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Conserved domains on  [gi|436805134|gb|AGB57935|]
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cytochrome oxidase subunit 1, partial (mitochondrion) [Oxyrrhis maritima]

Protein Classification

heme-copper oxidase family protein( domain architecture ID 14)

heme-copper oxidase family protein may catalyze the transfer of electrons from an electron donor onto molecular oxygen

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Heme_Cu_Oxidase_I super family cl00275
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-159 3.86e-63

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.


The actual alignment was detected with superfamily member cd01663:

Pssm-ID: 469701  Cd Length: 488  Bit Score: 201.94  E-value: 3.86e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 436805134   1 GHPEVYILIIPAFGIISEGISLFT-QKIILAFDSIILAMLCLSLLGSAVWAHHIYTVGLEVDTRAYFTAVTIMISLPTGT 79
Cdd:cd01663  230 GHPEVYILILPGFGIISHIISTFSgKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGI 309

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 436805134  80 KVFNWLCSYLGNSMQINniTSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLGAVIALFSSLILY 159
Cdd:cd01663  310 KVFSWLATMWGGSIKFE--TPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYW 387
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-159 3.86e-63

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: 201.94  E-value: 3.86e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 436805134   1 GHPEVYILIIPAFGIISEGISLFT-QKIILAFDSIILAMLCLSLLGSAVWAHHIYTVGLEVDTRAYFTAVTIMISLPTGT 79
Cdd:cd01663  230 GHPEVYILILPGFGIISHIISTFSgKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGI 309

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 436805134  80 KVFNWLCSYLGNSMQINniTSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLGAVIALFSSLILY 159
Cdd:cd01663  310 KVFSWLATMWGGSIKFE--TPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYW 387
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-164 1.20e-60

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 195.86  E-value: 1.20e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 436805134   1 GHPEVYILIIPAFGIISEGISLFTQKIiLAFDSI--ILAMLCLSLLGSAVWAHHIYTVGLEVDTRAYFTAVTIMISLPTG 78
Cdd:MTH00153 237 GHPEVYILILPGFGMISHIISQESGKK-ETFGTLgmIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTG 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 436805134  79 TKVFNWLCSYLGnsMQINNITSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLGAVIALFSSLIL 158
Cdd:MTH00153 316 IKIFSWLATLHG--SQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIH 393


                 ....*.
gi 436805134 159 YQKVFF 164
Cdd:MTH00153 394 WFPLFT 399
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-156 2.97e-47

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: 160.47  E-value: 2.97e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 436805134    1 GHPEVYILIIPAFGIISEGISLFTQKIILAFDSIILAMLCLSLLGSAVWAHHIYTVGLEVDTRAYFTAVTIMISLPTGTK 80
Cdd:TIGR02891 232 GHPEVYIIFLPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVK 311

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 436805134   81 VFNWLCSYLGNSMQINniTSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLGAVIALFSSL 156
Cdd:TIGR02891 312 VFNWIATLWGGSIRFT--TPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAI 385
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-153 4.57e-46

Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];


Pssm-ID: 440605  Cd Length: 535  Bit Score: 157.98  E-value: 4.57e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 436805134   1 GHPEVYILIIPAFGIISEGISLFTQKIILAFDSIILAMLCLSLLGSAVWAHHIYTVGLEVDTRAYFTAVTIMISLPTGTK 80
Cdd:COG0843  241 GHPEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVK 320

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 436805134  81 VFNWLCSYLGNSMQINniTSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLGAVIALF 153
Cdd:COG0843  321 VFNWIATMWRGRIRFT--TPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFF 391
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-156 1.10e-36

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: 131.54  E-value: 1.10e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 436805134    1 GHPEVYILIIPAFGIISEGISLFTQKIILAFDSIILAMLCLSLLGSAVWAHHIYTVGLEVDTRAYFTAVTIMISLPTGTK 80
Cdd:pfam00115 207 GHPEVYILILPAFGIIYYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVK 286

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 436805134   81 VFNWLCSYLGNSMQINNiTSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLGAVIALFSSL 156
Cdd:pfam00115 287 VFNWLATLWGGWIRFRT-TPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGI 361
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-159 3.86e-63

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: 201.94  E-value: 3.86e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 436805134   1 GHPEVYILIIPAFGIISEGISLFT-QKIILAFDSIILAMLCLSLLGSAVWAHHIYTVGLEVDTRAYFTAVTIMISLPTGT 79
Cdd:cd01663  230 GHPEVYILILPGFGIISHIISTFSgKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGI 309

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 436805134  80 KVFNWLCSYLGNSMQINniTSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLGAVIALFSSLILY 159
Cdd:cd01663  310 KVFSWLATMWGGSIKFE--TPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYW 387
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-164 1.20e-60

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 195.86  E-value: 1.20e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 436805134   1 GHPEVYILIIPAFGIISEGISLFTQKIiLAFDSI--ILAMLCLSLLGSAVWAHHIYTVGLEVDTRAYFTAVTIMISLPTG 78
Cdd:MTH00153 237 GHPEVYILILPGFGMISHIISQESGKK-ETFGTLgmIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTG 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 436805134  79 TKVFNWLCSYLGnsMQINNITSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLGAVIALFSSLIL 158
Cdd:MTH00153 316 IKIFSWLATLHG--SQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIH 393


                 ....*.
gi 436805134 159 YQKVFF 164
Cdd:MTH00153 394 WFPLFT 399
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-163 3.13e-56

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 184.41  E-value: 3.13e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 436805134   1 GHPEVYILIIPAFGIISEGISLFTQKIiLAFDSI--ILAMLCLSLLGSAVWAHHIYTVGLEVDTRAYFTAVTIMISLPTG 78
Cdd:MTH00223 236 GHPEVYILILPGFGMISHIVSHYSSKK-EVFGTLgmIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 314

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 436805134  79 TKVFNWLCSYLGNsmQINNITSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLGAVIALFSSLIL 158
Cdd:MTH00223 315 IKVFSWLATIYGS--KIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNH 392


                 ....*
gi 436805134 159 YQKVF 163
Cdd:MTH00223 393 WFPLF 397
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-180 3.66e-55

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 181.80  E-value: 3.66e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 436805134   1 GHPEVYILIIPAFGIISEGISLFT-QKIILAFDSIILAMLCLSLLGSAVWAHHIYTVGLEVDTRAYFTAVTIMISLPTGT 79
Cdd:MTH00167 239 GHPEVYILILPGFGMISHIVVYYSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGI 318

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 436805134  80 KVFNWLCSYLGNSMQINniTSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLGAVIALFSSLILY 159
Cdd:MTH00167 319 KVFSWLATLHGGKIKWE--TPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHW 396

                        170       180
                 ....*....|....*....|.
gi 436805134 160 QKVFFASEVSfYSNTVFHFFL 180
Cdd:MTH00167 397 FPLFTGLTLN-ETWTKIHFFV 416
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-157 1.54e-54

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 180.29  E-value: 1.54e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 436805134   1 GHPEVYILIIPAFGIISEGISLFT-QKIILAFDSIILAMLCLSLLGSAVWAHHIYTVGLEVDTRAYFTAVTIMISLPTGT 79
Cdd:MTH00116 239 GHPEVYILILPGFGIISHIVTYYAgKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGI 318

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 436805134  80 KVFNWLCSYLGNsmQINNITSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLGAVIALFSSLI 157
Cdd:MTH00116 319 KVFSWLATLHGG--TIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFT 394
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-159 6.31e-53

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 175.64  E-value: 6.31e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 436805134   1 GHPEVYILIIPAFGIISEGISLFT-QKIILAFDSIILAMLCLSLLGSAVWAHHIYTVGLEVDTRAYFTAVTIMISLPTGT 79
Cdd:MTH00079 239 GHPEVYILILPAFGIISQSTLYLTgKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGV 318

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 436805134  80 KVFNWLCSYLGNSMQINNItsIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLGAVIALFSSLILY 159
Cdd:MTH00079 319 KVFSWLATLFGMKMKFQPL--LLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLW 396
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-163 7.21e-52

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 172.99  E-value: 7.21e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 436805134   1 GHPEVYILIIPAFGIISEGISLFT-QKIILAFDSIILAMLCLSLLGSAVWAHHIYTVGLEVDTRAYFTAVTIMISLPTGT 79
Cdd:MTH00142 237 GHPEVYILILPGFGMISHIINHYSgKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGI 316

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 436805134  80 KVFNWLCSYLGNSMQINniTSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLGAVIALFSSLILY 159
Cdd:MTH00142 317 KVFSWLATLHGSKVKYE--PPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHW 394


                 ....
gi 436805134 160 QKVF 163
Cdd:MTH00142 395 FPLF 398
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-159 1.21e-49

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: 166.17  E-value: 1.21e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 436805134   1 GHPEVYILIIPAFGIISEGISLFTQKIILAFDSIILAMLCLSLLGSAVWAHHIYTVGLEVDTRAYFTAVTIMISLPTGTK 80
Cdd:cd00919  227 GHPEVYILILPAFGAISEIIPTFSGKPLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIK 306

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 436805134  81 VFNWLCSYLGNSMQINniTSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLGAVIALFSSLILY 159
Cdd:cd00919  307 VFNWLATLWGGRIRFD--PPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYW 383
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-153 1.80e-48

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 164.22  E-value: 1.80e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 436805134   1 GHPEVYILIIPAFGIISEGISLFT-QKIILAFDSIILAMLCLSLLGSAVWAHHIYTVGLEVDTRAYFTAVTIMISLPTGT 79
Cdd:MTH00182 241 GHPEVYILILPGFGMISQIIPTFVaKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 320

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 436805134  80 KVFNWLCSYLGNSMQINniTSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLGAVIALF 153
Cdd:MTH00182 321 KVFSWLATIYGGTLRLD--TPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIF 392
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-180 6.03e-48

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 162.69  E-value: 6.03e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 436805134   1 GHPEVYILIIPAFGIISEGISLFTQKI-ILAFDSIILAMLCLSLLGSAVWAHHIYTVGLEVDTRAYFTAVTIMISLPTGT 79
Cdd:MTH00037 239 GHPEVYILILPGFGMISHVIAHYSGKQePFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 318

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 436805134  80 KVFNWLCSYLGNSMQINniTSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLGAVIALFSSLILY 159
Cdd:MTH00037 319 KVFSWMATLQGSNLRWE--TPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHW 396

                        170       180
                 ....*....|....*....|.
gi 436805134 160 QKVFFASEVSFYSNTVfHFFL 180
Cdd:MTH00037 397 FPLFSGVSLHPLWSKV-HFFL 416
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-156 2.97e-47

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: 160.47  E-value: 2.97e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 436805134    1 GHPEVYILIIPAFGIISEGISLFTQKIILAFDSIILAMLCLSLLGSAVWAHHIYTVGLEVDTRAYFTAVTIMISLPTGTK 80
Cdd:TIGR02891 232 GHPEVYIIFLPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVK 311

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 436805134   81 VFNWLCSYLGNSMQINniTSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLGAVIALFSSL 156
Cdd:TIGR02891 312 VFNWIATLWGGSIRFT--TPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAI 385
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-153 4.93e-47

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 160.38  E-value: 4.93e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 436805134   1 GHPEVYILIIPAFGIISEGISLFT-QKIILAFDSIILAMLCLSLLGSAVWAHHIYTVGLEVDTRAYFTAVTIMISLPTGT 79
Cdd:MTH00184 241 GHPEVYILILPGFGIISQIIPTFAaKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 320

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 436805134  80 KVFNWLCSYLGNSMQINniTSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLGAVIALF 153
Cdd:MTH00184 321 KIFSWIATIFGGSLRLD--TPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIF 392
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-163 7.58e-47

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 160.09  E-value: 7.58e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 436805134   1 GHPEVYILIIPAFGIISEGISLFT-QKIILAFDSIILAMLCLSLLGSAVWAHHIYTVGLEVDTRAYFTAVTIMISLPTGT 79
Cdd:MTH00183 239 GHPEVYILILPGFGMISHIVAYYSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGV 318

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 436805134  80 KVFNWLCSYLGNSMQINniTSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLGAVIALFSSLILY 159
Cdd:MTH00183 319 KVFSWLATLHGGSIKWE--TPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHW 396


                 ....
gi 436805134 160 QKVF 163
Cdd:MTH00183 397 FPLF 400
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-163 3.61e-46

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 158.12  E-value: 3.61e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 436805134   1 GHPEVYILIIPAFGIISEGISLFT-QKIILAFDSIILAMLCLSLLGSAVWAHHIYTVGLEVDTRAYFTAVTIMISLPTGT 79
Cdd:MTH00103 239 GHPEVYILILPGFGMISHIVTYYSgKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGV 318

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 436805134  80 KVFNWLCSYLGNSmqINNITSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLGAVIALFSSLILY 159
Cdd:MTH00103 319 KVFSWLATLHGGN--IKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHW 396


                 ....
gi 436805134 160 QKVF 163
Cdd:MTH00103 397 FPLF 400
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-163 3.63e-46

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 158.18  E-value: 3.63e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 436805134   1 GHPEVYILIIPAFGIISEGISLF-TQKIILAFDSIILAMLCLSLLGSAVWAHHIYTVGLEVDTRAYFTAVTIMISLPTGT 79
Cdd:MTH00077 239 GHPEVYILILPGFGMISHIVTYYsAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGV 318

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 436805134  80 KVFNWLCSYLGNSMQINniTSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLGAVIALFSSLILY 159
Cdd:MTH00077 319 KVFSWLATMHGGAIKWD--AAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHW 396


                 ....
gi 436805134 160 QKVF 163
Cdd:MTH00077 397 FPLF 400
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-153 4.57e-46

Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];


Pssm-ID: 440605  Cd Length: 535  Bit Score: 157.98  E-value: 4.57e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 436805134   1 GHPEVYILIIPAFGIISEGISLFTQKIILAFDSIILAMLCLSLLGSAVWAHHIYTVGLEVDTRAYFTAVTIMISLPTGTK 80
Cdd:COG0843  241 GHPEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVK 320

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 436805134  81 VFNWLCSYLGNSMQINniTSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLGAVIALF 153
Cdd:COG0843  321 VFNWIATMWRGRIRFT--TPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFF 391
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-159 1.06e-45

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 157.10  E-value: 1.06e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 436805134   1 GHPEVYILIIPAFGIISEGISLFT-QKIILAFDSIILAMLCLSLLGSAVWAHHIYTVGLEVDTRAYFTAVTIMISLPTGT 79
Cdd:MTH00026 240 GHPEVYILILPGFGIISQILSLFSyKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGI 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 436805134  80 KVFNWLCSYLGNSMQINNITSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLGAVIALFSSLILY 159
Cdd:MTH00026 320 KIFSWLATVSGSGRNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLW 399
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-164 1.74e-45

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: 155.82  E-value: 1.74e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 436805134   1 GHPEVYILIIPAFGIISEGISLFTQKIILAFDSIILAMLCLSLLGSAVWAHHIYTVGLEVDTRAYFTAVTIMISLPTGTK 80
Cdd:cd01662  233 GHPEVYILILPAFGIFSEIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVK 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 436805134  81 VFNWLCSYLGNSMQINniTSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLGAVIALFSSLILYQ 160
Cdd:cd01662  313 IFNWLFTMWRGRIRFE--TPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWF 390


                 ....
gi 436805134 161 KVFF 164
Cdd:cd01662  391 PKMF 394
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-157 5.86e-40

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 141.35  E-value: 5.86e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 436805134   1 GHPEVYILIIPAFGIISE-GISLFTQKIILAFDSIILAMLCLSLLGSAVWAHHIYTVGLEVDTRAYFTAVTIMISLPTGT 79
Cdd:MTH00048 237 GHPEVYVLILPGFGIISHiCLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGI 316

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 436805134  80 KVFNWLCSYLGNSMQINNiTSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLGAVIALFSSLI 157
Cdd:MTH00048 317 KVFSWLYMLLNSRVRKSD-PVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFI 393
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-156 1.10e-36

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: 131.54  E-value: 1.10e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 436805134    1 GHPEVYILIIPAFGIISEGISLFTQKIILAFDSIILAMLCLSLLGSAVWAHHIYTVGLEVDTRAYFTAVTIMISLPTGTK 80
Cdd:pfam00115 207 GHPEVYILILPAFGIIYYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVK 286

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 436805134   81 VFNWLCSYLGNSMQINNiTSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLGAVIALFSSL 156
Cdd:pfam00115 287 VFNWLATLWGGWIRFRT-TPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGI 361
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-156 9.98e-36

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 131.21  E-value: 9.98e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 436805134   1 GHPEVYILIIPAFGIISEGISLFTQKIILAFDSIILAMLCLSLLGSAVWAHHIYTVGLEVDTRAYFTAVTIMISLPTGTK 80
Cdd:PRK15017 283 GHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVK 362

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 436805134  81 VFNWLCSYLGNSMQINniTSIKWIILFLLTFTLGGSTGVILANSATDLALHDTYYVVAHFHFVLSLGAVIALFSSL 156
Cdd:PRK15017 363 IFNWLFTMYQGRIVFH--SAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGM 436
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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