360  81 PRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHVSGASSILGAINFISTIINMRNS 160
Cdd:MTH00223   92 PRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSP 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 161 GQNMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMV 240
Cdd:MTH00223  172 GMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 241 SHVVSTFSRK-PVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWDGSIHL 319
Cdd:MTH00223  252 SHIVSHYSSKkEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKY 331

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 320 KTPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYSELLGQIHF 399
Cdd:MTH00223  332 EAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHF 411

                         410
                  ....*....|.
gi 1016561360 400 WSTFIGVNLTF 410
Cdd:MTH00223  412 FLMFLGVNLTF 422
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-410 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 630.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360   1 TLYLIFGAFSGILGGCMSVLIRMELAQPGNhlLLGNHQLYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00116   17 TLYLIFGAWAGMVGTALSLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360  81 PRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHVSGASSILGAINFISTIINMRNS 160
Cdd:MTH00116   95 PRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPP 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 161 GQNMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMV 240
Cdd:MTH00116  175 AMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGII 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 241 SHVVSTFS-RKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWDGSIHL 319
Cdd:MTH00116  255 SHIVTYYAgKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKW 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 320 KTPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYSELLGQIHF 399
Cdd:MTH00116  335 DPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQF 414

                         410
                  ....*....|.
gi 1016561360 400 WSTFIGVNLTF 410
Cdd:MTH00116  415 GVMFTGVNLTF 425
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-410 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 609.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360   1 TLYLIFGAFSGILGGCMSVLIRMELAQPGNhlLLGNHQLYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00142   15 TLYFLFGAWAGMVGTGLSLLIRAELGQPGS--LLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAF 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360  81 PRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHVSGASSILGAINFISTIINMRNS 160
Cdd:MTH00142   93 PRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAG 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 161 GQNMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMV 240
Cdd:MTH00142  173 GMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 241 SHVVSTFS-RKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWDGSIHL 319
Cdd:MTH00142  253 SHIINHYSgKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKY 332

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 320 KTPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYSELLGQIHF 399
Cdd:MTH00142  333 EPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHF 412

                         410
                  ....*....|.
gi 1016561360 400 WSTFIGVNLTF 410
Cdd:MTH00142  413 YTMFIGVNLTF 423
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-410 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 595.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360   1 TLYLIFGAFSGILGGCMSVLIRMELAQPGNhlLLGNHQLYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00182   19 TLYLVFGAGAGMIGTAFSMLIRLELSAPGA--MLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAF 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360  81 PRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHVSGASSILGAINFISTIINMRNS 160
Cdd:MTH00182   97 PRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAP 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 161 GQNMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMV 240
Cdd:MTH00182  177 GVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMI 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 241 SHVVSTFS-RKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWDGSIHL 319
Cdd:MTH00182  257 SQIIPTFVaKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRL 336

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 320 KTPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYSELLGQIHF 399
Cdd:MTH00182  337 DTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHF 416

                         410
                  ....*....|.
gi 1016561360 400 WSTFIGVNLTF 410
Cdd:MTH00182  417 WLMFIGVNLTF 427
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-410 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 591.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360   1 TLYLIFGAFSGILGGCMSVLIRMELAQPGNhlLLGNHQLYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00184   19 TLYLLFGAFAGMIGTAFSMLIRLELSAPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAF 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360  81 PRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHVSGASSILGAINFISTIINMRNS 160
Cdd:MTH00184   97 PRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAP 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 161 GQNMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMV 240
Cdd:MTH00184  177 GITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGII 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 241 SHVVSTFS-RKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWDGSIHL 319
Cdd:MTH00184  257 SQIIPTFAaKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRL 336

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 320 KTPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYSELLGQIHF 399
Cdd:MTH00184  337 DTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHF 416

                         410
                  ....*....|.
gi 1016561360 400 WSTFIGVNLTF 410
Cdd:MTH00184  417 WLMFIGVNLTF 427
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-410 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 566.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360   1 TLYLIFGAFSGILGGCMSVLIRMELAQPGNhlLLGNHQLYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00037   17 TLYLIFGAWAGMVGTAMSVIIRTELAQPGS--LLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360  81 PRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHVSGASSILGAINFISTIINMRNS 160
Cdd:MTH00037   95 PRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTP 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 161 GQNMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMV 240
Cdd:MTH00037  175 GMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMI 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 241 SHVVSTFSRK-PVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWDGSIHL 319
Cdd:MTH00037  255 SHVIAHYSGKqEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRW 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 320 KTPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYSELLGQIHF 399
Cdd:MTH00037  335 ETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHF 414

                         410
                  ....*....|.
gi 1016561360 400 WSTFIGVNLTF 410
Cdd:MTH00037  415 FLMFIGVNLTF 425
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-410 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 551.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360   1 TLYLIFGAFSGILGGCMSVLIRMELAQPGNhlLLGNHQLYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00183   17 TLYLVFGAWAGMVGTALSLLIRAELSQPGA--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360  81 PRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHVSGASSILGAINFISTIINMRNS 160
Cdd:MTH00183   95 PRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPP 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 161 GQNMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMV 240
Cdd:MTH00183  175 AISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 241 SHVVSTFS-RKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWDGSIHL 319
Cdd:MTH00183  255 SHIVAYYSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKW 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 320 KTPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYSELLGQIHF 399
Cdd:MTH00183  335 ETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHF 414

                         410
                  ....*....|.
gi 1016561360 400 WSTFIGVNLTF 410
Cdd:MTH00183  415 GVMFVGVNLTF 425
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-410 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 550.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360   1 TLYLIFGAFSGILGGCMSVLIRMELAQPGNhlLLGNHQLYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00103   17 TLYLLFGAWAGMVGTALSLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360  81 PRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHVSGASSILGAINFISTIINMRNS 160
Cdd:MTH00103   95 PRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPP 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 161 GQNMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMV 240
Cdd:MTH00103  175 AMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 241 SHVVSTFS-RKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWDGSIHL 319
Cdd:MTH00103  255 SHIVTYYSgKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKW 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 320 KTPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYSELLGQIHF 399
Cdd:MTH00103  335 SPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHF 414

                         410
                  ....*....|.
gi 1016561360 400 WSTFIGVNLTF 410
Cdd:MTH00103  415 TIMFVGVNMTF 425
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-410 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 549.50  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360   1 TLYLIFGAFSGILGGCMSVLIRMELAQPGNhlLLGNHQLYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00007   14 TLYFILGVWGGLLGTSMSLLIRIELGQPGA--FLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAF 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360  81 PRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHVSGASSILGAINFISTIINMRNS 160
Cdd:MTH00007   92 PRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWK 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 161 GQNMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMV 240
Cdd:MTH00007  172 GLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAI 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 241 SHVVSTFSRKP-VFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWDGSIHL 319
Cdd:MTH00007  252 SHIVTHYAGKLePFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKY 331

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 320 KTPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYSELLGQIHF 399
Cdd:MTH00007  332 ETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHF 411

                         410
                  ....*....|.
gi 1016561360 400 WSTFIGVNLTF 410
Cdd:MTH00007  412 FLMFLGVNLTF 422
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-410 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 547.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360   1 TLYLIFGAFSGILGGCMSVLIRMELAQPGNhlLLGNHQLYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00077   17 TLYLVFGAWAGMVGTALSLLIRAELSQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360  81 PRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHVSGASSILGAINFISTIINMRNS 160
Cdd:MTH00077   95 PRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPP 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 161 GQNMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMV 240
Cdd:MTH00077  175 SMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMI 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 241 SHVVSTFS-RKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWDGSIHL 319
Cdd:MTH00077  255 SHIVTYYSaKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKW 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 320 KTPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYSELLGQIHF 399
Cdd:MTH00077  335 DAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHF 414

                         410
                  ....*....|.
gi 1016561360 400 WSTFIGVNLTF 410
Cdd:MTH00077  415 GVMFIGVNLTF 425
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-410 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 533.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360   1 TLYLIFGAFSGILGGCMSVLIRMELAQPGnhLLLGNHQLYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00079   18 TLYFLFGLWSGMVGTSLSLIIRLELSKPG--LLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSF 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360  81 PRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSiQSHSGGAVDLAIFSLHVSGASSILGAINFISTIINMRNS 160
Cdd:MTH00079   96 PRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSS 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 161 GQNMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMV 240
Cdd:MTH00079  175 SISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGII 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 241 SHVVSTFS-RKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWDGSIHL 319
Cdd:MTH00079  255 SQSTLYLTgKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKF 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 320 KTPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYSELLGQIHF 399
Cdd:MTH00079  335 QPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVF 414

                         410
                  ....*....|.
gi 1016561360 400 WSTFIGVNLTF 410
Cdd:MTH00079  415 FLMFVGVNLTF 425
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-410 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: 531.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360   1 TLYLIFGAFSGILGGCMSVLIRMELAQPGNHLLlgNHQLYNVLITAHAFLMIFFMVMPvMIGGFGNWLVPIMIGSPDMAF 80
Cdd:TIGR02891  11 ILYLVTAFAFFLVGGVLALLMRAQLATPGNTFM--DAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIGARDMAF 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360  81 PRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHVSGASSILGAINFISTIINMRNS 160
Cdd:TIGR02891  88 PRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAP 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 161 GQNMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMV 240
Cdd:TIGR02891 168 GMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGII 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 241 SHVVSTFSRKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWDGSIHLK 320
Cdd:TIGR02891 248 SEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFT 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 321 TPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYSELLGQIHFW 400
Cdd:TIGR02891 328 TPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFW 407

                         410
                  ....*....|
gi 1016561360 401 STFIGVNLTF 410
Cdd:TIGR02891 408 LTFVGFNLTF 417
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-410 0e+00

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 519.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360   2 LYLIFGAFSGILGGCMSVLIRMELAQPGNHLLLGNHqlYNVLITAHAFLMIFFMVMPvMIGGFGNWLVPIMIGSPDMAFP 81
Cdd:COG0843    21 MYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPET--YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360  82 RLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHVSGASSILGAINFISTIINMRNSG 161
Cdd:COG0843    98 RLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPG 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 162 QNMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMVS 241
Cdd:COG0843   178 MTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVS 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 242 HVVSTFSRKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWDGSIHLKT 321
Cdd:COG0843   258 EIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTT 337

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 322 PMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYSELLGQIHFWS 401
Cdd:COG0843   338 PMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWL 417


                  ....*....
gi 1016561360 402 TFIGVNLTF 410
Cdd:COG0843   418 WFIGFNLTF 426
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-410 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 517.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360   1 TLYLIFGAFSGILGGCMSVLIRMELAQPGNhlLLGNHQLYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAF 80
Cdd:MTH00026   18 SLYLVFGALSGAIGTAFSMLIRLELSSPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAF 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360  81 PRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHVSGASSILGAINFISTIINMRNS 160
Cdd:MTH00026   96 PRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTP 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 161 GQNMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMV 240
Cdd:MTH00026  176 GMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGII 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 241 SHVVSTFS-RKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWDGSIHL 319
Cdd:MTH00026  256 SQILSLFSyKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSGRNL 335

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 320 --KTPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYSELLGQI 397
Cdd:MTH00026  336 ifTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLI 415

                         410
                  ....*....|...
gi 1016561360 398 HFWSTFIGVNLTF 410
Cdd:MTH00026  416 HFWLMFIGVNITF 428
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-410 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: 517.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360   1 TLYLIFGAFSGILGGCMSVLIRMELAQPGNhlLLGNHQLYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPiMIGSPDMAF 80
Cdd:cd00919     6 LLYLIFAFVALLLGGLLALLIRLELATPGS--LFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360  81 PRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHVSGASSILGAINFISTIINMRNS 160
Cdd:cd00919    83 PRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 161 GQNMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMV 240
Cdd:cd00919   163 GMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAI 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 241 SHVVSTFSRKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWDGSIHLK 320
Cdd:cd00919   243 SEIIPTFSGKPLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFD 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 321 TPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYSELLGQIHFW 400
Cdd:cd00919   323 PPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFW 402

                         410
                  ....*....|
gi 1016561360 401 STFIGVNLTF 410
Cdd:cd00919   403 LWFIGFNLTF 412
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 2-410 1.14e-163

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: 468.98  E-value: 1.14e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360   2 LYLIFGAFSGILGGCMSVLIRMELAQPGNHLLLGNHqlYNVLITAHAFLMIFFMVMPVMIGgFGNWLVPIMIGSPDMAFP 81
Cdd:cd01662    13 MYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEH--YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFP 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360  82 RLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHVSGASSILGAINFISTIINMRNSG 161
Cdd:cd01662    90 RLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPG 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 162 QNMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMVS 241
Cdd:cd01662   170 MTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFS 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 242 HVVSTFSRKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWDGSIHLKT 321
Cdd:cd01662   250 EIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFET 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 322 PMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYSELLGQIHFWS 401
Cdd:cd01662   330 PMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWL 409


                  ....*....
gi 1016561360 402 TFIGVNLTF 410
Cdd:cd01662   410 WFIGFNLTF 418
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 2-410 2.09e-132

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 389.81  E-value: 2.09e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360   2 LYLIFGAFSGILGGCMSVLIRMELAQPGNHLLlgNHQLYNVLITAHAFLMIFFMVMPVMIGGFGNWLVPIMIGSPDMAFP 81
Cdd:MTH00048   19 IYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVI--SLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360  82 RLNNISFWLLPPSLCLLLTSALVevGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHVSGASSILGAINFISTIINMRNSG 161
Cdd:MTH00048   97 RLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTN 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 162 QNmYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMVS 241
Cdd:MTH00048  175 VF-SRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIIS 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 242 HVVSTFSRKP-VFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWDGSIHLK 320
Cdd:MTH00048  254 HICLSLSNNDdPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKS 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 321 TPML-FAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYSELLGQIHF 399
Cdd:MTH00048  334 DPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHC 413

                         410
                  ....*....|.
gi 1016561360 400 WSTFIGVNLTF 410
Cdd:MTH00048  414 IISMIGFNLCF 424
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 2-410 3.59e-125

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: 368.44  E-value: 3.59e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360   2 LYLIFGAFSGILGGCMSVLIRMELAQPGNHLLlgNHQLYNVLITAHAFLMIFFMVMPvMIGGFGNWLVPIMIGSPDMAFP 81
Cdd:pfam00115   5 LYLVTALVWFLVGGLLGLLIRLQLAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360  82 RLNNISFWLLPPSLCLLLTSALvevGVGTGWTVYPPLssiqshsgGAVDLAIFSLHVSGASSILGAINFISTIINMRNSG 161
Cdd:pfam00115  82 RLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPG 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 162 QNMyRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNttffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGMVS 241
Cdd:pfam00115 151 MTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIY 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 242 HVVSTFSRKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWDGSIHL-K 320
Cdd:pfam00115 224 YILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrT 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 321 TPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYSELLGQIHFW 400
Cdd:pfam00115 304 TPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFW 383

                         410
                  ....*....|
gi 1016561360 401 STFIGVNLTF 410
Cdd:pfam00115 384 LLFIGFNLTF 393
CyoB TIGR02843
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ...
 19-410 5.91e-118

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: 357.44  E-value: 5.91e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360  19 VLIRME--LAQPGNHLLLGNHQlYNVLITAHAFLMIFFMVMPVMIGGFgNWLVPIMIGSPDMAFPRLNNISFWLLPPSLC 96
Cdd:TIGR02843  76 IMMRTQqaLASGGSAGYLPPHH-YDQIFTAHGVIMIFFVAMPFVFGLM-NLVVPLQIGARDVAFPFLNSLSFWLTVVGAI 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360  97 LLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHVSGASSILGAINFISTIINMRNSGQNMYRMPLFVWSIFV 176
Cdd:TIGR02843 154 LVNVSLGVGEFAQTGWLAYPPLSELQYSPGVGVDYYIWALQISGIGTLLTGINFFVTIIKMRAPGMTLMKMPVFTWTSLC 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 177 TAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHVVSTFSRKPVFGYI 256
Cdd:TIGR02843 234 SNVLIIASFPILTVTLALLTLDRYLGMHFFTNEAGGNPMMYVNLIWAWGHPEVYILILPAFGIFSEVVATFSRKRLFGYT 313

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 257 GMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWDGSIHLKTPMLFAIGFIFLFTIG 336
Cdd:TIGR02843 314 SMVWATIAITVLSFIVWLHHFFTMGAGANVNAFFGIATMIIAIPTGVKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIG 393

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1016561360 337 GLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYSELLGQIHFWSTFIGVNLTF 410
Cdd:TIGR02843 394 GMTGVLLAVPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWFPKAFGFKLNEKLGKRSFWCWFIGFYLAF 467
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 2-410 1.85e-98

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 307.63  E-value: 1.85e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360   2 LYLIFGAFSGILGGCMSVLIRME--LAQPGNHLLLGNHQlYNVLITAHAFLMIFFMVMPVMIGgFGNWLVPIMIGSPDMA 79
Cdd:PRK15017   60 MYIIVAIVMLLRGFADAIMMRSQqaLASAGEAGFLPPHH-YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVA 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360  80 FPRLNNISFWLLPPSLCLLLTSALVEVGVGTGWTVYPPLSSIQSHSGGAVDLAIFSLHVSGASSILGAINFISTIINMRN 159
Cdd:PRK15017  138 FPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRA 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 160 SGQNMYRMPLFVWSIFVTAFLLLLAVPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGM 239
Cdd:PRK15017  218 PGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGV 297

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 240 VSHVVSTFSRKPVFGYIGMVYAMVSIGVLGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWDGSIHL 319
Cdd:PRK15017  298 FSEIAATFSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVF 377

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 320 KTPMLFAIGFIFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGLQYSELLGQIHF 399
Cdd:PRK15017  378 HSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAF 457

                         410
                  ....*....|.
gi 1016561360 400 WSTFIGVNLTF 410
Cdd:PRK15017  458 WFWIIGFFVAF 468
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 1-405 4.11e-10

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: 61.15  E-value: 4.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360   1 TLYLIFGAFS-GILGGCMSVLIRMelaqpGNHLLLGNHQLYNVLITAHAFLMIFFMVMpVMIGGFGNWLVPIMIGSPDMA 79
Cdd:cd01660     9 HFVVAFLALLlGGLFGLLQVLVRT-----GVFPLPSSGILYYQGLTLHGVLLAIVFTT-FFIMGFFYAIVARALLRSLFN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360  80 fPRLNNISFWLLPPSlcllltSALVEVGVGTG-----WTVYPPLssiQSHSGGAVDLAIFSLhvsgASSILGAINFISTI 154
Cdd:cd01660    83 -RRLAWAGFWLMVIG------TVMAAVPILLGqasvlYTFYPPL---QAHPLFYIGAALVVV----GSWISGFAMFVTLW 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 155 I-NMRNSGQnmyRMPLFVWSIFVTAFLLLLAVPVLagAITMLLtdrnfnttFFDPAGGG-----DPILYQHLFWFFGHPE 228
Cdd:cd01660   149 RwKKANPGK---KVPLATFMVVTTMILWLVASLGV--ALEVLF--------QLLPWSLGlvdtvDVLLSRTLFWWFGHPL 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 229 VYILILPGFGMVSHVVSTFSRKPVFGYIGMVYAMVSIGVLGFIVWAHHMYT-VGLDVDTRAYFTAATMIIAVPTGIKIFS 307
Cdd:cd01660   216 VYFWLLPAYIAWYTILPKIAGGKLFSDPLARLAFILFLLFSTPVGFHHQFAdPGIGPGWKFIHMVLTFMVALPSLLTAFT 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016561360 308 WIATM--------------WDGSIHLKTPMLFAIGF-IFLFTIGGLTGIVLANSGLDISLHDTYYVVAHFHYVLSMGAVF 372
Cdd:cd01660   296 VFASLeiagrlrggkglfgWIRALPWGDPMFLALFLaMLMFIPGGAGGIINASYQLNYVVHNTAWVPGHFHLTVGGAVAL 375

                         410       420       430
                  ....*....|....*....|....*....|....
gi 1016561360 373 AIFAGFYYWFGKITGLQY-SELLGQIHFWSTFIG 405
Cdd:cd01660   376 TFMAVAYWLVPHLTGRELaAKRLALAQPWLWFVG 409
 
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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