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Conserved domains on  [gi|696110479|gb|AIT39738|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Sarcodexia lambens]

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 ...
 1-391 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: 737.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479   1 LLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFVWSVVI 80
Cdd:MTH00153 109 LLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLI 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479  81 TALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVY************************GS 160
Cdd:MTH00153 189 TAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGT 268

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 161 LGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYSPATLWALGFVFLFTV 240
Cdd:MTH00153 269 LGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTI 348

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 241 GGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFTIMFMGVNLTFFPQHF 320
Cdd:MTH00153 349 GGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHF 428

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 696110479 321 LGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLVSQRQVMFPVQLNSSIEWLQNTPPA 391
Cdd:MTH00153 429 LGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEWLQNLPPA 499
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-391 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 737.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479   1 LLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFVWSVVI 80
Cdd:MTH00153 109 LLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLI 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479  81 TALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVY************************GS 160
Cdd:MTH00153 189 TAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGT 268

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 161 LGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYSPATLWALGFVFLFTV 240
Cdd:MTH00153 269 LGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTI 348

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 241 GGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFTIMFMGVNLTFFPQHF 320
Cdd:MTH00153 349 GGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHF 428

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 696110479 321 LGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLVSQRQVMFPVQLNSSIEWLQNTPPA 391
Cdd:MTH00153 429 LGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEWLQNLPPA 499
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-386 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: 635.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479   1 LLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFVWSVVI 80
Cdd:cd01663  102 LLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLI 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479  81 TALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVY************************GS 160
Cdd:cd01663  182 TAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGY 261

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 161 LGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYSPATLWALGFVFLFTV 240
Cdd:cd01663  262 LGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTI 341

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 241 GGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFTIMFMGVNLTFFPQHF 320
Cdd:cd01663  342 GGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHF 421

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 696110479 321 LGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLVSQRQVMFPV-QLNSSIEWLQ 386
Cdd:cd01663  422 LGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVgEGSTSLEWTL 488
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-390 3.90e-139

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: 405.84  E-value: 3.90e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479    1 LLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFVWSVVI 80
Cdd:TIGR02891 104 LLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILV 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479   81 TALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVY************************GS 160
Cdd:TIGR02891 184 TSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKPIF-GY 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479  161 LGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYSPATLWALGFVFLFTV 240
Cdd:TIGR02891 263 RAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVI 342

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479  241 GGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFTIMFMGVNLTFFPQHF 320
Cdd:TIGR02891 343 GGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHL 422

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 696110479  321 LGLAGMPRRYSDYPDA--YTAWNVISTIGSTISLLGILFFFFIIWESLVSQRQVMFPVQLNSSIEWLQNTPP 390
Cdd:TIGR02891 423 LGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGANPWGATTLEWTTSSPP 494
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-390 7.43e-138

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 403.74  E-value: 7.43e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479   1 LLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFVWSVVI 80
Cdd:COG0843  113 LLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALV 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479  81 TALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVY************************GS 160
Cdd:COG0843  193 TSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKPLF-GY 271

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 161 LGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYSPATLWALGFVFLFTV 240
Cdd:COG0843  272 KAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVI 351

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 241 GGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFTIMFMGVNLTFFPQHF 320
Cdd:COG0843  352 GGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHI 431

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 696110479 321 LGLAGMPRRYSDYP--DAYTAWNVISTIGSTISLLGILFFFFIIWESLVSQRQV-MFPVQLNsSIEWLQNTPP 390
Cdd:COG0843  432 LGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPKAgGNPWGAR-TLEWATPSPP 503
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-350 1.01e-85

Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key enzyme in aerobic metabolism. Proton pumping haem-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-haem a3 (or haem o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxidases (E.C:1.10.3.11), is directly involved in the coupling between dioxygen reduction and proton pumping. Some terminal oxidases generate a transmembrane proton gradient across the plasma membrane (prokaryotes) or the mitochondrial inner membrane (eukaryotes). The enzyme complex consists of 3-4 subunits (prokaryotes) up to 13 polypeptides (mammals) of which only the catalytic subunit (equivalent to mammalian subunit I (COXI) is found in all haem-copper respiratory oxidases. The presence of a bimetallic centre (formed by a high-spin haem and copper B) as well as a low-spin haem, both ligated to six conserved histidine residues near the outer side of four transmembrane spans within CO I is common to all family members.


Pssm-ID: 459678  Cd Length: 432  Bit Score: 266.75  E-value: 1.01e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479    1 LLLVSSMveNGAGTGWTVYPPLssniahggASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFdRMPLFVWSVVI 80
Cdd:pfam00115  96 VLLLASF--GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILA 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479   81 TALLLLLSLPVLAGAITMLLTDRNINtsffdpAGGGDPILYQHLFWFFGHPEVY************************GS 160
Cdd:pfam00115 165 TAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRPLF-GY 237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479  161 LGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLN-YSPATLWALGFVFLFT 239
Cdd:pfam00115 238 KLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRfRTTPMLFFLGFAFLFI 317

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479  240 VGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFTIMFMGVNLTFFPQH 319
Cdd:pfam00115 318 IGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMH 397

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 696110479  320 FLGLAGMPRRYS----DYPDAYTAWNVISTIGSTI 350
Cdd:pfam00115 398 ILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-391 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 737.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479   1 LLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFVWSVVI 80
Cdd:MTH00153 109 LLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLI 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479  81 TALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVY************************GS 160
Cdd:MTH00153 189 TAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGT 268

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 161 LGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYSPATLWALGFVFLFTV 240
Cdd:MTH00153 269 LGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTI 348

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 241 GGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFTIMFMGVNLTFFPQHF 320
Cdd:MTH00153 349 GGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHF 428

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 696110479 321 LGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLVSQRQVMFPVQLNSSIEWLQNTPPA 391
Cdd:MTH00153 429 LGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEWLQNLPPA 499
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-386 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: 635.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479   1 LLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFVWSVVI 80
Cdd:cd01663  102 LLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLI 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479  81 TALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVY************************GS 160
Cdd:cd01663  182 TAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGY 261

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 161 LGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYSPATLWALGFVFLFTV 240
Cdd:cd01663  262 LGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTI 341

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 241 GGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFTIMFMGVNLTFFPQHF 320
Cdd:cd01663  342 GGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHF 421

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 696110479 321 LGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLVSQRQVMFPV-QLNSSIEWLQ 386
Cdd:cd01663  422 LGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVgEGSTSLEWTL 488
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-391 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 607.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479   1 LLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFVWSVVI 80
Cdd:MTH00223 108 LLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKV 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479  81 TALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVY************************GS 160
Cdd:MTH00223 188 TAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGT 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 161 LGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYSPATLWALGFVFLFTV 240
Cdd:MTH00223 268 LGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTV 347

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 241 GGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFTIMFMGVNLTFFPQHF 320
Cdd:MTH00223 348 GGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFLMFLGVNLTFFPQHF 427

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 696110479 321 LGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLVSQRQVMFPVQLNSSIEWLQNTPPA 391
Cdd:MTH00223 428 LGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVWSGHLSTSLEWDNLLPAD 498
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-391 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 606.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479   1 LLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFVWSVVI 80
Cdd:MTH00167 111 LLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILV 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479  81 TALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVY************************GS 160
Cdd:MTH00167 191 TTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGY 270

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 161 LGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYSPATLWALGFVFLFTV 240
Cdd:MTH00167 271 MGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTV 350

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 241 GGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFTIMFMGVNLTFFPQHF 320
Cdd:MTH00167 351 GGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFIGVNLTFFPQHF 430

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 696110479 321 LGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLVSQRQVMFPVQLNSSIEWLQNTPPA 391
Cdd:MTH00167 431 LGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLLPVELTSTNVEWLHGCPPP 501
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-391 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 601.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479   1 LLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFVWSVVI 80
Cdd:MTH00142 109 LLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKI 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479  81 TALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVY************************GS 160
Cdd:MTH00142 189 TAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGT 268

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 161 LGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYSPATLWALGFVFLFTV 240
Cdd:MTH00142 269 LGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTV 348

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 241 GGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFTIMFMGVNLTFFPQHF 320
Cdd:MTH00142 349 GGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYTMFIGVNLTFFPQHF 428

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 696110479 321 LGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLVSQRQVMFPVQLNSSIEWLQNTPPA 391
Cdd:MTH00142 429 LGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVMWSSHLSTSLEWSHRLPPD 499
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-390 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 595.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479   1 LLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFVWSVVI 80
Cdd:MTH00116 111 LLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLI 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479  81 TALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVY************************GS 160
Cdd:MTH00116 191 TAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGY 270

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 161 LGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYSPATLWALGFVFLFTV 240
Cdd:MTH00116 271 MGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTI 350

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 241 GGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFTIMFMGVNLTFFPQHF 320
Cdd:MTH00116 351 GGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHF 430

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 321 LGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLVSQRQVMFPVQLNSSIEWLQNTPP 390
Cdd:MTH00116 431 LGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVLQPELTTTNIEWIHGCPP 500
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-389 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 541.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479   1 LLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFVWSVVI 80
Cdd:MTH00007 108 LLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVI 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479  81 TALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVY************************GS 160
Cdd:MTH00007 188 TVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGT 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 161 LGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYSPATLWALGFVFLFTV 240
Cdd:MTH00007 268 LGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLFTT 347

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 241 GGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFTIMFMGVNLTFFPQHF 320
Cdd:MTH00007 348 GGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFLMFLGVNLTFFPQHF 427

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 696110479 321 LGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLVSQRQVMFPVQLNSSIEWLQNTP 389
Cdd:MTH00007 428 LGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIASPHMSSSLEWQDTLP 496
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-390 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 537.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479   1 LLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFVWSVVI 80
Cdd:MTH00037 111 LLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFI 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479  81 TALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVY************************GS 160
Cdd:MTH00037 191 TAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGY 270

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 161 LGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYSPATLWALGFVFLFTV 240
Cdd:MTH00037 271 LGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTI 350

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 241 GGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFTIMFMGVNLTFFPQHF 320
Cdd:MTH00037 351 GGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFLMFIGVNLTFFPQHF 430

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 321 LGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLVSQRQVMFPVQLNSSIEWLQNTPP 390
Cdd:MTH00037 431 LGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVISPEFSSSSLEWQYSSFP 500
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-390 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 536.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479   1 LLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFVWSVVI 80
Cdd:MTH00103 111 LLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLI 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479  81 TALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVY************************GS 160
Cdd:MTH00103 191 TAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGY 270

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 161 LGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYSPATLWALGFVFLFTV 240
Cdd:MTH00103 271 MGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTV 350

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 241 GGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFTIMFMGVNLTFFPQHF 320
Cdd:MTH00103 351 GGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIMFVGVNMTFFPQHF 430

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 321 LGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLVSQRQVMFPVQLNSSIEWLQNTPP 390
Cdd:MTH00103 431 LGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVLTVELTTTNLEWLHGCPP 500
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-390 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 530.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479   1 LLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFVWSVVI 80
Cdd:MTH00183 111 LLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLI 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479  81 TALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVY************************GS 160
Cdd:MTH00183 191 TAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGY 270

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 161 LGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYSPATLWALGFVFLFTV 240
Cdd:MTH00183 271 MGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTV 350

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 241 GGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFTIMFMGVNLTFFPQHF 320
Cdd:MTH00183 351 GGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVMFVGVNLTFFPQHF 430

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 321 LGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLVSQRQVMFPVQLNSSIEWLQNTPP 390
Cdd:MTH00183 431 LGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLSVELTSTNVEWLHGCPP 500
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-390 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 521.42  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479   1 LLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFVWSVVI 80
Cdd:MTH00077 111 LLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLI 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479  81 TALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVY************************GS 160
Cdd:MTH00077 191 TAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGY 270

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 161 LGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYSPATLWALGFVFLFTV 240
Cdd:MTH00077 271 MGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTV 350

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 241 GGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFTIMFMGVNLTFFPQHF 320
Cdd:MTH00077 351 GGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVMFIGVNLTFFPQHF 430

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 321 LGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLVSQRQVMFPVQLNSSIEWLQNTPP 390
Cdd:MTH00077 431 LGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREVLTTELTSTNIEWLHGCPP 500
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-391 1.85e-174

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 496.65  E-value: 1.85e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479   1 LLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFVWSVVI 80
Cdd:MTH00182 113 LLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILI 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479  81 TALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVY************************GS 160
Cdd:MTH00182 193 TAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGY 272

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 161 LGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYSPATLWALGFVFLFTV 240
Cdd:MTH00182 273 LGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTL 352

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 241 GGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFTIMFMGVNLTFFPQHF 320
Cdd:MTH00182 353 GGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWLMFIGVNLTFFPQHF 432

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 696110479 321 LGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLVSQRQVMFPVQLN----SSIEWLQNTPPA 391
Cdd:MTH00182 433 LGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKFIGWKEGTgeswASLEWVHSSPPL 507
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-390 5.66e-174

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 494.97  E-value: 5.66e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479   1 LLLVSSMVENGAGTGWTVYPPLSSnIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFVWSVVI 80
Cdd:MTH00079 112 LILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFV 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479  81 TALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVY************************GS 160
Cdd:MTH00079 191 TVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGS 270

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 161 LGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYSPATLWALGFVFLFTV 240
Cdd:MTH00079 271 LGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTI 350

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 241 GGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFTIMFMGVNLTFFPQHF 320
Cdd:MTH00079 351 GGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFVGVNLTFFPLHF 430

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 321 LGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLVSQRQVMFPVQLNSSIEWLQNTPP 390
Cdd:MTH00079 431 AGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLHDNYINSSPEYSLSSYV 500
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-391 1.50e-169

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 483.94  E-value: 1.50e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479   1 LLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFVWSVVI 80
Cdd:MTH00184 113 LLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILV 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479  81 TALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVY************************GS 160
Cdd:MTH00184 193 TTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGY 272

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 161 LGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYSPATLWALGFVFLFTV 240
Cdd:MTH00184 273 LGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTM 352

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 241 GGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFTIMFMGVNLTFFPQHF 320
Cdd:MTH00184 353 GGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMFIGVNLTFFPQHF 432

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 696110479 321 LGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLVSQRQV---MFPVQLNSSIEWLQNTPPA 391
Cdd:MTH00184 433 LGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVREIKFvgwVEDSGHYPSLEWAQTSPPA 506
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-366 2.47e-151

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: 435.42  E-value: 2.47e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479   1 LLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFVWSVVI 80
Cdd:cd00919   99 LLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLV 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479  81 TALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVY************************GS 160
Cdd:cd00919  179 TAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGKPLF-GY 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 161 LGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYSPATLWALGFVFLFTV 240
Cdd:cd00919  258 KLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTI 337

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 241 GGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFTIMFMGVNLTFFPQHF 320
Cdd:cd00919  338 GGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGFNLTFFPMHF 417

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 696110479 321 LGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESL 366
Cdd:cd00919  418 LGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-365 1.04e-143

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 419.03  E-value: 1.04e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479   1 LLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFVWSVVI 80
Cdd:MTH00026 112 LLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFI 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479  81 TALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVY************************GS 160
Cdd:MTH00026 192 TAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGY 271

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 161 LGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLN--YSPATLWALGFVFLF 238
Cdd:MTH00026 272 LGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSGRNliFTTPMAWALGFIFLF 351

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 239 TVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFTIMFMGVNLTFFPQ 318
Cdd:MTH00026 352 TIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLMFIGVNITFFPQ 431

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 696110479 319 HFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWES 365
Cdd:MTH00026 432 HFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDA 478
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-390 3.90e-139

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: 405.84  E-value: 3.90e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479    1 LLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFVWSVVI 80
Cdd:TIGR02891 104 LLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILV 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479   81 TALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVY************************GS 160
Cdd:TIGR02891 184 TSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKPIF-GY 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479  161 LGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYSPATLWALGFVFLFTV 240
Cdd:TIGR02891 263 RAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVI 342

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479  241 GGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFTIMFMGVNLTFFPQHF 320
Cdd:TIGR02891 343 GGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHL 422

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 696110479  321 LGLAGMPRRYSDYPDA--YTAWNVISTIGSTISLLGILFFFFIIWESLVSQRQVMFPVQLNSSIEWLQNTPP 390
Cdd:TIGR02891 423 LGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGANPWGATTLEWTTSSPP 494
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-390 7.43e-138

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 403.74  E-value: 7.43e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479   1 LLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFVWSVVI 80
Cdd:COG0843  113 LLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALV 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479  81 TALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVY************************GS 160
Cdd:COG0843  193 TSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKPLF-GY 271

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 161 LGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYSPATLWALGFVFLFTV 240
Cdd:COG0843  272 KAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVI 351

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 241 GGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFTIMFMGVNLTFFPQHF 320
Cdd:COG0843  352 GGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHI 431

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 696110479 321 LGLAGMPRRYSDYP--DAYTAWNVISTIGSTISLLGILFFFFIIWESLVSQRQV-MFPVQLNsSIEWLQNTPP 390
Cdd:COG0843  432 LGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPKAgGNPWGAR-TLEWATPSPP 503
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 11-373 7.25e-127

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 375.17  E-value: 7.25e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479  11 GAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFdRMPLFVWSVVITALLLLLSLP 90
Cdd:MTH00048 120 GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLP 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479  91 VLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVY************************GSLGMIYAMLAI 170
Cdd:MTH00048 199 VLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSI 278

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 171 GLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYS-PATLWALGFVFLFTVGGLTGVVLA 249
Cdd:MTH00048 279 VCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSdPVVWWVVSFIVLFTIGGVTGIVLS 358

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 250 NSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFTIMFMGVNLTFFPQHFLGLAGMPRR 329
Cdd:MTH00048 359 ASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRR 438

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 696110479 330 YSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLVSQRQVM 373
Cdd:MTH00048 439 VCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEVL 482
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-390 4.75e-121

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: 359.59  E-value: 4.75e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479   1 LLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFVWSVVI 80
Cdd:cd01662  105 LLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLV 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479  81 TALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVY************************GS 160
Cdd:cd01662  185 TSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRKPLF-GY 263

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 161 LGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYSPATLWALGFVFLFTV 240
Cdd:cd01662  264 RSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVI 343

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 241 GGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFTIMFMGVNLTFFPQHF 320
Cdd:cd01662  344 GGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFNLTFFPMHI 423

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 696110479 321 LGLAGMPRRYSDYP--DAYTAWNVISTIGSTISLLGILFFffiIWESLVSQRQVMFPVQLN----SSIEWLQNTPP 390
Cdd:cd01662  424 LGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLF---LINVIVSIRKGKRDATGDpwgaRTLEWATSSPP 496
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-350 1.01e-85

Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key enzyme in aerobic metabolism. Proton pumping haem-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-haem a3 (or haem o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxidases (E.C:1.10.3.11), is directly involved in the coupling between dioxygen reduction and proton pumping. Some terminal oxidases generate a transmembrane proton gradient across the plasma membrane (prokaryotes) or the mitochondrial inner membrane (eukaryotes). The enzyme complex consists of 3-4 subunits (prokaryotes) up to 13 polypeptides (mammals) of which only the catalytic subunit (equivalent to mammalian subunit I (COXI) is found in all haem-copper respiratory oxidases. The presence of a bimetallic centre (formed by a high-spin haem and copper B) as well as a low-spin haem, both ligated to six conserved histidine residues near the outer side of four transmembrane spans within CO I is common to all family members.


Pssm-ID: 459678  Cd Length: 432  Bit Score: 266.75  E-value: 1.01e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479    1 LLLVSSMveNGAGTGWTVYPPLssniahggASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFdRMPLFVWSVVI 80
Cdd:pfam00115  96 VLLLASF--GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILA 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479   81 TALLLLLSLPVLAGAITMLLTDRNINtsffdpAGGGDPILYQHLFWFFGHPEVY************************GS 160
Cdd:pfam00115 165 TAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRPLF-GY 237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479  161 LGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLN-YSPATLWALGFVFLFT 239
Cdd:pfam00115 238 KLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRfRTTPMLFFLGFAFLFI 317

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479  240 VGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFTIMFMGVNLTFFPQH 319
Cdd:pfam00115 318 IGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMH 397

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 696110479  320 FLGLAGMPRRYS----DYPDAYTAWNVISTIGSTI 350
Cdd:pfam00115 398 ILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-390 6.42e-75

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: 244.76  E-value: 6.42e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479    1 LLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFVWSVVI 80
Cdd:TIGR02882 148 LFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLI 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479   81 TALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVY************************GS 160
Cdd:TIGR02882 228 TTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIISTFAQKRLF-GY 306

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479  161 LGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYSPATLWALGFVFLFTV 240
Cdd:TIGR02882 307 KSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFLI 386

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479  241 GGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFTIMFMGVNLTFFPQHF 320
Cdd:TIGR02882 387 GGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLNERLGKWCFWFFMIGFNVCFFPMYI 466

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 696110479  321 LGLAGMPRRYSDY--PDAYTAWNVISTIGSTISLLGILFFFF-IIWESLVSQRQVMFPVQLNSSIEWLQNTPP 390
Cdd:TIGR02882 467 LGLDGMPRRMYTYspSDGWFPLNLISTIGALLMAIGFIFLVYnIYYSHRKSPREATGDPWNGRTLEWATASPP 539
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-390 3.97e-70

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 232.52  E-value: 3.97e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479   1 LLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFVWSVVI 80
Cdd:PRK15017 155 LVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLC 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479  81 TALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVY************************GS 160
Cdd:PRK15017 235 ANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLF-GY 313

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 161 LGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYSPATLWALGFVFLFTV 240
Cdd:PRK15017 314 TSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSV 393

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 241 GGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFTIMFMGVNLTFFPQHF 320
Cdd:PRK15017 394 GGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYA 473

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 696110479 321 LGLAGMPRRYSDYPD-AYTAWNVISTIGSTISLLGILFFFFIIWESLVSQ---RQVMFPVQLNSSIEWLQNTPP 390
Cdd:PRK15017 474 LGFMGMTRRLSQQIDpQFHTMLMIAASGAALIALGILCQVIQMYVSIRDRdqnRDLTGDPWGGRTLEWATSSPP 547
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 117-367 1.74e-13

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: 71.55  E-value: 1.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 117 DPILYQHLFWFFGHPEVY************************GSLGMIyAMLAIGLLGFIVWAHHMFT-VGMDVDTRAYF 195
Cdd:cd01660  200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARL-AFILFLLFSTPVGFHHQFAdPGIGPGWKFIH 278

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 196 TSATMIIAVPTGIKIFSWLAT------------LYG--TQLNYSPATLWALGFVFL-FTVGGLTGVVLANSSIDIILHDT 260
Cdd:cd01660  279 MVLTFMVALPSLLTAFTVFASleiagrlrggkgLFGwiRALPWGDPMFLALFLAMLmFIPGGAGGIINASYQLNYVVHNT 358

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 696110479 261 YYVVAHFHyvLSMGAVFAIMA-GFVHWY-PLFTGLTMNTKMLKS-QFTIMFMGVNLTFFPQHFLGLAGMPRR--YSDYPD 335
Cdd:cd01660  359 AWVPGHFH--LTVGGAVALTFmAVAYWLvPHLTGRELAAKRLALaQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGG 436

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 696110479 336 AY-----TAWNVISTIGSTISLLGILFFFFIIWESLV 367
Cdd:cd01660  437 LPaagewAPYQQLMAIGGTILFVSGALFLYILFRTLL 473
 
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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