|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-510 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 1005.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 1 NKWLLSTNHKDIGTLYFLFGAWAGVVGTSMSMLIRMELGQTGQLIGDDQIYNVIITSHAFIMIFFMVMPIMIGGFGNWLI 80
Cdd:MTH00153 2 NKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 81 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMINMGVGTGWTVYPPLAGSIAHNGGSVDLAIFSLHLAGVSSILGAVN 160
Cdd:MTH00153 82 PLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAIN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 161 FITTTINMRSSKMTFDQTPLFVWSVIITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPLLYQHLFWFFGHPEV 240
Cdd:MTH00153 162 FITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 241 YILILPGFGIISHIVYQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 320
Cdd:MTH00153 242 YILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSW 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 321 MATLYGSNLKMNPTLLWSLGFISLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGL 400
Cdd:MTH00153 322 LATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 401 TLNNKWLKIQFTIMFMGVNMTFFPQHFLGLAGMPRRYSDYPDAYSSWNSISSMGSTISVIGIIMFIIIMWESMITNRMVM 480
Cdd:MTH00153 402 TMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVL 481
|
490 500 510
....*....|....*....|....*....|
gi 1812094807 481 FTENMPSSNEWLQNNPPAEHSYSEIALITS 510
Cdd:MTH00153 482 FSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
7-493 |
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: 857.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 7 TNHKDIGTLYFLFGAWAGVVGTSMSMLIRMELGQTGQLIGDDQIYNVIITSHAFIMIFFMVMPIMIGGFGNWLIPLMIGA 86
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 87 PDMAFPRMNNMSFWLLPPSLTLLITSSMINMGVGTGWTVYPPLAGSIAHNGGSVDLAIFSLHLAGVSSILGAVNFITTTI 166
Cdd:cd01663 81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 167 NMRSSKMTFDQTPLFVWSVIITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPLLYQHLFWFFGHPEVYILILP 246
Cdd:cd01663 161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 247 GFGIISHIVYQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMATLYG 326
Cdd:cd01663 241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 327 SNLKMNPTLLWSLGFISLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGLTLNNKW 406
Cdd:cd01663 321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 407 LKIQFTIMFMGVNMTFFPQHFLGLAGMPRRYSDYPDAYSSWNSISSMGSTISVIGIIMFIIIMWESMITNRMVMFTENMP 486
Cdd:cd01663 401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGEG 480
|
....*...
gi 1812094807 487 SSN-EWLQ 493
Cdd:cd01663 481 STSlEWTL 488
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
4-457 |
0e+00 |
|
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) of cytochrome c oxidases of bacterial origin. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits I-III form the functional core of the enzyme complex. Subunit I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit II and heme a of subunit I to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. In the bacilli an apparent split (paralogism) has created a sister clade (TIGR02882) encoding subunits (QoxA) of the aa3-type quinone oxidase complex which reacts directly with quinones, bypassing the interaction with soluble cytochrome c. This model attempts to exclude these sequences, placing them between the trusted and noise cutoffs. These families, as well as archaeal and eukaryotic cytochrome c subunit I's are included within the superfamily model, pfam00115. [Energy metabolism, Electron transport]
Pssm-ID: 213748 Cd Length: 499 Bit Score: 537.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 4 LLSTNHKDIGTLYFLFGAWAGVVGTSMSMLIRMELGQTGQLIGDDQIYNVIITSHAFIMIFFMVMPIMiGGFGNWLIPLM 83
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 84 IGAPDMAFPRMNNMSFWLLPPSLTLLITSSMINMGVGTGWTVYPPLAGSIAHNGGSVDLAIFSLHLAGVSSILGAVNFIT 163
Cdd:TIGR02891 80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 164 TTINMRSSKMTFDQTPLFVWSVIITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPLLYQHLFWFFGHPEVYIL 243
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 244 ILPGFGIISHIVYQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMAT 323
Cdd:TIGR02891 240 FLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 324 LYGSNLKMNPTLLWSLGFISLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGLTLN 403
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1812094807 404 NKWLKIQFTIMFMGVNMTFFPQHFLGLAGMPRRYSDYPDA--YSSWNSISSMGSTI 457
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFI 454
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
2-510 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 535.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 2 KWLLSTNHKDIGTLYFLFGAWAGVVGTSMSMLIRMELGQTGQLIGDDQIYNVIITSHAFIMIFFMVMPiMIGGFGNWLIP 81
Cdd:COG0843 8 RWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 82 LMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMINMGVGTGWTVYPPLAGSIAHNGGSVDLAIFSLHLAGVSSILGAVNF 161
Cdd:COG0843 87 LQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 162 ITTTINMRSSKMTFDQTPLFVWSVIITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPLLYQHLFWFFGHPEVY 241
Cdd:COG0843 167 IVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 242 ILILPGFGIISHIVYQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWM 321
Cdd:COG0843 247 ILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 322 ATLYGSNLKMNPTLLWSLGFISLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGLT 401
Cdd:COG0843 326 ATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRM 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 402 LNNKWLKIQFTIMFMGVNMTFFPQHFLGLAGMPRRYSDYP--DAYSSWNSISSMGSTISVIGIIMFIIIMWESMITNRMV 479
Cdd:COG0843 406 LNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPKA 485
|
490 500 510
....*....|....*....|....*....|...
gi 1812094807 480 mfTENMPSSN--EWLQNNPPAEHSYSEIALITS 510
Cdd:COG0843 486 --GGNPWGARtlEWATPSPPPLYNFASIPVVRS 516
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
11-457 |
1.37e-131 |
|
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: 388.85 E-value: 1.37e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 11 DIGTLYFLFGAWAGVVGTSMSMLIRMELGQTGQLIGDDQIYNVIITSHAFIMIFFMVMPiMIGGFGNWLIPLMIGAPDMA 90
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 91 FPRMNNMSFWLLPPSLTLLITSSMinmGVGTGWTVYPPLAGsiahnggsVDLAIFSLHLAGVSSILGAVNFITTTINMRS 170
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 171 SKMTFdQTPLFVWSVIITALLLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPLLYQHLFWFFGHPEVYILILPGFGI 250
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 251 ISHIVYQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMATLYGSNLK 330
Cdd:pfam00115 222 IYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 331 MN-PTLLWSLGFISLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGLTLNNKWLKI 409
Cdd:pfam00115 301 FRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1812094807 410 QFTIMFMGVNMTFFPQHFLGLAGMPRRYS----DYPDAYSSWNSISSMGSTI 457
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-510 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 1005.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 1 NKWLLSTNHKDIGTLYFLFGAWAGVVGTSMSMLIRMELGQTGQLIGDDQIYNVIITSHAFIMIFFMVMPIMIGGFGNWLI 80
Cdd:MTH00153 2 NKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 81 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMINMGVGTGWTVYPPLAGSIAHNGGSVDLAIFSLHLAGVSSILGAVN 160
Cdd:MTH00153 82 PLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAIN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 161 FITTTINMRSSKMTFDQTPLFVWSVIITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPLLYQHLFWFFGHPEV 240
Cdd:MTH00153 162 FITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 241 YILILPGFGIISHIVYQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 320
Cdd:MTH00153 242 YILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSW 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 321 MATLYGSNLKMNPTLLWSLGFISLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGL 400
Cdd:MTH00153 322 LATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 401 TLNNKWLKIQFTIMFMGVNMTFFPQHFLGLAGMPRRYSDYPDAYSSWNSISSMGSTISVIGIIMFIIIMWESMITNRMVM 480
Cdd:MTH00153 402 TMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVL 481
|
490 500 510
....*....|....*....|....*....|
gi 1812094807 481 FTENMPSSNEWLQNNPPAEHSYSEIALITS 510
Cdd:MTH00153 482 FSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
7-493 |
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: 857.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 7 TNHKDIGTLYFLFGAWAGVVGTSMSMLIRMELGQTGQLIGDDQIYNVIITSHAFIMIFFMVMPIMIGGFGNWLIPLMIGA 86
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 87 PDMAFPRMNNMSFWLLPPSLTLLITSSMINMGVGTGWTVYPPLAGSIAHNGGSVDLAIFSLHLAGVSSILGAVNFITTTI 166
Cdd:cd01663 81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 167 NMRSSKMTFDQTPLFVWSVIITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPLLYQHLFWFFGHPEVYILILP 246
Cdd:cd01663 161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 247 GFGIISHIVYQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMATLYG 326
Cdd:cd01663 241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 327 SNLKMNPTLLWSLGFISLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGLTLNNKW 406
Cdd:cd01663 321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 407 LKIQFTIMFMGVNMTFFPQHFLGLAGMPRRYSDYPDAYSSWNSISSMGSTISVIGIIMFIIIMWESMITNRMVMFTENMP 486
Cdd:cd01663 401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGEG 480
|
....*...
gi 1812094807 487 SSN-EWLQ 493
Cdd:cd01663 481 STSlEWTL 488
|
|
| 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: 844.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 1 NKWLLSTNHKDIGTLYFLFGAWAGVVGTSMSMLIRMELGQTGQLIGDDQIYNVIITSHAFIMIFFMVMPIMIGGFGNWLI 80
Cdd:MTH00167 4 NRWLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 81 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMINMGVGTGWTVYPPLAGSIAHNGGSVDLAIFSLHLAGVSSILGAVN 160
Cdd:MTH00167 84 PLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSIN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 161 FITTTINMRSSKMTFDQTPLFVWSVIITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPLLYQHLFWFFGHPEV 240
Cdd:MTH00167 164 FITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 241 YILILPGFGIISHIVYQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 320
Cdd:MTH00167 244 YILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 321 MATLYGSNLKMNPTLLWSLGFISLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGL 400
Cdd:MTH00167 324 LATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 401 TLNNKWLKIQFTIMFMGVNMTFFPQHFLGLAGMPRRYSDYPDAYSSWNSISSMGSTISVIGIIMFIIIMWESMITNRMVM 480
Cdd:MTH00167 404 TLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLL 483
|
490 500
....*....|....*....|....*...
gi 1812094807 481 FTENMPSSNEWLQNNPPAEHSYSEIALI 508
Cdd:MTH00167 484 PVELTSTNVEWLHGCPPPHHTWEEPPFV 511
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-508 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 839.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 1 NKWLLSTNHKDIGTLYFLFGAWAGVVGTSMSMLIRMELGQTGQLIGDDQIYNVIITSHAFIMIFFMVMPIMIGGFGNWLI 80
Cdd:MTH00116 4 TRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 81 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMINMGVGTGWTVYPPLAGSIAHNGGSVDLAIFSLHLAGVSSILGAVN 160
Cdd:MTH00116 84 PLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAIN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 161 FITTTINMRSSKMTFDQTPLFVWSVIITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPLLYQHLFWFFGHPEV 240
Cdd:MTH00116 164 FITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 241 YILILPGFGIISHIVYQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 320
Cdd:MTH00116 244 YILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSW 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 321 MATLYGSNLKMNPTLLWSLGFISLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGL 400
Cdd:MTH00116 324 LATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGY 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 401 TLNNKWLKIQFTIMFMGVNMTFFPQHFLGLAGMPRRYSDYPDAYSSWNSISSMGSTISVIGIIMFIIIMWESMITNRMVM 480
Cdd:MTH00116 404 TLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVL 483
|
490 500
....*....|....*....|....*...
gi 1812094807 481 FTENMPSSNEWLQNNPPAEHSYSEIALI 508
Cdd:MTH00116 484 QPELTTTNIEWIHGCPPPYHTFEEPAFV 511
|
|
| 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: 822.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 1 NKWLLSTNHKDIGTLYFLFGAWAGVVGTSMSMLIRMELGQTGQLIGDDQIYNVIITSHAFIMIFFMVMPIMIGGFGNWLI 80
Cdd:MTH00142 2 MRWLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 81 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMINMGVGTGWTVYPPLAGSIAHNGGSVDLAIFSLHLAGVSSILGAVN 160
Cdd:MTH00142 82 PLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAIN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 161 FITTTINMRSSKMTFDQTPLFVWSVIITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPLLYQHLFWFFGHPEV 240
Cdd:MTH00142 162 FITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 241 YILILPGFGIISHIVYQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 320
Cdd:MTH00142 242 YILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSW 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 321 MATLYGSNLKMNPTLLWSLGFISLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGL 400
Cdd:MTH00142 322 LATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 401 TLNNKWLKIQFTIMFMGVNMTFFPQHFLGLAGMPRRYSDYPDAYSSWNSISSMGSTISVIGIIMFIIIMWESMITNRMVM 480
Cdd:MTH00142 402 TLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVM 481
|
490 500
....*....|....*....|....*...
gi 1812094807 481 FTENMPSSNEWLQNNPPAEHSYSEIALI 508
Cdd:MTH00142 482 WSSHLSTSLEWSHRLPPDFHTYDELPIL 509
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
2-508 |
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 1812094807 2 KWLLSTNHKDIGTLYFLFGAWAGVVGTSMSMLIRMELGQTGQLIGDDQIYNVIITSHAFIMIFFMVMPIMIGGFGNWLIP 81
Cdd:MTH00223 2 RWLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 82 LMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMINMGVGTGWTVYPPLAGSIAHNGGSVDLAIFSLHLAGVSSILGAVNF 161
Cdd:MTH00223 82 LMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 162 ITTTINMRSSKMTFDQTPLFVWSVIITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPLLYQHLFWFFGHPEVY 241
Cdd:MTH00223 162 ITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 242 ILILPGFGIISHIVYQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWM 321
Cdd:MTH00223 242 ILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 322 ATLYGSNLKMNPTLLWSLGFISLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGLT 401
Cdd:MTH00223 322 ATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 402 LNNKWLKIQFTIMFMGVNMTFFPQHFLGLAGMPRRYSDYPDAYSSWNSISSMGSTISVIGIIMFIIIMWESMITNRMVMF 481
Cdd:MTH00223 402 LHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVW 481
|
490 500
....*....|....*....|....*..
gi 1812094807 482 TENMPSSNEWLQNNPPAEHSYSEIALI 508
Cdd:MTH00223 482 SGHLSTSLEWDNLLPADFHNNSETGAL 508
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-510 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 763.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 1 NKWLLSTNHKDIGTLYFLFGAWAGVVGTSMSMLIRMELGQTGQLIGDDQIYNVIITSHAFIMIFFMVMPIMIGGFGNWLI 80
Cdd:MTH00103 4 NRWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 81 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMINMGVGTGWTVYPPLAGSIAHNGGSVDLAIFSLHLAGVSSILGAVN 160
Cdd:MTH00103 84 PLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAIN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 161 FITTTINMRSSKMTFDQTPLFVWSVIITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPLLYQHLFWFFGHPEV 240
Cdd:MTH00103 164 FITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 241 YILILPGFGIISHIVYQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 320
Cdd:MTH00103 244 YILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSW 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 321 MATLYGSNLKMNPTLLWSLGFISLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGL 400
Cdd:MTH00103 324 LATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGY 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 401 TLNNKWLKIQFTIMFMGVNMTFFPQHFLGLAGMPRRYSDYPDAYSSWNSISSMGSTISVIGIIMFIIIMWESMITNRMVM 480
Cdd:MTH00103 404 TLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVL 483
|
490 500 510
....*....|....*....|....*....|
gi 1812094807 481 FTENMPSSNEWLQNNPPAEHSYSEIALITS 510
Cdd:MTH00103 484 TVELTTTNLEWLHGCPPPYHTFEEPTYVKL 513
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
2-508 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 747.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 2 KWLLSTNHKDIGTLYFLFGAWAGVVGTSMSMLIRMELGQTGQLIGDDQIYNVIITSHAFIMIFFMVMPIMIGGFGNWLIP 81
Cdd:MTH00183 5 RWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 82 LMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMINMGVGTGWTVYPPLAGSIAHNGGSVDLAIFSLHLAGVSSILGAVNF 161
Cdd:MTH00183 85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 162 ITTTINMRSSKMTFDQTPLFVWSVIITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPLLYQHLFWFFGHPEVY 241
Cdd:MTH00183 165 ITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 242 ILILPGFGIISHIVYQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWM 321
Cdd:MTH00183 245 ILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 322 ATLYGSNLKMNPTLLWSLGFISLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGLT 401
Cdd:MTH00183 325 ATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 402 LNNKWLKIQFTIMFMGVNMTFFPQHFLGLAGMPRRYSDYPDAYSSWNSISSMGSTISVIGIIMFIIIMWESMITNRMVMF 481
Cdd:MTH00183 405 LHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLS 484
|
490 500
....*....|....*....|....*..
gi 1812094807 482 TENMPSSNEWLQNNPPAEHSYSEIALI 508
Cdd:MTH00183 485 VELTSTNVEWLHGCPPPYHTFEEPAFV 511
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
2-508 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 742.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 2 KWLLSTNHKDIGTLYFLFGAWAGVVGTSMSMLIRMELGQTGQLIGDDQIYNVIITSHAFIMIFFMVMPIMIGGFGNWLIP 81
Cdd:MTH00077 5 RWLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 82 LMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMINMGVGTGWTVYPPLAGSIAHNGGSVDLAIFSLHLAGVSSILGAVNF 161
Cdd:MTH00077 85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 162 ITTTINMRSSKMTFDQTPLFVWSVIITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPLLYQHLFWFFGHPEVY 241
Cdd:MTH00077 165 ITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 242 ILILPGFGIISHIVYQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWM 321
Cdd:MTH00077 245 ILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 322 ATLYGSNLKMNPTLLWSLGFISLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGLT 401
Cdd:MTH00077 325 ATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 402 LNNKWLKIQFTIMFMGVNMTFFPQHFLGLAGMPRRYSDYPDAYSSWNSISSMGSTISVIGIIMFIIIMWESMITNRMVMF 481
Cdd:MTH00077 405 LHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREVLT 484
|
490 500
....*....|....*....|....*..
gi 1812094807 482 TENMPSSNEWLQNNPPAEHSYSEIALI 508
Cdd:MTH00077 485 TELTSTNIEWLHGCPPPYHTFEEPSFV 511
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-505 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 742.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 1 NKWLLSTNHKDIGTLYFLFGAWAGVVGTSMSMLIRMELGQTGQLIGDDQIYNVIITSHAFIMIFFMVMPIMIGGFGNWLI 80
Cdd:MTH00037 4 SRWLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 81 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMINMGVGTGWTVYPPLAGSIAHNGGSVDLAIFSLHLAGVSSILGAVN 160
Cdd:MTH00037 84 PLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASIN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 161 FITTTINMRSSKMTFDQTPLFVWSVIITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPLLYQHLFWFFGHPEV 240
Cdd:MTH00037 164 FITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 241 YILILPGFGIISHIVYQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 320
Cdd:MTH00037 244 YILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSW 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 321 MATLYGSNLKMNPTLLWSLGFISLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGL 400
Cdd:MTH00037 324 MATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 401 TLNNKWLKIQFTIMFMGVNMTFFPQHFLGLAGMPRRYSDYPDAYSSWNSISSMGSTISVIGIIMFIIIMWESMITNRMVM 480
Cdd:MTH00037 404 SLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVI 483
|
490 500
....*....|....*....|....*.
gi 1812094807 481 FTENMPSSNEWLQNN-PPAEHSYSEI 505
Cdd:MTH00037 484 SPEFSSSSLEWQYSSfPPSHHTFDET 509
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
2-510 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 735.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 2 KWLLSTNHKDIGTLYFLFGAWAGVVGTSMSMLIRMELGQTGQLIGDDQIYNVIITSHAFIMIFFMVMPIMIGGFGNWLIP 81
Cdd:MTH00007 2 RWLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 82 LMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMINMGVGTGWTVYPPLAGSIAHNGGSVDLAIFSLHLAGVSSILGAVNF 161
Cdd:MTH00007 82 LMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 162 ITTTINMRSSKMTFDQTPLFVWSVIITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPLLYQHLFWFFGHPEVY 241
Cdd:MTH00007 162 ITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 242 ILILPGFGIISHIVYQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWM 321
Cdd:MTH00007 242 ILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 322 ATLYGSNLKMNPTLLWSLGFISLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGLT 401
Cdd:MTH00007 322 ATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 402 LNNKWLKIQFTIMFMGVNMTFFPQHFLGLAGMPRRYSDYPDAYSSWNSISSMGSTISVIGIIMFIIIMWESMITNRMVMF 481
Cdd:MTH00007 402 LHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIA 481
|
490 500
....*....|....*....|....*....
gi 1812094807 482 TENMPSSNEWLQNNPPAEHSYSEIALITS 510
Cdd:MTH00007 482 SPHMSSSLEWQDTLPLDFHNLPETGIITT 510
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
3-504 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 682.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 3 WLLSTNHKDIGTLYFLFGAWAGVVGTSMSMLIRMELGQTGQLIGDDQIYNVIITSHAFIMIFFMVMPIMIGGFGNWLIPL 82
Cdd:MTH00079 7 WLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 83 MIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMINMGVGTGWTVYPPLAgSIAHNGGSVDLAIFSLHLAGVSSILGAVNFI 162
Cdd:MTH00079 87 MLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGINFM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 163 TTTINMRSSKMTFDQTPLFVWSVIITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPLLYQHLFWFFGHPEVYI 242
Cdd:MTH00079 166 VTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 243 LILPGFGIISHIVYQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMA 322
Cdd:MTH00079 246 LILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 323 TLYGSNLKMNPTLLWSLGFISLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGLTL 402
Cdd:MTH00079 326 TLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVY 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 403 NNKWLKIQFTIMFMGVNMTFFPQHFLGLAGMPRRYSDYPDAYSSWNSISSMGSTISVIGIIMFIIIMWESMITNRMVMFT 482
Cdd:MTH00079 406 DKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLHD 485
|
490 500
....*....|....*....|..
gi 1812094807 483 ENMPSSNEWLQNNPPAEHSYSE 504
Cdd:MTH00079 486 NYINSSPEYSLSSYVFGHSYQS 507
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
2-508 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 676.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 2 KWLLSTNHKDIGTLYFLFGAWAGVVGTSMSMLIRMELGQTGQLIGDDQIYNVIITSHAFIMIFFMVMPIMIGGFGNWLIP 81
Cdd:MTH00182 7 RWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 82 LMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMINMGVGTGWTVYPPLAGSIAHNGGSVDLAIFSLHLAGVSSILGAVNF 161
Cdd:MTH00182 87 LYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 162 ITTTINMRSSKMTFDQTPLFVWSVIITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPLLYQHLFWFFGHPEVY 241
Cdd:MTH00182 167 ITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 242 ILILPGFGIISHIVYQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWM 321
Cdd:MTH00182 247 ILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 322 ATLYGSNLKMNPTLLWSLGFISLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGLT 401
Cdd:MTH00182 327 ATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYC 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 402 LNNKWLKIQFTIMFMGVNMTFFPQHFLGLAGMPRRYSDYPDAYSSWNSISSMGSTISVIGIIMFIIIMWESMITN-RMVM 480
Cdd:MTH00182 407 YNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREeKFIG 486
|
490 500 510
....*....|....*....|....*....|.
gi 1812094807 481 FTENMPSSN---EWLQNNPPAEHSYSEIALI 508
Cdd:MTH00182 487 WKEGTGESWaslEWVHSSPPLFHTYNELPFV 517
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
2-508 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 669.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 2 KWLLSTNHKDIGTLYFLFGAWAGVVGTSMSMLIRMELGQTGQLIGDDQIYNVIITSHAFIMIFFMVMPIMIGGFGNWLIP 81
Cdd:MTH00184 7 RWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 82 LMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMINMGVGTGWTVYPPLAGSIAHNGGSVDLAIFSLHLAGVSSILGAVNF 161
Cdd:MTH00184 87 LYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 162 ITTTINMRSSKMTFDQTPLFVWSVIITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPLLYQHLFWFFGHPEVY 241
Cdd:MTH00184 167 ITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 242 ILILPGFGIISHIVYQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWM 321
Cdd:MTH00184 247 ILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 322 ATLYGSNLKMNPTLLWSLGFISLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGLT 401
Cdd:MTH00184 327 ATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYC 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 402 LNNKWLKIQFTIMFMGVNMTFFPQHFLGLAGMPRRYSDYPDAYSSWNSISSMGSTISVIGIIMFIIIMWESMI-TNRMVM 480
Cdd:MTH00184 407 YNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVrEIKFVG 486
|
490 500 510
....*....|....*....|....*....|
gi 1812094807 481 FTENMP--SSNEWLQNNPPAEHSYSEIALI 508
Cdd:MTH00184 487 WVEDSGhyPSLEWAQTSPPAHHTYNELPYV 516
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
2-508 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 591.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 2 KWLLSTNHKDIGTLYFLFGAWAGVVGTSMSMLIRMELGQTGQLIGDDQIYNVIITSHAFIMIFFMVMPIMIGGFGNWLIP 81
Cdd:MTH00026 6 RWFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 82 LMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMINMGVGTGWTVYPPLAGSIAHNGGSVDLAIFSLHLAGVSSILGAVNF 161
Cdd:MTH00026 86 LMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 162 ITTTINMRSSKMTFDQTPLFVWSVIITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPLLYQHLFWFFGHPEVY 241
Cdd:MTH00026 166 ITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 242 ILILPGFGIISHIVYQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWM 321
Cdd:MTH00026 246 ILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 322 ATLYGS--NLKMNPTLLWSLGFISLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTG 399
Cdd:MTH00026 326 ATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 400 LTLNNKWLKIQFTIMFMGVNMTFFPQHFLGLAGMPRRYSDYPDAYSSWNSISSMGSTISVIGIIMFIIIMWES------- 472
Cdd:MTH00026 406 YAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAyyreepf 485
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1812094807 473 ----MITNRMVMFTENMPSSN--EWLQNNPPAEHSYSEIALI 508
Cdd:MTH00026 486 diniMAKGPLIPFSCQPAHFDtlEWSLTSPPEHHTYNELPYI 527
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
9-473 |
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: 584.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 9 HKDIGTLYFLFGAWAGVVGTSMSMLIRMELGQTGQLIGDDQIYNVIITSHAFIMIFFMVMPIMIGGFGNWLIPlMIGAPD 88
Cdd:cd00919 1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 89 MAFPRMNNMSFWLLPPSLTLLITSSMINMGVGTGWTVYPPLAGSIAHNGGSVDLAIFSLHLAGVSSILGAVNFITTTINM 168
Cdd:cd00919 80 LAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 169 RSSKMTFDQTPLFVWSVIITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPLLYQHLFWFFGHPEVYILILPGF 248
Cdd:cd00919 160 RAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 249 GIISHIVYQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMATLYGSN 328
Cdd:cd00919 240 GAISEIIPTFSGK-PLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 329 LKMNPTLLWSLGFISLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGLTLNNKWLK 408
Cdd:cd00919 319 IRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGK 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1812094807 409 IQFTIMFMGVNMTFFPQHFLGLAGMPRRYSDYPDAYSSWNSISSMGSTISVIGIIMFIIIMWESM 473
Cdd:cd00919 399 IHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
4-457 |
0e+00 |
|
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) of cytochrome c oxidases of bacterial origin. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits I-III form the functional core of the enzyme complex. Subunit I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit II and heme a of subunit I to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. In the bacilli an apparent split (paralogism) has created a sister clade (TIGR02882) encoding subunits (QoxA) of the aa3-type quinone oxidase complex which reacts directly with quinones, bypassing the interaction with soluble cytochrome c. This model attempts to exclude these sequences, placing them between the trusted and noise cutoffs. These families, as well as archaeal and eukaryotic cytochrome c subunit I's are included within the superfamily model, pfam00115. [Energy metabolism, Electron transport]
Pssm-ID: 213748 Cd Length: 499 Bit Score: 537.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 4 LLSTNHKDIGTLYFLFGAWAGVVGTSMSMLIRMELGQTGQLIGDDQIYNVIITSHAFIMIFFMVMPIMiGGFGNWLIPLM 83
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 84 IGAPDMAFPRMNNMSFWLLPPSLTLLITSSMINMGVGTGWTVYPPLAGSIAHNGGSVDLAIFSLHLAGVSSILGAVNFIT 163
Cdd:TIGR02891 80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 164 TTINMRSSKMTFDQTPLFVWSVIITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPLLYQHLFWFFGHPEVYIL 243
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 244 ILPGFGIISHIVYQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMAT 323
Cdd:TIGR02891 240 FLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 324 LYGSNLKMNPTLLWSLGFISLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGLTLN 403
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1812094807 404 NKWLKIQFTIMFMGVNMTFFPQHFLGLAGMPRRYSDYPDA--YSSWNSISSMGSTI 457
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFI 454
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
2-510 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 535.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 2 KWLLSTNHKDIGTLYFLFGAWAGVVGTSMSMLIRMELGQTGQLIGDDQIYNVIITSHAFIMIFFMVMPiMIGGFGNWLIP 81
Cdd:COG0843 8 RWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 82 LMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMINMGVGTGWTVYPPLAGSIAHNGGSVDLAIFSLHLAGVSSILGAVNF 161
Cdd:COG0843 87 LQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 162 ITTTINMRSSKMTFDQTPLFVWSVIITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPLLYQHLFWFFGHPEVY 241
Cdd:COG0843 167 IVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 242 ILILPGFGIISHIVYQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWM 321
Cdd:COG0843 247 ILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 322 ATLYGSNLKMNPTLLWSLGFISLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGLT 401
Cdd:COG0843 326 ATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRM 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 402 LNNKWLKIQFTIMFMGVNMTFFPQHFLGLAGMPRRYSDYP--DAYSSWNSISSMGSTISVIGIIMFIIIMWESMITNRMV 479
Cdd:COG0843 406 LNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPKA 485
|
490 500 510
....*....|....*....|....*....|...
gi 1812094807 480 mfTENMPSSN--EWLQNNPPAEHSYSEIALITS 510
Cdd:COG0843 486 --GGNPWGARtlEWATPSPPPLYNFASIPVVRS 516
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
3-501 |
3.57e-176 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 505.37 E-value: 3.57e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 3 WLLSTNHKDIGTLYFLFGAWAGVVGTSMSMLIRMELGQTGQLIGDDQIYNVIITSHAFIMIFFMVMPIMIGGFGNWLIPL 82
Cdd:MTH00048 7 WLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 83 MIGAPDMAFPRMNNMSFWLLPPSLTLLITSsmINMGVGTGWTVYPPLAGSIAHNGGSVDLAIFSLHLAGVSSILGAVNFI 162
Cdd:MTH00048 87 LLGLSDLNLPRLNALSAWLLVPSIVFLLLS--MCLGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 163 TTTINMRSSKMTFdQTPLFVWSVIITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPLLYQHLFWFFGHPEVYI 242
Cdd:MTH00048 165 CTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 243 LILPGFGIISHIVYQESGKIESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMA 322
Cdd:MTH00048 244 LILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 323 TLYGSNL-KMNPTLLWSLGFISLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGLT 401
Cdd:MTH00048 324 MLLNSRVrKSDPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 402 LNNKWLKIQFTIMFMGVNMTFFPQHFLGLAGMPRRYSDYPDAYSSWNSISSMGSTISVIGIIMFIIIMWESMITNRMVMF 481
Cdd:MTH00048 404 LNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEVLG 483
|
490 500
....*....|....*....|
gi 1812094807 482 TENMPSSNEWLQNNPPAEHS 501
Cdd:MTH00048 484 LWGSSSCVVNVLMSPVPYHN 503
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
3-457 |
4.81e-158 |
|
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: 458.97 E-value: 4.81e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 3 WLLSTNHKDIGTLYFLFGAWAGVVGTSMSMLIRMELGQTGQLIGDDQIYNVIITSHAFIMIFFMVMPIMIGgFGNWLIPL 82
Cdd:cd01662 1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 83 MIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMINMGVGTGWTVYPPLAGSIAHNGGSVDLAIFSLHLAGVSSILGAVNFI 162
Cdd:cd01662 80 QIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 163 TTTINMRSSKMTFDQTPLFVWSVIITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPLLYQHLFWFFGHPEVYI 242
Cdd:cd01662 160 VTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 243 LILPGFGIISHIVYQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMA 322
Cdd:cd01662 240 LILPAFGIFSEIVPTFSRK-PLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 323 TLYGSNLKMNPTLLWSLGFISLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGLTL 402
Cdd:cd01662 319 TMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRML 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1812094807 403 NNKWLKIQFTIMFMGVNMTFFPQHFLGLAGMPRRYSDYP--DAYSSWNSISSMGSTI 457
Cdd:cd01662 399 NERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFL 455
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
11-457 |
1.37e-131 |
|
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: 388.85 E-value: 1.37e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 11 DIGTLYFLFGAWAGVVGTSMSMLIRMELGQTGQLIGDDQIYNVIITSHAFIMIFFMVMPiMIGGFGNWLIPLMIGAPDMA 90
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 91 FPRMNNMSFWLLPPSLTLLITSSMinmGVGTGWTVYPPLAGsiahnggsVDLAIFSLHLAGVSSILGAVNFITTTINMRS 170
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 171 SKMTFdQTPLFVWSVIITALLLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPLLYQHLFWFFGHPEVYILILPGFGI 250
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 251 ISHIVYQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWMATLYGSNLK 330
Cdd:pfam00115 222 IYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 331 MN-PTLLWSLGFISLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGLTLNNKWLKI 409
Cdd:pfam00115 301 FRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1812094807 410 QFTIMFMGVNMTFFPQHFLGLAGMPRRYS----DYPDAYSSWNSISSMGSTI 457
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
1-457 |
6.04e-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: 329.89 E-value: 6.04e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 1 NKWLLSTNHKDIGTLYFLFGAWAGVVGTSMSMLIRMELGQTGQLIGDDQIYNVIITSHAFIMIFFMVMPIMIGgFGNWLI 80
Cdd:TIGR02882 42 NEWLTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 81 PLMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMINMGVGTGWTVYPPLAGSIAHNGGSVDLAIFSLHLAGVSSILGAVN 160
Cdd:TIGR02882 121 PLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGIN 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 161 FITTTINMRSSKMTFDQTPLFVWSVIITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPLLYQHLFWFFGHPEV 240
Cdd:TIGR02882 201 FFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEV 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 241 YILILPGFGIISHIVYQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 320
Cdd:TIGR02882 281 YIVILPAFGIYSEIISTFAQK-RLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNW 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 321 MATLYGSNLKMNPTLLWSLGFISLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYPLFTGL 400
Cdd:TIGR02882 360 LLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGY 439
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1812094807 401 TLNNKWLKIQFTIMFMGVNMTFFPQHFLGLAGMPRRYSDY--PDAYSSWNSISSMGSTI 457
Cdd:TIGR02882 440 KLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYspSDGWFPLNLISTIGALL 498
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
1-442 |
1.92e-98 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 311.10 E-value: 1.92e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 1 NKWLLSTNHKDIGTLYFLFGAWAGVVGTSMSMLIRME-----LGQTGQLigDDQIYNVIITSHAFIMIFFMVMPIMIGgF 75
Cdd:PRK15017 46 KEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQqalasAGEAGFL--PPHHYDQIFTAHGVIMIFFVAMPFVIG-L 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 76 GNWLIPLMIGAPDMAFPRMNNMSFWLLPPSLTLLITSSMINMGVGTGWTVYPPLAGSIAHNGGSVDLAIFSLHLAGVSSI 155
Cdd:PRK15017 123 MNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTT 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 156 LGAVNFITTTINMRSSKMTFDQTPLFVWSVIITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPLLYQHLFWFF 235
Cdd:PRK15017 203 LTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAW 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 236 GHPEVYILILPGFGIISHIVYQESGKiESFGTLGMIYAMLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGI 315
Cdd:PRK15017 283 GHPEVYILILPVFGVFSEIAATFSRK-RLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGV 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 316 KVFSWMATLYGSNLKMNPTLLWSLGFISLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIQWYP 395
Cdd:PRK15017 362 KIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWP 441
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1812094807 396 LFTGLTLNNKWLKIQFTIMFMGVNMTFFPQHFLGLAGMPRRYSDYPD 442
Cdd:PRK15017 442 KAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQID 488
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|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
12-442 |
1.64e-16 |
|
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: 81.95 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 12 IGTLYFLFGAWAGVvgtsMSMLIRmelGQTGQLIGDDQIYNVIITSHAFIM-IFFMVMPIMigGFGNWLIPLMIGAPDMA 90
Cdd:cd01660 12 VAFLALLLGGLFGL----LQVLVR---TGVFPLPSSGILYYQGLTLHGVLLaIVFTTFFIM--GFFYAIVARALLRSLFN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 91 fPRMNNMSFWLLppSLTLLITSSMINMGVGTG-WTVYPPLagsIAHNGGSVDLAIFSLHlagvSSILGAVNFITTTINMR 169
Cdd:cd01660 83 -RRLAWAGFWLM--VIGTVMAAVPILLGQASVlYTFYPPL---QAHPLFYIGAALVVVG----SWISGFAMFVTLWRWKK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 170 SSKMtfDQTPLFVWSVIITALLLLLSLPVLAGAITMLLtdrnLNTSFFDpAGGGDPLLYQHLFWFFGHPEVYILILPGFG 249
Cdd:cd01660 153 ANPG--KKVPLATFMVVTTMILWLVASLGVALEVLFQL----LPWSLGL-VDTVDVLLSRTLFWWFGHPLVYFWLLPAYI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 250 IISHIVYQESGKIESFGTLGMIYAMLSIgLMGFIVWAHHMFT-VGMDVDTRAYFTSATMIIAVPTGIKVFSWMATL-YGS 327
Cdd:cd01660 226 AWYTILPKIAGGKLFSDPLARLAFILFL-LFSTPVGFHHQFAdPGIGPGWKFIHMVLTFMVALPSLLTAFTVFASLeIAG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1812094807 328 NLKMNPTLLW---------------SLGFIsLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIQ 392
Cdd:cd01660 305 RLRGGKGLFGwiralpwgdpmflalFLAML-MFIPGGAGGIINASYQLNYVVHNTAWVPGHFHLTVGGAVALTFMAVAYW 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1812094807 393 WYPLFTGLTLNNKWL-KIQFTIMFMGVNMTFFPQHFLGLAGMPRR--YSDYPD 442
Cdd:cd01660 384 LVPHLTGRELAAKRLaLAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGG 436
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