|
Name |
Accession |
Description |
Interval |
E-value |
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
30-509 |
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: 804.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 30 DHKNIGTMYTNFSILAGIVGTLLSLVIRMELSTGNMLDGDGQQYNVIVTAHGLIMIFFVVMPAMLGGFANWFIPIMVGSP 109
Cdd:cd01663 2 NHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 110 DVAFPRLNNISLWLIIVSFFLLLTSSCVGIGVGTGWTVYPPLSTMEYHPGHAVDVGILSLHIAGASSLLGAINFLTTVFN 189
Cdd:cd01663 82 DMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 190 MKIAGLSWSKVSLFVWSILITAVLLVLSLPVLAGGLTMLITDRNFETTFFDPIGGGDPILYQHLFWFFGHPEVYILILPG 269
Cdd:cd01663 162 MRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 270 FGLVSIILSKYS-NKGIFGVKGMISAMSAIGFLGFLVWAHHMYTVGLDVDTRAYFTAATMIIAIPTGIKIFSWLATLWGG 348
Cdd:cd01663 242 FGIISHIISTFSgKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 349 VIKITTPMLFVIGFLVLFTIGGLTGVVLANGGLDISLHDTYYVVAHFHYVLSMGAIFAIFAGYYYYYSIMnstrlFGVVr 428
Cdd:cd01663 322 SIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKI-----TGLS- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 429 YNEQLGRIHFWTMFIGVNVTFFPMHFLGLAGMPRRIGDYPDAYIGWNLIASYGSLITAFGLLFFVVNIFTPYIRRSVNIK 508
Cdd:cd01663 396 YNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIF 475
|
.
gi 7524975 509 N 509
Cdd:cd01663 476 N 476
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
24-493 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 735.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 24 KWIISVDHKNIGTMYTNFSILAGIVGTLLSLVIRMELSTGNMLDGDGQQYNVIVTAHGLIMIFFVVMPAMLGGFANWFIP 103
Cdd:MTH00153 3 KWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 104 IMVGSPDVAFPRLNNISLWLIIVSFFLLLTSSCVGIGVGTGWTVYPPLSTMEYHPGHAVDVGILSLHIAGASSLLGAINF 183
Cdd:MTH00153 83 LMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 184 LTTVFNMKIAGLSWSKVSLFVWSILITAVLLVLSLPVLAGGLTMLITDRNFETTFFDPIGGGDPILYQHLFWFFGHPEVY 263
Cdd:MTH00153 163 ITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 264 ILILPGFGLVSIILSKYSNKG-IFGVKGMISAMSAIGFLGFLVWAHHMYTVGLDVDTRAYFTAATMIIAIPTGIKIFSWL 342
Cdd:MTH00153 243 ILILPGFGMISHIISQESGKKeTFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 343 ATLWGGVIKITTPMLFVIGFLVLFTIGGLTGVVLANGGLDISLHDTYYVVAHFHYVLSMGAIFAIFAGYYYYYSimnstr 422
Cdd:MTH00153 323 ATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFP------ 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7524975 423 LFGVVRYNEQLGRIHFWTMFIGVNVTFFPMHFLGLAGMPRRIGDYPDAYIGWNLIASYGSLITAFGLLFFV 493
Cdd:MTH00153 397 LFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFI 467
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
28-499 |
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: 590.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 28 SVDHKNIGTMYTNFSILAGIVGTLLSLVIRMELSTGNMLDGDGQQYNVIVTAHGLIMIFFVVMPaMLGGFANWFIPIMVG 107
Cdd:TIGR02891 3 TVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 108 SPDVAFPRLNNISLWLIIVSFFLLLTSSCVGIGVGTGWTVYPPLSTMEYHPGHAVDVGILSLHIAGASSLLGAINFLTTV 187
Cdd:TIGR02891 82 ARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 188 FNMKIAGLSWSKVSLFVWSILITAVLLVLSLPVLAGGLTMLITDRNFETTFFDPIGGGDPILYQHLFWFFGHPEVYILIL 267
Cdd:TIGR02891 162 LNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 268 PGFGLVSIILSKYSNKGIFGVKGMISAMSAIGFLGFLVWAHHMYTVGLDVDTRAYFTAATMIIAIPTGIKIFSWLATLWG 347
Cdd:TIGR02891 242 PAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 348 GVIKITTPMLFVIGFLVLFTIGGLTGVVLANGGLDISLHDTYYVVAHFHYVLSMGAIFAIFAGYYYYYSIMNSTrlfgvv 427
Cdd:TIGR02891 322 GSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGR------ 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7524975 428 RYNEQLGRIHFWTMFIGVNVTFFPMHFLGLAGMPRRIGDYPDA--YIGWNLIASYGSLITAFGLLFFVVNIFTP 499
Cdd:TIGR02891 396 MYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWS 469
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
21-503 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 582.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 21 FISKWIISVDHKNIGTMYTNFSILAGIVGTLLSLVIRMELSTGNMLDGDGQQYNVIVTAHGLIMIFFVVMPaMLGGFANW 100
Cdd:COG0843 5 GWRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 101 FIPIMVGSPDVAFPRLNNISLWLIIVSFFLLLTSSCVGIGVGTGWTVYPPLSTMEYHPGHAVDVGILSLHIAGASSLLGA 180
Cdd:COG0843 84 LVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 181 INFLTTVFNMKIAGLSWSKVSLFVWSILITAVLLVLSLPVLAGGLTMLITDRNFETTFFDPIGGGDPILYQHLFWFFGHP 260
Cdd:COG0843 164 VNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 261 EVYILILPGFGLVSIILSKYSNKGIFGVKGMISAMSAIGFLGFLVWAHHMYTVGLDVDTRAYFTAATMIIAIPTGIKIFS 340
Cdd:COG0843 244 EVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFN 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 341 WLATLWGGVIKITTPMLFVIGFLVLFTIGGLTGVVLANGGLDISLHDTYYVVAHFHYVLSMGAIFAIFAGYYYYYSIMns 420
Cdd:COG0843 324 WIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKM-- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 421 trlFGvVRYNEQLGRIHFWTMFIGVNVTFFPMHFLGLAGMPRRIGDYP--DAYIGWNLIASYGSLITAFGLLFFVVNIFT 498
Cdd:COG0843 402 ---TG-RMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVV 477
|
....*
gi 7524975 499 PYIRR 503
Cdd:COG0843 478 SLRKG 482
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
34-484 |
2.80e-137 |
|
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: 411.97 E-value: 2.80e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 34 IGTMYTNFSILAGIVGTLLSLVIRMELSTGNMLDGDGQQYNVIVTAHGLIMIFFVVMPAMlGGFANWFIPIMVGSPDVAF 113
Cdd:pfam00115 2 IGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPFL-FGFGNYLVPLMIGARDMAF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 114 PRLNNISLWLIIVSFFLLLTSscvGIGVGTGWTVYPPLStmeyhpghAVDVGILSLHIAGASSLLGAINFLTTVFNMKIA 193
Cdd:pfam00115 81 PRLNALSFWLVVLGAVLLLAS---FGGATTGWTEYPPLV--------GVDLWYIGLLLAGVSSLLGAINFIVTILKRRAP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 194 GLSWsKVSLFVWSILITAVLLVLSLPVLAGGLTMLITDRNFettffdPIGGGDPILYQHLFWFFGHPEVYILILPGFGLV 273
Cdd:pfam00115 150 GMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSL------GAGGGDPLLDQHLFWWFGHPEVYILILPAFGII 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 274 SIILSKYSNKGIFGVKGMISAMSAIGFLGFLVWAHHMYTVGLDVDTRAYFTAATMIIAIPTGIKIFSWLATLWGGVIKI- 352
Cdd:pfam00115 223 YYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFr 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 353 TTPMLFVIGFLVLFTIGGLTGVVLANGGLDISLHDTYYVVAHFHYVLSMGAIFAIFAGYYYYYSimnstRLFGvVRYNEQ 432
Cdd:pfam00115 303 TTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLP-----KLTG-RMYSEK 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 7524975 433 LGRIHFWTMFIGVNVTFFPMHFLGLAGMPRRI----GDYPDAYIGWNLIASYGSLI 484
Cdd:pfam00115 377 LGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYappfIETVPAFQPLNWIRTIGGVL 432
|
|
| COX2 |
MTH00023 |
cytochrome c oxidase subunit II; Validated |
514-759 |
2.26e-93 |
|
cytochrome c oxidase subunit II; Validated
Pssm-ID: 214402 [Multi-domain] Cd Length: 240 Bit Score: 291.27 E-value: 2.26e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 514 LMGLDFARDWQIGFQDPATPIMEGIIDLHNYIFFYLIVVAVFIGWVMgrilwrfsykwsyptigdIEIFKNFTAYNQIIH 593
Cdd:MTH00023 5 FFYRDIPEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLI------------------VEALNGKFYDRFLVD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 594 GTVIEIVWTLIPTVILYLIAIPSFTLLYAMDEIINPTVTIKIIGHQWYWSYEYGDNASNLIEFDSYMVYERDLAEGQLRL 673
Cdd:MTH00023 67 GTFLEIVWTIIPAVILVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYEGETLEFDSYMVPTSDLNSGDFRL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 674 LEVDNAMVVPVKTHIRLIITSGDVLHSWAIPSFGIKVDAVPGRLNQIGLYVKREGTFYGQCSELCGVDHGFMPIKVQAVK 753
Cdd:MTH00023 147 LEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVS 226
|
....*.
gi 7524975 754 LGEYFS 759
Cdd:MTH00023 227 LDKYIN 232
|
|
| CcO_II_C |
cd13912 |
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ... |
629-759 |
1.07e-81 |
|
C-terminal domain of Cytochrome c Oxidase subunit II; 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. 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 II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.
Pssm-ID: 259979 [Multi-domain] Cd Length: 130 Bit Score: 256.34 E-value: 1.07e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 629 PTVTIKIIGHQWYWSYEYGDNasNLIEFDSYMVYERDLAEGQLRLLEVDNAMVVPVKTHIRLIITSGDVLHSWAIPSFGI 708
Cdd:cd13912 1 PSLTIKAIGHQWYWSYEYSDF--NDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGI 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 7524975 709 KVDAVPGRLNQIGLYVKREGTFYGQCSELCGVDHGFMPIKVQAVKLGEYFS 759
Cdd:cd13912 79 KVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLS 129
|
|
| COX2 |
pfam00116 |
Cytochrome C oxidase subunit II, periplasmic domain; |
632-752 |
8.30e-68 |
|
Cytochrome C oxidase subunit II, periplasmic domain;
Pssm-ID: 395066 [Multi-domain] Cd Length: 120 Bit Score: 219.20 E-value: 8.30e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 632 TIKIIGHQWYWSYEYGDNASnlIEFDSYMVYERDLAEGQLRLLEVDNAMVVPVKTHIRLIITSGDVLHSWAIPSFGIKVD 711
Cdd:pfam00116 2 TIKAIGHQWYWSYEYTDFGD--LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTD 79
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 7524975 712 AVPGRLNQIGLYVKREGTFYGQCSELCGVDHGFMPIKVQAV 752
Cdd:pfam00116 80 AVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
|
|
| CyoA |
COG1622 |
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion]; |
508-757 |
8.36e-56 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
Pssm-ID: 441229 [Multi-domain] Cd Length: 229 Bit Score: 190.81 E-value: 8.36e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 508 KNGAIILMGLDFARDWQIGFQDPATPIMEGIIDLHNYIFFYLIVVAVFIGWVMGRILWRFSYKwsyptigdieifKNFTA 587
Cdd:COG1622 2 KRLLLALLLLALLLSGQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRR------------KGDAD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 588 YNQIIHGTVIEIVWTLIPTVILYLIAIPSFTLLYAMDEIINPTVTIKIIGHQWYWSYEYGDNASnliefdsymvyerdla 667
Cdd:COG1622 70 PAQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGI---------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 668 egqlrllEVDNAMVVPVKTHIRLIITSGDVLHSWAIPSFGIKVDAVPGRLNQIGLYVKREGTFYGQCSELCGVDHGFMPI 747
Cdd:COG1622 134 -------ATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRF 206
|
250
....*....|
gi 7524975 748 KVQAVKLGEY 757
Cdd:COG1622 207 KVVVVSPEEF 216
|
|
| CoxB |
TIGR02866 |
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ... |
530-757 |
2.64e-41 |
|
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]
Pssm-ID: 274329 [Multi-domain] Cd Length: 199 Bit Score: 149.84 E-value: 2.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 530 PATPIMEGIIDLHNYIFFYLIVVAVFIGWVMGRILWRFSYKwsyptiGDIEIFKnftaynQIIHGTVIEIVWTLIPTVIL 609
Cdd:TIGR02866 1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWKFRRK------GDEEKPS------QIHGNRRLEYVWTVIPLIIV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 610 YLIAIPSFT-LLYAMDEIINPTVTIKIIGHQWYWSYEYGDNAsnliefdsymvyerdlaegqlrlLEVDNAMVVPVKTHI 688
Cdd:TIGR02866 69 VGLFAATAKgLLYLERPIPKDALKVKVTGYQWWWDFEYPESG-----------------------FTTVNELVLPAGTPV 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7524975 689 RLIITSGDVLHSWAIPSFGIKVDAVPGRLNQIGLYVKREGTFYGQCSELCGVDHGFMPIKVQAVKLGEY 757
Cdd:TIGR02866 126 ELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEF 194
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
30-509 |
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: 804.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 30 DHKNIGTMYTNFSILAGIVGTLLSLVIRMELSTGNMLDGDGQQYNVIVTAHGLIMIFFVVMPAMLGGFANWFIPIMVGSP 109
Cdd:cd01663 2 NHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 110 DVAFPRLNNISLWLIIVSFFLLLTSSCVGIGVGTGWTVYPPLSTMEYHPGHAVDVGILSLHIAGASSLLGAINFLTTVFN 189
Cdd:cd01663 82 DMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 190 MKIAGLSWSKVSLFVWSILITAVLLVLSLPVLAGGLTMLITDRNFETTFFDPIGGGDPILYQHLFWFFGHPEVYILILPG 269
Cdd:cd01663 162 MRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 270 FGLVSIILSKYS-NKGIFGVKGMISAMSAIGFLGFLVWAHHMYTVGLDVDTRAYFTAATMIIAIPTGIKIFSWLATLWGG 348
Cdd:cd01663 242 FGIISHIISTFSgKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 349 VIKITTPMLFVIGFLVLFTIGGLTGVVLANGGLDISLHDTYYVVAHFHYVLSMGAIFAIFAGYYYYYSIMnstrlFGVVr 428
Cdd:cd01663 322 SIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKI-----TGLS- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 429 YNEQLGRIHFWTMFIGVNVTFFPMHFLGLAGMPRRIGDYPDAYIGWNLIASYGSLITAFGLLFFVVNIFTPYIRRSVNIK 508
Cdd:cd01663 396 YNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIF 475
|
.
gi 7524975 509 N 509
Cdd:cd01663 476 N 476
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
24-493 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 735.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 24 KWIISVDHKNIGTMYTNFSILAGIVGTLLSLVIRMELSTGNMLDGDGQQYNVIVTAHGLIMIFFVVMPAMLGGFANWFIP 103
Cdd:MTH00153 3 KWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 104 IMVGSPDVAFPRLNNISLWLIIVSFFLLLTSSCVGIGVGTGWTVYPPLSTMEYHPGHAVDVGILSLHIAGASSLLGAINF 183
Cdd:MTH00153 83 LMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 184 LTTVFNMKIAGLSWSKVSLFVWSILITAVLLVLSLPVLAGGLTMLITDRNFETTFFDPIGGGDPILYQHLFWFFGHPEVY 263
Cdd:MTH00153 163 ITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 264 ILILPGFGLVSIILSKYSNKG-IFGVKGMISAMSAIGFLGFLVWAHHMYTVGLDVDTRAYFTAATMIIAIPTGIKIFSWL 342
Cdd:MTH00153 243 ILILPGFGMISHIISQESGKKeTFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 343 ATLWGGVIKITTPMLFVIGFLVLFTIGGLTGVVLANGGLDISLHDTYYVVAHFHYVLSMGAIFAIFAGYYYYYSimnstr 422
Cdd:MTH00153 323 ATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFP------ 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7524975 423 LFGVVRYNEQLGRIHFWTMFIGVNVTFFPMHFLGLAGMPRRIGDYPDAYIGWNLIASYGSLITAFGLLFFV 493
Cdd:MTH00153 397 LFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFI 467
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
21-537 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 711.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 21 FISKWIISVDHKNIGTMYTNFSILAGIVGTLLSLVIRMELSTGNMLDGDGQQYNVIVTAHGLIMIFFVVMPAMLGGFANW 100
Cdd:MTH00167 2 WINRWLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 101 FIPIMVGSPDVAFPRLNNISLWLIIVSFFLLLTSSCVGIGVGTGWTVYPPLSTMEYHPGHAVDVGILSLHIAGASSLLGA 180
Cdd:MTH00167 82 LVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 181 INFLTTVFNMKIAGLSWSKVSLFVWSILITAVLLVLSLPVLAGGLTMLITDRNFETTFFDPIGGGDPILYQHLFWFFGHP 260
Cdd:MTH00167 162 INFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 261 EVYILILPGFGLVSIILSKYSNKG-IFGVKGMISAMSAIGFLGFLVWAHHMYTVGLDVDTRAYFTAATMIIAIPTGIKIF 339
Cdd:MTH00167 242 EVYILILPGFGMISHIVVYYSGKKePFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 340 SWLATLWGGVIKITTPMLFVIGFLVLFTIGGLTGVVLANGGLDISLHDTYYVVAHFHYVLSMGAIFAIFAGYYYYYSimn 419
Cdd:MTH00167 322 SWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFP--- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 420 strLFGVVRYNEQLGRIHFWTMFIGVNVTFFPMHFLGLAGMPRRIGDYPDAYIGWNLIASYGSLITAFGLLFFVVNIFTP 499
Cdd:MTH00167 399 ---LFTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEA 475
|
490 500 510
....*....|....*....|....*....|....*...
gi 7524975 500 YIRrsvniKNGAIILMGLDFARDWQIGFQDPATPIMEG 537
Cdd:MTH00167 476 FSS-----KRKLLPVELTSTNVEWLHGCPPPHHTWEEP 508
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
23-493 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 694.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 23 SKWIISVDHKNIGTMYTNFSILAGIVGTLLSLVIRMELSTGNMLDGDGQQYNVIVTAHGLIMIFFVVMPAMLGGFANWFI 102
Cdd:MTH00223 1 MRWLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 103 PIMVGSPDVAFPRLNNISLWLIIVSFFLLLTSSCVGIGVGTGWTVYPPLSTMEYHPGHAVDVGILSLHIAGASSLLGAIN 182
Cdd:MTH00223 81 PLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 183 FLTTVFNMKIAGLSWSKVSLFVWSILITAVLLVLSLPVLAGGLTMLITDRNFETTFFDPIGGGDPILYQHLFWFFGHPEV 262
Cdd:MTH00223 161 FITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 263 YILILPGFGLVSIILSKYSNKG-IFGVKGMISAMSAIGFLGFLVWAHHMYTVGLDVDTRAYFTAATMIIAIPTGIKIFSW 341
Cdd:MTH00223 241 YILILPGFGMISHIVSHYSSKKeVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSW 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 342 LATLWGGVIKITTPMLFVIGFLVLFTIGGLTGVVLANGGLDISLHDTYYVVAHFHYVLSMGAIFAIFAGYYYYYSIMNst 421
Cdd:MTH00223 321 LATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFT-- 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7524975 422 rlfGVVrYNEQLGRIHFWTMFIGVNVTFFPMHFLGLAGMPRRIGDYPDAYIGWNLIASYGSLITAFGLLFFV 493
Cdd:MTH00223 399 ---GVT-LHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFM 466
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
21-497 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 670.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 21 FISKWIISVDHKNIGTMYTNFSILAGIVGTLLSLVIRMELSTGNMLDGDGQQYNVIVTAHGLIMIFFVVMPAMLGGFANW 100
Cdd:MTH00116 2 FITRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 101 FIPIMVGSPDVAFPRLNNISLWLIIVSFFLLLTSSCVGIGVGTGWTVYPPLSTMEYHPGHAVDVGILSLHIAGASSLLGA 180
Cdd:MTH00116 82 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 181 INFLTTVFNMKIAGLSWSKVSLFVWSILITAVLLVLSLPVLAGGLTMLITDRNFETTFFDPIGGGDPILYQHLFWFFGHP 260
Cdd:MTH00116 162 INFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 261 EVYILILPGFGLVSIILSKYSNKG-IFGVKGMISAMSAIGFLGFLVWAHHMYTVGLDVDTRAYFTAATMIIAIPTGIKIF 339
Cdd:MTH00116 242 EVYILILPGFGIISHIVTYYAGKKePFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 340 SWLATLWGGVIKITTPMLFVIGFLVLFTIGGLTGVVLANGGLDISLHDTYYVVAHFHYVLSMGAIFAIFAGYYYYYSIMN 419
Cdd:MTH00116 322 SWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFT 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7524975 420 STRLfgvvryNEQLGRIHFWTMFIGVNVTFFPMHFLGLAGMPRRIGDYPDAYIGWNLIASYGSLITAFGLLFFVVNIF 497
Cdd:MTH00116 402 GYTL------HQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIW 473
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
22-503 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 651.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 22 ISKWIISVDHKNIGTMYTNFSILAGIVGTLLSLVIRMELS-TGNMLdGDGQQYNVIVTAHGLIMIFFVVMPAMLGGFANW 100
Cdd:MTH00142 1 MMRWLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGqPGSLL-GDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 101 FIPIMVGSPDVAFPRLNNISLWLIIVSFFLLLTSSCVGIGVGTGWTVYPPLSTMEYHPGHAVDVGILSLHIAGASSLLGA 180
Cdd:MTH00142 80 LVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 181 INFLTTVFNMKIAGLSWSKVSLFVWSILITAVLLVLSLPVLAGGLTMLITDRNFETTFFDPIGGGDPILYQHLFWFFGHP 260
Cdd:MTH00142 160 INFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 261 EVYILILPGFGLVSIILSKYSNKG-IFGVKGMISAMSAIGFLGFLVWAHHMYTVGLDVDTRAYFTAATMIIAIPTGIKIF 339
Cdd:MTH00142 240 EVYILILPGFGMISHIINHYSGKKeVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 340 SWLATLWGGVIKITTPMLFVIGFLVLFTIGGLTGVVLANGGLDISLHDTYYVVAHFHYVLSMGAIFAIFAGYYYYYSimn 419
Cdd:MTH00142 320 SWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFP--- 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 420 strLFGVVRYNEQLGRIHFWTMFIGVNVTFFPMHFLGLAGMPRRIGDYPDAYIGWNLIASYGSLITAFGLLFFVVNIFTP 499
Cdd:MTH00142 397 ---LFTGLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWES 473
|
....
gi 7524975 500 YIRR 503
Cdd:MTH00142 474 FVSQ 477
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
21-502 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 615.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 21 FISKWIISVDHKNIGTMYTNFSILAGIVGTLLSLVIRMELSTGNMLDGDGQQYNVIVTAHGLIMIFFVVMPAMLGGFANW 100
Cdd:MTH00182 4 YLTRWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 101 FIPIMVGSPDVAFPRLNNISLWLIIVSFFLLLTSSCVGIGVGTGWTVYPPLSTMEYHPGHAVDVGILSLHIAGASSLLGA 180
Cdd:MTH00182 84 LVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 181 INFLTTVFNMKIAGLSWSKVSLFVWSILITAVLLVLSLPVLAGGLTMLITDRNFETTFFDPIGGGDPILYQHLFWFFGHP 260
Cdd:MTH00182 164 INFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 261 EVYILILPGFGLVSIILSKYSNKG-IFGVKGMISAMSAIGFLGFLVWAHHMYTVGLDVDTRAYFTAATMIIAIPTGIKIF 339
Cdd:MTH00182 244 EVYILILPGFGMISQIIPTFVAKKqIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 340 SWLATLWGGVIKITTPMLFVIGFLVLFTIGGLTGVVLANGGLDISLHDTYYVVAHFHYVLSMGAIFAIFAGYYYYYSIMN 419
Cdd:MTH00182 324 SWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKIT 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 420 StrlfgvVRYNEQLGRIHFWTMFIGVNVTFFPMHFLGLAGMPRRIGDYPDAYIGWNLIASYGSLITAFGLLFFVVNIFTP 499
Cdd:MTH00182 404 G------YCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDA 477
|
...
gi 7524975 500 YIR 502
Cdd:MTH00182 478 YVR 480
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
18-502 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 603.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 18 IFIFISKWIISVDHKNIGTMYTNFSILAGIVGTLLSLVIRMELSTGNMLDGDGQQYNVIVTAHGLIMIFFVVMPAMLGGF 97
Cdd:MTH00184 1 MSLYLSRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 98 ANWFIPIMVGSPDVAFPRLNNISLWLIIVSFFLLLTSSCVGIGVGTGWTVYPPLSTMEYHPGHAVDVGILSLHIAGASSL 177
Cdd:MTH00184 81 GNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 178 LGAINFLTTVFNMKIAGLSWSKVSLFVWSILITAVLLVLSLPVLAGGLTMLITDRNFETTFFDPIGGGDPILYQHLFWFF 257
Cdd:MTH00184 161 LGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 258 GHPEVYILILPGFGLVSIILSKYS-NKGIFGVKGMISAMSAIGFLGFLVWAHHMYTVGLDVDTRAYFTAATMIIAIPTGI 336
Cdd:MTH00184 241 GHPEVYILILPGFGIISQIIPTFAaKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 337 KIFSWLATLWGGVIKITTPMLFVIGFLVLFTIGGLTGVVLANGGLDISLHDTYYVVAHFHYVLSMGAIFAIFAGYYYYYS 416
Cdd:MTH00184 321 KIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 417 IMNStrlfgvVRYNEQLGRIHFWTMFIGVNVTFFPMHFLGLAGMPRRIGDYPDAYIGWNLIASYGSLITAFGLLFFVVNI 496
Cdd:MTH00184 401 KITG------YCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIV 474
|
....*.
gi 7524975 497 FTPYIR 502
Cdd:MTH00184 475 YDAYVR 480
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
22-493 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 600.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 22 ISKWIISVDHKNIGTMYTNFSILAGIVGTLLSLVIRMELSTGNMLDGDGQQYNVIVTAHGLIMIFFVVMPAMLGGFANWF 101
Cdd:MTH00183 3 ITRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 102 IPIMVGSPDVAFPRLNNISLWLIIVSFFLLLTSSCVGIGVGTGWTVYPPLSTMEYHPGHAVDVGILSLHIAGASSLLGAI 181
Cdd:MTH00183 83 IPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 182 NFLTTVFNMKIAGLSWSKVSLFVWSILITAVLLVLSLPVLAGGLTMLITDRNFETTFFDPIGGGDPILYQHLFWFFGHPE 261
Cdd:MTH00183 163 NFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 262 VYILILPGFGLVSIILSKYSNKG-IFGVKGMISAMSAIGFLGFLVWAHHMYTVGLDVDTRAYFTAATMIIAIPTGIKIFS 340
Cdd:MTH00183 243 VYILILPGFGMISHIVAYYSGKKePFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 341 WLATLWGGVIKITTPMLFVIGFLVLFTIGGLTGVVLANGGLDISLHDTYYVVAHFHYVLSMGAIFAIFAGYYYYYSimns 420
Cdd:MTH00183 323 WLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFP---- 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7524975 421 trLFGVVRYNEQLGRIHFWTMFIGVNVTFFPMHFLGLAGMPRRIGDYPDAYIGWNLIASYGSLITAFGLLFFV 493
Cdd:MTH00183 399 --LFSGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFL 469
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
22-512 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 597.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 22 ISKWIISVDHKNIGTMYTNFSILAGIVGTLLSLVIRMELSTGNMLDGDGQQYNVIVTAHGLIMIFFVVMPAMLGGFANWF 101
Cdd:MTH00037 3 LSRWLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 102 IPIMVGSPDVAFPRLNNISLWLIIVSFFLLLTSSCVGIGVGTGWTVYPPLSTMEYHPGHAVDVGILSLHIAGASSLLGAI 181
Cdd:MTH00037 83 IPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 182 NFLTTVFNMKIAGLSWSKVSLFVWSILITAVLLVLSLPVLAGGLTMLITDRNFETTFFDPIGGGDPILYQHLFWFFGHPE 261
Cdd:MTH00037 163 NFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 262 VYILILPGFGLVSIILSKYSNKG-IFGVKGMISAMSAIGFLGFLVWAHHMYTVGLDVDTRAYFTAATMIIAIPTGIKIFS 340
Cdd:MTH00037 243 VYILILPGFGMISHVIAHYSGKQePFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 341 WLATLWGGVIKITTPMLFVIGFLVLFTIGGLTGVVLANGGLDISLHDTYYVVAHFHYVLSMGAIFAIFAGYYYYYSimns 420
Cdd:MTH00037 323 WMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFP---- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 421 trLFGVVRYNEQLGRIHFWTMFIGVNVTFFPMHFLGLAGMPRRIGDYPDAYIGWNLIASYGSLITAFGLLFFVVNIFTPY 500
Cdd:MTH00037 399 --LFSGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAF 476
|
490
....*....|..
gi 7524975 501 IRRSVNIKNGAI 512
Cdd:MTH00037 477 ASQREVISPEFS 488
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
22-493 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 596.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 22 ISKWIISVDHKNIGTMYTNFSILAGIVGTLLSLVIRMELSTGNMLDGDGQQYNVIVTAHGLIMIFFVVMPAMLGGFANWF 101
Cdd:MTH00079 4 LSVWLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 102 IPIMVGSPDVAFPRLNNISLWLIIVSFFLLLTSSCVGIGVGTGWTVYPPLSTmEYHPGHAVDVGILSLHIAGASSLLGAI 181
Cdd:MTH00079 84 LPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 182 NFLTTVFNMKIAGLSWSKVSLFVWSILITAVLLVLSLPVLAGGLTMLITDRNFETTFFDPIGGGDPILYQHLFWFFGHPE 261
Cdd:MTH00079 163 NFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 262 VYILILPGFGLVSIILSKYSNKG-IFGVKGMISAMSAIGFLGFLVWAHHMYTVGLDVDTRAYFTAATMIIAIPTGIKIFS 340
Cdd:MTH00079 243 VYILILPAFGIISQSTLYLTGKKeVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 341 WLATLWGGVIKITTPMLFVIGFLVLFTIGGLTGVVLANGGLDISLHDTYYVVAHFHYVLSMGAIFAIFAGYYYYYSIMns 420
Cdd:MTH00079 323 WLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFM-- 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7524975 421 trlFGVVrYNEQLGRIHFWTMFIGVNVTFFPMHFLGLAGMPRRIGDYPDAYIGWNLIASYGSLITAFGLLFFV 493
Cdd:MTH00079 401 ---TGIV-YDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFI 469
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
20-494 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 596.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 20 IFISKWIISVDHKNIGTMYTNFSILAGIVGTLLSLVIRMELSTGNMLDGDGQQYNVIVTAHGLIMIFFVVMPAMLGGFAN 99
Cdd:MTH00103 1 MFINRWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 100 WFIPIMVGSPDVAFPRLNNISLWLIIVSFFLLLTSSCVGIGVGTGWTVYPPLSTMEYHPGHAVDVGILSLHIAGASSLLG 179
Cdd:MTH00103 81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 180 AINFLTTVFNMKIAGLSWSKVSLFVWSILITAVLLVLSLPVLAGGLTMLITDRNFETTFFDPIGGGDPILYQHLFWFFGH 259
Cdd:MTH00103 161 AINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 260 PEVYILILPGFGLVSIILSKYSNKG-IFGVKGMISAMSAIGFLGFLVWAHHMYTVGLDVDTRAYFTAATMIIAIPTGIKI 338
Cdd:MTH00103 241 PEVYILILPGFGMISHIVTYYSGKKePFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 339 FSWLATLWGGVIKITTPMLFVIGFLVLFTIGGLTGVVLANGGLDISLHDTYYVVAHFHYVLSMGAIFAIFAGYYYYYSim 418
Cdd:MTH00103 321 FSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFP-- 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7524975 419 nstrLFGVVRYNEQLGRIHFWTMFIGVNVTFFPMHFLGLAGMPRRIGDYPDAYIGWNLIASYGSLI--TAFGLLFFVV 494
Cdd:MTH00103 399 ----LFSGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFIslTAVMLMIFMI 472
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
31-497 |
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: 596.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 31 HKNIGTMYTNFSILAGIVGTLLSLVIRMELSTGNMLDGDGQQYNVIVTAHGLIMIFFVVMPAMLGGFANWFIPiMVGSPD 110
Cdd:cd00919 1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 111 VAFPRLNNISLWLIIVSFFLLLTSSCVGIGVGTGWTVYPPLSTMEYHPGHAVDVGILSLHIAGASSLLGAINFLTTVFNM 190
Cdd:cd00919 80 LAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 191 KIAGLSWSKVSLFVWSILITAVLLVLSLPVLAGGLTMLITDRNFETTFFDPIGGGDPILYQHLFWFFGHPEVYILILPGF 270
Cdd:cd00919 160 RAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 271 GLVSIILSKYSNKGIFGVKGMISAMSAIGFLGFLVWAHHMYTVGLDVDTRAYFTAATMIIAIPTGIKIFSWLATLWGGVI 350
Cdd:cd00919 240 GAISEIIPTFSGKPLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 351 KITTPMLFVIGFLVLFTIGGLTGVVLANGGLDISLHDTYYVVAHFHYVLSMGAIFAIFAGYYYYYSIMnstrlFGvVRYN 430
Cdd:cd00919 320 RFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKM-----TG-RMLS 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7524975 431 EQLGRIHFWTMFIGVNVTFFPMHFLGLAGMPRRIGDYPDAYIGWNLIASYGSLITAFGLLFFVVNIF 497
Cdd:cd00919 394 EKLGKIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLF 460
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
20-500 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 591.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 20 IFISKWIISVDHKNIGTMYTNFSILAGIVGTLLSLVIRMELSTGNMLDGDGQQYNVIVTAHGLIMIFFVVMPAMLGGFAN 99
Cdd:MTH00077 1 MMITRWLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 100 WFIPIMVGSPDVAFPRLNNISLWLIIVSFFLLLTSSCVGIGVGTGWTVYPPLSTMEYHPGHAVDVGILSLHIAGASSLLG 179
Cdd:MTH00077 81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 180 AINFLTTVFNMKIAGLSWSKVSLFVWSILITAVLLVLSLPVLAGGLTMLITDRNFETTFFDPIGGGDPILYQHLFWFFGH 259
Cdd:MTH00077 161 AINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 260 PEVYILILPGFGLVSIILSKYSNKG-IFGVKGMISAMSAIGFLGFLVWAHHMYTVGLDVDTRAYFTAATMIIAIPTGIKI 338
Cdd:MTH00077 241 PEVYILILPGFGMISHIVTYYSAKKePFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 339 FSWLATLWGGVIKITTPMLFVIGFLVLFTIGGLTGVVLANGGLDISLHDTYYVVAHFHYVLSMGAIFAIFAGYYYYYSim 418
Cdd:MTH00077 321 FSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFP-- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 419 nstrLFGVVRYNEQLGRIHFWTMFIGVNVTFFPMHFLGLAGMPRRIGDYPDAYIGWNLIASYGSLITAFGLLFFVVNIFT 498
Cdd:MTH00077 399 ----LFSGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWE 474
|
..
gi 7524975 499 PY 500
Cdd:MTH00077 475 AF 476
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
28-499 |
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: 590.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 28 SVDHKNIGTMYTNFSILAGIVGTLLSLVIRMELSTGNMLDGDGQQYNVIVTAHGLIMIFFVVMPaMLGGFANWFIPIMVG 107
Cdd:TIGR02891 3 TVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 108 SPDVAFPRLNNISLWLIIVSFFLLLTSSCVGIGVGTGWTVYPPLSTMEYHPGHAVDVGILSLHIAGASSLLGAINFLTTV 187
Cdd:TIGR02891 82 ARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 188 FNMKIAGLSWSKVSLFVWSILITAVLLVLSLPVLAGGLTMLITDRNFETTFFDPIGGGDPILYQHLFWFFGHPEVYILIL 267
Cdd:TIGR02891 162 LNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 268 PGFGLVSIILSKYSNKGIFGVKGMISAMSAIGFLGFLVWAHHMYTVGLDVDTRAYFTAATMIIAIPTGIKIFSWLATLWG 347
Cdd:TIGR02891 242 PAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 348 GVIKITTPMLFVIGFLVLFTIGGLTGVVLANGGLDISLHDTYYVVAHFHYVLSMGAIFAIFAGYYYYYSIMNSTrlfgvv 427
Cdd:TIGR02891 322 GSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGR------ 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7524975 428 RYNEQLGRIHFWTMFIGVNVTFFPMHFLGLAGMPRRIGDYPDA--YIGWNLIASYGSLITAFGLLFFVVNIFTP 499
Cdd:TIGR02891 396 MYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWS 469
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
24-493 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 586.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 24 KWIISVDHKNIGTMYTNFSILAGIVGTLLSLVIRMELSTGNMLDGDGQQYNVIVTAHGLIMIFFVVMPAMLGGFANWFIP 103
Cdd:MTH00007 2 RWLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 104 IMVGSPDVAFPRLNNISLWLIIVSFFLLLTSSCVGIGVGTGWTVYPPLSTMEYHPGHAVDVGILSLHIAGASSLLGAINF 183
Cdd:MTH00007 82 LMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 184 LTTVFNMKIAGLSWSKVSLFVWSILITAVLLVLSLPVLAGGLTMLITDRNFETTFFDPIGGGDPILYQHLFWFFGHPEVY 263
Cdd:MTH00007 162 ITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 264 ILILPGFGLVSIILSKYSNK-GIFGVKGMISAMSAIGFLGFLVWAHHMYTVGLDVDTRAYFTAATMIIAIPTGIKIFSWL 342
Cdd:MTH00007 242 ILILPGFGAISHIVTHYAGKlEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 343 ATLWGGVIKITTPMLFVIGFLVLFTIGGLTGVVLANGGLDISLHDTYYVVAHFHYVLSMGAIFAIFAGYYYYYSimnstr 422
Cdd:MTH00007 322 ATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFP------ 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7524975 423 LFGVVRYNEQLGRIHFWTMFIGVNVTFFPMHFLGLAGMPRRIGDYPDAYIGWNLIASYGSLITAFGLLFFV 493
Cdd:MTH00007 396 LFTGLTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFI 466
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
21-503 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 582.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 21 FISKWIISVDHKNIGTMYTNFSILAGIVGTLLSLVIRMELSTGNMLDGDGQQYNVIVTAHGLIMIFFVVMPaMLGGFANW 100
Cdd:COG0843 5 GWRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 101 FIPIMVGSPDVAFPRLNNISLWLIIVSFFLLLTSSCVGIGVGTGWTVYPPLSTMEYHPGHAVDVGILSLHIAGASSLLGA 180
Cdd:COG0843 84 LVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 181 INFLTTVFNMKIAGLSWSKVSLFVWSILITAVLLVLSLPVLAGGLTMLITDRNFETTFFDPIGGGDPILYQHLFWFFGHP 260
Cdd:COG0843 164 VNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 261 EVYILILPGFGLVSIILSKYSNKGIFGVKGMISAMSAIGFLGFLVWAHHMYTVGLDVDTRAYFTAATMIIAIPTGIKIFS 340
Cdd:COG0843 244 EVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFN 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 341 WLATLWGGVIKITTPMLFVIGFLVLFTIGGLTGVVLANGGLDISLHDTYYVVAHFHYVLSMGAIFAIFAGYYYYYSIMns 420
Cdd:COG0843 324 WIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKM-- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 421 trlFGvVRYNEQLGRIHFWTMFIGVNVTFFPMHFLGLAGMPRRIGDYP--DAYIGWNLIASYGSLITAFGLLFFVVNIFT 498
Cdd:COG0843 402 ---TG-RMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVV 477
|
....*
gi 7524975 499 PYIRR 503
Cdd:COG0843 478 SLRKG 482
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
24-502 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 546.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 24 KWIISVDHKNIGTMYTNFSILAGIVGTLLSLVIRMELSTGNMLDGDGQQYNVIVTAHGLIMIFFVVMPAMLGGFANWFIP 103
Cdd:MTH00026 6 RWFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 104 IMVGSPDVAFPRLNNISLWLIIVSFFLLLTSSCVGIGVGTGWTVYPPLSTMEYHPGHAVDVGILSLHIAGASSLLGAINF 183
Cdd:MTH00026 86 LMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 184 LTTVFNMKIAGLSWSKVSLFVWSILITAVLLVLSLPVLAGGLTMLITDRNFETTFFDPIGGGDPILYQHLFWFFGHPEVY 263
Cdd:MTH00026 166 ITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 264 ILILPGFGLVSIILSKYS-NKGIFGVKGMISAMSAIGFLGFLVWAHHMYTVGLDVDTRAYFTAATMIIAIPTGIKIFSWL 342
Cdd:MTH00026 246 ILILPGFGIISQILSLFSyKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 343 ATLWGG--VIKITTPMLFVIGFLVLFTIGGLTGVVLANGGLDISLHDTYYVVAHFHYVLSMGAIFAIFAGYYYYYSIMNS 420
Cdd:MTH00026 326 ATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 421 trlfgvVRYNEQLGRIHFWTMFIGVNVTFFPMHFLGLAGMPRRIGDYPDAYIGWNLIASYGSLITAFGLLFFVVNIFTPY 500
Cdd:MTH00026 406 ------YAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAY 479
|
..
gi 7524975 501 IR 502
Cdd:MTH00026 480 YR 481
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
25-503 |
1.35e-180 |
|
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: 525.99 E-value: 1.35e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 25 WIISVDHKNIGTMYTNFSILAGIVGTLLSLVIRMELSTGNMLDGDGQQYNVIVTAHGLIMIFFVVMPAMLGgFANWFIPI 104
Cdd:cd01662 1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 105 MVGSPDVAFPRLNNISLWLIIVSFFLLLTSSCVGIGVGTGWTVYPPLSTMEYHPGHAVDVGILSLHIAGASSLLGAINFL 184
Cdd:cd01662 80 QIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 185 TTVFNMKIAGLSWSKVSLFVWSILITAVLLVLSLPVLAGGLTMLITDRNFETTFFDPIGGGDPILYQHLFWFFGHPEVYI 264
Cdd:cd01662 160 VTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 265 LILPGFGLVSIILSKYSNKGIFGVKGMISAMSAIGFLGFLVWAHHMYTVGLDVDTRAYFTAATMIIAIPTGIKIFSWLAT 344
Cdd:cd01662 240 LILPAFGIFSEIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 345 LWGGVIKITTPMLFVIGFLVLFTIGGLTGVVLANGGLDISLHDTYYVVAHFHYVLSMGAIFAIFAGYYYYYSIMNSTRLf 424
Cdd:cd01662 320 MWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRML- 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 425 gvvryNEQLGRIHFWTMFIGVNVTFFPMHFLGLAGMPRRIGDYP--DAYIGWNLIASYGSLITAFGLLFFVVNIFTPYIR 502
Cdd:cd01662 399 -----NERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLINVIVSIRK 473
|
.
gi 7524975 503 R 503
Cdd:cd01662 474 G 474
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
19-493 |
2.63e-147 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 441.04 E-value: 2.63e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 19 FIFISKWIISVDHKNIGTMYTNFSILAGIVGTLLSLVIRMelstgNMLDG-----DGQQYNVIVTAHGLIMIFFVVMPAM 93
Cdd:MTH00048 1 MNSLLSWLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRL-----NFLDPyynviSLDVYNFLITNHGIIMIFFFLMPVL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 94 LGGFANWFIPIMVGSPDVAFPRLNNISLWLIIVSFFLLLTSSCVGIGVGtgWTVYPPLSTMEYHPGHAVDVGILSLHIAG 173
Cdd:MTH00048 76 IGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCLGAGVG--WTFYPPLSSSLFSSSWGVDFLMFSLHLAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 174 ASSLLGAINFLTTVFNMKIAGLSwSKVSLFVWSILITAVLLVLSLPVLAGGLTMLITDRNFETTFFDPIGGGDPILYQHL 253
Cdd:MTH00048 154 VSSLFGSINFICTIYSAFMTNVF-SRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 254 FWFFGHPEVYILILPGFGLVS-IILSKYSNKGIFGVKGMISAMSAIGFLGFLVWAHHMYTVGLDVDTRAYFTAATMIIAI 332
Cdd:MTH00048 233 FWFFGHPEVYVLILPGFGIIShICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 333 PTGIKIFSWLATLWGGVIKITTPML-FVIGFLVLFTIGGLTGVVLANGGLDISLHDTYYVVAHFHYVLSMGAIFAIFAGY 411
Cdd:MTH00048 313 PTGIKVFSWLYMLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 412 YYYYSIMNSTRLfgvvryNEQLGRIHFWTMFIGVNVTFFPMHFLGLAGMPRRIGDYPDAYIGWNLIASYGSLITAFGLLF 491
Cdd:MTH00048 393 IWWWPLITGLSL------NKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCF 466
|
..
gi 7524975 492 FV 493
Cdd:MTH00048 467 FV 468
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
34-484 |
2.80e-137 |
|
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: 411.97 E-value: 2.80e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 34 IGTMYTNFSILAGIVGTLLSLVIRMELSTGNMLDGDGQQYNVIVTAHGLIMIFFVVMPAMlGGFANWFIPIMVGSPDVAF 113
Cdd:pfam00115 2 IGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPFL-FGFGNYLVPLMIGARDMAF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 114 PRLNNISLWLIIVSFFLLLTSscvGIGVGTGWTVYPPLStmeyhpghAVDVGILSLHIAGASSLLGAINFLTTVFNMKIA 193
Cdd:pfam00115 81 PRLNALSFWLVVLGAVLLLAS---FGGATTGWTEYPPLV--------GVDLWYIGLLLAGVSSLLGAINFIVTILKRRAP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 194 GLSWsKVSLFVWSILITAVLLVLSLPVLAGGLTMLITDRNFettffdPIGGGDPILYQHLFWFFGHPEVYILILPGFGLV 273
Cdd:pfam00115 150 GMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSL------GAGGGDPLLDQHLFWWFGHPEVYILILPAFGII 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 274 SIILSKYSNKGIFGVKGMISAMSAIGFLGFLVWAHHMYTVGLDVDTRAYFTAATMIIAIPTGIKIFSWLATLWGGVIKI- 352
Cdd:pfam00115 223 YYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFr 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 353 TTPMLFVIGFLVLFTIGGLTGVVLANGGLDISLHDTYYVVAHFHYVLSMGAIFAIFAGYYYYYSimnstRLFGvVRYNEQ 432
Cdd:pfam00115 303 TTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLP-----KLTG-RMYSEK 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 7524975 433 LGRIHFWTMFIGVNVTFFPMHFLGLAGMPRRI----GDYPDAYIGWNLIASYGSLI 484
Cdd:pfam00115 377 LGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYappfIETVPAFQPLNWIRTIGGVL 432
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
23-506 |
2.64e-103 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 331.51 E-value: 2.64e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 23 SKWIISVDHKNIGTMYtnfsILAGIVGTLLSLVIRMELSTGNMLDGDGQ-------QYNVIVTAHGLIMIFFVVMPAMLG 95
Cdd:PRK15017 46 KEWLTSVDHKRLGIMY----IIVAIVMLLRGFADAIMMRSQQALASAGEagflpphHYDQIFTAHGVIMIFFVAMPFVIG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 96 gFANWFIPIMVGSPDVAFPRLNNISLWLIIVSFFLLLTSSCVGIGVGTGWTVYPPLSTMEYHPGHAVDVGILSLHIAGAS 175
Cdd:PRK15017 122 -LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIG 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 176 SLLGAINFLTTVFNMKIAGLSWSKVSLFVWSILITAVLLVLSLPVLAGGLTMLITDRNFETTFFDPIGGGDPILYQHLFW 255
Cdd:PRK15017 201 TTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIW 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 256 FFGHPEVYILILPGFGLVSIILSKYSNKGIFGVKGMISAMSAIGFLGFLVWAHHMYTVGLDVDTRAYFTAATMIIAIPTG 335
Cdd:PRK15017 281 AWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTG 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 336 IKIFSWLATLWGGVIKITTPMLFVIGFLVLFTIGGLTGVVLANGGLDISLHDTYYVVAHFHYVLSMGAIFAIFAGYYYYY 415
Cdd:PRK15017 361 VKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWW 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 416 SimnstRLFGvVRYNEQLGRIHFWTMFIGVNVTFFPMHFLGLAGMPRRIGDYPDA-YIGWNLIASYGSLITAFGLLFFVV 494
Cdd:PRK15017 441 P-----KAFG-FKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDPqFHTMLMIAASGAALIALGILCQVI 514
|
490
....*....|..
gi 7524975 495 NIFTPYIRRSVN 506
Cdd:PRK15017 515 QMYVSIRDRDQN 526
|
|
| COX2 |
MTH00023 |
cytochrome c oxidase subunit II; Validated |
514-759 |
2.26e-93 |
|
cytochrome c oxidase subunit II; Validated
Pssm-ID: 214402 [Multi-domain] Cd Length: 240 Bit Score: 291.27 E-value: 2.26e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 514 LMGLDFARDWQIGFQDPATPIMEGIIDLHNYIFFYLIVVAVFIGWVMgrilwrfsykwsyptigdIEIFKNFTAYNQIIH 593
Cdd:MTH00023 5 FFYRDIPEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLI------------------VEALNGKFYDRFLVD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 594 GTVIEIVWTLIPTVILYLIAIPSFTLLYAMDEIINPTVTIKIIGHQWYWSYEYGDNASNLIEFDSYMVYERDLAEGQLRL 673
Cdd:MTH00023 67 GTFLEIVWTIIPAVILVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYEGETLEFDSYMVPTSDLNSGDFRL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 674 LEVDNAMVVPVKTHIRLIITSGDVLHSWAIPSFGIKVDAVPGRLNQIGLYVKREGTFYGQCSELCGVDHGFMPIKVQAVK 753
Cdd:MTH00023 147 LEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVS 226
|
....*.
gi 7524975 754 LGEYFS 759
Cdd:MTH00023 227 LDKYIN 232
|
|
| COX2 |
MTH00154 |
cytochrome c oxidase subunit II; Provisional |
524-762 |
7.88e-89 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 214438 [Multi-domain] Cd Length: 227 Bit Score: 278.64 E-value: 7.88e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 524 QIGFQDPATPIMEGIIDLHNYIFFYLIVVAVFIGWVMgrilwrfsykwsyptigdIEIFKNFTAYNQIIHGTVIEIVWTL 603
Cdd:MTH00154 6 NLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMM------------------ISLLFNKFTNRFLLEGQEIEIIWTI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 604 IPTVILYLIAIPSFTLLYAMDEIINPTVTIKIIGHQWYWSYEYGDnaSNLIEFDSYMVYERDLAEGQLRLLEVDNAMVVP 683
Cdd:MTH00154 68 LPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSD--FKNIEFDSYMIPTNELENNGFRLLDVDNRLVLP 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7524975 684 VKTHIRLIITSGDVLHSWAIPSFGIKVDAVPGRLNQIGLYVKREGTFYGQCSELCGVDHGFMPIKVQAVKLGEYFSKLN 762
Cdd:MTH00154 146 MNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIK 224
|
|
| COX2 |
MTH00051 |
cytochrome c oxidase subunit II; Provisional |
518-757 |
1.34e-88 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 177126 [Multi-domain] Cd Length: 234 Bit Score: 278.59 E-value: 1.34e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 518 DFARDWQIGFQDPATPIMEGIIDLHNYIFFYLIVVAVFIGWVMGRILwrfsykwsyptigdieIFKNFTAYnqIIHGTVI 597
Cdd:MTH00051 2 DAPEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRAL----------------TTKYYHKY--LFEGTLI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 598 EIVWTLIPTVILYLIAIPSFTLLYAMDEIINPTVTIKIIGHQWYWSYEYGDNASNLIEFDSYMVYERDLAEGQLRLLEVD 677
Cdd:MTH00051 64 EIIWTLIPAAILIFIAFPSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGTDTIEFDSYMIPTSDLNSGDLRLLEVD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 678 NAMVVPVKTHIRLIITSGDVLHSWAIPSFGIKVDAVPGRLNQIGLYVKREGTFYGQCSELCGVDHGFMPIKVQAVKLGEY 757
Cdd:MTH00051 144 NRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKY 223
|
|
| COX2 |
MTH00140 |
cytochrome c oxidase subunit II; Provisional |
524-760 |
6.77e-85 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 214430 [Multi-domain] Cd Length: 228 Bit Score: 268.35 E-value: 6.77e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 524 QIGFQDPATPIMEGIIDLHNYIFFYLIVVAVFIGWvMGRILwrfsykwsyptigdieIFKNFTAYNqIIHGTVIEIVWTL 603
Cdd:MTH00140 6 QLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMY-MLVLL----------------LFNKFSCRT-ILEAQKLETIWTI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 604 IPTVILYLIAIPSFTLLYAMDEIINPTVTIKIIGHQWYWSYEYGDnaSNLIEFDSYMVYERDLAEGQLRLLEVDNAMVVP 683
Cdd:MTH00140 68 VPALILVFLALPSLRLLYLLDETNNPLLTVKAIGHQWYWSYEYSD--FSVIEFDSYMVPENELELGDFRLLEVDNRLVLP 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7524975 684 VKTHIRLIITSGDVLHSWAIPSFGIKVDAVPGRLNQIGLYVKREGTFYGQCSELCGVDHGFMPIKVQAVKLgEYFSK 760
Cdd:MTH00140 146 YSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPL-EDFVK 221
|
|
| COX2 |
MTH00038 |
cytochrome c oxidase subunit II; Provisional |
524-763 |
1.41e-83 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 177113 [Multi-domain] Cd Length: 229 Bit Score: 265.03 E-value: 1.41e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 524 QIGFQDPATPIMEGIIDLHNY--IFFYLIVVAVFIGWvmgrilwrFSYKWSYPTigdieiFKNFTaynqiiHGTVIEIVW 601
Cdd:MTH00038 6 QLGLQDASSPLMEELIYFHDYalIILTLITILVFYGL--------ASLLFSSPT------NRFFL------EGQELETIW 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 602 TLIPTVILYLIAIPSFTLLYAMDEIINPTVTIKIIGHQWYWSYEYGDNasNLIEFDSYMVYERDLAEGQLRLLEVDNAMV 681
Cdd:MTH00038 66 TIVPAFILIFIALPSLQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDY--NDLEFDSYMVPTSDLSTGLPRLLEVDNRLV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 682 VPVKTHIRLIITSGDVLHSWAIPSFGIKVDAVPGRLNQIGLYVKREGTFYGQCSELCGVDHGFMPIKVQAVKLGEYFSKL 761
Cdd:MTH00038 144 LPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWV 223
|
..
gi 7524975 762 NE 763
Cdd:MTH00038 224 SN 225
|
|
| COX2 |
MTH00117 |
cytochrome c oxidase subunit II; Provisional |
524-754 |
1.45e-83 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 177178 [Multi-domain] Cd Length: 227 Bit Score: 264.85 E-value: 1.45e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 524 QIGFQDPATPIMEGIIDLHNYIffylIVVAVFIG-WVMGRILWRFSYKWSYPTIGDIEifknftaynqiihgtVIEIVWT 602
Cdd:MTH00117 6 QLGFQDASSPIMEELLFFHDHA----LMVALLISsLVLYLLTLMLTTKLTHTNTVDAQ---------------EVELIWT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 603 LIPTVILYLIAIPSFTLLYAMDEIINPTVTIKIIGHQWYWSYEYGDNASnlIEFDSYMVYERDLAEGQLRLLEVDNAMVV 682
Cdd:MTH00117 67 ILPAIVLILLALPSLRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKD--LSFDSYMIPTQDLPNGHFRLLEVDHRMVI 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7524975 683 PVKTHIRLIITSGDVLHSWAIPSFGIKVDAVPGRLNQIGLYVKREGTFYGQCSELCGVDHGFMPIKVQAVKL 754
Cdd:MTH00117 145 PMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPL 216
|
|
| COX2 |
MTH00168 |
cytochrome c oxidase subunit II; Provisional |
524-760 |
2.74e-83 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 177223 [Multi-domain] Cd Length: 225 Bit Score: 264.15 E-value: 2.74e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 524 QIGFQDPATPIMEGIIDLHNYIFFYLIVVAVFIGWVMGRILwrfSYKWSYPTIGDieifknftaynqiihGTVIEIVWTL 603
Cdd:MTH00168 6 QLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLV---TSKYTNRFLLD---------------SQMIEFVWTI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 604 IPTVILYLIAIPSFTLLYAMDEIINPTVTIKIIGHQWYWSYEYGDnaSNLIEFDSYMVYERDLAEGQLRLLEVDNAMVVP 683
Cdd:MTH00168 68 IPAFILISLALPSLRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTD--YNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLP 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7524975 684 VKTHIRLIITSGDVLHSWAIPSFGIKVDAVPGRLNQIGLYVKREGTFYGQCSELCGVDHGFMPIKVQAVKLgEYFSK 760
Cdd:MTH00168 146 MDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPW-ETFEN 221
|
|
| COX2 |
MTH00139 |
cytochrome c oxidase subunit II; Provisional |
524-764 |
8.69e-82 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 214429 [Multi-domain] Cd Length: 226 Bit Score: 260.42 E-value: 8.69e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 524 QIGFQDPATPIMEGIIDLHNYIFFYLIVVAVFIGWVMGRILWrfsykwsyptigdieifKNFTAYNqIIHGTVIEIVWTL 603
Cdd:MTH00139 6 QLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMS-----------------NKFTSRS-LLESQEVETIWTV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 604 IPTVILYLIAIPSFTLLYAMDEIINPTVTIKIIGHQWYWSYEYGDnaSNLIEFDSYMVYERDLAEGQLRLLEVDNAMVVP 683
Cdd:MTH00139 68 LPAFILLFLALPSLRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSD--FKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 684 VKTHIRLIITSGDVLHSWAIPSFGIKVDAVPGRLNQIGLYVKREGTFYGQCSELCGVDHGFMPIKVQAVKLGEYFSKLNE 763
Cdd:MTH00139 146 YKSNIRALITAADVLHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILE 225
|
.
gi 7524975 764 K 764
Cdd:MTH00139 226 K 226
|
|
| CcO_II_C |
cd13912 |
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ... |
629-759 |
1.07e-81 |
|
C-terminal domain of Cytochrome c Oxidase subunit II; 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. 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 II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.
Pssm-ID: 259979 [Multi-domain] Cd Length: 130 Bit Score: 256.34 E-value: 1.07e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 629 PTVTIKIIGHQWYWSYEYGDNasNLIEFDSYMVYERDLAEGQLRLLEVDNAMVVPVKTHIRLIITSGDVLHSWAIPSFGI 708
Cdd:cd13912 1 PSLTIKAIGHQWYWSYEYSDF--NDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGI 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 7524975 709 KVDAVPGRLNQIGLYVKREGTFYGQCSELCGVDHGFMPIKVQAVKLGEYFS 759
Cdd:cd13912 79 KVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLS 129
|
|
| COX2 |
MTH00129 |
cytochrome c oxidase subunit II; Provisional |
520-758 |
9.53e-77 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 177187 [Multi-domain] Cd Length: 230 Bit Score: 247.32 E-value: 9.53e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 520 ARDWQIGFQDPATPIMEGIIDLHNYIFFYLIVVAVFIGWVmgrILWRFSYKWSYPTIGDIEifknftaynqiihgtVIEI 599
Cdd:MTH00129 2 AHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYI---IVAMVSTKLTNKYILDSQ---------------EIEI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 600 VWTLIPTVILYLIAIPSFTLLYAMDEIINPTVTIKIIGHQWYWSYEYGDNASnlIEFDSYMVYERDLAEGQLRLLEVDNA 679
Cdd:MTH00129 64 IWTVLPAVILILIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYED--LGFDSYMIPTQDLTPGQFRLLEADHR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7524975 680 MVVPVKTHIRLIITSGDVLHSWAIPSFGIKVDAVPGRLNQIGLYVKREGTFYGQCSELCGVDHGFMPIKVQAVKLgEYF 758
Cdd:MTH00129 142 MVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPL-EHF 219
|
|
| COX2 |
MTH00008 |
cytochrome c oxidase subunit II; Validated |
524-752 |
5.11e-76 |
|
cytochrome c oxidase subunit II; Validated
Pssm-ID: 164584 [Multi-domain] Cd Length: 228 Bit Score: 245.15 E-value: 5.11e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 524 QIGFQDPATPIMEGIIDLHNYIFFYLIVVAVFIGWVMgrilwrfsykwsyptigdIEIFKNFTAYNQIIHGTVIEIVWTL 603
Cdd:MTH00008 6 QLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAM------------------TSLMFNKLSNRYILEAQQIETIWTI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 604 IPTVILYLIAIPSFTLLYAMDEIINPTVTIKIIGHQWYWSYEYGDNASnlIEFDSYMVYERDLAEGQLRLLEVDNAMVVP 683
Cdd:MTH00008 68 LPALILLFLAFPSLRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSN--LEFDSYMLPTSDLSPGQFRLLEVDNRAVLP 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7524975 684 VKTHIRLIITSGDVLHSWAIPSFGIKVDAVPGRLNQIGLYVKREGTFYGQCSELCGVDHGFMPIKVQAV 752
Cdd:MTH00008 146 MQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAV 214
|
|
| COX2 |
MTH00098 |
cytochrome c oxidase subunit II; Validated |
524-760 |
1.19e-75 |
|
cytochrome c oxidase subunit II; Validated
Pssm-ID: 177160 [Multi-domain] Cd Length: 227 Bit Score: 244.24 E-value: 1.19e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 524 QIGFQDPATPIMEGIIDLHNYIFFYLIVVAVFIGWVMGRILwrfSYKWSYPTIGDIEifknftaynqiihgtVIEIVWTL 603
Cdd:MTH00098 6 QLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLML---TTKLTHTSTMDAQ---------------EVETIWTI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 604 IPTVILYLIAIPSFTLLYAMDEIINPTVTIKIIGHQWYWSYEYGDnASNLIeFDSYMVYERDLAEGQLRLLEVDNAMVVP 683
Cdd:MTH00098 68 LPAIILILIALPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTD-YEDLS-FDSYMIPTSDLKPGELRLLEVDNRVVLP 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7524975 684 VKTHIRLIITSGDVLHSWAIPSFGIKVDAVPGRLNQIGLYVKREGTFYGQCSELCGVDHGFMPIKVQAVKLgEYFSK 760
Cdd:MTH00098 146 MEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPL-KYFEK 221
|
|
| COX2 |
MTH00076 |
cytochrome c oxidase subunit II; Provisional |
524-763 |
4.14e-74 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 164646 [Multi-domain] Cd Length: 228 Bit Score: 240.07 E-value: 4.14e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 524 QIGFQDPATPIMEGIIDLHNYIFFYLIVVAVFIGWVMgrilwrfsykwsyptigDIEIFKNFTAYNQIiHGTVIEIVWTL 603
Cdd:MTH00076 6 QLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYII-----------------TIMMTTKLTNTNTM-DAQEIEMVWTI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 604 IPTVILYLIAIPSFTLLYAMDEIINPTVTIKIIGHQWYWSYEYGDNASnlIEFDSYMVYERDLAEGQLRLLEVDNAMVVP 683
Cdd:MTH00076 68 MPAIILIVIALPSLRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYED--LSFDSYMIPTQDLTPGQFRLLEVDNRMVVP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 684 VKTHIRLIITSGDVLHSWAIPSFGIKVDAVPGRLNQIGLYVKREGTFYGQCSELCGVDHGFMPIKVQAVKLGEYFSKLNE 763
Cdd:MTH00076 146 MESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSS 225
|
|
| COX2 |
MTH00185 |
cytochrome c oxidase subunit II; Provisional |
520-758 |
6.70e-74 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 164736 [Multi-domain] Cd Length: 230 Bit Score: 239.79 E-value: 6.70e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 520 ARDWQIGFQDPATPIMEGIIDLHNYIFFYLIVVAVFIGWVM-GRILWRFSYKWsyptigdieifknftaynqIIHGTVIE 598
Cdd:MTH00185 2 AHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIvAMVTTKLTNKY-------------------ILDSQEIE 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 599 IVWTLIPTVILYLIAIPSFTLLYAMDEIINPTVTIKIIGHQWYWSYEYGDnaSNLIEFDSYMVYERDLAEGQLRLLEVDN 678
Cdd:MTH00185 63 IVWTILPAIILIMIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTD--YEQLEFDSYMTPTQDLTPGQFRLLETDH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 679 AMVVPVKTHIRLIITSGDVLHSWAIPSFGIKVDAVPGRLNQIGLYVKREGTFYGQCSELCGVDHGFMPIKVQAVKLgEYF 758
Cdd:MTH00185 141 RMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPL-EHF 219
|
|
| COX2 |
MTH00027 |
cytochrome c oxidase subunit II; Provisional |
518-757 |
1.44e-71 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 214405 [Multi-domain] Cd Length: 262 Bit Score: 234.53 E-value: 1.44e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 518 DFARDWQIGFQDPATPIMEGIIDLHNYIFFYLIVVAVFIGWVMGRILWRFSYkwsyptigdieifknFTAYNQIIHGTVI 597
Cdd:MTH00027 28 DANEPWQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNY---------------YSYYWNKLDGSLI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 598 EIVWTLIPTVILYLIAIPSFTLLYAMDE-IINPTVTIKIIGHQWYWSYEYGDNASNLIEFDSYMVYERDLAEGQLRLLEV 676
Cdd:MTH00027 93 EVIWTLIPAFILILIAFPSLRLLYIMDEcGFSANITIKVTGHQWYWSYSYEDYGEKNIEFDSYMIPTADLEFGDLRLLEV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 677 DNAMVVPVKTHIRLIITSGDVLHSWAIPSFGIKVDAVPGRLNQIGLYVKREGTFYGQCSELCGVDHGFMPIKVQAVKLGE 756
Cdd:MTH00027 173 DNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSK 252
|
.
gi 7524975 757 Y 757
Cdd:MTH00027 253 Y 253
|
|
| COX2 |
pfam00116 |
Cytochrome C oxidase subunit II, periplasmic domain; |
632-752 |
8.30e-68 |
|
Cytochrome C oxidase subunit II, periplasmic domain;
Pssm-ID: 395066 [Multi-domain] Cd Length: 120 Bit Score: 219.20 E-value: 8.30e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 632 TIKIIGHQWYWSYEYGDNASnlIEFDSYMVYERDLAEGQLRLLEVDNAMVVPVKTHIRLIITSGDVLHSWAIPSFGIKVD 711
Cdd:pfam00116 2 TIKAIGHQWYWSYEYTDFGD--LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTD 79
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 7524975 712 AVPGRLNQIGLYVKREGTFYGQCSELCGVDHGFMPIKVQAV 752
Cdd:pfam00116 80 AVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
|
|
| CyoA |
COG1622 |
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion]; |
508-757 |
8.36e-56 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
Pssm-ID: 441229 [Multi-domain] Cd Length: 229 Bit Score: 190.81 E-value: 8.36e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 508 KNGAIILMGLDFARDWQIGFQDPATPIMEGIIDLHNYIFFYLIVVAVFIGWVMGRILWRFSYKwsyptigdieifKNFTA 587
Cdd:COG1622 2 KRLLLALLLLALLLSGQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRR------------KGDAD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 588 YNQIIHGTVIEIVWTLIPTVILYLIAIPSFTLLYAMDEIINPTVTIKIIGHQWYWSYEYGDNASnliefdsymvyerdla 667
Cdd:COG1622 70 PAQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGI---------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 668 egqlrllEVDNAMVVPVKTHIRLIITSGDVLHSWAIPSFGIKVDAVPGRLNQIGLYVKREGTFYGQCSELCGVDHGFMPI 747
Cdd:COG1622 134 -------ATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRF 206
|
250
....*....|
gi 7524975 748 KVQAVKLGEY 757
Cdd:COG1622 207 KVVVVSPEEF 216
|
|
| COX2 |
MTH00080 |
cytochrome c oxidase subunit II; Provisional |
581-750 |
8.64e-53 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 177149 [Multi-domain] Cd Length: 231 Bit Score: 182.90 E-value: 8.64e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 581 IFKNFTAYNQIIHGTVIEIVWTLIPTVILYLIAIPSFTLLYAMdEIIN--PTVTIKIIGHQWYWSYEYGDNASnlIEFDS 658
Cdd:MTH00080 47 ISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYY-GLMNldSNLTVKVTGHQWYWSYEFSDIPG--LEFDS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 659 YMVYERDLAEGQLRLLEVDNAMVVPVKTHIRLIITSGDVLHSWAIPSFGIKVDAVPGRLNQIGLYVKREGTFYGQCSELC 738
Cdd:MTH00080 124 YMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEIC 203
|
170
....*....|..
gi 7524975 739 GVDHGFMPIKVQ 750
Cdd:MTH00080 204 GANHSFMPIAVE 215
|
|
| PTZ00047 |
PTZ00047 |
cytochrome c oxidase subunit II; Provisional |
656-752 |
9.23e-43 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 240243 [Multi-domain] Cd Length: 162 Bit Score: 152.28 E-value: 9.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 656 FDSYMVYERDLAEGQLRLLEVDNAMVVPVKTHIRLIITSGDVLHSWAIPSFGIKVDAVPGRLNQIGLYVKREGTFYGQCS 735
Cdd:PTZ00047 51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130
|
90
....*....|....*..
gi 7524975 736 ELCGVDHGFMPIKVQAV 752
Cdd:PTZ00047 131 EMCGTLHGFMPIVVEAV 147
|
|
| COX2 |
MTH00047 |
cytochrome c oxidase subunit II; Provisional |
548-753 |
1.16e-41 |
|
cytochrome c oxidase subunit II; Provisional
Pssm-ID: 214412 [Multi-domain] Cd Length: 194 Bit Score: 150.49 E-value: 1.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 548 YLIVVAVFI-GWVMGRILWR-FSYKWSYptigdieifkNFTAYNQiihgtVIEIVWTLIPTVI-LYLIAIPSFTLLYAMD 624
Cdd:MTH00047 13 YILALCVFIpCWVYIMLCWQvVSGNGSV----------NFGSENQ-----VLELLWTVVPTLLvLVLCFLNLNFITSDLD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 625 eiINPTVTIKIIGHQWYWSYEYGDNasnlIEFDSYMVyerDLAEGqlrlleVDNAMVVPVKTHIRLIITSGDVLHSWAIP 704
Cdd:MTH00047 78 --CFSSETIKVIGHQWYWSYEYSFG----GSYDSFMT---DDIFG------VDKPLRLVYGVPYHLLVTSSDVIHSFSVP 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 7524975 705 SFGIKVDAVPGRLNQIGLYVKREGTFYGQCSELCGVDHGFMPIKVQAVK 753
Cdd:MTH00047 143 DLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVVD 191
|
|
| CoxB |
TIGR02866 |
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ... |
530-757 |
2.64e-41 |
|
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]
Pssm-ID: 274329 [Multi-domain] Cd Length: 199 Bit Score: 149.84 E-value: 2.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 530 PATPIMEGIIDLHNYIFFYLIVVAVFIGWVMGRILWRFSYKwsyptiGDIEIFKnftaynQIIHGTVIEIVWTLIPTVIL 609
Cdd:TIGR02866 1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWKFRRK------GDEEKPS------QIHGNRRLEYVWTVIPLIIV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 610 YLIAIPSFT-LLYAMDEIINPTVTIKIIGHQWYWSYEYGDNAsnliefdsymvyerdlaegqlrlLEVDNAMVVPVKTHI 688
Cdd:TIGR02866 69 VGLFAATAKgLLYLERPIPKDALKVKVTGYQWWWDFEYPESG-----------------------FTTVNELVLPAGTPV 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7524975 689 RLIITSGDVLHSWAIPSFGIKVDAVPGRLNQIGLYVKREGTFYGQCSELCGVDHGFMPIKVQAVKLGEY 757
Cdd:TIGR02866 126 ELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEF 194
|
|
| CuRO_CcO_Caa3_II |
cd04213 |
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ... |
630-752 |
1.47e-24 |
|
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of most bacteria, is a multi-chain transmembrane protein located in the inner membrane the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. Caa3 type of CcO Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the cytochromes a, a3 and CuB active site in subunit I.
Pssm-ID: 259875 [Multi-domain] Cd Length: 103 Bit Score: 98.46 E-value: 1.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 630 TVTIKIIGHQWYWSYEYGDnasnliefdsymvyerdlaeGQLRLLEVDNAMVVPVKTHIRLIITSGDVLHSWAIPSFGIK 709
Cdd:cd04213 1 ALTIEVTGHQWWWEFRYPD--------------------EPGRGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGK 60
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 7524975 710 VDAVPGRLNQIGLYVKREGTFYGQCSELCGVDHGFMPIKVQAV 752
Cdd:cd04213 61 MDMIPGRTNRLWLQADEPGVYRGQCAEFCGASHALMRFKVIAL 103
|
|
| COX2_TM |
pfam02790 |
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ... |
523-619 |
8.64e-24 |
|
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C oxidase contains two transmembrane alpha-helices.
Pssm-ID: 397083 [Multi-domain] Cd Length: 89 Bit Score: 95.86 E-value: 8.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 523 WQIGFQDPATPIMEGIIDLHNYIFFYLIVVAVFIGWVMGRILWRFSYKwsyptigdieifKNFTAYNQIIHGTVIEIVWT 602
Cdd:pfam02790 5 WGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFNRR------------KNPITARYTTHGQTIEIIWT 72
|
90
....*....|....*..
gi 7524975 603 LIPTVILYLIAIPSFTL 619
Cdd:pfam02790 73 IIPAVILILIALPSFKL 89
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
40-497 |
2.41e-23 |
|
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: 104.29 E-value: 2.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 40 NFSILAGIVGTLLSLVIRMELSTGNMLDGDGQQYNVIVTAHGLIM-----IFFVVmpamlgGFANWFIPIMVGSPDVAfP 114
Cdd:cd01660 11 VVAFLALLLGGLFGLLQVLVRTGVFPLPSSGILYYQGLTLHGVLLaivftTFFIM------GFFYAIVARALLRSLFN-R 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 115 RLNNISLWLIIVSffLLLTSSCVGIGVGTG-WTVYPPlstMEYHPGHAVDVGILSLhiagaSSLLGAINFLTTVFNMKIA 193
Cdd:cd01660 84 RLAWAGFWLMVIG--TVMAAVPILLGQASVlYTFYPP---LQAHPLFYIGAALVVV-----GSWISGFAMFVTLWRWKKA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 194 GLSwSKVSLFVWSILITAVLLVLSLPVLAggLTMLITDRNFETTFFDPIgggDPILYQHLFWFFGHPEVYILILPGFGLV 273
Cdd:cd01660 154 NPG-KKVPLATFMVVTTMILWLVASLGVA--LEVLFQLLPWSLGLVDTV---DVLLSRTLFWWFGHPLVYFWLLPAYIAW 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 274 SIILSKysnkgIFGVKGMISAMSAIGFLGFLVWA-----HHMYT-VGLDVDTRAYFTAATMIIAIPT------------- 334
Cdd:cd01660 228 YTILPK-----IAGGKLFSDPLARLAFILFLLFStpvgfHHQFAdPGIGPGWKFIHMVLTFMVALPSlltaftvfaslei 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 335 ------GIKIFSWLATLWGGVIKITTPMLFvigfLVLFTIGGLTGVVLANGGLDISLHDTYYVVAHFHyvLSMGAIFAI- 407
Cdd:cd01660 303 agrlrgGKGLFGWIRALPWGDPMFLALFLA----MLMFIPGGAGGIINASYQLNYVVHNTAWVPGHFH--LTVGGAVALt 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 408 -FAGYYYYYSimnstRLFGVVRYNEQLGRIHFWTMFIGVNVTFFPMHFLGLAGMPRRIG--DYPDAY-----IGWNLIAS 479
Cdd:cd01660 377 fMAVAYWLVP-----HLTGRELAAKRLALAQPWLWFVGMTIMSTAMHVAGLLGAPRRTAeaQYGGLPaagewAPYQQLMA 451
|
490
....*....|....*...
gi 7524975 480 YGSLITAFGLLFFVVNIF 497
Cdd:cd01660 452 IGGTILFVSGALFLYILF 469
|
|
| CuRO_HCO_II_like |
cd13842 |
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ... |
631-749 |
4.03e-23 |
|
Cupredoxin domain of Heme-copper oxidase subunit II; 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 two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.
Pssm-ID: 259911 [Multi-domain] Cd Length: 95 Bit Score: 94.29 E-value: 4.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 631 VTIKIIGHQWYWSYEYGDnasnliefdsymvyerdlaegqlrlLEVDNAMVVPVKTHIRLIITSGDVLHSWAIPSFGIKV 710
Cdd:cd13842 1 LTVYVTGVQWSWTFIYPN-------------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKV 55
|
90 100 110
....*....|....*....|....*....|....*....
gi 7524975 711 DAVPGRLNQIGLYVKREGTFYGQCSELCGVDHGFMPIKV 749
Cdd:cd13842 56 DAVPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKV 94
|
|
| CuRO_HCO_II_like_5 |
cd13919 |
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ... |
630-745 |
6.73e-22 |
|
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; 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 two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.
Pssm-ID: 259986 [Multi-domain] Cd Length: 107 Bit Score: 91.16 E-value: 6.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 630 TVTIKIIGHQWYWSYEYGDnasnliefdsymvyeRDLAEGQLRLLEVdNAMVVPVKTHIRLIITSGDVLHSWAIPSFGIK 709
Cdd:cd13919 1 ALVVEVTAQQWAWTFRYPG---------------GDGKLGTDDDVTS-PELHLPVGRPVLFNLRSKDVIHSFWVPEFRVK 64
|
90 100 110
....*....|....*....|....*....|....*.
gi 7524975 710 VDAVPGRLNQIGLYVKREGTFYGQCSELCGVDHGFM 745
Cdd:cd13919 65 QDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
|
|
| CuRO_HCO_II_like_2 |
cd13915 |
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ... |
630-749 |
2.95e-21 |
|
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; 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 two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.
Pssm-ID: 259982 [Multi-domain] Cd Length: 98 Bit Score: 88.84 E-value: 2.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 630 TVTIKIIGHQWYWSYEYGDNASNliefdsymvyerdlaegqlrllevDNAMVVPVKTHIRLIITSGDVLHSWAIPSFGIK 709
Cdd:cd13915 1 ALEIQVTGRQWMWEFTYPNGKRE------------------------INELHVPVGKPVRLILTSKDVIHSFYVPAFRIK 56
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 7524975 710 VDAVPGRLNQIGLYVKREGTFYGQCSELCGVDHGFMPIKV 749
Cdd:cd13915 57 QDVVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKV 96
|
|
| CuRO_HCO_II_like_3 |
cd13914 |
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ... |
631-757 |
8.93e-19 |
|
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; 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 two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.
Pssm-ID: 259981 [Multi-domain] Cd Length: 108 Bit Score: 82.07 E-value: 8.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 631 VTIKIIGHQWYWSYEYGDnaSNLIEFDSymvyerdlaegqlrllevdnaMVVPVKTHIRLIITSGDVLHSWAIPSFGIKV 710
Cdd:cd13914 1 VEIEVEAYQWGWEFSYPE--ANVTTSEQ---------------------LVIPADRPVYFRITSRDVIHAFHVPELGLKQ 57
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 7524975 711 DAVPGRLNQIGLYVKREGTFYGQCSELCGVDHGFMPIKVQAVKLGEY 757
Cdd:cd13914 58 DAFPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEY 104
|
|
| CuRO_HCO_II_like_6 |
cd13918 |
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ... |
607-757 |
3.43e-18 |
|
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; 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 two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.
Pssm-ID: 259985 [Multi-domain] Cd Length: 139 Bit Score: 81.73 E-value: 3.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 607 VILYLIAIPSFTLLYAMD---EIINPTVTIKIIGHQWYWSYEYGDNASNLiefdsymvyerdlaegqlrllevdNAMVVP 683
Cdd:cd13918 6 IVISLIVWTYGMLLYVEDppdEADEDALEVEVEGFQFGWQFEYPNGVTTG------------------------NTLRVP 61
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7524975 684 VKTHIRLIITSGDVLHSWAIPSFGIKVDAVPGRLNQIGLYVKREGTFYGQCSELCGVDHGFMPIKVQAVKLGEY 757
Cdd:cd13918 62 ADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEF 135
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| ba3_CcO_II_C |
cd13913 |
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ... |
678-745 |
8.96e-09 |
|
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; 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.
Pssm-ID: 259980 [Multi-domain] Cd Length: 99 Bit Score: 53.34 E-value: 8.96e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7524975 678 NAMVVPVKTHIRLIITSGDVLHSWAIPSFGIKVDAVPGRLNQIGLYVKREGTFYGQCSELCGVDHGFM 745
Cdd:cd13913 25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
|
|
| Cupredoxin |
cd00920 |
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ... |
633-750 |
3.93e-04 |
|
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in inter-molecular electron transfer reactions. Cupredoxins are blue copper proteins, having an intense blue color due to the presence of a mononuclear type 1 (T1) copper site. Structurally, the cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel. Some of these proteins have lost the ability to bind copper. The majority of family members contain multiple cupredoxin domain repeats: ceruloplasmin and the coagulation factors V/VIII have six repeats; laccase, ascorbate oxidase, spore coat protein A, and multicopper oxidase CueO contain three repeats; and nitrite reductase has two repeats. Others are mono-domain cupredoxins, such as plastocyanin, pseudoazurin, plantacyanin, azurin, rusticyanin, stellacyanin, quinol oxidase, and the periplasmic domain of cytochrome c oxidase subunit II.
Pssm-ID: 259860 [Multi-domain] Cd Length: 110 Bit Score: 40.68 E-value: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 633 IKIIGHQWYWSYEYGDNasnliefdsymvyerdlaegqlrLLEVDNAMVVPVKTHIRLIITS-GDVLHSWAIPSFGIKVD 711
Cdd:cd00920 1 ITVTASDWGWSFTYNGV-----------------------LLFGPPVLVVPVGDTVRVQFVNkLGENHSVTIAGFGVPVV 57
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 7524975 712 A---------------VPGRLNQIGLYVKREGTFYGQCSELCGVDHGfMPIKVQ 750
Cdd:cd00920 58 AmagganpglvntlviGPGESAEVTFTTDQAGVYWFYCTIPGHNHAG-MVGTIN 110
|
|
| CuRO_UO_II |
cd04212 |
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ... |
678-752 |
6.62e-04 |
|
The cupredoxin domain of Ubiquinol oxidase subunit II; 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. Although subunit II of ubiquinol oxidase lacks the binuclear CuA site found in cytochrome c oxidases, the structure is conserved.
Pssm-ID: 259874 [Multi-domain] Cd Length: 99 Bit Score: 39.45 E-value: 6.62e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7524975 678 NAMVVPVKTHIRLIITSGDVLHSWAIPSFGIKVDAVPGRLNQIGLYVKREGTFYGQCSELCGvdHGF--MPIKVQAV 752
Cdd:cd04212 25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSG--EGFsdMKFKVLAV 99
|
|
| CuRO_HCO_II_like_1 |
cd13916 |
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ... |
631-745 |
5.43e-03 |
|
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; 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 two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.
Pssm-ID: 259983 [Multi-domain] Cd Length: 93 Bit Score: 36.98 E-value: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7524975 631 VTIKIIGHQWYWSyeygdnasnliefdsymvyerdLAEGQlrllevdnamvVPVKTHIRLIITSGDVLHSWAI--PSFGI 708
Cdd:cd13916 1 QVVAVTGHQWYWE----------------------LSRTE-----------IPAGKPVEFRVTSADVNHGFGIydPDMRL 47
|
90 100 110
....*....|....*....|....*....|....*....
gi 7524975 709 --KVDAVPGRLNQIGLYVKREGTFYGQCSELCGVDHGFM 745
Cdd:cd13916 48 laQTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
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