|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-412 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 695.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 1 MSFWLLPPSLSLLLLSSFISSGVGTGWTIYPPLASNIFHSGPSIDLSIFSLHIAGASSILGAINFITTILNMHHKNFSLD 80
Cdd:MTH00153 98 MSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLD 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 81 KLTLLIWSIFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIM 160
Cdd:MTH00153 178 RMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIIS 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 161 SESGKKETFGSLGMIYAMIAIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAVPTGIKIFSWISTLHGMKVSYNPTLW 240
Cdd:MTH00153 258 QESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLL 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 241 WSMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFSIIASFIHWFPLISGFSLNTFMLNIQFISMFI 320
Cdd:MTH00153 338 WALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFI 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 321 GVNLTFFPQHFLGLSGMPRRYSDYPDTFLSWNIISSIGSMISTISLIILMYIIWEALASKRKIINMFFLNSSLEWQNSYP 400
Cdd:MTH00153 418 GVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEWLQNLP 497
|
410
....*....|..
gi 574608904 401 PLNHSYNEIPAI 412
Cdd:MTH00153 498 PAEHSYSELPLL 509
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-396 |
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: 629.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 1 MSFWLLPPSLSLLLLSSFISSGVGTGWTIYPPLASNIFHSGPSIDLSIFSLHIAGASSILGAINFITTILNMHHKNFSLD 80
Cdd:cd01663 91 LSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLE 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 81 KLTLLIWSIFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIM 160
Cdd:cd01663 171 KMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIIS 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 161 SESGKKETFGSLGMIYAMIAIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAVPTGIKIFSWISTLHGMKVSYNPTLW 240
Cdd:cd01663 251 TFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPML 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 241 WSMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFSIIASFIHWFPLISGFSLNTFMLNIQFISMFI 320
Cdd:cd01663 331 WALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFI 410
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 574608904 321 GVNLTFFPQHFLGLSGMPRRYSDYPDTFLSWNIISSIGSMISTISLIILMYIIWEALASKRKII-NMFFLNSSLEWQ 396
Cdd:cd01663 411 GVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIfNVGEGSTSLEWT 487
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
2-406 |
2.18e-137 |
|
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: 402.37 E-value: 2.18e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 2 SFWLLPPSLSLLLLSSFISSGVGTGWTIYPPLASNIFHSGPSIDLSIFSLHIAGASSILGAINFITTILNMHHKNFSLDK 81
Cdd:TIGR02891 94 SYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMR 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 82 LTLLIWSIFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIMS 161
Cdd:TIGR02891 174 MPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPT 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 162 ESGKKeTFGSLGMIYAMIAIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAVPTGIKIFSWISTLHGMKVSYNPTLWW 241
Cdd:TIGR02891 254 FARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLF 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 242 SMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFSIIASFIHWFPLISGFSLNTFMLNIQFISMFIG 321
Cdd:TIGR02891 333 ALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVG 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 322 VNLTFFPQHFLGLSGMPRRYSDYPD--TFLSWNIISSIGSMISTISLIILMYIIWEALASKRKIINMFFLNSSLEWQNSY 399
Cdd:TIGR02891 413 FNLTFFPMHLLGLLGMPRRYYTYPPqmGFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGANPWGATTLEWTTSS 492
|
....*..
gi 574608904 400 PPLNHSY 406
Cdd:TIGR02891 493 PPPAHNF 499
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
2-412 |
9.98e-137 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 401.81 E-value: 9.98e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 2 SFWLLPPSLSLLLLSSFISSGVGTGWTIYPPLASNIFHSGPSIDLSIFSLHIAGASSILGAINFITTILNMHHKNFSLDK 81
Cdd:COG0843 103 SFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMR 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 82 LTLLIWSIFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIMS 161
Cdd:COG0843 183 MPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPT 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 162 ESGKKeTFGSLGMIYAMIAIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAVPTGIKIFSWISTLHGMKVSYNPTLWW 241
Cdd:COG0843 263 FSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLF 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 242 SMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFSIIASFIHWFPLISGFSLNTFMLNIQFISMFIG 321
Cdd:COG0843 342 ALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIG 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 322 VNLTFFPQHFLGLSGMPRRYSDYP--DTFLSWNIISSIGSMISTISLIILMYIIWEALASKRKIINMFFLNSSLEWQNSY 399
Cdd:COG0843 422 FNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPKAGGNPWGARTLEWATPS 501
|
410
....*....|...
gi 574608904 400 PPLNHSYNEIPAI 412
Cdd:COG0843 502 PPPLYNFASIPVV 514
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
22-343 |
1.11e-91 |
|
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: 282.92 E-value: 1.11e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 22 GVGTGWTIYPPLasnifhsgPSIDLSIFSLHIAGASSILGAINFITTILNMHHKNFSLdKLTLLIWSIFITAILLLLSLP 101
Cdd:pfam00115 104 GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFP 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 102 VLAGAITMLLTDRNLNTsffdpsGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIMSESGKKeTFGSLGMIYAMIAI 181
Cdd:pfam00115 175 VLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLI 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 182 GFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAVPTGIKIFSWISTLHGMKVSYN-PTLWWSMGFIFLFTMGGLTGIMLS 260
Cdd:pfam00115 248 AFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFRtTPMLFFLGFAFLFIIGGLTGVMLA 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 261 NSSIDIVLHDTYYVVAHFHYVLSMGAVFSIIASFIHWFPLISGFSLNTFMLNIQFISMFIGVNLTFFPQHFLGLSGMPRR 340
Cdd:pfam00115 328 LPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRR 407
|
...
gi 574608904 341 YSD 343
Cdd:pfam00115 408 YAP 410
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-412 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 695.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 1 MSFWLLPPSLSLLLLSSFISSGVGTGWTIYPPLASNIFHSGPSIDLSIFSLHIAGASSILGAINFITTILNMHHKNFSLD 80
Cdd:MTH00153 98 MSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLD 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 81 KLTLLIWSIFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIM 160
Cdd:MTH00153 178 RMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIIS 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 161 SESGKKETFGSLGMIYAMIAIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAVPTGIKIFSWISTLHGMKVSYNPTLW 240
Cdd:MTH00153 258 QESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLL 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 241 WSMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFSIIASFIHWFPLISGFSLNTFMLNIQFISMFI 320
Cdd:MTH00153 338 WALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFI 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 321 GVNLTFFPQHFLGLSGMPRRYSDYPDTFLSWNIISSIGSMISTISLIILMYIIWEALASKRKIINMFFLNSSLEWQNSYP 400
Cdd:MTH00153 418 GVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEWLQNLP 497
|
410
....*....|..
gi 574608904 401 PLNHSYNEIPAI 412
Cdd:MTH00153 498 PAEHSYSELPLL 509
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-396 |
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: 629.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 1 MSFWLLPPSLSLLLLSSFISSGVGTGWTIYPPLASNIFHSGPSIDLSIFSLHIAGASSILGAINFITTILNMHHKNFSLD 80
Cdd:cd01663 91 LSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLE 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 81 KLTLLIWSIFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIM 160
Cdd:cd01663 171 KMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIIS 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 161 SESGKKETFGSLGMIYAMIAIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAVPTGIKIFSWISTLHGMKVSYNPTLW 240
Cdd:cd01663 251 TFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPML 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 241 WSMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFSIIASFIHWFPLISGFSLNTFMLNIQFISMFI 320
Cdd:cd01663 331 WALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFI 410
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 574608904 321 GVNLTFFPQHFLGLSGMPRRYSDYPDTFLSWNIISSIGSMISTISLIILMYIIWEALASKRKII-NMFFLNSSLEWQ 396
Cdd:cd01663 411 GVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIfNVGEGSTSLEWT 487
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-412 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 602.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 1 MSFWLLPPSLSLLLLSSFISSGVGTGWTIYPPLASNIFHSGPSIDLSIFSLHIAGASSILGAINFITTILNMHHKNFSLD 80
Cdd:MTH00167 100 MSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQY 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 81 KLTLLIWSIFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIM 160
Cdd:MTH00167 180 QTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVV 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 161 SESGKKETFGSLGMIYAMIAIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAVPTGIKIFSWISTLHGMKVSYNPTLW 240
Cdd:MTH00167 260 YYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPML 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 241 WSMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFSIIASFIHWFPLISGFSLNTFMLNIQFISMFI 320
Cdd:MTH00167 340 WALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFI 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 321 GVNLTFFPQHFLGLSGMPRRYSDYPDTFLSWNIISSIGSMISTISLIILMYIIWEALASKRKIINMFFLNSSLEWQNSYP 400
Cdd:MTH00167 420 GVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLLPVELTSTNVEWLHGCP 499
|
410
....*....|..
gi 574608904 401 PLNHSYNEIPAI 412
Cdd:MTH00167 500 PPHHTWEEPPFV 511
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-412 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 595.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 1 MSFWLLPPSLSLLLLSSFISSGVGTGWTIYPPLASNIFHSGPSIDLSIFSLHIAGASSILGAINFITTILNMHHKNFSLD 80
Cdd:MTH00116 100 MSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQY 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 81 KLTLLIWSIFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIM 160
Cdd:MTH00116 180 QTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVT 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 161 SESGKKETFGSLGMIYAMIAIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAVPTGIKIFSWISTLHGMKVSYNPTLW 240
Cdd:MTH00116 260 YYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPML 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 241 WSMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFSIIASFIHWFPLISGFSLNTFMLNIQFISMFI 320
Cdd:MTH00116 340 WALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFT 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 321 GVNLTFFPQHFLGLSGMPRRYSDYPDTFLSWNIISSIGSMISTISLIILMYIIWEALASKRKIINMFFLNSSLEWQNSYP 400
Cdd:MTH00116 420 GVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVLQPELTTTNIEWIHGCP 499
|
410
....*....|..
gi 574608904 401 PLNHSYNEIPAI 412
Cdd:MTH00116 500 PPYHTFEEPAFV 511
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-412 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 590.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 1 MSFWLLPPSLSLLLLSSFISSGVGTGWTIYPPLASNIFHSGPSIDLSIFSLHIAGASSILGAINFITTILNMHHKNFSLD 80
Cdd:MTH00223 97 MSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 81 KLTLLIWSIFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIM 160
Cdd:MTH00223 177 RLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVS 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 161 SESGKKETFGSLGMIYAMIAIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAVPTGIKIFSWISTLHGMKVSYNPTLW 240
Cdd:MTH00223 257 HYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPML 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 241 WSMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFSIIASFIHWFPLISGFSLNTFMLNIQFISMFI 320
Cdd:MTH00223 337 WALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFLMFL 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 321 GVNLTFFPQHFLGLSGMPRRYSDYPDTFLSWNIISSIGSMISTISLIILMYIIWEALASKRKIINMFFLNSSLEWQNSYP 400
Cdd:MTH00223 417 GVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVWSGHLSTSLEWDNLLP 496
|
410
....*....|..
gi 574608904 401 PLNHSYNEIPAI 412
Cdd:MTH00223 497 ADFHNNSETGAL 508
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-412 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 581.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 1 MSFWLLPPSLSLLLLSSFISSGVGTGWTIYPPLASNIFHSGPSIDLSIFSLHIAGASSILGAINFITTILNMHHKNFSLD 80
Cdd:MTH00142 98 MSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 81 KLTLLIWSIFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIM 160
Cdd:MTH00142 178 RVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIIN 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 161 SESGKKETFGSLGMIYAMIAIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAVPTGIKIFSWISTLHGMKVSYNPTLW 240
Cdd:MTH00142 258 HYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPML 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 241 WSMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFSIIASFIHWFPLISGFSLNTFMLNIQFISMFI 320
Cdd:MTH00142 338 WALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYTMFI 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 321 GVNLTFFPQHFLGLSGMPRRYSDYPDTFLSWNIISSIGSMISTISLIILMYIIWEALASKRKIINMFFLNSSLEWQNSYP 400
Cdd:MTH00142 418 GVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVMWSSHLSTSLEWSHRLP 497
|
410
....*....|..
gi 574608904 401 PLNHSYNEIPAI 412
Cdd:MTH00142 498 PDFHTYDELPIL 509
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-408 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 532.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 1 MSFWLLPPSLSLLLLSSFISSGVGTGWTIYPPLASNIFHSGPSIDLSIFSLHIAGASSILGAINFITTILNMHHKNFSLD 80
Cdd:MTH00007 97 MSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 81 KLTLLIWSIFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIM 160
Cdd:MTH00007 177 RIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVT 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 161 SESGKKETFGSLGMIYAMIAIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAVPTGIKIFSWISTLHGMKVSYNPTLW 240
Cdd:MTH00007 257 HYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPML 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 241 WSMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFSIIASFIHWFPLISGFSLNTFMLNIQFISMFI 320
Cdd:MTH00007 337 WALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFLMFL 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 321 GVNLTFFPQHFLGLSGMPRRYSDYPDTFLSWNIISSIGSMISTISLIILMYIIWEALASKRKIINMFFLNSSLEWQNSYP 400
Cdd:MTH00007 417 GVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIASPHMSSSLEWQDTLP 496
|
....*...
gi 574608904 401 PLNHSYNE 408
Cdd:MTH00007 497 LDFHNLPE 504
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-408 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 528.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 1 MSFWLLPPSLSLLLLSSFISSGVGTGWTIYPPLASNIFHSGPSIDLSIFSLHIAGASSILGAINFITTILNMHHKNFSLD 80
Cdd:MTH00103 100 MSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQY 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 81 KLTLLIWSIFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIM 160
Cdd:MTH00103 180 QTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVT 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 161 SESGKKETFGSLGMIYAMIAIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAVPTGIKIFSWISTLHGMKVSYNPTLW 240
Cdd:MTH00103 260 YYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAML 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 241 WSMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFSIIASFIHWFPLISGFSLNTFMLNIQFISMFI 320
Cdd:MTH00103 340 WALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIMFV 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 321 GVNLTFFPQHFLGLSGMPRRYSDYPDTFLSWNIISSIGSMISTISLIILMYIIWEALASKRKIINMFFLNSSLEWQNSYP 400
Cdd:MTH00103 420 GVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVLTVELTTTNLEWLHGCP 499
|
....*...
gi 574608904 401 PLNHSYNE 408
Cdd:MTH00103 500 PPYHTFEE 507
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-410 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 526.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 1 MSFWLLPPSLSLLLLSSFISSGVGTGWTIYPPLASNIFHSGPSIDLSIFSLHIAGASSILGAINFITTILNMHHKNFSLD 80
Cdd:MTH00037 100 MSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFD 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 81 KLTLLIWSIFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIM 160
Cdd:MTH00037 180 RLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIA 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 161 SESGKKETFGSLGMIYAMIAIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAVPTGIKIFSWISTLHGMKVSYNPTLW 240
Cdd:MTH00037 260 HYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLL 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 241 WSMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFSIIASFIHWFPLISGFSLNTFMLNIQFISMFI 320
Cdd:MTH00037 340 WALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFLMFI 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 321 GVNLTFFPQHFLGLSGMPRRYSDYPDTFLSWNIISSIGSMISTISLIILMYIIWEALASKRKIINMFFLNSSLEWQ-NSY 399
Cdd:MTH00037 420 GVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVISPEFSSSSLEWQySSF 499
|
410
....*....|.
gi 574608904 400 PPLNHSYNEIP 410
Cdd:MTH00037 500 PPSHHTFDETP 510
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-408 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 519.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 1 MSFWLLPPSLSLLLLSSFISSGVGTGWTIYPPLASNIFHSGPSIDLSIFSLHIAGASSILGAINFITTILNMHHKNFSLD 80
Cdd:MTH00183 100 MSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQY 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 81 KLTLLIWSIFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIM 160
Cdd:MTH00183 180 QTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVA 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 161 SESGKKETFGSLGMIYAMIAIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAVPTGIKIFSWISTLHGMKVSYNPTLW 240
Cdd:MTH00183 260 YYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLL 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 241 WSMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFSIIASFIHWFPLISGFSLNTFMLNIQFISMFI 320
Cdd:MTH00183 340 WALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVMFV 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 321 GVNLTFFPQHFLGLSGMPRRYSDYPDTFLSWNIISSIGSMISTISLIILMYIIWEALASKRKIINMFFLNSSLEWQNSYP 400
Cdd:MTH00183 420 GVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLSVELTSTNVEWLHGCP 499
|
....*...
gi 574608904 401 PLNHSYNE 408
Cdd:MTH00183 500 PPYHTFEE 507
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-408 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 516.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 1 MSFWLLPPSLSLLLLSSFISSGVGTGWTIYPPLASNIFHSGPSIDLSIFSLHIAGASSILGAINFITTILNMHHKNFSLD 80
Cdd:MTH00077 100 MSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQY 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 81 KLTLLIWSIFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIM 160
Cdd:MTH00077 180 QTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVT 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 161 SESGKKETFGSLGMIYAMIAIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAVPTGIKIFSWISTLHGMKVSYNPTLW 240
Cdd:MTH00077 260 YYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAML 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 241 WSMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFSIIASFIHWFPLISGFSLNTFMLNIQFISMFI 320
Cdd:MTH00077 340 WALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVMFI 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 321 GVNLTFFPQHFLGLSGMPRRYSDYPDTFLSWNIISSIGSMISTISLIILMYIIWEALASKRKIINMFFLNSSLEWQNSYP 400
Cdd:MTH00077 420 GVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREVLTTELTSTNIEWLHGCP 499
|
....*...
gi 574608904 401 PLNHSYNE 408
Cdd:MTH00077 500 PPYHTFEE 507
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-408 |
1.59e-174 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 497.28 E-value: 1.59e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 1 MSFWLLPPSLSLLLLSSFISSGVGTGWTIYPPLaSNIFHSGPSIDLSIFSLHIAGASSILGAINFITTILNMHHKNFSLD 80
Cdd:MTH00079 101 LSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPL-STLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 81 KLTLLIWSIFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIM 160
Cdd:MTH00079 180 HMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTL 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 161 SESGKKETFGSLGMIYAMIAIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAVPTGIKIFSWISTLHGMKVSYNPTLW 240
Cdd:MTH00079 260 YLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLL 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 241 WSMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFSIIASFIHWFPLISGFSLNTFMLNIQFISMFI 320
Cdd:MTH00079 340 WVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFV 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 321 GVNLTFFPQHFLGLSGMPRRYSDYPDTFLSWNIISSIGSMISTISLIILMYIIWEALASKRKIINMFFLNSSLEWQNSYP 400
Cdd:MTH00079 420 GVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLHDNYINSSPEYSLSSY 499
|
....*...
gi 574608904 401 PLNHSYNE 408
Cdd:MTH00079 500 VFGHSYQS 507
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-412 |
1.47e-169 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 485.10 E-value: 1.47e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 1 MSFWLLPPSLSLLLLSSFISSGVGTGWTIYPPLASNIFHSGPSIDLSIFSLHIAGASSILGAINFITTILNMHHKNFSLD 80
Cdd:MTH00182 102 ISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFN 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 81 KLTLLIWSIFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIM 160
Cdd:MTH00182 182 RLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIP 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 161 SESGKKETFGSLGMIYAMIAIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAVPTGIKIFSWISTLHGMKVSYNPTLW 240
Cdd:MTH00182 262 TFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPML 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 241 WSMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFSIIASFIHWFPLISGFSLNTFMLNIQFISMFI 320
Cdd:MTH00182 342 WAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWLMFI 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 321 GVNLTFFPQHFLGLSGMPRRYSDYPDTFLSWNIISSIGSMISTISLIILMYIIWEALASKRKII----NMFFLNSSLEWQ 396
Cdd:MTH00182 422 GVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKFIgwkeGTGESWASLEWV 501
|
410
....*....|....*.
gi 574608904 397 NSYPPLNHSYNEIPAI 412
Cdd:MTH00182 502 HSSPPLFHTYNELPFV 517
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-410 |
2.13e-167 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 479.32 E-value: 2.13e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 1 MSFWLLPPSLSLLLLSSFISSGVGTGWTIYPPLASNIFHSGPSIDLSIFSLHIAGASSILGAINFITTILNMHHKNFSLD 80
Cdd:MTH00184 102 ISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMD 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 81 KLTLLIWSIFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIM 160
Cdd:MTH00184 182 RMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIP 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 161 SESGKKETFGSLGMIYAMIAIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAVPTGIKIFSWISTLHGMKVSYNPTLW 240
Cdd:MTH00184 262 TFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPML 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 241 WSMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFSIIASFIHWFPLISGFSLNTFMLNIQFISMFI 320
Cdd:MTH00184 342 WAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMFI 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 321 GVNLTFFPQHFLGLSGMPRRYSDYPDTFLSWNIISSIGSMISTISLIILMYIIWEALASKRKII---NMFFLNSSLEWQN 397
Cdd:MTH00184 422 GVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVREIKFVgwvEDSGHYPSLEWAQ 501
|
410
....*....|...
gi 574608904 398 SYPPLNHSYNEIP 410
Cdd:MTH00184 502 TSPPAHHTYNELP 514
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-377 |
1.40e-150 |
|
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: 434.65 E-value: 1.40e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 1 MSFWLLPPSLSLLLLSSFISSGVGTGWTIYPPLASNIFHSGPSIDLSIFSLHIAGASSILGAINFITTILNMHHKNFSLD 80
Cdd:cd00919 88 LSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLD 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 81 KLTLLIWSIFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIM 160
Cdd:cd00919 168 KMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIP 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 161 SESGKKeTFGSLGMIYAMIAIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAVPTGIKIFSWISTLHGMKVSYNPTLW 240
Cdd:cd00919 248 TFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPML 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 241 WSMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFSIIASFIHWFPLISGFSLNTFMLNIQFISMFI 320
Cdd:cd00919 327 FALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFI 406
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 574608904 321 GVNLTFFPQHFLGLSGMPRRYSDYPDTFLSWNIISSIGSMISTISLIILMYIIWEAL 377
Cdd:cd00919 407 GFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-412 |
2.55e-140 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 410.94 E-value: 2.55e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 1 MSFWLLPPSLSLLLLSSFISSGVGTGWTIYPPLASNIFHSGPSIDLSIFSLHIAGASSILGAINFITTILNMHHKNFSLD 80
Cdd:MTH00026 101 ISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMS 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 81 KLTLLIWSIFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIM 160
Cdd:MTH00026 181 RIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILS 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 161 SESGKKETFGSLGMIYAMIAIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAVPTGIKIFSWISTL--HGMKVSYNPT 238
Cdd:MTH00026 261 LFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVsgSGRNLIFTTP 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 239 LWWSMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFSIIASFIHWFPLISGFSLNTFMLNIQFISM 318
Cdd:MTH00026 341 MAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLM 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 319 FIGVNLTFFPQHFLGLSGMPRRYSDYPDTFLSWNIISSIGSMISTISLIILMYIIWEALASKRKI-INMFFLN------- 390
Cdd:MTH00026 421 FIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAYYREEPFdINIMAKGplipfsc 500
|
410 420
....*....|....*....|....*..
gi 574608904 391 -----SSLEWQNSYPPLNHSYNEIPAI 412
Cdd:MTH00026 501 qpahfDTLEWSLTSPPEHHTYNELPYI 527
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
2-406 |
2.18e-137 |
|
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: 402.37 E-value: 2.18e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 2 SFWLLPPSLSLLLLSSFISSGVGTGWTIYPPLASNIFHSGPSIDLSIFSLHIAGASSILGAINFITTILNMHHKNFSLDK 81
Cdd:TIGR02891 94 SYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMR 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 82 LTLLIWSIFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIMS 161
Cdd:TIGR02891 174 MPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPT 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 162 ESGKKeTFGSLGMIYAMIAIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAVPTGIKIFSWISTLHGMKVSYNPTLWW 241
Cdd:TIGR02891 254 FARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLF 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 242 SMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFSIIASFIHWFPLISGFSLNTFMLNIQFISMFIG 321
Cdd:TIGR02891 333 ALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVG 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 322 VNLTFFPQHFLGLSGMPRRYSDYPD--TFLSWNIISSIGSMISTISLIILMYIIWEALASKRKIINMFFLNSSLEWQNSY 399
Cdd:TIGR02891 413 FNLTFFPMHLLGLLGMPRRYYTYPPqmGFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGANPWGATTLEWTTSS 492
|
....*..
gi 574608904 400 PPLNHSY 406
Cdd:TIGR02891 493 PPPAHNF 499
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
2-412 |
9.98e-137 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 401.81 E-value: 9.98e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 2 SFWLLPPSLSLLLLSSFISSGVGTGWTIYPPLASNIFHSGPSIDLSIFSLHIAGASSILGAINFITTILNMHHKNFSLDK 81
Cdd:COG0843 103 SFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMR 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 82 LTLLIWSIFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIMS 161
Cdd:COG0843 183 MPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPT 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 162 ESGKKeTFGSLGMIYAMIAIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAVPTGIKIFSWISTLHGMKVSYNPTLWW 241
Cdd:COG0843 263 FSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLF 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 242 SMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFSIIASFIHWFPLISGFSLNTFMLNIQFISMFIG 321
Cdd:COG0843 342 ALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIG 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 322 VNLTFFPQHFLGLSGMPRRYSDYP--DTFLSWNIISSIGSMISTISLIILMYIIWEALASKRKIINMFFLNSSLEWQNSY 399
Cdd:COG0843 422 FNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPKAGGNPWGARTLEWATPS 501
|
410
....*....|...
gi 574608904 400 PPLNHSYNEIPAI 412
Cdd:COG0843 502 PPPLYNFASIPVV 514
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
22-393 |
1.42e-133 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 392.89 E-value: 1.42e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 22 GVGTGWTIYPPLASNIFHSGPSIDLSIFSLHIAGASSILGAINFITTILNMHHKNFSLdKLTLLIWSIFITAILLLLSLP 101
Cdd:MTH00048 120 GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLP 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 102 VLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIMSESGKKETFGSLGMIYAMIAI 181
Cdd:MTH00048 199 VLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSI 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 182 GFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAVPTGIKIFSWISTLHGMKVS-YNPTLWWSMGFIFLFTMGGLTGIMLS 260
Cdd:MTH00048 279 VCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRkSDPVVWWVVSFIVLFTIGGVTGIVLS 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 261 NSSIDIVLHDTYYVVAHFHYVLSMGAVFSIIASFIHWFPLISGFSLNTFMLNIQFISMFIGVNLTFFPQHFLGLSGMPRR 340
Cdd:MTH00048 359 ASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRR 438
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 574608904 341 YSDYPDTFLSWNIISSIGSMISTISLIILMYIIWEALASKRKIINMFFLNSSL 393
Cdd:MTH00048 439 VCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEVLGLWGSSSCV 491
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
2-406 |
9.86e-121 |
|
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: 359.59 E-value: 9.86e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 2 SFWLLPPSLSLLLLSSFISSGVGTGWTIYPPLASNIFHSGPSIDLSIFSLHIAGASSILGAINFITTILNMHHKNFSLDK 81
Cdd:cd01662 95 SFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMR 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 82 LTLLIWSIFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIMS 161
Cdd:cd01662 175 MPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPT 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 162 ESGKKeTFGSLGMIYAMIAIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAVPTGIKIFSWISTLHGMKVSYNPTLWW 241
Cdd:cd01662 255 FSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLW 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 242 SMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFSIIASFIHWFPLISGFSLNTFMLNIQFISMFIG 321
Cdd:cd01662 334 AIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIG 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 322 VNLTFFPQHFLGLSGMPRRYSDYP--DTFLSWNIISSIGSMISTISLIILMY-IIWEALASKRKIINMFFLNSSLEWQNS 398
Cdd:cd01662 414 FNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLInVIVSIRKGKRDATGDPWGARTLEWATS 493
|
....*...
gi 574608904 399 YPPLNHSY 406
Cdd:cd01662 494 SPPPAYNF 501
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
22-343 |
1.11e-91 |
|
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: 282.92 E-value: 1.11e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 22 GVGTGWTIYPPLasnifhsgPSIDLSIFSLHIAGASSILGAINFITTILNMHHKNFSLdKLTLLIWSIFITAILLLLSLP 101
Cdd:pfam00115 104 GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFP 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 102 VLAGAITMLLTDRNLNTsffdpsGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIMSESGKKeTFGSLGMIYAMIAI 181
Cdd:pfam00115 175 VLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLI 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 182 GFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAVPTGIKIFSWISTLHGMKVSYN-PTLWWSMGFIFLFTMGGLTGIMLS 260
Cdd:pfam00115 248 AFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFRtTPMLFFLGFAFLFIIGGLTGVMLA 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 261 NSSIDIVLHDTYYVVAHFHYVLSMGAVFSIIASFIHWFPLISGFSLNTFMLNIQFISMFIGVNLTFFPQHFLGLSGMPRR 340
Cdd:pfam00115 328 LPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRR 407
|
...
gi 574608904 341 YSD 343
Cdd:pfam00115 408 YAP 410
|
|
| CyoB |
TIGR02843 |
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ... |
1-412 |
2.95e-84 |
|
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain which reacts with oxygen, reducing it to water with the concomitant transport of 4 protons across the membrane. Also known as the cytochrome bo complex, cytochrome o ubiquinol oxidase contains four subunits, two heme b cofactors and a copper atom which is believed to be the oxygen active site. This complex is structurally related to the cytochrome caa3 oxidases which utilize cytochrome c as the reductant and contain heme a cofactors, as well as the intermediate form aa3 oxidases which also react directly with quinones as the reductant. [Energy metabolism, Electron transport]
Pssm-ID: 131890 Cd Length: 646 Bit Score: 270.00 E-value: 2.95e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 1 MSFWLLPPSLSLLLLSSFISSGVGTGWTIYPPLASNIFHSGPSIDLSIFSLHIAGASSILGAINFITTILNMHHKNFSLD 80
Cdd:TIGR02843 143 LSFWLTVVGAILVNVSLGVGEFAQTGWLAYPPLSELQYSPGVGVDYYIWALQISGIGTLLTGINFFVTIIKMRAPGMTLM 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 81 KLTLLIWSIFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIM 160
Cdd:TIGR02843 223 KMPVFTWTSLCSNVLIIASFPILTVTLALLTLDRYLGMHFFTNEAGGNPMMYVNLIWAWGHPEVYILILPAFGIFSEVVA 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 161 SESGKKeTFGSLGMIYAMIAIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAVPTGIKIFSWISTLHGMKVSYNPTLW 240
Cdd:TIGR02843 303 TFSRKR-LFGYTSMVWATIAITVLSFIVWLHHFFTMGAGANVNAFFGIATMIIAIPTGVKIFNWLFTMYKGRIRFETPML 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 241 WSMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFSIIASFIHWFPLISGFSLNTFMLNIQFISMFI 320
Cdd:TIGR02843 382 WTIGFMVTFSIGGMTGVLLAVPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWFPKAFGFKLNEKLGKRSFWCWFI 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 321 GVNLTFFPQHFLGLSGMPRRYSDYPD-TFLSWNIISSIGSMISTISLIILMYIIWEALASKRKIINMF---FLNSSLEWQ 396
Cdd:TIGR02843 462 GFYLAFMPLYILGFMGMTRRLNHYDNpEWHPMLIIAAFGAFLIACGILCQIIQIFVSIRDRDQNRDTTgdpWGGRTLEWS 541
|
410
....*....|....*.
gi 574608904 397 NSYPPLNHSYNEIPAI 412
Cdd:TIGR02843 542 TSSPPPFYNFAVIPKV 557
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
1-412 |
2.50e-80 |
|
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]
Pssm-ID: 131928 Cd Length: 643 Bit Score: 259.79 E-value: 2.50e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 1 MSFWLLPPSLSLLLLSSFISSGVGTGWTIYPPLASNIFHSGPSIDLSIFSLHIAGASSILGAINFITTILNMHHKNFSLD 80
Cdd:TIGR02882 137 LSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLM 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 81 KLTLLIWSIFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIm 160
Cdd:TIGR02882 217 QMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEII- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 161 SESGKKETFGSLGMIYAMIAIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAVPTGIKIFSWISTLHGMKVSYNPTLW 240
Cdd:TIGR02882 296 STFAQKRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPML 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 241 WSMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFSIIASFIHWFPLISGFSLNTFMLNIQFISMFI 320
Cdd:TIGR02882 376 FSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLNERLGKWCFWFFMI 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 321 GVNLTFFPQHFLGLSGMPRRYSDY--PDTFLSWNIISSIGSMISTISLIILMY-IIWEALASKRKIINMFFLNSSLEWQN 397
Cdd:TIGR02882 456 GFNVCFFPMYILGLDGMPRRMYTYspSDGWFPLNLISTIGALLMAIGFIFLVYnIYYSHRKSPREATGDPWNGRTLEWAT 535
|
410
....*....|....*
gi 574608904 398 SYPPLNHSYNEIPAI 412
Cdd:TIGR02882 536 ASPPPKYNFAVTPDV 550
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
1-412 |
1.40e-72 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 239.84 E-value: 1.40e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 1 MSFWLLPPSLSLLLLSSFISSGVGTGWTIYPPLASNIFHSGPSIDLSIFSLHIAGASSILGAINFITTILNMHHKNFSLD 80
Cdd:PRK15017 144 LSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMF 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 81 KLTLLIWSIFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGLISHIIM 160
Cdd:PRK15017 224 KMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAA 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 161 SESgKKETFGSLGMIYAMIAIGFLGFIVWAHHMFTIGLDVDTRAYFTSATMIIAVPTGIKIFSWISTLHGMKVSYNPTLW 240
Cdd:PRK15017 304 TFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAML 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 241 WSMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFSIIASFIHWFPLISGFSLNTFMLNIQFISMFI 320
Cdd:PRK15017 383 WTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWII 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 321 GVNLTFFPQHFLGLSGMPRRYSDYPD----TFLSWNIISSIGSMISTISLIILMYIIWEALASKRKIINMFFLNSSLEWQ 396
Cdd:PRK15017 463 GFFVAFMPLYALGFMGMTRRLSQQIDpqfhTMLMIAASGAALIALGILCQVIQMYVSIRDRDQNRDLTGDPWGGRTLEWA 542
|
410
....*....|....*.
gi 574608904 397 NSYPPLNHSYNEIPAI 412
Cdd:PRK15017 543 TSSPPPFYNFAVVPHV 558
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
128-346 |
6.75e-12 |
|
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: 66.93 E-value: 6.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 128 DPILYQHLFWFFGHPEVYILILPGFGLISHIIMSESGKKETFGSLGMIyAMIAIGFLGFIVWAHHMFT-IGLDVDTRAYF 206
Cdd:cd01660 200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARL-AFILFLLFSTPVGFHHQFAdPGIGPGWKFIH 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574608904 207 TSATMIIAVPTGIKIFSWISTL-------HGMK-VSYNPTLWWS----MGFIF---LFTMGGLTGIMLSNSSIDIVLHDT 271
Cdd:cd01660 279 MVLTFMVALPSLLTAFTVFASLeiagrlrGGKGlFGWIRALPWGdpmfLALFLamlMFIPGGAGGIINASYQLNYVVHNT 358
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 574608904 272 YYVVAHFHYVLSMGAVFSIIASFIHWFPLISGFSLNTFMLNI-QFISMFIGVNLTFFPQHFLGLSGMPRR--YSDYPD 346
Cdd:cd01660 359 AWVPGHFHLTVGGAVALTFMAVAYWLVPHLTGRELAAKRLALaQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGG 436
|
|
| |
