|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-519 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 945.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 1 MSLYLSRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDQLYNVIVTAHAFLMIFFLVMPVMIGGF 80
Cdd:MTH00184 1 MSLYLSRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 81 GNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGVGTGWTVYPPLAGIQAHSGGSVDMAIFSLHLAGISSI 160
Cdd:MTH00184 81 GNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 161 LGAMNFITTIFNMRAPGITMDRLPLFVWSILITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFF 240
Cdd:MTH00184 161 LGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 241 GHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFSAATMIIAVPTGI 320
Cdd:MTH00184 241 GHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 321 KIFSWVATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFG 400
Cdd:MTH00184 321 KIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 401 KISGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVAVVWFIYIVYDAYAR 480
Cdd:MTH00184 401 KITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVR 480
|
490 500 510
....*....|....*....|....*....|....*....
gi 284794669 481 EIKFVGWVEDSGYYPSLEWAQTSPPAHHTYNELPYVYAG 519
Cdd:MTH00184 481 EIKFVGWVEDSGHYPSLEWAQTSPPAHHTYNELPYVYKG 519
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
12-501 |
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: 883.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 12 TNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDQLYNVIVTAHAFLMIFFLVMPVMIGGFGNWFVPLYIGA 91
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 92 PDMAFPRLNNISFWLLPPALTLLLGSAFVEQGVGTGWTVYPPLAGIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIF 171
Cdd:cd01663 81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 172 NMRAPGITMDRLPLFVWSILITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILP 251
Cdd:cd01663 161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 252 GFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFSAATMIIAVPTGIKIFSWVATIFG 331
Cdd:cd01663 241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 332 GSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKISGYCYNEVY 411
Cdd:cd01663 321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 412 GKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVAVVWFIYIVYDAYAREIKFVGWVEDS 491
Cdd:cd01663 401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGEG 480
|
490
....*....|
gi 284794669 492 gyYPSLEWAQ 501
Cdd:cd01663 481 --STSLEWTL 488
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
9-510 |
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: 611.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 9 LFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDQLYNVIVTAHAFLMIFFLVMPvMIGGFGNWFVPLY 88
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 89 IGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGVGTGWTVYPPLAGIQAHSGGSVDMAIFSLHLAGISSILGAMNFIT 168
Cdd:TIGR02891 80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 169 TIFNMRAPGITMDRLPLFVWSILITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYIL 248
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 249 ILPGFGIISQIIPTFaAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFSAATMIIAVPTGIKIFSWVAT 328
Cdd:TIGR02891 240 FLPAFGIISEILPTF-ARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 329 IFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKISGYCYN 408
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 409 EVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDF--HDSFAGWNQISSLGSVISIVAVVWFIYIVYDAYAREIKFVG 486
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYppQMGFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGA 478
|
490 500
....*....|....*....|....
gi 284794669 487 WVEDSGyypSLEWAQTSPPAHHTY 510
Cdd:TIGR02891 479 NPWGAT---TLEWTTSSPPPAHNF 499
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
5-517 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 606.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 5 LSRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDQLYNVIVTAHAFLMIFFLVMPvMIGGFGNWF 84
Cdd:COG0843 6 WRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 85 VPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGVGTGWTVYPPLAGIQAHSGGSVDMAIFSLHLAGISSILGAM 164
Cdd:COG0843 85 VPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 165 NFITTIFNMRAPGITMDRLPLFVWSILITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPE 244
Cdd:COG0843 165 NFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 245 VYILILPGFGIISQIIPTFAAKKqIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFSAATMIIAVPTGIKIFS 324
Cdd:COG0843 245 VYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFN 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 325 WVATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKISG 404
Cdd:COG0843 324 WIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 405 YCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDF--HDSFAGWNQISSLGSVISIVAVVWFIYIVYDAYAREI 482
Cdd:COG0843 404 RMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYppEPGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGP 483
|
490 500 510
....*....|....*....|....*....|....*
gi 284794669 483 KFVGWVEDSGyypSLEWAQTSPPAHHTYNELPYVY 517
Cdd:COG0843 484 KAGGNPWGAR---TLEWATPSPPPLYNFASIPVVR 515
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
16-462 |
1.53e-142 |
|
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: 417.36 E-value: 1.53e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 16 DIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDQLYNVIVTAHAFLMIFFLVMPvMIGGFGNWFVPLYIGAPDMA 95
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 96 FPRLNNISFWLLPPALTLLLGSAfveQGVGTGWTVYPPLAGiqahsggsVDMAIFSLHLAGISSILGAMNFITTIFNMRA 175
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 176 PGITMdRLPLFVWSILITAFLLLLSLPVLAGGITMLLTDRNFNttffdpAGGGDPILFQHLFWFFGHPEVYILILPGFGI 255
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 256 ISQIIPTFAaKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFSAATMIIAVPTGIKIFSWVATIFGGSLR 335
Cdd:pfam00115 222 IYYILPKFA-GRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 336 L-DTPMLWAIGFVFLFTMGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKISGYCYNEVYGKI 414
Cdd:pfam00115 301 FrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 284794669 415 HFWLMFIGVNLTFFPQHFLGLAGLPRRYSDF----HDSFAGWNQISSLGSVI 462
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAPPfietVPAFQPLNWIRTIGGVL 432
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-519 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 945.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 1 MSLYLSRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDQLYNVIVTAHAFLMIFFLVMPVMIGGF 80
Cdd:MTH00184 1 MSLYLSRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 81 GNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGVGTGWTVYPPLAGIQAHSGGSVDMAIFSLHLAGISSI 160
Cdd:MTH00184 81 GNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 161 LGAMNFITTIFNMRAPGITMDRLPLFVWSILITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFF 240
Cdd:MTH00184 161 LGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 241 GHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFSAATMIIAVPTGI 320
Cdd:MTH00184 241 GHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 321 KIFSWVATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFG 400
Cdd:MTH00184 321 KIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 401 KISGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVAVVWFIYIVYDAYAR 480
Cdd:MTH00184 401 KITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVR 480
|
490 500 510
....*....|....*....|....*....|....*....
gi 284794669 481 EIKFVGWVEDSGYYPSLEWAQTSPPAHHTYNELPYVYAG 519
Cdd:MTH00184 481 EIKFVGWVEDSGHYPSLEWAQTSPPAHHTYNELPYVYKG 519
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
12-501 |
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: 883.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 12 TNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDQLYNVIVTAHAFLMIFFLVMPVMIGGFGNWFVPLYIGA 91
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 92 PDMAFPRLNNISFWLLPPALTLLLGSAFVEQGVGTGWTVYPPLAGIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIF 171
Cdd:cd01663 81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 172 NMRAPGITMDRLPLFVWSILITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILP 251
Cdd:cd01663 161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 252 GFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFSAATMIIAVPTGIKIFSWVATIFG 331
Cdd:cd01663 241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 332 GSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKISGYCYNEVY 411
Cdd:cd01663 321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 412 GKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVAVVWFIYIVYDAYAREIKFVGWVEDS 491
Cdd:cd01663 401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGEG 480
|
490
....*....|
gi 284794669 492 gyYPSLEWAQ 501
Cdd:cd01663 481 --STSLEWTL 488
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
5-517 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 874.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 5 LSRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDQLYNVIVTAHAFLMIFFLVMPVMIGGFGNWF 84
Cdd:MTH00153 1 MNKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 85 VPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGVGTGWTVYPPLAGIQAHSGGSVDMAIFSLHLAGISSILGAM 164
Cdd:MTH00153 81 VPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 165 NFITTIFNMRAPGITMDRLPLFVWSILITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPE 244
Cdd:MTH00153 161 NFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 245 VYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFSAATMIIAVPTGIKIFS 324
Cdd:MTH00153 241 VYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 325 WVATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKISG 404
Cdd:MTH00153 321 WLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 405 YCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVAVVWFIYIVYDAYA--REI 482
Cdd:MTH00153 401 LTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMIskRPV 480
|
490 500 510
....*....|....*....|....*....|....*
gi 284794669 483 KFVgwvedSGYYPSLEWAQTSPPAHHTYNELPYVY 517
Cdd:MTH00153 481 LFS-----LNLSSSIEWLQNLPPAEHSYSELPLLT 510
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-522 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 873.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 1 MSLYLSRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDQLYNVIVTAHAFLMIFFLVMPVMIGGF 80
Cdd:MTH00182 1 KNLYLTRWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 81 GNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGVGTGWTVYPPLAGIQAHSGGSVDMAIFSLHLAGISSI 160
Cdd:MTH00182 81 GNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 161 LGAMNFITTIFNMRAPGITMDRLPLFVWSILITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFF 240
Cdd:MTH00182 161 LGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 241 GHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFSAATMIIAVPTGI 320
Cdd:MTH00182 241 GHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 321 KIFSWVATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFG 400
Cdd:MTH00182 321 KVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 401 KISGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVAVVWFIYIVYDAYAR 480
Cdd:MTH00182 401 KITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVR 480
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 284794669 481 EIKFVGWVEDSGY-YPSLEWAQTSPPAHHTYNELPYVYAGQSG 522
Cdd:MTH00182 481 EEKFIGWKEGTGEsWASLEWVHSSPPLFHTYNELPFVYKSKLS 523
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
3-516 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 818.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 3 LYLSRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDQLYNVIVTAHAFLMIFFLVMPVMIGGFGN 82
Cdd:MTH00167 1 MWINRWLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 83 WFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGVGTGWTVYPPLAGIQAHSGGSVDMAIFSLHLAGISSILG 162
Cdd:MTH00167 81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 163 AMNFITTIFNMRAPGITMDRLPLFVWSILITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGH 242
Cdd:MTH00167 161 SINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 243 PEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFSAATMIIAVPTGIKI 322
Cdd:MTH00167 241 PEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 323 FSWVATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKI 402
Cdd:MTH00167 321 FSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 403 SGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVAVVWFIYIVYDAYAREI 482
Cdd:MTH00167 401 TGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKR 480
|
490 500 510
....*....|....*....|....*....|....
gi 284794669 483 KFVGWVEDSGyypSLEWAQTSPPAHHTYNELPYV 516
Cdd:MTH00167 481 KLLPVELTST---NVEWLHGCPPPHHTWEEPPFV 511
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
3-517 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 802.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 3 LYLSRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDQLYNVIVTAHAFLMIFFLVMPVMIGGFGN 82
Cdd:MTH00116 1 MFITRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 83 WFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGVGTGWTVYPPLAGIQAHSGGSVDMAIFSLHLAGISSILG 162
Cdd:MTH00116 81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 163 AMNFITTIFNMRAPGITMDRLPLFVWSILITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGH 242
Cdd:MTH00116 161 AINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 243 PEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFSAATMIIAVPTGIKI 322
Cdd:MTH00116 241 PEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 323 FSWVATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKI 402
Cdd:MTH00116 321 FSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 403 SGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVAVVWFIYIVYDAYAREI 482
Cdd:MTH00116 401 TGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKR 480
|
490 500 510
....*....|....*....|....*....|....*
gi 284794669 483 KFvgwVEDSGYYPSLEWAQTSPPAHHTYNELPYVY 517
Cdd:MTH00116 481 KV---LQPELTTTNIEWIHGCPPPYHTFEEPAFVQ 512
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
6-517 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 800.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 6 SRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDQLYNVIVTAHAFLMIFFLVMPVMIGGFGNWFV 85
Cdd:MTH00223 1 MRWLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 86 PLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGVGTGWTVYPPLAGIQAHSGGSVDMAIFSLHLAGISSILGAMN 165
Cdd:MTH00223 81 PLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 166 FITTIFNMRAPGITMDRLPLFVWSILITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEV 245
Cdd:MTH00223 161 FITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 246 YILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFSAATMIIAVPTGIKIFSW 325
Cdd:MTH00223 241 YILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSW 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 326 VATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKISGY 405
Cdd:MTH00223 321 LATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 406 CYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVAVVWFIYIVYDAYAREIKFV 485
Cdd:MTH00223 401 TLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVV 480
|
490 500 510
....*....|....*....|....*....|..
gi 284794669 486 GWVEDSGyypSLEWAQTSPPAHHTYNELPYVY 517
Cdd:MTH00223 481 WSGHLST---SLEWDNLLPADFHNNSETGALV 509
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
5-517 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 777.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 5 LSRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDQLYNVIVTAHAFLMIFFLVMPVMIGGFGNWF 84
Cdd:MTH00142 1 MMRWLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 85 VPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGVGTGWTVYPPLAGIQAHSGGSVDMAIFSLHLAGISSILGAM 164
Cdd:MTH00142 81 VPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 165 NFITTIFNMRAPGITMDRLPLFVWSILITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPE 244
Cdd:MTH00142 161 NFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 245 VYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFSAATMIIAVPTGIKIFS 324
Cdd:MTH00142 241 VYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 325 WVATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKISG 404
Cdd:MTH00142 321 WLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 405 YCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVAVVWFIYIVYDAYA--REI 482
Cdd:MTH00142 401 LTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVsqRLV 480
|
490 500 510
....*....|....*....|....*....|....*
gi 284794669 483 KFVGWVEDsgyypSLEWAQTSPPAHHTYNELPYVY 517
Cdd:MTH00142 481 MWSSHLST-----SLEWSHRLPPDFHTYDELPILV 510
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
3-516 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 724.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 3 LYLSRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDQLYNVIVTAHAFLMIFFLVMPVMIGGFGN 82
Cdd:MTH00037 1 MQLSRWLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 83 WFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGVGTGWTVYPPLAGIQAHSGGSVDMAIFSLHLAGISSILG 162
Cdd:MTH00037 81 WLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 163 AMNFITTIFNMRAPGITMDRLPLFVWSILITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGH 242
Cdd:MTH00037 161 SINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 243 PEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFSAATMIIAVPTGIKI 322
Cdd:MTH00037 241 PEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 323 FSWVATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKI 402
Cdd:MTH00037 321 FSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 403 SGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVAVVWFIYIVYDAYAREI 482
Cdd:MTH00037 401 SGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQR 480
|
490 500 510
....*....|....*....|....*....|....*
gi 284794669 483 KFVGWVEDSGyypSLEWAQTS-PPAHHTYNELPYV 516
Cdd:MTH00037 481 EVISPEFSSS---SLEWQYSSfPPSHHTFDETPST 512
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
5-516 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 717.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 5 LSRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDQLYNVIVTAHAFLMIFFLVMPVMIGGFGNWF 84
Cdd:MTH00183 3 ITRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 85 VPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGVGTGWTVYPPLAGIQAHSGGSVDMAIFSLHLAGISSILGAM 164
Cdd:MTH00183 83 IPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 165 NFITTIFNMRAPGITMDRLPLFVWSILITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPE 244
Cdd:MTH00183 163 NFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 245 VYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFSAATMIIAVPTGIKIFS 324
Cdd:MTH00183 243 VYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 325 WVATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKISG 404
Cdd:MTH00183 323 WLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 405 YCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVAVVWFIYIVYDAYA--REI 482
Cdd:MTH00183 403 YTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAakREV 482
|
490 500 510
....*....|....*....|....*....|....
gi 284794669 483 KFVGWVedsgyYPSLEWAQTSPPAHHTYNELPYV 516
Cdd:MTH00183 483 LSVELT-----STNVEWLHGCPPPYHTFEEPAFV 511
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
3-516 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 710.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 3 LYLSRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDQLYNVIVTAHAFLMIFFLVMPVMIGGFGN 82
Cdd:MTH00103 1 MFINRWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 83 WFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGVGTGWTVYPPLAGIQAHSGGSVDMAIFSLHLAGISSILG 162
Cdd:MTH00103 81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 163 AMNFITTIFNMRAPGITMDRLPLFVWSILITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGH 242
Cdd:MTH00103 161 AINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 243 PEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFSAATMIIAVPTGIKI 322
Cdd:MTH00103 241 PEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 323 FSWVATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKI 402
Cdd:MTH00103 321 FSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 403 SGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVAVVWFIYIVYDAYAREI 482
Cdd:MTH00103 401 SGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKR 480
|
490 500 510
....*....|....*....|....*....|....
gi 284794669 483 KfVGWVEDSGYypSLEWAQTSPPAHHTYNELPYV 516
Cdd:MTH00103 481 E-VLTVELTTT--NLEWLHGCPPPYHTFEEPTYV 511
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
7-519 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 709.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 7 RWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDQLYNVIVTAHAFLMIFFLVMPVMIGGFGNWFVP 86
Cdd:MTH00026 6 RWFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 87 LYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGVGTGWTVYPPLAGIQAHSGGSVDMAIFSLHLAGISSILGAMNF 166
Cdd:MTH00026 86 LMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 167 ITTIFNMRAPGITMDRLPLFVWSILITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVY 246
Cdd:MTH00026 166 ITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 247 ILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFSAATMIIAVPTGIKIFSWV 326
Cdd:MTH00026 246 ILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 327 ATIFGG--SLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKISG 404
Cdd:MTH00026 326 ATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 405 YCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVAVVWFIYIVYDAYAREIKF 484
Cdd:MTH00026 406 YAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAYYREEPF 485
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 284794669 485 ----------VGWVEDSGYYPSLEWAQTSPPAHHTYNELPYVYAG 519
Cdd:MTH00026 486 dinimakgplIPFSCQPAHFDTLEWSLTSPPEHHTYNELPYIVGG 530
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
3-516 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 706.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 3 LYLSRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDQLYNVIVTAHAFLMIFFLVMPVMIGGFGN 82
Cdd:MTH00077 1 MMITRWLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 83 WFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGVGTGWTVYPPLAGIQAHSGGSVDMAIFSLHLAGISSILG 162
Cdd:MTH00077 81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 163 AMNFITTIFNMRAPGITMDRLPLFVWSILITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGH 242
Cdd:MTH00077 161 AINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 243 PEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFSAATMIIAVPTGIKI 322
Cdd:MTH00077 241 PEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 323 FSWVATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKI 402
Cdd:MTH00077 321 FSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 403 SGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVAVVWFIYIVYDAYAREI 482
Cdd:MTH00077 401 SGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKR 480
|
490 500 510
....*....|....*....|....*....|....
gi 284794669 483 KFVGWVEDSgyyPSLEWAQTSPPAHHTYNELPYV 516
Cdd:MTH00077 481 EVLTTELTS---TNIEWLHGCPPPYHTFEEPSFV 511
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
7-512 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 684.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 7 RWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDQLYNVIVTAHAFLMIFFLVMPVMIGGFGNWFVP 86
Cdd:MTH00007 2 RWLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 87 LYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGVGTGWTVYPPLAGIQAHSGGSVDMAIFSLHLAGISSILGAMNF 166
Cdd:MTH00007 82 LMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 167 ITTIFNMRAPGITMDRLPLFVWSILITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVY 246
Cdd:MTH00007 162 ITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 247 ILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFSAATMIIAVPTGIKIFSWV 326
Cdd:MTH00007 242 ILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 327 ATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKISGYC 406
Cdd:MTH00007 322 ATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 407 YNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVAVVWFIYIVYDAYAREIKFVG 486
Cdd:MTH00007 402 LHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIA 481
|
490 500
....*....|....*....|....*.
gi 284794669 487 wveDSGYYPSLEWAQTSPPAHHTYNE 512
Cdd:MTH00007 482 ---SPHMSSSLEWQDTLPLDFHNLPE 504
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
4-512 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 649.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 4 YLSRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDQLYNVIVTAHAFLMIFFLVMPVMIGGFGNW 83
Cdd:MTH00079 3 GLSVWLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 84 FVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGVGTGWTVYPPLAgIQAHSGGSVDMAIFSLHLAGISSILGA 163
Cdd:MTH00079 83 MLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 164 MNFITTIFNMRAPGITMDRLPLFVWSILITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHP 243
Cdd:MTH00079 162 INFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 244 EVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFSAATMIIAVPTGIKIF 323
Cdd:MTH00079 242 EVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 324 SWVATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKIS 403
Cdd:MTH00079 322 SWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 404 GYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVAVVWFIYIVYDAYAREIK 483
Cdd:MTH00079 402 GIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRL 481
|
490 500
....*....|....*....|....*....
gi 284794669 484 FvgwVEDSGYYPSLEWAQTSPPAHHTYNE 512
Cdd:MTH00079 482 V---LHDNYINSSPEYSLSSYVFGHSYQS 507
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
9-510 |
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: 611.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 9 LFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDQLYNVIVTAHAFLMIFFLVMPvMIGGFGNWFVPLY 88
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 89 IGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGVGTGWTVYPPLAGIQAHSGGSVDMAIFSLHLAGISSILGAMNFIT 168
Cdd:TIGR02891 80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 169 TIFNMRAPGITMDRLPLFVWSILITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYIL 248
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 249 ILPGFGIISQIIPTFaAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFSAATMIIAVPTGIKIFSWVAT 328
Cdd:TIGR02891 240 FLPAFGIISEILPTF-ARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 329 IFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKISGYCYN 408
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 409 EVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDF--HDSFAGWNQISSLGSVISIVAVVWFIYIVYDAYAREIKFVG 486
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYppQMGFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGA 478
|
490 500
....*....|....*....|....
gi 284794669 487 WVEDSGyypSLEWAQTSPPAHHTY 510
Cdd:TIGR02891 479 NPWGAT---TLEWTTSSPPPAHNF 499
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
14-478 |
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: 607.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 14 HKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDQLYNVIVTAHAFLMIFFLVMPVMIGGFGNWFVPLyIGAPD 93
Cdd:cd00919 1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPPL-IGARD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 94 MAFPRLNNISFWLLPPALTLLLGSAFVEQGVGTGWTVYPPLAGIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNM 173
Cdd:cd00919 80 LAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 174 RAPGITMDRLPLFVWSILITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGF 253
Cdd:cd00919 160 RAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 254 GIISQIIPTFAAKKqIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFSAATMIIAVPTGIKIFSWVATIFGGS 333
Cdd:cd00919 240 GAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 334 LRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKISGYCYNEVYGK 413
Cdd:cd00919 319 IRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGK 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 284794669 414 IHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVAVVWFIYIVYDAY 478
Cdd:cd00919 399 IHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
5-517 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 606.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 5 LSRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDQLYNVIVTAHAFLMIFFLVMPvMIGGFGNWF 84
Cdd:COG0843 6 WRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 85 VPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGVGTGWTVYPPLAGIQAHSGGSVDMAIFSLHLAGISSILGAM 164
Cdd:COG0843 85 VPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 165 NFITTIFNMRAPGITMDRLPLFVWSILITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPE 244
Cdd:COG0843 165 NFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 245 VYILILPGFGIISQIIPTFAAKKqIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFSAATMIIAVPTGIKIFS 324
Cdd:COG0843 245 VYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFN 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 325 WVATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKISG 404
Cdd:COG0843 324 WIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 405 YCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDF--HDSFAGWNQISSLGSVISIVAVVWFIYIVYDAYAREI 482
Cdd:COG0843 404 RMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYppEPGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGP 483
|
490 500 510
....*....|....*....|....*....|....*
gi 284794669 483 KFVGWVEDSGyypSLEWAQTSPPAHHTYNELPYVY 517
Cdd:COG0843 484 KAGGNPWGAR---TLEWATPSPPPLYNFASIPVVR 515
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
8-508 |
0e+00 |
|
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: 534.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 8 WLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDQLYNVIVTAHAFLMIFFLVMPVMIGgFGNWFVPL 87
Cdd:cd01662 1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 88 YIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGVGTGWTVYPPLAGIQAHSGGSVDMAIFSLHLAGISSILGAMNFI 167
Cdd:cd01662 80 QIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 168 TTIFNMRAPGITMDRLPLFVWSILITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYI 247
Cdd:cd01662 160 VTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 248 LILPGFGIISQIIPTFAaKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFSAATMIIAVPTGIKIFSWVA 327
Cdd:cd01662 240 LILPAFGIFSEIVPTFS-RKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 328 TIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKISGYCY 407
Cdd:cd01662 319 TMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRML 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 408 NEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDF--HDSFAGWNQISSLGSVISIVAVVWFIY-IVYDAYAREIKF 484
Cdd:cd01662 399 NERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYlpGPGWDPLNLISTIGAFLIAAGVLLFLInVIVSIRKGKRDA 478
|
490 500
....*....|....*....|....
gi 284794669 485 VGwveDSGYYPSLEWAQTSPPAHH 508
Cdd:cd01662 479 TG---DPWGARTLEWATSSPPPAY 499
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
3-509 |
3.18e-166 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 480.71 E-value: 3.18e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 3 LYLSRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDQLYNVIVTAHAFLMIFFLVMPVMIGGFGN 82
Cdd:MTH00048 2 NSLLSWLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 83 WFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVeqGVGTGWTVYPPLAGIQAHSGGSVDMAIFSLHLAGISSILG 162
Cdd:MTH00048 82 YLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 163 AMNFITTIFNMRAPGITMdRLPLFVWSILITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGH 242
Cdd:MTH00048 160 SINFICTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 243 PEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFSAATMIIAVPTGIKI 322
Cdd:MTH00048 239 PEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 323 FSWVATIFGGSLRLDTPML-WAIGFVFLFTMGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGK 401
Cdd:MTH00048 319 FSWLYMLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 402 ISGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVAVVWFIYIVYDAYARE 481
Cdd:MTH00048 399 ITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVK 478
|
490 500
....*....|....*....|....*...
gi 284794669 482 IKFVGWVEDSGYYPSLewaQTSPPAHHT 509
Cdd:MTH00048 479 NEVLGLWGSSSCVVNV---LMSPVPYHN 503
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
16-462 |
1.53e-142 |
|
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: 417.36 E-value: 1.53e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 16 DIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDQLYNVIVTAHAFLMIFFLVMPvMIGGFGNWFVPLYIGAPDMA 95
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 96 FPRLNNISFWLLPPALTLLLGSAfveQGVGTGWTVYPPLAGiqahsggsVDMAIFSLHLAGISSILGAMNFITTIFNMRA 175
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 176 PGITMdRLPLFVWSILITAFLLLLSLPVLAGGITMLLTDRNFNttffdpAGGGDPILFQHLFWFFGHPEVYILILPGFGI 255
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 256 ISQIIPTFAaKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFSAATMIIAVPTGIKIFSWVATIFGGSLR 335
Cdd:pfam00115 222 IYYILPKFA-GRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 336 L-DTPMLWAIGFVFLFTMGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKISGYCYNEVYGKI 414
Cdd:pfam00115 301 FrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 284794669 415 HFWLMFIGVNLTFFPQHFLGLAGLPRRYSDF----HDSFAGWNQISSLGSVI 462
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAPPfietVPAFQPLNWIRTIGGVL 432
|
|
| CyoB |
TIGR02843 |
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ... |
8-516 |
3.62e-129 |
|
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: 390.57 E-value: 3.62e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 8 WLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELS-APGSMLG--DDQLYNVIVTAHAFLMIFFLVMPVMIGGFgNWF 84
Cdd:TIGR02843 47 WLTTVDHKKIGIMYIIVALVMLLRGFADAIMMRTQQAlASGGSAGylPPHHYDQIFTAHGVIMIFFVAMPFVFGLM-NLV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 85 VPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGVGTGWTVYPPLAGIQAHSGGSVDMAIFSLHLAGISSILGAM 164
Cdd:TIGR02843 126 VPLQIGARDVAFPFLNSLSFWLTVVGAILVNVSLGVGEFAQTGWLAYPPLSELQYSPGVGVDYYIWALQISGIGTLLTGI 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 165 NFITTIFNMRAPGITMDRLPLFVWSILITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPE 244
Cdd:TIGR02843 206 NFFVTIIKMRAPGMTLMKMPVFTWTSLCSNVLIIASFPILTVTLALLTLDRYLGMHFFTNEAGGNPMMYVNLIWAWGHPE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 245 VYILILPGFGIISQIIPTFAaKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFSAATMIIAVPTGIKIFS 324
Cdd:TIGR02843 286 VYILILPAFGIFSEVVATFS-RKRLFGYTSMVWATIAITVLSFIVWLHHFFTMGAGANVNAFFGIATMIIAIPTGVKIFN 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 325 WVATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKISG 404
Cdd:TIGR02843 365 WLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLLAVPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWFPKAFG 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 405 YCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHD-SFAGWNQISSLGSVISIVAVVWFIYIVYDAYAREIK 483
Cdd:TIGR02843 445 FKLNEKLGKRSFWCWFIGFYLAFMPLYILGFMGMTRRLNHYDNpEWHPMLIIAAFGAFLIACGILCQIIQIFVSIRDRDQ 524
|
490 500 510
....*....|....*....|....*....|...
gi 284794669 484 FVGWVEDSGYYPSLEWAQTSPPAHHTYNELPYV 516
Cdd:TIGR02843 525 NRDTTGDPWGGRTLEWSTSSPPPFYNFAVIPKV 557
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
6-517 |
6.34e-113 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 349.23 E-value: 6.34e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 6 SRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLE---LSAPGSMLGDDQLYNVIVTAHAFLMIFFLVMPVMIGgFGN 82
Cdd:PRK15017 46 KEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQqalASAGEAGFLPPHHYDQIFTAHGVIMIFFVAMPFVIG-LMN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 83 WFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGVGTGWTVYPPLAGIQAHSGGSVDMAIFSLHLAGISSILG 162
Cdd:PRK15017 125 LVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLT 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 163 AMNFITTIFNMRAPGITMDRLPLFVWSILITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGH 242
Cdd:PRK15017 205 GINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGH 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 243 PEVYILILPGFGIISQIIPTFAaKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFSAATMIIAVPTGIKI 322
Cdd:PRK15017 285 PEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKI 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 323 FSWVATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKI 402
Cdd:PRK15017 364 FNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKA 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 403 SGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYS-DFHDSFAGWNQISSLGSVISIVAVVWFIYIVYDAYARE 481
Cdd:PRK15017 444 FGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSqQIDPQFHTMLMIAASGAALIALGILCQVIQMYVSIRDR 523
|
490 500 510
....*....|....*....|....*....|....*.
gi 284794669 482 IKFVGWVEDSGYYPSLEWAQTSPPAHHTYNELPYVY 517
Cdd:PRK15017 524 DQNRDLTGDPWGGRTLEWATSSPPPFYNFAVVPHVH 559
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
21-476 |
2.97e-19 |
|
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: 90.42 E-value: 2.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 21 YLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDQLYNVIVTAHAFLMIFFLVMpVMIGGFGNWFVPLYIGAPDMAfPRLN 100
Cdd:cd01660 9 HFVVAFLALLLGGLFGLLQVLVRTGVFPLPSSGILYYQGLTLHGVLLAIVFTT-FFIMGFFYAIVARALLRSLFN-RRLA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 101 NISFWLLPPaltlllGSAFVEQGVGTG-----WTVYPPLagiQAHSGGSVDMAIFSLHlagiSSILGAMNFITT-IFNMR 174
Cdd:cd01660 87 WAGFWLMVI------GTVMAAVPILLGqasvlYTFYPPL---QAHPLFYIGAALVVVG----SWISGFAMFVTLwRWKKA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 175 APGitmDRLPLFVWSILITAFLLLLSLPVLAGGITMLLTDRNFNTTffdpaGGGDPILFQHLFWFFGHPEVYILILPGFG 254
Cdd:cd01660 154 NPG---KKVPLATFMVVTTMILWLVASLGVALEVLFQLLPWSLGLV-----DTVDVLLSRTLFWWFGHPLVYFWLLPAYI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 255 IISQIIPTFAAKKQIFGYLGMVyAMVSIGILGFIVWAHHMFT-VGMDVDTRAYFSAATMIIAVPTGIKIFSWVATI-FGG 332
Cdd:cd01660 226 AWYTILPKIAGGKLFSDPLARL-AFILFLLFSTPVGFHHQFAdPGIGPGWKFIHMVLTFMVALPSLLTAFTVFASLeIAG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 333 SLR-------------LDTPMLWAIGFVFL-FTMGGLTGIVLANSSLDIALHDTYYVVAHFHyvLSMGAVFAI-FGGFYY 397
Cdd:cd01660 305 RLRggkglfgwiralpWGDPMFLALFLAMLmFIPGGAGGIINASYQLNYVVHNTAWVPGHFH--LTVGGAVALtFMAVAY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284794669 398 WFgkISGYCYNEVYGK----IHFWLMFIGVNLTFFPQHFLGLAGLPRR-----YSDFH--DSFAGWNQISSLGSVISIVA 466
Cdd:cd01660 383 WL--VPHLTGRELAAKrlalAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaeaqYGGLPaaGEWAPYQQLMAIGGTILFVS 460
|
490
....*....|
gi 284794669 467 VVWFIYIVYD 476
Cdd:cd01660 461 GALFLYILFR 470
|
|
| |
