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Conserved domains on  [gi|1896069569|gb|QNJ46940|]
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cytochrome c oxidase subunit I, partial (mitochondrion) [Monistria consobrina]

Protein Classification

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
6-516 0e+00

cytochrome c oxidase subunit I; Provisional


:

Pssm-ID: 177210  Cd Length: 511  Bit Score: 1029.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569   6 PNKWLFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWL 85
Cdd:MTH00153    1 MNKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569  86 VPLMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAV 165
Cdd:MTH00153   81 VPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 166 NFITTSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 245
Cdd:MTH00153  161 NFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 246 VYILILPGFGIISHIVCQESGKIESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFS 325
Cdd:MTH00153  241 VYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 326 WLATLYGTKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTG 405
Cdd:MTH00153  321 WLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTG 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 406 MTLNNKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDSYTKWNVISSIGSTISIVGIILFIVILWESMISKREV 485
Cdd:MTH00153  401 LTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPV 480
                         490       500       510
                  ....*....|....*....|....*....|.
gi 1896069569 486 MFSKNMTSSNEWLQNKPPAEHSYSELPLISS 516
Cdd:MTH00153  481 LFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
6-516 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 1029.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569   6 PNKWLFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWL 85
Cdd:MTH00153    1 MNKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569  86 VPLMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAV 165
Cdd:MTH00153   81 VPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 166 NFITTSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 245
Cdd:MTH00153  161 NFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 246 VYILILPGFGIISHIVCQESGKIESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFS 325
Cdd:MTH00153  241 VYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 326 WLATLYGTKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTG 405
Cdd:MTH00153  321 WLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTG 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 406 MTLNNKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDSYTKWNVISSIGSTISIVGIILFIVILWESMISKREV 485
Cdd:MTH00153  401 LTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPV 480
                         490       500       510
                  ....*....|....*....|....*....|.
gi 1896069569 486 MFSKNMTSSNEWLQNKPPAEHSYSELPLISS 516
Cdd:MTH00153  481 LFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
13-499 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: 868.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569  13 TNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGA 92
Cdd:cd01663     1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569  93 PDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAVNFITTSI 172
Cdd:cd01663    81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 173 NMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 252
Cdd:cd01663   161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 253 GFGIISHIVCQESGKIESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYG 332
Cdd:cd01663   241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 333 TKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGMTLNNKW 412
Cdd:cd01663   321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 413 LKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDSYTKWNVISSIGSTISIVGIILFIVILWESMISKREVMFSKNMT 492
Cdd:cd01663   401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGEG 480

                  ....*...
gi 1896069569 493 SSN-EWLQ 499
Cdd:cd01663   481 STSlEWTL 488
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
8-516 0e+00

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 562.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569   8 KWLFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPiMIGGFGNWLVP 87
Cdd:COG0843     8 RWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVP 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569  88 LMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAVNF 167
Cdd:COG0843    87 LQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNF 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 168 ITTSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 247
Cdd:COG0843   167 IVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVY 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 248 ILILPGFGIISHIVCQESGKiESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 327
Cdd:COG0843   247 ILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWI 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 328 ATLYGTKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGMT 407
Cdd:COG0843   326 ATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRM 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 408 LNNKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYP--DSYTKWNVISSIGSTISIVGIILFIVILWESMISKREV 485
Cdd:COG0843   406 LNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPKA 485
                         490       500       510
                  ....*....|....*....|....*....|...
gi 1896069569 486 mfSKNMTSSN--EWLQNKPPAEHSYSELPLISS 516
Cdd:COG0843   486 --GGNPWGARtlEWATPSPPPLYNFASIPVVRS 516
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
10-508 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: 561.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569  10 LFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMiGGFGNWLVPLM 89
Cdd:TIGR02891   1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569  90 IGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAVNFIT 169
Cdd:TIGR02891  80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 170 TSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 249
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 250 ILPGFGIISHIVCQESGKiESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLAT 329
Cdd:TIGR02891 240 FLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 330 LYGTKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGMTLN 409
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 410 NKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDS--YTKWNVISSIGSTISIVGIILFIVILWESMISKREVMF 487
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGA 478
                         490       500
                  ....*....|....*....|.
gi 1896069569 488 SKNMTSSNEWLQNKPPAEHSY 508
Cdd:TIGR02891 479 NPWGATTLEWTTSSPPPAHNF 499
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
17-445 1.76e-134

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: 396.56  E-value: 1.76e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569  17 DIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPiMIGGFGNWLVPLMIGAPDMA 96
Cdd:pfam00115   1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569  97 FPRMNNMSFWLLPPSLTLLISSsmvDMGAGTGWTVYPPLAGpiahgggsVDLAIFSLHLAGVSSILGAVNFITTSINMRP 176
Cdd:pfam00115  80 FPRLNALSFWLVVLGAVLLLAS---FGGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 177 SGMSLdQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGI 256
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 257 ISHIVCQESGKiESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKLK 336
Cdd:pfam00115 222 IYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 337 FN-PALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGMTLNNKWLKI 415
Cdd:pfam00115 301 FRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
                         410       420       430
                  ....*....|....*....|....*....|
gi 1896069569 416 QFIIMFIGVNMTFFPQHFLGLAGMPRRYSD 445
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAP 410
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
6-516 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 1029.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569   6 PNKWLFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWL 85
Cdd:MTH00153    1 MNKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569  86 VPLMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAV 165
Cdd:MTH00153   81 VPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 166 NFITTSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 245
Cdd:MTH00153  161 NFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 246 VYILILPGFGIISHIVCQESGKIESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFS 325
Cdd:MTH00153  241 VYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 326 WLATLYGTKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTG 405
Cdd:MTH00153  321 WLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTG 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 406 MTLNNKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDSYTKWNVISSIGSTISIVGIILFIVILWESMISKREV 485
Cdd:MTH00153  401 LTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPV 480
                         490       500       510
                  ....*....|....*....|....*....|.
gi 1896069569 486 MFSKNMTSSNEWLQNKPPAEHSYSELPLISS 516
Cdd:MTH00153  481 LFSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
13-499 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: 868.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569  13 TNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLVPLMIGA 92
Cdd:cd01663     1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569  93 PDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAVNFITTSI 172
Cdd:cd01663    81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 173 NMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 252
Cdd:cd01663   161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 253 GFGIISHIVCQESGKIESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYG 332
Cdd:cd01663   241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 333 TKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGMTLNNKW 412
Cdd:cd01663   321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 413 LKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDSYTKWNVISSIGSTISIVGIILFIVILWESMISKREVMFSKNMT 492
Cdd:cd01663   401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGEG 480

                  ....*...
gi 1896069569 493 SSN-EWLQ 499
Cdd:cd01663   481 STSlEWTL 488
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
7-514 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 859.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569   7 NKWLFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLV 86
Cdd:MTH00167    4 NRWLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569  87 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAVN 166
Cdd:MTH00167   84 PLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSIN 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 167 FITTSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 246
Cdd:MTH00167  164 FITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 247 YILILPGFGIISHIVCQESGKIESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 326
Cdd:MTH00167  244 YILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 327 LATLYGTKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGM 406
Cdd:MTH00167  324 LATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGL 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 407 TLNNKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDSYTKWNVISSIGSTISIVGIILFIVILWESMISKREVM 486
Cdd:MTH00167  404 TLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLL 483
                         490       500
                  ....*....|....*....|....*...
gi 1896069569 487 FSKNMTSSNEWLQNKPPAEHSYSELPLI 514
Cdd:MTH00167  484 PVELTSTNVEWLHGCPPPHHTWEEPPFV 511
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
7-514 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 857.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569   7 NKWLFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLV 86
Cdd:MTH00116    4 TRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569  87 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAVN 166
Cdd:MTH00116   84 PLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAIN 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 167 FITTSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 246
Cdd:MTH00116  164 FITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 247 YILILPGFGIISHIVCQESGKIESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 326
Cdd:MTH00116  244 YILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSW 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 327 LATLYGTKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGM 406
Cdd:MTH00116  324 LATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGY 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 407 TLNNKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDSYTKWNVISSIGSTISIVGIILFIVILWESMISKREVM 486
Cdd:MTH00116  404 TLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVL 483
                         490       500
                  ....*....|....*....|....*...
gi 1896069569 487 FSKNMTSSNEWLQNKPPAEHSYSELPLI 514
Cdd:MTH00116  484 QPELTTTNIEWIHGCPPPYHTFEEPAFV 511
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
7-514 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 846.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569   7 NKWLFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLV 86
Cdd:MTH00142    2 MRWLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569  87 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAVN 166
Cdd:MTH00142   82 PLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAIN 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 167 FITTSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 246
Cdd:MTH00142  162 FITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 247 YILILPGFGIISHIVCQESGKIESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 326
Cdd:MTH00142  242 YILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSW 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 327 LATLYGTKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGM 406
Cdd:MTH00142  322 LATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGL 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 407 TLNNKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDSYTKWNVISSIGSTISIVGIILFIVILWESMISKREVM 486
Cdd:MTH00142  402 TLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVM 481
                         490       500
                  ....*....|....*....|....*...
gi 1896069569 487 FSKNMTSSNEWLQNKPPAEHSYSELPLI 514
Cdd:MTH00142  482 WSSHLSTSLEWSHRLPPDFHTYDELPIL 509
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
8-514 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 846.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569   8 KWLFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLVP 87
Cdd:MTH00223    2 RWLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569  88 LMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAVNF 167
Cdd:MTH00223   82 LMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 168 ITTSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 247
Cdd:MTH00223  162 ITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 248 ILILPGFGIISHIVCQESGKIESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 327
Cdd:MTH00223  242 ILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 328 ATLYGTKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGMT 407
Cdd:MTH00223  322 ATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVT 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 408 LNNKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDSYTKWNVISSIGSTISIVGIILFIVILWESMISKREVMF 487
Cdd:MTH00223  402 LHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVW 481
                         490       500
                  ....*....|....*....|....*..
gi 1896069569 488 SKNMTSSNEWLQNKPPAEHSYSELPLI 514
Cdd:MTH00223  482 SGHLSTSLEWDNLLPADFHNNSETGAL 508
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
7-516 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 777.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569   7 NKWLFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLV 86
Cdd:MTH00103    4 NRWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569  87 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAVN 166
Cdd:MTH00103   84 PLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAIN 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 167 FITTSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 246
Cdd:MTH00103  164 FITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 247 YILILPGFGIISHIVCQESGKIESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 326
Cdd:MTH00103  244 YILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSW 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 327 LATLYGTKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGM 406
Cdd:MTH00103  324 LATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGY 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 407 TLNNKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDSYTKWNVISSIGSTISIVGIILFIVILWESMISKREVM 486
Cdd:MTH00103  404 TLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVL 483
                         490       500       510
                  ....*....|....*....|....*....|
gi 1896069569 487 FSKNMTSSNEWLQNKPPAEHSYSELPLISS 516
Cdd:MTH00103  484 TVELTTTNLEWLHGCPPPYHTFEEPTYVKL 513
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
8-514 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 765.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569   8 KWLFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLVP 87
Cdd:MTH00183    5 RWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569  88 LMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAVNF 167
Cdd:MTH00183   85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINF 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 168 ITTSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 247
Cdd:MTH00183  165 ITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVY 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 248 ILILPGFGIISHIVCQESGKIESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 327
Cdd:MTH00183  245 ILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWL 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 328 ATLYGTKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGMT 407
Cdd:MTH00183  325 ATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYT 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 408 LNNKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDSYTKWNVISSIGSTISIVGIILFIVILWESMISKREVMF 487
Cdd:MTH00183  405 LHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLS 484
                         490       500
                  ....*....|....*....|....*..
gi 1896069569 488 SKNMTSSNEWLQNKPPAEHSYSELPLI 514
Cdd:MTH00183  485 VELTSTNVEWLHGCPPPYHTFEEPAFV 511
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
5-510 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 760.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569   5 LPNKWLFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNW 84
Cdd:MTH00077    2 MITRWLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNW 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569  85 LVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGA 164
Cdd:MTH00077   82 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 165 VNFITTSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHP 244
Cdd:MTH00077  162 INFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHP 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 245 EVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVF 324
Cdd:MTH00077  242 EVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVF 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 325 SWLATLYGTKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFT 404
Cdd:MTH00077  322 SWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFS 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 405 GMTLNNKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDSYTKWNVISSIGSTISIVGIILFIVILWESMISKRE 484
Cdd:MTH00077  402 GYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKRE 481
                         490       500
                  ....*....|....*....|....*.
gi 1896069569 485 VMFSKNMTSSNEWLQNKPPAEHSYSE 510
Cdd:MTH00077  482 VLTTELTSTNIEWLHGCPPPYHTFEE 507
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
8-516 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 756.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569   8 KWLFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLVP 87
Cdd:MTH00007    2 RWLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569  88 LMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAVNF 167
Cdd:MTH00007   82 LMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 168 ITTSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 247
Cdd:MTH00007  162 ITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 248 ILILPGFGIISHIVCQESGKIESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 327
Cdd:MTH00007  242 ILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 328 ATLYGTKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGMT 407
Cdd:MTH00007  322 ATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLT 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 408 LNNKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDSYTKWNVISSIGSTISIVGIILFIVILWESMISKREVMF 487
Cdd:MTH00007  402 LHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIA 481
                         490       500
                  ....*....|....*....|....*....
gi 1896069569 488 SKNMTSSNEWLQNKPPAEHSYSELPLISS 516
Cdd:MTH00007  482 SPHMSSSLEWQDTLPLDFHNLPETGIITT 510
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
7-513 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 752.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569   7 NKWLFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLV 86
Cdd:MTH00037    4 SRWLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569  87 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAVN 166
Cdd:MTH00037   84 PLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASIN 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 167 FITTSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 246
Cdd:MTH00037  164 FITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEV 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 247 YILILPGFGIISHIVCQESGKIESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 326
Cdd:MTH00037  244 YILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSW 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 327 LATLYGTKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGM 406
Cdd:MTH00037  324 MATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGV 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 407 TLNNKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDSYTKWNVISSIGSTISIVGIILFIVILWESMISKREVM 486
Cdd:MTH00037  404 SLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVI 483
                         490       500
                  ....*....|....*....|....*...
gi 1896069569 487 FSKNMTSSNEWLQNK-PPAEHSYSELPL 513
Cdd:MTH00037  484 SPEFSSSSLEWQYSSfPPSHHTFDETPS 511
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
8-517 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 691.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569   8 KWLFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLVP 87
Cdd:MTH00182    7 RWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVP 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569  88 LMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAVNF 167
Cdd:MTH00182   87 LYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINF 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 168 ITTSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 247
Cdd:MTH00182  167 ITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVY 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 248 ILILPGFGIISHIVCQESGKIESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 327
Cdd:MTH00182  247 ILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 328 ATLYGTKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGMT 407
Cdd:MTH00182  327 ATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYC 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 408 LNNKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDSYTKWNVISSIGSTISIVGIILFIVILWESMISKREVMF 487
Cdd:MTH00182  407 YNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKFIG 486
                         490       500       510
                  ....*....|....*....|....*....|....
gi 1896069569 488 SKNMTSSN----EWLQNKPPAEHSYSELPLISSF 517
Cdd:MTH00182  487 WKEGTGESwaslEWVHSSPPLFHTYNELPFVYKS 520
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
9-510 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 684.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569   9 WLFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLVPL 88
Cdd:MTH00079    7 WLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569  89 MIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGpIAHGGGSVDLAIFSLHLAGVSSILGAVNFI 168
Cdd:MTH00079   87 MLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFM 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 169 TTSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 248
Cdd:MTH00079  166 VTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYI 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 249 LILPGFGIISHIVCQESGKIESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLA 328
Cdd:MTH00079  246 LILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLA 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 329 TLYGTKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGMTL 408
Cdd:MTH00079  326 TLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVY 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 409 NNKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDSYTKWNVISSIGSTISIVGIILFIVILWESMISKREVMFS 488
Cdd:MTH00079  406 DKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLHD 485
                         490       500
                  ....*....|....*....|..
gi 1896069569 489 KNMTSSNEWLQNKPPAEHSYSE 510
Cdd:MTH00079  486 NYINSSPEYSLSSYVFGHSYQS 507
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
8-517 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 683.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569   8 KWLFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLVP 87
Cdd:MTH00184    7 RWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVP 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569  88 LMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAVNF 167
Cdd:MTH00184   87 LYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNF 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 168 ITTSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 247
Cdd:MTH00184  167 ITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVY 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 248 ILILPGFGIISHIVCQESGKIESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 327
Cdd:MTH00184  247 ILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWI 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 328 ATLYGTKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGMT 407
Cdd:MTH00184  327 ATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYC 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 408 LNNKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDSYTKWNVISSIGSTISIVGIILFIVILWESMisKREVMF 487
Cdd:MTH00184  407 YNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAY--VREIKF 484
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 1896069569 488 -----SKNMTSSNEWLQNKPPAEHSYSELPLISSF 517
Cdd:MTH00184  485 vgwveDSGHYPSLEWAQTSPPAHHTYNELPYVYKG 519
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
8-514 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 601.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569   8 KWLFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLVP 87
Cdd:MTH00026    6 RWFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569  88 LMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAVNF 167
Cdd:MTH00026   86 LMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNF 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 168 ITTSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 247
Cdd:MTH00026  166 ITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVY 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 248 ILILPGFGIISHIVCQESGKIESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 327
Cdd:MTH00026  246 ILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWL 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 328 ATLYGT--KLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTG 405
Cdd:MTH00026  326 ATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITG 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 406 MTLNNKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDSYTKWNVISSIGSTISIVGIILFIVILWESMIskREV 485
Cdd:MTH00026  406 YAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAYY--REE 483
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 1896069569 486 MFSKNMTSSN---------------EWLQNKPPAEHSYSELPLI 514
Cdd:MTH00026  484 PFDINIMAKGplipfscqpahfdtlEWSLTSPPEHHTYNELPYI 527
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
15-479 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: 600.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569  15 HKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLVPlMIGAPD 94
Cdd:cd00919     1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569  95 MAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAVNFITTSINM 174
Cdd:cd00919    80 LAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNM 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 175 RPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 254
Cdd:cd00919   160 RAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 255 GIISHIVCQESGKiESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTK 334
Cdd:cd00919   240 GAISEIIPTFSGK-PLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGR 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 335 LKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGMTLNNKWLK 414
Cdd:cd00919   319 IRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGK 398
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1896069569 415 IQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDSYTKWNVISSIGSTISIVGIILFIVILWESM 479
Cdd:cd00919   399 IHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
8-516 0e+00

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 562.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569   8 KWLFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPiMIGGFGNWLVP 87
Cdd:COG0843     8 RWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVP 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569  88 LMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAVNF 167
Cdd:COG0843    87 LQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNF 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 168 ITTSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 247
Cdd:COG0843   167 IVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVY 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 248 ILILPGFGIISHIVCQESGKiESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 327
Cdd:COG0843   247 ILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWI 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 328 ATLYGTKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGMT 407
Cdd:COG0843   326 ATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRM 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 408 LNNKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYP--DSYTKWNVISSIGSTISIVGIILFIVILWESMISKREV 485
Cdd:COG0843   406 LNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPKA 485
                         490       500       510
                  ....*....|....*....|....*....|...
gi 1896069569 486 mfSKNMTSSN--EWLQNKPPAEHSYSELPLISS 516
Cdd:COG0843   486 --GGNPWGARtlEWATPSPPPLYNFASIPVVRS 516
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
10-508 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: 561.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569  10 LFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMiGGFGNWLVPLM 89
Cdd:TIGR02891   1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569  90 IGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAVNFIT 169
Cdd:TIGR02891  80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 170 TSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 249
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 250 ILPGFGIISHIVCQESGKiESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLAT 329
Cdd:TIGR02891 240 FLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 330 LYGTKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGMTLN 409
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 410 NKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDS--YTKWNVISSIGSTISIVGIILFIVILWESMISKREVMF 487
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGA 478
                         490       500
                  ....*....|....*....|.
gi 1896069569 488 SKNMTSSNEWLQNKPPAEHSY 508
Cdd:TIGR02891 479 NPWGATTLEWTTSSPPPAHNF 499
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
9-486 3.08e-177

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 508.45  E-value: 3.08e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569   9 WLFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMIGGFGNWLVPL 88
Cdd:MTH00048    7 WLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569  89 MIGAPDMAFPRMNNMSFWLLPPSLTLLISSsmVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAVNFI 168
Cdd:MTH00048   87 LLGLSDLNLPRLNALSAWLLVPSIVFLLLS--MCLGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFI 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 169 TTSINMRPSGMSLdQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 248
Cdd:MTH00048  165 CTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYV 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 249 LILPGFGIISHIVCQESGKIESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLA 328
Cdd:MTH00048  244 LILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLY 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 329 TLYGTKLKF-NPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGMT 407
Cdd:MTH00048  324 MLLNSRVRKsDPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLS 403
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1896069569 408 LNNKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDSYTKWNVISSIGSTISIVGIILFIVILWESMISKREVM 486
Cdd:MTH00048  404 LNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEVL 482
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
9-508 3.15e-168

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: 485.16  E-value: 3.15e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569   9 WLFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQP-GQFIGDDQiYNVIITSHAFVMIFFMVMPIMIGgFGNWLVP 87
Cdd:cd01662     1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPgNDFLSPEH-YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569  88 LMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGAVNF 167
Cdd:cd01662    79 LQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 168 ITTSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 247
Cdd:cd01662   159 IVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVY 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 248 ILILPGFGIISHIVCQESGKiESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 327
Cdd:cd01662   239 ILILPAFGIFSEIVPTFSRK-PLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWL 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 328 ATLYGTKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGMT 407
Cdd:cd01662   318 FTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRM 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 408 LNNKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYP--DSYTKWNVISSIGSTISIVGIILFIVILWESmISKREV 485
Cdd:cd01662   398 LNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLINVIVS-IRKGKR 476
                         490       500
                  ....*....|....*....|....*
gi 1896069569 486 MFSKNM--TSSNEWLQNKPPAEHSY 508
Cdd:cd01662   477 DATGDPwgARTLEWATSSPPPAYNF 501
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
17-445 1.76e-134

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: 396.56  E-value: 1.76e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569  17 DIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPiMIGGFGNWLVPLMIGAPDMA 96
Cdd:pfam00115   1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569  97 FPRMNNMSFWLLPPSLTLLISSsmvDMGAGTGWTVYPPLAGpiahgggsVDLAIFSLHLAGVSSILGAVNFITTSINMRP 176
Cdd:pfam00115  80 FPRLNALSFWLVVLGAVLLLAS---FGGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 177 SGMSLdQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGI 256
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 257 ISHIVCQESGKiESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKLK 336
Cdd:pfam00115 222 IYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 337 FN-PALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGMTLNNKWLKI 415
Cdd:pfam00115 301 FRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
                         410       420       430
                  ....*....|....*....|....*....|
gi 1896069569 416 QFIIMFIGVNMTFFPQHFLGLAGMPRRYSD 445
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAP 410
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
5-517 1.35e-112

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: 347.61  E-value: 1.35e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569   5 LPNKWLFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTELGQPGQFIGDDQIYNVIITSHAFVMIFFMVMPIMIGgFGNW 84
Cdd:TIGR02882  40 LWNEWLTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNI 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569  85 LVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSILGA 164
Cdd:TIGR02882 119 VVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTG 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 165 VNFITTSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHP 244
Cdd:TIGR02882 199 INFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHP 278
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 245 EVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVF 324
Cdd:TIGR02882 279 EVYIVILPAFGIYSEIISTFAQK-RLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIF 357
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 325 SWLATLYGTKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFT 404
Cdd:TIGR02882 358 NWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMF 437
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 405 GMTLNNKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDY--PDSYTKWNVISSIGSTISIVGIILFIV-ILWESMIS 481
Cdd:TIGR02882 438 GYKLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYspSDGWFPLNLISTIGALLMAIGFIFLVYnIYYSHRKS 517
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 1896069569 482 KREVMFSKNMTSSNEWLQNKPPAEHSYSELPLISSF 517
Cdd:TIGR02882 518 PREATGDPWNGRTLEWATASPPPKYNFAVTPDVNDY 553
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
5-514 4.58e-103

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 323.43  E-value: 4.58e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569   5 LPNKWLFSTNHKDIGTMYFLFGAWAGMVGTSMSMLIRTE--LGQPGQF-IGDDQIYNVIITSHAFVMIFFMVMPIMIGgF 81
Cdd:PRK15017   44 LWKEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQqaLASAGEAgFLPPHHYDQIFTAHGVIMIFFVAMPFVIG-L 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569  82 GNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMVDMGAGTGWTVYPPLAGPIAHGGGSVDLAIFSLHLAGVSSI 161
Cdd:PRK15017  123 MNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTT 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 162 LGAVNFITTSINMRPSGMSLDQTPLFVWSVTITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFF 241
Cdd:PRK15017  203 LTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAW 282
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 242 GHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMMSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGI 321
Cdd:PRK15017  283 GHPEVYILILPVFGVFSEIAATFSRK-RLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGV 361
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 322 KVFSWLATLYGTKLKFNPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYP 401
Cdd:PRK15017  362 KIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWP 441
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 402 LFTGMTLNNKWLKIQFIIMFIGVNMTFFPQHFLGLAGMPRRYSDYPD-SYTKWNVISSIGSTISIVGIILFIVILWesmI 480
Cdd:PRK15017  442 KAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDpQFHTMLMIAASGAALIALGILCQVIQMY---V 518
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 1896069569 481 SKREVMFSKNMTS------SNEWLQNKPPAEHSYSELPLI 514
Cdd:PRK15017  519 SIRDRDQNRDLTGdpwggrTLEWATSSPPPFYNFAVVPHV 558
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
23-479 8.42e-22

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: 98.13  E-value: 8.42e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569  23 FLFGAWAGMvgtsMSMLIRTELGQpgqFIGDDQIYNVIITSHAFVM-IFFMVMPIMigGFGNWLVPLMIGAPDMAfPRMN 101
Cdd:cd01660    17 LLLGGLFGL----LQVLVRTGVFP---LPSSGILYYQGLTLHGVLLaIVFTTFFIM--GFFYAIVARALLRSLFN-RRLA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 102 NMSFWLLppSLTLLISSSMVDMG-AGTGWTVYPPLagpIAHGGGSVDLAIFSLHlagvSSILGAVNFITTSINMRPSGMS 180
Cdd:cd01660    87 WAGFWLM--VIGTVMAAVPILLGqASVLYTFYPPL---QAHPLFYIGAALVVVG----SWISGFAMFVTLWRWKKANPGK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 181 LdqTPLFVWSVTITAILLLLSLPVLAGAITMLLtdrnLNTSFFDpAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHI 260
Cdd:cd01660   158 K--VPLATFMVVTTMILWLVASLGVALEVLFQL----LPWSLGL-VDTVDVLLSRTLFWWFGHPLVYFWLLPAYIAWYTI 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 261 VCQESGkIESFGTLGMIYAMMSIGLMGFIVWAHHMFT-VGMDVDTRAYFTSATMIIAVPTGIKVFSWLAT---------- 329
Cdd:cd01660   231 LPKIAG-GKLFSDPLARLAFILFLLFSTPVGFHHQFAdPGIGPGWKFIHMVLTFMVALPSLLTAFTVFASleiagrlrgg 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 330 --LYG--TKLKF-NPALLWAIGFILLFTIGGLTGLILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFT 404
Cdd:cd01660   310 kgLFGwiRALPWgDPMFLALFLAMLMFIPGGAGGIINASYQLNYVVHNTAWVPGHFHLTVGGAVALTFMAVAYWLVPHLT 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069569 405 GMTLNNKWL-KIQFIIMFIGVNMTFFPQHFLGLAGMPRR--YSDYPDSY-----TKWNVISSIGSTISIVGIILFIVILW 476
Cdd:cd01660   390 GRELAAKRLaLAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGGLPaagewAPYQQLMAIGGTILFVSGALFLYILF 469

                  ...
gi 1896069569 477 ESM 479
Cdd:cd01660   470 RTL 472
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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