NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|330375199|gb|AEC12737|]
View 

cytochrome c oxidase subunit I, partial (mitochondrion) [Filchnerella kukunoris]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
1-511 0e+00

cytochrome c oxidase subunit I; Provisional


:

Pssm-ID: 177210  Cd Length: 511  Bit Score: 993.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199   1 PQKWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMIGGFGNWL 80
Cdd:MTH00153   1 MNKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199  81 VPLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAV 160
Cdd:MTH00153  81 VPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 161 NFITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
Cdd:MTH00153 161 NFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 241 VYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFS 320
Cdd:MTH00153 241 VYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 321 WLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTG 400
Cdd:MTH00153 321 WLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTG 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 401 LTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIIIMWESMISNRAV 480
Cdd:MTH00153 401 LTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPV 480
                        490       500       510
                 ....*....|....*....|....*....|.
gi 330375199 481 MFSSNMSSSTEWLQNNPPAEHSYSELPLISS 511
Cdd:MTH00153 481 LFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
1-511 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 993.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199   1 PQKWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMIGGFGNWL 80
Cdd:MTH00153   1 MNKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199  81 VPLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAV 160
Cdd:MTH00153  81 VPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 161 NFITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
Cdd:MTH00153 161 NFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 241 VYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFS 320
Cdd:MTH00153 241 VYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 321 WLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTG 400
Cdd:MTH00153 321 WLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTG 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 401 LTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIIIMWESMISNRAV 480
Cdd:MTH00153 401 LTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPV 480
                        490       500       510
                 ....*....|....*....|....*....|.
gi 330375199 481 MFSSNMSSSTEWLQNNPPAEHSYSELPLISS 511
Cdd:MTH00153 481 LFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
8-494 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: 837.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199   8 TNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGA 87
Cdd:cd01663    1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199  88 PDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAVNFITTAI 167
Cdd:cd01663   81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 168 NMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 247
Cdd:cd01663  161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 248 GFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYG 327
Cdd:cd01663  241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 328 TKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTW 407
Cdd:cd01663  321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 408 LKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIIIMWESMISNRAVMFSSN-M 486
Cdd:cd01663  401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGeG 480

                 ....*...
gi 330375199 487 SSSTEWLQ 494
Cdd:cd01663  481 STSLEWTL 488
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
5-503 0e+00

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: 537.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199    5 LFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMiGGFGNWLVPLM 84
Cdd:TIGR02891   1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199   85 IGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAVNFIT 164
Cdd:TIGR02891  80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199  165 TAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 244
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199  245 ILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLAT 324
Cdd:TIGR02891 240 FLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199  325 LYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMN 404
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199  405 NTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTSWNVISSIGSTISIVGIIMFIIIMWESMISNRAVMF 482
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGA 478
                         490       500
                  ....*....|....*....|.
gi 330375199  483 SSNMSSSTEWLQNNPPAEHSY 503
Cdd:TIGR02891 479 NPWGATTLEWTTSSPPPAHNF 499
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
3-450 0e+00

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 536.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199   3 KWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPiMIGGFGNWLVP 82
Cdd:COG0843    8 RWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199  83 LMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAVNF 162
Cdd:COG0843   87 LQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNF 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 163 ITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
Cdd:COG0843  167 IVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVY 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 243 ILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 322
Cdd:COG0843  247 ILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWI 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 323 ATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLT 402
Cdd:COG0843  326 ATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRM 405
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 330375199 403 MNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTSWNV 450
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 ...
12-440 1.33e-129

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: 383.85  E-value: 1.33e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199   12 DIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPiMIGGFGNWLVPLMIGAPDMA 91
Cdd:pfam00115   1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199   92 FPRMNNMSFWLLPPSLTLLLTSSMvdsGAGTGWTVYPPLAGaiahggasVDLAIFSLHLAGVSSILGAVNFITTAINMRS 171
Cdd:pfam00115  80 FPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199  172 ESMTLdQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGI 251
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199  252 ISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFK 331
Cdd:pfam00115 222 IYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199  332 FN-PPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKI 410
Cdd:pfam00115 301 FRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
                         410       420       430
                  ....*....|....*....|....*....|
gi 330375199  411 QFAIMFIGVNLTFFPQHFLGLAGMPRRYSD 440
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAP 410
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
1-511 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 993.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199   1 PQKWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMIGGFGNWL 80
Cdd:MTH00153   1 MNKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199  81 VPLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAV 160
Cdd:MTH00153  81 VPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 161 NFITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
Cdd:MTH00153 161 NFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 241 VYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFS 320
Cdd:MTH00153 241 VYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 321 WLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTG 400
Cdd:MTH00153 321 WLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTG 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 401 LTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIIIMWESMISNRAV 480
Cdd:MTH00153 401 LTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPV 480
                        490       500       510
                 ....*....|....*....|....*....|.
gi 330375199 481 MFSSNMSSSTEWLQNNPPAEHSYSELPLISS 511
Cdd:MTH00153 481 LFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
8-494 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: 837.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199   8 TNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGA 87
Cdd:cd01663    1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199  88 PDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAVNFITTAI 167
Cdd:cd01663   81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 168 NMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 247
Cdd:cd01663  161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 248 GFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYG 327
Cdd:cd01663  241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 328 TKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTW 407
Cdd:cd01663  321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 408 LKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIIIMWESMISNRAVMFSSN-M 486
Cdd:cd01663  401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGeG 480

                 ....*...
gi 330375199 487 SSSTEWLQ 494
Cdd:cd01663  481 STSLEWTL 488
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
3-509 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 833.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199   3 KWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMIGGFGNWLVP 82
Cdd:MTH00167   5 RWLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199  83 LMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAVNF 162
Cdd:MTH00167  85 LMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINF 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 163 ITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
Cdd:MTH00167 165 ITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVY 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 243 ILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 322
Cdd:MTH00167 245 ILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 323 ATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLT 402
Cdd:MTH00167 325 ATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLT 404
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 403 MNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIIIMWESMISNRAVMF 482
Cdd:MTH00167 405 LNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLLP 484
                        490       500
                 ....*....|....*....|....*..
gi 330375199 483 SSNMSSSTEWLQNNPPAEHSYSELPLI 509
Cdd:MTH00167 485 VELTSTNVEWLHGCPPPHHTWEEPPFV 511
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
3-509 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 825.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199   3 KWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMIGGFGNWLVP 82
Cdd:MTH00116   5 RWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199  83 LMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAVNF 162
Cdd:MTH00116  85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINF 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 163 ITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
Cdd:MTH00116 165 ITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVY 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 243 ILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 322
Cdd:MTH00116 245 ILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWL 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 323 ATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLT 402
Cdd:MTH00116 325 ATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYT 404
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 403 MNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIIIMWESMISNRAVMF 482
Cdd:MTH00116 405 LHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVLQ 484
                        490       500
                 ....*....|....*....|....*..
gi 330375199 483 SSNMSSSTEWLQNNPPAEHSYSELPLI 509
Cdd:MTH00116 485 PELTTTNIEWIHGCPPPYHTFEEPAFV 511
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
2-509 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 813.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199   2 QKWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMIGGFGNWLV 81
Cdd:MTH00142   2 MRWLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199  82 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAVN 161
Cdd:MTH00142  82 PLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAIN 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 162 FITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
Cdd:MTH00142 162 FITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 242 YILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 321
Cdd:MTH00142 242 YILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSW 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 322 LATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGL 401
Cdd:MTH00142 322 LATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGL 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 402 TMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIIIMWESMISNRAVM 481
Cdd:MTH00142 402 TLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVM 481
                        490       500
                 ....*....|....*....|....*...
gi 330375199 482 FSSNMSSSTEWLQNNPPAEHSYSELPLI 509
Cdd:MTH00142 482 WSSHLSTSLEWSHRLPPDFHTYDELPIL 509
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
3-509 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 810.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199   3 KWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMIGGFGNWLVP 82
Cdd:MTH00223   2 RWLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199  83 LMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAVNF 162
Cdd:MTH00223  82 LMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 163 ITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
Cdd:MTH00223 162 ITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 243 ILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 322
Cdd:MTH00223 242 ILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 323 ATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLT 402
Cdd:MTH00223 322 ATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVT 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 403 MNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIIIMWESMISNRAVMF 482
Cdd:MTH00223 402 LHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVW 481
                        490       500
                 ....*....|....*....|....*..
gi 330375199 483 SSNMSSSTEWLQNNPPAEHSYSELPLI 509
Cdd:MTH00223 482 SGHLSTSLEWDNLLPADFHNNSETGAL 508
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
3-511 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 747.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199   3 KWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMIGGFGNWLVP 82
Cdd:MTH00103   5 RWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199  83 LMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAVNF 162
Cdd:MTH00103  85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINF 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 163 ITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
Cdd:MTH00103 165 ITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVY 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 243 ILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 322
Cdd:MTH00103 245 ILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWL 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 323 ATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLT 402
Cdd:MTH00103 325 ATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYT 404
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 403 MNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIIIMWESMISNRAVMF 482
Cdd:MTH00103 405 LNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVLT 484
                        490       500
                 ....*....|....*....|....*....
gi 330375199 483 SSNMSSSTEWLQNNPPAEHSYSELPLISS 511
Cdd:MTH00103 485 VELTTTNLEWLHGCPPPYHTFEEPTYVKL 513
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
3-509 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 736.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199   3 KWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMIGGFGNWLVP 82
Cdd:MTH00183   5 RWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199  83 LMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAVNF 162
Cdd:MTH00183  85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINF 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 163 ITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
Cdd:MTH00183 165 ITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVY 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 243 ILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 322
Cdd:MTH00183 245 ILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWL 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 323 ATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLT 402
Cdd:MTH00183 325 ATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYT 404
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 403 MNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIIIMWESMISNRAVMF 482
Cdd:MTH00183 405 LHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLS 484
                        490       500
                 ....*....|....*....|....*..
gi 330375199 483 SSNMSSSTEWLQNNPPAEHSYSELPLI 509
Cdd:MTH00183 485 VELTSTNVEWLHGCPPPYHTFEEPAFV 511
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
1-505 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 733.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199   1 PQKWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMIGGFGNWL 80
Cdd:MTH00077   3 ITRWLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199  81 VPLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAV 160
Cdd:MTH00077  83 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 161 NFITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
Cdd:MTH00077 163 NFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPE 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 241 VYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFS 320
Cdd:MTH00077 243 VYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFS 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 321 WLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTG 400
Cdd:MTH00077 323 WLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSG 402
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 401 LTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIIIMWESMISNRAV 480
Cdd:MTH00077 403 YTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREV 482
                        490       500
                 ....*....|....*....|....*
gi 330375199 481 MFSSNMSSSTEWLQNNPPAEHSYSE 505
Cdd:MTH00077 483 LTTELTSTNIEWLHGCPPPYHTFEE 507
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
3-508 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 731.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199   3 KWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMIGGFGNWLVP 82
Cdd:MTH00037   5 RWLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199  83 LMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAVNF 162
Cdd:MTH00037  85 LMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINF 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 163 ITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
Cdd:MTH00037 165 ITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVY 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 243 ILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 322
Cdd:MTH00037 245 ILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWM 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 323 ATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLT 402
Cdd:MTH00037 325 ATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVS 404
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 403 MNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIIIMWESMISNRAVMF 482
Cdd:MTH00037 405 LHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVIS 484
                        490       500
                 ....*....|....*....|....*..
gi 330375199 483 SSNMSSSTEWLQNN-PPAEHSYSELPL 508
Cdd:MTH00037 485 PEFSSSSLEWQYSSfPPSHHTFDETPS 511
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
3-511 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 724.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199   3 KWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMIGGFGNWLVP 82
Cdd:MTH00007   2 RWLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199  83 LMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAVNF 162
Cdd:MTH00007  82 LMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 163 ITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
Cdd:MTH00007 162 ITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 243 ILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 322
Cdd:MTH00007 242 ILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 323 ATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLT 402
Cdd:MTH00007 322 ATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLT 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 403 MNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIIIMWESMISNRAVMF 482
Cdd:MTH00007 402 LHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIA 481
                        490       500
                 ....*....|....*....|....*....
gi 330375199 483 SSNMSSSTEWLQNNPPAEHSYSELPLISS 511
Cdd:MTH00007 482 SPHMSSSLEWQDTLPLDFHNLPETGIITT 510
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
4-505 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 671.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199   4 WLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMIGGFGNWLVPL 83
Cdd:MTH00079   7 WLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199  84 MIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAgAIAHGGASVDLAIFSLHLAGVSSILGAVNFI 163
Cdd:MTH00079  87 MLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGINFM 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 164 TTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 243
Cdd:MTH00079 166 VTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYI 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 244 LILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLA 323
Cdd:MTH00079 246 LILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLA 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 324 TLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTM 403
Cdd:MTH00079 326 TLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVY 405
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 404 NNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIIIMWESMISNRAVMFS 483
Cdd:MTH00079 406 DKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLHD 485
                        490       500
                 ....*....|....*....|..
gi 330375199 484 SNMSSSTEWLQNNPPAEHSYSE 505
Cdd:MTH00079 486 NYINSSPEYSLSSYVFGHSYQS 507
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
3-512 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 660.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199   3 KWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMIGGFGNWLVP 82
Cdd:MTH00182   7 RWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199  83 LMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAVNF 162
Cdd:MTH00182  87 LYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINF 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 163 ITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
Cdd:MTH00182 167 ITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVY 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 243 ILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 322
Cdd:MTH00182 247 ILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 323 ATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLT 402
Cdd:MTH00182 327 ATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYC 406
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 403 MNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIIIMWESMISNRA--- 479
Cdd:MTH00182 407 YNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKfig 486
                        490       500       510
                 ....*....|....*....|....*....|....
gi 330375199 480 -VMFSSNMSSSTEWLQNNPPAEHSYSELPLISSF 512
Cdd:MTH00182 487 wKEGTGESWASLEWVHSSPPLFHTYNELPFVYKS 520
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
3-512 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 654.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199   3 KWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMIGGFGNWLVP 82
Cdd:MTH00184   7 RWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199  83 LMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAVNF 162
Cdd:MTH00184  87 LYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNF 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 163 ITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
Cdd:MTH00184 167 ITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVY 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 243 ILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 322
Cdd:MTH00184 247 ILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWI 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 323 ATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLT 402
Cdd:MTH00184 327 ATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYC 406
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 403 MNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIIIMWESM---ISNRA 479
Cdd:MTH00184 407 YNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYvreIKFVG 486
                        490       500       510
                 ....*....|....*....|....*....|...
gi 330375199 480 VMFSSNMSSSTEWLQNNPPAEHSYSELPLISSF 512
Cdd:MTH00184 487 WVEDSGHYPSLEWAQTSPPAHHTYNELPYVYKG 519
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
3-509 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 575.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199   3 KWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMIGGFGNWLVP 82
Cdd:MTH00026   6 RWFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVP 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199  83 LMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAVNF 162
Cdd:MTH00026  86 LMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNF 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 163 ITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
Cdd:MTH00026 166 ITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVY 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 243 ILILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 322
Cdd:MTH00026 246 ILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWL 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 323 ATLYGT--KFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTG 400
Cdd:MTH00026 326 ATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITG 405
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 401 LTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIIIMWES------- 473
Cdd:MTH00026 406 YAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAyyreepf 485
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|..
gi 330375199 474 ----MISNRAVMFSSNMS--SSTEWLQNNPPAEHSYSELPLI 509
Cdd:MTH00026 486 diniMAKGPLIPFSCQPAhfDTLEWSLTSPPEHHTYNELPYI 527
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
10-450 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: 570.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199  10 HKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMIGGFGNWLVPlMIGAPD 89
Cdd:cd00919    1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199  90 MAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAVNFITTAINM 169
Cdd:cd00919   80 LAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNM 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 170 RSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 249
Cdd:cd00919  160 RAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAF 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 250 GIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTK 329
Cdd:cd00919  240 GAISEIIPTFSGK-PLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGR 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 330 FKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLK 409
Cdd:cd00919  319 IRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGK 398
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 330375199 410 IQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNV 450
Cdd:cd00919  399 IHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNF 439
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
5-503 0e+00

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: 537.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199    5 LFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMiGGFGNWLVPLM 84
Cdd:TIGR02891   1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199   85 IGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAVNFIT 164
Cdd:TIGR02891  80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199  165 TAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 244
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199  245 ILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLAT 324
Cdd:TIGR02891 240 FLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199  325 LYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMN 404
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199  405 NTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTSWNVISSIGSTISIVGIIMFIIIMWESMISNRAVMF 482
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGA 478
                         490       500
                  ....*....|....*....|.
gi 330375199  483 SSNMSSSTEWLQNNPPAEHSY 503
Cdd:TIGR02891 479 NPWGATTLEWTTSSPPPAHNF 499
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
3-450 0e+00

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 536.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199   3 KWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPiMIGGFGNWLVP 82
Cdd:COG0843    8 RWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199  83 LMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAVNF 162
Cdd:COG0843   87 LQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNF 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 163 ITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
Cdd:COG0843  167 IVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVY 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 243 ILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 322
Cdd:COG0843  247 ILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWI 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 323 ATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLT 402
Cdd:COG0843  326 ATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRM 405
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 330375199 403 MNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTSWNV 450
Cdd:COG0843  406 LNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNL 455
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
4-502 2.39e-168

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 485.72  E-value: 2.39e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199   4 WLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMIGGFGNWLVPL 83
Cdd:MTH00048   7 WLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199  84 MIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVdsGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAVNFI 163
Cdd:MTH00048  87 LLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFI 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 164 TTAINMRSESMTLdQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 243
Cdd:MTH00048 165 CTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYV 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 244 LILPGFGIISHIVCQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLA 323
Cdd:MTH00048 244 LILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLY 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 324 TLYGTKFKFNPPLL-WALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLT 402
Cdd:MTH00048 324 MLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLS 403
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 403 MNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIIIMWESMISNRAVMF 482
Cdd:MTH00048 404 LNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEVLG 483
                        490       500
                 ....*....|....*....|
gi 330375199 483 SSNMSSSTEWLQNNPPAEHS 502
Cdd:MTH00048 484 LWGSSSCVVNVLMSPVPYHN 503
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
4-450 2.93e-161

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: 467.06  E-value: 2.93e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199   4 WLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMIGgFGNWLVPL 83
Cdd:cd01662    1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199  84 MIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAVNFI 163
Cdd:cd01662   80 QIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 164 TTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 243
Cdd:cd01662  160 VTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYI 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 244 LILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLA 323
Cdd:cd01662  240 LILPAFGIFSEIVPTFSRK-PLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLF 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 324 TLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTM 403
Cdd:cd01662  319 TMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRML 398
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 330375199 404 NNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTSWNV 450
Cdd:cd01662  399 NERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNL 447
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
12-440 1.33e-129

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: 383.85  E-value: 1.33e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199   12 DIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPiMIGGFGNWLVPLMIGAPDMA 91
Cdd:pfam00115   1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199   92 FPRMNNMSFWLLPPSLTLLLTSSMvdsGAGTGWTVYPPLAGaiahggasVDLAIFSLHLAGVSSILGAVNFITTAINMRS 171
Cdd:pfam00115  80 FPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199  172 ESMTLdQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGI 251
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199  252 ISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFK 331
Cdd:pfam00115 222 IYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199  332 FN-PPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKI 410
Cdd:pfam00115 301 FRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
                         410       420       430
                  ....*....|....*....|....*....|
gi 330375199  411 QFAIMFIGVNLTFFPQHFLGLAGMPRRYSD 440
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAP 410
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
2-512 2.65e-106

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: 331.05  E-value: 2.65e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199    2 QKWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIRAELGQPGQLIGDDQIYNVVITSHAFVMIFFMVMPIMIGgFGNWLV 81
Cdd:TIGR02882  42 NEWLTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVV 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199   82 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSILGAVN 161
Cdd:TIGR02882 121 PLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGIN 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199  162 FITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
Cdd:TIGR02882 201 FFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEV 280
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199  242 YILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 321
Cdd:TIGR02882 281 YIVILPAFGIYSEIISTFAQK-RLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNW 359
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199  322 LATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGL 401
Cdd:TIGR02882 360 LLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGY 439
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199  402 TMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDY--PDAYTSWNVISSIGSTISIVGIIMFIIIMWESMISNRA 479
Cdd:TIGR02882 440 KLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYspSDGWFPLNLISTIGALLMAIGFIFLVYNIYYSHRKSPR 519
                         490       500       510
                  ....*....|....*....|....*....|....
gi 330375199  480 VMFSSNMSSST-EWLQNNPPAEHSYSELPLISSF 512
Cdd:TIGR02882 520 EATGDPWNGRTlEWATASPPPKYNFAVTPDVNDY 553
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
3-443 2.88e-99

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 313.41  E-value: 2.88e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199   3 KWLFSTNHKDIGTLYFLFGAWAGMVGTSMSMIIR-----AELGQPGQLigDDQIYNVVITSHAFVMIFFMVMPIMIGgFG 77
Cdd:PRK15017  47 EWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRsqqalASAGEAGFL--PPHHYDQIFTAHGVIMIFFVAMPFVIG-LM 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199  78 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLLTSSMVDSGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGVSSIL 157
Cdd:PRK15017 124 NLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTL 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 158 GAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFG 237
Cdd:PRK15017 204 TGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWG 283
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 238 HPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIK 317
Cdd:PRK15017 284 HPEVYILILPVFGVFSEIAATFSRK-RLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVK 362
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 318 VFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPL 397
Cdd:PRK15017 363 IFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPK 442
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 330375199 398 FTGLTMNNTWLKIQFAIMFIGVNLTFFPQHFLGLAGMPRRYSDYPD 443
Cdd:PRK15017 443 AFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQID 488
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
225-448 3.07e-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: 78.10  E-value: 3.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 225 DPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGkIESFGTLGMIYAMLSIGLMGFIVWAHHMFT-VGMDVDTRAYF 303
Cdd:cd01660  200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAG-GKLFSDPLARLAFILFLLFSTPVGFHHQFAdPGIGPGWKFIH 278
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 304 TSATMIIAVPTGIKVFSWLATL-YGTKFKFNPPLLW---------------ALGFIFlFTIGGLTGLILANSSLDIVLHD 367
Cdd:cd01660  279 MVLTFMVALPSLLTAFTVFASLeIAGRLRGGKGLFGwiralpwgdpmflalFLAMLM-FIPGGAGGIINASYQLNYVVHN 357
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330375199 368 TYYVVAHFHyvLSMGAVFAIMG-GIIQWY-PLFTGLTMNNTWL-KIQFAIMFIGVNLTFFPQHFLGLAGMPRR--YSDYP 442
Cdd:cd01660  358 TAWVPGHFH--LTVGGAVALTFmAVAYWLvPHLTGRELAAKRLaLAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYG 435

                 ....*...
gi 330375199 443 D--AYTSW 448
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH