|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-508 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 961.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 1 KWMFSTNHKDIGTLYFLFGAWAGMLGTALSMLIRMELGTPGHLINDDQIFNVIITAHAFVMIFFMVMPIMIGGFGNWLIP 80
Cdd:MTH00153 3 KWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 81 LMIGAPDMAFPRMNNMSFWLLPPSLSLLISSMIMDNGVGTGWTVYPPLASNIAHSGSAVDLAIFSLHLAGVSSILGAINF 160
Cdd:MTH00153 83 LMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 161 ITTTINMKSPDMKNDQMPLFVWSVAITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGEAILFLHLFWFFGHPEIY 240
Cdd:MTH00153 163 ITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 241 ILILPGFGMISHIINQESSKNESFGTLGMIYTMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 320
Cdd:MTH00153 243 ILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 321 ATLHGSKFKLTPELSWAMGFIFLFTIGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITGLT 400
Cdd:MTH00153 323 ATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLT 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 401 MNPKLLKIQFLIMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYSSWNILSSMGSIISTAGIMMFLFILWESMMYKRTTLF 480
Cdd:MTH00153 403 MNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLF 482
|
490 500
....*....|....*....|....*...
gi 1938966218 481 SQHSMISIEWLQNTPPKEHSFSELPILN 508
Cdd:MTH00153 483 SLNLSSSIEWLQNLPPAEHSYSELPLLT 510
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
6-492 |
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: 828.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 6 TNHKDIGTLYFLFGAWAGMLGTALSMLIRMELGTPGHLINDDQIFNVIITAHAFVMIFFMVMPIMIGGFGNWLIPLMIGA 85
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 86 PDMAFPRMNNMSFWLLPPSLSLLISSMIMDNGVGTGWTVYPPLASNIAHSGSAVDLAIFSLHLAGVSSILGAINFITTTI 165
Cdd:cd01663 81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 166 NMKSPDMKNDQMPLFVWSVAITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGEAILFLHLFWFFGHPEIYILILP 245
Cdd:cd01663 161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 246 GFGMISHIINQESSKNESFGTLGMIYTMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHG 325
Cdd:cd01663 241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 326 SKFKLTPELSWAMGFIFLFTIGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITGLTMNPKL 405
Cdd:cd01663 321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 406 LKIQFLIMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYSSWNILSSMGSIISTAGIMMFLFILWESMMYKRTTLFSQ-HS 484
Cdd:cd01663 401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVgEG 480
|
....*...
gi 1938966218 485 MISIEWLQ 492
Cdd:cd01663 481 STSLEWTL 488
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
3-501 |
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: 535.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 3 MFSTNHKDIGTLYFLFGAWAGMLGTALSMLIRMELGTPGHLINDDQIFNVIITAHAFVMIFFMVMPIMiGGFGNWLIPLM 82
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 83 IGAPDMAFPRMNNMSFWLLPPSLSLLISSMIMDNGVGTGWTVYPPLASNIAHSGSAVDLAIFSLHLAGVSSILGAINFIT 162
Cdd:TIGR02891 80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 163 TTINMKSPDMKNDQMPLFVWSVAITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGEAILFLHLFWFFGHPEIYIL 242
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 243 ILPGFGMISHIINQESSKNeSFGTLGMIYTMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLAT 322
Cdd:TIGR02891 240 FLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 323 LHGSKFKLTPELSWAMGFIFLFTIGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITGLTMN 402
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 403 PKLLKIQFLIMFLGVNLTFFPQHFLGLAGMPRRYSDYPD--CYSSWNILSSMGSIISTAGIMMFLFILWESMMYKRTTLF 480
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPqmGFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGA 478
|
490 500
....*....|....*....|.
gi 1938966218 481 SQHSMISIEWLQNTPPKEHSF 501
Cdd:TIGR02891 479 NPWGATTLEWTTSSPPPAHNF 499
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-508 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 527.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 1 KWMFSTNHKDIGTLYFLFGAWAGMLGTALSMLIRMELGTPGHLINDDQIFNVIITAHAFVMIFFMVMPiMIGGFGNWLIP 80
Cdd:COG0843 8 RWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 81 LMIGAPDMAFPRMNNMSFWLLPPSLSLLISSMIMDNGVGTGWTVYPPLASNIAHSGSAVDLAIFSLHLAGVSSILGAINF 160
Cdd:COG0843 87 LQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 161 ITTTINMKSPDMKNDQMPLFVWSVAITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGEAILFLHLFWFFGHPEIY 240
Cdd:COG0843 167 IVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 241 ILILPGFGMISHIINQESSKNeSFGTLGMIYTMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 320
Cdd:COG0843 247 ILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 321 ATLHGSKFKLTPELSWAMGFIFLFTIGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITGLT 400
Cdd:COG0843 326 ATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRM 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 401 MNPKLLKIQFLIMFLGVNLTFFPQHFLGLAGMPRRYSDYP--DCYSSWNILSSMGSIISTAGIMMFLFILWESMMY-KRT 477
Cdd:COG0843 406 LNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKgPKA 485
|
490 500 510
....*....|....*....|....*....|.
gi 1938966218 478 TLFSQHSmISIEWLQNTPPKEHSFSELPILN 508
Cdd:COG0843 486 GGNPWGA-RTLEWATPSPPPLYNFASIPVVR 515
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
10-456 |
3.64e-122 |
|
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: 364.59 E-value: 3.64e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 10 DIGTLYFLFGAWAGMLGTALSMLIRMELGTPGHLINDDQIFNVIITAHAFVMIFFMVMPiMIGGFGNWLIPLMIGAPDMA 89
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 90 FPRMNNMSFWLLPPSLSLLISSMimdNGVGTGWTVYPPLAsniahsgsAVDLAIFSLHLAGVSSILGAINFITTTINMKS 169
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPLV--------GVDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 170 PDMKNdQMPLFVWSVAITAILLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGEAILFLHLFWFFGHPEIYILILPGFGM 249
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 250 ISHIInQESSKNESFGTLGMIYTMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGS--K 327
Cdd:pfam00115 222 IYYIL-PKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGwiR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 328 FKLTPELsWAMGFIFLFTIGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITGLTMNPKLLK 407
Cdd:pfam00115 301 FRTTPML-FFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGK 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1938966218 408 IQFLIMFLGVNLTFFPQHFLGLAGMPRRYS----DYPDCYSSWNILSSMGSII 456
Cdd:pfam00115 380 LHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-508 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 961.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 1 KWMFSTNHKDIGTLYFLFGAWAGMLGTALSMLIRMELGTPGHLINDDQIFNVIITAHAFVMIFFMVMPIMIGGFGNWLIP 80
Cdd:MTH00153 3 KWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 81 LMIGAPDMAFPRMNNMSFWLLPPSLSLLISSMIMDNGVGTGWTVYPPLASNIAHSGSAVDLAIFSLHLAGVSSILGAINF 160
Cdd:MTH00153 83 LMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 161 ITTTINMKSPDMKNDQMPLFVWSVAITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGEAILFLHLFWFFGHPEIY 240
Cdd:MTH00153 163 ITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 241 ILILPGFGMISHIINQESSKNESFGTLGMIYTMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 320
Cdd:MTH00153 243 ILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 321 ATLHGSKFKLTPELSWAMGFIFLFTIGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITGLT 400
Cdd:MTH00153 323 ATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLT 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 401 MNPKLLKIQFLIMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYSSWNILSSMGSIISTAGIMMFLFILWESMMYKRTTLF 480
Cdd:MTH00153 403 MNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLF 482
|
490 500
....*....|....*....|....*...
gi 1938966218 481 SQHSMISIEWLQNTPPKEHSFSELPILN 508
Cdd:MTH00153 483 SLNLSSSIEWLQNLPPAEHSYSELPLLT 510
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
6-492 |
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: 828.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 6 TNHKDIGTLYFLFGAWAGMLGTALSMLIRMELGTPGHLINDDQIFNVIITAHAFVMIFFMVMPIMIGGFGNWLIPLMIGA 85
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 86 PDMAFPRMNNMSFWLLPPSLSLLISSMIMDNGVGTGWTVYPPLASNIAHSGSAVDLAIFSLHLAGVSSILGAINFITTTI 165
Cdd:cd01663 81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 166 NMKSPDMKNDQMPLFVWSVAITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGEAILFLHLFWFFGHPEIYILILP 245
Cdd:cd01663 161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 246 GFGMISHIINQESSKNESFGTLGMIYTMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHG 325
Cdd:cd01663 241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 326 SKFKLTPELSWAMGFIFLFTIGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITGLTMNPKL 405
Cdd:cd01663 321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 406 LKIQFLIMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYSSWNILSSMGSIISTAGIMMFLFILWESMMYKRTTLFSQ-HS 484
Cdd:cd01663 401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVgEG 480
|
....*...
gi 1938966218 485 MISIEWLQ 492
Cdd:cd01663 481 STSLEWTL 488
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-507 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 818.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 1 KWMFSTNHKDIGTLYFLFGAWAGMLGTALSMLIRMELGTPGHLINDDQIFNVIITAHAFVMIFFMVMPIMIGGFGNWLIP 80
Cdd:MTH00116 5 RWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 81 LMIGAPDMAFPRMNNMSFWLLPPSLSLLISSMIMDNGVGTGWTVYPPLASNIAHSGSAVDLAIFSLHLAGVSSILGAINF 160
Cdd:MTH00116 85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 161 ITTTINMKSPDMKNDQMPLFVWSVAITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGEAILFLHLFWFFGHPEIY 240
Cdd:MTH00116 165 ITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 241 ILILPGFGMISHIINQESSKNESFGTLGMIYTMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 320
Cdd:MTH00116 245 ILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 321 ATLHGSKFKLTPELSWAMGFIFLFTIGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITGLT 400
Cdd:MTH00116 325 ATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 401 MNPKLLKIQFLIMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYSSWNILSSMGSIISTAGIMMFLFILWESMMYKRTTLF 480
Cdd:MTH00116 405 LHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVLQ 484
|
490 500
....*....|....*....|....*..
gi 1938966218 481 SQHSMISIEWLQNTPPKEHSFSELPIL 507
Cdd:MTH00116 485 PELTTTNIEWIHGCPPPYHTFEEPAFV 511
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-508 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 818.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 1 KWMFSTNHKDIGTLYFLFGAWAGMLGTALSMLIRMELGTPGHLINDDQIFNVIITAHAFVMIFFMVMPIMIGGFGNWLIP 80
Cdd:MTH00167 5 RWLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 81 LMIGAPDMAFPRMNNMSFWLLPPSLSLLISSMIMDNGVGTGWTVYPPLASNIAHSGSAVDLAIFSLHLAGVSSILGAINF 160
Cdd:MTH00167 85 LMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 161 ITTTINMKSPDMKNDQMPLFVWSVAITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGEAILFLHLFWFFGHPEIY 240
Cdd:MTH00167 165 ITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 241 ILILPGFGMISHIINQESSKNESFGTLGMIYTMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 320
Cdd:MTH00167 245 ILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 321 ATLHGSKFKLTPELSWAMGFIFLFTIGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITGLT 400
Cdd:MTH00167 325 ATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 401 MNPKLLKIQFLIMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYSSWNILSSMGSIISTAGIMMFLFILWESMMYKRTTLF 480
Cdd:MTH00167 405 LNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLLP 484
|
490 500
....*....|....*....|....*...
gi 1938966218 481 SQHSMISIEWLQNTPPKEHSFSELPILN 508
Cdd:MTH00167 485 VELTSTNVEWLHGCPPPHHTWEEPPFVQ 512
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-508 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 803.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 1 KWMFSTNHKDIGTLYFLFGAWAGMLGTALSMLIRMELGTPGHLINDDQIFNVIITAHAFVMIFFMVMPIMIGGFGNWLIP 80
Cdd:MTH00142 3 RWLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 81 LMIGAPDMAFPRMNNMSFWLLPPSLSLLISSMIMDNGVGTGWTVYPPLASNIAHSGSAVDLAIFSLHLAGVSSILGAINF 160
Cdd:MTH00142 83 LMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 161 ITTTINMKSPDMKNDQMPLFVWSVAITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGEAILFLHLFWFFGHPEIY 240
Cdd:MTH00142 163 ITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 241 ILILPGFGMISHIINQESSKNESFGTLGMIYTMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 320
Cdd:MTH00142 243 ILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 321 ATLHGSKFKLTPELSWAMGFIFLFTIGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITGLT 400
Cdd:MTH00142 323 ATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLT 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 401 MNPKLLKIQFLIMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYSSWNILSSMGSIISTAGIMMFLFILWESMMYKRTTLF 480
Cdd:MTH00142 403 LNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVMW 482
|
490 500
....*....|....*....|....*...
gi 1938966218 481 SQHSMISIEWLQNTPPKEHSFSELPILN 508
Cdd:MTH00142 483 SSHLSTSLEWSHRLPPDFHTYDELPILV 510
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-505 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 800.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 1 KWMFSTNHKDIGTLYFLFGAWAGMLGTALSMLIRMELGTPGHLINDDQIFNVIITAHAFVMIFFMVMPIMIGGFGNWLIP 80
Cdd:MTH00223 2 RWLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 81 LMIGAPDMAFPRMNNMSFWLLPPSLSLLISSMIMDNGVGTGWTVYPPLASNIAHSGSAVDLAIFSLHLAGVSSILGAINF 160
Cdd:MTH00223 82 LMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 161 ITTTINMKSPDMKNDQMPLFVWSVAITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGEAILFLHLFWFFGHPEIY 240
Cdd:MTH00223 162 ITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 241 ILILPGFGMISHIINQESSKNESFGTLGMIYTMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 320
Cdd:MTH00223 242 ILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 321 ATLHGSKFKLTPELSWAMGFIFLFTIGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITGLT 400
Cdd:MTH00223 322 ATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 401 MNPKLLKIQFLIMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYSSWNILSSMGSIISTAGIMMFLFILWESMMYKRTTLF 480
Cdd:MTH00223 402 LHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVW 481
|
490 500
....*....|....*....|....*
gi 1938966218 481 SQHSMISIEWLQNTPPKEHSFSELP 505
Cdd:MTH00223 482 SGHLSTSLEWDNLLPADFHNNSETG 506
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-508 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 729.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 1 KWMFSTNHKDIGTLYFLFGAWAGMLGTALSMLIRMELGTPGHLINDDQIFNVIITAHAFVMIFFMVMPIMIGGFGNWLIP 80
Cdd:MTH00103 5 RWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 81 LMIGAPDMAFPRMNNMSFWLLPPSLSLLISSMIMDNGVGTGWTVYPPLASNIAHSGSAVDLAIFSLHLAGVSSILGAINF 160
Cdd:MTH00103 85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 161 ITTTINMKSPDMKNDQMPLFVWSVAITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGEAILFLHLFWFFGHPEIY 240
Cdd:MTH00103 165 ITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 241 ILILPGFGMISHIINQESSKNESFGTLGMIYTMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 320
Cdd:MTH00103 245 ILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 321 ATLHGSKFKLTPELSWAMGFIFLFTIGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITGLT 400
Cdd:MTH00103 325 ATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 401 MNPKLLKIQFLIMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYSSWNILSSMGSIISTAGIMMFLFILWESMMYKRTTLF 480
Cdd:MTH00103 405 LNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVLT 484
|
490 500
....*....|....*....|....*...
gi 1938966218 481 SQHSMISIEWLQNTPPKEHSFSELPILN 508
Cdd:MTH00103 485 VELTTTNLEWLHGCPPPYHTFEEPTYVK 512
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-503 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 724.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 1 KWMFSTNHKDIGTLYFLFGAWAGMLGTALSMLIRMELGTPGHLINDDQIFNVIITAHAFVMIFFMVMPIMIGGFGNWLIP 80
Cdd:MTH00183 5 RWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 81 LMIGAPDMAFPRMNNMSFWLLPPSLSLLISSMIMDNGVGTGWTVYPPLASNIAHSGSAVDLAIFSLHLAGVSSILGAINF 160
Cdd:MTH00183 85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 161 ITTTINMKSPDMKNDQMPLFVWSVAITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGEAILFLHLFWFFGHPEIY 240
Cdd:MTH00183 165 ITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 241 ILILPGFGMISHIINQESSKNESFGTLGMIYTMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 320
Cdd:MTH00183 245 ILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 321 ATLHGSKFKLTPELSWAMGFIFLFTIGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITGLT 400
Cdd:MTH00183 325 ATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 401 MNPKLLKIQFLIMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYSSWNILSSMGSIISTAGIMMFLFILWESMMYKRTTLF 480
Cdd:MTH00183 405 LHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLS 484
|
490 500
....*....|....*....|...
gi 1938966218 481 SQHSMISIEWLQNTPPKEHSFSE 503
Cdd:MTH00183 485 VELTSTNVEWLHGCPPPYHTFEE 507
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-503 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 717.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 1 KWMFSTNHKDIGTLYFLFGAWAGMLGTALSMLIRMELGTPGHLINDDQIFNVIITAHAFVMIFFMVMPIMIGGFGNWLIP 80
Cdd:MTH00077 5 RWLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 81 LMIGAPDMAFPRMNNMSFWLLPPSLSLLISSMIMDNGVGTGWTVYPPLASNIAHSGSAVDLAIFSLHLAGVSSILGAINF 160
Cdd:MTH00077 85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 161 ITTTINMKSPDMKNDQMPLFVWSVAITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGEAILFLHLFWFFGHPEIY 240
Cdd:MTH00077 165 ITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 241 ILILPGFGMISHIINQESSKNESFGTLGMIYTMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 320
Cdd:MTH00077 245 ILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 321 ATLHGSKFKLTPELSWAMGFIFLFTIGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITGLT 400
Cdd:MTH00077 325 ATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 401 MNPKLLKIQFLIMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYSSWNILSSMGSIISTAGIMMFLFILWESMMYKRTTLF 480
Cdd:MTH00077 405 LHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREVLT 484
|
490 500
....*....|....*....|...
gi 1938966218 481 SQHSMISIEWLQNTPPKEHSFSE 503
Cdd:MTH00077 485 TELTSTNIEWLHGCPPPYHTFEE 507
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-506 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 716.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 1 KWMFSTNHKDIGTLYFLFGAWAGMLGTALSMLIRMELGTPGHLINDDQIFNVIITAHAFVMIFFMVMPIMIGGFGNWLIP 80
Cdd:MTH00037 5 RWLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 81 LMIGAPDMAFPRMNNMSFWLLPPSLSLLISSMIMDNGVGTGWTVYPPLASNIAHSGSAVDLAIFSLHLAGVSSILGAINF 160
Cdd:MTH00037 85 LMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 161 ITTTINMKSPDMKNDQMPLFVWSVAITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGEAILFLHLFWFFGHPEIY 240
Cdd:MTH00037 165 ITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 241 ILILPGFGMISHIINQESSKNESFGTLGMIYTMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 320
Cdd:MTH00037 245 ILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWM 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 321 ATLHGSKFKLTPELSWAMGFIFLFTIGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITGLT 400
Cdd:MTH00037 325 ATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVS 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 401 MNPKLLKIQFLIMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYSSWNILSSMGSIISTAGIMMFLFILWESMMYKRTTLF 480
Cdd:MTH00037 405 LHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVIS 484
|
490 500
....*....|....*....|....*..
gi 1938966218 481 SQHSMISIEWLQNT-PPKEHSFSELPI 506
Cdd:MTH00037 485 PEFSSSSLEWQYSSfPPSHHTFDETPS 511
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-507 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 704.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 1 KWMFSTNHKDIGTLYFLFGAWAGMLGTALSMLIRMELGTPGHLINDDQIFNVIITAHAFVMIFFMVMPIMIGGFGNWLIP 80
Cdd:MTH00007 2 RWLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 81 LMIGAPDMAFPRMNNMSFWLLPPSLSLLISSMIMDNGVGTGWTVYPPLASNIAHSGSAVDLAIFSLHLAGVSSILGAINF 160
Cdd:MTH00007 82 LMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 161 ITTTINMKSPDMKNDQMPLFVWSVAITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGEAILFLHLFWFFGHPEIY 240
Cdd:MTH00007 162 ITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 241 ILILPGFGMISHIINQESSKNESFGTLGMIYTMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 320
Cdd:MTH00007 242 ILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 321 ATLHGSKFKLTPELSWAMGFIFLFTIGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITGLT 400
Cdd:MTH00007 322 ATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 401 MNPKLLKIQFLIMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYSSWNILSSMGSIISTAGIMMFLFILWESMMYKRTTLF 480
Cdd:MTH00007 402 LHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIA 481
|
490 500
....*....|....*....|....*..
gi 1938966218 481 SQHSMISIEWLQNTPPKEHSFSELPIL 507
Cdd:MTH00007 482 SPHMSSSLEWQDTLPLDFHNLPETGII 508
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-508 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 669.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 1 KWMFSTNHKDIGTLYFLFGAWAGMLGTALSMLIRMELGTPGHLINDDQIFNVIITAHAFVMIFFMVMPIMIGGFGNWLIP 80
Cdd:MTH00182 7 RWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 81 LMIGAPDMAFPRMNNMSFWLLPPSLSLLISSMIMDNGVGTGWTVYPPLASNIAHSGSAVDLAIFSLHLAGVSSILGAINF 160
Cdd:MTH00182 87 LYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 161 ITTTINMKSPDMKNDQMPLFVWSVAITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGEAILFLHLFWFFGHPEIY 240
Cdd:MTH00182 167 ITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 241 ILILPGFGMISHIINQESSKNESFGTLGMIYTMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 320
Cdd:MTH00182 247 ILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 321 ATLHGSKFKLTPELSWAMGFIFLFTIGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITGLT 400
Cdd:MTH00182 327 ATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYC 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 401 MNPKLLKIQFLIMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYSSWNILSSMGSIISTAGIMMFLFILWESMMYKRTTL- 479
Cdd:MTH00182 407 YNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKFIg 486
|
490 500 510
....*....|....*....|....*....|..
gi 1938966218 480 ---FSQHSMISIEWLQNTPPKEHSFSELPILN 508
Cdd:MTH00182 487 wkeGTGESWASLEWVHSSPPLFHTYNELPFVY 518
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-505 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 657.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 1 KWMFSTNHKDIGTLYFLFGAWAGMLGTALSMLIRMELGTPGHLINDDQIFNVIITAHAFVMIFFMVMPIMIGGFGNWLIP 80
Cdd:MTH00184 7 RWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 81 LMIGAPDMAFPRMNNMSFWLLPPSLSLLISSMIMDNGVGTGWTVYPPLASNIAHSGSAVDLAIFSLHLAGVSSILGAINF 160
Cdd:MTH00184 87 LYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 161 ITTTINMKSPDMKNDQMPLFVWSVAITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGEAILFLHLFWFFGHPEIY 240
Cdd:MTH00184 167 ITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 241 ILILPGFGMISHIINQESSKNESFGTLGMIYTMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 320
Cdd:MTH00184 247 ILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 321 ATLHGSKFKLTPELSWAMGFIFLFTIGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITGLT 400
Cdd:MTH00184 327 ATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYC 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 401 MNPKLLKIQFLIMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYSSWNILSSMGSIISTAGIMMFLFILWESmmYKRTTLF 480
Cdd:MTH00184 407 YNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDA--YVREIKF 484
|
490 500 510
....*....|....*....|....*....|
gi 1938966218 481 -----SQHSMISIEWLQNTPPKEHSFSELP 505
Cdd:MTH00184 485 vgwveDSGHYPSLEWAQTSPPAHHTYNELP 514
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
2-503 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 653.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 2 WMFSTNHKDIGTLYFLFGAWAGMLGTALSMLIRMELGTPGHLINDDQIFNVIITAHAFVMIFFMVMPIMIGGFGNWLIPL 81
Cdd:MTH00079 7 WLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 82 MIGAPDMAFPRMNNMSFWLLPPSLSLLISSMIMDNGVGTGWTVYPPLaSNIAHSGSAVDLAIFSLHLAGVSSILGAINFI 161
Cdd:MTH00079 87 MLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPL-STLGHPGSSVDLAIFSLHCAGISSILGGINFM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 162 TTTINMKSPDMKNDQMPLFVWSVAITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGEAILFLHLFWFFGHPEIYI 241
Cdd:MTH00079 166 VTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 242 LILPGFGMISHIINQESSKNESFGTLGMIYTMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLA 321
Cdd:MTH00079 246 LILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 322 TLHGSKFKLTPELSWAMGFIFLFTIGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITGLTM 401
Cdd:MTH00079 326 TLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVY 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 402 NPKLLKIQFLIMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYSSWNILSSMGSIISTAGIMMFLFILWESMMYKRTTLFS 481
Cdd:MTH00079 406 DKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLHD 485
|
490 500
....*....|....*....|..
gi 1938966218 482 QHSMISIEWLQNTPPKEHSFSE 503
Cdd:MTH00079 486 NYINSSPEYSLSSYVFGHSYQS 507
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-507 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 578.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 1 KWMFSTNHKDIGTLYFLFGAWAGMLGTALSMLIRMELGTPGHLINDDQIFNVIITAHAFVMIFFMVMPIMIGGFGNWLIP 80
Cdd:MTH00026 6 RWFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 81 LMIGAPDMAFPRMNNMSFWLLPPSLSLLISSMIMDNGVGTGWTVYPPLASNIAHSGSAVDLAIFSLHLAGVSSILGAINF 160
Cdd:MTH00026 86 LMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 161 ITTTINMKSPDMKNDQMPLFVWSVAITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGEAILFLHLFWFFGHPEIY 240
Cdd:MTH00026 166 ITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 241 ILILPGFGMISHIINQESSKNESFGTLGMIYTMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 320
Cdd:MTH00026 246 ILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 321 ATLHGSKFKL--TPELSWAMGFIFLFTIGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITG 398
Cdd:MTH00026 326 ATVSGSGRNLifTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 399 LTMNPKLLKIQFLIMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYSSWNILSSMGSIISTAGIMMFLFILWESmmYKRTT 478
Cdd:MTH00026 406 YAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDA--YYREE 483
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1938966218 479 LFSQHSMI---------------SIEWLQNTPPKEHSFSELPIL 507
Cdd:MTH00026 484 PFDINIMAkgplipfscqpahfdTLEWSLTSPPEHHTYNELPYI 527
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
8-472 |
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: 565.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 8 HKDIGTLYFLFGAWAGMLGTALSMLIRMELGTPGHLINDDQIFNVIITAHAFVMIFFMVMPIMIGGFGNWLIPlMIGAPD 87
Cdd:cd00919 1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 88 MAFPRMNNMSFWLLPPSLSLLISSMIMDNGVGTGWTVYPPLASNIAHSGSAVDLAIFSLHLAGVSSILGAINFITTTINM 167
Cdd:cd00919 80 LAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 168 KSPDMKNDQMPLFVWSVAITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGEAILFLHLFWFFGHPEIYILILPGF 247
Cdd:cd00919 160 RAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 248 GMISHIINQESSKnESFGTLGMIYTMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGSK 327
Cdd:cd00919 240 GAISEIIPTFSGK-PLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 328 FKLTPELSWAMGFIFLFTIGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITGLTMNPKLLK 407
Cdd:cd00919 319 IRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGK 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1938966218 408 IQFLIMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYSSWNILSSMGSIISTAGIMMFLFILWESM 472
Cdd:cd00919 399 IHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
3-501 |
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: 535.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 3 MFSTNHKDIGTLYFLFGAWAGMLGTALSMLIRMELGTPGHLINDDQIFNVIITAHAFVMIFFMVMPIMiGGFGNWLIPLM 82
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 83 IGAPDMAFPRMNNMSFWLLPPSLSLLISSMIMDNGVGTGWTVYPPLASNIAHSGSAVDLAIFSLHLAGVSSILGAINFIT 162
Cdd:TIGR02891 80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 163 TTINMKSPDMKNDQMPLFVWSVAITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGEAILFLHLFWFFGHPEIYIL 242
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 243 ILPGFGMISHIINQESSKNeSFGTLGMIYTMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLAT 322
Cdd:TIGR02891 240 FLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 323 LHGSKFKLTPELSWAMGFIFLFTIGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITGLTMN 402
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 403 PKLLKIQFLIMFLGVNLTFFPQHFLGLAGMPRRYSDYPD--CYSSWNILSSMGSIISTAGIMMFLFILWESMMYKRTTLF 480
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPqmGFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGA 478
|
490 500
....*....|....*....|.
gi 1938966218 481 SQHSMISIEWLQNTPPKEHSF 501
Cdd:TIGR02891 479 NPWGATTLEWTTSSPPPAHNF 499
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-508 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 527.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 1 KWMFSTNHKDIGTLYFLFGAWAGMLGTALSMLIRMELGTPGHLINDDQIFNVIITAHAFVMIFFMVMPiMIGGFGNWLIP 80
Cdd:COG0843 8 RWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 81 LMIGAPDMAFPRMNNMSFWLLPPSLSLLISSMIMDNGVGTGWTVYPPLASNIAHSGSAVDLAIFSLHLAGVSSILGAINF 160
Cdd:COG0843 87 LQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 161 ITTTINMKSPDMKNDQMPLFVWSVAITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGEAILFLHLFWFFGHPEIY 240
Cdd:COG0843 167 IVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 241 ILILPGFGMISHIINQESSKNeSFGTLGMIYTMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 320
Cdd:COG0843 247 ILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 321 ATLHGSKFKLTPELSWAMGFIFLFTIGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITGLT 400
Cdd:COG0843 326 ATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRM 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 401 MNPKLLKIQFLIMFLGVNLTFFPQHFLGLAGMPRRYSDYP--DCYSSWNILSSMGSIISTAGIMMFLFILWESMMY-KRT 477
Cdd:COG0843 406 LNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKgPKA 485
|
490 500 510
....*....|....*....|....*....|.
gi 1938966218 478 TLFSQHSmISIEWLQNTPPKEHSFSELPILN 508
Cdd:COG0843 486 GGNPWGA-RTLEWATPSPPPLYNFASIPVVR 515
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
2-479 |
7.58e-172 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 494.20 E-value: 7.58e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 2 WMFSTNHKDIGTLYFLFGAWAGMLGTALSMLIRMELGTPGHLINDDQIFNVIITAHAFVMIFFMVMPIMIGGFGNWLIPL 81
Cdd:MTH00048 7 WLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 82 MIGAPDMAFPRMNNMSFWLLPPSLSLLISSMIMdnGVGTGWTVYPPLASNIAHSGSAVDLAIFSLHLAGVSSILGAINFI 161
Cdd:MTH00048 87 LLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 162 TTtINMKSPDMKNDQMPLFVWSVAITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGEAILFLHLFWFFGHPEIYI 241
Cdd:MTH00048 165 CT-IYSAFMTNVFSRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 242 LILPGFGMISHIINQESSKNESFGTLGMIYTMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLA 321
Cdd:MTH00048 244 LILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 322 TLHGSKFKLT-PELSWAMGFIFLFTIGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITGLT 400
Cdd:MTH00048 324 MLLNSRVRKSdPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLS 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1938966218 401 MNPKLLKIQFLIMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYSSWNILSSMGSIISTAGIMMFLFILWESMMYKRTTL 479
Cdd:MTH00048 404 LNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEVL 482
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
2-501 |
8.34e-154 |
|
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: 447.80 E-value: 8.34e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 2 WMFSTNHKDIGTLYFLFGAWAGMLGTALSMLIRMELGTPGHLINDDQIFNVIITAHAFVMIFFMVMPIMIGgFGNWLIPL 81
Cdd:cd01662 1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 82 MIGAPDMAFPRMNNMSFWLLPPSLSLLISSMIMDNGVGTGWTVYPPLASNIAHSGSAVDLAIFSLHLAGVSSILGAINFI 161
Cdd:cd01662 80 QIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 162 TTTINMKSPDMKNDQMPLFVWSVAITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGEAILFLHLFWFFGHPEIYI 241
Cdd:cd01662 160 VTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 242 LILPGFGMISHIINQESSKnESFGTLGMIYTMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLA 321
Cdd:cd01662 240 LILPAFGIFSEIVPTFSRK-PLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 322 TLHGSKFKLTPELSWAMGFIFLFTIGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITGLTM 401
Cdd:cd01662 319 TMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRML 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 402 NPKLLKIQFLIMFLGVNLTFFPQHFLGLAGMPRRYSDYP--DCYSSWNILSSMGSIISTAGIMMFLFILWESMMY-KRTT 478
Cdd:cd01662 399 NERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLINVIVSIRKgKRDA 478
|
490 500
....*....|....*....|...
gi 1938966218 479 LFSQHSMISIEWLQNTPPKEHSF 501
Cdd:cd01662 479 TGDPWGARTLEWATSSPPPAYNF 501
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
10-456 |
3.64e-122 |
|
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: 364.59 E-value: 3.64e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 10 DIGTLYFLFGAWAGMLGTALSMLIRMELGTPGHLINDDQIFNVIITAHAFVMIFFMVMPiMIGGFGNWLIPLMIGAPDMA 89
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 90 FPRMNNMSFWLLPPSLSLLISSMimdNGVGTGWTVYPPLAsniahsgsAVDLAIFSLHLAGVSSILGAINFITTTINMKS 169
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPLV--------GVDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 170 PDMKNdQMPLFVWSVAITAILLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGEAILFLHLFWFFGHPEIYILILPGFGM 249
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 250 ISHIInQESSKNESFGTLGMIYTMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGS--K 327
Cdd:pfam00115 222 IYYIL-PKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGwiR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 328 FKLTPELsWAMGFIFLFTIGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITGLTMNPKLLK 407
Cdd:pfam00115 301 FRTTPML-FFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGK 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1938966218 408 IQFLIMFLGVNLTFFPQHFLGLAGMPRRYS----DYPDCYSSWNILSSMGSII 456
Cdd:pfam00115 380 LHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
1-508 |
1.24e-106 |
|
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]
Pssm-ID: 131928 Cd Length: 643 Bit Score: 331.82 E-value: 1.24e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 1 KWMFSTNHKDIGTLYFLFGAWAGMLGTALSMLIRMELGTPGHLINDDQIFNVIITAHAFVMIFFMVMPIMIGgFGNWLIP 80
Cdd:TIGR02882 43 EWLTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 81 LMIGAPDMAFPRMNNMSFWLLPPSLSLLISSMIMDNGVGTGWTVYPPLASNIAHSGSAVDLAIFSLHLAGVSSILGAINF 160
Cdd:TIGR02882 122 LQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINF 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 161 ITTTINMKSPDMKNDQMPLFVWSVAITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGEAILFLHLFWFFGHPEIY 240
Cdd:TIGR02882 202 FVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVY 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 241 ILILPGFGMISHIINQESSKNeSFGTLGMIYTMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 320
Cdd:TIGR02882 282 IVILPAFGIYSEIISTFAQKR-LFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWL 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 321 ATLHGSKFKLTPELSWAMGFIFLFTIGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLITGLT 400
Cdd:TIGR02882 361 LTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYK 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 401 MNPKLLKIQFLIMFLGVNLTFFPQHFLGLAGMPRRYSDY--PDCYSSWNILSSMGSIISTAGIMMFLFILWESMMY-KRT 477
Cdd:TIGR02882 441 LNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYspSDGWFPLNLISTIGALLMAIGFIFLVYNIYYSHRKsPRE 520
|
490 500 510
....*....|....*....|....*....|.
gi 1938966218 478 TLFSQHSMISIEWLQNTPPKEHSFSELPILN 508
Cdd:TIGR02882 521 ATGDPWNGRTLEWATASPPPKYNFAVTPDVN 551
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
1-505 |
1.28e-93 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 298.39 E-value: 1.28e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 1 KWMFSTNHKDIGTLYFLFGAWAGMLGTALSMLIRME-----LGTPGHLI--NDDQIFnviiTAHAFVMIFFMVMPIMIGg 73
Cdd:PRK15017 47 EWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQqalasAGEAGFLPphHYDQIF----TAHGVIMIFFVAMPFVIG- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 74 FGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSLSLLISSMIMDNGVGTGWTVYPPLASNIAHSGSAVDLAIFSLHLAGVSS 153
Cdd:PRK15017 122 LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGT 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 154 ILGAINFITTTINMKSPDMKNDQMPLFVWSVAITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGEAILFLHLFWF 233
Cdd:PRK15017 202 TLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 234 FGHPEIYILILPGFGMISHIInQESSKNESFGTLGMIYTMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTG 313
Cdd:PRK15017 282 WGHPEVYILILPVFGVFSEIA-ATFSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTG 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 314 IKVFSWLATLHGSKFKLTPELSWAMGFIFLFTIGGLTGLILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWY 393
Cdd:PRK15017 361 VKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWW 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 394 PLITGLTMNPKLLKIQFLIMFLGVNLTFFPQHFLGLAGMPRRYSDYPD-CYSSWNILSSMGSIISTAGIMMFLFILWESM 472
Cdd:PRK15017 441 PKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDpQFHTMLMIAASGAALIALGILCQVIQMYVSI 520
|
490 500 510
....*....|....*....|....*....|....*.
gi 1938966218 473 MYK---RTTLFSQHSMISIEWLQNTPPKEHSFSELP 505
Cdd:PRK15017 521 RDRdqnRDLTGDPWGGRTLEWATSSPPPFYNFAVVP 556
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
230-472 |
2.90e-17 |
|
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: 84.26 E-value: 2.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 230 LFWFFGHPEIYILILPGFGMISHIINQESSKNESFGTLGMIYTMLSIgLMGFIVWAHHMFT-VGMDVDTRAYFTSATMII 308
Cdd:cd01660 207 LFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARLAFILFL-LFSTPVGFHHQFAdPGIGPGWKFIHMVLTFMV 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 309 AVPTGIKVFSWLATL-------HGSK----FKLTPELSWAMGFIFL----FTIGGLTGLILANSSIDIILHDTYYVVAHF 373
Cdd:cd01660 286 ALPSLLTAFTVFASLeiagrlrGGKGlfgwIRALPWGDPMFLALFLamlmFIPGGAGGIINASYQLNYVVHNTAWVPGHF 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1938966218 374 HyvLSMGAVFAIMG-GIIQWY-PLITGLTM-NPKLLKIQFLIMFLGVNLTFFPQHFLGLAGMPRR--YSDYPDCY----- 443
Cdd:cd01660 366 H--LTVGGAVALTFmAVAYWLvPHLTGRELaAKRLALAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGGLPaagew 443
|
250 260
....*....|....*....|....*....
gi 1938966218 444 SSWNILSSMGSIISTAGIMMFLFILWESM 472
Cdd:cd01660 444 APYQQLMAIGGTILFVSGALFLYILFRTL 472
|
|
| |
