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Conserved domains on  [gi|1824665928|ref|YP_009740863|]
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cytochrome c oxidase subunit I (mitochondrion) [Bryodemella tuberculata diluta]

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
 3-513 0e+00

cytochrome c oxidase subunit I; Provisional


:

Pssm-ID: 177210  Cd Length: 511  Bit Score: 930.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928   3 SQKWLFSTNHKDIGTLYFMFGAWAGMIGTSMSMIIRAELGQPGSMIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWL 82
Cdd:MTH00153    1 MNKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928  83 VPLMIGAPDMAFPRMNNMSFWLLPPSLILLLSSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGISSILGAV 162
Cdd:MTH00153   81 VPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 163 NFITTTTNMRSNSMSLDQTPLFVWSVAITALLLPVlpfvlfvlkSLfgPSLVRGVTYL------NS-----AGGGDPILY 231
Cdd:MTH00153  161 NFITTIINMRSKGMTLDRMPLFVWSVLITAILLLL---------SL--PVLAGAITMLltdrnlNTsffdpAGGGDPILY 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 232 QHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMI 311
Cdd:MTH00153  230 QHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMI 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 312 IAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMG 391
Cdd:MTH00153  310 IAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMG 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 392 GIIQWYPLFTGLTMNNKWLKIQFTIMFFGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIMSIIMFIMI 471
Cdd:MTH00153  390 GFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFI 469

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 1824665928 472 MWESMIKNRTIIFSMNMSSSTEWLQNNPPAEHSYSELPLINK 513
Cdd:MTH00153  470 IWESMISKRPVLFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 3-513 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 930.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928   3 SQKWLFSTNHKDIGTLYFMFGAWAGMIGTSMSMIIRAELGQPGSMIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWL 82
Cdd:MTH00153    1 MNKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928  83 VPLMIGAPDMAFPRMNNMSFWLLPPSLILLLSSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGISSILGAV 162
Cdd:MTH00153   81 VPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 163 NFITTTTNMRSNSMSLDQTPLFVWSVAITALLLPVlpfvlfvlkSLfgPSLVRGVTYL------NS-----AGGGDPILY 231
Cdd:MTH00153  161 NFITTIINMRSKGMTLDRMPLFVWSVLITAILLLL---------SL--PVLAGAITMLltdrnlNTsffdpAGGGDPILY 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 232 QHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMI 311
Cdd:MTH00153  230 QHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMI 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 312 IAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMG 391
Cdd:MTH00153  310 IAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMG 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 392 GIIQWYPLFTGLTMNNKWLKIQFTIMFFGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIMSIIMFIMI 471
Cdd:MTH00153  390 GFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFI 469

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 1824665928 472 MWESMIKNRTIIFSMNMSSSTEWLQNNPPAEHSYSELPLINK 513
Cdd:MTH00153  470 IWESMISKRPVLFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 10-496 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: 779.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928  10 TNHKDIGTLYFMFGAWAGMIGTSMSMIIRAELGQPGSMIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWLVPLMIGA 89
Cdd:cd01663     1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928  90 PDMAFPRMNNMSFWLLPPSLILLLSSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTTT 169
Cdd:cd01663    81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 170 NMRSNSMSLDQTPLFVWSVAITALLLPVlpfvlfvlkSLfgPSLVRGVTYL-----------NSAGGGDPILYQHLFWFF 238
Cdd:cd01663   161 NMRAPGMTLEKMPLFVWSVLITAFLLLL---------SL--PVLAGAITMLltdrnfntsffDPAGGGDPILYQHLFWFF 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 239 GHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGI 318
Cdd:cd01663   230 GHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGI 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 319 KVFSWMATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYP 398
Cdd:cd01663   310 KVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFP 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 399 LFTGLTMNNKWLKIQFTIMFFGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIMSIIMFIMIMWESMIK 478
Cdd:cd01663   390 KITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVS 469

                         490
                  ....*....|....*....
gi 1824665928 479 NRTIIF-SMNMSSSTEWLQ 496
Cdd:cd01663   470 GRKVIFnVGEGSTSLEWTL 488
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 7-452 1.75e-173

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: 498.29  E-value: 1.75e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928   7 LFSTNHKDIGTLYFMFGAWAGMIGTSMSMIIRAELGQPGSMIGDDQIYNVIITAHAFVMIFFMVMPIMiGGFGNWLVPLM 86
Cdd:TIGR02891   1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928  87 IGAPDMAFPRMNNMSFWLLPPSLILLLSSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGISSILGAVNFIT 166
Cdd:TIGR02891  80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 167 TTTNMRSNSMSLDQTPLFVWSVAITALLLPVLPFVLFVLKSLFGPSLVRGVTYLNSAGGGDPILYQHLFWFFGHPEVYIL 246
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 247 ILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMAT 326
Cdd:TIGR02891 240 FLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 327 LYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMN 406
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1824665928 407 NKWLKIQFTIMFFGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTSWNV 452
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNL 446
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
5-452 3.44e-173

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 498.88  E-value: 3.44e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928   5 KWLFSTNHKDIGTLYFMFGAWAGMIGTSMSMIIRAELGQPGSMIGDDQIYNVIITAHAFVMIFFMVMPiMIGGFGNWLVP 84
Cdd:COG0843     8 RWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928  85 LMIGAPDMAFPRMNNMSFWLLPPSLILLLSSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGISSILGAVNF 164
Cdd:COG0843    87 LQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNF 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 165 ITTTTNMRSNSMSLDQTPLFVWSVAITALLLPVLPFVLFVLKSLFGPSLVRGVTYLNSAGGGDPILYQHLFWFFGHPEVY 244
Cdd:COG0843   167 IVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVY 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 245 ILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWM 324
Cdd:COG0843   247 ILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWI 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 325 ATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLT 404
Cdd:COG0843   326 ATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRM 405

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1824665928 405 MNNKWLKIQFTIMFFGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTSWNV 452
Cdd:COG0843   406 LNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNL 455
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 14-452 1.20e-124

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: 371.14  E-value: 1.20e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928  14 DIGTLYFMFGAWAGMIGTSMSMIIRAELGQPGSMIGDDQIYNVIITAHAFVMIFFMVMPiMIGGFGNWLVPLMIGAPDMA 93
Cdd:pfam00115   1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928  94 FPRMNNMSFWLLPPSLILLLSSSMvdsGAGTGWTVYPPLAGaiahggssVDLAIFSLHLAGISSILGAVNFITTTTNMRS 173
Cdd:pfam00115  80 FPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 174 NSMSLdQTPLFVWSVAITALLLPVLPFvlfvlkSLFGPSLVRGVTYLNSAGGGDPILYQHLFWFFGHPEVYILILPGFGI 253
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFP------VLAAALLLLLLDRSLGAGGGDPLLDQHLFWWFGHPEVYILILPAFGI 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 254 ISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMATLYGTKFK 333
Cdd:pfam00115 222 IYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 334 FN-PPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNKWLKI 412
Cdd:pfam00115 301 FRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1824665928 413 QFTIMFFGVNLTFFPQHFLGLAGMPRRYS----DYPDAYTSWNV 452
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNW 424
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 3-513 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 930.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928   3 SQKWLFSTNHKDIGTLYFMFGAWAGMIGTSMSMIIRAELGQPGSMIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWL 82
Cdd:MTH00153    1 MNKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928  83 VPLMIGAPDMAFPRMNNMSFWLLPPSLILLLSSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGISSILGAV 162
Cdd:MTH00153   81 VPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 163 NFITTTTNMRSNSMSLDQTPLFVWSVAITALLLPVlpfvlfvlkSLfgPSLVRGVTYL------NS-----AGGGDPILY 231
Cdd:MTH00153  161 NFITTIINMRSKGMTLDRMPLFVWSVLITAILLLL---------SL--PVLAGAITMLltdrnlNTsffdpAGGGDPILY 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 232 QHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMI 311
Cdd:MTH00153  230 QHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMI 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 312 IAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMG 391
Cdd:MTH00153  310 IAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMG 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 392 GIIQWYPLFTGLTMNNKWLKIQFTIMFFGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIMSIIMFIMI 471
Cdd:MTH00153  390 GFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFI 469

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 1824665928 472 MWESMIKNRTIIFSMNMSSSTEWLQNNPPAEHSYSELPLINK 513
Cdd:MTH00153  470 IWESMISKRPVLFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 10-496 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: 779.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928  10 TNHKDIGTLYFMFGAWAGMIGTSMSMIIRAELGQPGSMIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWLVPLMIGA 89
Cdd:cd01663     1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928  90 PDMAFPRMNNMSFWLLPPSLILLLSSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTTT 169
Cdd:cd01663    81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 170 NMRSNSMSLDQTPLFVWSVAITALLLPVlpfvlfvlkSLfgPSLVRGVTYL-----------NSAGGGDPILYQHLFWFF 238
Cdd:cd01663   161 NMRAPGMTLEKMPLFVWSVLITAFLLLL---------SL--PVLAGAITMLltdrnfntsffDPAGGGDPILYQHLFWFF 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 239 GHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGI 318
Cdd:cd01663   230 GHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGI 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 319 KVFSWMATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYP 398
Cdd:cd01663   310 KVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFP 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 399 LFTGLTMNNKWLKIQFTIMFFGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIMSIIMFIMIMWESMIK 478
Cdd:cd01663   390 KITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVS 469

                         490
                  ....*....|....*....
gi 1824665928 479 NRTIIF-SMNMSSSTEWLQ 496
Cdd:cd01663   470 GRKVIFnVGEGSTSLEWTL 488
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-512 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 771.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928   1 MLSQKWLFSTNHKDIGTLYFMFGAWAGMIGTSMSMIIRAELGQPGSMIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGN 80
Cdd:MTH00167    1 MWINRWLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928  81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSLILLLSSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGISSILG 160
Cdd:MTH00167   81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 161 AVNFITTTTNMRSNSMSLDQTPLFVWSVAITALLLPvlpfvlfvlksLFGPSLVRGVTYL-----------NSAGGGDPI 229
Cdd:MTH00167  161 SINFITTIINMKPPGITQYQTPLFVWSILVTTILLL-----------LSLPVLAAAITMLltdrnlnttffDPAGGGDPI 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 230 LYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSAT 309
Cdd:MTH00167  230 LYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSAT 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 310 MIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAI 389
Cdd:MTH00167  310 MIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAI 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 390 MGGIIQWYPLFTGLTMNNKWLKIQFTIMFFGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIMSIIMFI 469
Cdd:MTH00167  390 MAGFTHWFPLFTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFL 469

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 1824665928 470 MIMWESMIKNRTIIFSMNMSSSTEWLQNNPPAEHSYSELPLIN 512
Cdd:MTH00167  470 FIIWEAFSSKRKLLPVELTSTNVEWLHGCPPPHHTWEEPPFVQ 512
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-511 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 765.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928   1 MLSQKWLFSTNHKDIGTLYFMFGAWAGMIGTSMSMIIRAELGQPGSMIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGN 80
Cdd:MTH00116    1 MFITRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928  81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSLILLLSSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGISSILG 160
Cdd:MTH00116   81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 161 AVNFITTTTNMRSNSMSLDQTPLFVWSVAITALLLPvlpfvlfvlksLFGPSLVRGVTYL-----------NSAGGGDPI 229
Cdd:MTH00116  161 AINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLL-----------LSLPVLAAGITMLltdrnlnttffDPAGGGDPI 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 230 LYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSAT 309
Cdd:MTH00116  230 LYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSAT 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 310 MIIAVPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAI 389
Cdd:MTH00116  310 MIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAI 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 390 MGGIIQWYPLFTGLTMNNKWLKIQFTIMFFGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIMSIIMFI 469
Cdd:MTH00116  390 MAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLM 469

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 1824665928 470 MIMWESMIKNRTIIFSMNMSSSTEWLQNNPPAEHSYSELPLI 511
Cdd:MTH00116  470 FIIWEAFSSKRKVLQPELTTTNIEWIHGCPPPYHTFEEPAFV 511
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 4-513 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 760.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928   4 QKWLFSTNHKDIGTLYFMFGAWAGMIGTSMSMIIRAELGQPGSMIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWLV 83
Cdd:MTH00142    2 MRWLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928  84 PLMIGAPDMAFPRMNNMSFWLLPPSLILLLSSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGISSILGAVN 163
Cdd:MTH00142   82 PLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAIN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 164 FITTTTNMRSNSMSLDQTPLFVWSVAITALLLPVLPFVLFVLKSLFGPSLVRGVTYLNSAGGGDPILYQHLFWFFGHPEV 243
Cdd:MTH00142  162 FITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 244 YILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 323
Cdd:MTH00142  242 YILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSW 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 324 MATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGL 403
Cdd:MTH00142  322 LATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGL 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 404 TMNNKWLKIQFTIMFFGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIMSIIMFIMIMWESMIKNRTII 483
Cdd:MTH00142  402 TLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVM 481

                         490       500       510
                  ....*....|....*....|....*....|
gi 1824665928 484 FSMNMSSSTEWLQNNPPAEHSYSELPLINK 513
Cdd:MTH00142  482 WSSHLSTSLEWSHRLPPDFHTYDELPILVV 511
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 5-511 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 754.89  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928   5 KWLFSTNHKDIGTLYFMFGAWAGMIGTSMSMIIRAELGQPGSMIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWLVP 84
Cdd:MTH00223    2 RWLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928  85 LMIGAPDMAFPRMNNMSFWLLPPSLILLLSSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGISSILGAVNF 164
Cdd:MTH00223   82 LMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 165 ITTTTNMRSNSMSLDQTPLFVWSVAITALLLPVLPfvlfvlkslfgPSLVRGVTYL-----------NSAGGGDPILYQH 233
Cdd:MTH00223  162 ITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSL-----------PVLAGAITMLltdrnfntsffDPAGGGDPILYQH 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 234 LFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIA 313
Cdd:MTH00223  231 LFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIA 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 314 VPTGIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGI 393
Cdd:MTH00223  311 VPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGF 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 394 IQWYPLFTGLTMNNKWLKIQFTIMFFGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIMSIIMFIMIMW 473
Cdd:MTH00223  391 NHWFPLFTGVTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVW 470

                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 1824665928 474 ESMIKNRTIIFSMNMSSSTEWLQNNPPAEHSYSELPLI 511
Cdd:MTH00223  471 EAFVSQRSVVWSGHLSTSLEWDNLLPADFHNNSETGAL 508
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-512 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 702.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928   1 MLSQKWLFSTNHKDIGTLYFMFGAWAGMIGTSMSMIIRAELGQPGSMIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGN 80
Cdd:MTH00103    1 MFINRWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928  81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSLILLLSSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGISSILG 160
Cdd:MTH00103   81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 161 AVNFITTTTNMRSNSMSLDQTPLFVWSVAITALLLPVLPFVLFVLKSLFGPSLVRGVTYLNSAGGGDPILYQHLFWFFGH 240
Cdd:MTH00103  161 AINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 241 PEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKV 320
Cdd:MTH00103  241 PEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 321 FSWMATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLF 400
Cdd:MTH00103  321 FSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLF 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 401 TGLTMNNKWLKIQFTIMFFGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIMSIIMFIMIMWESMIKNR 480
Cdd:MTH00103  401 SGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKR 480

                         490       500       510
                  ....*....|....*....|....*....|..
gi 1824665928 481 TIIFSMNMSSSTEWLQNNPPAEHSYSELPLIN 512
Cdd:MTH00103  481 EVLTVELTTTNLEWLHGCPPPYHTFEEPTYVK 512
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-507 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 692.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928   1 MLSQKWLFSTNHKDIGTLYFMFGAWAGMIGTSMSMIIRAELGQPGSMIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGN 80
Cdd:MTH00077    1 MMITRWLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928  81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSLILLLSSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGISSILG 160
Cdd:MTH00077   81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 161 AVNFITTTTNMRSNSMSLDQTPLFVWSVAITALLLPVLPFVLFVLKSLFGPSLVRGVTYLNSAGGGDPILYQHLFWFFGH 240
Cdd:MTH00077  161 AINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGH 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 241 PEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKV 320
Cdd:MTH00077  241 PEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 321 FSWMATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLF 400
Cdd:MTH00077  321 FSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLF 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 401 TGLTMNNKWLKIQFTIMFFGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIMSIIMFIMIMWESMIKNR 480
Cdd:MTH00077  401 SGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKR 480

                         490       500
                  ....*....|....*....|....*..
gi 1824665928 481 TIIFSMNMSSSTEWLQNNPPAEHSYSE 507
Cdd:MTH00077  481 EVLTTELTSTNIEWLHGCPPPYHTFEE 507
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-511 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 691.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928   1 MLSQKWLFSTNHKDIGTLYFMFGAWAGMIGTSMSMIIRAELGQPGSMIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGN 80
Cdd:MTH00183    1 MAITRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928  81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSLILLLSSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGISSILG 160
Cdd:MTH00183   81 WLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 161 AVNFITTTTNMRSNSMSLDQTPLFVWSVAITALLLPVLPFVLFVLKSLFGPSLVRGVTYLNSAGGGDPILYQHLFWFFGH 240
Cdd:MTH00183  161 AINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 241 PEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKV 320
Cdd:MTH00183  241 PEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 321 FSWMATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLF 400
Cdd:MTH00183  321 FSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLF 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 401 TGLTMNNKWLKIQFTIMFFGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIMSIIMFIMIMWESMIKNR 480
Cdd:MTH00183  401 SGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKR 480

                         490       500       510
                  ....*....|....*....|....*....|.
gi 1824665928 481 TIIFSMNMSSSTEWLQNNPPAEHSYSELPLI 511
Cdd:MTH00183  481 EVLSVELTSTNVEWLHGCPPPYHTFEEPAFV 511
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-510 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 683.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928   1 MLSQKWLFSTNHKDIGTLYFMFGAWAGMIGTSMSMIIRAELGQPGSMIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGN 80
Cdd:MTH00037    1 MQLSRWLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928  81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSLILLLSSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGISSILG 160
Cdd:MTH00037   81 WLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 161 AVNFITTTTNMRSNSMSLDQTPLFVWSVAITALLLPVLPFVLFVLKSLFGPSLVRGVTYLNSAGGGDPILYQHLFWFFGH 240
Cdd:MTH00037  161 SINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGH 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 241 PEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKV 320
Cdd:MTH00037  241 PEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 321 FSWMATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLF 400
Cdd:MTH00037  321 FSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLF 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 401 TGLTMNNKWLKIQFTIMFFGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIMSIIMFIMIMWESMIKNR 480
Cdd:MTH00037  401 SGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQR 480

                         490       500       510
                  ....*....|....*....|....*....|.
gi 1824665928 481 TIIFSMNMSSSTEWLQNN-PPAEHSYSELPL 510
Cdd:MTH00037  481 EVISPEFSSSSLEWQYSSfPPSHHTFDETPS 511
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 5-511 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 678.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928   5 KWLFSTNHKDIGTLYFMFGAWAGMIGTSMSMIIRAELGQPGSMIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWLVP 84
Cdd:MTH00007    2 RWLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928  85 LMIGAPDMAFPRMNNMSFWLLPPSLILLLSSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGISSILGAVNF 164
Cdd:MTH00007   82 LMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 165 ITTTTNMRSNSMSLDQTPLFVWSVAITALLLPVLPFVLFVLKSLFGPSLVRGVTYLNSAGGGDPILYQHLFWFFGHPEVY 244
Cdd:MTH00007  162 ITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 245 ILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWM 324
Cdd:MTH00007  242 ILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 325 ATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLT 404
Cdd:MTH00007  322 ATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLT 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 405 MNNKWLKIQFTIMFFGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIMSIIMFIMIMWESMIKNRTIIF 484
Cdd:MTH00007  402 LHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIA 481

                         490       500
                  ....*....|....*....|....*..
gi 1824665928 485 SMNMSSSTEWLQNNPPAEHSYSELPLI 511
Cdd:MTH00007  482 SPHMSSSLEWQDTLPLDFHNLPETGII 508
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 5-513 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 620.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928   5 KWLFSTNHKDIGTLYFMFGAWAGMIGTSMSMIIRAELGQPGSMIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWLVP 84
Cdd:MTH00182    7 RWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928  85 LMIGAPDMAFPRMNNMSFWLLPPSLILLLSSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGISSILGAVNF 164
Cdd:MTH00182   87 LYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINF 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 165 ITTTTNMRSNSMSLDQTPLFVWSVAITALLLPVLPFVLFVLKSLFGPSLVRGVTYLNSAGGGDPILYQHLFWFFGHPEVY 244
Cdd:MTH00182  167 ITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVY 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 245 ILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWM 324
Cdd:MTH00182  247 ILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 325 ATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLT 404
Cdd:MTH00182  327 ATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYC 406

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 405 MNNKWLKIQFTIMFFGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIMSIIMFIMIMWESMIKNRTIIF 484
Cdd:MTH00182  407 YNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKFIG 486

                         490       500       510
                  ....*....|....*....|....*....|...
gi 1824665928 485 SMNMS----SSTEWLQNNPPAEHSYSELPLINK 513
Cdd:MTH00182  487 WKEGTgeswASLEWVHSSPPLFHTYNELPFVYK 519
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 5-513 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 616.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928   5 KWLFSTNHKDIGTLYFMFGAWAGMIGTSMSMIIRAELGQPGSMIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWLVP 84
Cdd:MTH00184    7 RWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928  85 LMIGAPDMAFPRMNNMSFWLLPPSLILLLSSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGISSILGAVNF 164
Cdd:MTH00184   87 LYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNF 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 165 ITTTTNMRSNSMSLDQTPLFVWSVAITALLLPVLPFVLFVLKSLFGPSLVRGVTYLNSAGGGDPILYQHLFWFFGHPEVY 244
Cdd:MTH00184  167 ITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVY 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 245 ILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWM 324
Cdd:MTH00184  247 ILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWI 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 325 ATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLT 404
Cdd:MTH00184  327 ATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYC 406

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 405 MNNKWLKIQFTIMFFGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIMSIIMFIMIMWESMIKNRTIIF 484
Cdd:MTH00184  407 YNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVREIKFVG 486

                         490       500       510
                  ....*....|....*....|....*....|..
gi 1824665928 485 SMN---MSSSTEWLQNNPPAEHSYSELPLINK 513
Cdd:MTH00184  487 WVEdsgHYPSLEWAQTSPPAHHTYNELPYVYK 518
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 6-507 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 614.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928   6 WLFSTNHKDIGTLYFMFGAWAGMIGTSMSMIIRAELGQPGSMIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWLVPL 85
Cdd:MTH00079    7 WLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928  86 MIGAPDMAFPRMNNMSFWLLPPSLILLLSSSMVDSGAGTGWTVYPPLAgAIAHGGSSVDLAIFSLHLAGISSILGAVNFI 165
Cdd:MTH00079   87 MLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGINFM 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 166 TTTTNMRSNSMSLDQTPLFVWSVAITALLLPVLPFVLFVLKSLFGPSLVRGVTYLNSAGGGDPILYQHLFWFFGHPEVYI 245
Cdd:MTH00079  166 VTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYI 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 246 LILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMA 325
Cdd:MTH00079  246 LILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLA 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 326 TLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTM 405
Cdd:MTH00079  326 TLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVY 405

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 406 NNKWLKIQFTIMFFGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIMSIIMFIMIMWESMIKNRTIIFS 485
Cdd:MTH00079  406 DKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLHD 485

                         490       500
                  ....*....|....*....|..
gi 1824665928 486 MNMSSSTEWLQNNPPAEHSYSE 507
Cdd:MTH00079  486 NYINSSPEYSLSSYVFGHSYQS 507
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 5-511 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 543.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928   5 KWLFSTNHKDIGTLYFMFGAWAGMIGTSMSMIIRAELGQPGSMIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWLVP 84
Cdd:MTH00026    6 RWFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928  85 LMIGAPDMAFPRMNNMSFWLLPPSLILLLSSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGISSILGAVNF 164
Cdd:MTH00026   86 LMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNF 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 165 ITTTTNMRSNSMSLDQTPLFVWSVAITALLLPVLPFVLFVLKSLFGPSLVRGVTYLNSAGGGDPILYQHLFWFFGHPEVY 244
Cdd:MTH00026  166 ITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVY 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 245 ILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWM 324
Cdd:MTH00026  246 ILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWL 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 325 ATLYGT--KFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTG 402
Cdd:MTH00026  326 ATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITG 405

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 403 LTMNNKWLKIQFTIMFFGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIMSIIMFIMIMWES------- 475
Cdd:MTH00026  406 YAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAyyreepf 485

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 1824665928 476 ----MIKNRTIIFSMNMS--SSTEWLQNNPPAEHSYSELPLI 511
Cdd:MTH00026  486 diniMAKGPLIPFSCQPAhfDTLEWSLTSPPEHHTYNELPYI 527
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 12-452 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.


Pssm-ID: 238461  Cd Length: 463  Bit Score: 532.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928  12 HKDIGTLYFMFGAWAGMIGTSMSMIIRAELGQPGSMIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWLVPlMIGAPD 91
Cdd:cd00919     1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928  92 MAFPRMNNMSFWLLPPSLILLLSSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGISSILGAVNFITTTTNM 171
Cdd:cd00919    80 LAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNM 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 172 RSNSMSLDQTPLFVWSVAITALLLPVLPFVLFVLKSLFGPSLVRGVTYLNSAGGGDPILYQHLFWFFGHPEVYILILPGF 251
Cdd:cd00919   160 RAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAF 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 252 GIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMATLYGTK 331
Cdd:cd00919   240 GAISEIIPTFSGK-PLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGR 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 332 FKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNKWLK 411
Cdd:cd00919   319 IRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGK 398

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1824665928 412 IQFTIMFFGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNV 452
Cdd:cd00919   399 IHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNF 439
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 7-452 1.75e-173

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: 498.29  E-value: 1.75e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928   7 LFSTNHKDIGTLYFMFGAWAGMIGTSMSMIIRAELGQPGSMIGDDQIYNVIITAHAFVMIFFMVMPIMiGGFGNWLVPLM 86
Cdd:TIGR02891   1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928  87 IGAPDMAFPRMNNMSFWLLPPSLILLLSSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGISSILGAVNFIT 166
Cdd:TIGR02891  80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 167 TTTNMRSNSMSLDQTPLFVWSVAITALLLPVLPFVLFVLKSLFGPSLVRGVTYLNSAGGGDPILYQHLFWFFGHPEVYIL 246
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 247 ILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMAT 326
Cdd:TIGR02891 240 FLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 327 LYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMN 406
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1824665928 407 NKWLKIQFTIMFFGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTSWNV 452
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNL 446
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
5-452 3.44e-173

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 498.88  E-value: 3.44e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928   5 KWLFSTNHKDIGTLYFMFGAWAGMIGTSMSMIIRAELGQPGSMIGDDQIYNVIITAHAFVMIFFMVMPiMIGGFGNWLVP 84
Cdd:COG0843     8 RWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928  85 LMIGAPDMAFPRMNNMSFWLLPPSLILLLSSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGISSILGAVNF 164
Cdd:COG0843    87 LQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNF 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 165 ITTTTNMRSNSMSLDQTPLFVWSVAITALLLPVLPFVLFVLKSLFGPSLVRGVTYLNSAGGGDPILYQHLFWFFGHPEVY 244
Cdd:COG0843   167 IVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVY 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 245 ILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWM 324
Cdd:COG0843   247 ILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWI 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 325 ATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLT 404
Cdd:COG0843   326 ATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRM 405

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1824665928 405 MNNKWLKIQFTIMFFGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTSWNV 452
Cdd:COG0843   406 LNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNL 455
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 6-452 6.36e-151

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: 440.86  E-value: 6.36e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928   6 WLFSTNHKDIGTLYFMFGAWAGMIGTSMSMIIRAELGQPGSMIGDDQIYNVIITAHAFVMIFFMVMPIMIGgFGNWLVPL 85
Cdd:cd01662     1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928  86 MIGAPDMAFPRMNNMSFWLLPPSLILLLSSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGISSILGAVNFI 165
Cdd:cd01662    80 QIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 166 TTTTNMRSNSMSLDQTPLFVWSVAITALLLPVLPFVLFVLKSLFGPSLVRGVTYLNSAGGGDPILYQHLFWFFGHPEVYI 245
Cdd:cd01662   160 VTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 246 LILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMA 325
Cdd:cd01662   240 LILPAFGIFSEIVPTFSRK-PLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLF 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 326 TLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTM 405
Cdd:cd01662   319 TMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRML 398

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 1824665928 406 NNKWLKIQFTIMFFGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTSWNV 452
Cdd:cd01662   399 NERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNL 447
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 6-504 5.84e-149

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 436.03  E-value: 5.84e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928   6 WLFSTNHKDIGTLYFMFGAWAGMIGTSMSMIIRAELGQPGSMIGDDQIYNVIITAHAFVMIFFMVMPIMIGGFGNWLVPL 85
Cdd:MTH00048    7 WLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928  86 MIGAPDMAFPRMNNMSFWLLPPSLILLLSSSMVdsGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGISSILGAVNFI 165
Cdd:MTH00048   87 LLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFI 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 166 TTTTNMRSNSMSLdQTPLFVWSVAITALLLPVLPfvlfvlkslfgPSLVRGVTYL-----------NSAGGGDPILYQHL 234
Cdd:MTH00048  165 CTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSL-----------PVLAAAITMLlfdrnfgsaffDPLGGGDPVLFQHM 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 235 FWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAV 314
Cdd:MTH00048  233 FWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGV 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 315 PTGIKVFSWMATLYGTKFKFNPPLL-WALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGI 393
Cdd:MTH00048  313 PTGIKVFSWLYMLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMF 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 394 IQWYPLFTGLTMNNKWLKIQFTIMFFGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIMSIIMFIMIMW 473
Cdd:MTH00048  393 IWWWPLITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILW 472

                         490       500       510
                  ....*....|....*....|....*....|.
gi 1824665928 474 ESMIKNRTIIFSMNMSSSTEWLQNNPPAEHS 504
Cdd:MTH00048  473 ESLVVKNEVLGLWGSSSCVVNVLMSPVPYHN 503
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 14-452 1.20e-124

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: 371.14  E-value: 1.20e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928  14 DIGTLYFMFGAWAGMIGTSMSMIIRAELGQPGSMIGDDQIYNVIITAHAFVMIFFMVMPiMIGGFGNWLVPLMIGAPDMA 93
Cdd:pfam00115   1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928  94 FPRMNNMSFWLLPPSLILLLSSSMvdsGAGTGWTVYPPLAGaiahggssVDLAIFSLHLAGISSILGAVNFITTTTNMRS 173
Cdd:pfam00115  80 FPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 174 NSMSLdQTPLFVWSVAITALLLPVLPFvlfvlkSLFGPSLVRGVTYLNSAGGGDPILYQHLFWFFGHPEVYILILPGFGI 253
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFP------VLAAALLLLLLDRSLGAGGGDPLLDQHLFWWFGHPEVYILILPAFGI 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 254 ISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMATLYGTKFK 333
Cdd:pfam00115 222 IYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 334 FN-PPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNKWLKI 412
Cdd:pfam00115 301 FRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1824665928 413 QFTIMFFGVNLTFFPQHFLGLAGMPRRYS----DYPDAYTSWNV 452
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNW 424
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 2-512 7.11e-98

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: 309.09  E-value: 7.11e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928   2 LSQKWLFSTNHKDIGTLYFMFGAWAGMIGTSMSMIIRAELGQPGSMIGDDQIYNVIITAHAFVMIFFMVMPIMIGgFGNW 81
Cdd:TIGR02882  40 LWNEWLTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNI 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928  82 LVPLMIGAPDMAFPRMNNMSFWLLPPSLILLLSSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGISSILGA 161
Cdd:TIGR02882 119 VVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTG 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 162 VNFITTTTNMRSNSMSLDQTPLFVWSVAITALLLPVLPFVLFVLKSLFGPSLVRGVTYLNSAGGGDPILYQHLFWFFGHP 241
Cdd:TIGR02882 199 INFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHP 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 242 EVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVF 321
Cdd:TIGR02882 279 EVYIVILPAFGIYSEIISTFAQK-RLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIF 357

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 322 SWMATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFT 401
Cdd:TIGR02882 358 NWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMF 437

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 402 GLTMNNKWLKIQFTIMFFGVNLTFFPQHFLGLAGMPRRYSDY--PDAYTSWNVISSIGSTISIMSIIMFIMIMWESMIKN 479
Cdd:TIGR02882 438 GYKLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYspSDGWFPLNLISTIGALLMAIGFIFLVYNIYYSHRKS 517

                         490       500       510
                  ....*....|....*....|....*....|....
gi 1824665928 480 RTIIFSMNMSSST-EWLQNNPPAEHSYSELPLIN 512
Cdd:TIGR02882 518 PREATGDPWNGRTlEWATASPPPKYNFAVTPDVN 551
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 2-445 1.51e-92

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 295.69  E-value: 1.51e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928   2 LSQKWLFSTNHKDIGTLYFMFGAWAGMIGTSMSMIIR-----AELGQPGSMigDDQIYNVIITAHAFVMIFFMVMPIMIG 76
Cdd:PRK15017   44 LWKEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRsqqalASAGEAGFL--PPHHYDQIFTAHGVIMIFFVAMPFVIG 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928  77 gFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLILLLSSSMVDSGAGTGWTVYPPLAGAIAHGGSSVDLAIFSLHLAGIS 156
Cdd:PRK15017  122 -LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIG 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 157 SILGAVNFITTTTNMRSNSMSLDQTPLFVWSVAITALLLPVLPFVLFVLKSLFGPSLVRGVTYLNSAGGGDPILYQHLFW 236
Cdd:PRK15017  201 TTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIW 280

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 237 FFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPT 316
Cdd:PRK15017  281 AWGHPEVYILILPVFGVFSEIAATFSRK-RLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPT 359

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 317 GIKVFSWMATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQW 396
Cdd:PRK15017  360 GVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYW 439

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 1824665928 397 YPLFTGLTMNNKWLKIQFTIMFFGVNLTFFPQHFLGLAGMPRRYSDYPD 445
Cdd:PRK15017  440 WPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQID 488
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 227-450 1.82e-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: 78.87  E-value: 1.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 227 DPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGkIESFGTLGMIYAMLSIGLMGFIVWAHHMFT-VGMDVDTRAYF 305
Cdd:cd01660   200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAG-GKLFSDPLARLAFILFLLFSTPVGFHHQFAdPGIGPGWKFIH 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 306 TSATMIIAVPTGIKVFSWMATL-YGTKFKFNPPLLW---------------ALGFIFlFTIGGLTGLVLANSSLDIVLHD 369
Cdd:cd01660   279 MVLTFMVALPSLLTAFTVFASLeIAGRLRGGKGLFGwiralpwgdpmflalFLAMLM-FIPGGAGGIINASYQLNYVVHN 357

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824665928 370 TYYVVAHFHyvLSMGAVFAIMG-GIIQWY-PLFTGLTMNNKWL-KIQFTIMFFGVNLTFFPQHFLGLAGMPRR--YSDYP 444
Cdd:cd01660   358 TAWVPGHFH--LTVGGAVALTFmAVAYWLvPHLTGRELAAKRLaLAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYG 435


                  ....*...
gi 1824665928 445 D--AYTSW 450
Cdd:cd01660   436 GlpAAGEW 443
 
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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