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Conserved domains on  [gi|992008190|gb|AMH39975|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Aglaothorax ovata armiger]

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 ...
 1-266 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: 550.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190   1 ILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAMGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:MTH00153 243 ILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190  81 ATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLT 160
Cdd:MTH00153 323 ATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLT 402

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190 161 LNPKWLKIQFVTMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVVSSLGSTISFIGIILLIFIIWESMISNRTVLF 240
Cdd:MTH00153 403 MNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLF 482

                        250       260
                 ....*....|....*....|....*.
gi 992008190 241 PLSMVSSLEWYQNLPPAEHSYSELPM 266
Cdd:MTH00153 483 SLNLSSSIEWLQNLPPAEHSYSELPL 508
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-266 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 550.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190   1 ILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAMGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:MTH00153 243 ILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190  81 ATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLT 160
Cdd:MTH00153 323 ATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLT 402

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190 161 LNPKWLKIQFVTMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVVSSLGSTISFIGIILLIFIIWESMISNRTVLF 240
Cdd:MTH00153 403 MNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLF 482

                        250       260
                 ....*....|....*....|....*.
gi 992008190 241 PLSMVSSLEWYQNLPPAEHSYSELPM 266
Cdd:MTH00153 483 SLNLSSSIEWLQNLPPAEHSYSELPL 508
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-250 4.79e-155

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: 440.77  E-value: 4.79e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190   1 ILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAMGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:cd01663  236 ILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWL 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190  81 ATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLT 160
Cdd:cd01663  316 ATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLS 395

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190 161 LNPKWLKIQFVTMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVVSSLGSTISFIGIILLIFIIWESMISNRTVLF 240
Cdd:cd01663  396 YNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIF 475

                        250
                 ....*....|.
gi 992008190 241 -PLSMVSSLEW 250
Cdd:cd01663  476 nVGEGSTSLEW 486
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-265 2.03e-91

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 279.70  E-value: 2.03e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190   1 ILILPGFGMISHIISQESGKKeAFGTLGMIYAMLAMGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:COG0843  247 ILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWI 325

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190  81 ATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLT 160
Cdd:COG0843  326 ATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRM 405

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190 161 LNPKWLKIQFVTMFVGVNLTFFPQHFLGLAGMPRRYSDYP--DSYTSWNVVSSLGSTISFIGIILLIFIIWESMISNRTV 238
Cdd:COG0843  406 LNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPKA 485

                        250       260
                 ....*....|....*....|....*...
gi 992008190 239 L-FPLSmVSSLEWYQNLPPAEHSYSELP 265
Cdd:COG0843  486 GgNPWG-ARTLEWATPSPPPLYNFASIP 512
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-261 1.07e-89

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: 274.49  E-value: 1.07e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190    1 ILILPGFGMISHIISQESGKKeAFGTLGMIYAMLAMGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:TIGR02891 238 IIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWI 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190   81 ATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLT 160
Cdd:TIGR02891 317 ATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRM 396

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190  161 LNPKWLKIQFVTMFVGVNLTFFPQHFLGLAGMPRRYSDYPDS--YTSWNVVSSLGSTISFIGIILLIFIIWESMISNRTV 238
Cdd:TIGR02891 397 YNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKA 476

                         250       260
                  ....*....|....*....|...
gi 992008190  239 LFPLSMVSSLEWYQNLPPAEHSY 261
Cdd:TIGR02891 477 GANPWGATTLEWTTSSPPPAHNF 499
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-216 3.22e-67

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: 214.36  E-value: 3.22e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190    1 ILILPGFGMISHIISQESGKKeAFGTLGMIYAMLAMGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:pfam00115 213 ILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWL 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190   81 ATLHGTQLN-YSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGL 159
Cdd:pfam00115 292 ATLWGGWIRfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGR 371

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992008190  160 TLNPKWLKIQFVTMFVGVNLTFFPQHFLGLAGMPRRYS----DYPDSYTSWNVVSSLGSTI 216
Cdd:pfam00115 372 MYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-266 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 550.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190   1 ILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAMGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:MTH00153 243 ILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190  81 ATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLT 160
Cdd:MTH00153 323 ATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLT 402

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190 161 LNPKWLKIQFVTMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVVSSLGSTISFIGIILLIFIIWESMISNRTVLF 240
Cdd:MTH00153 403 MNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLF 482

                        250       260
                 ....*....|....*....|....*.
gi 992008190 241 PLSMVSSLEWYQNLPPAEHSYSELPM 266
Cdd:MTH00153 483 SLNLSSSIEWLQNLPPAEHSYSELPL 508
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-250 4.79e-155

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: 440.77  E-value: 4.79e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190   1 ILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAMGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:cd01663  236 ILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWL 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190  81 ATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLT 160
Cdd:cd01663  316 ATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLS 395

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190 161 LNPKWLKIQFVTMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVVSSLGSTISFIGIILLIFIIWESMISNRTVLF 240
Cdd:cd01663  396 YNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIF 475

                        250
                 ....*....|.
gi 992008190 241 -PLSMVSSLEW 250
Cdd:cd01663  476 nVGEGSTSLEW 486
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-266 6.03e-154

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 438.77  E-value: 6.03e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190   1 ILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAMGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:MTH00142 243 ILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWL 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190  81 ATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLT 160
Cdd:MTH00142 323 ATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLT 402

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190 161 LNPKWLKIQFVTMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVVSSLGSTISFIGIILLIFIIWESMISNRTVLF 240
Cdd:MTH00142 403 LNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVMW 482

                        250       260
                 ....*....|....*....|....*.
gi 992008190 241 PLSMVSSLEWYQNLPPAEHSYSELPM 266
Cdd:MTH00142 483 SSHLSTSLEWSHRLPPDFHTYDELPI 508
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-265 1.07e-150

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 430.55  E-value: 1.07e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190   1 ILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAMGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:MTH00223 242 ILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190  81 ATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLT 160
Cdd:MTH00223 322 ATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVT 401

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190 161 LNPKWLKIQFVTMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVVSSLGSTISFIGIILLIFIIWESMISNRTVLF 240
Cdd:MTH00223 402 LHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVW 481

                        250       260
                 ....*....|....*....|....*
gi 992008190 241 PLSMVSSLEWYQNLPPAEHSYSELP 265
Cdd:MTH00223 482 SGHLSTSLEWDNLLPADFHNNSETG 506
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-266 2.86e-150

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 429.51  E-value: 2.86e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190   1 ILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAMGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:MTH00116 245 ILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWL 324

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190  81 ATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLT 160
Cdd:MTH00116 325 ATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYT 404

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190 161 LNPKWLKIQFVTMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVVSSLGSTISFIGIILLIFIIWESMISNRTVLF 240
Cdd:MTH00116 405 LHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVLQ 484

                        250       260
                 ....*....|....*....|....*.
gi 992008190 241 PLSMVSSLEWYQNLPPAEHSYSELPM 266
Cdd:MTH00116 485 PELTTTNIEWIHGCPPPYHTFEEPAF 510
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-265 2.35e-149

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 427.17  E-value: 2.35e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190   1 ILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAMGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:MTH00167 245 ILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 324

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190  81 ATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLT 160
Cdd:MTH00167 325 ATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLT 404

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190 161 LNPKWLKIQFVTMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVVSSLGSTISFIGIILLIFIIWESMISNRTVLF 240
Cdd:MTH00167 405 LNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLLP 484

                        250       260
                 ....*....|....*....|....*
gi 992008190 241 PLSMVSSLEWYQNLPPAEHSYSELP 265
Cdd:MTH00167 485 VELTSTNVEWLHGCPPPHHTWEEPP 509
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-265 4.45e-133

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 385.72  E-value: 4.45e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190   1 ILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAMGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:MTH00037 245 ILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWM 324

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190  81 ATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLT 160
Cdd:MTH00037 325 ATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVS 404

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190 161 LNPKWLKIQFVTMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVVSSLGSTISFIGIILLIFIIWESMISNRTVLF 240
Cdd:MTH00037 405 LHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVIS 484

                        250       260
                 ....*....|....*....|....*.
gi 992008190 241 PLSMVSSLEW-YQNLPPAEHSYSELP 265
Cdd:MTH00037 485 PEFSSSSLEWqYSSFPPSHHTFDETP 510
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-263 1.01e-131

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 382.31  E-value: 1.01e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190   1 ILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAMGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:MTH00103 245 ILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWL 324

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190  81 ATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLT 160
Cdd:MTH00103 325 ATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYT 404

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190 161 LNPKWLKIQFVTMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVVSSLGSTISFIGIILLIFIIWESMISNRTVLF 240
Cdd:MTH00103 405 LNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVLT 484

                        250       260
                 ....*....|....*....|...
gi 992008190 241 PLSMVSSLEWYQNLPPAEHSYSE 263
Cdd:MTH00103 485 VELTTTNLEWLHGCPPPYHTFEE 507
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-263 2.45e-128

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 373.87  E-value: 2.45e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190   1 ILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAMGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:MTH00183 245 ILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWL 324

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190  81 ATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLT 160
Cdd:MTH00183 325 ATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYT 404

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190 161 LNPKWLKIQFVTMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVVSSLGSTISFIGIILLIFIIWESMISNRTVLF 240
Cdd:MTH00183 405 LHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLS 484

                        250       260
                 ....*....|....*....|...
gi 992008190 241 PLSMVSSLEWYQNLPPAEHSYSE 263
Cdd:MTH00183 485 VELTSTNVEWLHGCPPPYHTFEE 507
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-263 2.16e-127

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 371.16  E-value: 2.16e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190   1 ILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAMGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:MTH00007 242 ILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190  81 ATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLT 160
Cdd:MTH00007 322 ATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLT 401

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190 161 LNPKWLKIQFVTMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVVSSLGSTISFIGIILLIFIIWESMISNRTVLF 240
Cdd:MTH00007 402 LHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIA 481

                        250       260
                 ....*....|....*....|...
gi 992008190 241 PLSMVSSLEWYQNLPPAEHSYSE 263
Cdd:MTH00007 482 SPHMSSSLEWQDTLPLDFHNLPE 504
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-263 3.65e-126

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 368.11  E-value: 3.65e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190   1 ILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAMGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:MTH00077 245 ILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWL 324

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190  81 ATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLT 160
Cdd:MTH00077 325 ATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYT 404

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190 161 LNPKWLKIQFVTMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVVSSLGSTISFIGIILLIFIIWESMISNRTVLF 240
Cdd:MTH00077 405 LHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREVLT 484

                        250       260
                 ....*....|....*....|...
gi 992008190 241 PLSMVSSLEWYQNLPPAEHSYSE 263
Cdd:MTH00077 485 TELTSTNIEWLHGCPPPYHTFEE 507
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-263 4.03e-116

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 342.43  E-value: 4.03e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190   1 ILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAMGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:MTH00079 245 ILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWL 324

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190  81 ATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLT 160
Cdd:MTH00079 325 ATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIV 404

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190 161 LNPKWLKIQFVTMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVVSSLGSTISFIGIILLIFIIWESMISNRTVLF 240
Cdd:MTH00079 405 YDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLH 484

                        250       260
                 ....*....|....*....|...
gi 992008190 241 PLSMVSSLEWYQNLPPAEHSYSE 263
Cdd:MTH00079 485 DNYINSSPEYSLSSYVFGHSYQS 507
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-265 2.94e-113

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 335.64  E-value: 2.94e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190   1 ILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAMGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:MTH00182 247 ILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 326

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190  81 ATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLT 160
Cdd:MTH00182 327 ATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYC 406

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190 161 LNPKWLKIQFVTMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVVSSLGSTISFIGIILLIFIIWESMISNRTVL- 239
Cdd:MTH00182 407 YNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKFIg 486

                        250       260
                 ....*....|....*....|....*....
gi 992008190 240 ---FPLSMVSSLEWYQNLPPAEHSYSELP 265
Cdd:MTH00182 487 wkeGTGESWASLEWVHSSPPLFHTYNELP 515
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-265 4.21e-109

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 324.86  E-value: 4.21e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190   1 ILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAMGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:MTH00184 247 ILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWI 326

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190  81 ATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLT 160
Cdd:MTH00184 327 ATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYC 406

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190 161 LNPKWLKIQFVTMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVVSSLGSTISFIGIILLIFIIWESMIsnRTVLF 240
Cdd:MTH00184 407 YNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYV--REIKF 484

                        250       260       270
                 ....*....|....*....|....*....|
gi 992008190 241 -----PLSMVSSLEWYQNLPPAEHSYSELP 265
Cdd:MTH00184 485 vgwveDSGHYPSLEWAQTSPPAHHTYNELP 514
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-232 1.33e-100

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: 300.99  E-value: 1.33e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190   1 ILILPGFGMISHIISQESGKKeAFGTLGMIYAMLAMGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:cd00919  233 ILILPAFGAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWL 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190  81 ATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLT 160
Cdd:cd00919  312 ATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRM 391

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 992008190 161 LNPKWLKIQFVTMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVVSSLGSTISFIGIILLIFIIWESM 232
Cdd:cd00919  392 LSEKLGKIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-265 2.03e-91

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 279.70  E-value: 2.03e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190   1 ILILPGFGMISHIISQESGKKeAFGTLGMIYAMLAMGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:COG0843  247 ILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWI 325

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190  81 ATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLT 160
Cdd:COG0843  326 ATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRM 405

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190 161 LNPKWLKIQFVTMFVGVNLTFFPQHFLGLAGMPRRYSDYP--DSYTSWNVVSSLGSTISFIGIILLIFIIWESMISNRTV 238
Cdd:COG0843  406 LNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPKA 485

                        250       260
                 ....*....|....*....|....*...
gi 992008190 239 L-FPLSmVSSLEWYQNLPPAEHSYSELP 265
Cdd:COG0843  486 GgNPWG-ARTLEWATPSPPPLYNFASIP 512
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-265 4.78e-91

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 278.82  E-value: 4.78e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190   1 ILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAMGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:MTH00026 246 ILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWL 325

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190  81 ATLHGTQLN--YSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTG 158
Cdd:MTH00026 326 ATVSGSGRNliFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITG 405

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190 159 LTLNPKWLKIQFVTMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVVSSLGSTISFIGIILLIFIIWESM------ 232
Cdd:MTH00026 406 YAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAYyreepf 485

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 992008190 233 ---ISNRTVLFPLSM----VSSLEWYQNLPPAEHSYSELP 265
Cdd:MTH00026 486 dinIMAKGPLIPFSCqpahFDTLEWSLTSPPEHHTYNELP 525
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-261 1.07e-89

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: 274.49  E-value: 1.07e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190    1 ILILPGFGMISHIISQESGKKeAFGTLGMIYAMLAMGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:TIGR02891 238 IIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWI 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190   81 ATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLT 160
Cdd:TIGR02891 317 ATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRM 396

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190  161 LNPKWLKIQFVTMFVGVNLTFFPQHFLGLAGMPRRYSDYPDS--YTSWNVVSSLGSTISFIGIILLIFIIWESMISNRTV 238
Cdd:TIGR02891 397 YNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKA 476

                         250       260
                  ....*....|....*....|...
gi 992008190  239 LFPLSMVSSLEWYQNLPPAEHSY 261
Cdd:TIGR02891 477 GANPWGATTLEWTTSSPPPAHNF 499
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-260 2.97e-84

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 260.77  E-value: 2.97e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190   1 ILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAMGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:MTH00048 243 VLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWL 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190  81 ATLHGTQLNYS-PALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGL 159
Cdd:MTH00048 323 YMLLNSRVRKSdPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGL 402

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190 160 TLNPKWLKIQFVTMFVGVNLTFFPQHFLGLAGMPRRYSDYPDSYTSWNVVSSLGSTISFIGIILLIFIIWESMISNRTVL 239
Cdd:MTH00048 403 SLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEVL 482

                        250       260
                 ....*....|....*....|.
gi 992008190 240 FPLSMVSSLEWYQNLPPAEHS 260
Cdd:MTH00048 483 GLWGSSSCVVNVLMSPVPYHN 503
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-216 1.03e-82

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: 256.35  E-value: 1.03e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190   1 ILILPGFGMISHIISQESGKKeAFGTLGMIYAMLAMGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:cd01662  239 ILILPAFGIFSEIVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWL 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190  81 ATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLT 160
Cdd:cd01662  318 FTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRM 397

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 992008190 161 LNPKWLKIQFVTMFVGVNLTFFPQHFLGLAGMPRRYSDYP--DSYTSWNVVSSLGSTI 216
Cdd:cd01662  398 LNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFL 455
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-216 3.22e-67

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: 214.36  E-value: 3.22e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190    1 ILILPGFGMISHIISQESGKKeAFGTLGMIYAMLAMGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:pfam00115 213 ILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWL 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190   81 ATLHGTQLN-YSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGL 159
Cdd:pfam00115 292 ATLWGGWIRfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGR 371

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992008190  160 TLNPKWLKIQFVTMFVGVNLTFFPQHFLGLAGMPRRYS----DYPDSYTSWNVVSSLGSTI 216
Cdd:pfam00115 372 MYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-265 2.34e-52

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: 180.05  E-value: 2.34e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190    1 ILILPGFGMISHIISQESgKKEAFGTLGMIYAMLAMGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:TIGR02882 282 IVILPAFGIYSEIISTFA-QKRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWL 360

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190   81 ATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLT 160
Cdd:TIGR02882 361 LTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYK 440

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190  161 LNPKWLKIQFVTMFVGVNLTFFPQHFLGLAGMPRRYSDY--PDSYTSWNVVSSLGSTISFIGIILLIFIIWESMI-SNRT 237
Cdd:TIGR02882 441 LNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYspSDGWFPLNLISTIGALLMAIGFIFLVYNIYYSHRkSPRE 520

                         250       260
                  ....*....|....*....|....*...
gi 992008190  238 VLFPLSMVSSLEWYQNLPPAEHSYSELP 265
Cdd:TIGR02882 521 ATGDPWNGRTLEWATASPPPKYNFAVTP 548
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-265 3.60e-48

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 168.96  E-value: 3.60e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190   1 ILILPGFGMISHIISQESgKKEAFGTLGMIYAMLAMGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 80
Cdd:PRK15017 289 ILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWL 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190  81 ATLHGTQLNYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLFTGLT 160
Cdd:PRK15017 368 FTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFK 447

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190 161 LNPKWLKIQFVTMFVGVNLTFFPQHFLGLAGMPRRYSDYPD-SYTSWNVVSSLGSTISFIGIILLIFIIWESMIS---NR 236
Cdd:PRK15017 448 LNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDpQFHTMLMIAASGAALIALGILCQVIQMYVSIRDrdqNR 527

                        250       260
                 ....*....|....*....|....*....
gi 992008190 237 TVLFPLSMVSSLEWYQNLPPAEHSYSELP 265
Cdd:PRK15017 528 DLTGDPWGGRTLEWATSSPPPFYNFAVVP 556
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 65-216 7.19e-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: 67.70  E-value: 7.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190  65 TMIIAVPTGIKIFSWLATL-HGTQLNYSPALLW---------------ALGFVFlFTIGGLTGVVLANSSLDIILHDTYY 128
Cdd:cd01660  282 TFMVALPSLLTAFTVFASLeIAGRLRGGKGLFGwiralpwgdpmflalFLAMLM-FIPGGAGGIINASYQLNYVVHNTAW 360

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992008190 129 VVAHFHyvLSMGAVFAIMAGFIQWY--PLFTGLTLNPKWL-KIQFVTMFVGVNLTFFPQHFLGLAGMPRR--YSDYPDSY 203
Cdd:cd01660  361 VPGHFH--LTVGGAVALTFMAVAYWlvPHLTGRELAAKRLaLAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGGLP 438

                        170
                 ....*....|....*...
gi 992008190 204 -----TSWNVVSSLGSTI 216
Cdd:cd01660  439 aagewAPYQQLMAIGGTI 456
 
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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