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Conserved domains on  [gi|158421025|gb|ABW37892|]
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cytochrome c oxidase subunit I, partial (mitochondrion) [Pleurocera canaliculata fila]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Heme_Cu_Oxidase_I super family cl00275
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-278 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: 581.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025   1 LLLSLPVLAGAITMLLTDRNFNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKETFGTLGMI 80
Cdd:MTH00153 193 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMI 272

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025  81 YAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGAKIKYETPMLWALGFIFLFTVGGLT 160
Cdd:MTH00153 273 YAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLT 352

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025 161 GIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVTLHSRWTKAHFYIMFIGVNVTFFPQHFLGLS 240
Cdd:MTH00153 353 GVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLA 432

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 158421025 241 GMPRRYSDYPDCYTKWNVISSMGSMISFVAVLYFMVIV 278
Cdd:MTH00153 433 GMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFII 470
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-278 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 581.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025   1 LLLSLPVLAGAITMLLTDRNFNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKETFGTLGMI 80
Cdd:MTH00153 193 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMI 272

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025  81 YAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGAKIKYETPMLWALGFIFLFTVGGLT 160
Cdd:MTH00153 273 YAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLT 352

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025 161 GIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVTLHSRWTKAHFYIMFIGVNVTFFPQHFLGLS 240
Cdd:MTH00153 353 GVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLA 432

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 158421025 241 GMPRRYSDYPDCYTKWNVISSMGSMISFVAVLYFMVIV 278
Cdd:MTH00153 433 GMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFII 470
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-278 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: 557.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025   1 LLLSLPVLAGAITMLLTDRNFNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKETFGTLGMI 80
Cdd:cd01663  186 LLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMV 265

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025  81 YAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGAKIKYETPMLWALGFIFLFTVGGLT 160
Cdd:cd01663  266 YAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLT 345

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025 161 GIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVTLHSRWTKAHFYIMFIGVNVTFFPQHFLGLS 240
Cdd:cd01663  346 GVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLA 425

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 158421025 241 GMPRRYSDYPDCYTKWNVISSMGSMISFVAVLYFMVIV 278
Cdd:cd01663  426 GMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIV 463
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-278 8.16e-126

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 368.30  E-value: 8.16e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025   2 LLSLPVLAGAITMLLTDRNFNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKeTFGTLGMIY 81
Cdd:COG0843  198 LLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVL 276

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025  82 AMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGAKIKYETPMLWALGFIFLFTVGGLTG 161
Cdd:COG0843  277 ATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTG 356

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025 162 IVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVTLHSRWTKAHFYIMFIGVNVTFFPQHFLGLSG 241
Cdd:COG0843  357 VMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLG 436

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 158421025 242 MPRRYSDYP--DCYTKWNVISSMGSMISFVAVLYFMVIV 278
Cdd:COG0843  437 MPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINL 475
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-278 3.12e-125

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: 365.78  E-value: 3.12e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025    1 LLLSLPVLAGAITMLLTDRNFNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSsKKETFGTLGMI 80
Cdd:TIGR02891 188 ILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFA-RKPIFGYRAMV 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025   81 YAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGAKIKYETPMLWALGFIFLFTVGGLT 160
Cdd:TIGR02891 267 YATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLT 346

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025  161 GIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVTLHSRWTKAHFYIMFIGVNVTFFPQHFLGLS 240
Cdd:TIGR02891 347 GVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLL 426

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 158421025  241 GMPRRYSDYPD--CYTKWNVISSMGSMISFVAVLYFMVIV 278
Cdd:TIGR02891 427 GMPRRYYTYPPqmGFATLNLISTIGAFILAAGFLVFLWNL 466
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-266 2.79e-85

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: 261.35  E-value: 2.79e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025    1 LLLSLPVLAGAITMLLTDRNFNTtffdptGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSsKKETFGTLGMI 80
Cdd:pfam00115 169 ILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFA-GRPLFGYKLSV 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025   81 YAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGAKIK-YETPMLWALGFIFLFTVGGL 159
Cdd:pfam00115 242 LAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRfRTTPMLFFLGFAFLFIIGGL 321

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025  160 TGIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVTLHSRWTKAHFYIMFIGVNVTFFPQHFLGL 239
Cdd:pfam00115 322 TGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGL 401

                         250       260       270
                  ....*....|....*....|....*....|.
gi 158421025  240 SGMPRRYS----DYPDCYTKWNVISSMGSMI 266
Cdd:pfam00115 402 LGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-278 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 581.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025   1 LLLSLPVLAGAITMLLTDRNFNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKETFGTLGMI 80
Cdd:MTH00153 193 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMI 272

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025  81 YAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGAKIKYETPMLWALGFIFLFTVGGLT 160
Cdd:MTH00153 273 YAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLT 352

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025 161 GIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVTLHSRWTKAHFYIMFIGVNVTFFPQHFLGLS 240
Cdd:MTH00153 353 GVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLA 432

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 158421025 241 GMPRRYSDYPDCYTKWNVISSMGSMISFVAVLYFMVIV 278
Cdd:MTH00153 433 GMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFII 470
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-278 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: 557.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025   1 LLLSLPVLAGAITMLLTDRNFNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKETFGTLGMI 80
Cdd:cd01663  186 LLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMV 265

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025  81 YAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGAKIKYETPMLWALGFIFLFTVGGLT 160
Cdd:cd01663  266 YAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLT 345

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025 161 GIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVTLHSRWTKAHFYIMFIGVNVTFFPQHFLGLS 240
Cdd:cd01663  346 GVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLA 425

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 158421025 241 GMPRRYSDYPDCYTKWNVISSMGSMISFVAVLYFMVIV 278
Cdd:cd01663  426 GMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIV 463
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-278 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 541.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025   1 LLLSLPVLAGAITMLLTDRNFNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKETFGTLGMI 80
Cdd:MTH00223 192 LLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMI 271

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025  81 YAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGAKIKYETPMLWALGFIFLFTVGGLT 160
Cdd:MTH00223 272 YAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLT 351

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025 161 GIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVTLHSRWTKAHFYIMFIGVNVTFFPQHFLGLS 240
Cdd:MTH00223 352 GIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLA 431

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 158421025 241 GMPRRYSDYPDCYTKWNVISSMGSMISFVAVLYFMVIV 278
Cdd:MTH00223 432 GMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIV 469
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-278 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 522.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025   1 LLLSLPVLAGAITMLLTDRNFNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKETFGTLGMI 80
Cdd:MTH00142 193 LLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMI 272

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025  81 YAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGAKIKYETPMLWALGFIFLFTVGGLT 160
Cdd:MTH00142 273 YAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLT 352

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025 161 GIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVTLHSRWTKAHFYIMFIGVNVTFFPQHFLGLS 240
Cdd:MTH00142 353 GIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLA 432

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 158421025 241 GMPRRYSDYPDCYTKWNVISSMGSMISFVAVLYFMVIV 278
Cdd:MTH00142 433 GMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIV 470
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-278 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 520.42  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025   1 LLLSLPVLAGAITMLLTDRNFNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKETFGTLGMI 80
Cdd:MTH00116 195 LLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMV 274

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025  81 YAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGAKIKYETPMLWALGFIFLFTVGGLT 160
Cdd:MTH00116 275 WAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLT 354

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025 161 GIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVTLHSRWTKAHFYIMFIGVNVTFFPQHFLGLS 240
Cdd:MTH00116 355 GIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLA 434

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 158421025 241 GMPRRYSDYPDCYTKWNVISSMGSMISFVAVLYFMVIV 278
Cdd:MTH00116 435 GMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFII 472
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-278 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 519.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025   1 LLLSLPVLAGAITMLLTDRNFNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKETFGTLGMI 80
Cdd:MTH00167 195 LLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMV 274

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025  81 YAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGAKIKYETPMLWALGFIFLFTVGGLT 160
Cdd:MTH00167 275 WAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLT 354

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025 161 GIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVTLHSRWTKAHFYIMFIGVNVTFFPQHFLGLS 240
Cdd:MTH00167 355 GIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLA 434

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 158421025 241 GMPRRYSDYPDCYTKWNVISSMGSMISFVAVLYFMVIV 278
Cdd:MTH00167 435 GMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFII 472
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-278 1.13e-173

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 489.41  E-value: 1.13e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025   1 LLLSLPVLAGAITMLLTDRNFNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKETFGTLGMI 80
Cdd:MTH00007 192 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMI 271

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025  81 YAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGAKIKYETPMLWALGFIFLFTVGGLT 160
Cdd:MTH00007 272 YAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGGLT 351

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025 161 GIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVTLHSRWTKAHFYIMFIGVNVTFFPQHFLGLS 240
Cdd:MTH00007 352 GIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLS 431

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 158421025 241 GMPRRYSDYPDCYTKWNVISSMGSMISFVAVLYFMVIV 278
Cdd:MTH00007 432 GMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFIL 469
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-278 6.96e-163

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 462.09  E-value: 6.96e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025   1 LLLSLPVLAGAITMLLTDRNFNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKETFGTLGMI 80
Cdd:MTH00183 195 LLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMV 274

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025  81 YAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGAKIKYETPMLWALGFIFLFTVGGLT 160
Cdd:MTH00183 275 WAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLT 354

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025 161 GIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVTLHSRWTKAHFYIMFIGVNVTFFPQHFLGLS 240
Cdd:MTH00183 355 GIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLA 434

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 158421025 241 GMPRRYSDYPDCYTKWNVISSMGSMISFVAVLYFMVIV 278
Cdd:MTH00183 435 GMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFIL 472
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-278 1.43e-162

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 461.22  E-value: 1.43e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025   1 LLLSLPVLAGAITMLLTDRNFNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKETFGTLGMI 80
Cdd:MTH00037 195 LLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMV 274

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025  81 YAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGAKIKYETPMLWALGFIFLFTVGGLT 160
Cdd:MTH00037 275 YAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLT 354

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025 161 GIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVTLHSRWTKAHFYIMFIGVNVTFFPQHFLGLS 240
Cdd:MTH00037 355 GIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLA 434

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 158421025 241 GMPRRYSDYPDCYTKWNVISSMGSMISFVAVLYFMVIV 278
Cdd:MTH00037 435 GMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLI 472
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-278 6.49e-159

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 452.03  E-value: 6.49e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025   1 LLLSLPVLAGAITMLLTDRNFNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKETFGTLGMI 80
Cdd:MTH00103 195 LLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMV 274

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025  81 YAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGAKIKYETPMLWALGFIFLFTVGGLT 160
Cdd:MTH00103 275 WAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLT 354

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025 161 GIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVTLHSRWTKAHFYIMFIGVNVTFFPQHFLGLS 240
Cdd:MTH00103 355 GIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLS 434

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 158421025 241 GMPRRYSDYPDCYTKWNVISSMGSMISFVAVLYFMVIV 278
Cdd:MTH00103 435 GMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMI 472
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-278 4.59e-158

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 449.78  E-value: 4.59e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025   1 LLLSLPVLAGAITMLLTDRNFNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKETFGTLGMI 80
Cdd:MTH00077 195 LLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMV 274

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025  81 YAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGAKIKYETPMLWALGFIFLFTVGGLT 160
Cdd:MTH00077 275 WAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLT 354

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025 161 GIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVTLHSRWTKAHFYIMFIGVNVTFFPQHFLGLS 240
Cdd:MTH00077 355 GIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLA 434

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 158421025 241 GMPRRYSDYPDCYTKWNVISSMGSMISFVAVLYFMVIV 278
Cdd:MTH00077 435 GMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFII 472
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-278 4.93e-150

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 430.01  E-value: 4.93e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025   1 LLLSLPVLAGAITMLLTDRNFNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKETFGTLGMI 80
Cdd:MTH00182 197 LLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMV 276

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025  81 YAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGAKIKYETPMLWALGFIFLFTVGGLT 160
Cdd:MTH00182 277 YAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLT 356

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025 161 GIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVTLHSRWTKAHFYIMFIGVNVTFFPQHFLGLS 240
Cdd:MTH00182 357 GVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLA 436

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 158421025 241 GMPRRYSDYPDCYTKWNVISSMGSMISFVAVLYFMVIV 278
Cdd:MTH00182 437 GFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYII 474
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-278 3.85e-147

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 422.31  E-value: 3.85e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025   1 LLLSLPVLAGAITMLLTDRNFNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKETFGTLGMI 80
Cdd:MTH00184 197 LLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMV 276

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025  81 YAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGAKIKYETPMLWALGFIFLFTVGGLT 160
Cdd:MTH00184 277 YAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLT 356

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025 161 GIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVTLHSRWTKAHFYIMFIGVNVTFFPQHFLGLS 240
Cdd:MTH00184 357 GIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLA 436

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 158421025 241 GMPRRYSDYPDCYTKWNVISSMGSMISFVAVLYFMVIV 278
Cdd:MTH00184 437 GLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIV 474
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-274 3.51e-146

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 419.47  E-value: 3.51e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025   1 LLLSLPVLAGAITMLLTDRNFNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKETFGTLGMI 80
Cdd:MTH00079 195 LVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMV 274

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025  81 YAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGAKIKYETPMLWALGFIFLFTVGGLT 160
Cdd:MTH00079 275 YAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLT 354

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025 161 GIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVTLHSRWTKAHFYIMFIGVNVTFFPQHFLGLS 240
Cdd:MTH00079 355 GVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLH 434

                        250       260       270
                 ....*....|....*....|....*....|....
gi 158421025 241 GMPRRYSDYPDCYTKWNVISSMGSMISFVAVLYF 274
Cdd:MTH00079 435 GMPRKYLDYPDVYSVWNVISSYGSMISVFALFLF 468
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-278 4.11e-134

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: 386.89  E-value: 4.11e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025   1 LLLSLPVLAGAITMLLTDRNFNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSsKKETFGTLGMI 80
Cdd:cd00919  183 LLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFS-GKPLFGYKLMV 261

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025  81 YAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGAKIKYETPMLWALGFIFLFTVGGLT 160
Cdd:cd00919  262 YAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGLT 341

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025 161 GIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVTLHSRWTKAHFYIMFIGVNVTFFPQHFLGLS 240
Cdd:cd00919  342 GVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGFNLTFFPMHFLGLL 421

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 158421025 241 GMPRRYSDYPDCYTKWNVISSMGSMISFVAVLYFMVIV 278
Cdd:cd00919  422 GMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNL 459
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-278 1.88e-129

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 377.82  E-value: 1.88e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025   1 LLLSLPVLAGAITMLLTDRNFNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKETFGTLGMI 80
Cdd:MTH00026 196 LLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMV 275

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025  81 YAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGA--KIKYETPMLWALGFIFLFTVGG 158
Cdd:MTH00026 276 YAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGG 355

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025 159 LTGIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVTLHSRWTKAHFYIMFIGVNVTFFPQHFLG 238
Cdd:MTH00026 356 LTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLG 435

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 158421025 239 LSGMPRRYSDYPDCYTKWNVISSMGSMISFVAVLYFMVIV 278
Cdd:MTH00026 436 LAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVI 475
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-278 8.16e-126

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 368.30  E-value: 8.16e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025   2 LLSLPVLAGAITMLLTDRNFNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKeTFGTLGMIY 81
Cdd:COG0843  198 LLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVL 276

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025  82 AMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGAKIKYETPMLWALGFIFLFTVGGLTG 161
Cdd:COG0843  277 ATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTG 356

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025 162 IVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVTLHSRWTKAHFYIMFIGVNVTFFPQHFLGLSG 241
Cdd:COG0843  357 VMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLG 436

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 158421025 242 MPRRYSDYP--DCYTKWNVISSMGSMISFVAVLYFMVIV 278
Cdd:COG0843  437 MPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINL 475
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-278 3.12e-125

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: 365.78  E-value: 3.12e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025    1 LLLSLPVLAGAITMLLTDRNFNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSsKKETFGTLGMI 80
Cdd:TIGR02891 188 ILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFA-RKPIFGYRAMV 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025   81 YAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGAKIKYETPMLWALGFIFLFTVGGLT 160
Cdd:TIGR02891 267 YATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLT 346

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025  161 GIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVTLHSRWTKAHFYIMFIGVNVTFFPQHFLGLS 240
Cdd:TIGR02891 347 GVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLL 426

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 158421025  241 GMPRRYSDYPD--CYTKWNVISSMGSMISFVAVLYFMVIV 278
Cdd:TIGR02891 427 GMPRRYYTYPPqmGFATLNLISTIGAFILAAGFLVFLWNL 466
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-278 2.18e-113

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 335.88  E-value: 2.18e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025   1 LLLSLPVLAGAITMLLTDRNFNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKETFGTLGMI 80
Cdd:MTH00048 193 LLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLV 272

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025  81 YAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGAKIKYETPML-WALGFIFLFTVGGL 159
Cdd:MTH00048 273 FAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSDPVVwWVVSFIVLFTIGGV 352

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025 160 TGIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVTLHSRWTKAHFYIMFIGVNVTFFPQHFLGL 239
Cdd:MTH00048 353 TGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGL 432

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 158421025 240 SGMPRRYSDYPDCYTKWNVISSMGSMISFVAVLYFMVIV 278
Cdd:MTH00048 433 CGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFIL 471
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 2-276 1.63e-112

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: 333.39  E-value: 1.63e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025   2 LLSLPVLAGAITMLLTDRNFNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSsKKETFGTLGMIY 81
Cdd:cd01662  190 LFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFS-RKPLFGYRSMVY 268

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025  82 AMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGAKIKYETPMLWALGFIFLFTVGGLTG 161
Cdd:cd01662  269 ATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTG 348

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025 162 IVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVTLHSRWTKAHFYIMFIGVNVTFFPQHFLGLSG 241
Cdd:cd01662  349 VMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFNLTFFPMHILGLMG 428

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 158421025 242 MPRRYSDYP--DCYTKWNVISSMGSMISFVAVLYFMV 276
Cdd:cd01662  429 MPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLI 465
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-266 2.79e-85

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: 261.35  E-value: 2.79e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025    1 LLLSLPVLAGAITMLLTDRNFNTtffdptGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSsKKETFGTLGMI 80
Cdd:pfam00115 169 ILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFA-GRPLFGYKLSV 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025   81 YAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGAKIK-YETPMLWALGFIFLFTVGGL 159
Cdd:pfam00115 242 LAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRfRTTPMLFFLGFAFLFIIGGL 321

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025  160 TGIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVTLHSRWTKAHFYIMFIGVNVTFFPQHFLGL 239
Cdd:pfam00115 322 TGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGL 401

                         250       260       270
                  ....*....|....*....|....*....|.
gi 158421025  240 SGMPRRYS----DYPDCYTKWNVISSMGSMI 266
Cdd:pfam00115 402 LGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
CyoB TIGR02843
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ...
 1-276 3.01e-78

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: 249.20  E-value: 3.01e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025    1 LLLSLPVLAGAITMLLTDRNFNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKeTFGTLGMI 80
Cdd:TIGR02843 238 IIASFPILTVTLALLTLDRYLGMHFFTNEAGGNPMMYVNLIWAWGHPEVYILILPAFGIFSEVVATFSRKR-LFGYTSMV 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025   81 YAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGAKIKYETPMLWALGFIFLFTVGGLT 160
Cdd:TIGR02843 317 WATIAITVLSFIVWLHHFFTMGAGANVNAFFGIATMIIAIPTGVKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMT 396

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025  161 GIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVTLHSRWTKAHFYIMFIGVNVTFFPQHFLGLS 240
Cdd:TIGR02843 397 GVLLAVPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWFPKAFGFKLNEKLGKRSFWCWFIGFYLAFMPLYILGFM 476

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 158421025  241 GMPRRYSDYPD-CYTKWNVISSMGSMISFVAVLYFMV 276
Cdd:TIGR02843 477 GMTRRLNHYDNpEWHPMLIIAAFGAFLIACGILCQII 513
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-251 3.25e-65

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 215.18  E-value: 3.25e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025   1 LLLSLPVLAGAITMLLTDRNFNTTFFDPTGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSsKKETFGTLGMI 80
Cdd:PRK15017 239 IIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLV 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025  81 YAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGAKIKYETPMLWALGFIFLFTVGGLT 160
Cdd:PRK15017 318 WATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMT 397

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025 161 GIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVTLHSRWTKAHFYIMFIGVNVTFFPQHFLGLS 240
Cdd:PRK15017 398 GVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFM 477

                        250
                 ....*....|.
gi 158421025 241 GMPRRYSDYPD 251
Cdd:PRK15017 478 GMTRRLSQQID 488
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 33-278 7.61e-19

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: 85.80  E-value: 7.61e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025  33 DPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKETFGTLGMIyAMLAIGVLGFIVWAHHMFT-VGMDVDTRAYF 111
Cdd:cd01660  200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARL-AFILFLLFSTPVGFHHQFAdPGIGPGWKFIH 278

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025 112 TAATMIIAVPTGIKVFSWLATIHGA--------------KIKYETPMLWALGF-IFLFTVGGLTGIVLSNSSLDIMLHDT 176
Cdd:cd01660  279 MVLTFMVALPSLLTAFTVFASLEIAgrlrggkglfgwirALPWGDPMFLALFLaMLMFIPGGAGGIINASYQLNYVVHNT 358

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158421025 177 YYVVAHFHyvLSMGAVFAL-FGAFNYWF-PLLSGVTLHSRW-TKAHFYIMFIGVNVTFFPQHFLGLSGMPRR--YSDYPD 251
Cdd:cd01660  359 AWVPGHFH--LTVGGAVALtFMAVAYWLvPHLTGRELAAKRlALAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGG 436

                        250       260       270
                 ....*....|....*....|....*....|..
gi 158421025 252 CY-----TKWNVISSMGSMISFVAVLYFMVIV 278
Cdd:cd01660  437 LPaagewAPYQQLMAIGGTILFVSGALFLYIL 468
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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