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Conserved domains on  [gi|931147779|gb|ALG35813|]
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cytochrome c oxidase subunit I (mitochondrion) [Parevania sp. SJW-2015]

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 ...
 1-506 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: 767.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779   1 MMMWLLSSNHKNIALLYF-----SHMISYNW-FIIKTDYSNsvkhPKLFINNEQIYNSMVTLHAFIMIFFMVMPFMIGGF 74
Cdd:MTH00153   1 MNKWLFSTNHKDIGTLYFifgawSGMVGTSLsLLIRAELGQ----PGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779  75 GNWLIPLMISTPDLAFPRMNNSSFWLLPPSLTLLITAGFSNSGVGTGWTIYPPLSSNLFHSGYSVDLSIFSLHLSGTASI 154
Cdd:MTH00153  77 GNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSI 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 155 LGSINFMVSILSMKHYYIYLNKLSLLTWSIFLTTILLLLSIPVLAGAITMLLMDRNLNTSFFDPCGGGDPVLFQHLFWFF 234
Cdd:MTH00153 157 LGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFF 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 235 GHPEVYILIIPGFGIMSHIIANEMNKKTTFGPISMIYALISITFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGI 314
Cdd:MTH00153 237 GHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGI 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 315 KIFSWLASFYGSKFDpLNTSLLWAMGFITMFTIGGLSGVILSNSSIDISLHDTYYVVAHFHYVLSMGAVFSILGGLIYWY 394
Cdd:MTH00153 317 KIFSWLATLHGSQIN-YSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWF 395

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 395 PLFTGVSLNKFLINIQFYSLFIGTNLTFFPQHFLGLGGMPRRYSEYPDSFTLWNMISSVGSIISIYALIILIIALWESLV 474
Cdd:MTH00153 396 PLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMI 475

                        490       500       510
                 ....*....|....*....|....*....|....
gi 931147779 475 SQREVIFKFNK--SMEWMLSYPPMNHTYTESPSV 506
Cdd:MTH00153 476 SKRPVLFSLNLssSIEWLQNLPPAEHSYSELPLL 509
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-506 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 767.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779   1 MMMWLLSSNHKNIALLYF-----SHMISYNW-FIIKTDYSNsvkhPKLFINNEQIYNSMVTLHAFIMIFFMVMPFMIGGF 74
Cdd:MTH00153   1 MNKWLFSTNHKDIGTLYFifgawSGMVGTSLsLLIRAELGQ----PGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779  75 GNWLIPLMISTPDLAFPRMNNSSFWLLPPSLTLLITAGFSNSGVGTGWTIYPPLSSNLFHSGYSVDLSIFSLHLSGTASI 154
Cdd:MTH00153  77 GNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSI 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 155 LGSINFMVSILSMKHYYIYLNKLSLLTWSIFLTTILLLLSIPVLAGAITMLLMDRNLNTSFFDPCGGGDPVLFQHLFWFF 234
Cdd:MTH00153 157 LGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFF 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 235 GHPEVYILIIPGFGIMSHIIANEMNKKTTFGPISMIYALISITFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGI 314
Cdd:MTH00153 237 GHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGI 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 315 KIFSWLASFYGSKFDpLNTSLLWAMGFITMFTIGGLSGVILSNSSIDISLHDTYYVVAHFHYVLSMGAVFSILGGLIYWY 394
Cdd:MTH00153 317 KIFSWLATLHGSQIN-YSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWF 395

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 395 PLFTGVSLNKFLINIQFYSLFIGTNLTFFPQHFLGLGGMPRRYSEYPDSFTLWNMISSVGSIISIYALIILIIALWESLV 474
Cdd:MTH00153 396 PLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMI 475

                        490       500       510
                 ....*....|....*....|....*....|....
gi 931147779 475 SQREVIFKFNK--SMEWMLSYPPMNHTYTESPSV 506
Cdd:MTH00153 476 SKRPVLFSLNLssSIEWLQNLPPAEHSYSELPLL 509
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 9-491 0e+00

Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, may play a role in assembly or oxygen delivery to the active site. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center.


Pssm-ID: 238833  Cd Length: 488  Bit Score: 702.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779   9 NHKNIALLYFshMISYNWFIIKTDYSNSVK----HPKLFINNEQIYNSMVTLHAFIMIFFMVMPFMIGGFGNWLIPLMIS 84
Cdd:cd01663    2 NHKDIGTLYL--IFGLWSGLVGTSLSLLIRlelsQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779  85 TPDLAFPRMNNSSFWLLPPSLTLLITAGFSNSGVGTGWTIYPPLSSNLFHSGYSVDLSIFSLHLSGTASILGSINFMVSI 164
Cdd:cd01663   80 APDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 165 LSMKHYYIYLNKLSLLTWSIFLTTILLLLSIPVLAGAITMLLMDRNLNTSFFDPCGGGDPVLFQHLFWFFGHPEVYILII 244
Cdd:cd01663  160 FNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILIL 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 245 PGFGIMSHIIANEMNKKTTFGPISMIYALISITFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLASFY 324
Cdd:cd01663  240 PGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMW 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 325 GSKFdPLNTSLLWAMGFITMFTIGGLSGVILSNSSIDISLHDTYYVVAHFHYVLSMGAVFSILGGLIYWYPLFTGVSLNK 404
Cdd:cd01663  320 GGSI-KFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNE 398

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 405 FLINIQFYSLFIGTNLTFFPQHFLGLGGMPRRYSEYPDSFTLWNMISSVGSIISIYALIILIIALWESLVSQREVIFKFN 484
Cdd:cd01663  399 TLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVG 478

                        490
                 ....*....|
gi 931147779 485 K---SMEWML 491
Cdd:cd01663  479 EgstSLEWTL 488
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-449 2.08e-162

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 471.15  E-value: 2.08e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779   1 MMMWLLSSNHKNIALLYFshMISYNWF--------IIKTDYSNSVKHpklFINNEQiYNSMVTLHAFIMIFFMVMPFmIG 72
Cdd:COG0843    6 WRRWLTTVDHKRIGIMYL--VTAFVFLliggllalLMRLQLAGPGLG---LLSPET-YNQLFTMHGTIMIFFFATPF-LA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779  73 GFGNWLIPLMISTPDLAFPRMNNSSFWLLPPSLTLLITAGFSNSGVGTGWTIYPPLSSNLFHSGYSVDLSIFSLHLSGTA 152
Cdd:COG0843   79 GFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 153 SILGSINFMVSILSMKHYYIYLNKLSLLTWSIFLTTILLLLSIPVLAGAITMLLMDRNLNTSFFDPCGGGDPVLFQHLFW 232
Cdd:COG0843  159 SILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFW 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 233 FFGHPEVYILIIPGFGIMSHIIANeMNKKTTFGPISMIYALISITFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPT 312
Cdd:COG0843  239 FFGHPEVYILILPAFGIVSEIIPT-FSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPT 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 313 GIKIFSWLASFYGSKFdPLNTSLLWAMGFITMFTIGGLSGVILSNSSIDISLHDTYYVVAHFHYVLSMGAVFSILGGLIY 392
Cdd:COG0843  318 GVKVFNWIATMWRGRI-RFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYY 396

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 931147779 393 WYPLFTGVSLNKFLINIQFYSLFIGTNLTFFPQHFLGLGGMPRRYSEYP--DSFTLWNM 449
Cdd:COG0843  397 WFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNL 455
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 5-449 8.80e-160

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: 463.23  E-value: 8.80e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779    5 LLSSNHKNIALLYFshMISYNWFIIKTDYSNSVK----HPKLFINNEQIYNSMVTLHAFIMIFFMVMPfMIGGFGNWLIP 80
Cdd:TIGR02891   1 LTTVDHKRIGILYL--VTAFAFFLVGGVLALLMRaqlaTPGNTFMDAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779   81 LMISTPDLAFPRMNNSSFWLLPPSLTLLITAGFSNSGVGTGWTIYPPLSSNLFHSGYSVDLSIFSLHLSGTASILGSINF 160
Cdd:TIGR02891  78 LMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNF 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779  161 MVSILSMKHYYIYLNKLSLLTWSIFLTTILLLLSIPVLAGAITMLLMDRNLNTSFFDPCGGGDPVLFQHLFWFFGHPEVY 240
Cdd:TIGR02891 158 IVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVY 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779  241 ILIIPGFGIMSHIIANeMNKKTTFGPISMIYALISITFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWL 320
Cdd:TIGR02891 238 IIFLPAFGIISEILPT-FARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWI 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779  321 ASFYGSKFDpLNTSLLWAMGFITMFTIGGLSGVILSNSSIDISLHDTYYVVAHFHYVLSMGAVFSILGGLIYWYPLFTGV 400
Cdd:TIGR02891 317 ATLWGGSIR-FTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGR 395

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 931147779  401 SLNKFLINIQFYSLFIGTNLTFFPQHFLGLGGMPRRYSEYPDS--FTLWNM 449
Cdd:TIGR02891 396 MYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNL 446
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 40-449 8.90e-114

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: 343.02  E-value: 8.90e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779   40 PKLFINNEQIYNSMVTLHAFIMIFFMVMPFmIGGFGNWLIPLMISTPDLAFPRMNNSSFWLLPPSLTLLItagFSNSGVG 119
Cdd:pfam00115  31 PGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLL---ASFGGAT 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779  120 TGWTIYPPLSSnlfhsgysVDLSIFSLHLSGTASILGSINFMVSILSMKHYYIYLnKLSLLTWSIFLTTILLLLSIPVLA 199
Cdd:pfam00115 107 TGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLA 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779  200 GAITMLLMDRNLNTsffdpcGGGDPVLFQHLFWFFGHPEVYILIIPGFGIMSHIIANeMNKKTTFGPISMIYALISITFL 279
Cdd:pfam00115 178 AALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPK-FAGRPLFGYKLSVLAFWLIAFL 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779  280 GFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLASFYGSKFDPLNTSLLWAMGFITMFTIGGLSGVILSNSS 359
Cdd:pfam00115 251 GFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFRTTPMLFFLGFAFLFIIGGLTGVMLALPP 330

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779  360 IDISLHDTYYVVAHFHYVLSMGAVFSILGGLIYWYPLFTGVSLNKFLINIQFYSLFIGTNLTFFPQHFLGLGGMPRRYS- 438
Cdd:pfam00115 331 VNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAp 410

                         410
                  ....*....|....
gi 931147779  439 ---EYPDSFTLWNM 449
Cdd:pfam00115 411 pfiETVPAFQPLNW 424
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-506 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 767.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779   1 MMMWLLSSNHKNIALLYF-----SHMISYNW-FIIKTDYSNsvkhPKLFINNEQIYNSMVTLHAFIMIFFMVMPFMIGGF 74
Cdd:MTH00153   1 MNKWLFSTNHKDIGTLYFifgawSGMVGTSLsLLIRAELGQ----PGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779  75 GNWLIPLMISTPDLAFPRMNNSSFWLLPPSLTLLITAGFSNSGVGTGWTIYPPLSSNLFHSGYSVDLSIFSLHLSGTASI 154
Cdd:MTH00153  77 GNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSI 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 155 LGSINFMVSILSMKHYYIYLNKLSLLTWSIFLTTILLLLSIPVLAGAITMLLMDRNLNTSFFDPCGGGDPVLFQHLFWFF 234
Cdd:MTH00153 157 LGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFF 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 235 GHPEVYILIIPGFGIMSHIIANEMNKKTTFGPISMIYALISITFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGI 314
Cdd:MTH00153 237 GHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGI 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 315 KIFSWLASFYGSKFDpLNTSLLWAMGFITMFTIGGLSGVILSNSSIDISLHDTYYVVAHFHYVLSMGAVFSILGGLIYWY 394
Cdd:MTH00153 317 KIFSWLATLHGSQIN-YSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWF 395

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 395 PLFTGVSLNKFLINIQFYSLFIGTNLTFFPQHFLGLGGMPRRYSEYPDSFTLWNMISSVGSIISIYALIILIIALWESLV 474
Cdd:MTH00153 396 PLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMI 475

                        490       500       510
                 ....*....|....*....|....*....|....
gi 931147779 475 SQREVIFKFNK--SMEWMLSYPPMNHTYTESPSV 506
Cdd:MTH00153 476 SKRPVLFSLNLssSIEWLQNLPPAEHSYSELPLL 509
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 9-491 0e+00

Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, may play a role in assembly or oxygen delivery to the active site. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center.


Pssm-ID: 238833  Cd Length: 488  Bit Score: 702.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779   9 NHKNIALLYFshMISYNWFIIKTDYSNSVK----HPKLFINNEQIYNSMVTLHAFIMIFFMVMPFMIGGFGNWLIPLMIS 84
Cdd:cd01663    2 NHKDIGTLYL--IFGLWSGLVGTSLSLLIRlelsQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779  85 TPDLAFPRMNNSSFWLLPPSLTLLITAGFSNSGVGTGWTIYPPLSSNLFHSGYSVDLSIFSLHLSGTASILGSINFMVSI 164
Cdd:cd01663   80 APDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 165 LSMKHYYIYLNKLSLLTWSIFLTTILLLLSIPVLAGAITMLLMDRNLNTSFFDPCGGGDPVLFQHLFWFFGHPEVYILII 244
Cdd:cd01663  160 FNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILIL 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 245 PGFGIMSHIIANEMNKKTTFGPISMIYALISITFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLASFY 324
Cdd:cd01663  240 PGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMW 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 325 GSKFdPLNTSLLWAMGFITMFTIGGLSGVILSNSSIDISLHDTYYVVAHFHYVLSMGAVFSILGGLIYWYPLFTGVSLNK 404
Cdd:cd01663  320 GGSI-KFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNE 398

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 405 FLINIQFYSLFIGTNLTFFPQHFLGLGGMPRRYSEYPDSFTLWNMISSVGSIISIYALIILIIALWESLVSQREVIFKFN 484
Cdd:cd01663  399 TLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVG 478

                        490
                 ....*....|
gi 931147779 485 K---SMEWML 491
Cdd:cd01663  479 EgstSLEWTL 488
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-507 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 677.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779   1 MMMWLLSSNHKNIALLYF-----SHMISYNW-FIIKTDYSnsvkHPKLFINNEQIYNSMVTLHAFIMIFFMVMPFMIGGF 74
Cdd:MTH00167   3 INRWLFSTNHKDIGTLYFifgawAGMVGTALsLLIRAELS----QPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779  75 GNWLIPLMISTPDLAFPRMNNSSFWLLPPSLTLLITAGFSNSGVGTGWTIYPPLSSNLFHSGYSVDLSIFSLHLSGTASI 154
Cdd:MTH00167  79 GNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSI 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 155 LGSINFMVSILSMKHYYIYLNKLSLLTWSIFLTTILLLLSIPVLAGAITMLLMDRNLNTSFFDPCGGGDPVLFQHLFWFF 234
Cdd:MTH00167 159 LGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFF 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 235 GHPEVYILIIPGFGIMSHIIANEMNKKTTFGPISMIYALISITFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGI 314
Cdd:MTH00167 239 GHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGI 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 315 KIFSWLASFYGSKFdPLNTSLLWAMGFITMFTIGGLSGVILSNSSIDISLHDTYYVVAHFHYVLSMGAVFSILGGLIYWY 394
Cdd:MTH00167 319 KVFSWLATLHGGKI-KWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWF 397

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 395 PLFTGVSLNKFLINIQFYSLFIGTNLTFFPQHFLGLGGMPRRYSEYPDSFTLWNMISSVGSIISIYALIILIIALWESLV 474
Cdd:MTH00167 398 PLFTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFS 477

                        490       500       510
                 ....*....|....*....|....*....|....*
gi 931147779 475 SQREVIF--KFNKSMEWMLSYPPMNHTYTESPSVQ 507
Cdd:MTH00167 478 SKRKLLPveLTSTNVEWLHGCPPPHHTWEEPPFVQ 512
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-507 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 668.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779   1 MMMWLLSSNHKNIALLYF-----SHMI-SYNWFIIKTDYSnsvkHPKLFINNEQIYNSMVTLHAFIMIFFMVMPFMIGGF 74
Cdd:MTH00116   3 ITRWLFSTNHKDIGTLYLifgawAGMVgTALSLLIRAELG----QPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779  75 GNWLIPLMISTPDLAFPRMNNSSFWLLPPSLTLLITAGFSNSGVGTGWTIYPPLSSNLFHSGYSVDLSIFSLHLSGTASI 154
Cdd:MTH00116  79 GNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSI 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 155 LGSINFMVSILSMKHYYIYLNKLSLLTWSIFLTTILLLLSIPVLAGAITMLLMDRNLNTSFFDPCGGGDPVLFQHLFWFF 234
Cdd:MTH00116 159 LGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFF 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 235 GHPEVYILIIPGFGIMSHIIANEMNKKTTFGPISMIYALISITFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGI 314
Cdd:MTH00116 239 GHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGI 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 315 KIFSWLASFYGSKFDpLNTSLLWAMGFITMFTIGGLSGVILSNSSIDISLHDTYYVVAHFHYVLSMGAVFSILGGLIYWY 394
Cdd:MTH00116 319 KVFSWLATLHGGTIK-WDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWF 397

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 395 PLFTGVSLNKFLINIQFYSLFIGTNLTFFPQHFLGLGGMPRRYSEYPDSFTLWNMISSVGSIISIYALIILIIALWESLV 474
Cdd:MTH00116 398 PLFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFS 477

                        490       500       510
                 ....*....|....*....|....*....|....*
gi 931147779 475 SQREVIFKFNKSM--EWMLSYPPMNHTYTESPSVQ 507
Cdd:MTH00116 478 SKRKVLQPELTTTniEWIHGCPPPYHTFEEPAFVQ 512
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 2-504 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 663.98  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779   2 MMWLLSSNHKNIALLYfshMISYNWF-IIKTDYSNSVK----HPKLFINNEQIYNSMVTLHAFIMIFFMVMPFMIGGFGN 76
Cdd:MTH00223   1 MRWLFSTNHKDIGTLY---LIFGMWSgLVGTSLSLLIRaelgQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGN 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779  77 WLIPLMISTPDLAFPRMNNSSFWLLPPSLTLLITAGFSNSGVGTGWTIYPPLSSNLFHSGYSVDLSIFSLHLSGTASILG 156
Cdd:MTH00223  78 WLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 157 SINFMVSILSMKHYYIYLNKLSLLTWSIFLTTILLLLSIPVLAGAITMLLMDRNLNTSFFDPCGGGDPVLFQHLFWFFGH 236
Cdd:MTH00223 158 AINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGH 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 237 PEVYILIIPGFGIMSHIIANEMNKKTTFGPISMIYALISITFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKI 316
Cdd:MTH00223 238 PEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKV 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 317 FSWLASFYGSKFdPLNTSLLWAMGFITMFTIGGLSGVILSNSSIDISLHDTYYVVAHFHYVLSMGAVFSILGGLIYWYPL 396
Cdd:MTH00223 318 FSWLATIYGSKI-KYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPL 396

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 397 FTGVSLNKFLINIQFYSLFIGTNLTFFPQHFLGLGGMPRRYSEYPDSFTLWNMISSVGSIISIYALIILIIALWESLVSQ 476
Cdd:MTH00223 397 FTGVTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQ 476

                        490       500       510
                 ....*....|....*....|....*....|
gi 931147779 477 REVIFKFNK--SMEWMLSYPPMNHTYTESP 504
Cdd:MTH00223 477 RSVVWSGHLstSLEWDNLLPADFHNNSETG 506
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-506 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 647.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779   1 MMMWLLSSNHKNIALLYF-----SHMISYNW-FIIKTDYSNsvkhPKLFINNEQIYNSMVTLHAFIMIFFMVMPFMIGGF 74
Cdd:MTH00142   1 MMRWLFSTNHKDIGTLYFlfgawAGMVGTGLsLLIRAELGQ----PGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779  75 GNWLIPLMISTPDLAFPRMNNSSFWLLPPSLTLLITAGFSNSGVGTGWTIYPPLSSNLFHSGYSVDLSIFSLHLSGTASI 154
Cdd:MTH00142  77 GNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSI 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 155 LGSINFMVSILSMKHYYIYLNKLSLLTWSIFLTTILLLLSIPVLAGAITMLLMDRNLNTSFFDPCGGGDPVLFQHLFWFF 234
Cdd:MTH00142 157 LGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFF 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 235 GHPEVYILIIPGFGIMSHIIANEMNKKTTFGPISMIYALISITFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGI 314
Cdd:MTH00142 237 GHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGI 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 315 KIFSWLASFYGSKFDpLNTSLLWAMGFITMFTIGGLSGVILSNSSIDISLHDTYYVVAHFHYVLSMGAVFSILGGLIYWY 394
Cdd:MTH00142 317 KVFSWLATLHGSKVK-YEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWF 395

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 395 PLFTGVSLNKFLINIQFYSLFIGTNLTFFPQHFLGLGGMPRRYSEYPDSFTLWNMISSVGSIISIYALIILIIALWESLV 474
Cdd:MTH00142 396 PLFTGLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFV 475

                        490       500       510
                 ....*....|....*....|....*....|....
gi 931147779 475 SQREVIFK--FNKSMEWMLSYPPMNHTYTESPSV 506
Cdd:MTH00142 476 SQRLVMWSshLSTSLEWSHRLPPDFHTYDELPIL 509
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 4-506 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 594.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779   4 WLLSSNHKNIALLYFshmISYNWF-IIKTDYSNSVK----HPKLFINNEQIYNSMVTLHAFIMIFFMVMPFMIGGFGNWL 78
Cdd:MTH00037   6 WLFSTNHKDIGTLYL---IFGAWAgMVGTAMSVIIRtelaQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779  79 IPLMISTPDLAFPRMNNSSFWLLPPSLTLLITAGFSNSGVGTGWTIYPPLSSNLFHSGYSVDLSIFSLHLSGTASILGSI 158
Cdd:MTH00037  83 IPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 159 NFMVSILSMKHYYIYLNKLSLLTWSIFLTTILLLLSIPVLAGAITMLLMDRNLNTSFFDPCGGGDPVLFQHLFWFFGHPE 238
Cdd:MTH00037 163 NFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPE 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 239 VYILIIPGFGIMSHIIANEMNKKTTFGPISMIYALISITFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFS 318
Cdd:MTH00037 243 VYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFS 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 319 WLASFYGSKFDpLNTSLLWAMGFITMFTIGGLSGVILSNSSIDISLHDTYYVVAHFHYVLSMGAVFSILGGLIYWYPLFT 398
Cdd:MTH00037 323 WMATLQGSNLR-WETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFS 401

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 399 GVSLNKFLINIQFYSLFIGTNLTFFPQHFLGLGGMPRRYSEYPDSFTLWNMISSVGSIISIYALIILIIALWESLVSQRE 478
Cdd:MTH00037 402 GVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQRE 481

                        490       500       510
                 ....*....|....*....|....*....|.
gi 931147779 479 VIFK--FNKSMEWML-SYPPMNHTYTESPSV 506
Cdd:MTH00037 482 VISPefSSSSLEWQYsSFPPSHHTFDETPST 512
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 4-509 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 579.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779   4 WLLSSNHKNIALLY-----FSHMISYNW-FIIKTDYSnsvkHPKLFINNEQIYNSMVTLHAFIMIFFMVMPFMIGGFGNW 77
Cdd:MTH00183   6 WFFSTNHKDIGTLYlvfgaWAGMVGTALsLLIRAELS----QPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNW 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779  78 LIPLMISTPDLAFPRMNNSSFWLLPPSLTLLITAGFSNSGVGTGWTIYPPLSSNLFHSGYSVDLSIFSLHLSGTASILGS 157
Cdd:MTH00183  82 LIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 158 INFMVSILSMKHYYIYLNKLSLLTWSIFLTTILLLLSIPVLAGAITMLLMDRNLNTSFFDPCGGGDPVLFQHLFWFFGHP 237
Cdd:MTH00183 162 INFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 238 EVYILIIPGFGIMSHIIANEMNKKTTFGPISMIYALISITFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIF 317
Cdd:MTH00183 242 EVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVF 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 318 SWLASFYGSKFDpLNTSLLWAMGFITMFTIGGLSGVILSNSSIDISLHDTYYVVAHFHYVLSMGAVFSILGGLIYWYPLF 397
Cdd:MTH00183 322 SWLATLHGGSIK-WETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLF 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 398 TGVSLNKFLINIQFYSLFIGTNLTFFPQHFLGLGGMPRRYSEYPDSFTLWNMISSVGSIISIYALIILIIALWESLVSQR 477
Cdd:MTH00183 401 SGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKR 480

                        490       500       510
                 ....*....|....*....|....*....|....
gi 931147779 478 EVIFK--FNKSMEWMLSYPPMNHTYTESPSVQLE 509
Cdd:MTH00183 481 EVLSVelTSTNVEWLHGCPPPYHTFEEPAFVQVQ 514
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 4-507 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 576.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779   4 WLLSSNHKNIALLYfshMISYNWF-IIKTDYSNSVK----HPKLFINNEQIYNSMVTLHAFIMIFFMVMPFMIGGFGNWL 78
Cdd:MTH00103   6 WLFSTNHKDIGTLY---LLFGAWAgMVGTALSLLIRaelgQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779  79 IPLMISTPDLAFPRMNNSSFWLLPPSLTLLITAGFSNSGVGTGWTIYPPLSSNLFHSGYSVDLSIFSLHLSGTASILGSI 158
Cdd:MTH00103  83 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 159 NFMVSILSMKHYYIYLNKLSLLTWSIFLTTILLLLSIPVLAGAITMLLMDRNLNTSFFDPCGGGDPVLFQHLFWFFGHPE 238
Cdd:MTH00103 163 NFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 239 VYILIIPGFGIMSHIIANEMNKKTTFGPISMIYALISITFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFS 318
Cdd:MTH00103 243 VYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFS 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 319 WLASFYGS--KFDPlntSLLWAMGFITMFTIGGLSGVILSNSSIDISLHDTYYVVAHFHYVLSMGAVFSILGGLIYWYPL 396
Cdd:MTH00103 323 WLATLHGGniKWSP---AMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPL 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 397 FTGVSLNKFLINIQFYSLFIGTNLTFFPQHFLGLGGMPRRYSEYPDSFTLWNMISSVGSIISIYALIILIIALWESLVSQ 476
Cdd:MTH00103 400 FSGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASK 479

                        490       500       510
                 ....*....|....*....|....*....|...
gi 931147779 477 REVIF--KFNKSMEWMLSYPPMNHTYTESPSVQ 507
Cdd:MTH00103 480 REVLTveLTTTNLEWLHGCPPPYHTFEEPTYVK 512
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 2-503 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 576.08  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779   2 MMWLLSSNHKNIALLYFshMISYNWFIIKTDYSNSVK----HPKLFINNEQIYNSMVTLHAFIMIFFMVMPFMIGGFGNW 77
Cdd:MTH00007   1 MRWLYSTNHKDIGTLYF--ILGVWGGLLGTSMSLLIRielgQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNW 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779  78 LIPLMISTPDLAFPRMNNSSFWLLPPSLTLLITAGFSNSGVGTGWTIYPPLSSNLFHSGYSVDLSIFSLHLSGTASILGS 157
Cdd:MTH00007  79 LVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 158 INFMVSILSMKHYYIYLNKLSLLTWSIFLTTILLLLSIPVLAGAITMLLMDRNLNTSFFDPCGGGDPVLFQHLFWFFGHP 237
Cdd:MTH00007 159 INFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHP 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 238 EVYILIIPGFGIMSHIIANEMNKKTTFGPISMIYALISITFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIF 317
Cdd:MTH00007 239 EVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVF 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 318 SWLASFYGSKFDpLNTSLLWAMGFITMFTIGGLSGVILSNSSIDISLHDTYYVVAHFHYVLSMGAVFSILGGLIYWYPLF 397
Cdd:MTH00007 319 SWLATIHGSPIK-YETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLF 397

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 398 TGVSLNKFLINIQFYSLFIGTNLTFFPQHFLGLGGMPRRYSEYPDSFTLWNMISSVGSIISIYALIILIIALWESLVSQR 477
Cdd:MTH00007 398 TGLTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQR 477

                        490       500
                 ....*....|....*....|....*...
gi 931147779 478 EVIFK--FNKSMEWMLSYPPMNHTYTES 503
Cdd:MTH00007 478 GVIASphMSSSLEWQDTLPLDFHNLPET 505
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 4-507 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 574.97  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779   4 WLLSSNHKNIALLYfshMISYNWF-IIKTDYSNSVK----HPKLFINNEQIYNSMVTLHAFIMIFFMVMPFMIGGFGNWL 78
Cdd:MTH00077   6 WLFSTNHKDIGTLY---LVFGAWAgMVGTALSLLIRaelsQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779  79 IPLMISTPDLAFPRMNNSSFWLLPPSLTLLITAGFSNSGVGTGWTIYPPLSSNLFHSGYSVDLSIFSLHLSGTASILGSI 158
Cdd:MTH00077  83 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 159 NFMVSILSMKHYYIYLNKLSLLTWSIFLTTILLLLSIPVLAGAITMLLMDRNLNTSFFDPCGGGDPVLFQHLFWFFGHPE 238
Cdd:MTH00077 163 NFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPE 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 239 VYILIIPGFGIMSHIIANEMNKKTTFGPISMIYALISITFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFS 318
Cdd:MTH00077 243 VYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFS 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 319 WLASFYGSKFDpLNTSLLWAMGFITMFTIGGLSGVILSNSSIDISLHDTYYVVAHFHYVLSMGAVFSILGGLIYWYPLFT 398
Cdd:MTH00077 323 WLATMHGGAIK-WDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFS 401

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 399 GVSLNKFLINIQFYSLFIGTNLTFFPQHFLGLGGMPRRYSEYPDSFTLWNMISSVGSIISIYALIILIIALWESLVSQRE 478
Cdd:MTH00077 402 GYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKRE 481

                        490       500       510
                 ....*....|....*....|....*....|.
gi 931147779 479 VIFK--FNKSMEWMLSYPPMNHTYTESPSVQ 507
Cdd:MTH00077 482 VLTTelTSTNIEWLHGCPPPYHTFEEPSFVQ 512
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-502 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 551.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779   1 MMMWLLSSNHKNIALLYFshMISYNWFIIKTDYSN----SVKHPKLFINNEQIYNSMVTLHAFIMIFFMVMPFMIGGFGN 76
Cdd:MTH00079   4 LSVWLESSNHKDIGTLYF--LFGLWSGMVGTSLSLiirlELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779  77 WLIPLMISTPDLAFPRMNNSSFWLLPPSLTLLITAGFSNSGVGTGWTIYPPLSSnLFHSGYSVDLSIFSLHLSGTASILG 156
Cdd:MTH00079  82 WMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 157 SINFMVSILSMKHYYIYLNKLSLLTWSIFLTTILLLLSIPVLAGAITMLLMDRNLNTSFFDPCGGGDPVLFQHLFWFFGH 236
Cdd:MTH00079 161 GINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGH 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 237 PEVYILIIPGFGIMSHIIANEMNKKTTFGPISMIYALISITFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKI 316
Cdd:MTH00079 241 PEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKV 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 317 FSWLASFYGSKFDpLNTSLLWAMGFITMFTIGGLSGVILSNSSIDISLHDTYYVVAHFHYVLSMGAVFSILGGLIYWYPL 396
Cdd:MTH00079 321 FSWLATLFGMKMK-FQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPF 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 397 FTGVSLNKFLINIQFYSLFIGTNLTFFPQHFLGLGGMPRRYSEYPDSFTLWNMISSVGSIISIYALIILIIALWESLVSQ 476
Cdd:MTH00079 400 MTGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSY 479

                        490       500
                 ....*....|....*....|....*...
gi 931147779 477 REVIFKF--NKSMEWMLSYPPMNHTYTE 502
Cdd:MTH00079 480 RLVLHDNyiNSSPEYSLSSYVFGHSYQS 507
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 4-507 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 549.42  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779   4 WLLSSNHKNIALLYFSHMISYNwfIIKTDYSNSVK----HPKLFINNEQIYNSMVTLHAFIMIFFMVMPFMIGGFGNWLI 79
Cdd:MTH00182   8 WVFSTNHKDIGTLYLVFGAGAG--MIGTAFSMLIRlelsAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779  80 PLMISTPDLAFPRMNNSSFWLLPPSLTLLITAGFSNSGVGTGWTIYPPLSSNLFHSGYSVDLSIFSLHLSGTASILGSIN 159
Cdd:MTH00182  86 PLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAIN 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 160 FMVSILSMKHYYIYLNKLSLLTWSIFLTTILLLLSIPVLAGAITMLLMDRNLNTSFFDPCGGGDPVLFQHLFWFFGHPEV 239
Cdd:MTH00182 166 FITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEV 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 240 YILIIPGFGIMSHIIANEMNKKTTFGPISMIYALISITFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSW 319
Cdd:MTH00182 246 YILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSW 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 320 LASFYGSKFDpLNTSLLWAMGFITMFTIGGLSGVILSNSSIDISLHDTYYVVAHFHYVLSMGAVFSILGGLIYWYPLFTG 399
Cdd:MTH00182 326 LATIYGGTLR-LDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITG 404

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 400 VSLNKFLINIQFYSLFIGTNLTFFPQHFLGLGGMPRRYSEYPDSFTLWNMISSVGSIISIYALIILIIALWESLVSQREV 479
Cdd:MTH00182 405 YCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKF 484

                        490       500       510
                 ....*....|....*....|....*....|....
gi 931147779 480 IFKFN------KSMEWMLSYPPMNHTYTESPSVQ 507
Cdd:MTH00182 485 IGWKEgtgeswASLEWVHSSPPLFHTYNELPFVY 518
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 4-506 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 540.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779   4 WLLSSNHKNIALLY-----FSHMISYNW-FIIKTDYSNsvkhPKLFINNEQIYNSMVTLHAFIMIFFMVMPFMIGGFGNW 77
Cdd:MTH00184   8 WLFSTNHKDIGTLYllfgaFAGMIGTAFsMLIRLELSA----PGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNW 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779  78 LIPLMISTPDLAFPRMNNSSFWLLPPSLTLLITAGFSNSGVGTGWTIYPPLSSNLFHSGYSVDLSIFSLHLSGTASILGS 157
Cdd:MTH00184  84 FVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 158 INFMVSILSMKHYYIYLNKLSLLTWSIFLTTILLLLSIPVLAGAITMLLMDRNLNTSFFDPCGGGDPVLFQHLFWFFGHP 237
Cdd:MTH00184 164 MNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHP 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 238 EVYILIIPGFGIMSHIIANEMNKKTTFGPISMIYALISITFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIF 317
Cdd:MTH00184 244 EVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIF 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 318 SWLASFYGSKFDpLNTSLLWAMGFITMFTIGGLSGVILSNSSIDISLHDTYYVVAHFHYVLSMGAVFSILGGLIYWYPLF 397
Cdd:MTH00184 324 SWIATIFGGSLR-LDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKI 402

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 398 TGVSLNKFLINIQFYSLFIGTNLTFFPQHFLGLGGMPRRYSEYPDSFTLWNMISSVGSIISIYALIILIIALWESLVsqR 477
Cdd:MTH00184 403 TGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYV--R 480

                        490       500       510
                 ....*....|....*....|....*....|....*.
gi 931147779 478 EVIFK-------FNKSMEWMLSYPPMNHTYTESPSV 506
Cdd:MTH00184 481 EIKFVgwvedsgHYPSLEWAQTSPPAHHTYNELPYV 516
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 39-449 1.22e-173

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: 497.05  E-value: 1.22e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779  39 HPKLFINNEQIYNSMVTLHAFIMIFFMVMPFMIGGFGNWLIPlMISTPDLAFPRMNNSSFWLLPPSLTLLITAGFSNSGV 118
Cdd:cd00919   32 TPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGA 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 119 GTGWTIYPPLSSNLFHSGYSVDLSIFSLHLSGTASILGSINFMVSILSMKHYYIYLNKLSLLTWSIFLTTILLLLSIPVL 198
Cdd:cd00919  111 GTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLALPVL 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 199 AGAITMLLMDRNLNTSFFDPCGGGDPVLFQHLFWFFGHPEVYILIIPGFGIMSHIIANeMNKKTTFGPISMIYALISITF 278
Cdd:cd00919  191 AAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPT-FSGKPLFGYKLMVYAFLAIGF 269

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 279 LGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLASFYGSKfDPLNTSLLWAMGFITMFTIGGLSGVILSNS 358
Cdd:cd00919  270 LSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGR-IRFDPPMLFALGFLFLFTIGGLTGVVLANV 348

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 359 SIDISLHDTYYVVAHFHYVLSMGAVFSILGGLIYWYPLFTGVSLNKFLINIQFYSLFIGTNLTFFPQHFLGLGGMPRRYS 438
Cdd:cd00919  349 PLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGFNLTFFPMHFLGLLGMPRRYA 428

                        410
                 ....*....|.
gi 931147779 439 EYPDSFTLWNM 449
Cdd:cd00919  429 DYPDGFAPWNF 439
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-449 2.08e-162

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 471.15  E-value: 2.08e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779   1 MMMWLLSSNHKNIALLYFshMISYNWF--------IIKTDYSNSVKHpklFINNEQiYNSMVTLHAFIMIFFMVMPFmIG 72
Cdd:COG0843    6 WRRWLTTVDHKRIGIMYL--VTAFVFLliggllalLMRLQLAGPGLG---LLSPET-YNQLFTMHGTIMIFFFATPF-LA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779  73 GFGNWLIPLMISTPDLAFPRMNNSSFWLLPPSLTLLITAGFSNSGVGTGWTIYPPLSSNLFHSGYSVDLSIFSLHLSGTA 152
Cdd:COG0843   79 GFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 153 SILGSINFMVSILSMKHYYIYLNKLSLLTWSIFLTTILLLLSIPVLAGAITMLLMDRNLNTSFFDPCGGGDPVLFQHLFW 232
Cdd:COG0843  159 SILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFW 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 233 FFGHPEVYILIIPGFGIMSHIIANeMNKKTTFGPISMIYALISITFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPT 312
Cdd:COG0843  239 FFGHPEVYILILPAFGIVSEIIPT-FSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPT 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 313 GIKIFSWLASFYGSKFdPLNTSLLWAMGFITMFTIGGLSGVILSNSSIDISLHDTYYVVAHFHYVLSMGAVFSILGGLIY 392
Cdd:COG0843  318 GVKVFNWIATMWRGRI-RFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYY 396

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 931147779 393 WYPLFTGVSLNKFLINIQFYSLFIGTNLTFFPQHFLGLGGMPRRYSEYP--DSFTLWNM 449
Cdd:COG0843  397 WFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNL 455
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 4-506 1.03e-161

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 469.49  E-value: 1.03e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779   4 WLLSSNHKNIALLYFshMISYNWFIIKTDYSNSVK----HPKLFINNEQIYNSMVTLHAFIMIFFMVMPFMIGGFGNWLI 79
Cdd:MTH00026   7 WFFSCNHKDIGSLYL--VFGALSGAIGTAFSMLIRlelsSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779  80 PLMISTPDLAFPRMNNSSFWLLPPSLTLLITAGFSNSGVGTGWTIYPPLSSNLFHSGYSVDLSIFSLHLSGTASILGSIN 159
Cdd:MTH00026  85 PLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMN 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 160 FMVSILSMKHYYIYLNKLSLLTWSIFLTTILLLLSIPVLAGAITMLLMDRNLNTSFFDPCGGGDPVLFQHLFWFFGHPEV 239
Cdd:MTH00026 165 FITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEV 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 240 YILIIPGFGIMSHIIANEMNKKTTFGPISMIYALISITFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSW 319
Cdd:MTH00026 245 YILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSW 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 320 LASFYGSKFDPL-NTSLLWAMGFITMFTIGGLSGVILSNSSIDISLHDTYYVVAHFHYVLSMGAVFSILGGLIYWYPLFT 398
Cdd:MTH00026 325 LATVSGSGRNLIfTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKIT 404

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 399 GVSLNKFLINIQFYSLFIGTNLTFFPQHFLGLGGMPRRYSEYPDSFTLWNMISSVGSIISIYALIILIIALWESLVsqRE 478
Cdd:MTH00026 405 GYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAYY--RE 482

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*
gi 931147779 479 VIFKFN-----------------KSMEWMLSYPPMNHTYTESPSV 506
Cdd:MTH00026 483 EPFDINimakgplipfscqpahfDTLEWSLTSPPEHHTYNELPYI 527
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 5-449 8.80e-160

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: 463.23  E-value: 8.80e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779    5 LLSSNHKNIALLYFshMISYNWFIIKTDYSNSVK----HPKLFINNEQIYNSMVTLHAFIMIFFMVMPfMIGGFGNWLIP 80
Cdd:TIGR02891   1 LTTVDHKRIGILYL--VTAFAFFLVGGVLALLMRaqlaTPGNTFMDAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779   81 LMISTPDLAFPRMNNSSFWLLPPSLTLLITAGFSNSGVGTGWTIYPPLSSNLFHSGYSVDLSIFSLHLSGTASILGSINF 160
Cdd:TIGR02891  78 LMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNF 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779  161 MVSILSMKHYYIYLNKLSLLTWSIFLTTILLLLSIPVLAGAITMLLMDRNLNTSFFDPCGGGDPVLFQHLFWFFGHPEVY 240
Cdd:TIGR02891 158 IVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVY 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779  241 ILIIPGFGIMSHIIANeMNKKTTFGPISMIYALISITFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWL 320
Cdd:TIGR02891 238 IIFLPAFGIISEILPT-FARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWI 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779  321 ASFYGSKFDpLNTSLLWAMGFITMFTIGGLSGVILSNSSIDISLHDTYYVVAHFHYVLSMGAVFSILGGLIYWYPLFTGV 400
Cdd:TIGR02891 317 ATLWGGSIR-FTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGR 395

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 931147779  401 SLNKFLINIQFYSLFIGTNLTFFPQHFLGLGGMPRRYSEYPDS--FTLWNM 449
Cdd:TIGR02891 396 MYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNL 446
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-480 3.76e-150

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 439.11  E-value: 3.76e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779   1 MMMWLLSSNHKNIALLYfshMISYNW---------FIIKTDYSNsvkhPKLFINNEQIYNSMVTLHAFIMIFFMVMPFMI 71
Cdd:MTH00048   4 LLSWLFTLDHKRIGVIY---TLLGVWsgfvglslsLLIRLNFLD----PYYNVISLDVYNFLITNHGIIMIFFFLMPVLI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779  72 GGFGNWLIPLMISTPDLAFPRMNNSSFWLLPPSLTLLITAGFSnsGVGTGWTIYPPLSSNLFHSGYSVDLSIFSLHLSGT 151
Cdd:MTH00048  77 GGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 152 ASILGSINFMVSILSMKHYYIYLnKLSLLTWSIFLTTILLLLSIPVLAGAITMLLMDRNLNTSFFDPCGGGDPVLFQHLF 231
Cdd:MTH00048 155 SSLFGSINFICTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMF 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 232 WFFGHPEVYILIIPGFGIMSHIIANEMNKKTTFGPISMIYALISITFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIP 311
Cdd:MTH00048 234 WFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVP 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 312 TGIKIFSWLASFYGSKFDPLNTSLLWAMGFITMFTIGGLSGVILSNSSIDISLHDTYYVVAHFHYVLSMGAVFSILGGLI 391
Cdd:MTH00048 314 TGIKVFSWLYMLLNSRVRKSDPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFI 393

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 392 YWYPLFTGVSLNKFLINIQFYSLFIGTNLTFFPQHFLGLGGMPRRYSEYPDSFTLWNMISSVGSIISIYALIILIIALWE 471
Cdd:MTH00048 394 WWWPLITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWE 473


                 ....*....
gi 931147779 472 SLVSQREVI 480
Cdd:MTH00048 474 SLVVKNEVL 482
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 43-449 8.08e-139

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: 409.66  E-value: 8.08e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779  43 FINNEQiYNSMVTLHAFIMIFFMVMPFMIGgFGNWLIPLMISTPDLAFPRMNNSSFWLLPPSLTLLITAGFSNSGVGTGW 122
Cdd:cd01662   43 FLSPEH-YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGW 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 123 TIYPPLSSNLFHSGYSVDLSIFSLHLSGTASILGSINFMVSILSMKHYYIYLNKLSLLTWSIFLTTILLLLSIPVLAGAI 202
Cdd:cd01662  121 FAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAAL 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 203 TMLLMDRNLNTSFFDPCGGGDPVLFQHLFWFFGHPEVYILIIPGFGIMSHIIANeMNKKTTFGPISMIYALISITFLGFI 282
Cdd:cd01662  201 ALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPT-FSRKPLFGYRSMVYATVAIGFLSFG 279

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 283 VWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLASFYGSKFDpLNTSLLWAMGFITMFTIGGLSGVILSNSSIDI 362
Cdd:cd01662  280 VWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIR-FETPMLWAIGFLVTFVIGGLTGVMLASPPADF 358

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 363 SLHDTYYVVAHFHYVLSMGAVFSILGGLIYWYPLFTGVSLNKFLINIQFYSLFIGTNLTFFPQHFLGLGGMPRRYSEYP- 441
Cdd:cd01662  359 QVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLp 438


                 ....*....
gi 931147779 442 -DSFTLWNM 449
Cdd:cd01662  439 gPGWDPLNL 447
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 40-449 8.90e-114

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: 343.02  E-value: 8.90e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779   40 PKLFINNEQIYNSMVTLHAFIMIFFMVMPFmIGGFGNWLIPLMISTPDLAFPRMNNSSFWLLPPSLTLLItagFSNSGVG 119
Cdd:pfam00115  31 PGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLL---ASFGGAT 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779  120 TGWTIYPPLSSnlfhsgysVDLSIFSLHLSGTASILGSINFMVSILSMKHYYIYLnKLSLLTWSIFLTTILLLLSIPVLA 199
Cdd:pfam00115 107 TGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLA 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779  200 GAITMLLMDRNLNTsffdpcGGGDPVLFQHLFWFFGHPEVYILIIPGFGIMSHIIANeMNKKTTFGPISMIYALISITFL 279
Cdd:pfam00115 178 AALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPK-FAGRPLFGYKLSVLAFWLIAFL 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779  280 GFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLASFYGSKFDPLNTSLLWAMGFITMFTIGGLSGVILSNSS 359
Cdd:pfam00115 251 GFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFRTTPMLFFLGFAFLFIIGGLTGVMLALPP 330

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779  360 IDISLHDTYYVVAHFHYVLSMGAVFSILGGLIYWYPLFTGVSLNKFLINIQFYSLFIGTNLTFFPQHFLGLGGMPRRYS- 438
Cdd:pfam00115 331 VNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAp 410

                         410
                  ....*....|....
gi 931147779  439 ---EYPDSFTLWNM 449
Cdd:pfam00115 411 pfiETVPAFQPLNW 424
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 4-449 8.89e-94

cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]


Pssm-ID: 131928  Cd Length: 643  Bit Score: 298.31  E-value: 8.89e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779    4 WLLSSNHKNIALLYfshMISYNWFIIKTDYSNSVKHPKLFINN-----EQIYNSMVTLHAFIMIFFMVMPFMIGgFGNWL 78
Cdd:TIGR02882  44 WLTTVDHKKIGVMY---IICAVLMLFRGGIDALLMRAQLTVPDnkfldAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIV 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779   79 IPLMISTPDLAFPRMNNSSFWLLPPSLTLLITAGFSNSGVGTGWTIYPPLSSNLFHSGYSVDLSIFSLHLSGTASILGSI 158
Cdd:TIGR02882 120 VPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGI 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779  159 NFMVSILSMKHYYIYLNKLSLLTWSIFLTTILLLLSIPVLAGAITMLLMDRNLNTSFFDPCGGGDPVLFQHLFWFFGHPE 238
Cdd:TIGR02882 200 NFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPE 279

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779  239 VYILIIPGFGIMSHIIANeMNKKTTFGPISMIYALISITFLGFIVWGHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFS 318
Cdd:TIGR02882 280 VYIVILPAFGIYSEIIST-FAQKRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFN 358

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779  319 WLASFYGSKFDpLNTSLLWAMGFITMFTIGGLSGVILSNSSIDISLHDTYYVVAHFHYVLSMGAVFSILGGLIYWYPLFT 398
Cdd:TIGR02882 359 WLLTLYKGKIR-FTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMF 437

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 931147779  399 GVSLNKFLINIQFYSLFIGTNLTFFPQHFLGLGGMPRRYSEY--PDSFTLWNM 449
Cdd:TIGR02882 438 GYKLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYspSDGWFPLNL 490
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 50-442 1.88e-90

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 290.30  E-value: 1.88e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779  50 YNSMVTLHAFIMIFFMVMPFMIGgFGNWLIPLMISTPDLAFPRMNNSSFWLLPPSLTLLITAGFSNSGVGTGWTIYPPLS 129
Cdd:PRK15017  99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 130 SNLFHSGYSVDLSIFSLHLSGTASILGSINFMVSILSMKHYYIYLNKLSLLTWSIFLTTILLLLSIPVLAGAITMLLMDR 209
Cdd:PRK15017 178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 210 NLNTSFFDPCGGGDPVLFQHLFWFFGHPEVYILIIPGFGIMSHIIANeMNKKTTFGPISMIYALISITFLGFIVWGHHMF 289
Cdd:PRK15017 258 YLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAAT-FSRKRLFGYTSLVWATVCITVLSFIVWLHHFF 336

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 290 TVGMDVDTRAYFTSATMIIAIPTGIKIFSWLASFYGSKFDpLNTSLLWAMGFITMFTIGGLSGVILSNSSIDISLHDTYY 369
Cdd:PRK15017 337 TMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIV-FHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLF 415

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 931147779 370 VVAHFHYVLSMGAVFSILGGLIYWYPLFTGVSLNKFLINIQFYSLFIGTNLTFFPQHFLGLGGMPRRYSEYPD 442
Cdd:PRK15017 416 LIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQID 488
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 223-443 5.89e-15

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: 76.94  E-value: 5.89e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 223 DPVLFQHLFWFFGHPEVYILIIPGFGIMSHIIANEMNKKTTFGPISMIyALISITFLGFIVWGHHMFT-VGMDVDTRAYF 301
Cdd:cd01660  200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARL-AFILFLLFSTPVGFHHQFAdPGIGPGWKFIH 278

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 302 TSATMIIAIPTGIKIFSWLASFY-------GSKFDPLNTSLLW--------AMGFItMFTIGGLSGVILSNSSIDISLHD 366
Cdd:cd01660  279 MVLTFMVALPSLLTAFTVFASLEiagrlrgGKGLFGWIRALPWgdpmflalFLAML-MFIPGGAGGIINASYQLNYVVHN 357

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931147779 367 TYYVVAHFHYVLSmGAVFSILGGLIYWY-PLFTGVSL-NKFLINIQFYSLFIGTNLTFFPQHFLGLGGMPRR--YSEYPD 442
Cdd:cd01660  358 TAWVPGHFHLTVG-GAVALTFMAVAYWLvPHLTGRELaAKRLALAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGG 436


                 .
gi 931147779 443 S 443
Cdd:cd01660  437 L 437
 
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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