|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
2-515 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 919.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 2 STMNRWFLSTNHKDIGTLYFVFGIMAGISGSVTSLMVRMQLIQPGQSSGGDSLYNMFITYHALTMIFFMVMPIMIGGFGN 81
Cdd:MTH00116 1 MFITRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 82 WLVPLMLGAPDMAFPRLNNMSFWLLPPAFLLLVSSAWFNSGVGTGWTIYPPLSGNLAHAGPSMDLAIFALHLAGASSILG 161
Cdd:MTH00116 81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 162 AINFITTCINMSPHHMSPHNWPLFVWSVFLTAVLLLLSLPVLAAAITMLLTDRNLNTTFFDPNGGGDPILFQHLFWFFGH 241
Cdd:MTH00116 161 AINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 242 PEVYILILPGFGIISHIVMHHSSKKEPFGYVSMVWAMLAITVLGFIVWAHHMFTVGLDIDTRAYFSAATMTIAVPTGIKV 321
Cdd:MTH00116 241 PEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 322 FSWAATIFGGKIHWTVPMFWAAGFIYLFTLGGLTGIMLSNSSIDTMLHDTYYVVAHFHYVLSMGAVFAILAGLTYWFPML 401
Cdd:MTH00116 321 FSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 402 TGYSLNQTMAKAQFWTMFTGVNITFFPQHMLGLAGMPRRYSDFPDAYAIWSTMSTTGSIISFTSAISMIAILWEAFSKKR 481
Cdd:MTH00116 401 TGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKR 480
|
490 500 510
....*....|....*....|....*....|....
gi 145976930 482 LTTPITTDTKSQEWTQGTPPPQHTFNTPPMIQQT 515
Cdd:MTH00116 481 KVLQPELTTTNIEWIHGCPPPYHTFEEPAFVQVQ 514
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
11-497 |
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: 813.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 11 TNHKDIGTLYFVFGIMAGISGSVTSLMVRMQLIQPGQSSGGDSLYNMFITYHALTMIFFMVMPIMIGGFGNWLVPLMLGA 90
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 91 PDMAFPRLNNMSFWLLPPAFLLLVSSAWFNSGVGTGWTIYPPLSGNLAHAGPSMDLAIFALHLAGASSILGAINFITTCI 170
Cdd:cd01663 81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 171 NMSPHHMSPHNWPLFVWSVFLTAVLLLLSLPVLAAAITMLLTDRNLNTTFFDPNGGGDPILFQHLFWFFGHPEVYILILP 250
Cdd:cd01663 161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 251 GFGIISHIVMHHSSKKEPFGYVSMVWAMLAITVLGFIVWAHHMFTVGLDIDTRAYFSAATMTIAVPTGIKVFSWAATIFG 330
Cdd:cd01663 241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 331 GKIHWTVPMFWAAGFIYLFTLGGLTGIMLSNSSIDTMLHDTYYVVAHFHYVLSMGAVFAILAGLTYWFPMLTGYSLNQTM 410
Cdd:cd01663 321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 411 AKAQFWTMFTGVNITFFPQHMLGLAGMPRRYSDFPDAYAIWSTMSTTGSIISFTSAISMIAILWEAF-SKKRLTTPITTD 489
Cdd:cd01663 401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFvSGRKVIFNVGEG 480
|
....*...
gi 145976930 490 TKSQEWTQ 497
Cdd:cd01663 481 STSLEWTL 488
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
2-512 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 557.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 2 STMNRWFLSTNHKDIGTLYFVFGIMAGISGSVTSLMVRMQLIQPGQSSGGDSLYNMFITYHALTMIFFMVMPiMIGGFGN 81
Cdd:COG0843 4 SGWRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 82 WLVPLMLGAPDMAFPRLNNMSFWLLPPAFLLLVSSAWFNSGVGTGWTIYPPLSGNLAHAGPSMDLAIFALHLAGASSILG 161
Cdd:COG0843 83 YLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 162 AINFITTCINMSPHHMSPHNWPLFVWSVFLTAVLLLLSLPVLAAAITMLLTDRNLNTTFFDPNGGGDPILFQHLFWFFGH 241
Cdd:COG0843 163 GVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 242 PEVYILILPGFGIISHIVMHHSSKKePFGYVSMVWAMLAITVLGFIVWAHHMFTVGLDIDTRAYFSAATMTIAVPTGIKV 321
Cdd:COG0843 243 PEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 322 FSWAATIFGGKIHWTVPMFWAAGFIYLFTLGGLTGIMLSNSSIDTMLHDTYYVVAHFHYVLSMGAVFAILAGLTYWFPML 401
Cdd:COG0843 322 FNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKM 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 402 TGYSLNQTMAKAQFWTMFTGVNITFFPQHMLGLAGMPRRYSDFP--DAYAIWSTMSTTGSIISFTSAISMIAILWEAFSK 479
Cdd:COG0843 402 TGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRK 481
|
490 500 510
....*....|....*....|....*....|...
gi 145976930 480 KRLTTPITTDTKSQEWTQGTPPPQHTFNTPPMI 512
Cdd:COG0843 482 GPKAGGNPWGARTLEWATPSPPPLYNFASIPVV 514
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
8-506 |
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: 555.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 8 FLSTNHKDIGTLYFVFGIMAGISGSVTSLMVRMQLIQPGQSSGGDSLYNMFITYHALTMIFFMVMPIMiGGFGNWLVPLM 87
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 88 LGAPDMAFPRLNNMSFWLLPPAFLLLVSSAWFNSGVGTGWTIYPPLSGNLAHAGPSMDLAIFALHLAGASSILGAINFIT 167
Cdd:TIGR02891 80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 168 TCINMSPHHMSPHNWPLFVWSVFLTAVLLLLSLPVLAAAITMLLTDRNLNTTFFDPNGGGDPILFQHLFWFFGHPEVYIL 247
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 248 ILPGFGIISHIVMHHSsKKEPFGYVSMVWAMLAITVLGFIVWAHHMFTVGLDIDTRAYFSAATMTIAVPTGIKVFSWAAT 327
Cdd:TIGR02891 240 FLPAFGIISEILPTFA-RKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 328 IFGGKIHWTVPMFWAAGFIYLFTLGGLTGIMLSNSSIDTMLHDTYYVVAHFHYVLSMGAVFAILAGLTYWFPMLTGYSLN 407
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 408 QTMAKAQFWTMFTGVNITFFPQHMLGLAGMPRRYSDFPDA--YAIWSTMSTTGSIISFTSAISMIAILWEAFSKKRLTTP 485
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGA 478
|
490 500
....*....|....*....|.
gi 145976930 486 ITTDTKSQEWTQGTPPPQHTF 506
Cdd:TIGR02891 479 NPWGATTLEWTTSSPPPAHNF 499
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
15-461 |
2.13e-127 |
|
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: 378.07 E-value: 2.13e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 15 DIGTLYFVFGIMAGISGSVTSLMVRMQLIQPGQSSGGDSLYNMFITYHALTMIFFMVMPiMIGGFGNWLVPLMLGAPDMA 94
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 95 FPRLNNMSFWLLPPAFLLLVSSAwfnSGVGTGWTIYPPLSGnlahagpsMDLAIFALHLAGASSILGAINFITTCINMSP 174
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 175 HHMSPhNWPLFVWSVFLTAVLLLLSLPVLAAAITMLLTDRNLNTtffdpnGGGDPILFQHLFWFFGHPEVYILILPGFGI 254
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 255 ISHIVMHHSsKKEPFGYVSMVWAMLAITVLGFIVWAHHMFTVGLDIDTRAYFSAATMTIAVPTGIKVFSWAATIFGGKIH 334
Cdd:pfam00115 222 IYYILPKFA-GRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 335 W-TVPMFWAAGFIYLFTLGGLTGIMLSNSSIDTMLHDTYYVVAHFHYVLSMGAVFAILAGLTYWFPMLTGYSLNQTMAKA 413
Cdd:pfam00115 301 FrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 145976930 414 QFWTMFTGVNITFFPQHMLGLAGMPRRYSDF----PDAYAIWSTMSTTGSII 461
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAPPfietVPAFQPLNWIRTIGGVL 432
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
2-515 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 919.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 2 STMNRWFLSTNHKDIGTLYFVFGIMAGISGSVTSLMVRMQLIQPGQSSGGDSLYNMFITYHALTMIFFMVMPIMIGGFGN 81
Cdd:MTH00116 1 MFITRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 82 WLVPLMLGAPDMAFPRLNNMSFWLLPPAFLLLVSSAWFNSGVGTGWTIYPPLSGNLAHAGPSMDLAIFALHLAGASSILG 161
Cdd:MTH00116 81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 162 AINFITTCINMSPHHMSPHNWPLFVWSVFLTAVLLLLSLPVLAAAITMLLTDRNLNTTFFDPNGGGDPILFQHLFWFFGH 241
Cdd:MTH00116 161 AINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 242 PEVYILILPGFGIISHIVMHHSSKKEPFGYVSMVWAMLAITVLGFIVWAHHMFTVGLDIDTRAYFSAATMTIAVPTGIKV 321
Cdd:MTH00116 241 PEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 322 FSWAATIFGGKIHWTVPMFWAAGFIYLFTLGGLTGIMLSNSSIDTMLHDTYYVVAHFHYVLSMGAVFAILAGLTYWFPML 401
Cdd:MTH00116 321 FSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 402 TGYSLNQTMAKAQFWTMFTGVNITFFPQHMLGLAGMPRRYSDFPDAYAIWSTMSTTGSIISFTSAISMIAILWEAFSKKR 481
Cdd:MTH00116 401 TGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKR 480
|
490 500 510
....*....|....*....|....*....|....
gi 145976930 482 LTTPITTDTKSQEWTQGTPPPQHTFNTPPMIQQT 515
Cdd:MTH00116 481 KVLQPELTTTNIEWIHGCPPPYHTFEEPAFVQVQ 514
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
4-512 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 823.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 4 MNRWFLSTNHKDIGTLYFVFGIMAGISGSVTSLMVRMQLIQPGQSSGGDSLYNMFITYHALTMIFFMVMPIMIGGFGNWL 83
Cdd:MTH00153 1 MNKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 84 VPLMLGAPDMAFPRLNNMSFWLLPPAFLLLVSSAWFNSGVGTGWTIYPPLSGNLAHAGPSMDLAIFALHLAGASSILGAI 163
Cdd:MTH00153 81 VPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 164 NFITTCINMSPHHMSPHNWPLFVWSVFLTAVLLLLSLPVLAAAITMLLTDRNLNTTFFDPNGGGDPILFQHLFWFFGHPE 243
Cdd:MTH00153 161 NFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 244 VYILILPGFGIISHIVMHHSSKKEPFGYVSMVWAMLAITVLGFIVWAHHMFTVGLDIDTRAYFSAATMTIAVPTGIKVFS 323
Cdd:MTH00153 241 VYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 324 WAATIFGGKIHWTVPMFWAAGFIYLFTLGGLTGIMLSNSSIDTMLHDTYYVVAHFHYVLSMGAVFAILAGLTYWFPMLTG 403
Cdd:MTH00153 321 WLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 404 YSLNQTMAKAQFWTMFTGVNITFFPQHMLGLAGMPRRYSDFPDAYAIWSTMSTTGSIISFTSAISMIAILWEAFSKKRLT 483
Cdd:MTH00153 401 LTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPV 480
|
490 500
....*....|....*....|....*....
gi 145976930 484 TPITTDTKSQEWTQGTPPPQHTFNTPPMI 512
Cdd:MTH00153 481 LFSLNLSSSIEWLQNLPPAEHSYSELPLL 509
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
11-497 |
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: 813.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 11 TNHKDIGTLYFVFGIMAGISGSVTSLMVRMQLIQPGQSSGGDSLYNMFITYHALTMIFFMVMPIMIGGFGNWLVPLMLGA 90
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 91 PDMAFPRLNNMSFWLLPPAFLLLVSSAWFNSGVGTGWTIYPPLSGNLAHAGPSMDLAIFALHLAGASSILGAINFITTCI 170
Cdd:cd01663 81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 171 NMSPHHMSPHNWPLFVWSVFLTAVLLLLSLPVLAAAITMLLTDRNLNTTFFDPNGGGDPILFQHLFWFFGHPEVYILILP 250
Cdd:cd01663 161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 251 GFGIISHIVMHHSSKKEPFGYVSMVWAMLAITVLGFIVWAHHMFTVGLDIDTRAYFSAATMTIAVPTGIKVFSWAATIFG 330
Cdd:cd01663 241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 331 GKIHWTVPMFWAAGFIYLFTLGGLTGIMLSNSSIDTMLHDTYYVVAHFHYVLSMGAVFAILAGLTYWFPMLTGYSLNQTM 410
Cdd:cd01663 321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 411 AKAQFWTMFTGVNITFFPQHMLGLAGMPRRYSDFPDAYAIWSTMSTTGSIISFTSAISMIAILWEAF-SKKRLTTPITTD 489
Cdd:cd01663 401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFvSGRKVIFNVGEG 480
|
....*...
gi 145976930 490 TKSQEWTQ 497
Cdd:cd01663 481 STSLEWTL 488
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
3-513 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 795.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 3 TMNRWFLSTNHKDIGTLYFVFGIMAGISGSVTSLMVRMQLIQPGQSSGGDSLYNMFITYHALTMIFFMVMPIMIGGFGNW 82
Cdd:MTH00167 2 WINRWLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 83 LVPLMLGAPDMAFPRLNNMSFWLLPPAFLLLVSSAWFNSGVGTGWTIYPPLSGNLAHAGPSMDLAIFALHLAGASSILGA 162
Cdd:MTH00167 82 LVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 163 INFITTCINMSPHHMSPHNWPLFVWSVFLTAVLLLLSLPVLAAAITMLLTDRNLNTTFFDPNGGGDPILFQHLFWFFGHP 242
Cdd:MTH00167 162 INFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 243 EVYILILPGFGIISHIVMHHSSKKEPFGYVSMVWAMLAITVLGFIVWAHHMFTVGLDIDTRAYFSAATMTIAVPTGIKVF 322
Cdd:MTH00167 242 EVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 323 SWAATIFGGKIHWTVPMFWAAGFIYLFTLGGLTGIMLSNSSIDTMLHDTYYVVAHFHYVLSMGAVFAILAGLTYWFPMLT 402
Cdd:MTH00167 322 SWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 403 GYSLNQTMAKAQFWTMFTGVNITFFPQHMLGLAGMPRRYSDFPDAYAIWSTMSTTGSIISFTSAISMIAILWEAFSKKRL 482
Cdd:MTH00167 402 GLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRK 481
|
490 500 510
....*....|....*....|....*....|.
gi 145976930 483 TTPITTDTKSQEWTQGTPPPQHTFNTPPMIQ 513
Cdd:MTH00167 482 LLPVELTSTNVEWLHGCPPPHHTWEEPPFVQ 512
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
6-506 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 746.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 6 RWFLSTNHKDIGTLYFVFGIMAGISGSVTSLMVRMQLIQPGQSSGGDSLYNMFITYHALTMIFFMVMPIMIGGFGNWLVP 85
Cdd:MTH00223 2 RWLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 86 LMLGAPDMAFPRLNNMSFWLLPPAFLLLVSSAWFNSGVGTGWTIYPPLSGNLAHAGPSMDLAIFALHLAGASSILGAINF 165
Cdd:MTH00223 82 LMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 166 ITTCINMSPHHMSPHNWPLFVWSVFLTAVLLLLSLPVLAAAITMLLTDRNLNTTFFDPNGGGDPILFQHLFWFFGHPEVY 245
Cdd:MTH00223 162 ITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 246 ILILPGFGIISHIVMHHSSKKEPFGYVSMVWAMLAITVLGFIVWAHHMFTVGLDIDTRAYFSAATMTIAVPTGIKVFSWA 325
Cdd:MTH00223 242 ILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 326 ATIFGGKIHWTVPMFWAAGFIYLFTLGGLTGIMLSNSSIDTMLHDTYYVVAHFHYVLSMGAVFAILAGLTYWFPMLTGYS 405
Cdd:MTH00223 322 ATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 406 LNQTMAKAQFWTMFTGVNITFFPQHMLGLAGMPRRYSDFPDAYAIWSTMSTTGSIISFTSAISMIAILWEAFSKKRLTTP 485
Cdd:MTH00223 402 LHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVW 481
|
490 500
....*....|....*....|.
gi 145976930 486 ITTDTKSQEWTQGTPPPQHTF 506
Cdd:MTH00223 482 SGHLSTSLEWDNLLPADFHNN 502
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
4-512 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 740.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 4 MNRWFLSTNHKDIGTLYFVFGIMAGISGSVTSLMVRMQLIQPGQSSGGDSLYNMFITYHALTMIFFMVMPIMIGGFGNWL 83
Cdd:MTH00142 1 MMRWLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 84 VPLMLGAPDMAFPRLNNMSFWLLPPAFLLLVSSAWFNSGVGTGWTIYPPLSGNLAHAGPSMDLAIFALHLAGASSILGAI 163
Cdd:MTH00142 81 VPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 164 NFITTCINMSPHHMSPHNWPLFVWSVFLTAVLLLLSLPVLAAAITMLLTDRNLNTTFFDPNGGGDPILFQHLFWFFGHPE 243
Cdd:MTH00142 161 NFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 244 VYILILPGFGIISHIVMHHSSKKEPFGYVSMVWAMLAITVLGFIVWAHHMFTVGLDIDTRAYFSAATMTIAVPTGIKVFS 323
Cdd:MTH00142 241 VYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 324 WAATIFGGKIHWTVPMFWAAGFIYLFTLGGLTGIMLSNSSIDTMLHDTYYVVAHFHYVLSMGAVFAILAGLTYWFPMLTG 403
Cdd:MTH00142 321 WLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 404 YSLNQTMAKAQFWTMFTGVNITFFPQHMLGLAGMPRRYSDFPDAYAIWSTMSTTGSIISFTSAISMIAILWEAFSKKRLT 483
Cdd:MTH00142 401 LTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLV 480
|
490 500
....*....|....*....|....*....
gi 145976930 484 TPITTDTKSQEWTQGTPPPQHTFNTPPMI 512
Cdd:MTH00142 481 MWSSHLSTSLEWSHRLPPDFHTYDELPIL 509
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
3-513 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 709.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 3 TMNRWFLSTNHKDIGTLYFVFGIMAGISGSVTSLMVRMQLIQPGQSSGGDSLYNMFITYHALTMIFFMVMPIMIGGFGNW 82
Cdd:MTH00183 2 AITRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 83 LVPLMLGAPDMAFPRLNNMSFWLLPPAFLLLVSSAWFNSGVGTGWTIYPPLSGNLAHAGPSMDLAIFALHLAGASSILGA 162
Cdd:MTH00183 82 LIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 163 INFITTCINMSPHHMSPHNWPLFVWSVFLTAVLLLLSLPVLAAAITMLLTDRNLNTTFFDPNGGGDPILFQHLFWFFGHP 242
Cdd:MTH00183 162 INFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 243 EVYILILPGFGIISHIVMHHSSKKEPFGYVSMVWAMLAITVLGFIVWAHHMFTVGLDIDTRAYFSAATMTIAVPTGIKVF 322
Cdd:MTH00183 242 EVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 323 SWAATIFGGKIHWTVPMFWAAGFIYLFTLGGLTGIMLSNSSIDTMLHDTYYVVAHFHYVLSMGAVFAILAGLTYWFPMLT 402
Cdd:MTH00183 322 SWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFS 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 403 GYSLNQTMAKAQFWTMFTGVNITFFPQHMLGLAGMPRRYSDFPDAYAIWSTMSTTGSIISFTSAISMIAILWEAFSKKRL 482
Cdd:MTH00183 402 GYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKRE 481
|
490 500 510
....*....|....*....|....*....|.
gi 145976930 483 TTPITTDTKSQEWTQGTPPPQHTFNTPPMIQ 513
Cdd:MTH00183 482 VLSVELTSTNVEWLHGCPPPYHTFEEPAFVQ 512
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
4-513 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 706.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 4 MNRWFLSTNHKDIGTLYFVFGIMAGISGSVTSLMVRMQLIQPGQSSGGDSLYNMFITYHALTMIFFMVMPIMIGGFGNWL 83
Cdd:MTH00103 3 INRWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 84 VPLMLGAPDMAFPRLNNMSFWLLPPAFLLLVSSAWFNSGVGTGWTIYPPLSGNLAHAGPSMDLAIFALHLAGASSILGAI 163
Cdd:MTH00103 83 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 164 NFITTCINMSPHHMSPHNWPLFVWSVFLTAVLLLLSLPVLAAAITMLLTDRNLNTTFFDPNGGGDPILFQHLFWFFGHPE 243
Cdd:MTH00103 163 NFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 244 VYILILPGFGIISHIVMHHSSKKEPFGYVSMVWAMLAITVLGFIVWAHHMFTVGLDIDTRAYFSAATMTIAVPTGIKVFS 323
Cdd:MTH00103 243 VYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 324 WAATIFGGKIHWTVPMFWAAGFIYLFTLGGLTGIMLSNSSIDTMLHDTYYVVAHFHYVLSMGAVFAILAGLTYWFPMLTG 403
Cdd:MTH00103 323 WLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 404 YSLNQTMAKAQFWTMFTGVNITFFPQHMLGLAGMPRRYSDFPDAYAIWSTMSTTGSIISFTSAISMIAILWEAFSKKRLT 483
Cdd:MTH00103 403 YTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREV 482
|
490 500 510
....*....|....*....|....*....|
gi 145976930 484 TPITTDTKSQEWTQGTPPPQHTFNTPPMIQ 513
Cdd:MTH00103 483 LTVELTTTNLEWLHGCPPPYHTFEEPTYVK 512
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
4-515 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 705.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 4 MNRWFLSTNHKDIGTLYFVFGIMAGISGSVTSLMVRMQLIQPGQSSGGDSLYNMFITYHALTMIFFMVMPIMIGGFGNWL 83
Cdd:MTH00077 3 ITRWLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 84 VPLMLGAPDMAFPRLNNMSFWLLPPAFLLLVSSAWFNSGVGTGWTIYPPLSGNLAHAGPSMDLAIFALHLAGASSILGAI 163
Cdd:MTH00077 83 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 164 NFITTCINMSPHHMSPHNWPLFVWSVFLTAVLLLLSLPVLAAAITMLLTDRNLNTTFFDPNGGGDPILFQHLFWFFGHPE 243
Cdd:MTH00077 163 NFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 244 VYILILPGFGIISHIVMHHSSKKEPFGYVSMVWAMLAITVLGFIVWAHHMFTVGLDIDTRAYFSAATMTIAVPTGIKVFS 323
Cdd:MTH00077 243 VYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 324 WAATIFGGKIHWTVPMFWAAGFIYLFTLGGLTGIMLSNSSIDTMLHDTYYVVAHFHYVLSMGAVFAILAGLTYWFPMLTG 403
Cdd:MTH00077 323 WLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 404 YSLNQTMAKAQFWTMFTGVNITFFPQHMLGLAGMPRRYSDFPDAYAIWSTMSTTGSIISFTSAISMIAILWEAFSKKRLT 483
Cdd:MTH00077 403 YTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREV 482
|
490 500 510
....*....|....*....|....*....|..
gi 145976930 484 TPITTDTKSQEWTQGTPPPQHTFNTPPMIQQT 515
Cdd:MTH00077 483 LTTELTSTNIEWLHGCPPPYHTFEEPSFVQTR 514
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
4-510 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 681.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 4 MNRWFLSTNHKDIGTLYFVFGIMAGISGSVTSLMVRMQLIQPGQSSGGDSLYNMFITYHALTMIFFMVMPIMIGGFGNWL 83
Cdd:MTH00037 3 LSRWLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 84 VPLMLGAPDMAFPRLNNMSFWLLPPAFLLLVSSAWFNSGVGTGWTIYPPLSGNLAHAGPSMDLAIFALHLAGASSILGAI 163
Cdd:MTH00037 83 IPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 164 NFITTCINMSPHHMSPHNWPLFVWSVFLTAVLLLLSLPVLAAAITMLLTDRNLNTTFFDPNGGGDPILFQHLFWFFGHPE 243
Cdd:MTH00037 163 NFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 244 VYILILPGFGIISHIVMHHSSKKEPFGYVSMVWAMLAITVLGFIVWAHHMFTVGLDIDTRAYFSAATMTIAVPTGIKVFS 323
Cdd:MTH00037 243 VYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 324 WAATIFGGKIHWTVPMFWAAGFIYLFTLGGLTGIMLSNSSIDTMLHDTYYVVAHFHYVLSMGAVFAILAGLTYWFPMLTG 403
Cdd:MTH00037 323 WMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 404 YSLNQTMAKAQFWTMFTGVNITFFPQHMLGLAGMPRRYSDFPDAYAIWSTMSTTGSIISFTSAISMIAILWEAFSKKRLT 483
Cdd:MTH00037 403 VSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREV 482
|
490 500
....*....|....*....|....*...
gi 145976930 484 TPITTDTKSQEWTQGTPPPQ-HTFNTPP 510
Cdd:MTH00037 483 ISPEFSSSSLEWQYSSFPPShHTFDETP 510
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
6-514 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 674.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 6 RWFLSTNHKDIGTLYFVFGIMAGISGSVTSLMVRMQLIQPGQSSGGDSLYNMFITYHALTMIFFMVMPIMIGGFGNWLVP 85
Cdd:MTH00007 2 RWLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 86 LMLGAPDMAFPRLNNMSFWLLPPAFLLLVSSAWFNSGVGTGWTIYPPLSGNLAHAGPSMDLAIFALHLAGASSILGAINF 165
Cdd:MTH00007 82 LMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 166 ITTCINMSPHHMSPHNWPLFVWSVFLTAVLLLLSLPVLAAAITMLLTDRNLNTTFFDPNGGGDPILFQHLFWFFGHPEVY 245
Cdd:MTH00007 162 ITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 246 ILILPGFGIISHIVMHHSSKKEPFGYVSMVWAMLAITVLGFIVWAHHMFTVGLDIDTRAYFSAATMTIAVPTGIKVFSWA 325
Cdd:MTH00007 242 ILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 326 ATIFGGKIHWTVPMFWAAGFIYLFTLGGLTGIMLSNSSIDTMLHDTYYVVAHFHYVLSMGAVFAILAGLTYWFPMLTGYS 405
Cdd:MTH00007 322 ATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 406 LNQTMAKAQFWTMFTGVNITFFPQHMLGLAGMPRRYSDFPDAYAIWSTMSTTGSIISFTSAISMIAILWEAFSKKRLTTP 485
Cdd:MTH00007 402 LHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIA 481
|
490 500
....*....|....*....|....*....
gi 145976930 486 ITTDTKSQEWTQGTPPPQHTFNTPPMIQQ 514
Cdd:MTH00007 482 SPHMSSSLEWQDTLPLDFHNLPETGIITT 510
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
6-514 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 638.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 6 RWFLSTNHKDIGTLYFVFGIMAGISGSVTSLMVRMQLIQPGQSSGGDSLYNMFITYHALTMIFFMVMPIMIGGFGNWLVP 85
Cdd:MTH00182 7 RWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 86 LMLGAPDMAFPRLNNMSFWLLPPAFLLLVSSAWFNSGVGTGWTIYPPLSGNLAHAGPSMDLAIFALHLAGASSILGAINF 165
Cdd:MTH00182 87 LYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 166 ITTCINMSPHHMSPHNWPLFVWSVFLTAVLLLLSLPVLAAAITMLLTDRNLNTTFFDPNGGGDPILFQHLFWFFGHPEVY 245
Cdd:MTH00182 167 ITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 246 ILILPGFGIISHIVMHHSSKKEPFGYVSMVWAMLAITVLGFIVWAHHMFTVGLDIDTRAYFSAATMTIAVPTGIKVFSWA 325
Cdd:MTH00182 247 ILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 326 ATIFGGKIHWTVPMFWAAGFIYLFTLGGLTGIMLSNSSIDTMLHDTYYVVAHFHYVLSMGAVFAILAGLTYWFPMLTGYS 405
Cdd:MTH00182 327 ATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYC 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 406 LNQTMAKAQFWTMFTGVNITFFPQHMLGLAGMPRRYSDFPDAYAIWSTMSTTGSIISFTSAISMIAILWEAFSKKRLTTP 485
Cdd:MTH00182 407 YNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKFIG 486
|
490 500 510
....*....|....*....|....*....|...
gi 145976930 486 ITTDT----KSQEWTQGTPPPQHTFNTPPMIQQ 514
Cdd:MTH00182 487 WKEGTgeswASLEWVHSSPPLFHTYNELPFVYK 519
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
4-512 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 630.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 4 MNRWFLSTNHKDIGTLYFVFGIMAGISGSVTSLMVRMQLIQPGQSSGGDSLYNMFITYHALTMIFFMVMPIMIGGFGNWL 83
Cdd:MTH00184 5 LSRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 84 VPLMLGAPDMAFPRLNNMSFWLLPPAFLLLVSSAWFNSGVGTGWTIYPPLSGNLAHAGPSMDLAIFALHLAGASSILGAI 163
Cdd:MTH00184 85 VPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 164 NFITTCINMSPHHMSPHNWPLFVWSVFLTAVLLLLSLPVLAAAITMLLTDRNLNTTFFDPNGGGDPILFQHLFWFFGHPE 243
Cdd:MTH00184 165 NFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 244 VYILILPGFGIISHIVMHHSSKKEPFGYVSMVWAMLAITVLGFIVWAHHMFTVGLDIDTRAYFSAATMTIAVPTGIKVFS 323
Cdd:MTH00184 245 VYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 324 WAATIFGGKIHWTVPMFWAAGFIYLFTLGGLTGIMLSNSSIDTMLHDTYYVVAHFHYVLSMGAVFAILAGLTYWFPMLTG 403
Cdd:MTH00184 325 WIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 404 YSLNQTMAKAQFWTMFTGVNITFFPQHMLGLAGMPRRYSDFPDAYAIWSTMSTTGSIISFTSAISMIAILWEAFSKKRLT 483
Cdd:MTH00184 405 YCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVREIKF 484
|
490 500 510
....*....|....*....|....*....|..
gi 145976930 484 TPITTDT---KSQEWTQGTPPPQHTFNTPPMI 512
Cdd:MTH00184 485 VGWVEDSghyPSLEWAQTSPPAHHTYNELPYV 516
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-507 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 617.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 1 MSTMNRWFLSTNHKDIGTLYFVFGIMAGISGSVTSLMVRMQLIQPGQSSGGDSLYNMFITYHALTMIFFMVMPIMIGGFG 80
Cdd:MTH00079 1 QGGLSVWLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 81 NWLVPLMLGAPDMAFPRLNNMSFWLLPPAFLLLVSSAWFNSGVGTGWTIYPPLSgNLAHAGPSMDLAIFALHLAGASSIL 160
Cdd:MTH00079 81 NWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 161 GAINFITTCINMSPHHMSPHNWPLFVWSVFLTAVLLLLSLPVLAAAITMLLTDRNLNTTFFDPNGGGDPILFQHLFWFFG 240
Cdd:MTH00079 160 GGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 241 HPEVYILILPGFGIISHIVMHHSSKKEPFGYVSMVWAMLAITVLGFIVWAHHMFTVGLDIDTRAYFSAATMTIAVPTGIK 320
Cdd:MTH00079 240 HPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 321 VFSWAATIFGGKIHWTVPMFWAAGFIYLFTLGGLTGIMLSNSSIDTMLHDTYYVVAHFHYVLSMGAVFAILAGLTYWFPM 400
Cdd:MTH00079 320 VFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 401 LTGYSLNQTMAKAQFWTMFTGVNITFFPQHMLGLAGMPRRYSDFPDAYAIWSTMSTTGSIISFTSAISMIAILWEAFSKK 480
Cdd:MTH00079 400 MTGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSY 479
|
490 500
....*....|....*....|....*..
gi 145976930 481 RLTTPITTDTKSQEWTQGTPPPQHTFN 507
Cdd:MTH00079 480 RLVLHDNYINSSPEYSLSSYVFGHSYQ 506
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
13-477 |
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: 577.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 13 HKDIGTLYFVFGIMAGISGSVTSLMVRMQLIQPGQSSGGDSLYNMFITYHALTMIFFMVMPIMIGGFGNWLVPlMLGAPD 92
Cdd:cd00919 1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 93 MAFPRLNNMSFWLLPPAFLLLVSSAWFNSGVGTGWTIYPPLSGNLAHAGPSMDLAIFALHLAGASSILGAINFITTCINM 172
Cdd:cd00919 80 LAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 173 SPHHMSPHNWPLFVWSVFLTAVLLLLSLPVLAAAITMLLTDRNLNTTFFDPNGGGDPILFQHLFWFFGHPEVYILILPGF 252
Cdd:cd00919 160 RAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 253 GIISHIVMHHSsKKEPFGYVSMVWAMLAITVLGFIVWAHHMFTVGLDIDTRAYFSAATMTIAVPTGIKVFSWAATIFGGK 332
Cdd:cd00919 240 GAISEIIPTFS-GKPLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 333 IHWTVPMFWAAGFIYLFTLGGLTGIMLSNSSIDTMLHDTYYVVAHFHYVLSMGAVFAILAGLTYWFPMLTGYSLNQTMAK 412
Cdd:cd00919 319 IRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGK 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145976930 413 AQFWTMFTGVNITFFPQHMLGLAGMPRRYSDFPDAYAIWSTMSTTGSIISFTSAISMIAILWEAF 477
Cdd:cd00919 399 IHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
2-512 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 557.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 2 STMNRWFLSTNHKDIGTLYFVFGIMAGISGSVTSLMVRMQLIQPGQSSGGDSLYNMFITYHALTMIFFMVMPiMIGGFGN 81
Cdd:COG0843 4 SGWRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 82 WLVPLMLGAPDMAFPRLNNMSFWLLPPAFLLLVSSAWFNSGVGTGWTIYPPLSGNLAHAGPSMDLAIFALHLAGASSILG 161
Cdd:COG0843 83 YLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 162 AINFITTCINMSPHHMSPHNWPLFVWSVFLTAVLLLLSLPVLAAAITMLLTDRNLNTTFFDPNGGGDPILFQHLFWFFGH 241
Cdd:COG0843 163 GVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 242 PEVYILILPGFGIISHIVMHHSSKKePFGYVSMVWAMLAITVLGFIVWAHHMFTVGLDIDTRAYFSAATMTIAVPTGIKV 321
Cdd:COG0843 243 PEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 322 FSWAATIFGGKIHWTVPMFWAAGFIYLFTLGGLTGIMLSNSSIDTMLHDTYYVVAHFHYVLSMGAVFAILAGLTYWFPML 401
Cdd:COG0843 322 FNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKM 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 402 TGYSLNQTMAKAQFWTMFTGVNITFFPQHMLGLAGMPRRYSDFP--DAYAIWSTMSTTGSIISFTSAISMIAILWEAFSK 479
Cdd:COG0843 402 TGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRK 481
|
490 500 510
....*....|....*....|....*....|...
gi 145976930 480 KRLTTPITTDTKSQEWTQGTPPPQHTFNTPPMI 512
Cdd:COG0843 482 GPKAGGNPWGARTLEWATPSPPPLYNFASIPVV 514
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
8-506 |
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: 555.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 8 FLSTNHKDIGTLYFVFGIMAGISGSVTSLMVRMQLIQPGQSSGGDSLYNMFITYHALTMIFFMVMPIMiGGFGNWLVPLM 87
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 88 LGAPDMAFPRLNNMSFWLLPPAFLLLVSSAWFNSGVGTGWTIYPPLSGNLAHAGPSMDLAIFALHLAGASSILGAINFIT 167
Cdd:TIGR02891 80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 168 TCINMSPHHMSPHNWPLFVWSVFLTAVLLLLSLPVLAAAITMLLTDRNLNTTFFDPNGGGDPILFQHLFWFFGHPEVYIL 247
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 248 ILPGFGIISHIVMHHSsKKEPFGYVSMVWAMLAITVLGFIVWAHHMFTVGLDIDTRAYFSAATMTIAVPTGIKVFSWAAT 327
Cdd:TIGR02891 240 FLPAFGIISEILPTFA-RKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 328 IFGGKIHWTVPMFWAAGFIYLFTLGGLTGIMLSNSSIDTMLHDTYYVVAHFHYVLSMGAVFAILAGLTYWFPMLTGYSLN 407
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 408 QTMAKAQFWTMFTGVNITFFPQHMLGLAGMPRRYSDFPDA--YAIWSTMSTTGSIISFTSAISMIAILWEAFSKKRLTTP 485
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGA 478
|
490 500
....*....|....*....|.
gi 145976930 486 ITTDTKSQEWTQGTPPPQHTF 506
Cdd:TIGR02891 479 NPWGATTLEWTTSSPPPAHNF 499
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-512 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 555.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 1 MSTMNRWFLSTNHKDIGTLYFVFGIMAGISGSVTSLMVRMQLIQPGQSSGGDSLYNMFITYHALTMIFFMVMPIMIGGFG 80
Cdd:MTH00026 1 MTSFVRWFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 81 NWLVPLMLGAPDMAFPRLNNMSFWLLPPAFLLLVSSAWFNSGVGTGWTIYPPLSGNLAHAGPSMDLAIFALHLAGASSIL 160
Cdd:MTH00026 81 NWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 161 GAINFITTCINMSPHHMSPHNWPLFVWSVFLTAVLLLLSLPVLAAAITMLLTDRNLNTTFFDPNGGGDPILFQHLFWFFG 240
Cdd:MTH00026 161 GAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 241 HPEVYILILPGFGIISHIVMHHSSKKEPFGYVSMVWAMLAITVLGFIVWAHHMFTVGLDIDTRAYFSAATMTIAVPTGIK 320
Cdd:MTH00026 241 HPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 321 VFSWAATIFGG--KIHWTVPMFWAAGFIYLFTLGGLTGIMLSNSSIDTMLHDTYYVVAHFHYVLSMGAVFAILAGLTYWF 398
Cdd:MTH00026 321 IFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 399 PMLTGYSLNQTMAKAQFWTMFTGVNITFFPQHMLGLAGMPRRYSDFPDAYAIWSTMSTTGSIISFTSAISMIAILWEAFS 478
Cdd:MTH00026 401 GKITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAYY 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 145976930 479 KKR---------------LTTPITTDTksQEWTQGTPPPQHTFNTPPMI 512
Cdd:MTH00026 481 REEpfdinimakgplipfSCQPAHFDT--LEWSLTSPPEHHTYNELPYI 527
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
7-506 |
5.66e-169 |
|
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: 486.70 E-value: 5.66e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 7 WFLSTNHKDIGTLYFVFGIMAGISGSVTSLMVRMQLIQPGQSSGGDSLYNMFITYHALTMIFFMVMPIMIGgFGNWLVPL 86
Cdd:cd01662 1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 87 MLGAPDMAFPRLNNMSFWLLPPAFLLLVSSAWFNSGVGTGWTIYPPLSGNLAHAGPSMDLAIFALHLAGASSILGAINFI 166
Cdd:cd01662 80 QIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 167 TTCINMSPHHMSPHNWPLFVWSVFLTAVLLLLSLPVLAAAITMLLTDRNLNTTFFDPNGGGDPILFQHLFWFFGHPEVYI 246
Cdd:cd01662 160 VTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 247 LILPGFGIISHIVMHHSsKKEPFGYVSMVWAMLAITVLGFIVWAHHMFTVGLDIDTRAYFSAATMTIAVPTGIKVFSWAA 326
Cdd:cd01662 240 LILPAFGIFSEIVPTFS-RKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 327 TIFGGKIHWTVPMFWAAGFIYLFTLGGLTGIMLSNSSIDTMLHDTYYVVAHFHYVLSMGAVFAILAGLTYWFPMLTGYSL 406
Cdd:cd01662 319 TMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRML 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 407 NQTMAKAQFWTMFTGVNITFFPQHMLGLAGMPRRYSDFPDAYAiWSTMSTTGSIISFTSAISMIAILWEAFSKKRLTTPI 486
Cdd:cd01662 399 NERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLPGPG-WDPLNLISTIGAFLIAAGVLLFLINVIVSIRKGKRD 477
|
490 500
....*....|....*....|....
gi 145976930 487 TT----DTKSQEWTQGTPPPQHTF 506
Cdd:cd01662 478 ATgdpwGARTLEWATSSPPPAYNF 501
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-481 |
7.83e-167 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 481.87 E-value: 7.83e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 1 MSTMNRWFLSTNHKDIGTLYFVFGIMAGISGSVTSLMVRMQLIQPGQSSGGDSLYNMFITYHALTMIFFMVMPIMIGGFG 80
Cdd:MTH00048 1 MNSLLSWLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 81 NWLVPLMLGAPDMAFPRLNNMSFWLLPPAFLLLVSSAWFnsGVGTGWTIYPPLSGNLAHAGPSMDLAIFALHLAGASSIL 160
Cdd:MTH00048 81 NYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 161 GAINFITTCINMSPHHMSpHNWPLFVWSVFLTAVLLLLSLPVLAAAITMLLTDRNLNTTFFDPNGGGDPILFQHLFWFFG 240
Cdd:MTH00048 159 GSINFICTIYSAFMTNVF-SRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 241 HPEVYILILPGFGIISHIVMHHSSKKEPFGYVSMVWAMLAITVLGFIVWAHHMFTVGLDIDTRAYFSAATMTIAVPTGIK 320
Cdd:MTH00048 238 HPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 321 VFSWAATIFGGKIHWTVP-MFWAAGFIYLFTLGGLTGIMLSNSSIDTMLHDTYYVVAHFHYVLSMGAVFAILAGLTYWFP 399
Cdd:MTH00048 318 VFSWLYMLLNSRVRKSDPvVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWP 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 400 MLTGYSLNQTMAKAQFWTMFTGVNITFFPQHMLGLAGMPRRYSDFPDAYAIWSTMSTTGSIISFTSAISMIAILWEAFSK 479
Cdd:MTH00048 398 LITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVV 477
|
..
gi 145976930 480 KR 481
Cdd:MTH00048 478 KN 479
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
15-461 |
2.13e-127 |
|
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: 378.07 E-value: 2.13e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 15 DIGTLYFVFGIMAGISGSVTSLMVRMQLIQPGQSSGGDSLYNMFITYHALTMIFFMVMPiMIGGFGNWLVPLMLGAPDMA 94
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 95 FPRLNNMSFWLLPPAFLLLVSSAwfnSGVGTGWTIYPPLSGnlahagpsMDLAIFALHLAGASSILGAINFITTCINMSP 174
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 175 HHMSPhNWPLFVWSVFLTAVLLLLSLPVLAAAITMLLTDRNLNTtffdpnGGGDPILFQHLFWFFGHPEVYILILPGFGI 254
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 255 ISHIVMHHSsKKEPFGYVSMVWAMLAITVLGFIVWAHHMFTVGLDIDTRAYFSAATMTIAVPTGIKVFSWAATIFGGKIH 334
Cdd:pfam00115 222 IYYILPKFA-GRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 335 W-TVPMFWAAGFIYLFTLGGLTGIMLSNSSIDTMLHDTYYVVAHFHYVLSMGAVFAILAGLTYWFPMLTGYSLNQTMAKA 413
Cdd:pfam00115 301 FrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 145976930 414 QFWTMFTGVNITFFPQHMLGLAGMPRRYSDF----PDAYAIWSTMSTTGSII 461
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAPPfietVPAFQPLNWIRTIGGVL 432
|
|
| CyoB |
TIGR02843 |
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ... |
5-514 |
3.96e-124 |
|
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain which reacts with oxygen, reducing it to water with the concomitant transport of 4 protons across the membrane. Also known as the cytochrome bo complex, cytochrome o ubiquinol oxidase contains four subunits, two heme b cofactors and a copper atom which is believed to be the oxygen active site. This complex is structurally related to the cytochrome caa3 oxidases which utilize cytochrome c as the reductant and contain heme a cofactors, as well as the intermediate form aa3 oxidases which also react directly with quinones as the reductant. [Energy metabolism, Electron transport]
Pssm-ID: 131890 Cd Length: 646 Bit Score: 377.09 E-value: 3.96e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 5 NRWFLSTNHKDIGTLYFVFGIMAGISGSVTSLMVRMQL-IQPGQSSG--GDSLYNMFITYHALTMIFFMVMPIMIGGFgN 81
Cdd:TIGR02843 45 NEWLTTVDHKKIGIMYIIVALVMLLRGFADAIMMRTQQaLASGGSAGylPPHHYDQIFTAHGVIMIFFVAMPFVFGLM-N 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 82 WLVPLMLGAPDMAFPRLNNMSFWLLPPAFLLLVSSAWFNSGVGTGWTIYPPLSGNLAHAGPSMDLAIFALHLAGASSILG 161
Cdd:TIGR02843 124 LVVPLQIGARDVAFPFLNSLSFWLTVVGAILVNVSLGVGEFAQTGWLAYPPLSELQYSPGVGVDYYIWALQISGIGTLLT 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 162 AINFITTCINMSPHHMSPHNWPLFVWSVFLTAVLLLLSLPVLAAAITMLLTDRNLNTTFFDPNGGGDPILFQHLFWFFGH 241
Cdd:TIGR02843 204 GINFFVTIIKMRAPGMTLMKMPVFTWTSLCSNVLIIASFPILTVTLALLTLDRYLGMHFFTNEAGGNPMMYVNLIWAWGH 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 242 PEVYILILPGFGIISHIVMHHSSKKEpFGYVSMVWAMLAITVLGFIVWAHHMFTVGLDIDTRAYFSAATMTIAVPTGIKV 321
Cdd:TIGR02843 284 PEVYILILPAFGIFSEVVATFSRKRL-FGYTSMVWATIAITVLSFIVWLHHFFTMGAGANVNAFFGIATMIIAIPTGVKI 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 322 FSWAATIFGGKIHWTVPMFWAAGFIYLFTLGGLTGIMLSNSSIDTMLHDTYYVVAHFHYVLSMGAVFAILAGLTYWFPML 401
Cdd:TIGR02843 363 FNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLLAVPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWFPKA 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 402 TGYSLNQTMAKAQFWTMFTGVNITFFPQHMLGLAGMPRRYSDFPD-AYAIWSTMSTTGSIISFTSAISMIAILWEAFSKK 480
Cdd:TIGR02843 443 FGFKLNEKLGKRSFWCWFIGFYLAFMPLYILGFMGMTRRLNHYDNpEWHPMLIIAAFGAFLIACGILCQIIQIFVSIRDR 522
|
490 500 510
....*....|....*....|....*....|....*..
gi 145976930 481 RLTTPITTDT---KSQEWTQGTPPPQHTFNTPPMIQQ 514
Cdd:TIGR02843 523 DQNRDTTGDPwggRTLEWSTSSPPPFYNFAVIPKVQD 559
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
5-514 |
3.17e-107 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 334.21 E-value: 3.17e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 5 NRWFLSTNHKDIGTLYFVFGIMAGISGSVTSLMVRMQLIQPGQSSGG---DSLYNMFITYHALTMIFFMVMPIMIGgFGN 81
Cdd:PRK15017 46 KEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQQALASAGEAGflpPHHYDQIFTAHGVIMIFFVAMPFVIG-LMN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 82 WLVPLMLGAPDMAFPRLNNMSFWLLPPAFLLLVSSAWFNSGVGTGWTIYPPLSGNLAHAGPSMDLAIFALHLAGASSILG 161
Cdd:PRK15017 125 LVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLT 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 162 AINFITTCINMSPHHMSPHNWPLFVWSVFLTAVLLLLSLPVLAAAITMLLTDRNLNTTFFDPNGGGDPILFQHLFWFFGH 241
Cdd:PRK15017 205 GINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGH 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 242 PEVYILILPGFGIISHIVMHHSsKKEPFGYVSMVWAMLAITVLGFIVWAHHMFTVGLDIDTRAYFSAATMTIAVPTGIKV 321
Cdd:PRK15017 285 PEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKI 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 322 FSWAATIFGGKIHWTVPMFWAAGFIYLFTLGGLTGIMLSNSSIDTMLHDTYYVVAHFHYVLSMGAVFAILAGLTYWFPML 401
Cdd:PRK15017 364 FNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKA 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 402 TGYSLNQTMAKAQFWTMFTGVNITFFPQHMLGLAGMPRRYS-DFPDAYAIWSTMSTTGSIISFTSAISMIAILWEAFSKK 480
Cdd:PRK15017 444 FGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSqQIDPQFHTMLMIAASGAALIALGILCQVIQMYVSIRDR 523
|
490 500 510
....*....|....*....|....*....|....*..
gi 145976930 481 RLTTPITTD---TKSQEWTQGTPPPQHTFNTPPMIQQ 514
Cdd:PRK15017 524 DQNRDLTGDpwgGRTLEWATSSPPPFYNFAVVPHVHE 560
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
228-473 |
1.28e-21 |
|
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: 97.74 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 228 DPILFQHLFWFFGHPEVYILILPGFGIISHIVMHHSSKK---EPFGYVSMVWAMLAITVLGFivwaHHMFT-VGLDIDTR 303
Cdd:cd01660 200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKlfsDPLARLAFILFLLFSTPVGF----HHQFAdPGIGPGWK 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 304 AYFSAATMTIAVPTGIKVFSWAATI------------FG--GKIHWTVPMFWAAGF-IYLFTLGGLTGIMLSNSSIDTML 368
Cdd:cd01660 276 FIHMVLTFMVALPSLLTAFTVFASLeiagrlrggkglFGwiRALPWGDPMFLALFLaMLMFIPGGAGGIINASYQLNYVV 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145976930 369 HDTYYVVAHFHyvLSMGAVFAILA-GLTYWF-PMLTGYSLNQ-TMAKAQFWTMFTGVNITFFPQHMLGLAGMPRR--YSD 443
Cdd:cd01660 356 HNTAWVPGHFH--LTVGGAVALTFmAVAYWLvPHLTGRELAAkRLALAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQ 433
|
250 260 270
....*....|....*....|....*....|....*
gi 145976930 444 FPDAYAI-----WSTMSTTGSIISFTSAISMIAIL 473
Cdd:cd01660 434 YGGLPAAgewapYQQLMAIGGTILFVSGALFLYIL 468
|
|
| |
