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Conserved domains on  [gi|669633590|gb|AII23321|]
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cytochrome c oxidase subunit I, partial (mitochondrion) [Papilio hyppason]

Protein Classification

cytochrome-c oxidase subunit 1( domain architecture ID 10009591)

cytochrome-c oxidase subunit 1 is the catalytic subunit of cytochrome c oxidase, which is the component of the respiratory chain that catalyzes the reduction of oxygen to water

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-479 0e+00

cytochrome c oxidase subunit I; Provisional


:

Pssm-ID: 177210  Cd Length: 511  Bit Score: 868.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590   1 FGIWASMLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMS 80
Cdd:MTH00153  20 FGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMS 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590  81 FWLLPPSLTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQM 160
Cdd:MTH00153 100 FWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRM 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 161 PLFIWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF************GFGMISHIISQE 240
Cdd:MTH00153 180 PLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQE 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 241 SGKKETFGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWS 320
Cdd:MTH00153 260 SGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWA 339

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 321 LGFVFLFTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGV 400
Cdd:MTH00153 340 LGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGV 419

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 669633590 401 NLTFFPQHFLGLSGMPRRYSDYPDSFTSWNIISSFGSYISLLSLMMMMMIIWESMINQRIIMFSLNMPSSIEWLQNLPP 479
Cdd:MTH00153 420 NLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEWLQNLPP 498
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-479 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 868.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590   1 FGIWASMLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMS 80
Cdd:MTH00153  20 FGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMS 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590  81 FWLLPPSLTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQM 160
Cdd:MTH00153 100 FWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRM 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 161 PLFIWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF************GFGMISHIISQE 240
Cdd:MTH00153 180 PLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQE 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 241 SGKKETFGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWS 320
Cdd:MTH00153 260 SGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWA 339

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 321 LGFVFLFTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGV 400
Cdd:MTH00153 340 LGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGV 419

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 669633590 401 NLTFFPQHFLGLSGMPRRYSDYPDSFTSWNIISSFGSYISLLSLMMMMMIIWESMINQRIIMFSLNMPSSIEWLQNLPP 479
Cdd:MTH00153 420 NLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEWLQNLPP 498
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-475 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: 752.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590   1 FGIWASMLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMS 80
Cdd:cd01663   13 FGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLS 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590  81 FWLLPPSLTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQM 160
Cdd:cd01663   93 FWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKM 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 161 PLFIWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF************GFGMISHIISQE 240
Cdd:cd01663  173 PLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTF 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 241 SGKKETFGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWS 320
Cdd:cd01663  253 SGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWA 332

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 321 LGFVFLFTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGV 400
Cdd:cd01663  333 LGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGV 412

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 669633590 401 NLTFFPQHFLGLSGMPRRYSDYPDSFTSWNIISSFGSYISLLSLMMMMMIIWESMINQRIIMFSLN-MPSSIEWLQ 475
Cdd:cd01663  413 NLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGeGSTSLEWTL 488
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-438 1.13e-163

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: 471.71  E-value: 1.13e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590    1 FGIWASMLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMiGGFGNWLIPLMLGAPDMAFPRMNNMS 80
Cdd:TIGR02891  16 TAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFS 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590   81 FWLLPPSLTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQM 160
Cdd:TIGR02891  95 YWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRM 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590  161 PLFIWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF************GFGMISHIISQE 240
Cdd:TIGR02891 175 PLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTF 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590  241 SGKKeTFGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWS 320
Cdd:TIGR02891 255 ARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFA 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590  321 LGFVFLFTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGV 400
Cdd:TIGR02891 334 LGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGF 413

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 669633590  401 NLTFFPQHFLGLSGMPRRYSDYPDS--FTSWNIISSFGSY 438
Cdd:TIGR02891 414 NLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAF 453
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
7-438 1.30e-160

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 465.37  E-value: 1.30e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590   7 MLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPP 86
Cdd:COG0843   31 LIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLF 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590  87 SLTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQMPLFIWA 166
Cdd:COG0843  110 GGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWA 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 167 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF************GFGMISHIISQESGKKeT 246
Cdd:COG0843  190 ALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-L 268

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 247 FGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWSLGFVFL 326
Cdd:COG0843  269 FGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIIL 348

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 327 FTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGVNLTFFP 406
Cdd:COG0843  349 FVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFP 428

                        410       420       430
                 ....*....|....*....|....*....|....
gi 669633590 407 QHFLGLSGMPRRYSDYP--DSFTSWNIISSFGSY 438
Cdd:COG0843  429 MHILGLLGMPRRYATYPpePGWQPLNLISTIGAF 462
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-438 2.15e-112

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: 338.39  E-value: 2.15e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590    1 FGIWASMLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRMNNMS 80
Cdd:pfam00115   9 TALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590   81 FWLLPPSLTLLISSMiveNGAGTGWTIYPPLSSnaihssssVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFdQM 160
Cdd:pfam00115  88 FWLVVLGAVLLLASF---GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RM 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590  161 PLFIWAVGITALLLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWF************GFGMISHIISQE 240
Cdd:pfam00115 156 PLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKF 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590  241 SGKKeTFGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMN-YSPSILW 319
Cdd:pfam00115 230 AGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRfRTTPMLF 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590  320 SLGFVFLFTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIG 399
Cdd:pfam00115 309 FLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIG 388

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 669633590  400 VNLTFFPQHFLGLSGMPRRYS----DYPDSFTSWNIISSFGSY 438
Cdd:pfam00115 389 FNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGV 431
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-479 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 868.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590   1 FGIWASMLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMS 80
Cdd:MTH00153  20 FGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMS 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590  81 FWLLPPSLTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQM 160
Cdd:MTH00153 100 FWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRM 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 161 PLFIWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF************GFGMISHIISQE 240
Cdd:MTH00153 180 PLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQE 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 241 SGKKETFGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWS 320
Cdd:MTH00153 260 SGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWA 339

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 321 LGFVFLFTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGV 400
Cdd:MTH00153 340 LGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGV 419

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 669633590 401 NLTFFPQHFLGLSGMPRRYSDYPDSFTSWNIISSFGSYISLLSLMMMMMIIWESMINQRIIMFSLNMPSSIEWLQNLPP 479
Cdd:MTH00153 420 NLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEWLQNLPP 498
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-475 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: 752.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590   1 FGIWASMLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMS 80
Cdd:cd01663   13 FGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLS 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590  81 FWLLPPSLTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQM 160
Cdd:cd01663   93 FWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKM 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 161 PLFIWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF************GFGMISHIISQE 240
Cdd:cd01663  173 PLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTF 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 241 SGKKETFGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWS 320
Cdd:cd01663  253 SGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWA 332

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 321 LGFVFLFTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGV 400
Cdd:cd01663  333 LGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGV 412

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 669633590 401 NLTFFPQHFLGLSGMPRRYSDYPDSFTSWNIISSFGSYISLLSLMMMMMIIWESMINQRIIMFSLN-MPSSIEWLQ 475
Cdd:cd01663  413 NLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGeGSTSLEWTL 488
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-479 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 714.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590   1 FGIWASMLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMS 80
Cdd:MTH00167  22 FGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMS 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590  81 FWLLPPSLTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQM 160
Cdd:MTH00167 102 FWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQT 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 161 PLFIWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF************GFGMISHIISQE 240
Cdd:MTH00167 182 PLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYY 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 241 SGKKETFGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWS 320
Cdd:MTH00167 262 SGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWA 341

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 321 LGFVFLFTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGV 400
Cdd:MTH00167 342 LGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFIGV 421

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 669633590 401 NLTFFPQHFLGLSGMPRRYSDYPDSFTSWNIISSFGSYISLLSLMMMMMIIWESMINQRIIMFSLNMPSSIEWLQNLPP 479
Cdd:MTH00167 422 NLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLLPVELTSTNVEWLHGCPP 500
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-479 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 711.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590   1 FGIWASMLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMS 80
Cdd:MTH00142  20 FGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMS 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590  81 FWLLPPSLTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQM 160
Cdd:MTH00142 100 FWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERV 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 161 PLFIWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF************GFGMISHIISQE 240
Cdd:MTH00142 180 PLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHY 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 241 SGKKETFGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWS 320
Cdd:MTH00142 260 SGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWA 339

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 321 LGFVFLFTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGV 400
Cdd:MTH00142 340 LGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYTMFIGV 419

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 669633590 401 NLTFFPQHFLGLSGMPRRYSDYPDSFTSWNIISSFGSYISLLSLMMMMMIIWESMINQRIIMFSLNMPSSIEWLQNLPP 479
Cdd:MTH00142 420 NLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVMWSSHLSTSLEWSHRLPP 498
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-479 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 707.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590   1 FGIWASMLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMS 80
Cdd:MTH00116  22 FGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMS 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590  81 FWLLPPSLTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQM 160
Cdd:MTH00116 102 FWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQT 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 161 PLFIWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF************GFGMISHIISQE 240
Cdd:MTH00116 182 PLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYY 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 241 SGKKETFGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWS 320
Cdd:MTH00116 262 AGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWA 341

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 321 LGFVFLFTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGV 400
Cdd:MTH00116 342 LGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGV 421

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 669633590 401 NLTFFPQHFLGLSGMPRRYSDYPDSFTSWNIISSFGSYISLLSLMMMMMIIWESMINQRIIMFSLNMPSSIEWLQNLPP 479
Cdd:MTH00116 422 NLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVLQPELTTTNIEWIHGCPP 500
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-479 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 707.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590   1 FGIWASMLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMS 80
Cdd:MTH00223  19 FGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMS 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590  81 FWLLPPSLTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQM 160
Cdd:MTH00223  99 FWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERL 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 161 PLFIWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF************GFGMISHIISQE 240
Cdd:MTH00223 179 PLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHY 258

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 241 SGKKETFGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWS 320
Cdd:MTH00223 259 SSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWA 338

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 321 LGFVFLFTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGV 400
Cdd:MTH00223 339 LGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFLMFLGV 418

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 669633590 401 NLTFFPQHFLGLSGMPRRYSDYPDSFTSWNIISSFGSYISLLSLMMMMMIIWESMINQRIIMFSLNMPSSIEWLQNLPP 479
Cdd:MTH00223 419 NLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVWSGHLSTSLEWDNLLPA 497
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-479 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 648.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590   1 FGIWASMLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMS 80
Cdd:MTH00103  22 FGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMS 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590  81 FWLLPPSLTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQM 160
Cdd:MTH00103 102 FWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQT 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 161 PLFIWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF************GFGMISHIISQE 240
Cdd:MTH00103 182 PLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYY 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 241 SGKKETFGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWS 320
Cdd:MTH00103 262 SGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWA 341

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 321 LGFVFLFTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGV 400
Cdd:MTH00103 342 LGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIMFVGV 421

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 669633590 401 NLTFFPQHFLGLSGMPRRYSDYPDSFTSWNIISSFGSYISLLSLMMMMMIIWESMINQRIIMFSLNMPSSIEWLQNLPP 479
Cdd:MTH00103 422 NMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVLTVELTTTNLEWLHGCPP 500
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-478 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 642.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590   1 FGIWASMLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMS 80
Cdd:MTH00007  19 LGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMS 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590  81 FWLLPPSLTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQM 160
Cdd:MTH00007  99 FWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERI 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 161 PLFIWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF************GFGMISHIISQE 240
Cdd:MTH00007 179 PLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHY 258

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 241 SGKKETFGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWS 320
Cdd:MTH00007 259 AGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWA 338

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 321 LGFVFLFTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGV 400
Cdd:MTH00007 339 LGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFLMFLGV 418

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 669633590 401 NLTFFPQHFLGLSGMPRRYSDYPDSFTSWNIISSFGSYISLLSLMMMMMIIWESMINQRIIMFSLNMPSSIEWLQNLP 478
Cdd:MTH00007 419 NLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIASPHMSSSLEWQDTLP 496
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-479 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 637.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590   1 FGIWASMLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMS 80
Cdd:MTH00183  22 FGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMS 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590  81 FWLLPPSLTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQM 160
Cdd:MTH00183 102 FWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQT 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 161 PLFIWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF************GFGMISHIISQE 240
Cdd:MTH00183 182 PLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYY 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 241 SGKKETFGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWS 320
Cdd:MTH00183 262 SGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWA 341

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 321 LGFVFLFTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGV 400
Cdd:MTH00183 342 LGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVMFVGV 421

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 669633590 401 NLTFFPQHFLGLSGMPRRYSDYPDSFTSWNIISSFGSYISLLSLMMMMMIIWESMINQRIIMFSLNMPSSIEWLQNLPP 479
Cdd:MTH00183 422 NLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLSVELTSTNVEWLHGCPP 500
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-479 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 629.66  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590   1 FGIWASMLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMS 80
Cdd:MTH00077  22 FGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMS 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590  81 FWLLPPSLTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQM 160
Cdd:MTH00077 102 FWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQT 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 161 PLFIWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF************GFGMISHIISQE 240
Cdd:MTH00077 182 PLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYY 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 241 SGKKETFGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWS 320
Cdd:MTH00077 262 SAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWA 341

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 321 LGFVFLFTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGV 400
Cdd:MTH00077 342 LGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVMFIGV 421

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 669633590 401 NLTFFPQHFLGLSGMPRRYSDYPDSFTSWNIISSFGSYISLLSLMMMMMIIWESMINQRIIMFSLNMPSSIEWLQNLPP 479
Cdd:MTH00077 422 NLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREVLTTELTSTNIEWLHGCPP 500
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-479 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 624.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590   1 FGIWASMLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMS 80
Cdd:MTH00037  22 FGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMS 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590  81 FWLLPPSLTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQM 160
Cdd:MTH00037 102 FWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRL 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 161 PLFIWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF************GFGMISHIISQE 240
Cdd:MTH00037 182 PLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHY 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 241 SGKKETFGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWS 320
Cdd:MTH00037 262 SGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWA 341

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 321 LGFVFLFTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGV 400
Cdd:MTH00037 342 LGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFLMFIGV 421

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 669633590 401 NLTFFPQHFLGLSGMPRRYSDYPDSFTSWNIISSFGSYISLLSLMMMMMIIWESMINQRIIMFSLNMPSSIEWLQNLPP 479
Cdd:MTH00037 422 NLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVISPEFSSSSLEWQYSSFP 500
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-437 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 584.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590   1 FGIWASMLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMS 80
Cdd:MTH00182  24 FGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNIS 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590  81 FWLLPPSLTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQM 160
Cdd:MTH00182 104 FWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRL 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 161 PLFIWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF************GFGMISHIISQE 240
Cdd:MTH00182 184 PLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTF 263

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 241 SGKKETFGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWS 320
Cdd:MTH00182 264 VAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWA 343

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 321 LGFVFLFTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGV 400
Cdd:MTH00182 344 MGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWLMFIGV 423

                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 669633590 401 NLTFFPQHFLGLSGMPRRYSDYPDSFTSWNIISSFGS 437
Cdd:MTH00182 424 NLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGS 460
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-479 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 581.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590   1 FGIWASMLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMS 80
Cdd:MTH00079  23 FGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLS 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590  81 FWLLPPSLTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSsVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQM 160
Cdd:MTH00079 103 FWLLPTSLFLILDSCFVDMGPGTSWTVYPPLSTLGHPGSS-VDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHM 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 161 PLFIWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF************GFGMISHIISQE 240
Cdd:MTH00079 182 SLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYL 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 241 SGKKETFGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWS 320
Cdd:MTH00079 262 TGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWV 341

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 321 LGFVFLFTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGV 400
Cdd:MTH00079 342 LGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFVGV 421

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 669633590 401 NLTFFPQHFLGLSGMPRRYSDYPDSFTSWNIISSFGSYISLLSLMMMMMIIWESMINQRIIMFSLNMPSSIEWLQNLPP 479
Cdd:MTH00079 422 NLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLHDNYINSSPEYSLSSYV 500
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-479 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 576.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590   1 FGIWASMLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMS 80
Cdd:MTH00184  24 FGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNIS 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590  81 FWLLPPSLTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQM 160
Cdd:MTH00184 104 FWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRM 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 161 PLFIWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF************GFGMISHIISQE 240
Cdd:MTH00184 184 PLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTF 263

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 241 SGKKETFGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWS 320
Cdd:MTH00184 264 AAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWA 343

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 321 LGFVFLFTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGV 400
Cdd:MTH00184 344 IGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMFIGV 423

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 401 NLTFFPQHFLGLSGMPRRYSDYPDSFTSWNIISSFGSYISLLSLMMMMMIIWESMINQRII---MFSLNMPSSIEWLQNL 477
Cdd:MTH00184 424 NLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVREIKFvgwVEDSGHYPSLEWAQTS 503


                 ..
gi 669633590 478 PP 479
Cdd:MTH00184 504 PP 505
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-437 1.62e-178

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 511.10  E-value: 1.62e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590   1 FGIWASMLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMS 80
Cdd:MTH00026  23 FGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNIS 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590  81 FWLLPPSLTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQM 160
Cdd:MTH00026 103 FWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRI 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 161 PLFIWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF************GFGMISHIISQE 240
Cdd:MTH00026 183 PLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLF 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 241 SGKKETFGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMN--YSPSIL 318
Cdd:MTH00026 263 SYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSGRNliFTTPMA 342

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 319 WSLGFVFLFTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFI 398
Cdd:MTH00026 343 WALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLMFI 422

                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 669633590 399 GVNLTFFPQHFLGLSGMPRRYSDYPDSFTSWNIISSFGS 437
Cdd:MTH00026 423 GVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGS 461
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-438 2.19e-178

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: 507.84  E-value: 2.19e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590   1 FGIWASMLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPlMLGAPDMAFPRMNNMS 80
Cdd:cd00919   11 FAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLS 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590  81 FWLLPPSLTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQM 160
Cdd:cd00919   90 FWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKM 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 161 PLFIWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF************GFGMISHIISQE 240
Cdd:cd00919  170 PLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTF 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 241 SGKKeTFGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWS 320
Cdd:cd00919  250 SGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFA 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 321 LGFVFLFTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGV 400
Cdd:cd00919  329 LGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGF 408

                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 669633590 401 NLTFFPQHFLGLSGMPRRYSDYPDSFTSWNIISSFGSY 438
Cdd:cd00919  409 NLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAF 446
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-438 1.13e-163

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: 471.71  E-value: 1.13e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590    1 FGIWASMLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMiGGFGNWLIPLMLGAPDMAFPRMNNMS 80
Cdd:TIGR02891  16 TAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFS 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590   81 FWLLPPSLTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQM 160
Cdd:TIGR02891  95 YWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRM 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590  161 PLFIWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF************GFGMISHIISQE 240
Cdd:TIGR02891 175 PLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTF 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590  241 SGKKeTFGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWS 320
Cdd:TIGR02891 255 ARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFA 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590  321 LGFVFLFTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGV 400
Cdd:TIGR02891 334 LGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGF 413

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 669633590  401 NLTFFPQHFLGLSGMPRRYSDYPDS--FTSWNIISSFGSY 438
Cdd:TIGR02891 414 NLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAF 453
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
7-438 1.30e-160

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 465.37  E-value: 1.30e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590   7 MLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPP 86
Cdd:COG0843   31 LIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLF 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590  87 SLTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQMPLFIWA 166
Cdd:COG0843  110 GGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWA 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 167 VGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF************GFGMISHIISQESGKKeT 246
Cdd:COG0843  190 ALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-L 268

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 247 FGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWSLGFVFL 326
Cdd:COG0843  269 FGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIIL 348

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 327 FTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGVNLTFFP 406
Cdd:COG0843  349 FVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFP 428

                        410       420       430
                 ....*....|....*....|....*....|....
gi 669633590 407 QHFLGLSGMPRRYSDYP--DSFTSWNIISSFGSY 438
Cdd:COG0843  429 MHILGLLGMPRRYATYPpePGWQPLNLISTIGAF 462
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-438 2.75e-149

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 435.65  E-value: 2.75e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590   1 FGIWASMLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMS 80
Cdd:MTH00048  23 LGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALS 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590  81 FWLLPPSLTLLISSMIVenGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFdQM 160
Cdd:MTH00048 103 AWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RT 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 161 PLFIWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF************GFGMISHIISQE 240
Cdd:MTH00048 180 SIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSL 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 241 SGKKETFGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYS-PSILW 319
Cdd:MTH00048 260 SNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSdPVVWW 339

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 320 SLGFVFLFTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIG 399
Cdd:MTH00048 340 VVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIG 419

                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 669633590 400 VNLTFFPQHFLGLSGMPRRYSDYPDSFTSWNIISSFGSY 438
Cdd:MTH00048 420 FNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSF 458
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 8-438 1.17e-138

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: 408.12  E-value: 1.17e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590   8 LGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGgFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPS 87
Cdd:cd01662   24 RGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFG 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590  88 LTLLISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQMPLFIWAV 167
Cdd:cd01662  103 GLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTT 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 168 GITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF************GFGMISHIISQESGKKeTF 247
Cdd:cd01662  183 LVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRKP-LF 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 248 GCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWSLGFVFLF 327
Cdd:cd01662  262 GYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTF 341

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 328 TIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGVNLTFFPQ 407
Cdd:cd01662  342 VIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFNLTFFPM 421

                        410       420       430
                 ....*....|....*....|....*....|...
gi 669633590 408 HFLGLSGMPRRYSDYP--DSFTSWNIISSFGSY 438
Cdd:cd01662  422 HILGLMGMPRRVYTYLpgPGWDPLNLISTIGAF 454
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-438 2.15e-112

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: 338.39  E-value: 2.15e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590    1 FGIWASMLGTSLSLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPiMIGGFGNWLIPLMLGAPDMAFPRMNNMS 80
Cdd:pfam00115   9 TALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590   81 FWLLPPSLTLLISSMiveNGAGTGWTIYPPLSSnaihssssVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFdQM 160
Cdd:pfam00115  88 FWLVVLGAVLLLASF---GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RM 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590  161 PLFIWAVGITALLLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWF************GFGMISHIISQE 240
Cdd:pfam00115 156 PLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKF 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590  241 SGKKeTFGCLGMIYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMN-YSPSILW 319
Cdd:pfam00115 230 AGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRfRTTPMLF 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590  320 SLGFVFLFTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIG 399
Cdd:pfam00115 309 FLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIG 388

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 669633590  400 VNLTFFPQHFLGLSGMPRRYS----DYPDSFTSWNIISSFGSY 438
Cdd:pfam00115 389 FNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGV 431
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 13-437 7.57e-92

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: 292.14  E-value: 7.57e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590   13 SLLIRTELGMPNSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGgFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLTLLI 92
Cdd:TIGR02882  72 ALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFN 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590   93 SSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQMPLFIWAVGITAL 172
Cdd:TIGR02882 151 ISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTL 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590  173 LLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF************GFGMISHIISQESgKKETFGCLGM 252
Cdd:TIGR02882 231 IIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIISTFA-QKRLFGYKSM 309

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590  253 IYAMMTIGLLGFIVWAHHMFTIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWSLGFVFLFTIGGL 332
Cdd:TIGR02882 310 VWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGV 389

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590  333 TGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGVNLTFFPQHFLGL 412
Cdd:TIGR02882 390 TGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLNERLGKWCFWFFMIGFNVCFFPMYILGL 469

                         410       420
                  ....*....|....*....|....*..
gi 669633590  413 SGMPRRYSDY--PDSFTSWNIISSFGS 437
Cdd:TIGR02882 470 DGMPRRMYTYspSDGWFPLNLISTIGA 496
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 33-437 9.78e-82

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 266.03  E-value: 9.78e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590  33 YNTIVTAHAFIMIFFMVMPIMIGgFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLTLLISSMIVENGAGTGWTIYPPLS 112
Cdd:PRK15017  99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 113 SNAIHSSSSVDLVIFSLHLAGISSILGAINFITTIINMRINKMTFDQMPLFIWAVGITALLLLLSLPVLAGAITMLLTDR 192
Cdd:PRK15017 178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 193 NLNTSFFDPAGGGDPILYQHLFWF************GFGMISHIISQESgKKETFGCLGMIYAMMTIGLLGFIVWAHHMF 272
Cdd:PRK15017 258 YLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFF 336

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 273 TIGMDTDTRAYFTSATMIIAVPTGIKIFSWLATFHGTQMNYSPSILWSLGFVFLFTIGGLTGVILANSSIDVTLHDTYYV 352
Cdd:PRK15017 337 TMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFL 416

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 353 VAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSYLLKIQFFTMFIGVNLTFFPQHFLGLSGMPRRYSDYPD-SFTSWNI 431
Cdd:PRK15017 417 IAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDpQFHTMLM 496


                 ....*.
gi 669633590 432 ISSFGS 437
Cdd:PRK15017 497 IAASGA 502
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 12-425 1.72e-09

ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively. For general information on the heme-copper oxidase superfamily, please see cd00919.


Pssm-ID: 238830  Cd Length: 473  Bit Score: 59.61  E-value: 1.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590  12 LSLLIRTELgmpNSLIGDDQIYNTIVTAHAFIM-IFFMVMPIMigGFGNWLIPLMLGAPDMAfPRMNNMSFWLLPPSlTL 90
Cdd:cd01660   26 LQVLVRTGV---FPLPSSGILYYQGLTLHGVLLaIVFTTFFIM--GFFYAIVARALLRSLFN-RRLAWAGFWLMVIG-TV 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590  91 LISSMIVENGAGTGWTIYPPLSSNAIHSSSSVDLVIFSLhlagissILGAINFITTIINMRINKMtfDQMPLFIWAVGIT 170
Cdd:cd01660   99 MAAVPILLGQASVLYTFYPPLQAHPLFYIGAALVVVGSW-------ISGFAMFVTLWRWKKANPG--KKVPLATFMVVTT 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 171 ALLLLLSLPVLAGAITMLLtdrnLNTSFFDpAGGGDPILYQHLFWF************GFGMISHIISQESGKKeTFGCL 250
Cdd:cd01660  170 MILWLVASLGVALEVLFQL----LPWSLGL-VDTVDVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGK-LFSDP 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 251 GMIYAMMTIGLLGFIVWAHHMFT-IGMDTDTRAYFTSATMIIAVPTGIKIFSWLATF-HGTQMNYSPSILW--------- 319
Cdd:cd01660  244 LARLAFILFLLFSTPVGFHHQFAdPGIGPGWKFIHMVLTFMVALPSLLTAFTVFASLeIAGRLRGGKGLFGwiralpwgd 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 669633590 320 ------SLGFVFlFTIGGLTGVILANSSIDVTLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWYPLFTGLSLNSY-LLKIQ 392
Cdd:cd01660  324 pmflalFLAMLM-FIPGGAGGIINASYQLNYVVHNTAWVPGHFHLTVGGAVALTFMAVAYWLVPHLTGRELAAKrLALAQ 402

                        410       420       430
                 ....*....|....*....|....*....|....*
gi 669633590 393 FFTMFIGVNLTFFPQHFLGLSGMPRR--YSDYPDS 425
Cdd:cd01660  403 PWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGGL 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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