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Conserved domains on  [gi|1561324683|gb|QAT77691|]
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cytochrome oxidase subunit I, partial [Sarcophaga seniorwhitei]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-498 0e+00

cytochrome c oxidase subunit I; Provisional


:

Pssm-ID: 177210  Cd Length: 511  Bit Score: 1004.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683   1 GTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIMLGAPDMAFP 80
Cdd:MTH00153   14 GTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFP 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683  81 RMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTG 160
Cdd:MTH00153   94 RMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKG 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 161 ITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 240
Cdd:MTH00153  174 MTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 241 HIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYS 320
Cdd:MTH00153  254 HIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYS 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 321 PATLWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFT 400
Cdd:MTH00153  334 PSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFF 413

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 401 IMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGIIFFFFIIWESFASQRQVMFPVQLNSSIEWL 480
Cdd:MTH00153  414 IMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEWL 493

                         490
                  ....*....|....*...
gi 1561324683 481 QNTPPAEHSYSELPLLTN 498
Cdd:MTH00153  494 QNLPPAEHSYSELPLLTN 511
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-498 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 1004.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683   1 GTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIMLGAPDMAFP 80
Cdd:MTH00153   14 GTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFP 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683  81 RMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTG 160
Cdd:MTH00153   94 RMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKG 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 161 ITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 240
Cdd:MTH00153  174 MTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 241 HIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYS 320
Cdd:MTH00153  254 HIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYS 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 321 PATLWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFT 400
Cdd:MTH00153  334 PSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFF 413

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 401 IMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGIIFFFFIIWESFASQRQVMFPVQLNSSIEWL 480
Cdd:MTH00153  414 IMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEWL 493

                         490
                  ....*....|....*...
gi 1561324683 481 QNTPPAEHSYSELPLLTN 498
Cdd:MTH00153  494 QNLPPAEHSYSELPLLTN 511
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-481 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: 854.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683   1 GTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIMLGAPDMAFP 80
Cdd:cd01663     7 GTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683  81 RMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTG 160
Cdd:cd01663    87 RLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPG 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 161 ITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 240
Cdd:cd01663   167 MTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIIS 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 241 HIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYS 320
Cdd:cd01663   247 HIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFE 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 321 PATLWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFT 400
Cdd:cd01663   327 TPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFW 406

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 401 IMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGIIFFFFIIWESFASQRQVMFPV-QLNSSIEW 479
Cdd:cd01663   407 LMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVgEGSTSLEW 486


                  ..
gi 1561324683 480 LQ 481
Cdd:cd01663   487 TL 488
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-490 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: 533.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683   1 GTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMiGGFGNWLVPIMLGAPDMAFP 80
Cdd:TIGR02891  10 GILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFP 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683  81 RMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTG 160
Cdd:TIGR02891  89 RLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPG 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 161 ITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 240
Cdd:TIGR02891 169 MTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIIS 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 241 HIISQESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYS 320
Cdd:TIGR02891 249 EILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFT 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 321 PATLWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFT 400
Cdd:TIGR02891 328 TPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFW 407

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 401 IMFMGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTAWNVISTIGSTISLLGIIFFFFIIWESFASQRQVMFPVQLNSSIE 478
Cdd:TIGR02891 408 LTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGANPWGATTLE 487

                         490
                  ....*....|..
gi 1561324683 479 WLQNTPPAEHSY 490
Cdd:TIGR02891 488 WTTSSPPPAHNF 499
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-497 0e+00

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 533.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683   1 GTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPiMIGGFGNWLVPIMLGAPDMAFP 80
Cdd:COG0843    19 GIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683  81 RMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTG 160
Cdd:COG0843    98 RLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPG 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 161 ITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 240
Cdd:COG0843   178 MTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVS 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 241 HIISQESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYS 320
Cdd:COG0843   258 EIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFT 336

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 321 PATLWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFT 400
Cdd:COG0843   337 TPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFW 416

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 401 IMFMGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTAWNVISTIGSTISLLGIIFFFFIIWES-FASQRQVMFPVQLNsSI 477
Cdd:COG0843   417 LWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSlRKGPKAGGNPWGAR-TL 495

                         490       500
                  ....*....|....*....|
gi 1561324683 478 EWLQNTPPAEHSYSELPLLT 497
Cdd:COG0843   496 EWATPSPPPLYNFASIPVVR 515
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-445 3.77e-129

Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key enzyme in aerobic metabolism. Proton pumping haem-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-haem a3 (or haem o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxidases (E.C:1.10.3.11), is directly involved in the coupling between dioxygen reduction and proton pumping. Some terminal oxidases generate a transmembrane proton gradient across the plasma membrane (prokaryotes) or the mitochondrial inner membrane (eukaryotes). The enzyme complex consists of 3-4 subunits (prokaryotes) up to 13 polypeptides (mammals) of which only the catalytic subunit (equivalent to mammalian subunit I (COXI) is found in all haem-copper respiratory oxidases. The presence of a bimetallic centre (formed by a high-spin haem and copper B) as well as a low-spin haem, both ligated to six conserved histidine residues near the outer side of four transmembrane spans within CO I is common to all family members.


Pssm-ID: 459678  Cd Length: 432  Bit Score: 381.92  E-value: 3.77e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683   1 GTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPiMIGGFGNWLVPIMLGAPDMAFP 80
Cdd:pfam00115   3 GLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683  81 RMNNMSFWLLPPALTLLLVSSMvenGAGTGWTVYPPLssniahggASVDLAIFSLHLAGISSILGAVNFITTVINMRSTG 160
Cdd:pfam00115  82 RLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPG 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 161 ITFdRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 240
Cdd:pfam00115 151 MTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIY 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 241 HIISQESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLN-Y 319
Cdd:pfam00115 224 YILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRfR 302

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 320 SPATLWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQF 399
Cdd:pfam00115 303 TTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHF 382

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1561324683 400 TIMFMGVNLTFFPQHFLGLAGMPRRYS----DYPDAYTAWNVISTIGSTI 445
Cdd:pfam00115 383 WLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-498 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 1004.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683   1 GTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIMLGAPDMAFP 80
Cdd:MTH00153   14 GTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFP 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683  81 RMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTG 160
Cdd:MTH00153   94 RMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKG 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 161 ITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 240
Cdd:MTH00153  174 MTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 241 HIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYS 320
Cdd:MTH00153  254 HIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYS 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 321 PATLWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFT 400
Cdd:MTH00153  334 PSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFF 413

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 401 IMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGIIFFFFIIWESFASQRQVMFPVQLNSSIEWL 480
Cdd:MTH00153  414 IMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEWL 493

                         490
                  ....*....|....*...
gi 1561324683 481 QNTPPAEHSYSELPLLTN 498
Cdd:MTH00153  494 QNLPPAEHSYSELPLLTN 511
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-481 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: 854.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683   1 GTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIMLGAPDMAFP 80
Cdd:cd01663     7 GTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683  81 RMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTG 160
Cdd:cd01663    87 RLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPG 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 161 ITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 240
Cdd:cd01663   167 MTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIIS 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 241 HIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYS 320
Cdd:cd01663   247 HIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFE 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 321 PATLWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFT 400
Cdd:cd01663   327 TPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFW 406

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 401 IMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGIIFFFFIIWESFASQRQVMFPV-QLNSSIEW 479
Cdd:cd01663   407 LMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVgEGSTSLEW 486


                  ..
gi 1561324683 480 LQ 481
Cdd:cd01663   487 TL 488
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-496 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 828.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683   1 GTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIMLGAPDMAFP 80
Cdd:MTH00167   16 GTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFP 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683  81 RMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTG 160
Cdd:MTH00167   96 RMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPG 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 161 ITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 240
Cdd:MTH00167  176 ITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 241 HIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYS 320
Cdd:MTH00167  256 HIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWE 335

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 321 PATLWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFT 400
Cdd:MTH00167  336 TPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFF 415

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 401 IMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGIIFFFFIIWESFASQRQVMFPVQLNSSIEWL 480
Cdd:MTH00167  416 VMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLLPVELTSTNVEWL 495

                         490
                  ....*....|....*.
gi 1561324683 481 QNTPPAEHSYSELPLL 496
Cdd:MTH00167  496 HGCPPPHHTWEEPPFV 511
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-498 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 822.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683   1 GTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIMLGAPDMAFP 80
Cdd:MTH00116   16 GTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFP 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683  81 RMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTG 160
Cdd:MTH00116   96 RMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPA 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 161 ITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 240
Cdd:MTH00116  176 MSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIIS 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 241 HIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYS 320
Cdd:MTH00116  256 HIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWD 335

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 321 PATLWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFT 400
Cdd:MTH00116  336 PPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFG 415

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 401 IMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGIIFFFFIIWESFASQRQVMFPVQLNSSIEWL 480
Cdd:MTH00116  416 VMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVLQPELTTTNIEWI 495

                         490
                  ....*....|....*...
gi 1561324683 481 QNTPPAEHSYSELPLLTN 498
Cdd:MTH00116  496 HGCPPPYHTFEEPAFVQV 513
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-498 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 819.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683   1 GTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIMLGAPDMAFP 80
Cdd:MTH00142   14 GTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFP 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683  81 RMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTG 160
Cdd:MTH00142   94 RMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGG 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 161 ITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 240
Cdd:MTH00142  174 MKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 241 HIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYS 320
Cdd:MTH00142  254 HIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYE 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 321 PATLWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFT 400
Cdd:MTH00142  334 PPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFY 413

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 401 IMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGIIFFFFIIWESFASQRQVMFPVQLNSSIEWL 480
Cdd:MTH00142  414 TMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVMWSSHLSTSLEWS 493

                         490
                  ....*....|....*...
gi 1561324683 481 QNTPPAEHSYSELPLLTN 498
Cdd:MTH00142  494 HRLPPDFHTYDELPILVV 511
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-494 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 818.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683   1 GTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIMLGAPDMAFP 80
Cdd:MTH00223   13 GTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFP 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683  81 RMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTG 160
Cdd:MTH00223   93 RLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPG 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 161 ITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 240
Cdd:MTH00223  173 MQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 241 HIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYS 320
Cdd:MTH00223  253 HIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYE 332

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 321 PATLWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFT 400
Cdd:MTH00223  333 APMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFF 412

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 401 IMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGIIFFFFIIWESFASQRQVMFPVQLNSSIEWL 480
Cdd:MTH00223  413 LMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVWSGHLSTSLEWD 492

                         490
                  ....*....|....
gi 1561324683 481 QNTPPAEHSYSELP 494
Cdd:MTH00223  493 NLLPADFHNNSETG 506
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-492 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 740.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683   1 GTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIMLGAPDMAFP 80
Cdd:MTH00103   16 GTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFP 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683  81 RMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTG 160
Cdd:MTH00103   96 RMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPA 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 161 ITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 240
Cdd:MTH00103  176 MSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 241 HIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYS 320
Cdd:MTH00103  256 HIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWS 335

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 321 PATLWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFT 400
Cdd:MTH00103  336 PAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFT 415

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 401 IMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGIIFFFFIIWESFASQRQVMFPVQLNSSIEWL 480
Cdd:MTH00103  416 IMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVLTVELTTTNLEWL 495

                         490
                  ....*....|..
gi 1561324683 481 QNTPPAEHSYSE 492
Cdd:MTH00103  496 HGCPPPYHTFEE 507
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-495 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 735.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683   1 GTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIMLGAPDMAFP 80
Cdd:MTH00037   16 GTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFP 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683  81 RMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTG 160
Cdd:MTH00037   96 RMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPG 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 161 ITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 240
Cdd:MTH00037  176 MTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMIS 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 241 HIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYS 320
Cdd:MTH00037  256 HVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWE 335

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 321 PATLWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFT 400
Cdd:MTH00037  336 TPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFF 415

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 401 IMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGIIFFFFIIWESFASQRQVMFPVQLNSSIEWL 480
Cdd:MTH00037  416 LMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVISPEFSSSSLEWQ 495

                         490
                  ....*....|....*.
gi 1561324683 481 QNT-PPAEHSYSELPL 495
Cdd:MTH00037  496 YSSfPPSHHTFDETPS 511
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-492 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 732.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683   1 GTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIMLGAPDMAFP 80
Cdd:MTH00183   16 GTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFP 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683  81 RMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTG 160
Cdd:MTH00183   96 RMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPA 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 161 ITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 240
Cdd:MTH00183  176 ISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 241 HIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYS 320
Cdd:MTH00183  256 HIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWE 335

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 321 PATLWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFT 400
Cdd:MTH00183  336 TPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFG 415

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 401 IMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGIIFFFFIIWESFASQRQVMFPVQLNSSIEWL 480
Cdd:MTH00183  416 VMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLSVELTSTNVEWL 495

                         490
                  ....*....|..
gi 1561324683 481 QNTPPAEHSYSE 492
Cdd:MTH00183  496 HGCPPPYHTFEE 507
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-497 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 724.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683   1 GTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIMLGAPDMAFP 80
Cdd:MTH00007   13 GTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFP 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683  81 RMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTG 160
Cdd:MTH00007   93 RLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKG 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 161 ITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 240
Cdd:MTH00007  173 LRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAIS 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 241 HIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYS 320
Cdd:MTH00007  253 HIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYE 332

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 321 PATLWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFT 400
Cdd:MTH00007  333 TPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFF 412

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 401 IMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGIIFFFFIIWESFASQRQVMFPVQLNSSIEWL 480
Cdd:MTH00007  413 LMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIASPHMSSSLEWQ 492

                         490
                  ....*....|....*..
gi 1561324683 481 QNTPPAEHSYSELPLLT 497
Cdd:MTH00007  493 DTLPLDFHNLPETGIIT 509
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-498 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 722.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683   1 GTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIMLGAPDMAFP 80
Cdd:MTH00077   16 GTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFP 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683  81 RMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTG 160
Cdd:MTH00077   96 RMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPS 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 161 ITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 240
Cdd:MTH00077  176 MSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMIS 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 241 HIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYS 320
Cdd:MTH00077  256 HIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWD 335

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 321 PATLWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFT 400
Cdd:MTH00077  336 AAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFG 415

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 401 IMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGIIFFFFIIWESFASQRQVMFPVQLNSSIEWL 480
Cdd:MTH00077  416 VMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREVLTTELTSTNIEWL 495

                         490
                  ....*....|....*...
gi 1561324683 481 QNTPPAEHSYSELPLLTN 498
Cdd:MTH00077  496 HGCPPPYHTFEEPSFVQT 513
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-496 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 669.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683   1 GTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIMLGAPDMAFP 80
Cdd:MTH00182   18 GTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683  81 RMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTG 160
Cdd:MTH00182   98 RLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPG 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 161 ITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 240
Cdd:MTH00182  178 VTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMIS 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 241 HIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYS 320
Cdd:MTH00182  258 QIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLD 337

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 321 PATLWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFT 400
Cdd:MTH00182  338 TPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFW 417

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 401 IMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGIIFFFFIIWESFASQRQVMFPVQLN----SS 476
Cdd:MTH00182  418 LMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKFIGWKEGTgeswAS 497

                         490       500
                  ....*....|....*....|
gi 1561324683 477 IEWLQNTPPAEHSYSELPLL 496
Cdd:MTH00182  498 LEWVHSSPPLFHTYNELPFV 517
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-492 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 667.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683   1 GTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIMLGAPDMAFP 80
Cdd:MTH00079   17 GTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683  81 RMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSnIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTG 160
Cdd:MTH00079   97 RLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSS 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 161 ITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 240
Cdd:MTH00079  176 ISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIIS 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 241 HIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYS 320
Cdd:MTH00079  256 QSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQ 335

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 321 PATLWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFT 400
Cdd:MTH00079  336 PLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFF 415

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 401 IMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGIIFFFFIIWESFASQRQVMFPVQLNSSIEWL 480
Cdd:MTH00079  416 LMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLHDNYINSSPEYS 495

                         490
                  ....*....|..
gi 1561324683 481 QNTPPAEHSYSE 492
Cdd:MTH00079  496 LSSYVFGHSYQS 507
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-496 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 654.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683   1 GTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIMLGAPDMAFP 80
Cdd:MTH00184   18 GTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683  81 RMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTG 160
Cdd:MTH00184   98 RLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPG 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 161 ITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 240
Cdd:MTH00184  178 ITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIIS 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 241 HIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYS 320
Cdd:MTH00184  258 QIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLD 337

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 321 PATLWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFT 400
Cdd:MTH00184  338 TPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFW 417

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 401 IMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGIIFFFFIIWESFASQRQV---MFPVQLNSSI 477
Cdd:MTH00184  418 LMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVREIKFvgwVEDSGHYPSL 497

                         490
                  ....*....|....*....
gi 1561324683 478 EWLQNTPPAEHSYSELPLL 496
Cdd:MTH00184  498 EWAQTSPPAHHTYNELPYV 516
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-461 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: 578.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683   1 GTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPiMLGAPDMAFP 80
Cdd:cd00919     5 GLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683  81 RMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTG 160
Cdd:cd00919    84 RLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 161 ITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 240
Cdd:cd00919   164 MTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAIS 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 241 HIISQESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYS 320
Cdd:cd00919   244 EIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFD 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 321 PATLWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFT 400
Cdd:cd00919   323 PPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFW 402

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1561324683 401 IMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGIIFFFFIIWESF 461
Cdd:cd00919   403 LWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-496 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 573.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683   1 GTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIMLGAPDMAFP 80
Cdd:MTH00026   17 GSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683  81 RMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTG 160
Cdd:MTH00026   97 RLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPG 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 161 ITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 240
Cdd:MTH00026  177 MTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIIS 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 241 HIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLN-- 318
Cdd:MTH00026  257 QILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSGRNli 336

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 319 YSPATLWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQ 398
Cdd:MTH00026  337 FTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIH 416

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 399 FTIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGIIFFFFIIWESFASQRQVMFPVQLN---- 474
Cdd:MTH00026  417 FWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAYYREEPFDINIMAKgpli 496

                         490       500       510
                  ....*....|....*....|....*....|.
gi 1561324683 475 ---------SSIEWLQNTPPAEHSYSELPLL 496
Cdd:MTH00026  497 pfscqpahfDTLEWSLTSPPEHHTYNELPYI 527
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-490 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: 533.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683   1 GTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMiGGFGNWLVPIMLGAPDMAFP 80
Cdd:TIGR02891  10 GILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFP 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683  81 RMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTG 160
Cdd:TIGR02891  89 RLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPG 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 161 ITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 240
Cdd:TIGR02891 169 MTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIIS 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 241 HIISQESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYS 320
Cdd:TIGR02891 249 EILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFT 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 321 PATLWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFT 400
Cdd:TIGR02891 328 TPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFW 407

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 401 IMFMGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTAWNVISTIGSTISLLGIIFFFFIIWESFASQRQVMFPVQLNSSIE 478
Cdd:TIGR02891 408 LTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGANPWGATTLE 487

                         490
                  ....*....|..
gi 1561324683 479 WLQNTPPAEHSY 490
Cdd:TIGR02891 488 WTTSSPPPAHNF 499
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-497 0e+00

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 533.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683   1 GTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPiMIGGFGNWLVPIMLGAPDMAFP 80
Cdd:COG0843    19 GIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683  81 RMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTG 160
Cdd:COG0843    98 RLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPG 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 161 ITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 240
Cdd:COG0843   178 MTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVS 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 241 HIISQESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYS 320
Cdd:COG0843   258 EIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFT 336

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 321 PATLWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFT 400
Cdd:COG0843   337 TPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFW 416

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 401 IMFMGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTAWNVISTIGSTISLLGIIFFFFIIWES-FASQRQVMFPVQLNsSI 477
Cdd:COG0843   417 LWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSlRKGPKAGGNPWGAR-TL 495

                         490       500
                  ....*....|....*....|
gi 1561324683 478 EWLQNTPPAEHSYSELPLLT 497
Cdd:COG0843   496 EWATPSPPPLYNFASIPVVR 515
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-468 2.49e-170

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 489.96  E-value: 2.49e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683   1 GTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPIMLGAPDMAFP 80
Cdd:MTH00048   17 GVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683  81 RMNNMSFWLLPPALTLLLVSSMVenGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTG 160
Cdd:MTH00048   97 RLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTN 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 161 ITFdRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 240
Cdd:MTH00048  175 VFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIIS 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 241 HIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYS 320
Cdd:MTH00048  254 HICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKS 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 321 -PATLWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQF 399
Cdd:MTH00048  334 dPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHC 413

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1561324683 400 TIMFMGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGIIFFFFIIWESFASQRQVM 468
Cdd:MTH00048  414 IISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEVL 482
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-490 6.05e-161

Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits in ubiquinol oxidase varies from two to five. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons from ubiquinol to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from ubiquinol on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. It is generally believed that the channels contain water molecules that act as 'proton wires' to transfer the protons. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are believed to be transferred directly from ubiquinol (the electron donor) to the low-spin heme, and directly from the low-spin heme to the binuclear center.


Pssm-ID: 238832  Cd Length: 501  Bit Score: 465.90  E-value: 6.05e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683   1 GTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGgFGNWLVPIMLGAPDMAFP 80
Cdd:cd01662    11 GIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFP 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683  81 RMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTG 160
Cdd:cd01662    90 RLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPG 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 161 ITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 240
Cdd:cd01662   170 MTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFS 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 241 HIISQESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYS 320
Cdd:cd01662   250 EIVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFE 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 321 PATLWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFT 400
Cdd:cd01662   329 TPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFW 408

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 401 IMFMGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTAWNVISTIGSTISLLGiifFFFIIWESFASQRQVMFPVQLN---- 474
Cdd:cd01662   409 LWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAG---VLLFLINVIVSIRKGKRDATGDpwga 485

                         490
                  ....*....|....*.
gi 1561324683 475 SSIEWLQNTPPAEHSY 490
Cdd:cd01662   486 RTLEWATSSPPPAYNF 501
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-445 3.77e-129

Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key enzyme in aerobic metabolism. Proton pumping haem-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-haem a3 (or haem o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxidases (E.C:1.10.3.11), is directly involved in the coupling between dioxygen reduction and proton pumping. Some terminal oxidases generate a transmembrane proton gradient across the plasma membrane (prokaryotes) or the mitochondrial inner membrane (eukaryotes). The enzyme complex consists of 3-4 subunits (prokaryotes) up to 13 polypeptides (mammals) of which only the catalytic subunit (equivalent to mammalian subunit I (COXI) is found in all haem-copper respiratory oxidases. The presence of a bimetallic centre (formed by a high-spin haem and copper B) as well as a low-spin haem, both ligated to six conserved histidine residues near the outer side of four transmembrane spans within CO I is common to all family members.


Pssm-ID: 459678  Cd Length: 432  Bit Score: 381.92  E-value: 3.77e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683   1 GTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPiMIGGFGNWLVPIMLGAPDMAFP 80
Cdd:pfam00115   3 GLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683  81 RMNNMSFWLLPPALTLLLVSSMvenGAGTGWTVYPPLssniahggASVDLAIFSLHLAGISSILGAVNFITTVINMRSTG 160
Cdd:pfam00115  82 RLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPG 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 161 ITFdRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 240
Cdd:pfam00115 151 MTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIY 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 241 HIISQESGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLN-Y 319
Cdd:pfam00115 224 YILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRfR 302

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 320 SPATLWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQF 399
Cdd:pfam00115 303 TTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHF 382

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1561324683 400 TIMFMGVNLTFFPQHFLGLAGMPRRYS----DYPDAYTAWNVISTIGSTI 445
Cdd:pfam00115 383 WLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-494 5.55e-108

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: 334.90  E-value: 5.55e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683   1 GTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGgFGNWLVPIMLGAPDMAFP 80
Cdd:TIGR02882  54 GVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFP 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683  81 RMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTG 160
Cdd:TIGR02882 133 VLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPG 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 161 ITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 240
Cdd:TIGR02882 213 MKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYS 292

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 241 HIISQESgKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYS 320
Cdd:TIGR02882 293 EIISTFA-QKRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFT 371

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 321 PATLWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFT 400
Cdd:TIGR02882 372 TPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLNERLGKWCFW 451

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 401 IMFMGVNLTFFPQHFLGLAGMPRRYSDY--PDAYTAWNVISTIGSTISLLGIIFFFFIIWESF-ASQRQVMFPVQLNSSI 477
Cdd:TIGR02882 452 FFMIGFNVCFFPMYILGLDGMPRRMYTYspSDGWFPLNLISTIGALLMAIGFIFLVYNIYYSHrKSPREATGDPWNGRTL 531

                         490
                  ....*....|....*..
gi 1561324683 478 EWLQNTPPAEHSYSELP 494
Cdd:TIGR02882 532 EWATASPPPKYNFAVTP 548
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 39-494 9.23e-99

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 311.48  E-value: 9.23e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683  39 YNVIVTAHAFIMIFFMVMPIMIGgFGNWLVPIMLGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLS 118
Cdd:PRK15017   99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 119 SNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDR 198
Cdd:PRK15017  178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 199 NINTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESgKKETFGSLGMIYAMLAIGLLGFIVWAHHMF 278
Cdd:PRK15017  258 YLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFF 336

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 279 TVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLYGTQLNYSPATLWALGFVFLFTVGGLTGVVLANSSIDIILHDTYYV 358
Cdd:PRK15017  337 TMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFL 416

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 359 VAHFHYVLSMGAVFAIMAGFVHWYPLFTGLTMNTKMLKSQFTIMFMGVNLTFFPQHFLGLAGMPRRYSDYPD-AYTAWNV 437
Cdd:PRK15017  417 IAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDpQFHTMLM 496

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 438 ISTIGSTISLLGIIFFFFIIWESFASQ---RQVMFPVQLNSSIEWLQNTPPAEHSYSELP 494
Cdd:PRK15017  497 IAASGAALIALGILCQVIQMYVSIRDRdqnRDLTGDPWGGRTLEWATSSPPPFYNFAVVP 556
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 1-449 5.43e-18

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: 86.57  E-value: 5.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683   1 GTLYFIFGAWAGMvgtsLSILIRAELGhpgALIGDDQIYNVIVTAHAFIM-IFFMVMPIMigGFGNWLVPIMLGAPDMAf 79
Cdd:cd01660    13 AFLALLLGGLFGL----LQVLVRTGVF---PLPSSGILYYQGLTLHGVLLaIVFTTFFIM--GFFYAIVARALLRSLFN- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683  80 PRMNNMSFWLLPPALTLLLVSsMVENGAGTGWTVYPPLssnIAHGGASVDLAIFSLHlagiSSILGAVNFITTVINMRSt 159
Cdd:cd01660    83 RRLAWAGFWLMVIGTVMAAVP-ILLGQASVLYTFYPPL---QAHPLFYIGAALVVVG----SWISGFAMFVTLWRWKKA- 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 160 gITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLtdrnINTSFFDpAGGGDPILYQHLFWFFGHPEVYILILPGFGMI 239
Cdd:cd01660   154 -NPGKKVPLATFMVVTTMILWLVASLGVALEVLFQL----LPWSLGL-VDTVDVLLSRTLFWWFGHPLVYFWLLPAYIAW 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 240 SHIISQESGKKETFGSLGMIyAMLAIGLLGFIVWAHHMFT-VGMDVDTRAYFTSATMIIAVPTGIKIFSWLAT------- 311
Cdd:cd01660   228 YTILPKIAGGKLFSDPLARL-AFILFLLFSTPVGFHHQFAdPGIGPGWKFIHMVLTFMVALPSLLTAFTVFASleiagrl 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1561324683 312 -----LYG--TQLNYSPATLWALGFVFL-FTVGGLTGVVLANSSIDIILHDTYYVVAHFHyvLSMGAVFAIMA-GFVHWY 382
Cdd:cd01660   307 rggkgLFGwiRALPWGDPMFLALFLAMLmFIPGGAGGIINASYQLNYVVHNTAWVPGHFH--LTVGGAVALTFmAVAYWL 384

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1561324683 383 -PLFTGLTMNTKMLKS-QFTIMFMGVNLTFFPQHFLGLAGMPRR--YSDYPDAY-----TAWNVISTIGSTISLLG 449
Cdd:cd01660   385 vPHLTGRELAAKRLALaQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGGLPaagewAPYQQLMAIGGTILFVS 460
 
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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