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Conserved domains on  [gi|951271612|gb|ALN50165|]
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cytochrome c oxidase subunit I, partial (mitochondrion) [Aphonopelma sp. APH_1219]

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 ...
 1-299 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: 546.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612   1 LSSLTDIGVGAGWTIYPPLSSFVGHSGGGMDFAIFSLHLAGASSIMGSVNFISTVVNMRSSGMSMERVPLFVWSVLITTV 80
Cdd:MTH00153 112 SSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAI 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612  81 LLLLSLPVLAGAITMLLSDRNFNTSFFDPAGGGDPVLFQHLFWFFGHPEVYILILPGFGMISHIISSSVGKSEPFGSLGM 160
Cdd:MTH00153 192 LLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGM 271

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612 161 IYAMVSIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAVPTGISVFSWMATLYGSYFKMDASLMWCMGFVFLFTIGGL 240
Cdd:MTH00153 272 IYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGL 351

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 951271612 241 TGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAILGGLVYWFPLFFGVFMNYKWVKL 299
Cdd:MTH00153 352 TGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKI 410
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-299 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 546.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612   1 LSSLTDIGVGAGWTIYPPLSSFVGHSGGGMDFAIFSLHLAGASSIMGSVNFISTVVNMRSSGMSMERVPLFVWSVLITTV 80
Cdd:MTH00153 112 SSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAI 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612  81 LLLLSLPVLAGAITMLLSDRNFNTSFFDPAGGGDPVLFQHLFWFFGHPEVYILILPGFGMISHIISSSVGKSEPFGSLGM 160
Cdd:MTH00153 192 LLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGM 271

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612 161 IYAMVSIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAVPTGISVFSWMATLYGSYFKMDASLMWCMGFVFLFTIGGL 240
Cdd:MTH00153 272 IYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGL 351

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 951271612 241 TGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAILGGLVYWFPLFFGVFMNYKWVKL 299
Cdd:MTH00153 352 TGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKI 410
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-299 1.64e-177

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: 498.93  E-value: 1.64e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612   1 LSSLTDIGVGAGWTIYPPLSSFVGHSGGGMDFAIFSLHLAGASSIMGSVNFISTVVNMRSSGMSMERVPLFVWSVLITTV 80
Cdd:cd01663  105 LSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAF 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612  81 LLLLSLPVLAGAITMLLSDRNFNTSFFDPAGGGDPVLFQHLFWFFGHPEVYILILPGFGMISHIISSSVGKSEPFGSLGM 160
Cdd:cd01663  185 LLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGM 264

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612 161 IYAMVSIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAVPTGISVFSWMATLYGSYFKMDASLMWCMGFVFLFTIGGL 240
Cdd:cd01663  265 VYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGL 344

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 951271612 241 TGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAILGGLVYWFPLFFGVFMNYKWVKL 299
Cdd:cd01663  345 TGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKI 403
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 2-299 6.65e-118

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: 348.06  E-value: 6.65e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612    2 SSLTDIGVGAGWTIYPPLSSFVGHSGGGMDFAIFSLHLAGASSIMGSVNFISTVVNMRSSGMSMERVPLFVWSVLITTVL 81
Cdd:TIGR02891 108 SFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSIL 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612   82 LLLSLPVLAGAITMLLSDRNFNTSFFDPAGGGDPVLFQHLFWFFGHPEVYILILPGFGMISHIISSSVGKsEPFGSLGMI 161
Cdd:TIGR02891 188 ILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARK-PIFGYRAMV 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612  162 YAMVSIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAVPTGISVFSWMATLYGSYFKMDASLMWCMGFVFLFTIGGLT 241
Cdd:TIGR02891 267 YATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLT 346

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 951271612  242 GVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAILGGLVYWFPLFFGVFMNYKWVKL 299
Cdd:TIGR02891 347 GVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRW 404
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-299 1.35e-114

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 340.57  E-value: 1.35e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612   1 LSSLTDIGVGAGWTIYPPLSSFVGHSGGGMDFAIFSLHLAGASSIMGSVNFISTVVNMRSSGMSMERVPLFVWSVLITTV 80
Cdd:COG0843  116 ISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSI 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612  81 LLLLSLPVLAGAITMLLSDRNFNTSFFDPAGGGDPVLFQHLFWFFGHPEVYILILPGFGMISHIISSSVGKsEPFGSLGM 160
Cdd:COG0843  196 LILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRK-PLFGYKAM 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612 161 IYAMVSIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAVPTGISVFSWMATLYGSYFKMDASLMWCMGFVFLFTIGGL 240
Cdd:COG0843  275 VLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGL 354

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 951271612 241 TGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAILGGLVYWFPLFFGVFMNYKWVKL 299
Cdd:COG0843  355 TGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKI 413
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 8-299 2.70e-75

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: 236.70  E-value: 2.70e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612    8 GVGAGWTIYPPLssfvghsgGGMDFAIFSLHLAGASSIMGSVNFISTVVNMRSSGMSMeRVPLFVWSVLITTVLLLLSLP 87
Cdd:pfam00115 104 GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFP 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612   88 VLAGAITMLLSDRNFNtsffdpAGGGDPVLFQHLFWFFGHPEVYILILPGFGMISHIISSSVGKsEPFGSLGMIYAMVSI 167
Cdd:pfam00115 175 VLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWLI 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612  168 GGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAVPTGISVFSWMATLYGSYFKM-DASLMWCMGFVFLFTIGGLTGVVLA 246
Cdd:pfam00115 248 AFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFFLGFAFLFIIGGLTGVMLA 327

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 951271612  247 NSSLDIVLHDTYYVVAHFHYVLSMGAVFAILGGLVYWFPLFFGVFMNYKWVKL 299
Cdd:pfam00115 328 LPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-299 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 546.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612   1 LSSLTDIGVGAGWTIYPPLSSFVGHSGGGMDFAIFSLHLAGASSIMGSVNFISTVVNMRSSGMSMERVPLFVWSVLITTV 80
Cdd:MTH00153 112 SSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAI 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612  81 LLLLSLPVLAGAITMLLSDRNFNTSFFDPAGGGDPVLFQHLFWFFGHPEVYILILPGFGMISHIISSSVGKSEPFGSLGM 160
Cdd:MTH00153 192 LLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGM 271

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612 161 IYAMVSIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAVPTGISVFSWMATLYGSYFKMDASLMWCMGFVFLFTIGGL 240
Cdd:MTH00153 272 IYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGL 351

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 951271612 241 TGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAILGGLVYWFPLFFGVFMNYKWVKL 299
Cdd:MTH00153 352 TGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKI 410
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-299 1.64e-177

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: 498.93  E-value: 1.64e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612   1 LSSLTDIGVGAGWTIYPPLSSFVGHSGGGMDFAIFSLHLAGASSIMGSVNFISTVVNMRSSGMSMERVPLFVWSVLITTV 80
Cdd:cd01663  105 LSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAF 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612  81 LLLLSLPVLAGAITMLLSDRNFNTSFFDPAGGGDPVLFQHLFWFFGHPEVYILILPGFGMISHIISSSVGKSEPFGSLGM 160
Cdd:cd01663  185 LLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGM 264

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612 161 IYAMVSIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAVPTGISVFSWMATLYGSYFKMDASLMWCMGFVFLFTIGGL 240
Cdd:cd01663  265 VYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGL 344

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 951271612 241 TGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAILGGLVYWFPLFFGVFMNYKWVKL 299
Cdd:cd01663  345 TGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKI 403
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-298 7.91e-167

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 472.93  E-value: 7.91e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612   1 LSSLTDIGVGAGWTIYPPLSSFVGHSGGGMDFAIFSLHLAGASSIMGSVNFISTVVNMRSSGMSMERVPLFVWSVLITTV 80
Cdd:MTH00223 111 SSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAF 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612  81 LLLLSLPVLAGAITMLLSDRNFNTSFFDPAGGGDPVLFQHLFWFFGHPEVYILILPGFGMISHIISSSVGKSEPFGSLGM 160
Cdd:MTH00223 191 LLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGM 270

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612 161 IYAMVSIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAVPTGISVFSWMATLYGSYFKMDASLMWCMGFVFLFTIGGL 240
Cdd:MTH00223 271 IYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGL 350

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 951271612 241 TGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAILGGLVYWFPLFFGVFMNYKWVK 298
Cdd:MTH00223 351 TGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAK 408
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-299 3.64e-161

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 458.37  E-value: 3.64e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612   1 LSSLTDIGVGAGWTIYPPLSSFVGHSGGGMDFAIFSLHLAGASSIMGSVNFISTVVNMRSSGMSMERVPLFVWSVLITTV 80
Cdd:MTH00167 114 ASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTI 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612  81 LLLLSLPVLAGAITMLLSDRNFNTSFFDPAGGGDPVLFQHLFWFFGHPEVYILILPGFGMISHIISSSVGKSEPFGSLGM 160
Cdd:MTH00167 194 LLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGM 273

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612 161 IYAMVSIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAVPTGISVFSWMATLYGSYFKMDASLMWCMGFVFLFTIGGL 240
Cdd:MTH00167 274 VWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGL 353

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 951271612 241 TGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAILGGLVYWFPLFFGVFMNYKWVKL 299
Cdd:MTH00167 354 TGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKI 412
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 2-298 5.17e-160

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 455.71  E-value: 5.17e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612   2 SSLTDIGVGAGWTIYPPLSSFVGHSGGGMDFAIFSLHLAGASSIMGSVNFISTVVNMRSSGMSMERVPLFVWSVLITTVL 81
Cdd:MTH00116 115 SSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVL 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612  82 LLLSLPVLAGAITMLLSDRNFNTSFFDPAGGGDPVLFQHLFWFFGHPEVYILILPGFGMISHIISSSVGKSEPFGSLGMI 161
Cdd:MTH00116 195 LLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMV 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612 162 YAMVSIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAVPTGISVFSWMATLYGSYFKMDASLMWCMGFVFLFTIGGLT 241
Cdd:MTH00116 275 WAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLT 354

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 951271612 242 GVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAILGGLVYWFPLFFGVFMNYKWVK 298
Cdd:MTH00116 355 GIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTK 411
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 2-298 5.45e-160

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 455.34  E-value: 5.45e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612   2 SSLTDIGVGAGWTIYPPLSSFVGHSGGGMDFAIFSLHLAGASSIMGSVNFISTVVNMRSSGMSMERVPLFVWSVLITTVL 81
Cdd:MTH00142 113 SAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAIL 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612  82 LLLSLPVLAGAITMLLSDRNFNTSFFDPAGGGDPVLFQHLFWFFGHPEVYILILPGFGMISHIISSSVGKSEPFGSLGMI 161
Cdd:MTH00142 193 LLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMI 272

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612 162 YAMVSIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAVPTGISVFSWMATLYGSYFKMDASLMWCMGFVFLFTIGGLT 241
Cdd:MTH00142 273 YAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLT 352

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 951271612 242 GVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAILGGLVYWFPLFFGVFMNYKWVK 298
Cdd:MTH00142 353 GIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLK 409
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 8-298 4.87e-148

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 425.40  E-value: 4.87e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612   8 GVGAGWTIYPPLSSFVGHSGGGMDFAIFSLHLAGASSIMGSVNFISTVVNMRSSGMSMERVPLFVWSVLITTVLLLLSLP 87
Cdd:MTH00037 121 GAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLP 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612  88 VLAGAITMLLSDRNFNTSFFDPAGGGDPVLFQHLFWFFGHPEVYILILPGFGMISHIISSSVGKSEPFGSLGMIYAMVSI 167
Cdd:MTH00037 201 VLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAI 280

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612 168 GGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAVPTGISVFSWMATLYGSYFKMDASLMWCMGFVFLFTIGGLTGVVLAN 247
Cdd:MTH00037 281 GILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLAN 360

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 951271612 248 SSLDIVLHDTYYVVAHFHYVLSMGAVFAILGGLVYWFPLFFGVFMNYKWVK 298
Cdd:MTH00037 361 SSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSK 411
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 2-298 1.29e-143

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 413.91  E-value: 1.29e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612   2 SSLTDIGVGAGWTIYPPLSSFVGHSGGGMDFAIFSLHLAGASSIMGSVNFISTVVNMRSSGMSMERVPLFVWSVLITTVL 81
Cdd:MTH00007 112 SAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVL 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612  82 LLLSLPVLAGAITMLLSDRNFNTSFFDPAGGGDPVLFQHLFWFFGHPEVYILILPGFGMISHIISSSVGKSEPFGSLGMI 161
Cdd:MTH00007 192 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMI 271

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612 162 YAMVSIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAVPTGISVFSWMATLYGSYFKMDASLMWCMGFVFLFTIGGLT 241
Cdd:MTH00007 272 YAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGGLT 351

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 951271612 242 GVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAILGGLVYWFPLFFGVFMNYKWVK 298
Cdd:MTH00007 352 GIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAK 408
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 2-299 2.12e-139

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 403.11  E-value: 2.12e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612   2 SSLTDIGVGAGWTIYPPLSSFVGHSGGGMDFAIFSLHLAGASSIMGSVNFISTVVNMRSSGMSMERVPLFVWSVLITTVL 81
Cdd:MTH00103 115 SSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVL 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612  82 LLLSLPVLAGAITMLLSDRNFNTSFFDPAGGGDPVLFQHLFWFFGHPEVYILILPGFGMISHIISSSVGKSEPFGSLGMI 161
Cdd:MTH00103 195 LLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMV 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612 162 YAMVSIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAVPTGISVFSWMATLYGSYFKMDASLMWCMGFVFLFTIGGLT 241
Cdd:MTH00103 275 WAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLT 354

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 951271612 242 GVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAILGGLVYWFPLFFGVFMNYKWVKL 299
Cdd:MTH00103 355 GIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKI 412
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 2-293 1.32e-138

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 401.51  E-value: 1.32e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612   2 SSLTDIGVGAGWTIYPPLSSFVGHSGGGMDFAIFSLHLAGASSIMGSVNFISTVVNMRSSGMSMERVPLFVWSVLITTVL 81
Cdd:MTH00182 117 SAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFL 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612  82 LLLSLPVLAGAITMLLSDRNFNTSFFDPAGGGDPVLFQHLFWFFGHPEVYILILPGFGMISHIISSSVGKSEPFGSLGMI 161
Cdd:MTH00182 197 LLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMV 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612 162 YAMVSIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAVPTGISVFSWMATLYGSYFKMDASLMWCMGFVFLFTIGGLT 241
Cdd:MTH00182 277 YAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLT 356

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 951271612 242 GVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAILGGLVYWFPLFFGVFMN 293
Cdd:MTH00182 357 GVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYN 408
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 2-299 2.02e-138

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 400.84  E-value: 2.02e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612   2 SSLTDIGVGAGWTIYPPLSSFVGHSGGGMDFAIFSLHLAGASSIMGSVNFISTVVNMRSSGMSMERVPLFVWSVLITTVL 81
Cdd:MTH00183 115 SSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVL 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612  82 LLLSLPVLAGAITMLLSDRNFNTSFFDPAGGGDPVLFQHLFWFFGHPEVYILILPGFGMISHIISSSVGKSEPFGSLGMI 161
Cdd:MTH00183 195 LLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMV 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612 162 YAMVSIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAVPTGISVFSWMATLYGSYFKMDASLMWCMGFVFLFTIGGLT 241
Cdd:MTH00183 275 WAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLT 354

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 951271612 242 GVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAILGGLVYWFPLFFGVFMNYKWVKL 299
Cdd:MTH00183 355 GIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKI 412
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 2-299 2.68e-136

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 395.46  E-value: 2.68e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612   2 SSLTDIGVGAGWTIYPPLSSFVGHSGGGMDFAIFSLHLAGASSIMGSVNFISTVVNMRSSGMSMERVPLFVWSVLITTVL 81
Cdd:MTH00077 115 SSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVL 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612  82 LLLSLPVLAGAITMLLSDRNFNTSFFDPAGGGDPVLFQHLFWFFGHPEVYILILPGFGMISHIISSSVGKSEPFGSLGMI 161
Cdd:MTH00077 195 LLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMV 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612 162 YAMVSIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAVPTGISVFSWMATLYGSYFKMDASLMWCMGFVFLFTIGGLT 241
Cdd:MTH00077 275 WAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLT 354

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 951271612 242 GVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAILGGLVYWFPLFFGVFMNYKWVKL 299
Cdd:MTH00077 355 GIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKI 412
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 2-294 1.39e-135

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 393.28  E-value: 1.39e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612   2 SSLTDIGVGAGWTIYPPLSSfVGHSGGGMDFAIFSLHLAGASSIMGSVNFISTVVNMRSSGMSMERVPLFVWSVLITTVL 81
Cdd:MTH00079 116 SCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFL 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612  82 LLLSLPVLAGAITMLLSDRNFNTSFFDPAGGGDPVLFQHLFWFFGHPEVYILILPGFGMISHIISSSVGKSEPFGSLGMI 161
Cdd:MTH00079 195 LVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMV 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612 162 YAMVSIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAVPTGISVFSWMATLYGSYFKMDASLMWCMGFVFLFTIGGLT 241
Cdd:MTH00079 275 YAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLT 354

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 951271612 242 GVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAILGGLVYWFPLFFGVFMNY 294
Cdd:MTH00079 355 GVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDK 407
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 2-284 1.08e-134

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 391.50  E-value: 1.08e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612   2 SSLTDIGVGAGWTIYPPLSSFVGHSGGGMDFAIFSLHLAGASSIMGSVNFISTVVNMRSSGMSMERVPLFVWSVLITTVL 81
Cdd:MTH00184 117 SAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFL 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612  82 LLLSLPVLAGAITMLLSDRNFNTSFFDPAGGGDPVLFQHLFWFFGHPEVYILILPGFGMISHIISSSVGKSEPFGSLGMI 161
Cdd:MTH00184 197 LLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMV 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612 162 YAMVSIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAVPTGISVFSWMATLYGSYFKMDASLMWCMGFVFLFTIGGLT 241
Cdd:MTH00184 277 YAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLT 356

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 951271612 242 GVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAILGGLVYWF 284
Cdd:MTH00184 357 GIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWF 399
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-299 2.14e-119

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: 350.29  E-value: 2.14e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612   1 LSSLTDIGVGAGWTIYPPLSSFVGHSGGGMDFAIFSLHLAGASSIMGSVNFISTVVNMRSSGMSMERVPLFVWSVLITTV 80
Cdd:cd00919  102 SSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAI 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612  81 LLLLSLPVLAGAITMLLSDRNFNTSFFDPAGGGDPVLFQHLFWFFGHPEVYILILPGFGMISHIISSSVGKsEPFGSLGM 160
Cdd:cd00919  182 LLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGK-PLFGYKLM 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612 161 IYAMVSIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAVPTGISVFSWMATLYGSYFKMDASLMWCMGFVFLFTIGGL 240
Cdd:cd00919  261 VYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGL 340

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 951271612 241 TGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAILGGLVYWFPLFFGVFMNYKWVKL 299
Cdd:cd00919  341 TGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKI 399
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 2-299 6.65e-118

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: 348.06  E-value: 6.65e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612    2 SSLTDIGVGAGWTIYPPLSSFVGHSGGGMDFAIFSLHLAGASSIMGSVNFISTVVNMRSSGMSMERVPLFVWSVLITTVL 81
Cdd:TIGR02891 108 SFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSIL 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612   82 LLLSLPVLAGAITMLLSDRNFNTSFFDPAGGGDPVLFQHLFWFFGHPEVYILILPGFGMISHIISSSVGKsEPFGSLGMI 161
Cdd:TIGR02891 188 ILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARK-PIFGYRAMV 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612  162 YAMVSIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAVPTGISVFSWMATLYGSYFKMDASLMWCMGFVFLFTIGGLT 241
Cdd:TIGR02891 267 YATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLT 346

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 951271612  242 GVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAILGGLVYWFPLFFGVFMNYKWVKL 299
Cdd:TIGR02891 347 GVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRW 404
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 2-284 6.14e-117

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 346.62  E-value: 6.14e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612   2 SSLTDIGVGAGWTIYPPLSSFVGHSGGGMDFAIFSLHLAGASSIMGSVNFISTVVNMRSSGMSMERVPLFVWSVLITTVL 81
Cdd:MTH00026 116 SSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAIL 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612  82 LLLSLPVLAGAITMLLSDRNFNTSFFDPAGGGDPVLFQHLFWFFGHPEVYILILPGFGMISHIISSSVGKSEPFGSLGMI 161
Cdd:MTH00026 196 LLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMV 275

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612 162 YAMVSIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAVPTGISVFSWMATLYGSYFKM--DASLMWCMGFVFLFTIGG 239
Cdd:MTH00026 276 YAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSGRNLifTTPMAWALGFIFLFTIGG 355

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 951271612 240 LTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAILGGLVYWF 284
Cdd:MTH00026 356 LTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWF 400
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-299 1.35e-114

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 340.57  E-value: 1.35e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612   1 LSSLTDIGVGAGWTIYPPLSSFVGHSGGGMDFAIFSLHLAGASSIMGSVNFISTVVNMRSSGMSMERVPLFVWSVLITTV 80
Cdd:COG0843  116 ISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSI 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612  81 LLLLSLPVLAGAITMLLSDRNFNTSFFDPAGGGDPVLFQHLFWFFGHPEVYILILPGFGMISHIISSSVGKsEPFGSLGM 160
Cdd:COG0843  196 LILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRK-PLFGYKAM 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612 161 IYAMVSIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAVPTGISVFSWMATLYGSYFKMDASLMWCMGFVFLFTIGGL 240
Cdd:COG0843  275 VLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGL 354

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 951271612 241 TGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAILGGLVYWFPLFFGVFMNYKWVKL 299
Cdd:COG0843  355 TGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKI 413
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 7-293 7.83e-107

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 320.09  E-value: 7.83e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612   7 IGVGAGWTIYPPLSSFVGHSGGGMDFAIFSLHLAGASSIMGSVNFISTVVNMRSSGMSmERVPLFVWSVLITTVLLLLSL 86
Cdd:MTH00048 119 LGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVF-SRTSIILWSYLFTSILLLLSL 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612  87 PVLAGAITMLLSDRNFNTSFFDPAGGGDPVLFQHLFWFFGHPEVYILILPGFGMISHIISSSVGKSEPFGSLGMIYAMVS 166
Cdd:MTH00048 198 PVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFS 277

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612 167 IGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAVPTGISVFSWMATLYGSYF-KMDASLMWCMGFVFLFTIGGLTGVVL 245
Cdd:MTH00048 278 IVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVrKSDPVVWWVVSFIVLFTIGGVTGIVL 357

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 951271612 246 ANSSLDIVLHDTYYVVAHFHYVLSMGAVFAILGGLVYWFPLFFGVFMN 293
Cdd:MTH00048 358 SASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLN 405
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-299 2.10e-99

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: 300.65  E-value: 2.10e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612   1 LSSLTDIGVGAGWTIYPPLSSFVGHSGGGMDFAIFSLHLAGASSIMGSVNFISTVVNMRSSGMSMERVPLFVWSVLITTV 80
Cdd:cd01662  108 ASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSI 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612  81 LLLLSLPVLAGAITMLLSDRNFNTSFFDPAGGGDPVLFQHLFWFFGHPEVYILILPGFGMISHIISSSVGKsEPFGSLGM 160
Cdd:cd01662  188 LILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRK-PLFGYRSM 266

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612 161 IYAMVSIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAVPTGISVFSWMATLYGSYFKMDASLMWCMGFVFLFTIGGL 240
Cdd:cd01662  267 VYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGL 346

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 951271612 241 TGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAILGGLVYWFPLFFGVFMNYKWVKL 299
Cdd:cd01662  347 TGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKW 405
CyoB TIGR02843
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ...
 11-299 1.28e-77

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: 248.43  E-value: 1.28e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612   11 AGWTIYPPLSSFVGHSGGGMDFAIFSLHLAGASSIMGSVNFISTVVNMRSSGMSMERVPLFVWSVLITTVLLLLSLPVLA 90
Cdd:TIGR02843 167 TGWLAYPPLSELQYSPGVGVDYYIWALQISGIGTLLTGINFFVTIIKMRAPGMTLMKMPVFTWTSLCSNVLIIASFPILT 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612   91 GAITMLLSDRNFNTSFFDPAGGGDPVLFQHLFWFFGHPEVYILILPGFGMISHIISSSVGKsEPFGSLGMIYAMVSIGGM 170
Cdd:TIGR02843 247 VTLALLTLDRYLGMHFFTNEAGGNPMMYVNLIWAWGHPEVYILILPAFGIFSEVVATFSRK-RLFGYTSMVWATIAITVL 325

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612  171 GFVVWAHHMFSVGMDVDTRAYFTAATMVIAVPTGISVFSWMATLYGSYFKMDASLMWCMGFVFLFTIGGLTGVVLANSSL 250
Cdd:TIGR02843 326 SFIVWLHHFFTMGAGANVNAFFGIATMIIAIPTGVKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLLAVPPA 405

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 951271612  251 DIVLHDTYYVVAHFHYVLSMGAVFAILGGLVYWFPLFFGVFMNYKWVKL 299
Cdd:TIGR02843 406 DFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWFPKAFGFKLNEKLGKR 454
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 8-299 2.70e-75

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: 236.70  E-value: 2.70e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612    8 GVGAGWTIYPPLssfvghsgGGMDFAIFSLHLAGASSIMGSVNFISTVVNMRSSGMSMeRVPLFVWSVLITTVLLLLSLP 87
Cdd:pfam00115 104 GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFP 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612   88 VLAGAITMLLSDRNFNtsffdpAGGGDPVLFQHLFWFFGHPEVYILILPGFGMISHIISSSVGKsEPFGSLGMIYAMVSI 167
Cdd:pfam00115 175 VLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWLI 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612  168 GGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAVPTGISVFSWMATLYGSYFKM-DASLMWCMGFVFLFTIGGLTGVVLA 246
Cdd:pfam00115 248 AFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFFLGFAFLFIIGGLTGVMLA 327

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 951271612  247 NSSLDIVLHDTYYVVAHFHYVLSMGAVFAILGGLVYWFPLFFGVFMNYKWVKL 299
Cdd:pfam00115 328 LPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 7-298 6.05e-67

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 220.58  E-value: 6.05e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612   7 IGVG----AGWTIYPPLSSFVGHSGGGMDFAIFSLHLAGASSIMGSVNFISTVVNMRSSGMSMERVPLFVWSVLITTVLL 82
Cdd:PRK15017 160 LGVGefaqTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLI 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612  83 LLSLPVLAGAITMLLSDRNFNTSFFDPAGGGDPVLFQHLFWFFGHPEVYILILPGFGMISHIiSSSVGKSEPFGSLGMIY 162
Cdd:PRK15017 240 IASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEI-AATFSRKRLFGYTSLVW 318

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612 163 AMVSIGGMGFVVWAHHMFSVGMDVDTRAYFTAATMVIAVPTGISVFSWMATLYGSYFKMDASLMWCMGFVFLFTIGGLTG 242
Cdd:PRK15017 319 ATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTG 398

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 951271612 243 VVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAILGGLVYWFPLFFGVFMNYKWVK 298
Cdd:PRK15017 399 VLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGK 454
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 114-289 1.19e-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: 58.84  E-value: 1.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612 114 DPVLFQHLFWFFGHPEVYILILPGFGMISHIISSSVGK---SEPFGSLGMIYAMVSIGGMGFvvwaHHMFsvgMDVDTRA 190
Cdd:cd01660  200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGklfSDPLARLAFILFLLFSTPVGF----HHQF---ADPGIGP 272

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951271612 191 YF----TAATMVIAVPTGISVFSWMAT------------LYGSYFKM---DASLMWCMGFVFLFTIGGLTGVVLANSSLD 251
Cdd:cd01660  273 GWkfihMVLTFMVALPSLLTAFTVFASleiagrlrggkgLFGWIRALpwgDPMFLALFLAMLMFIPGGAGGIINASYQLN 352

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 951271612 252 IVLHDTYYVVAHFHyvLSMGAVFAILG-GLVYWF-PLFFG 289
Cdd:cd01660  353 YVVHNTAWVPGHFH--LTVGGAVALTFmAVAYWLvPHLTG 390
 
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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