|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-510 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 1034.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 1 PNKWLFSTNHKDIGTMYFMFGVWAGMMGMSMSLVIRAELGYPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMIGGFGNWL 80
Cdd:MTH00153 1 MNKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 81 VPIMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMIDSGVGTGWTVYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAI 160
Cdd:MTH00153 81 VPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 161 NFITTTINMRSKNMTLDQTPLFVWSVVITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
Cdd:MTH00153 161 NFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 241 VYILILPGFGIISHIICQESGKIESFGSLGMIYAMLSIGVMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFS 320
Cdd:MTH00153 241 VYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 321 WLATLYGTKIKFNPTLMWAIGFIFLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTG 400
Cdd:MTH00153 321 WLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 401 LSMNNKWLKIQFTIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYLSWNILSSMGSMISLTSIIMFIIILWESMISKRMI 480
Cdd:MTH00153 401 LTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPV 480
|
490 500 510
....*....|....*....|....*....|
gi 2559106368 481 LFTMNLPSSNEWLQNSPPAEHSYSELPLMS 510
Cdd:MTH00153 481 LFSLNLSSSIEWLQNLPPAEHSYSELPLLT 510
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
8-494 |
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: 882.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 8 TNHKDIGTMYFMFGVWAGMMGMSMSLVIRAELGYPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMIGGFGNWLVPIMIGA 87
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 88 PDMAFPRMNNMSFWLLPPSLTLLISSSMIDSGVGTGWTVYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAINFITTTI 167
Cdd:cd01663 81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 168 NMRSKNMTLDQTPLFVWSVVITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 247
Cdd:cd01663 161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 248 GFGIISHIICQESGKIESFGSLGMIYAMLSIGVMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYG 327
Cdd:cd01663 241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 328 TKIKFNPTLMWAIGFIFLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLSMNNKW 407
Cdd:cd01663 321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 408 LKIQFTIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYLSWNILSSMGSMISLTSIIMFIIILWESMISKRMILFTMNLP 487
Cdd:cd01663 401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGEG 480
|
....*...
gi 2559106368 488 SSN-EWLQ 494
Cdd:cd01663 481 STSlEWTL 488
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
3-508 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 565.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 3 KWLFSTNHKDIGTMYFMFGVWAGMMGMSMSLVIRAELGYPGQLIGDDQIYNTIITSHAFVMIFFMVMPiMIGGFGNWLVP 82
Cdd:COG0843 8 RWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 83 IMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMIDSGVGTGWTVYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAINF 162
Cdd:COG0843 87 LQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 163 ITTTINMRSKNMTLDQTPLFVWSVVITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
Cdd:COG0843 167 IVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 243 ILILPGFGIISHIICQESGKiESFGSLGMIYAMLSIGVMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 322
Cdd:COG0843 247 ILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 323 ATLYGTKIKFNPTLMWAIGFIFLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLS 402
Cdd:COG0843 326 ATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRM 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 403 MNNKWLKIQFTIMFIGVNMTFFPQHFLGLAGMPRRYSDYP--DAYLSWNILSSMGSMISLTSIIMFIIILWESMISKRMI 480
Cdd:COG0843 406 LNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPKA 485
|
490 500 510
....*....|....*....|....*....|
gi 2559106368 481 lfTMN--LPSSNEWLQNSPPAEHSYSELPL 508
Cdd:COG0843 486 --GGNpwGARTLEWATPSPPPLYNFASIPV 513
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
5-503 |
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: 563.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 5 LFSTNHKDIGTMYFMFGVWAGMMGMSMSLVIRAELGYPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMiGGFGNWLVPIM 84
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 85 IGAPDMAFPRMNNMSFWLLPPSLTLLISSSMIDSGVGTGWTVYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAINFIT 164
Cdd:TIGR02891 80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 165 TTINMRSKNMTLDQTPLFVWSVVITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 244
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 245 ILPGFGIISHIICQESGKiESFGSLGMIYAMLSIGVMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLAT 324
Cdd:TIGR02891 240 FLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 325 LYGTKIKFNPTLMWAIGFIFLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLSMN 404
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 405 NKWLKIQFTIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDA--YLSWNILSSMGSMISLTSIIMFIIILWESMISKRmilf 482
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGP---- 474
|
490 500
....*....|....*....|....*...
gi 2559106368 483 tmnLPSSN-------EWLQNSPPAEHSY 503
Cdd:TIGR02891 475 ---KAGANpwgattlEWTTSSPPPAHNF 499
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
12-458 |
4.03e-134 |
|
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: 395.40 E-value: 4.03e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 12 DIGTMYFMFGVWAGMMGMSMSLVIRAELGYPGQLIGDDQIYNTIITSHAFVMIFFMVMPiMIGGFGNWLVPIMIGAPDMA 91
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 92 FPRMNNMSFWLLPPSLTLLISSSMidsGVGTGWTVYPPLASniahsggsVDLAIFSLHLAGISSILGAINFITTTINMRS 171
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 172 KNMTLdQTPLFVWSVVITAILLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGI 251
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 252 ISHIICQESGKiESFGSLGMIYAMLSIGVMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKIK 331
Cdd:pfam00115 222 IYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 332 FN-PTLMWAIGFIFLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLSMNNKWLKI 410
Cdd:pfam00115 301 FRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2559106368 411 QFTIMFIGVNMTFFPQHFLGLAGMPRRYS----DYPDAYLSWNILSSMGSMI 458
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-510 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 1034.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 1 PNKWLFSTNHKDIGTMYFMFGVWAGMMGMSMSLVIRAELGYPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMIGGFGNWL 80
Cdd:MTH00153 1 MNKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 81 VPIMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMIDSGVGTGWTVYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAI 160
Cdd:MTH00153 81 VPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 161 NFITTTINMRSKNMTLDQTPLFVWSVVITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
Cdd:MTH00153 161 NFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 241 VYILILPGFGIISHIICQESGKIESFGSLGMIYAMLSIGVMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFS 320
Cdd:MTH00153 241 VYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 321 WLATLYGTKIKFNPTLMWAIGFIFLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTG 400
Cdd:MTH00153 321 WLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 401 LSMNNKWLKIQFTIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYLSWNILSSMGSMISLTSIIMFIIILWESMISKRMI 480
Cdd:MTH00153 401 LTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPV 480
|
490 500 510
....*....|....*....|....*....|
gi 2559106368 481 LFTMNLPSSNEWLQNSPPAEHSYSELPLMS 510
Cdd:MTH00153 481 LFSLNLSSSIEWLQNLPPAEHSYSELPLLT 510
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
8-494 |
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: 882.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 8 TNHKDIGTMYFMFGVWAGMMGMSMSLVIRAELGYPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMIGGFGNWLVPIMIGA 87
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 88 PDMAFPRMNNMSFWLLPPSLTLLISSSMIDSGVGTGWTVYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAINFITTTI 167
Cdd:cd01663 81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 168 NMRSKNMTLDQTPLFVWSVVITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 247
Cdd:cd01663 161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 248 GFGIISHIICQESGKIESFGSLGMIYAMLSIGVMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYG 327
Cdd:cd01663 241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 328 TKIKFNPTLMWAIGFIFLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLSMNNKW 407
Cdd:cd01663 321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 408 LKIQFTIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYLSWNILSSMGSMISLTSIIMFIIILWESMISKRMILFTMNLP 487
Cdd:cd01663 401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGEG 480
|
....*...
gi 2559106368 488 SSN-EWLQ 494
Cdd:cd01663 481 STSlEWTL 488
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
2-509 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 865.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 2 NKWLFSTNHKDIGTMYFMFGVWAGMMGMSMSLVIRAELGYPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMIGGFGNWLV 81
Cdd:MTH00167 4 NRWLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 82 PIMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMIDSGVGTGWTVYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAIN 161
Cdd:MTH00167 84 PLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSIN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 162 FITTTINMRSKNMTLDQTPLFVWSVVITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
Cdd:MTH00167 164 FITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 242 YILILPGFGIISHIICQESGKIESFGSLGMIYAMLSIGVMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 321
Cdd:MTH00167 244 YILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 322 LATLYGTKIKFNPTLMWAIGFIFLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGL 401
Cdd:MTH00167 324 LATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 402 SMNNKWLKIQFTIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYLSWNILSSMGSMISLTSIIMFIIILWESMISKRMIL 481
Cdd:MTH00167 404 TLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLL 483
|
490 500
....*....|....*....|....*...
gi 2559106368 482 FTMNLPSSNEWLQNSPPAEHSYSELPLM 509
Cdd:MTH00167 484 PVELTSTNVEWLHGCPPPHHTWEEPPFV 511
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
2-511 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 864.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 2 NKWLFSTNHKDIGTMYFMFGVWAGMMGMSMSLVIRAELGYPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMIGGFGNWLV 81
Cdd:MTH00116 4 TRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 82 PIMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMIDSGVGTGWTVYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAIN 161
Cdd:MTH00116 84 PLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAIN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 162 FITTTINMRSKNMTLDQTPLFVWSVVITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
Cdd:MTH00116 164 FITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 242 YILILPGFGIISHIICQESGKIESFGSLGMIYAMLSIGVMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 321
Cdd:MTH00116 244 YILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSW 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 322 LATLYGTKIKFNPTLMWAIGFIFLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGL 401
Cdd:MTH00116 324 LATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGY 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 402 SMNNKWLKIQFTIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYLSWNILSSMGSMISLTSIIMFIIILWESMISKRMIL 481
Cdd:MTH00116 404 TLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVL 483
|
490 500 510
....*....|....*....|....*....|
gi 2559106368 482 FTMNLPSSNEWLQNSPPAEHSYSELPLMST 511
Cdd:MTH00116 484 QPELTTTNIEWIHGCPPPYHTFEEPAFVQV 513
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
2-509 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 847.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 2 NKWLFSTNHKDIGTMYFMFGVWAGMMGMSMSLVIRAELGYPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMIGGFGNWLV 81
Cdd:MTH00142 2 MRWLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 82 PIMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMIDSGVGTGWTVYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAIN 161
Cdd:MTH00142 82 PLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAIN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 162 FITTTINMRSKNMTLDQTPLFVWSVVITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
Cdd:MTH00142 162 FITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 242 YILILPGFGIISHIICQESGKIESFGSLGMIYAMLSIGVMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 321
Cdd:MTH00142 242 YILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSW 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 322 LATLYGTKIKFNPTLMWAIGFIFLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGL 401
Cdd:MTH00142 322 LATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 402 SMNNKWLKIQFTIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYLSWNILSSMGSMISLTSIIMFIIILWESMISKRMIL 481
Cdd:MTH00142 402 TLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVM 481
|
490 500
....*....|....*....|....*...
gi 2559106368 482 FTMNLPSSNEWLQNSPPAEHSYSELPLM 509
Cdd:MTH00142 482 WSSHLSTSLEWSHRLPPDFHTYDELPIL 509
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
3-507 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 846.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 3 KWLFSTNHKDIGTMYFMFGVWAGMMGMSMSLVIRAELGYPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMIGGFGNWLVP 82
Cdd:MTH00223 2 RWLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 83 IMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMIDSGVGTGWTVYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAINF 162
Cdd:MTH00223 82 LMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 163 ITTTINMRSKNMTLDQTPLFVWSVVITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
Cdd:MTH00223 162 ITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 243 ILILPGFGIISHIICQESGKIESFGSLGMIYAMLSIGVMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 322
Cdd:MTH00223 242 ILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 323 ATLYGTKIKFNPTLMWAIGFIFLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLS 402
Cdd:MTH00223 322 ATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 403 MNNKWLKIQFTIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYLSWNILSSMGSMISLTSIIMFIIILWESMISKRMILF 482
Cdd:MTH00223 402 LHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVW 481
|
490 500
....*....|....*....|....*
gi 2559106368 483 TMNLPSSNEWLQNSPPAEHSYSELP 507
Cdd:MTH00223 482 SGHLSTSLEWDNLLPADFHNNSETG 506
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
2-511 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 776.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 2 NKWLFSTNHKDIGTMYFMFGVWAGMMGMSMSLVIRAELGYPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMIGGFGNWLV 81
Cdd:MTH00103 4 NRWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 82 PIMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMIDSGVGTGWTVYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAIN 161
Cdd:MTH00103 84 PLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAIN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 162 FITTTINMRSKNMTLDQTPLFVWSVVITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
Cdd:MTH00103 164 FITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 242 YILILPGFGIISHIICQESGKIESFGSLGMIYAMLSIGVMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 321
Cdd:MTH00103 244 YILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSW 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 322 LATLYGTKIKFNPTLMWAIGFIFLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGL 401
Cdd:MTH00103 324 LATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGY 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 402 SMNNKWLKIQFTIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYLSWNILSSMGSMISLTSIIMFIIILWESMISKRMIL 481
Cdd:MTH00103 404 TLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVL 483
|
490 500 510
....*....|....*....|....*....|.
gi 2559106368 482 fTMNLPSSN-EWLQNSPPAEHSYSELPLMST 511
Cdd:MTH00103 484 -TVELTTTNlEWLHGCPPPYHTFEEPTYVKL 513
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
3-511 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 765.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 3 KWLFSTNHKDIGTMYFMFGVWAGMMGMSMSLVIRAELGYPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMIGGFGNWLVP 82
Cdd:MTH00007 2 RWLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 83 IMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMIDSGVGTGWTVYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAINF 162
Cdd:MTH00007 82 LMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 163 ITTTINMRSKNMTLDQTPLFVWSVVITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
Cdd:MTH00007 162 ITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 243 ILILPGFGIISHIICQESGKIESFGSLGMIYAMLSIGVMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 322
Cdd:MTH00007 242 ILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 323 ATLYGTKIKFNPTLMWAIGFIFLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLS 402
Cdd:MTH00007 322 ATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 403 MNNKWLKIQFTIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYLSWNILSSMGSMISLTSIIMFIIILWESMISKRMILF 482
Cdd:MTH00007 402 LHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIA 481
|
490 500
....*....|....*....|....*....
gi 2559106368 483 TMNLPSSNEWLQNSPPAEHSYSELPLMST 511
Cdd:MTH00007 482 SPHMSSSLEWQDTLPLDFHNLPETGIITT 510
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
3-505 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 761.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 3 KWLFSTNHKDIGTMYFMFGVWAGMMGMSMSLVIRAELGYPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMIGGFGNWLVP 82
Cdd:MTH00183 5 RWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 83 IMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMIDSGVGTGWTVYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAINF 162
Cdd:MTH00183 85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 163 ITTTINMRSKNMTLDQTPLFVWSVVITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
Cdd:MTH00183 165 ITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 243 ILILPGFGIISHIICQESGKIESFGSLGMIYAMLSIGVMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 322
Cdd:MTH00183 245 ILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 323 ATLYGTKIKFNPTLMWAIGFIFLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLS 402
Cdd:MTH00183 325 ATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 403 MNNKWLKIQFTIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYLSWNILSSMGSMISLTSIIMFIIILWESMISKRMILF 482
Cdd:MTH00183 405 LHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLS 484
|
490 500
....*....|....*....|...
gi 2559106368 483 TMNLPSSNEWLQNSPPAEHSYSE 505
Cdd:MTH00183 485 VELTSTNVEWLHGCPPPYHTFEE 507
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-505 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 759.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 1 PNKWLFSTNHKDIGTMYFMFGVWAGMMGMSMSLVIRAELGYPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMIGGFGNWL 80
Cdd:MTH00077 3 ITRWLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 81 VPIMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMIDSGVGTGWTVYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAI 160
Cdd:MTH00077 83 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 161 NFITTTINMRSKNMTLDQTPLFVWSVVITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
Cdd:MTH00077 163 NFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 241 VYILILPGFGIISHIICQESGKIESFGSLGMIYAMLSIGVMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFS 320
Cdd:MTH00077 243 VYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 321 WLATLYGTKIKFNPTLMWAIGFIFLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTG 400
Cdd:MTH00077 323 WLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 401 LSMNNKWLKIQFTIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYLSWNILSSMGSMISLTSIIMFIIILWESMISKRMI 480
Cdd:MTH00077 403 YTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREV 482
|
490 500
....*....|....*....|....*
gi 2559106368 481 LFTMNLPSSNEWLQNSPPAEHSYSE 505
Cdd:MTH00077 483 LTTELTSTNIEWLHGCPPPYHTFEE 507
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
2-508 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 752.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 2 NKWLFSTNHKDIGTMYFMFGVWAGMMGMSMSLVIRAELGYPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMIGGFGNWLV 81
Cdd:MTH00037 4 SRWLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 82 PIMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMIDSGVGTGWTVYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAIN 161
Cdd:MTH00037 84 PLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASIN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 162 FITTTINMRSKNMTLDQTPLFVWSVVITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
Cdd:MTH00037 164 FITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 242 YILILPGFGIISHIICQESGKIESFGSLGMIYAMLSIGVMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 321
Cdd:MTH00037 244 YILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSW 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 322 LATLYGTKIKFNPTLMWAIGFIFLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGL 401
Cdd:MTH00037 324 MATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 402 SMNNKWLKIQFTIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYLSWNILSSMGSMISLTSIIMFIIILWESMISKRMIL 481
Cdd:MTH00037 404 SLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVI 483
|
490 500
....*....|....*....|....*...
gi 2559106368 482 FTMNLPSSNEWLQNS-PPAEHSYSELPL 508
Cdd:MTH00037 484 SPEFSSSSLEWQYSSfPPSHHTFDETPS 511
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
4-505 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 695.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 4 WLFSTNHKDIGTMYFMFGVWAGMMGMSMSLVIRAELGYPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMIGGFGNWLVPI 83
Cdd:MTH00079 7 WLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 84 MIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMIDSGVGTGWTVYPPLaSNIAHSGGSVDLAIFSLHLAGISSILGAINFI 163
Cdd:MTH00079 87 MLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPL-STLGHPGSSVDLAIFSLHCAGISSILGGINFM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 164 TTTINMRSKNMTLDQTPLFVWSVVITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 243
Cdd:MTH00079 166 VTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 244 LILPGFGIISHIICQESGKIESFGSLGMIYAMLSIGVMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLA 323
Cdd:MTH00079 246 LILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 324 TLYGTKIKFNPTLMWAIGFIFLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLSM 403
Cdd:MTH00079 326 TLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVY 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 404 NNKWLKIQFTIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYLSWNILSSMGSMISLTSIIMFIIILWESMISKRMILFT 483
Cdd:MTH00079 406 DKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLHD 485
|
490 500
....*....|....*....|..
gi 2559106368 484 MNLPSSNEWLQNSPPAEHSYSE 505
Cdd:MTH00079 486 NYINSSPEYSLSSYVFGHSYQS 507
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
3-509 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 694.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 3 KWLFSTNHKDIGTMYFMFGVWAGMMGMSMSLVIRAELGYPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMIGGFGNWLVP 82
Cdd:MTH00182 7 RWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 83 IMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMIDSGVGTGWTVYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAINF 162
Cdd:MTH00182 87 LYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 163 ITTTINMRSKNMTLDQTPLFVWSVVITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
Cdd:MTH00182 167 ITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 243 ILILPGFGIISHIICQESGKIESFGSLGMIYAMLSIGVMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 322
Cdd:MTH00182 247 ILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 323 ATLYGTKIKFNPTLMWAIGFIFLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLS 402
Cdd:MTH00182 327 ATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYC 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 403 MNNKWLKIQFTIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYLSWNILSSMGSMISLTSIIMFIIILWESMISKRMILF 482
Cdd:MTH00182 407 YNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKFIG 486
|
490 500 510
....*....|....*....|....*....|.
gi 2559106368 483 TMNLPSSN----EWLQNSPPAEHSYSELPLM 509
Cdd:MTH00182 487 WKEGTGESwaslEWVHSSPPLFHTYNELPFV 517
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
3-509 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 688.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 3 KWLFSTNHKDIGTMYFMFGVWAGMMGMSMSLVIRAELGYPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMIGGFGNWLVP 82
Cdd:MTH00184 7 RWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 83 IMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMIDSGVGTGWTVYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAINF 162
Cdd:MTH00184 87 LYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 163 ITTTINMRSKNMTLDQTPLFVWSVVITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
Cdd:MTH00184 167 ITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 243 ILILPGFGIISHIICQESGKIESFGSLGMIYAMLSIGVMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 322
Cdd:MTH00184 247 ILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 323 ATLYGTKIKFNPTLMWAIGFIFLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLS 402
Cdd:MTH00184 327 ATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYC 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 403 MNNKWLKIQFTIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYLSWNILSSMGSMISLTSIIMFIIILWESMisKRMILF 482
Cdd:MTH00184 407 YNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAY--VREIKF 484
|
490 500 510
....*....|....*....|....*....|..
gi 2559106368 483 T-----MNLPSSNEWLQNSPPAEHSYSELPLM 509
Cdd:MTH00184 485 VgwvedSGHYPSLEWAQTSPPAHHTYNELPYV 516
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
10-474 |
0e+00 |
|
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. Membership in the superfamily is defined by subunit I, which contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons to the binuclear center. Only subunit I is common to the entire superfamily. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from the electron donor on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I of cytochrome c oxidase (CcO) and ubiquinol oxidase. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electron transfer occurs in two segments: from the electron donor to the low-spin heme, and from the low-spin heme to the binuclear center. The first segment can be a multi-step process and varies among the different families, while the second segment, a direct transfer, is consistent throughout the superfamily.
Pssm-ID: 238461 Cd Length: 463 Bit Score: 607.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 10 HKDIGTMYFMFGVWAGMMGMSMSLVIRAELGYPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMIGGFGNWLVPiMIGAPD 89
Cdd:cd00919 1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 90 MAFPRMNNMSFWLLPPSLTLLISSSMIDSGVGTGWTVYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAINFITTTINM 169
Cdd:cd00919 80 LAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 170 RSKNMTLDQTPLFVWSVVITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 249
Cdd:cd00919 160 RAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 250 GIISHIICQESGKiESFGSLGMIYAMLSIGVMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTK 329
Cdd:cd00919 240 GAISEIIPTFSGK-PLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 330 IKFNPTLMWAIGFIFLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLSMNNKWLK 409
Cdd:cd00919 319 IRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGK 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2559106368 410 IQFTIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYLSWNILSSMGSMISLTSIIMFIIILWESM 474
Cdd:cd00919 399 IHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
3-509 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 604.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 3 KWLFSTNHKDIGTMYFMFGVWAGMMGMSMSLVIRAELGYPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMIGGFGNWLVP 82
Cdd:MTH00026 6 RWFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 83 IMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMIDSGVGTGWTVYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAINF 162
Cdd:MTH00026 86 LMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 163 ITTTINMRSKNMTLDQTPLFVWSVVITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
Cdd:MTH00026 166 ITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 243 ILILPGFGIISHIICQESGKIESFGSLGMIYAMLSIGVMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 322
Cdd:MTH00026 246 ILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 323 ATLYGT--KIKFNPTLMWAIGFIFLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTG 400
Cdd:MTH00026 326 ATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 401 LSMNNKWLKIQFTIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYLSWNILSSMGSMISLTSIIMFIIILWES------- 473
Cdd:MTH00026 406 YAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAyyreepf 485
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2559106368 474 ----MISKRMILFTMNLPSSN--EWLQNSPPAEHSYSELPLM 509
Cdd:MTH00026 486 diniMAKGPLIPFSCQPAHFDtlEWSLTSPPEHHTYNELPYI 527
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
3-508 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 565.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 3 KWLFSTNHKDIGTMYFMFGVWAGMMGMSMSLVIRAELGYPGQLIGDDQIYNTIITSHAFVMIFFMVMPiMIGGFGNWLVP 82
Cdd:COG0843 8 RWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 83 IMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMIDSGVGTGWTVYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAINF 162
Cdd:COG0843 87 LQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 163 ITTTINMRSKNMTLDQTPLFVWSVVITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
Cdd:COG0843 167 IVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 243 ILILPGFGIISHIICQESGKiESFGSLGMIYAMLSIGVMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 322
Cdd:COG0843 247 ILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 323 ATLYGTKIKFNPTLMWAIGFIFLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLS 402
Cdd:COG0843 326 ATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRM 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 403 MNNKWLKIQFTIMFIGVNMTFFPQHFLGLAGMPRRYSDYP--DAYLSWNILSSMGSMISLTSIIMFIIILWESMISKRMI 480
Cdd:COG0843 406 LNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPKA 485
|
490 500 510
....*....|....*....|....*....|
gi 2559106368 481 lfTMN--LPSSNEWLQNSPPAEHSYSELPL 508
Cdd:COG0843 486 --GGNpwGARTLEWATPSPPPLYNFASIPV 513
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
5-503 |
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: 563.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 5 LFSTNHKDIGTMYFMFGVWAGMMGMSMSLVIRAELGYPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMiGGFGNWLVPIM 84
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 85 IGAPDMAFPRMNNMSFWLLPPSLTLLISSSMIDSGVGTGWTVYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAINFIT 164
Cdd:TIGR02891 80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 165 TTINMRSKNMTLDQTPLFVWSVVITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 244
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 245 ILPGFGIISHIICQESGKiESFGSLGMIYAMLSIGVMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLAT 324
Cdd:TIGR02891 240 FLPAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 325 LYGTKIKFNPTLMWAIGFIFLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLSMN 404
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 405 NKWLKIQFTIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDA--YLSWNILSSMGSMISLTSIIMFIIILWESMISKRmilf 482
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGP---- 474
|
490 500
....*....|....*....|....*...
gi 2559106368 483 tmnLPSSN-------EWLQNSPPAEHSY 503
Cdd:TIGR02891 475 ---KAGANpwgattlEWTTSSPPPAHNF 499
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
4-502 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 517.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 4 WLFSTNHKDIGTMYFMFGVWAGMMGMSMSLVIRAELGYPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMIGGFGNWLVPI 83
Cdd:MTH00048 7 WLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 84 MIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMIdsGVGTGWTVYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAINFI 163
Cdd:MTH00048 87 LLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 164 TTTINMRSKNMTLdQTPLFVWSVVITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 243
Cdd:MTH00048 165 CTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 244 LILPGFGIISHIICQESGKIESFGSLGMIYAMLSIGVMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLA 323
Cdd:MTH00048 244 LILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 324 TLYGTKIKF-NPTLMWAIGFIFLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLS 402
Cdd:MTH00048 324 MLLNSRVRKsDPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 403 MNNKWLKIQFTIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYLSWNILSSMGSMISLTSIIMFIIILWESMISKRMILF 482
Cdd:MTH00048 404 LNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEVLG 483
|
490 500
....*....|....*....|
gi 2559106368 483 TMNLPSSNEWLQNSPPAEHS 502
Cdd:MTH00048 484 LWGSSSCVVNVLMSPVPYHN 503
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
4-503 |
1.65e-167 |
|
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: 482.85 E-value: 1.65e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 4 WLFSTNHKDIGTMYFMFGVWAGMMGMSMSLVIRAELGYPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMIGgFGNWLVPI 83
Cdd:cd01662 1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 84 MIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMIDSGVGTGWTVYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAINFI 163
Cdd:cd01662 80 QIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 164 TTTINMRSKNMTLDQTPLFVWSVVITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 243
Cdd:cd01662 160 VTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 244 LILPGFGIISHIICQESGKiESFGSLGMIYAMLSIGVMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLA 323
Cdd:cd01662 240 LILPAFGIFSEIVPTFSRK-PLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 324 TLYGTKIKFNPTLMWAIGFIFLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLSM 403
Cdd:cd01662 319 TMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRML 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 404 NNKWLKIQFTIMFIGVNMTFFPQHFLGLAGMPRRYSDYP--DAYLSWNILSSMGSMISLTSIIMFIIILWESMISKRMIl 481
Cdd:cd01662 399 NERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLINVIVSIRKGKRD- 477
|
490 500
....*....|....*....|....*
gi 2559106368 482 fTMNLP---SSNEWLQNSPPAEHSY 503
Cdd:cd01662 478 -ATGDPwgaRTLEWATSSPPPAYNF 501
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
12-458 |
4.03e-134 |
|
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: 395.40 E-value: 4.03e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 12 DIGTMYFMFGVWAGMMGMSMSLVIRAELGYPGQLIGDDQIYNTIITSHAFVMIFFMVMPiMIGGFGNWLVPIMIGAPDMA 91
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 92 FPRMNNMSFWLLPPSLTLLISSSMidsGVGTGWTVYPPLASniahsggsVDLAIFSLHLAGISSILGAINFITTTINMRS 171
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 172 KNMTLdQTPLFVWSVVITAILLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGI 251
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 252 ISHIICQESGKiESFGSLGMIYAMLSIGVMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKIK 331
Cdd:pfam00115 222 IYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 332 FN-PTLMWAIGFIFLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGLSMNNKWLKI 410
Cdd:pfam00115 301 FRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2559106368 411 QFTIMFIGVNMTFFPQHFLGLAGMPRRYS----DYPDAYLSWNILSSMGSMI 458
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
|
|
| CyoB |
TIGR02843 |
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ... |
2-507 |
1.08e-122 |
|
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: 373.24 E-value: 1.08e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 2 NKWLFSTNHKDIGTMYFMFGVWAGMMGMSMSLVIRAEL-----GYPGQLIGDDqiYNTIITSHAFVMIFFMVMPIMIGGF 76
Cdd:TIGR02843 45 NEWLTTVDHKKIGIMYIIVALVMLLRGFADAIMMRTQQalasgGSAGYLPPHH--YDQIFTAHGVIMIFFVAMPFVFGLM 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 77 gNWLVPIMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMIDSGVGTGWTVYPPLaSNIAHSGG-SVDLAIFSLHLAGISS 155
Cdd:TIGR02843 123 -NLVVPLQIGARDVAFPFLNSLSFWLTVVGAILVNVSLGVGEFAQTGWLAYPPL-SELQYSPGvGVDYYIWALQISGIGT 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 156 ILGAINFITTTINMRSKNMTLDQTPLFVWSVVITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWF 235
Cdd:TIGR02843 201 LLTGINFFVTIIKMRAPGMTLMKMPVFTWTSLCSNVLIIASFPILTVTLALLTLDRYLGMHFFTNEAGGNPMMYVNLIWA 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 236 FGHPEVYILILPGFGIISHIICQESGKiESFGSLGMIYAMLSIGVMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTG 315
Cdd:TIGR02843 281 WGHPEVYILILPAFGIFSEVVATFSRK-RLFGYTSMVWATIAITVLSFIVWLHHFFTMGAGANVNAFFGIATMIIAIPTG 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 316 IKVFSWLATLYGTKIKFNPTLMWAIGFIFLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWF 395
Cdd:TIGR02843 360 VKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLLAVPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWF 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 396 PLFTGLSMNNKWLKIQFTIMFIGVNMTFFPQHFLGLAGMPRRYSDYPD-AYLSWNILSSMGSMISLTSIIMFIIILWESM 474
Cdd:TIGR02843 440 PKAFGFKLNEKLGKRSFWCWFIGFYLAFMPLYILGFMGMTRRLNHYDNpEWHPMLIIAAFGAFLIACGILCQIIQIFVSI 519
|
490 500 510
....*....|....*....|....*....|....*.
gi 2559106368 475 ISKRMILFTMNLP---SSNEWLQNSPPAEHSYSELP 507
Cdd:TIGR02843 520 RDRDQNRDTTGDPwggRTLEWSTSSPPPFYNFAVIP 555
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
2-507 |
2.95e-110 |
|
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: 341.06 E-value: 2.95e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 2 NKWLFSTNHKDIGTMYFMFGVWAGMMGMSMSLVIRAELGYPGQLIGDDQIYNTIITSHAFVMIFFMVMPIMIGgFGNWLV 81
Cdd:TIGR02882 42 NEWLTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 82 PIMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMIDSGVGTGWTVYPPLASNIAHSGGSVDLAIFSLHLAGISSILGAIN 161
Cdd:TIGR02882 121 PLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGIN 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 162 FITTTINMRSKNMTLDQTPLFVWSVVITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
Cdd:TIGR02882 201 FFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEV 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 242 YILILPGFGIISHIICQESGKiESFGSLGMIYAMLSIGVMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 321
Cdd:TIGR02882 281 YIVILPAFGIYSEIISTFAQK-RLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNW 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 322 LATLYGTKIKFNPTLMWAIGFIFLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLFTGL 401
Cdd:TIGR02882 360 LLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGY 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 402 SMNNKWLKIQFTIMFIGVNMTFFPQHFLGLAGMPRRYSDY--PDAYLSWNILSSMGS-MISLTSIIMFIIILWESMISKR 478
Cdd:TIGR02882 440 KLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYspSDGWFPLNLISTIGAlLMAIGFIFLVYNIYYSHRKSPR 519
|
490 500
....*....|....*....|....*....
gi 2559106368 479 MILFTMNLPSSNEWLQNSPPAEHSYSELP 507
Cdd:TIGR02882 520 EATGDPWNGRTLEWATASPPPKYNFAVTP 548
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
2-507 |
5.07e-103 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 323.04 E-value: 5.07e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 2 NKWLFSTNHKDIGTMYFMFGVWAGMMGMSMSLVIRAE--LGYPGQL-IGDDQIYNTIITSHAFVMIFFMVMPIMIGgFGN 78
Cdd:PRK15017 46 KEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQqaLASAGEAgFLPPHHYDQIFTAHGVIMIFFVAMPFVIG-LMN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 79 WLVPIMIGAPDMAFPRMNNMSFWLLPPSLTLLISSSMIDSGVGTGWTVYPPLASNIAHSGGSVDLAIFSLHLAGISSILG 158
Cdd:PRK15017 125 LVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLT 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 159 AINFITTTINMRSKNMTLDQTPLFVWSVVITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 238
Cdd:PRK15017 205 GINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGH 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 239 PEVYILILPGFGIISHIICQESGKiESFGSLGMIYAMLSIGVMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKV 318
Cdd:PRK15017 285 PEVYILILPVFGVFSEIAATFSRK-RLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKI 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 319 FSWLATLYGTKIKFNPTLMWAIGFIFLFTIGGLTGLVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGLIHWFPLF 398
Cdd:PRK15017 364 FNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKA 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 399 TGLSMNNKWLKIQFTIMFIGVNMTFFPQHFLGLAGMPRRYSDYPD-AYLSWNILSSMGSMISLTSIIMFIIILWESMISK 477
Cdd:PRK15017 444 FGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDpQFHTMLMIAASGAALIALGILCQVIQMYVSIRDR 523
|
490 500 510
....*....|....*....|....*....|...
gi 2559106368 478 RMILFTMNLP---SSNEWLQNSPPAEHSYSELP 507
Cdd:PRK15017 524 DQNRDLTGDPwggRTLEWATSSPPPFYNFAVVP 556
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
44-474 |
1.00e-21 |
|
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively. For general information on the heme-copper oxidase superfamily, please see cd00919.
Pssm-ID: 238830 Cd Length: 473 Bit Score: 97.74 E-value: 1.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 44 QLIGDDQIYNTIITSHAFVM-IFFMVMPIMigGFGNWLVPIMIGAPDMAfPRMNNMSFWLLppSLTLLISSSMIDSGVGT 122
Cdd:cd01660 36 PLPSSGILYYQGLTLHGVLLaIVFTTFFIM--GFFYAIVARALLRSLFN-RRLAWAGFWLM--VIGTVMAAVPILLGQAS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 123 G-WTVYPPLasnIAHSGGSVDLAIFSLHlagiSSILGAINFITTTInMRSKNMTLdQTPLFVWSVVITAILLLLSLPVLA 201
Cdd:cd01660 111 VlYTFYPPL---QAHPLFYIGAALVVVG----SWISGFAMFVTLWR-WKKANPGK-KVPLATFMVVTTMILWLVASLGVA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 202 GAITMLLtdrnLNTSFFDpAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIICQESGKIESFGSLG----MIYAMLS 277
Cdd:cd01660 182 LEVLFQL----LPWSLGL-VDTVDVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLArlafILFLLFS 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 278 IGVmGFivwaHHMFT-VGMDVDTRAYFTSATMIIAVPTGIKVFSWLATL-YGTKIKFNPTLMW---------------AI 340
Cdd:cd01660 257 TPV-GF----HHQFAdPGIGPGWKFIHMVLTFMVALPSLLTAFTVFASLeIAGRLRGGKGLFGwiralpwgdpmflalFL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2559106368 341 GFIFlFTIGGLTGLVLANSSLDIILHDTYYVVAHFHyvLSMGAVFAIMG-GLIHWF-PLFTGLSMNNKWL-KIQFTIMFI 417
Cdd:cd01660 332 AMLM-FIPGGAGGIINASYQLNYVVHNTAWVPGHFH--LTVGGAVALTFmAVAYWLvPHLTGRELAAKRLaLAQPWLWFV 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2559106368 418 GVNMTFFPQHFLGLAGMPRR--YSDYPDAYL-----SWNILSSMGSMISLTSIIMFIIILWESM 474
Cdd:cd01660 409 GMTIMSTAMHVAGLLGAPRRtaEAQYGGLPAagewaPYQQLMAIGGTILFVSGALFLYILFRTL 472
|
|
| |
