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Conserved domains on  [gi|1036393008|gb|ANJ89163|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Phytophthora sp. occultans-like]

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 ...
 1-353 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 cd01663:

Pssm-ID: 469701  Cd Length: 488  Bit Score: 632.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008   1 LAQPGNQIfmGNHQLYNVIVTAHAFIMVFFLVMPALIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:cd01663    32 LSQPGSQL--GNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALV 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008  81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAI*SLHLTGISSLLGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:cd01663   110 EGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLS 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIISQVSAAFA-KKNVFGYLGMVYAML 239
Cdd:cd01663   190 LPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSgKKPVFGYLGMVYAML 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 240 SIGLLGSIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFTLGFILLFVMGGVTGVAM 319
Cdd:cd01663   270 SIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVL 349

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1036393008 320 SNSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTG 353
Cdd:cd01663   350 ANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAG 383
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-353 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: 632.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008   1 LAQPGNQIfmGNHQLYNVIVTAHAFIMVFFLVMPALIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:cd01663    32 LSQPGSQL--GNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALV 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008  81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAI*SLHLTGISSLLGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:cd01663   110 EGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLS 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIISQVSAAFA-KKNVFGYLGMVYAML 239
Cdd:cd01663   190 LPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSgKKPVFGYLGMVYAML 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 240 SIGLLGSIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFTLGFILLFVMGGVTGVAM 319
Cdd:cd01663   270 SIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVL 349

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1036393008 320 SNSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTG 353
Cdd:cd01663   350 ANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAG 383
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-353 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 608.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008   1 LAQPGNqiFMGNHQLYNVIVTAHAFIMVFFLVMPALIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:MTH00153   39 LGQPGS--LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMV 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008  81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAI*SLHLTGISSLLGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:MTH00153  117 ESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLS 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIISQ-VSAAFAKKNVFGYLGMVYAML 239
Cdd:MTH00153  197 LPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHiISQESGKKETFGTLGMIYAML 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 240 SIGLLGSIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFTLGFILLFVMGGVTGVAM 319
Cdd:MTH00153  277 AIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVL 356

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1036393008 320 SNSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTG 353
Cdd:MTH00153  357 ANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGG 390
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-353 4.52e-155

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: 444.74  E-value: 4.52e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008   1 LAQPGNQiFMGNhQLYNVIVTAHAFIMVFFLVMPaLIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:TIGR02891  35 LATPGNT-FMDA-ETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFT 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008  81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAI*SLHLTGISSLLGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:TIGR02891 112 GGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLA 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIISQVSAAFAKKNVFGYLGMVYAMLS 240
Cdd:TIGR02891 192 FPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKPIFGYRAMVYATVA 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 241 IGLLGSIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFTLGFILLFVMGGVTGVAMS 320
Cdd:TIGR02891 272 IGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLA 351

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1036393008 321 NSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTG 353
Cdd:TIGR02891 352 SVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAA 384
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-353 2.15e-153

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 441.87  E-value: 2.15e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008   1 LAQPGNQiFMGNHQlYNVIVTAHAFIMVFFLVMPaLIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:COG0843    44 LAGPGLG-LLSPET-YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFV 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008  81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAI*SLHLTGISSLLGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:COG0843   121 GGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLA 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIISQVSAAFAKKNVFGYLGMVYAMLS 240
Cdd:COG0843   201 FPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVA 280

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 241 IGLLGSIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFTLGFILLFVMGGVTGVAMS 320
Cdd:COG0843   281 IAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLA 360

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1036393008 321 NSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTG 353
Cdd:COG0843   361 SVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAG 393
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-353 7.69e-102

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: 306.81  E-value: 7.69e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008   1 LAQPGNQIFmgNHQLYNVIVTAHAFIMVFFLVMPAlIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAiv 80
Cdd:pfam00115  28 LAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASF-- 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008  81 eSGAGTGWTVYPPLssvqahsgPSVDLAI*SLHLTGISSLLGAINFISTIYNMRAPGLSFhRLPLFVWSVLITAFLLLLT 160
Cdd:pfam00115 103 -GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLA 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 161 LPVLAGAITMLLTDRNLNTsfydpsGGGDPVLYQHLFWFFGHPEVYILILPGFGIISQVSAAFAKKNVFGYLGMVYAMLS 240
Cdd:pfam00115 173 FPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRPLFGYKLSVLAFWL 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 241 IGLLGSIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKF-ETPLLFTLGFILLFVMGGVTGVAM 319
Cdd:pfam00115 247 IAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFFLGFAFLFIIGGLTGVML 326

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1036393008 320 SNSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTG 353
Cdd:pfam00115 327 ALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGG 360
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-353 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: 632.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008   1 LAQPGNQIfmGNHQLYNVIVTAHAFIMVFFLVMPALIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:cd01663    32 LSQPGSQL--GNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALV 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008  81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAI*SLHLTGISSLLGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:cd01663   110 EGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLS 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIISQVSAAFA-KKNVFGYLGMVYAML 239
Cdd:cd01663   190 LPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSgKKPVFGYLGMVYAML 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 240 SIGLLGSIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFTLGFILLFVMGGVTGVAM 319
Cdd:cd01663   270 SIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVL 349

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1036393008 320 SNSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTG 353
Cdd:cd01663   350 ANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAG 383
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-353 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 608.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008   1 LAQPGNqiFMGNHQLYNVIVTAHAFIMVFFLVMPALIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:MTH00153   39 LGQPGS--LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMV 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008  81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAI*SLHLTGISSLLGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:MTH00153  117 ESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLS 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIISQ-VSAAFAKKNVFGYLGMVYAML 239
Cdd:MTH00153  197 LPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHiISQESGKKETFGTLGMIYAML 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 240 SIGLLGSIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFTLGFILLFVMGGVTGVAM 319
Cdd:MTH00153  277 AIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVL 356

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1036393008 320 SNSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTG 353
Cdd:MTH00153  357 ANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGG 390
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-353 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 558.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008   1 LAQPGnqIFMGNHQLYNVIVTAHAFIMVFFLVMPALIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:MTH00223   38 LGQPG--ALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAV 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008  81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAI*SLHLTGISSLLGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:MTH00223  116 ESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLS 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIISQVSAAFA-KKNVFGYLGMVYAML 239
Cdd:MTH00223  196 LPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSsKKEVFGTLGMIYAML 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 240 SIGLLGSIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFTLGFILLFVMGGVTGVAM 319
Cdd:MTH00223  276 SIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIIL 355

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1036393008 320 SNSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTG 353
Cdd:MTH00223  356 SNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAG 389
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-353 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 551.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008   1 LAQPGNQIfmGNHQLYNVIVTAHAFIMVFFLVMPALIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:MTH00167   41 LSQPGSLL--GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGV 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008  81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAI*SLHLTGISSLLGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:MTH00167  119 EAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLS 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIISQVSAAFA-KKNVFGYLGMVYAML 239
Cdd:MTH00167  199 LPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSgKKEPFGYMGMVWAMM 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 240 SIGLLGSIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFTLGFILLFVMGGVTGVAM 319
Cdd:MTH00167  279 AIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVL 358

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1036393008 320 SNSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTG 353
Cdd:MTH00167  359 ANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAG 392
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-353 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 547.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008   1 LAQPGNqiFMGNHQLYNVIVTAHAFIMVFFLVMPALIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:MTH00116   41 LGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTV 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008  81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAI*SLHLTGISSLLGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:MTH00116  119 EAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLS 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIISQVSAAFA-KKNVFGYLGMVYAML 239
Cdd:MTH00116  199 LPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAgKKEPFGYMGMVWAML 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 240 SIGLLGSIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFTLGFILLFVMGGVTGVAM 319
Cdd:MTH00116  279 SIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVL 358

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1036393008 320 SNSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTG 353
Cdd:MTH00116  359 ANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAG 392
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-353 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 541.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008   1 LAQPGNqiFMGNHQLYNVIVTAHAFIMVFFLVMPALIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:MTH00142   39 LGQPGS--LLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAV 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008  81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAI*SLHLTGISSLLGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:MTH00142  117 ESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLS 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIISQVSAAFA-KKNVFGYLGMVYAML 239
Cdd:MTH00142  197 LPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSgKKEVFGTLGMIYAML 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 240 SIGLLGSIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFTLGFILLFVMGGVTGVAM 319
Cdd:MTH00142  277 SIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVL 356

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1036393008 320 SNSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTG 353
Cdd:MTH00142  357 ANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAG 390
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-353 1.79e-178

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 505.13  E-value: 1.79e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008   1 LAQPGNQIfmGNHQLYNVIVTAHAFIMVFFLVMPALIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:MTH00182   43 LSAPGAML--GDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFV 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008  81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAI*SLHLTGISSLLGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:MTH00182  121 EQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLS 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIISQVSAAF-AKKNVFGYLGMVYAML 239
Cdd:MTH00182  201 LPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFvAKKQIFGYLGMVYAML 280

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 240 SIGLLGSIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFTLGFILLFVMGGVTGVAM 319
Cdd:MTH00182  281 SIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVL 360

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1036393008 320 SNSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTG 353
Cdd:MTH00182  361 ANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGG 394
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-353 1.36e-176

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 500.51  E-value: 1.36e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008   1 LAQPGNqiFMGNHQLYNVIVTAHAFIMVFFLVMPALIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:MTH00184   43 LSAPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFV 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008  81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAI*SLHLTGISSLLGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:MTH00184  121 EQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLS 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIISQVSAAF-AKKNVFGYLGMVYAML 239
Cdd:MTH00184  201 LPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFaAKKQIFGYLGMVYAMV 280

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 240 SIGLLGSIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFTLGFILLFVMGGVTGVAM 319
Cdd:MTH00184  281 SIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVL 360

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1036393008 320 SNSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTG 353
Cdd:MTH00184  361 ANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGG 394
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-353 8.27e-175

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 495.89  E-value: 8.27e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008   1 LAQPGNqiFMGNHQLYNVIVTAHAFIMVFFLVMPALIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:MTH00037   41 LAQPGS--LLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGV 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008  81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAI*SLHLTGISSLLGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:MTH00037  119 ESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLS 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIISQVSAAFA-KKNVFGYLGMVYAML 239
Cdd:MTH00037  199 LPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSgKQEPFGYLGMVYAMI 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 240 SIGLLGSIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFTLGFILLFVMGGVTGVAM 319
Cdd:MTH00037  279 AIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVL 358

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1036393008 320 SNSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTG 353
Cdd:MTH00037  359 ANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAG 392
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-353 3.37e-174

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 493.81  E-value: 3.37e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008   1 LAQPGnqIFMGNHQLYNVIVTAHAFIMVFFLVMPALIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:MTH00079   42 LSKPG--LLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFV 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008  81 ESGAGTGWTVYPPLSSvQAHSGPSVDLAI*SLHLTGISSLLGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:MTH00079  120 DMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLS 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIISQVSAAFA-KKNVFGYLGMVYAML 239
Cdd:MTH00079  199 LPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTgKKEVFGSLGMVYAIL 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 240 SIGLLGSIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFTLGFILLFVMGGVTGVAM 319
Cdd:MTH00079  279 SIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVIL 358

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1036393008 320 SNSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTG 353
Cdd:MTH00079  359 SNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTG 392
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-353 2.23e-173

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 491.72  E-value: 2.23e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008   1 LAQPGNqiFMGNHQLYNVIVTAHAFIMVFFLVMPALIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:MTH00007   38 LGQPGA--FLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAV 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008  81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAI*SLHLTGISSLLGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:MTH00007  116 EKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLS 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIISQVSAAFAKK-NVFGYLGMVYAML 239
Cdd:MTH00007  196 LPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKlEPFGTLGMIYAML 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 240 SIGLLGSIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFTLGFILLFVMGGVTGVAM 319
Cdd:MTH00007  276 GIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVL 355

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1036393008 320 SNSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTG 353
Cdd:MTH00007  356 SNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAA 389
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-353 6.51e-173

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 490.98  E-value: 6.51e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008   1 LAQPGNqiFMGNHQLYNVIVTAHAFIMVFFLVMPALIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:MTH00183   41 LSQPGA--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGV 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008  81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAI*SLHLTGISSLLGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:MTH00183  119 EAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLS 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIISQVSAAFA-KKNVFGYLGMVYAML 239
Cdd:MTH00183  199 LPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSgKKEPFGYMGMVWAMM 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 240 SIGLLGSIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFTLGFILLFVMGGVTGVAM 319
Cdd:MTH00183  279 AIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVL 358

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1036393008 320 SNSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTG 353
Cdd:MTH00183  359 ANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAA 392
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-353 3.56e-171

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 486.37  E-value: 3.56e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008   1 LAQPGNqiFMGNHQLYNVIVTAHAFIMVFFLVMPALIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:MTH00077   41 LSQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGV 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008  81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAI*SLHLTGISSLLGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:MTH00077  119 EAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLS 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIISQVSAAFA-KKNVFGYLGMVYAML 239
Cdd:MTH00077  199 LPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSaKKEPFGYMGMVWAMM 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 240 SIGLLGSIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFTLGFILLFVMGGVTGVAM 319
Cdd:MTH00077  279 SIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVL 358

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1036393008 320 SNSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTG 353
Cdd:MTH00077  359 ANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGG 392
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-353 1.91e-169

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 482.07  E-value: 1.91e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008   1 LAQPGNqiFMGNHQLYNVIVTAHAFIMVFFLVMPALIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:MTH00103   41 LGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMV 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008  81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAI*SLHLTGISSLLGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:MTH00103  119 EAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLS 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIISQVSAAFA-KKNVFGYLGMVYAML 239
Cdd:MTH00103  199 LPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSgKKEPFGYMGMVWAMM 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 240 SIGLLGSIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFTLGFILLFVMGGVTGVAM 319
Cdd:MTH00103  279 SIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVL 358

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1036393008 320 SNSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTG 353
Cdd:MTH00103  359 ANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGG 392
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-353 5.81e-156

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 448.31  E-value: 5.81e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008   1 LAQPGNqiFMGNHQLYNVIVTAHAFIMVFFLVMPALIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:MTH00026   42 LSSPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLV 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008  81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAI*SLHLTGISSLLGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:MTH00026  120 EQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLS 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIISQVSAAFA-KKNVFGYLGMVYAML 239
Cdd:MTH00026  200 LPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSyKKQIFGYLGMVYAML 279

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 240 SIGLLGSIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGG--SLKFETPLLFTLGFILLFVMGGVTGV 317
Cdd:MTH00026  280 AIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGI 359

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1036393008 318 AMSNSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTG 353
Cdd:MTH00026  360 VLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGG 395
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-353 2.80e-155

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: 443.90  E-value: 2.80e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008   1 LAQPGNQIfmGNHQLYNVIVTAHAFIMVFFLVMPALIGGFGNWFVPlMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:cd00919    30 LATPGSLF--LDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGLLLLLSSVLV 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008  81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAI*SLHLTGISSLLGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:cd00919   107 GGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLA 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIISQVSAAFAKKNVFGYLGMVYAMLS 240
Cdd:cd00919   187 LPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGKPLFGYKLMVYAFLA 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 241 IGLLGSIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFTLGFILLFVMGGVTGVAMS 320
Cdd:cd00919   267 IGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLA 346

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1036393008 321 NSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTG 353
Cdd:cd00919   347 NVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAG 379
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-353 4.52e-155

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: 444.74  E-value: 4.52e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008   1 LAQPGNQiFMGNhQLYNVIVTAHAFIMVFFLVMPaLIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:TIGR02891  35 LATPGNT-FMDA-ETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFT 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008  81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAI*SLHLTGISSLLGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:TIGR02891 112 GGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLA 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIISQVSAAFAKKNVFGYLGMVYAMLS 240
Cdd:TIGR02891 192 FPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKPIFGYRAMVYATVA 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 241 IGLLGSIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFTLGFILLFVMGGVTGVAMS 320
Cdd:TIGR02891 272 IGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLA 351

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1036393008 321 NSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTG 353
Cdd:TIGR02891 352 SVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAA 384
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-353 2.15e-153

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 441.87  E-value: 2.15e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008   1 LAQPGNQiFMGNHQlYNVIVTAHAFIMVFFLVMPaLIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:COG0843    44 LAGPGLG-LLSPET-YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFV 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008  81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAI*SLHLTGISSLLGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:COG0843   121 GGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLA 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIISQVSAAFAKKNVFGYLGMVYAMLS 240
Cdd:COG0843   201 FPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVA 280

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 241 IGLLGSIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFTLGFILLFVMGGVTGVAMS 320
Cdd:COG0843   281 IAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLA 360

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1036393008 321 NSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTG 353
Cdd:COG0843   361 SVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAG 393
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-353 1.79e-137

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: 400.03  E-value: 1.79e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008   1 LAQPGNQiFMGNHQlYNVIVTAHAFIMVFFLVMPALIGgFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:cd01662    36 LALPGND-FLSPEH-YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLI 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008  81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAI*SLHLTGISSLLGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:cd01662   113 GGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFA 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIISQVSAAFAKKNVFGYLGMVYAMLS 240
Cdd:cd01662   193 FPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRKPLFGYRSMVYATVA 272

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 241 IGLLGSIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFTLGFILLFVMGGVTGVAMS 320
Cdd:cd01662   273 IGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLA 352

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1036393008 321 NSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTG 353
Cdd:cd01662   353 SPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAG 385
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 16-350 5.19e-122

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 360.92  E-value: 5.19e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008  16 YNVIVTAHAFIMVFFLVMPALIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIVesGAGTGWTVYPPLS 95
Cdd:MTH00048   55 YNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLS 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008  96 SVQAHSGPSVDLAI*SLHLTGISSLLGAINFISTIYNMRAPGLsFHRLPLFVWSVLITAFLLLLTLPVLAGAITMLLTDR 175
Cdd:MTH00048  133 SSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNV-FSRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDR 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 176 NLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIISQVSAAFAKKN-VFGYLGMVYAMLSIGLLGSIVWAHHMF 254
Cdd:MTH00048  212 NFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDdPFGYYGLVFAMFSIVCLGSVVWAHHMF 291

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 255 TVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLL-FTLGFILLFVMGGVTGVAMSNSGLDIAIHDTYY 333
Cdd:MTH00048  292 TVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWF 371

                         330
                  ....*....|....*..
gi 1036393008 334 IVGHFHYVLSMGAVFGI 350
Cdd:MTH00048  372 VVAHFHYVLSLGSYSSV 388
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-353 7.69e-102

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: 306.81  E-value: 7.69e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008   1 LAQPGNQIFmgNHQLYNVIVTAHAFIMVFFLVMPAlIGGFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAiv 80
Cdd:pfam00115  28 LAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASF-- 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008  81 eSGAGTGWTVYPPLssvqahsgPSVDLAI*SLHLTGISSLLGAINFISTIYNMRAPGLSFhRLPLFVWSVLITAFLLLLT 160
Cdd:pfam00115 103 -GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLA 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 161 LPVLAGAITMLLTDRNLNTsfydpsGGGDPVLYQHLFWFFGHPEVYILILPGFGIISQVSAAFAKKNVFGYLGMVYAMLS 240
Cdd:pfam00115 173 FPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRPLFGYKLSVLAFWL 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 241 IGLLGSIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKF-ETPLLFTLGFILLFVMGGVTGVAM 319
Cdd:pfam00115 247 IAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFFLGFAFLFIIGGLTGVML 326

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1036393008 320 SNSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTG 353
Cdd:pfam00115 327 ALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGG 360
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-353 4.32e-94

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: 293.30  E-value: 4.32e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008   1 LAQPGNQIFMGNHqlYNVIVTAHAFIMVFFLVMPALIGgFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:TIGR02882  79 LTVPDNKFLDAQH--YNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVI 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008  81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAI*SLHLTGISSLLGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:TIGR02882 156 GGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFA 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIISQVSAAFAKKNVFGYLGMVYAMLS 240
Cdd:TIGR02882 236 FPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIISTFAQKRLFGYKSMVWSTVG 315

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 241 IGLLGSIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFTLGFILLFVMGGVTGVAMS 320
Cdd:TIGR02882 316 IAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLA 395

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1036393008 321 NSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTG 353
Cdd:TIGR02882 396 MASADYQYHNTYFLVAHFHYVLITGVVFACLAG 428
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-353 6.65e-92

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 288.37  E-value: 6.65e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008   1 LAQPGNQIFMGNHQlYNVIVTAHAFIMVFFLVMPALIGgFGNWFVPLMIGAPDMAFPRMNNISFWLLPPALLLLVSSAIV 80
Cdd:PRK15017   85 LASAGEAGFLPPHH-YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGV 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008  81 ESGAGTGWTVYPPLSSVQAHSGPSVDLAI*SLHLTGISSLLGAINFISTIYNMRAPGLSFHRLPLFVWSVLITAFLLLLT 160
Cdd:PRK15017  163 GEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIAS 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 161 LPVLAGAITMLLTDRNLNTSFYDPSGGGDPVLYQHLFWFFGHPEVYILILPGFGIISQVSAAFAKKNVFGYLGMVYAMLS 240
Cdd:PRK15017  243 FPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWATVC 322

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 241 IGLLGSIVWAHHMFTVGLDVDTRAYFSAATMIIAVPTGIKIFSWLATLWGGSLKFETPLLFTLGFILLFVMGGVTGVAMS 320
Cdd:PRK15017  323 ITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLA 402

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1036393008 321 NSGLDIAIHDTYYIVGHFHYVLSMGAVFGIFTG 353
Cdd:PRK15017  403 VPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAG 435
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 9-339 4.10e-09

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: 57.68  E-value: 4.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008   9 FMGNHQLYNVIVTAHAFIMVffLVMPAL-IGGFGNWFVPLMIGAPDMAfPRMNNISFWLLPPALLLLVSsAIVESGAGTG 87
Cdd:cd01660    37 LPSSGILYYQGLTLHGVLLA--IVFTTFfIMGFFYAIVARALLRSLFN-RRLAWAGFWLMVIGTVMAAV-PILLGQASVL 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008  88 WTVYPPLssvQAHSGPSVDLAI*slhLTGISSLLGAINFI-STIYNMRAPGLsfhRLPLFVWSVLITAFLLLLTLPVLAg 166
Cdd:cd01660   113 YTFYPPL---QAHPLFYIGAAL----VVVGSWISGFAMFVtLWRWKKANPGK---KVPLATFMVVTTMILWLVASLGVA- 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 167 aITMLLTDRNLNTSFYDPSgggDPVLYQHLFWFFGHPEVYILILPGFGIISQVSAAFAKKNVFGYLGMVYAMLSIGLLGS 246
Cdd:cd01660   182 -LEVLFQLLPWSLGLVDTV---DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARLAFILFLLFST 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036393008 247 IVWAHHMFT-VGLDVDTRAYFSAATMIIAVPT-------------------GIKIFSWLATLWGGSLKFETPLLFtlgfI 306
Cdd:cd01660   258 PVGFHHQFAdPGIGPGWKFIHMVLTFMVALPSlltaftvfasleiagrlrgGKGLFGWIRALPWGDPMFLALFLA----M 333

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1036393008 307 LLFVMGGVTGVAMSNSGLDIAIHDTYYIVGHFH 339
Cdd:cd01660   334 LMFIPGGAGGIINASYQLNYVVHNTAWVPGHFH 366
 
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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