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Conserved domains on  [gi|1028567450|gb|ANE83795|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Eristalis pertinax]

Protein Classification

heme-copper oxidase family protein( domain architecture ID 14)

heme-copper oxidase family protein may catalyze the transfer of electrons from an electron donor onto molecular oxygen

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Heme_Cu_Oxidase_I super family cl00275
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 2-282 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.


The actual alignment was detected with superfamily member MTH00153:

Pssm-ID: 469701  Cd Length: 511  Bit Score: 592.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450   2 HLFWFFGHPEVYILILPGFGMISHIISQECGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMII 81
Cdd:MTH00153  231 HLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMII 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450  82 AIPTGIKIFSWLATLHGTQLVYSPAIIWALGFVFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAG 161
Cdd:MTH00153  311 AVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGG 390

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450 162 FVHWYPLFTGLTLNNKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNIVSTVGSTISLVSIIFFMIII 241
Cdd:MTH00153  391 FIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFII 470

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1028567450 242 WKSMIKQRQVIYPMQLNSSIEWYQNIPPAEHSYSELPLLSN 282
Cdd:MTH00153  471 WESMISKRPVLFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 2-282 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 592.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450   2 HLFWFFGHPEVYILILPGFGMISHIISQECGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMII 81
Cdd:MTH00153  231 HLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMII 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450  82 AIPTGIKIFSWLATLHGTQLVYSPAIIWALGFVFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAG 161
Cdd:MTH00153  311 AVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGG 390

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450 162 FVHWYPLFTGLTLNNKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNIVSTVGSTISLVSIIFFMIII 241
Cdd:MTH00153  391 FIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFII 470

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1028567450 242 WKSMIKQRQVIYPMQLNSSIEWYQNIPPAEHSYSELPLLSN 282
Cdd:MTH00153  471 WESMISKRPVLFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 2-263 2.24e-172

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: 485.45  E-value: 2.24e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450   2 HLFWFFGHPEVYILILPGFGMISHIISQECGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMII 81
Cdd:cd01663   224 HLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMII 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450  82 AIPTGIKIFSWLATLHGTQLVYSPAIIWALGFVFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAG 161
Cdd:cd01663   304 AVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAG 383

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450 162 FVHWYPLFTGLTLNNKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNIVSTVGSTISLVSIIFFMIII 241
Cdd:cd01663   384 FYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIV 463

                         250       260
                  ....*....|....*....|...
gi 1028567450 242 WKSMIKQRQVIY-PMQLNSSIEW 263
Cdd:cd01663   464 WESFVSGRKVIFnVGEGSTSLEW 486
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-280 1.32e-109

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 327.08  E-value: 1.32e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450   2 HLFWFFGHPEVYILILPGFGMISHIISQECGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMII 81
Cdd:COG0843   235 HLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLI 313

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450  82 AIPTGIKIFSWLATLHGTQLVYSPAIIWALGFVFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAG 161
Cdd:COG0843   314 AVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAG 393

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450 162 FVHWYPLFTGLTLNNKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTAWNIVSTVGSTISLVSIIFFMI 239
Cdd:COG0843   394 LYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLI 473

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1028567450 240 IIWKSMIKQRQV-IYPMQLNsSIEWYQNIPPAEHSYSELPLL 280
Cdd:COG0843   474 NLVVSLRKGPKAgGNPWGAR-TLEWATPSPPPLYNFASIPVV 514
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 2-274 1.41e-104

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: 313.39  E-value: 1.41e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450   2 HLFWFFGHPEVYILILPGFGMISHIISQECGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMII 81
Cdd:TIGR02891 226 HLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLI 304

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450  82 AIPTGIKIFSWLATLHGTQLVYSPAIIWALGFVFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAG 161
Cdd:TIGR02891 305 AVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAA 384

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450 162 FVHWYPLFTGLTLNNKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTAWNIVSTVGSTISLVSIIFFMI 239
Cdd:TIGR02891 385 IYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLW 464

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1028567450 240 IIWKSMIKQRQVIYPMQLNSSIEWYQNIPPAEHSY 274
Cdd:TIGR02891 465 NLIWSLRKGPKAGANPWGATTLEWTTSSPPPAHNF 499
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 2-229 5.16e-77

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: 240.55  E-value: 5.16e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450   2 HLFWFFGHPEVYILILPGFGMISHIISQECGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMII 81
Cdd:pfam00115 201 HLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLI 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450  82 AIPTGIKIFSWLATLHGTQL-VYSPAIIWALGFVFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMA 160
Cdd:pfam00115 280 AVPSGVKVFNWLATLWGGWIrFRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFG 359

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1028567450 161 GFVHWYPLFTGLTLNNKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYS----DYPDAYTAWNIVSTVGSTI 229
Cdd:pfam00115 360 GIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 2-282 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 592.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450   2 HLFWFFGHPEVYILILPGFGMISHIISQECGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMII 81
Cdd:MTH00153  231 HLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMII 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450  82 AIPTGIKIFSWLATLHGTQLVYSPAIIWALGFVFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAG 161
Cdd:MTH00153  311 AVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGG 390

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450 162 FVHWYPLFTGLTLNNKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNIVSTVGSTISLVSIIFFMIII 241
Cdd:MTH00153  391 FIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFII 470

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1028567450 242 WKSMIKQRQVIYPMQLNSSIEWYQNIPPAEHSYSELPLLSN 282
Cdd:MTH00153  471 WESMISKRPVLFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 2-263 2.24e-172

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: 485.45  E-value: 2.24e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450   2 HLFWFFGHPEVYILILPGFGMISHIISQECGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMII 81
Cdd:cd01663   224 HLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMII 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450  82 AIPTGIKIFSWLATLHGTQLVYSPAIIWALGFVFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAG 161
Cdd:cd01663   304 AVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAG 383

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450 162 FVHWYPLFTGLTLNNKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNIVSTVGSTISLVSIIFFMIII 241
Cdd:cd01663   384 FYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIV 463

                         250       260
                  ....*....|....*....|...
gi 1028567450 242 WKSMIKQRQVIY-PMQLNSSIEW 263
Cdd:cd01663   464 WESFVSGRKVIFnVGEGSTSLEW 486
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 2-278 1.30e-167

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 474.08  E-value: 1.30e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450   2 HLFWFFGHPEVYILILPGFGMISHIISQECGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMII 81
Cdd:MTH00223  230 HLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMII 309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450  82 AIPTGIKIFSWLATLHGTQLVYSPAIIWALGFVFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAG 161
Cdd:MTH00223  310 AVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAG 389

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450 162 FVHWYPLFTGLTLNNKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNIVSTVGSTISLVSIIFFMIII 241
Cdd:MTH00223  390 FNHWFPLFTGVTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIV 469

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1028567450 242 WKSMIKQRQVIYPMQLNSSIEWYQNIPPAEHSYSELP 278
Cdd:MTH00223  470 WEAFVSQRSVVWSGHLSTSLEWDNLLPADFHNNSETG 506
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 2-280 1.99e-167

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 473.78  E-value: 1.99e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450   2 HLFWFFGHPEVYILILPGFGMISHIISQECGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMII 81
Cdd:MTH00167  233 HLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMII 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450  82 AIPTGIKIFSWLATLHGTQLVYSPAIIWALGFVFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAG 161
Cdd:MTH00167  313 AVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAG 392

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450 162 FVHWYPLFTGLTLNNKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNIVSTVGSTISLVSIIFFMIII 241
Cdd:MTH00167  393 FTHWFPLFTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFII 472

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1028567450 242 WKSMIKQRQVIYPMQLNSSIEWYQNIPPAEHSYSELPLL 280
Cdd:MTH00167  473 WEAFSSKRKLLPVELTSTNVEWLHGCPPPHHTWEEPPFV 511
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 2-282 1.76e-166

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 471.13  E-value: 1.76e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450   2 HLFWFFGHPEVYILILPGFGMISHIISQECGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMII 81
Cdd:MTH00142  231 HLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVI 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450  82 AIPTGIKIFSWLATLHGTQLVYSPAIIWALGFVFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAG 161
Cdd:MTH00142  311 AVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAG 390

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450 162 FVHWYPLFTGLTLNNKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNIVSTVGSTISLVSIIFFMIII 241
Cdd:MTH00142  391 FIHWFPLFTGLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIV 470

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1028567450 242 WKSMIKQRQVIYPMQLNSSIEWYQNIPPAEHSYSELPLLSN 282
Cdd:MTH00142  471 WESFVSQRLVMWSSHLSTSLEWSHRLPPDFHTYDELPILVV 511
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 2-282 6.93e-166

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 469.96  E-value: 6.93e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450   2 HLFWFFGHPEVYILILPGFGMISHIISQECGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMII 81
Cdd:MTH00116  233 HLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMII 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450  82 AIPTGIKIFSWLATLHGTQLVYSPAIIWALGFVFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAG 161
Cdd:MTH00116  313 AIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAG 392

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450 162 FVHWYPLFTGLTLNNKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNIVSTVGSTISLVSIIFFMIII 241
Cdd:MTH00116  393 FTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFII 472

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1028567450 242 WKSMIKQRQVIYPMQLNSSIEWYQNIPPAEHSYSELPLLSN 282
Cdd:MTH00116  473 WEAFSSKRKVLQPELTTTNIEWIHGCPPPYHTFEEPAFVQV 513
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 2-279 1.34e-147

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 423.47  E-value: 1.34e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450   2 HLFWFFGHPEVYILILPGFGMISHIISQECGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMII 81
Cdd:MTH00037  233 HLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMII 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450  82 AIPTGIKIFSWLATLHGTQLVYSPAIIWALGFVFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAG 161
Cdd:MTH00037  313 AVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAG 392

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450 162 FVHWYPLFTGLTLNNKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNIVSTVGSTISLVSIIFFMIII 241
Cdd:MTH00037  393 FTHWFPLFSGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLI 472

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1028567450 242 WKSMIKQRQVIYPMQLNSSIEW-YQNIPPAEHSYSELPL 279
Cdd:MTH00037  473 WEAFASQREVISPEFSSSSLEWqYSSFPPSHHTFDETPS 511
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 2-276 2.07e-145

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 417.75  E-value: 2.07e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450   2 HLFWFFGHPEVYILILPGFGMISHIISQECGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMII 81
Cdd:MTH00103  233 HLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMII 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450  82 AIPTGIKIFSWLATLHGTQLVYSPAIIWALGFVFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAG 161
Cdd:MTH00103  313 AIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGG 392

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450 162 FVHWYPLFTGLTLNNKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNIVSTVGSTISLVSIIFFMIII 241
Cdd:MTH00103  393 FVHWFPLFSGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMI 472

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1028567450 242 WKSMIKQRQVIYPMQLNSSIEWYQNIPPAEHSYSE 276
Cdd:MTH00103  473 WEAFASKREVLTVELTTTNLEWLHGCPPPYHTFEE 507
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 2-276 3.73e-144

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 414.71  E-value: 3.73e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450   2 HLFWFFGHPEVYILILPGFGMISHIISQECGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMII 81
Cdd:MTH00183  233 HLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMII 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450  82 AIPTGIKIFSWLATLHGTQLVYSPAIIWALGFVFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAG 161
Cdd:MTH00183  313 AIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAA 392

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450 162 FVHWYPLFTGLTLNNKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNIVSTVGSTISLVSIIFFMIII 241
Cdd:MTH00183  393 FVHWFPLFSGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFIL 472

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1028567450 242 WKSMIKQRQVIYPMQLNSSIEWYQNIPPAEHSYSE 276
Cdd:MTH00183  473 WEAFAAKREVLSVELTSTNVEWLHGCPPPYHTFEE 507
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 2-281 5.86e-143

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 411.60  E-value: 5.86e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450   2 HLFWFFGHPEVYILILPGFGMISHIISQECGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMII 81
Cdd:MTH00007  230 HLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMII 309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450  82 AIPTGIKIFSWLATLHGTQLVYSPAIIWALGFVFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAG 161
Cdd:MTH00007  310 AVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAA 389

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450 162 FVHWYPLFTGLTLNNKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNIVSTVGSTISLVSIIFFMIII 241
Cdd:MTH00007  390 FNHWFPLFTGLTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFIL 469

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1028567450 242 WKSMIKQRQVIYPMQLNSSIEWYQNIPPAEHSYSELPLLS 281
Cdd:MTH00007  470 WEAFSAQRGVIASPHMSSSLEWQDTLPLDFHNLPETGIIT 509
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 2-282 1.16e-142

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 410.87  E-value: 1.16e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450   2 HLFWFFGHPEVYILILPGFGMISHIISQECGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMII 81
Cdd:MTH00077  233 HLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMII 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450  82 AIPTGIKIFSWLATLHGTQLVYSPAIIWALGFVFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAG 161
Cdd:MTH00077  313 AIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGG 392

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450 162 FVHWYPLFTGLTLNNKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNIVSTVGSTISLVSIIFFMIII 241
Cdd:MTH00077  393 FVHWFPLFSGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFII 472

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1028567450 242 WKSMIKQRQVIYPMQLNSSIEWYQNIPPAEHSYSELPLLSN 282
Cdd:MTH00077  473 WEAFSSKREVLTTELTSTNIEWLHGCPPPYHTFEEPSFVQT 513
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 2-276 1.14e-127

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 372.48  E-value: 1.14e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450   2 HLFWFFGHPEVYILILPGFGMISHIISQECGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMII 81
Cdd:MTH00079  233 HLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVI 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450  82 AIPTGIKIFSWLATLHGTQLVYSPAIIWALGFVFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAG 161
Cdd:MTH00079  313 AVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTG 392

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450 162 FVHWYPLFTGLTLNNKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNIVSTVGSTISLVSIIFFMIII 241
Cdd:MTH00079  393 ISLWWPFMTGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVL 472

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1028567450 242 WKSMIKQRQVIYPMQLNSSIEWYQNIPPAEHSYSE 276
Cdd:MTH00079  473 LESFFSYRLVLHDNYINSSPEYSLSSYVFGHSYQS 507
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 2-283 2.88e-126

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 369.54  E-value: 2.88e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450   2 HLFWFFGHPEVYILILPGFGMISHIISQECGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMII 81
Cdd:MTH00182  235 HLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMII 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450  82 AIPTGIKIFSWLATLHGTQLVYSPAIIWALGFVFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAG 161
Cdd:MTH00182  315 AVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGG 394

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450 162 FVHWYPLFTGLTLNNKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNIVSTVGSTISLVSIIFFMIII 241
Cdd:MTH00182  395 FYYWFGKITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYII 474

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1028567450 242 WKSMIKQRQVI----YPMQLNSSIEWYQNIPPAEHSYSELPLLSNF 283
Cdd:MTH00182  475 YDAYVREEKFIgwkeGTGESWASLEWVHSSPPLFHTYNELPFVYKS 520
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 2-283 2.59e-122

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 359.14  E-value: 2.59e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450   2 HLFWFFGHPEVYILILPGFGMISHIISQECGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMII 81
Cdd:MTH00184  235 HLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMII 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450  82 AIPTGIKIFSWLATLHGTQLVYSPAIIWALGFVFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAG 161
Cdd:MTH00184  315 AVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGG 394

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450 162 FVHWYPLFTGLTLNNKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNIVSTVGSTISLVSIIFFMIII 241
Cdd:MTH00184  395 FYYWFGKITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIV 474

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1028567450 242 WKSMIKQRQVIYPMQ---LNSSIEWYQNIPPAEHSYSELPLLSNF 283
Cdd:MTH00184  475 YDAYVREIKFVGWVEdsgHYPSLEWAQTSPPAHHTYNELPYVYKG 519
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 2-245 1.87e-114

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: 337.20  E-value: 1.87e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450   2 HLFWFFGHPEVYILILPGFGMISHIISQECGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMII 81
Cdd:cd00919   221 HLFWFFGHPEVYILILPAFGAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMII 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450  82 AIPTGIKIFSWLATLHGTQLVYSPAIIWALGFVFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAG 161
Cdd:cd00919   300 AVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAG 379

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450 162 FVHWYPLFTGLTLNNKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNIVSTVGSTISLVSIIFFMIII 241
Cdd:cd00919   380 LYYWFPKMTGRMLSEKLGKIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNL 459


                  ....
gi 1028567450 242 WKSM 245
Cdd:cd00919   460 FLSL 463
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-280 1.32e-109

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 327.08  E-value: 1.32e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450   2 HLFWFFGHPEVYILILPGFGMISHIISQECGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMII 81
Cdd:COG0843   235 HLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLI 313

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450  82 AIPTGIKIFSWLATLHGTQLVYSPAIIWALGFVFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAG 161
Cdd:COG0843   314 AVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAG 393

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450 162 FVHWYPLFTGLTLNNKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTAWNIVSTVGSTISLVSIIFFMI 239
Cdd:COG0843   394 LYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLI 473

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1028567450 240 IIWKSMIKQRQV-IYPMQLNsSIEWYQNIPPAEHSYSELPLL 280
Cdd:COG0843   474 NLVVSLRKGPKAgGNPWGAR-TLEWATPSPPPLYNFASIPVV 514
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 2-274 1.41e-104

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: 313.39  E-value: 1.41e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450   2 HLFWFFGHPEVYILILPGFGMISHIISQECGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMII 81
Cdd:TIGR02891 226 HLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLI 304

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450  82 AIPTGIKIFSWLATLHGTQLVYSPAIIWALGFVFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAG 161
Cdd:TIGR02891 305 AVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAA 384

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450 162 FVHWYPLFTGLTLNNKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTAWNIVSTVGSTISLVSIIFFMI 239
Cdd:TIGR02891 385 IYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLW 464

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1028567450 240 IIWKSMIKQRQVIYPMQLNSSIEWYQNIPPAEHSY 274
Cdd:TIGR02891 465 NLIWSLRKGPKAGANPWGATTLEWTTSSPPPAHNF 499
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 2-280 7.17e-103

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 310.02  E-value: 7.17e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450   2 HLFWFFGHPEVYILILPGFGMISHIISQECGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMII 81
Cdd:MTH00026  234 HLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMII 313

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450  82 AIPTGIKIFSWLATLHGT--QLVYSPAIIWALGFVFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIM 159
Cdd:MTH00026  314 AVPTGIKIFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIF 393

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450 160 AGFVHWYPLFTGLTLNNKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNIVSTVGSTISLVSIIFFMI 239
Cdd:MTH00026  394 GGFYLWFGKITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIV 473

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1028567450 240 IIWKSMIKQRqviyPMQLN-----------------SSIEWYQNIPPAEHSYSELPLL 280
Cdd:MTH00026  474 VIFDAYYREE----PFDINimakgplipfscqpahfDTLEWSLTSPPEHHTYNELPYI 527
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 2-273 7.17e-97

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 293.89  E-value: 7.17e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450   2 HLFWFFGHPEVYILILPGFGMISHIISQECGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMII 81
Cdd:MTH00048  231 HMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMII 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450  82 AIPTGIKIFSWLATLHGTQL-VYSPAIIWALGFVFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMA 160
Cdd:MTH00048  311 GVPTGIKVFSWLYMLLNSRVrKSDPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVI 390

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450 161 GFVHWYPLFTGLTLNNKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNIVSTVGSTISLVSIIFFMII 240
Cdd:MTH00048  391 MFIWWWPLITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFI 470

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1028567450 241 IWKSMIKQRQVIYPMQLNSSIEWYQNIPPAEHS 273
Cdd:MTH00048  471 LWESLVVKNEVLGLWGSSSCVVNVLMSPVPYHN 503
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 2-274 1.47e-96

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: 292.56  E-value: 1.47e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450   2 HLFWFFGHPEVYILILPGFGMISHIISQECGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMII 81
Cdd:cd01662   227 HLFWIFGHPEVYILILPAFGIFSEIVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMII 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450  82 AIPTGIKIFSWLATLHGTQLVYSPAIIWALGFVFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAG 161
Cdd:cd01662   306 AVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAG 385

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450 162 FVHWYPLFTGLTLNNKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTAWNIVSTVGSTISLVSIIFFMI 239
Cdd:cd01662   386 FYYWFPKMFGRMLNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLI 465

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1028567450 240 IIWKSMIKQRQVIYPMQLN-SSIEWYQNIPPAEHSY 274
Cdd:cd01662   466 NVIVSIRKGKRDATGDPWGaRTLEWATSSPPPAYNF 501
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 2-229 5.16e-77

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: 240.55  E-value: 5.16e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450   2 HLFWFFGHPEVYILILPGFGMISHIISQECGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMII 81
Cdd:pfam00115 201 HLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLI 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450  82 AIPTGIKIFSWLATLHGTQL-VYSPAIIWALGFVFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMA 160
Cdd:pfam00115 280 AVPSGVKVFNWLATLWGGWIrFRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFG 359

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1028567450 161 GFVHWYPLFTGLTLNNKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYS----DYPDAYTAWNIVSTVGSTI 229
Cdd:pfam00115 360 GIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 2-278 1.51e-62

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


Pssm-ID: 131928  Cd Length: 643  Bit Score: 208.17  E-value: 1.51e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450   2 HLFWFFGHPEVYILILPGFGMISHIISQeCGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMII 81
Cdd:TIGR02882 270 NLFWIWGHPEVYIVILPAFGIYSEIIST-FAQKRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAI 348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450  82 AIPTGIKIFSWLATLHGTQLVYSPAIIWALGFVFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAG 161
Cdd:TIGR02882 349 AIPTGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAG 428

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450 162 FVHWYPLFTGLTLNNKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDY--PDAYTAWNIVSTVGSTISLVSIIFFMI 239
Cdd:TIGR02882 429 LIYWYPKMFGYKLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYspSDGWFPLNLISTIGALLMAIGFIFLVY 508

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1028567450 240 IIWKSMIK-QRQVIYPMQLNSSIEWYQNIPPAEHSYSELP 278
Cdd:TIGR02882 509 NIYYSHRKsPREATGDPWNGRTLEWATASPPPKYNFAVTP 548
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 2-278 3.10e-57

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 194.38  E-value: 3.10e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450   2 HLFWFFGHPEVYILILPGFGMISHIISQeCGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMII 81
Cdd:PRK15017  277 NLIWAWGHPEVYILILPVFGVFSEIAAT-FSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMII 355

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450  82 AIPTGIKIFSWLATLHGTQLVYSPAIIWALGFVFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAG 161
Cdd:PRK15017  356 AIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAG 435

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450 162 FVHWYPLFTGLTLNNKWLKTQFLIMFIGVNLTFFPQHFLGLAGMPRRYSDYPD-AYTAWNIVSTVGSTISLVSIIFFMII 240
Cdd:PRK15017  436 MTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDpQFHTMLMIAASGAALIALGILCQVIQ 515

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1028567450 241 IWKSMI---KQRQVIYPMQLNSSIEWYQNIPPAEHSYSELP 278
Cdd:PRK15017  516 MYVSIRdrdQNRDLTGDPWGGRTLEWATSSPPPFYNFAVVP 556
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 3-245 5.13e-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: 89.27  E-value: 5.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450   3 LFWFFGHPEVYILILPGFGMISHIISQECGKKETFGSLGMIyAMLAIGLLGFIVWAHHMFT-VGMDVDTRAYFTSATMII 81
Cdd:cd01660   207 LFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARL-AFILFLLFSTPVGFHHQFAdPGIGPGWKFIHMVLTFMV 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450  82 AIPTGIKIFSWLATL-------HG-------TQLVYSPAIIWALGFVFL-FTVGGLTGVILANSSIDIILHDTYYVVAHF 146
Cdd:cd01660   286 ALPSLLTAFTVFASLeiagrlrGGkglfgwiRALPWGDPMFLALFLAMLmFIPGGAGGIINASYQLNYVVHNTAWVPGHF 365

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028567450 147 HyvLSMGAVFAIMA-GFVHWY-PLFTGLTLNNKWL-KTQFLIMFIGVNLTFFPQHFLGLAGMPRR--YSDYPDAY----- 216
Cdd:cd01660   366 H--LTVGGAVALTFmAVAYWLvPHLTGRELAAKRLaLAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGGLPaagew 443

                         250       260
                  ....*....|....*....|....*....
gi 1028567450 217 TAWNIVSTVGSTISLVSIIFFMIIIWKSM 245
Cdd:cd01660   444 APYQQLMAIGGTILFVSGALFLYILFRTL 472
 
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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