NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1197265417|ref|WP_086509685|]
View 

c-type cytochrome [Billgrantia desiderata]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-259 7.42e-70

Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];


:

Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 221.63  E-value: 7.42e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417   1 MAIAVAVIVLAVgsvLFFFLSPWYLTPLASNWGTIDDTITITLWVTGAVFLAVNLFLAYVVVRYRfnkRRRSQYDP---- 76
Cdd:COG1622     1 MKRLLLALLLLA---LLLSGQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYR---RRKGDADPaqfh 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417  77 ENKSLELWLTGLTTLGIAGLLAPGLLVWGSFVSPPQEAHQVEVVGQQWHWSFRFPGEDGrfgaahnrfidernpfgmvdd 156
Cdd:COG1622    75 HNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGI--------------------- 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 157 pagqddilITSPHLVLPVDRPVKMVLRSKDVLHNVKVANFRAKMDMVPGQTSYFWFTPTVVGEYEIVCAQLCGIAHFAMR 236
Cdd:COG1622   134 --------ATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMR 205

                         250       260
                  ....*....|....*....|...
gi 1197265417 237 GRIEVVEQEVFDAWLSEQPTYAE 259
Cdd:COG1622   206 FKVVVVSPEEFDAWLAEQKASAA 228
CytC553 COG2863
Cytochrome c553 [Energy production and conversion];
264-359 3.17e-25

Cytochrome c553 [Energy production and conversion];


:

Pssm-ID: 442110 [Multi-domain]  Cd Length: 98  Bit Score: 99.03  E-value: 3.17e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 264 APGDPEAGAERYATCAACHGAEGQGNAALNAPKLAGMDAWYLERQLALFRSGARgsheddtYGQQMRPFATMLPDRQaIV 343
Cdd:COG2863    11 AAGDAARGKAYAAACAACHGADGEGNPGGGAPRLAGQHAEYLVAQLKAFRSGAR-------KNGVMPAIAKGLSDED-IK 82

                          90
                  ....*....|....*.
gi 1197265417 344 DVSAFIETLPDQAVET 359
Cdd:COG2863    83 ALAAYIASLKAPPGAA 98
CytC553 COG2863
Cytochrome c553 [Energy production and conversion];
356-453 4.86e-23

Cytochrome c553 [Energy production and conversion];


:

Pssm-ID: 442110 [Multi-domain]  Cd Length: 98  Bit Score: 93.26  E-value: 4.86e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 356 AVETSLAGGDPERGARRYRTCANCHGQQGEGIRATNGPRLAGLPDWYLERQLQNFRHGVRgrhredpYGNQMIEMAQVLv 435
Cdd:COG2863     5 LLAAPAAAGDAARGKAYAAACAACHGADGEGNPGGGAPRLAGQHAEYLVAQLKAFRSGAR-------KNGVMPAIAKGL- 76

                          90
                  ....*....|....*...
gi 1197265417 436 DDRAVRDVVAYITTLPQP 453
Cdd:COG2863    77 SDEDIKALAAYIASLKAP 94
 
Name Accession Description Interval E-value
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-259 7.42e-70

Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 221.63  E-value: 7.42e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417   1 MAIAVAVIVLAVgsvLFFFLSPWYLTPLASNWGTIDDTITITLWVTGAVFLAVNLFLAYVVVRYRfnkRRRSQYDP---- 76
Cdd:COG1622     1 MKRLLLALLLLA---LLLSGQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYR---RRKGDADPaqfh 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417  77 ENKSLELWLTGLTTLGIAGLLAPGLLVWGSFVSPPQEAHQVEVVGQQWHWSFRFPGEDGrfgaahnrfidernpfgmvdd 156
Cdd:COG1622    75 HNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGI--------------------- 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 157 pagqddilITSPHLVLPVDRPVKMVLRSKDVLHNVKVANFRAKMDMVPGQTSYFWFTPTVVGEYEIVCAQLCGIAHFAMR 236
Cdd:COG1622   134 --------ATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMR 205

                         250       260
                  ....*....|....*....|...
gi 1197265417 237 GRIEVVEQEVFDAWLSEQPTYAE 259
Cdd:COG1622   206 FKVVVVSPEEFDAWLAEQKASAA 228
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 116-242 8.73e-47

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 157.42  E-value: 8.73e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 116 QVEVVGQQWHWSFRFPGEDGRFGAahnrfidernpfgmvddpagqdDILITSPHLVLPVDRPVKMVLRSKDVLHNVKVAN 195
Cdd:cd13919     3 VVEVTAQQWAWTFRYPGGDGKLGT----------------------DDDVTSPELHLPVGRPVLFNLRSKDVIHSFWVPE 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1197265417 196 FRAKMDMVPGQTSYFWFTPTVVGEYEIVCAQLCGIAHFAMRGRIEVV 242
Cdd:cd13919    61 FRVKQDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRMRATVKVV 107
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 32-252 1.69e-34

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 127.88  E-value: 1.69e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417  32 WGTIDDTITITLWVTGAVFLAVNLFLAYVVVRYRfnkRRRSQYDPENKSLELWLTGLTTLgIAGLLAPGLLVWGSF---- 107
Cdd:TIGR02866   6 AQQIAFLFLFVLAVSTLISLLVAALLAYVVWKFR---RKGDEEKPSQIHGNRRLEYVWTV-IPLIIVVGLFAATAKglly 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 108 --VSPPQEAHQVEVVGQQWHWSFRFPgedgrfgaahnrfidernpfgmvddpagqDDILITSPHLVLPVDRPVKMVLRSK 185
Cdd:TIGR02866  82 leRPIPKDALKVKVTGYQWWWDFEYP-----------------------------ESGFTTVNELVLPAGTPVELQVTSK 132

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1197265417 186 DVLHNVKVANFRAKMDMVPGQTSYFWFTPTVVGEYEIVCAQLCGIAHFAMRGRIEVVEQEVFDAWLS 252
Cdd:TIGR02866 133 DVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
CytC553 COG2863
Cytochrome c553 [Energy production and conversion];
264-359 3.17e-25

Cytochrome c553 [Energy production and conversion];


Pssm-ID: 442110 [Multi-domain]  Cd Length: 98  Bit Score: 99.03  E-value: 3.17e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 264 APGDPEAGAERYATCAACHGAEGQGNAALNAPKLAGMDAWYLERQLALFRSGARgsheddtYGQQMRPFATMLPDRQaIV 343
Cdd:COG2863    11 AAGDAARGKAYAAACAACHGADGEGNPGGGAPRLAGQHAEYLVAQLKAFRSGAR-------KNGVMPAIAKGLSDED-IK 82

                          90
                  ....*....|....*.
gi 1197265417 344 DVSAFIETLPDQAVET 359
Cdd:COG2863    83 ALAAYIASLKAPPGAA 98
CytC553 COG2863
Cytochrome c553 [Energy production and conversion];
356-453 4.86e-23

Cytochrome c553 [Energy production and conversion];


Pssm-ID: 442110 [Multi-domain]  Cd Length: 98  Bit Score: 93.26  E-value: 4.86e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 356 AVETSLAGGDPERGARRYRTCANCHGQQGEGIRATNGPRLAGLPDWYLERQLQNFRHGVRgrhredpYGNQMIEMAQVLv 435
Cdd:COG2863     5 LLAAPAAAGDAARGKAYAAACAACHGADGEGNPGGGAPRLAGQHAEYLVAQLKAFRSGAR-------KNGVMPAIAKGL- 76

                          90
                  ....*....|....*...
gi 1197265417 436 DDRAVRDVVAYITTLPQP 453
Cdd:COG2863    77 SDEDIKALAAYIASLKAP 94
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
117-242 1.73e-14

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 69.75  E-value: 1.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 117 VEVVGQQWHWSFRFPGedgrfgaahnrFIDERNPFGMV---DDPAGQDDILITSPHLVLPVDRPVKMVLRSKDVLHNVKV 193
Cdd:pfam00116   3 IKAIGHQWYWSYEYTD-----------FGDLEFDSYMIpteDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAV 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1197265417 194 ANFRAKMDMVPGQTSYFWFTPTVVGEYEIVCAQLCGIAHFAMRGRIEVV 242
Cdd:pfam00116  72 PSLGIKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 41-243 2.37e-14

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 71.52  E-value: 2.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417  41 ITLWVTgaVFLAVNLFLAYVVVRYRfnkrrrsqydPENKSLELWLTGLTTLGIAGLLAPGL--LVWGS--FVSPPqeahq 116
Cdd:MTH00047   21 IPCWVY--IMLCWQVVSGNGSVNFG----------SENQVLELLWTVVPTLLVLVLCFLNLnfITSDLdcFSSET----- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 117 VEVVGQQWHWSFRFPGeDGRFGAAHNRFIDernpfgMVDDPagqddilitsphLVLPVDRPVKMVLRSKDVLHNVKVANF 196
Cdd:MTH00047   84 IKVIGHQWYWSYEYSF-GGSYDSFMTDDIF------GVDKP------------LRLVYGVPYHLLVTSSDVIHSFSVPDL 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1197265417 197 RAKMDMVPGQTSYFWFTPTVVGEYEIVCAQLCGIAHFAMRGRIEVVE 243
Cdd:MTH00047  145 NLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVVD 191
Cytochrom_C pfam00034
Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and ...
 269-352 2.74e-11

Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and cytochrome c' families are not included. All these are now in a new clan together. The C-terminus of DUF989, pfam06181, has now been merged into this family.


Pssm-ID: 459641 [Multi-domain]  Cd Length: 89  Bit Score: 59.47  E-value: 2.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 269 EAGAERYAT-CAACHGAEGQGnAALNAPKLAGMDAWYLERQLALFRSGARGSHE--DDTYGQQMRPFATMLP--DRQAIV 343
Cdd:pfam00034   1 ARGKKLFAAnCAACHGVNGEG-AGAGGPDLAGLAARYPGDALGAIRENKHAIGGggVDRAGGPPGTGMPAFDglTDEEIA 79


                  ....*....
gi 1197265417 344 DVSAFIETL 352
Cdd:pfam00034  80 DLVAYLLSL 88
Cytochrom_C pfam00034
Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and ...
 367-450 1.28e-09

Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and cytochrome c' families are not included. All these are now in a new clan together. The C-terminus of DUF989, pfam06181, has now been merged into this family.


Pssm-ID: 459641 [Multi-domain]  Cd Length: 89  Bit Score: 54.85  E-value: 1.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 367 ERGARRY-RTCANCHGQQGEGIrATNGPRLAGLPDWYLERQLQNFRHGVR----GRHREDPYGNQMIEMAQVLVDDRAVR 441
Cdd:pfam00034   1 ARGKKLFaANCAACHGVNGEGA-GAGGPDLAGLAARYPGDALGAIRENKHaiggGGVDRAGGPPGTGMPAFDGLTDEEIA 79


                  ....*....
gi 1197265417 442 DVVAYITTL 450
Cdd:pfam00034  80 DLVAYLLSL 88
ccoP TIGR00782
cytochrome c oxidase, cbb3-type, subunit III; This model describes a di-heme subunit of ...
 259-354 3.68e-04

cytochrome c oxidase, cbb3-type, subunit III; This model describes a di-heme subunit of approximately 26 kDa of the cbb3 type copper and heme-containing cytochrome oxidase. [Energy metabolism, Electron transport]


Pssm-ID: 129864 [Multi-domain]  Cd Length: 285  Bit Score: 42.19  E-value: 3.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 259 ELAQLAPGDPEA---GAERYAT-CAACHGAEGQGNAALNAPKLAGmDAW-YLERQLALFRSGARGSheddtyGQQMRPFA 333
Cdd:TIGR00782 191 SLSSGKPKDEALaakGQELFADnCTTCHGEDGKGLQELGAPNLTD-DVWlYGGDLKTITTTITNGR------GGVMPAWG 263

                          90       100
                  ....*....|....*....|.
gi 1197265417 334 TMLPDRQaIVDVSAFIETLPD 354
Cdd:TIGR00782 264 PRLSEAQ-IKALAAYVHSLGG 283
 
Name Accession Description Interval E-value
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-259 7.42e-70

Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 221.63  E-value: 7.42e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417   1 MAIAVAVIVLAVgsvLFFFLSPWYLTPLASNWGTIDDTITITLWVTGAVFLAVNLFLAYVVVRYRfnkRRRSQYDP---- 76
Cdd:COG1622     1 MKRLLLALLLLA---LLLSGQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYR---RRKGDADPaqfh 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417  77 ENKSLELWLTGLTTLGIAGLLAPGLLVWGSFVSPPQEAHQVEVVGQQWHWSFRFPGEDGrfgaahnrfidernpfgmvdd 156
Cdd:COG1622    75 HNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGI--------------------- 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 157 pagqddilITSPHLVLPVDRPVKMVLRSKDVLHNVKVANFRAKMDMVPGQTSYFWFTPTVVGEYEIVCAQLCGIAHFAMR 236
Cdd:COG1622   134 --------ATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMR 205

                         250       260
                  ....*....|....*....|...
gi 1197265417 237 GRIEVVEQEVFDAWLSEQPTYAE 259
Cdd:COG1622   206 FKVVVVSPEEFDAWLAEQKASAA 228
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 116-242 8.73e-47

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 157.42  E-value: 8.73e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 116 QVEVVGQQWHWSFRFPGEDGRFGAahnrfidernpfgmvddpagqdDILITSPHLVLPVDRPVKMVLRSKDVLHNVKVAN 195
Cdd:cd13919     3 VVEVTAQQWAWTFRYPGGDGKLGT----------------------DDDVTSPELHLPVGRPVLFNLRSKDVIHSFWVPE 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1197265417 196 FRAKMDMVPGQTSYFWFTPTVVGEYEIVCAQLCGIAHFAMRGRIEVV 242
Cdd:cd13919    61 FRVKQDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRMRATVKVV 107
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 32-252 1.69e-34

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 127.88  E-value: 1.69e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417  32 WGTIDDTITITLWVTGAVFLAVNLFLAYVVVRYRfnkRRRSQYDPENKSLELWLTGLTTLgIAGLLAPGLLVWGSF---- 107
Cdd:TIGR02866   6 AQQIAFLFLFVLAVSTLISLLVAALLAYVVWKFR---RKGDEEKPSQIHGNRRLEYVWTV-IPLIIVVGLFAATAKglly 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 108 --VSPPQEAHQVEVVGQQWHWSFRFPgedgrfgaahnrfidernpfgmvddpagqDDILITSPHLVLPVDRPVKMVLRSK 185
Cdd:TIGR02866  82 leRPIPKDALKVKVTGYQWWWDFEYP-----------------------------ESGFTTVNELVLPAGTPVELQVTSK 132

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1197265417 186 DVLHNVKVANFRAKMDMVPGQTSYFWFTPTVVGEYEIVCAQLCGIAHFAMRGRIEVVEQEVFDAWLS 252
Cdd:TIGR02866 133 DVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 114-241 9.17e-33

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 119.66  E-value: 9.17e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 114 AHQVEVVGQQWHWSFRFPGEDGrfgaahnrfidernpfgmvddpagqddiliTSPHLVLPVDRPVKMVLRSKDVLHNVKV 193
Cdd:cd13915     1 ALEIQVTGRQWMWEFTYPNGKR------------------------------EINELHVPVGKPVRLILTSKDVIHSFYV 50

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1197265417 194 ANFRAKMDMVPGQTSYFWFTPTVVGEYEIVCAQLCGIAHFAMRGRIEV 241
Cdd:cd13915    51 PAFRIKQDVVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKVRV 98
CytC553 COG2863
Cytochrome c553 [Energy production and conversion];
264-359 3.17e-25

Cytochrome c553 [Energy production and conversion];


Pssm-ID: 442110 [Multi-domain]  Cd Length: 98  Bit Score: 99.03  E-value: 3.17e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 264 APGDPEAGAERYATCAACHGAEGQGNAALNAPKLAGMDAWYLERQLALFRSGARgsheddtYGQQMRPFATMLPDRQaIV 343
Cdd:COG2863    11 AAGDAARGKAYAAACAACHGADGEGNPGGGAPRLAGQHAEYLVAQLKAFRSGAR-------KNGVMPAIAKGLSDED-IK 82

                          90
                  ....*....|....*.
gi 1197265417 344 DVSAFIETLPDQAVET 359
Cdd:COG2863    83 ALAAYIASLKAPPGAA 98
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 92-251 1.95e-24

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 98.30  E-value: 1.95e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417  92 GIAGLLAPGLLVWGSFV-----SPP----QEAHQVEVVGQQWHWSFRFPGEDGrfgaahnrfidernpfgmvddpagqdd 162
Cdd:cd13918     1 GLSAIIVISLIVWTYGMllyveDPPdeadEDALEVEVEGFQFGWQFEYPNGVT--------------------------- 53

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 163 iliTSPHLVLPVDRPVKMVLRSKDVLHNVKVANFRAKMDMVPGQTSYFWFTPTVVGEYEIVCAQLCGIAHFAMRGRIEVV 242
Cdd:cd13918    54 ---TGNTLRVPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVM 130


                  ....*....
gi 1197265417 243 EQEVFDAWL 251
Cdd:cd13918   131 DEEEFEAWY 139
CytC553 COG2863
Cytochrome c553 [Energy production and conversion];
356-453 4.86e-23

Cytochrome c553 [Energy production and conversion];


Pssm-ID: 442110 [Multi-domain]  Cd Length: 98  Bit Score: 93.26  E-value: 4.86e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 356 AVETSLAGGDPERGARRYRTCANCHGQQGEGIRATNGPRLAGLPDWYLERQLQNFRHGVRgrhredpYGNQMIEMAQVLv 435
Cdd:COG2863     5 LLAAPAAAGDAARGKAYAAACAACHGADGEGNPGGGAPRLAGQHAEYLVAQLKAFRSGAR-------KNGVMPAIAKGL- 76

                          90
                  ....*....|....*...
gi 1197265417 436 DDRAVRDVVAYITTLPQP 453
Cdd:COG2863    77 SDEDIKALAAYIASLKAP 94
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 117-242 1.06e-22

The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of most bacteria, is a multi-chain transmembrane protein located in the inner membrane the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. Caa3 type of CcO Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the cytochromes a, a3 and CuB active site in subunit I.


Pssm-ID: 259875 [Multi-domain]  Cd Length: 103  Bit Score: 92.30  E-value: 1.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 117 VEVVGQQWHWSFRFPGEDGRfgaahnrfidernpfgmvddpagqddILITSPHLVLPVDRPVKMVLRSKDVLHNVKVANF 196
Cdd:cd04213     4 IEVTGHQWWWEFRYPDEPGR--------------------------GIVTANELHIPVGRPVRLRLTSADVIHSFWVPSL 57

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1197265417 197 RAKMDMVPGQTSYFWFTPTVVGEYEIVCAQLCGIAHFAMRGRIEVV 242
Cdd:cd04213    58 AGKMDMIPGRTNRLWLQADEPGVYRGQCAEFCGASHALMRFKVIAL 103
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 116-251 5.85e-22

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 90.55  E-value: 5.85e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 116 QVEVVGQQWHWSFRFPGEDgrfgaahnrfidernpfgmvddpagqddiLITSPHLVLPVDRPVKMVLRSKDVLHNVKVAN 195
Cdd:cd13914     2 EIEVEAYQWGWEFSYPEAN-----------------------------VTTSEQLVIPADRPVYFRITSRDVIHAFHVPE 52

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1197265417 196 FRAKMDMVPGQTSYFWFTPTVVGEYEIVCAQLCGIAHFAMRGRIEVVEQEVFDAWL 251
Cdd:cd13914    53 LGLKQDAFPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 116-240 6.93e-22

Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259911 [Multi-domain]  Cd Length: 95  Bit Score: 89.66  E-value: 6.93e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 116 QVEVVGQQWHWSFRFPGedgrfgaahnrfidernpfgmvddpagqddiLITSPHLVLPVDRPVKMVLRSKDVLHNVKVAN 195
Cdd:cd13842     2 TVYVTGVQWSWTFIYPN-------------------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPN 50

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1197265417 196 FRAKMDMVPGQTSYFWFTPTVVGEYEIVCAQLCGIAHFAMRGRIE 240
Cdd:cd13842    51 LGVKVDAVPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 117-250 2.32e-16

C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 75.30  E-value: 2.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 117 VEVVGQQWHWSFRFP-GEDGRFGAAhnrfidernpfgMVDDP---AGQDDILITSPHLVLPVDRPVKMVLRSKDVLHNVK 192
Cdd:cd13912     5 IKAIGHQWYWSYEYSdFNDLEFDSY------------MIPEDdleKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWA 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1197265417 193 VANFRAKMDMVPGQTSYFWFTPTVVGEYEIVCAQLCGIAHFAMRGRIEVVEQEVFDAW 250
Cdd:cd13912    73 VPSLGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 166-242 1.44e-15

C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea, which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead, they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively.


Pssm-ID: 259980 [Multi-domain]  Cd Length: 99  Bit Score: 72.22  E-value: 1.44e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1197265417 166 TSPHLVLPVDRPVKMVLRSKDVLHNVKVANFRAKMDMVPGQTSYFWFTPTVVGEYEIVCAQLCGIAHFAMRGRIEVV 242
Cdd:cd13913    23 NPNEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMYGKIIVE 99
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
117-242 1.73e-14

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 69.75  E-value: 1.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 117 VEVVGQQWHWSFRFPGedgrfgaahnrFIDERNPFGMV---DDPAGQDDILITSPHLVLPVDRPVKMVLRSKDVLHNVKV 193
Cdd:pfam00116   3 IKAIGHQWYWSYEYTD-----------FGDLEFDSYMIpteDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAV 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1197265417 194 ANFRAKMDMVPGQTSYFWFTPTVVGEYEIVCAQLCGIAHFAMRGRIEVV 242
Cdd:pfam00116  72 PSLGIKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 41-243 2.37e-14

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 71.52  E-value: 2.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417  41 ITLWVTgaVFLAVNLFLAYVVVRYRfnkrrrsqydPENKSLELWLTGLTTLGIAGLLAPGL--LVWGS--FVSPPqeahq 116
Cdd:MTH00047   21 IPCWVY--IMLCWQVVSGNGSVNFG----------SENQVLELLWTVVPTLLVLVLCFLNLnfITSDLdcFSSET----- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 117 VEVVGQQWHWSFRFPGeDGRFGAAHNRFIDernpfgMVDDPagqddilitsphLVLPVDRPVKMVLRSKDVLHNVKVANF 196
Cdd:MTH00047   84 IKVIGHQWYWSYEYSF-GGSYDSFMTDDIF------GVDKP------------LRLVYGVPYHLLVTSSDVIHSFSVPDL 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1197265417 197 RAKMDMVPGQTSYFWFTPTVVGEYEIVCAQLCGIAHFAMRGRIEVVE 243
Cdd:MTH00047  145 NLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVVD 191
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 49-251 2.16e-13

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 69.20  E-value: 2.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417  49 VFLAVNLFLAYVVVRYRFNKRRRSQYdPENKSLELWLTglttlgiaglLAPG-LLVWGSFVS-----------PPqeAHQ 116
Cdd:MTH00140   30 VLVLIFSFVMYMLVLLLFNKFSCRTI-LEAQKLETIWT----------IVPAlILVFLALPSlrllylldetnNP--LLT 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 117 VEVVGQQWHWSFRFPGEDG-RFgaahnrfiDERnpfgMVDD---PAGQDDILITSPHLVLPVDRPVKMVLRSKDVLHNVK 192
Cdd:MTH00140   97 VKAIGHQWYWSYEYSDFSViEF--------DSY----MVPEnelELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWT 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1197265417 193 VANFRAKMDMVPGQTSYFWFTPTVVGEYEIVCAQLCGIAHFAMRGRIEVVEQEVFDAWL 251
Cdd:MTH00140  165 VPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWL 223
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 117-252 3.77e-13

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 68.76  E-value: 3.77e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 117 VEVVGQQWHWSFRFPGEDGRFGAAHNRFIDERNPfgmvddpaGQDDILITSPHLVLPVDRPVKMVLRSKDVLHNVKVANF 196
Cdd:MTH00185   97 IKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTP--------GQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPAL 168

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1197265417 197 RAKMDMVPGQTSYFWFTPTVVGEYEIVCAQLCGIAHFAMRGRIEVVEQEVFDAWLS 252
Cdd:MTH00185  169 GVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSS 224
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 49-252 3.08e-12

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 66.03  E-value: 3.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417  49 VFLAVNLFLAYVVVRYRFNKRRrSQYDPENKSLELWLTGLTTLGIAGLLAPGLLVWGSFVSPPQEAHQVEVVGQQWHWSF 128
Cdd:MTH00008   30 ILTLVLTVVGYAMTSLMFNKLS-NRYILEAQQIETIWTILPALILLFLAFPSLRLLYLMDEVSNPSITLKTIGHQWYWSY 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 129 RFpgedgrfgaahNRFIDERNPFGMV---DDPAGQDDILITSPHLVLPVDRPVKMVLRSKDVLHNVKVANFRAKMDMVPG 205
Cdd:MTH00008  109 EY-----------SDFSNLEFDSYMLptsDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPG 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1197265417 206 QTSYFWFTPTVVGEYEIVCAQLCGIAHFAMRGRIEVVEQEVFDAWLS 252
Cdd:MTH00008  178 RLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVS 224
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 117-253 4.11e-12

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 65.39  E-value: 4.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 117 VEVVGQQWHWSFRFpgedgrfgaahNRFIDernpFG----MV---DDPAGQDDILITSPHLVLPVDRPVKMVLRSKDVLH 189
Cdd:MTH00168   97 IKAVGHQWYWSYEY-----------TDYND----LEfdsyMVptqDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLH 161

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1197265417 190 NVKVANFRAKMDMVPG---QTSYFWFTPtvvGEYEIVCAQLCGIAHFAMRGRIEVVEQEVFDAWLSE 253
Cdd:MTH00168  162 SWTLPSLGLKMDAVPGrlnQLAFLSSRP---GSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 77-253 5.53e-12

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 65.11  E-value: 5.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417  77 ENKSLELWLTGLTTLGIAGLLAPG--LLVWGSFVSPPQEAhqVEVVGQQWHWSFRFpgedgrfgAAHNRF-IDERnpfgM 153
Cdd:MTH00038   57 EGQELETIWTIVPAFILIFIALPSlqLLYLMDEVNNPFLT--IKAIGHQWYWSYEY--------TDYNDLeFDSY----M 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 154 V---DDPAGQDDILITSPHLVLPVDRPVKMVLRSKDVLHNVKVANFRAKMDMVPGQTSYFWFTPTVVGEYEIVCAQLCGI 230
Cdd:MTH00038  123 VptsDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGA 202

                         170       180
                  ....*....|....*....|...
gi 1197265417 231 AHFAMRGRIEVVEQEVFDAWLSE 253
Cdd:MTH00038  203 NHSFMPIVIESVPFNTFENWVSN 225
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 117-252 5.67e-12

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 65.12  E-value: 5.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 117 VEVVGQQWHWSFRFPG-EDGRFGAAhnrfidernpfgMV---DDPAGQDDILITSPHLVLPVDRPVKMVLRSKDVLHNVK 192
Cdd:MTH00129   97 IKAMGHQWYWSYEYTDyEDLGFDSY------------MIptqDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWA 164

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 193 VANFRAKMDMVPGQTSYFWFTPTVVGEYEIVCAQLCGIAHFAMRGRIEVVEQEVFDAWLS 252
Cdd:MTH00129  165 VPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSS 224
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 117-252 1.29e-11

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 64.35  E-value: 1.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 117 VEVVGQQWHWSFRFPGEDGRFGAAHNRFIDERNPfgmvddpaGQDDILITSPHLVLPVDRPVKMVLRSKDVLHNVKVANF 196
Cdd:MTH00098   97 VKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKP--------GELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSL 168

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1197265417 197 RAKMDMVPGQTSYFWFTPTVVGEYEIVCAQLCGIAHFAMRGRIEVVEQEVFDAWLS 252
Cdd:MTH00098  169 GLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSA 224
Cytochrom_C pfam00034
Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and ...
 269-352 2.74e-11

Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and cytochrome c' families are not included. All these are now in a new clan together. The C-terminus of DUF989, pfam06181, has now been merged into this family.


Pssm-ID: 459641 [Multi-domain]  Cd Length: 89  Bit Score: 59.47  E-value: 2.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 269 EAGAERYAT-CAACHGAEGQGnAALNAPKLAGMDAWYLERQLALFRSGARGSHE--DDTYGQQMRPFATMLP--DRQAIV 343
Cdd:pfam00034   1 ARGKKLFAAnCAACHGVNGEG-AGAGGPDLAGLAARYPGDALGAIRENKHAIGGggVDRAGGPPGTGMPAFDglTDEEIA 79


                  ....*....
gi 1197265417 344 DVSAFIETL 352
Cdd:pfam00034  80 DLVAYLLSL 88
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 117-252 7.07e-11

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 62.08  E-value: 7.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 117 VEVVGQQWHWSFRFpgedgrfgaahNRFIDERNPFG--MV---DDPAGQDDILITSPHLVLPVDRPVKMVLRSKDVLHNV 191
Cdd:MTH00023  106 IKAIGHQWYWSYEY-----------SDYEGETLEFDsyMVptsDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSF 174

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1197265417 192 KVANFRAKMDMVPG---QTSYFWFTPtvvGEYEIVCAQLCGIAHFAMRGRIEVVEQEVFDAWLS 252
Cdd:MTH00023  175 AVPSLGLKIDAVPGrlnQTGFFIKRP---GVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLL 235
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 117-254 1.81e-10

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 61.19  E-value: 1.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 117 VEVVGQQWHWSFRFpgEDgrFGAAHNRFIDERNPfgMVDDPAGQDDILITSPHLVLPVDRPVKMVLRSKDVLHNVKVANF 196
Cdd:MTH00027  129 IKVTGHQWYWSYSY--ED--YGEKNIEFDSYMIP--TADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSL 202

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1197265417 197 RAKMDMVPGQTSYFWFTPTVVGEYEIVCAQLCGIAHFAMRGRIEVVEQEVFDAWLSEQ 254
Cdd:MTH00027  203 AVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWIGRE 260
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 114-254 2.14e-10

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 60.56  E-value: 2.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 114 AHQVEVVGQQWHWSFrfpgEDGRFGAAHNRFidERNPFGMVDDPAGQDDILITSPHLVLPVDRPVKMVLRSKDVLHNVKV 193
Cdd:MTH00051   96 ALTIKAIGHQWYWSY----EYSDYGTDTIEF--DSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAV 169

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1197265417 194 ANFRAKMDMVPG---QTSYFWFTPtvvGEYEIVCAQLCGIAHFAMRGRIEVVEQEVFDAWLSEQ 254
Cdd:MTH00051  170 PSLSVKIDAVPGrlnQTSFFIKRP---GVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQ 230
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 117-251 3.73e-10

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 60.02  E-value: 3.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 117 VEVVGQQWHWSFRFPGEDGRFGAAHNRFIDERNpfgmvddpAGQDDILITSPHLVLPVDRPVKMVLRSKDVLHNVKVANF 196
Cdd:MTH00080  100 VKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLR--------LGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSL 171

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1197265417 197 RAKMDMVPGQTSYFWFTPTVVGEYEIVCAQLCGIAHFAMRGRIEVVEQEVFDAWL 251
Cdd:MTH00080  172 SIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWC 226
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 117-256 3.99e-10

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 59.79  E-value: 3.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 117 VEVVGQQWHWSFRFpgedgrfgaahNRFIDERNPFGMV---DDPAGQDDILITSPHLVLPVDRPVKMVLRSKDVLHNVKV 193
Cdd:MTH00076   97 VKAIGHQWYWSYEY-----------TDYEDLSFDSYMIptqDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAV 165

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1197265417 194 ANFRAKMDMVPGQTSYFWFTPTVVGEYEIVCAQLCGIAHFAMRGRIEVVEQEVFDAWLSEQPT 256
Cdd:MTH00076  166 PSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSMLE 228
TsdA COG3258
Thiosulfate dehydrogenase TsdA, contains C-terminal cytochrome c domain [Inorganic ion ...
 277-456 5.54e-10

Thiosulfate dehydrogenase TsdA, contains C-terminal cytochrome c domain [Inorganic ion transport and metabolism];


Pssm-ID: 442489 [Multi-domain]  Cd Length: 216  Bit Score: 59.10  E-value: 5.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 277 TCAACHGAEGQGNAALNA------PKLAGMDAWYlERQLALFRSGARGsheddtygqqmRPFATMLPDRQAIVdvsAFIE 350
Cdd:COG3258    24 SCASCHLDAGTKPWGVAAaypayrARNGKVVTLE-DRINGCFTRSMNG-----------KPLPLDSAEMKALV---AYLR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 351 TL-PDQAVETSLAG------------GDPERGARRYRT-CANCHGQQGEGIRATNG----PRLAGlpdwylerqLQNFRH 412
Cdd:COG3258    89 WLsRGLPVGVKLDGrglpklpkpaasADVERGKALYAErCASCHGADGEGQGRADGqygfPPLWG---------GDSYND 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1197265417 413 GvRGRHRED-----------PYGNqmiemAQVLVDDRAVrDVVAYITTL--PQPRVD 456
Cdd:COG3258   160 G-AGMARLGtladfikgrnmPLGK-----PGSLSDDEAW-DVAAYVRSLprPVPRKT 209
Cytochrom_C pfam00034
Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and ...
 367-450 1.28e-09

Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and cytochrome c' families are not included. All these are now in a new clan together. The C-terminus of DUF989, pfam06181, has now been merged into this family.


Pssm-ID: 459641 [Multi-domain]  Cd Length: 89  Bit Score: 54.85  E-value: 1.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 367 ERGARRY-RTCANCHGQQGEGIrATNGPRLAGLPDWYLERQLQNFRHGVR----GRHREDPYGNQMIEMAQVLVDDRAVR 441
Cdd:pfam00034   1 ARGKKLFaANCAACHGVNGEGA-GAGGPDLAGLAARYPGDALGAIRENKHaiggGGVDRAGGPPGTGMPAFDGLTDEEIA 79


                  ....*....
gi 1197265417 442 DVVAYITTL 450
Cdd:pfam00034  80 DLVAYLLSL 88
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 117-253 3.83e-09

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 56.65  E-value: 3.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 117 VEVVGQQWHWSFRFPGEDGRFGAAHnrfidernpfgMV--DDPAGQDDILITSPH-LVLPVDRPVKMVLRSKDVLHNVKV 193
Cdd:MTH00139   97 FKAVGHQWYWSYEYSDFKNLSFDSY-----------MIptEDLSSGEFRLLEVDNrLVLPYKSNIRALITAADVLHSWTV 165

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 194 ANFRAKMDMVPGQTSYFWFTPTVVGEYEIVCAQLCGIAHFAMRGRIEVVEQEVFDAWLSE 253
Cdd:MTH00139  166 PSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILE 225
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 171-242 4.14e-08

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 50.84  E-value: 4.14e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1197265417 171 VLPVDRPVKMVLRSKDVLHNVKVANfrAKMDMV------PGQTSYFWFTPTVVGEYEIVCAQLCGIAHFAMRGRIEVV 242
Cdd:cd13916    18 EIPAGKPVEFRVTSADVNHGFGIYD--PDMRLLaqtqamPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVMMAEFTVV 93
TsdA COG3258
Thiosulfate dehydrogenase TsdA, contains C-terminal cytochrome c domain [Inorganic ion ...
 264-353 6.29e-08

Thiosulfate dehydrogenase TsdA, contains C-terminal cytochrome c domain [Inorganic ion transport and metabolism];


Pssm-ID: 442489 [Multi-domain]  Cd Length: 216  Bit Score: 52.93  E-value: 6.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 264 APGDPEAGAERYAT-CAACHGAEGQGNAALNA----PKLAGMDAwylerqlalFRSGArGSHEDDT-----YGQQMRPFA 333
Cdd:COG3258   113 ASADVERGKALYAErCASCHGADGEGQGRADGqygfPPLWGGDS---------YNDGA-GMARLGTladfiKGRNMPLGK 182

                          90       100
                  ....*....|....*....|.
gi 1197265417 334 T-MLPDRQAiVDVSAFIETLP 353
Cdd:COG3258   183 PgSLSDDEA-WDVAAYVRSLP 202
ccoP TIGR00782
cytochrome c oxidase, cbb3-type, subunit III; This model describes a di-heme subunit of ...
 229-450 1.76e-07

cytochrome c oxidase, cbb3-type, subunit III; This model describes a di-heme subunit of approximately 26 kDa of the cbb3 type copper and heme-containing cytochrome oxidase. [Energy metabolism, Electron transport]


Pssm-ID: 129864 [Multi-domain]  Cd Length: 285  Bit Score: 52.59  E-value: 1.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 229 GIAHFAMRGRievVEQEVFDAWLSEQPTYAELAQL----APGDPE-------AGAERYAT-CAACHGAEGQGNAALnaPK 296
Cdd:TIGR00782  60 GLLGWSSRSQ---VEEEIKKFNEKNAAKWAKLAQTpledIAKDPElkqyarnAGAAIFRTwCAQCHGSGAGGAKGF--PN 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 297 LAGMDaWY----LERQLALFRSGARGSHEDDTYGQQMRPFATMLPDRQaIVDVSAFIETLpdqaveTSLAGGDPERGARR 372
Cdd:TIGR00782 135 LLDND-WLwggtLEGIHTTIKHGIRDPDDGDTYVGEMPAFGPLLEEAD-IKDVASYVMSL------SSGKPKDEALAAKG 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 373 YR----TCANCHGQQGEGIRATNGPRLAGLPDWYLERQLQNFRHGVRGRhredpyGNQMIEMAQVLVDDRaVRDVVAYIT 448
Cdd:TIGR00782 207 QElfadNCTTCHGEDGKGLQELGAPNLTDDVWLYGGDLKTITTTITNGR------GGVMPAWGPRLSEAQ-IKALAAYVH 279


                  ..
gi 1197265417 449 TL 450
Cdd:TIGR00782 280 SL 281
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 117-252 3.05e-07

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 51.07  E-value: 3.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 117 VEVVGQQWHWSFRFP-GEDGRFGAAhnrfidernpfgMV---DDPAGQDDILITSPHLVLPVDRPVKMVLRSKDVLHNVK 192
Cdd:MTH00117   97 IKAIGHQWYWSYEYTdYKDLSFDSY------------MIptqDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWA 164

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1197265417 193 VANFRAKMDMVPG---QTSyfwFTPTVVGEYEIVCAQLCGIAHFAMRGRIEVVEQEVFDAWLS 252
Cdd:MTH00117  165 VPSLGVKTDAVPGrlnQTS---FITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSS 224
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 168-242 4.32e-07

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259984 [Multi-domain]  Cd Length: 88  Bit Score: 47.75  E-value: 4.32e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1197265417 168 PHLVLPVDRPVKMVLRSKDVLHNVKVANFRAKMDMVPGQTSYFWFTPTVVGEYEIVCAQLCGIAHFAMRGRIEVV 242
Cdd:cd13917    14 PVLVLKKGKTYRLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTMHGRIIVE 88
CccA COG2010
Cytochrome c, mono- and diheme variants [Energy production and conversion];
258-355 7.21e-07

Cytochrome c, mono- and diheme variants [Energy production and conversion];


Pssm-ID: 441613 [Multi-domain]  Cd Length: 169  Bit Score: 49.18  E-value: 7.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 258 AELAQLAPGDPEAGAERYAT-CAACHGAEGQGNA----ALNAPKLAGMDAWYLERQLalfRSGARGSheddtygqQMRPF 332
Cdd:COG2010    79 ADAPAADAEALARGKALYEQnCAACHGADGKGGLgaapNLTDDALYGGDPEALVETI---LNGRPGG--------AMPAF 147

                          90       100
                  ....*....|....*....|...
gi 1197265417 333 ATMLPDRQaIVDVSAFIETLPDQ 355
Cdd:COG2010   148 GGQLSDEE-IAALAAYLRSLSGN 169
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 119-252 2.39e-06

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 48.67  E-value: 2.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 119 VVGQQWHWSFRFPgeDgrfgaahnrFID-ERNPFgMVDDPAGQDD---ILITSPHLVLPVDRPVKMVLRSKDVLHNVKVA 194
Cdd:MTH00154   99 TIGHQWYWSYEYS--D---------FKNiEFDSY-MIPTNELENNgfrLLDVDNRLVLPMNTQIRILITAADVIHSWTVP 166

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1197265417 195 NFRAKMDMVPG---QTSyfwFTPTVVGEYEIVCAQLCGIAHFAMRGRIEVVEQEVFDAWLS 252
Cdd:MTH00154  167 SLGVKVDAVPGrlnQLN---FLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIK 224
CytC5 COG3245
Cytochrome c5 [Energy production and conversion];
260-303 1.75e-05

Cytochrome c5 [Energy production and conversion];


Pssm-ID: 442476 [Multi-domain]  Cd Length: 108  Bit Score: 43.51  E-value: 1.75e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1197265417 260 LAQLAPGDPEAGAERY-ATCAACHGAegqgnAALNAPKLAGMDAW 303
Cdd:COG3245    24 AAAAAAAAARSGEAVYnATCAACHAT-----GVAGAPKLGDKAAW 63
CccA COG2010
Cytochrome c, mono- and diheme variants [Energy production and conversion];
298-452 1.81e-05

Cytochrome c, mono- and diheme variants [Energy production and conversion];


Pssm-ID: 441613 [Multi-domain]  Cd Length: 169  Bit Score: 44.94  E-value: 1.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 298 AGMDAWYLERQLALFRSGARGSHEDDTYGQQMRPFATMLPDRQAIVDVSAFIETLPdQAVETSLAGGDPERGARRYRT-C 376
Cdd:COG2010    22 AGAAGAGGVAAAGAGLAGALVDGAAAAAALGAAAAAAAAAAALALALLLALLLAAA-AADAPAADAEALARGKALYEQnC 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 377 ANCHGQQGEGIRAT----NGPRLAGLPDWYLERQLQNfrhgvrGRHredpyGNQMIEMAQVLvDDRAVRDVVAYITTLPQ 452
Cdd:COG2010   101 AACHGADGKGGLGAapnlTDDALYGGDPEALVETILN------GRP-----GGAMPAFGGQL-SDEEIAALAAYLRSLSG 168
Cytochrome_CBB3 pfam13442
Cytochrome C oxidase, cbb3-type, subunit III;
266-349 4.09e-05

Cytochrome C oxidase, cbb3-type, subunit III;


Pssm-ID: 463879 [Multi-domain]  Cd Length: 67  Bit Score: 41.62  E-value: 4.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 266 GDPEAGAERY-ATCAACHGAEGQGnaalnaPKLAGmDAWYLERQLALFRSGARGsheddtygqqMRPFATMLPDRQaIVD 344
Cdd:pfam13442   1 AAAAAGEALYaANCASCHGTGGAG------PSLAG-RALPPEALVDIIRNGKGA----------MPAFGGDLSDEE-LEA 62


                  ....*
gi 1197265417 345 VSAFI 349
Cdd:pfam13442  63 LAAYL 67
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 183-241 4.49e-05

The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase participates in nitrogen metabolism and catalyzes the last step in dissimilatory nitrate reduction, the two-electron reduction of N2O to N2. It contains copper ions as cofactors in the form of a binuclear CuA center at the site of electron entry and a tetranuclear CuZ centre at the active site. The C-terminus of Nitrous-oxide reductase is a cupredoxin domain.


Pssm-ID: 259885 [Multi-domain]  Cd Length: 95  Bit Score: 42.22  E-value: 4.49e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1197265417 183 RSKDVLHNVKVANFRAKMDMVPGQTSYFWFTPTVVGEYEIVCAQLCGIAHFAMRGRIEV 241
Cdd:cd04223    35 QDEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEMQGYLIV 93
Cytochrome_CBB3 pfam13442
Cytochrome C oxidase, cbb3-type, subunit III;
364-447 9.89e-05

Cytochrome C oxidase, cbb3-type, subunit III;


Pssm-ID: 463879 [Multi-domain]  Cd Length: 67  Bit Score: 40.47  E-value: 9.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 364 GDPERGARRYR-TCANCHGQQGegiratNGPRLAG--LPDWYLERQLqnfRHGVRGrhredpygnqMIEMAQVLvDDRAV 440
Cdd:pfam13442   1 AAAAAGEALYAaNCASCHGTGG------AGPSLAGraLPPEALVDII---RNGKGA----------MPAFGGDL-SDEEL 60


                  ....*..
gi 1197265417 441 RDVVAYI 447
Cdd:pfam13442  61 EALAAYL 67
ccoP TIGR00782
cytochrome c oxidase, cbb3-type, subunit III; This model describes a di-heme subunit of ...
 259-354 3.68e-04

cytochrome c oxidase, cbb3-type, subunit III; This model describes a di-heme subunit of approximately 26 kDa of the cbb3 type copper and heme-containing cytochrome oxidase. [Energy metabolism, Electron transport]


Pssm-ID: 129864 [Multi-domain]  Cd Length: 285  Bit Score: 42.19  E-value: 3.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 259 ELAQLAPGDPEA---GAERYAT-CAACHGAEGQGNAALNAPKLAGmDAW-YLERQLALFRSGARGSheddtyGQQMRPFA 333
Cdd:TIGR00782 191 SLSSGKPKDEALaakGQELFADnCTTCHGEDGKGLQELGAPNLTD-DVWlYGGDLKTITTTITNGR------GGVMPAWG 263

                          90       100
                  ....*....|....*....|.
gi 1197265417 334 TMLPDRQaIVDVSAFIETLPD 354
Cdd:TIGR00782 264 PRLSEAQ-IKALAAYVHSLGG 283
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 164-240 7.49e-03

Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in inter-molecular electron transfer reactions. Cupredoxins are blue copper proteins, having an intense blue color due to the presence of a mononuclear type 1 (T1) copper site. Structurally, the cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel. Some of these proteins have lost the ability to bind copper. The majority of family members contain multiple cupredoxin domain repeats: ceruloplasmin and the coagulation factors V/VIII have six repeats; laccase, ascorbate oxidase, spore coat protein A, and multicopper oxidase CueO contain three repeats; and nitrite reductase has two repeats. Others are mono-domain cupredoxins, such as plastocyanin, pseudoazurin, plantacyanin, azurin, rusticyanin, stellacyanin, quinol oxidase, and the periplasmic domain of cytochrome c oxidase subunit II.


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 36.05  E-value: 7.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1197265417 164 LITSPHLVLPVDRPVKMVLRSK-DVLHNVKVANFRAKMD---------------MVPGQTSYFWFTPTVVGEYEIVCAQL 227
Cdd:cd00920    19 LFGPPVLVVPVGDTVRVQFVNKlGENHSVTIAGFGVPVVamagganpglvntlvIGPGESAEVTFTTDQAGVYWFYCTIP 98

                          90
                  ....*....|...
gi 1197265417 228 CGIAHFaMRGRIE 240
Cdd:cd00920    99 GHNHAG-MVGTIN 110
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH