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Conserved domains on  [gi|1033936138|gb|ANI23151|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Rhaphiomidas sp. 1 MHVD-2016]

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 ...
 1-267 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: 560.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138   1 ILPGFGMISHIISQESGKKETFGALGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 80
Cdd:MTH00153  245 ILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 324

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138  81 LHGTQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGFVHWYPLFTGLTMN 160
Cdd:MTH00153  325 LHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMN 404

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138 161 PKWLKSQFMIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSTISLIGILFFIFIMWESMVMHRQVITPI 240
Cdd:MTH00153  405 PKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSL 484

                         250       260
                  ....*....|....*....|....*..
gi 1033936138 241 QLNSSIEWYQNIPPAEHSYS*LPLLTN 267
Cdd:MTH00153  485 NLSSSIEWLQNLPPAEHSYSELPLLTN 511
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-267 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 560.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138   1 ILPGFGMISHIISQESGKKETFGALGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 80
Cdd:MTH00153  245 ILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 324

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138  81 LHGTQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGFVHWYPLFTGLTMN 160
Cdd:MTH00153  325 LHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMN 404

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138 161 PKWLKSQFMIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSTISLIGILFFIFIMWESMVMHRQVITPI 240
Cdd:MTH00153  405 PKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSL 484

                         250       260
                  ....*....|....*....|....*..
gi 1033936138 241 QLNSSIEWYQNIPPAEHSYS*LPLLTN 267
Cdd:MTH00153  485 NLSSSIEWLQNLPPAEHSYSELPLLTN 511
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-248 1.71e-159

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: 451.94  E-value: 1.71e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138   1 ILPGFGMISHIISQESGKKETFGALGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 80
Cdd:cd01663   238 ILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLAT 317

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138  81 LHGTQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGFVHWYPLFTGLTMN 160
Cdd:cd01663   318 MWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYN 397

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138 161 PKWLKSQFMIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSTISLIGILFFIFIMWESMVMHRQVITPI 240
Cdd:cd01663   398 ETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNV 477


                  ....*....
gi 1033936138 241 -QLNSSIEW 248
Cdd:cd01663   478 gEGSTSLEW 486
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-266 5.57e-96

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 291.65  E-value: 5.57e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138   1 ILPGFGMISHIISQESGKKeTFGALGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 80
Cdd:COG0843   249 ILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIAT 327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138  81 LHGTQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGFVHWYPLFTGLTMN 160
Cdd:COG0843   328 MWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLN 407

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138 161 PKWLKSQFMIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTTWNVVSTIGSTISLIGILFFIFIMWESMvMHRQVIT 238
Cdd:COG0843   408 ERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSL-RKGPKAG 486

                         250       260
                  ....*....|....*....|....*....
gi 1033936138 239 PIQLNS-SIEWYQNIPPAEHSYS*LPLLT 266
Cdd:COG0843   487 GNPWGArTLEWATPSPPPLYNFASIPVVR 515
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-259 1.75e-92

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: 281.42  E-value: 1.75e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138   1 ILPGFGMISHIISQESGKKeTFGALGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 80
Cdd:TIGR02891 240 FLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138  81 LHGTQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGFVHWYPLFTGLTMN 160
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138 161 PKWLKSQFMIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTTWNVVSTIGSTISLIGILFFIFIMWESMVMHRQVIT 238
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGA 478

                         250       260
                  ....*....|....*....|.
gi 1033936138 239 PIQLNSSIEWYQNIPPAEHSY 259
Cdd:TIGR02891 479 NPWGATTLEWTTSSPPPAHNF 499
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-214 1.71e-64

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: 207.43  E-value: 1.71e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138   1 ILPGFGMISHIISQESGKKeTFGALGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 80
Cdd:pfam00115 215 ILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLAT 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138  81 LHGTQLN-YSPSLLWALGFVFLFTVGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGFVHWYPLFTGLTM 159
Cdd:pfam00115 294 LWGGWIRfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMY 373

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1033936138 160 NPKWLKSQFMIMFIGVNLTFFPQHFLGLAGMPRRYS----DYPDAYTTWNVVSTIGSTI 214
Cdd:pfam00115 374 SEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-267 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 560.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138   1 ILPGFGMISHIISQESGKKETFGALGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 80
Cdd:MTH00153  245 ILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 324

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138  81 LHGTQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGFVHWYPLFTGLTMN 160
Cdd:MTH00153  325 LHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMN 404

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138 161 PKWLKSQFMIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSTISLIGILFFIFIMWESMVMHRQVITPI 240
Cdd:MTH00153  405 PKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSL 484

                         250       260
                  ....*....|....*....|....*..
gi 1033936138 241 QLNSSIEWYQNIPPAEHSYS*LPLLTN 267
Cdd:MTH00153  485 NLSSSIEWLQNLPPAEHSYSELPLLTN 511
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-248 1.71e-159

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: 451.94  E-value: 1.71e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138   1 ILPGFGMISHIISQESGKKETFGALGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 80
Cdd:cd01663   238 ILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLAT 317

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138  81 LHGTQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGFVHWYPLFTGLTMN 160
Cdd:cd01663   318 MWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYN 397

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138 161 PKWLKSQFMIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSTISLIGILFFIFIMWESMVMHRQVITPI 240
Cdd:cd01663   398 ETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNV 477


                  ....*....
gi 1033936138 241 -QLNSSIEW 248
Cdd:cd01663   478 gEGSTSLEW 486
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-267 8.97e-155

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 441.08  E-value: 8.97e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138   1 ILPGFGMISHIISQESGKKETFGALGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 80
Cdd:MTH00142  245 ILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLAT 324

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138  81 LHGTQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGFVHWYPLFTGLTMN 160
Cdd:MTH00142  325 LHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLN 404

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138 161 PKWLKSQFMIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSTISLIGILFFIFIMWESMVMHRQVITPI 240
Cdd:MTH00142  405 PRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVMWSS 484

                         250       260
                  ....*....|....*....|....*..
gi 1033936138 241 QLNSSIEWYQNIPPAEHSYS*LPLLTN 267
Cdd:MTH00142  485 HLSTSLEWSHRLPPDFHTYDELPILVV 511
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-263 3.05e-154

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 439.41  E-value: 3.05e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138   1 ILPGFGMISHIISQESGKKETFGALGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 80
Cdd:MTH00223  244 ILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLAT 323

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138  81 LHGTQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGFVHWYPLFTGLTMN 160
Cdd:MTH00223  324 IYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLH 403

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138 161 PKWLKSQFMIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSTISLIGILFFIFIMWESMVMHRQVITPI 240
Cdd:MTH00223  404 RRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVWSG 483

                         250       260
                  ....*....|....*....|...
gi 1033936138 241 QLNSSIEWYQNIPPAEHSYS*LP 263
Cdd:MTH00223  484 HLSTSLEWDNLLPADFHNNSETG 506
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-267 1.09e-153

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 438.37  E-value: 1.09e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138   1 ILPGFGMISHIISQESGKKETFGALGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 80
Cdd:MTH00116  247 ILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLAT 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138  81 LHGTQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGFVHWYPLFTGLTMN 160
Cdd:MTH00116  327 LHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLH 406

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138 161 PKWLKSQFMIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSTISLIGILFFIFIMWESMVMHRQVITPI 240
Cdd:MTH00116  407 QTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVLQPE 486

                         250       260
                  ....*....|....*....|....*..
gi 1033936138 241 QLNSSIEWYQNIPPAEHSYS*LPLLTN 267
Cdd:MTH00116  487 LTTTNIEWIHGCPPPYHTFEEPAFVQV 513
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-265 1.88e-152

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 434.87  E-value: 1.88e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138   1 ILPGFGMISHIISQESGKKETFGALGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 80
Cdd:MTH00167  247 ILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLAT 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138  81 LHGTQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGFVHWYPLFTGLTMN 160
Cdd:MTH00167  327 LHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLN 406

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138 161 PKWLKSQFMIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSTISLIGILFFIFIMWESMVMHRQVITPI 240
Cdd:MTH00167  407 ETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLLPVE 486

                         250       260
                  ....*....|....*....|....*
gi 1033936138 241 QLNSSIEWYQNIPPAEHSYS*LPLL 265
Cdd:MTH00167  487 LTSTNVEWLHGCPPPHHTWEEPPFV 511
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-264 1.76e-136

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 394.58  E-value: 1.76e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138   1 ILPGFGMISHIISQESGKKETFGALGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 80
Cdd:MTH00037  247 ILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMAT 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138  81 LHGTQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGFVHWYPLFTGLTMN 160
Cdd:MTH00037  327 LQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLH 406

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138 161 PKWLKSQFMIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSTISLIGILFFIFIMWESMVMHRQVITPI 240
Cdd:MTH00037  407 PLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVISPE 486

                         250       260
                  ....*....|....*....|....*
gi 1033936138 241 QLNSSIEW-YQNIPPAEHSYS*LPL 264
Cdd:MTH00037  487 FSSSSLEWqYSSFPPSHHTFDETPS 511
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-259 2.94e-134

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 388.86  E-value: 2.94e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138   1 ILPGFGMISHIISQESGKKETFGALGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 80
Cdd:MTH00103  247 ILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLAT 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138  81 LHGTQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGFVHWYPLFTGLTMN 160
Cdd:MTH00103  327 LHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLN 406

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138 161 PKWLKSQFMIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSTISLIGILFFIFIMWESMVMHRQVITPI 240
Cdd:MTH00103  407 DTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVLTVE 486

                         250
                  ....*....|....*....
gi 1033936138 241 QLNSSIEWYQNIPPAEHSY 259
Cdd:MTH00103  487 LTTTNLEWLHGCPPPYHTF 505
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-259 2.14e-132

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 384.27  E-value: 2.14e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138   1 ILPGFGMISHIISQESGKKETFGALGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 80
Cdd:MTH00183  247 ILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLAT 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138  81 LHGTQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGFVHWYPLFTGLTMN 160
Cdd:MTH00183  327 LHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLH 406

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138 161 PKWLKSQFMIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSTISLIGILFFIFIMWESMVMHRQVITPI 240
Cdd:MTH00183  407 STWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLSVE 486

                         250
                  ....*....|....*....
gi 1033936138 241 QLNSSIEWYQNIPPAEHSY 259
Cdd:MTH00183  487 LTSTNVEWLHGCPPPYHTF 505
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-266 8.39e-131

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 380.02  E-value: 8.39e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138   1 ILPGFGMISHIISQESGKKETFGALGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 80
Cdd:MTH00007  244 ILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLAT 323

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138  81 LHGTQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGFVHWYPLFTGLTMN 160
Cdd:MTH00007  324 IHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLH 403

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138 161 PKWLKSQFMIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSTISLIGILFFIFIMWESMVMHRQVITPI 240
Cdd:MTH00007  404 DRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIASP 483

                         250       260
                  ....*....|....*....|....*.
gi 1033936138 241 QLNSSIEWYQNIPPAEHSYS*LPLLT 266
Cdd:MTH00007  484 HMSSSLEWQDTLPLDFHNLPETGIIT 509
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-259 1.29e-129

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 376.97  E-value: 1.29e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138   1 ILPGFGMISHIISQESGKKETFGALGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 80
Cdd:MTH00077  247 ILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLAT 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138  81 LHGTQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGFVHWYPLFTGLTMN 160
Cdd:MTH00077  327 MHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLH 406

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138 161 PKWLKSQFMIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSTISLIGILFFIFIMWESMVMHRQVITPI 240
Cdd:MTH00077  407 STWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREVLTTE 486

                         250
                  ....*....|....*....
gi 1033936138 241 QLNSSIEWYQNIPPAEHSY 259
Cdd:MTH00077  487 LTSTNIEWLHGCPPPYHTF 505
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-265 3.27e-117

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 345.65  E-value: 3.27e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138   1 ILPGFGMISHIISQESGKKETFGALGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 80
Cdd:MTH00182  249 ILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLAT 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138  81 LHGTQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGFVHWYPLFTGLTMN 160
Cdd:MTH00182  329 IYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYN 408

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138 161 PKWLKSQFMIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSTISLIGILFFIFIMWESMVMHRQVITPI 240
Cdd:MTH00182  409 ELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKFIGWK 488

                         250       260
                  ....*....|....*....|....*....
gi 1033936138 241 QLN----SSIEWYQNIPPAEHSYS*LPLL 265
Cdd:MTH00182  489 EGTgeswASLEWVHSSPPLFHTYNELPFV 517
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-259 7.58e-117

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 344.36  E-value: 7.58e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138   1 ILPGFGMISHIISQESGKKETFGALGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 80
Cdd:MTH00079  247 ILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLAT 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138  81 LHGTQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGFVHWYPLFTGLTMN 160
Cdd:MTH00079  327 LFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYD 406

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138 161 PKWLKSQFMIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSTISLIGILFFIFIMWESMVMHRQVITPI 240
Cdd:MTH00079  407 KLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLHDN 486

                         250
                  ....*....|....*....
gi 1033936138 241 QLNSSIEWYQNIPPAEHSY 259
Cdd:MTH00079  487 YINSSPEYSLSSYVFGHSY 505
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-265 4.99e-111

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 329.87  E-value: 4.99e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138   1 ILPGFGMISHIISQESGKKETFGALGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 80
Cdd:MTH00184  249 ILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIAT 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138  81 LHGTQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGFVHWYPLFTGLTMN 160
Cdd:MTH00184  329 IFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYN 408

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138 161 PKWLKSQFMIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSTISLIGILFFIFIMWESMVMHRQVITPI 240
Cdd:MTH00184  409 EVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVREIKFVGWV 488

                         250       260
                  ....*....|....*....|....*...
gi 1033936138 241 Q---LNSSIEWYQNIPPAEHSYS*LPLL 265
Cdd:MTH00184  489 EdsgHYPSLEWAQTSPPAHHTYNELPYV 516
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-230 8.58e-104

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: 309.46  E-value: 8.58e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138   1 ILPGFGMISHIISQESGKKeTFGALGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 80
Cdd:cd00919   235 ILPAFGAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLAT 313

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138  81 LHGTQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGFVHWYPLFTGLTMN 160
Cdd:cd00919   314 LWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLS 393

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138 161 PKWLKSQFMIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSTISLIGILFFIFIMWESM 230
Cdd:cd00919   394 EKLGKIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-266 5.57e-96

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 291.65  E-value: 5.57e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138   1 ILPGFGMISHIISQESGKKeTFGALGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 80
Cdd:COG0843   249 ILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIAT 327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138  81 LHGTQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGFVHWYPLFTGLTMN 160
Cdd:COG0843   328 MWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLN 407

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138 161 PKWLKSQFMIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTTWNVVSTIGSTISLIGILFFIFIMWESMvMHRQVIT 238
Cdd:COG0843   408 ERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSL-RKGPKAG 486

                         250       260
                  ....*....|....*....|....*....
gi 1033936138 239 PIQLNS-SIEWYQNIPPAEHSYS*LPLLT 266
Cdd:COG0843   487 GNPWGArTLEWATPSPPPLYNFASIPVVR 515
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-259 1.75e-92

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: 281.42  E-value: 1.75e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138   1 ILPGFGMISHIISQESGKKeTFGALGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 80
Cdd:TIGR02891 240 FLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138  81 LHGTQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGFVHWYPLFTGLTMN 160
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138 161 PKWLKSQFMIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTTWNVVSTIGSTISLIGILFFIFIMWESMVMHRQVIT 238
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGA 478

                         250       260
                  ....*....|....*....|.
gi 1033936138 239 PIQLNSSIEWYQNIPPAEHSY 259
Cdd:TIGR02891 479 NPWGATTLEWTTSSPPPAHNF 499
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-265 7.08e-92

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 281.13  E-value: 7.08e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138   1 ILPGFGMISHIISQESGKKETFGALGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 80
Cdd:MTH00026  248 ILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLAT 327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138  81 LHGTQLN--YSPSLLWALGFVFLFTVGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGFVHWYPLFTGLT 158
Cdd:MTH00026  328 VSGSGRNliFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYA 407

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138 159 MNPKWLKSQFMIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSTISLIGILFFIFIMWESM-------- 230
Cdd:MTH00026  408 YKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAYyreepfdi 487

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1033936138 231 -VMHRQVITPIQLN----SSIEWYQNIPPAEHSYS*LPLL 265
Cdd:MTH00026  488 nIMAKGPLIPFSCQpahfDTLEWSLTSPPEHHTYNELPYI 527
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-258 7.29e-87

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 267.70  E-value: 7.29e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138   1 ILPGFGMISHIISQESGKKETFGALGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 80
Cdd:MTH00048  245 ILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYM 324

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138  81 LHGTQLNYS-PSLLWALGFVFLFTVGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGFVHWYPLFTGLTM 159
Cdd:MTH00048  325 LLNSRVRKSdPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSL 404

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138 160 NPKWLKSQFMIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSTIGSTISLIGILFFIFIMWESMVMHRQVITP 239
Cdd:MTH00048  405 NKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEVLGL 484

                         250
                  ....*....|....*....
gi 1033936138 240 IQLNSSIEWYQNIPPAEHS 258
Cdd:MTH00048  485 WGSSSCVVNVLMSPVPYHN 503
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-259 7.32e-84

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: 259.44  E-value: 7.32e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138   1 ILPGFGMISHIISQESGKKeTFGALGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 80
Cdd:cd01662   241 ILPAFGIFSEIVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFT 319

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138  81 LHGTQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGFVHWYPLFTGLTMN 160
Cdd:cd01662   320 MWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLN 399

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138 161 PKWLKSQFMIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTTWNVVSTIGSTISLIGILFFIFIMWESMVMHRQVIT 238
Cdd:cd01662   400 ERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLINVIVSIRKGKRDAT 479

                         250       260
                  ....*....|....*....|..
gi 1033936138 239 PIQLN-SSIEWYQNIPPAEHSY 259
Cdd:cd01662   480 GDPWGaRTLEWATSSPPPAYNF 501
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-214 1.71e-64

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: 207.43  E-value: 1.71e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138   1 ILPGFGMISHIISQESGKKeTFGALGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 80
Cdd:pfam00115 215 ILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLAT 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138  81 LHGTQLN-YSPSLLWALGFVFLFTVGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGFVHWYPLFTGLTM 159
Cdd:pfam00115 294 LWGGWIRfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMY 373

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1033936138 160 NPKWLKSQFMIMFIGVNLTFFPQHFLGLAGMPRRYS----DYPDAYTTWNVVSTIGSTI 214
Cdd:pfam00115 374 SEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-263 1.28e-54

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: 186.21  E-value: 1.28e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138   1 ILPGFGMISHIISQESgKKETFGALGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 80
Cdd:TIGR02882 284 ILPAFGIYSEIISTFA-QKRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLT 362

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138  81 LHGTQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGFVHWYPLFTGLTMN 160
Cdd:TIGR02882 363 LYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLN 442

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138 161 PKWLKSQFMIMFIGVNLTFFPQHFLGLAGMPRRYSDY--PDAYTTWNVVSTIGSTISLIGILFFIFIMWESMVMHRQVIT 238
Cdd:TIGR02882 443 ERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYspSDGWFPLNLISTIGALLMAIGFIFLVYNIYYSHRKSPREAT 522

                         250       260
                  ....*....|....*....|....*.
gi 1033936138 239 PIQLNS-SIEWYQNIPPAEHSYS*LP 263
Cdd:TIGR02882 523 GDPWNGrTLEWATASPPPKYNFAVTP 548
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-263 1.73e-50

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 175.51  E-value: 1.73e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138   1 ILPGFGMISHIISQESgKKETFGALGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT 80
Cdd:PRK15017  291 ILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFT 369

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138  81 LHGTQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGFVHWYPLFTGLTMN 160
Cdd:PRK15017  370 MYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLN 449

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138 161 PKWLKSQFMIMFIGVNLTFFPQHFLGLAGMPRRYSDYPD-AYTTWNVVSTIGSTISLIGILFFIFIMWESMV---MHRQV 236
Cdd:PRK15017  450 ETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDpQFHTMLMIAASGAALIALGILCQVIQMYVSIRdrdQNRDL 529

                         250       260
                  ....*....|....*....|....*..
gi 1033936138 237 ITPIQLNSSIEWYQNIPPAEHSYS*LP 263
Cdd:PRK15017  530 TGDPWGGRTLEWATSSPPPFYNFAVVP 556
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 63-231 5.35e-14

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: 71.16  E-value: 5.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138  63 TMIIAVPTGIKIFSWLATL-HGTQLNYSPSLLW---------------ALGFVFlFTVGGLTGVVLANSSLDIILHDTYY 126
Cdd:cd01660   282 TFMVALPSLLTAFTVFASLeIAGRLRGGKGLFGwiralpwgdpmflalFLAMLM-FIPGGAGGIINASYQLNYVVHNTAW 360

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1033936138 127 VVAHFHYVLSMGAVFAIMGGFVHWYPLFTGLTMNPKWLKS-QFMIMFIGVNLTFFPQHFLGLAGMPRR--YSDYPDAY-- 201
Cdd:cd01660   361 VPGHFHLTVGGAVALTFMAVAYWLVPHLTGRELAAKRLALaQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGGLPaa 440

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1033936138 202 ---TTWNVVSTIGSTISLIGILFFIFIMWESMV 231
Cdd:cd01660   441 gewAPYQQLMAIGGTILFVSGALFLYILFRTLL 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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